ID AA1R_HUMAN Reviewed; 326 AA. AC P30542; A6NFY5; A6NGP4; A8K1L3; B3KXQ4; D2CGD0; Q6FHK3; Q8TAM8; DT 01-APR-1993, integrated into UniProtKB/Swiss-Prot. DT 01-APR-1993, sequence version 1. DT 28-JAN-2026, entry version 214. DE RecName: Full=Adenosine receptor A1; GN Name=ADORA1; OS Homo sapiens (Human). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia; OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae; OC Homo. OX NCBI_TaxID=9606; RN [1] RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1). RC TISSUE=Hippocampus; RX PubMed=1530647; DOI=10.1016/0006-291x(92)91285-x; RA Libert F., van Sande J., Lefort A., Czernilofsky A., Dumont J.E., RA Vassart G., Ensinger H.A., Mendla K.D.; RT "Cloning and functional characterization of a human A1 adenosine RT receptor."; RL Biochem. Biophys. Res. Commun. 187:919-926(1992). RN [2] RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1). RC TISSUE=Brain; RX PubMed=1339301; DOI=10.1016/0169-328x(92)90248-a; RA Townsend-Nicholson A., Shine J.; RT "Molecular cloning and characterisation of a human brain A1 adenosine RT receptor cDNA."; RL Brain Res. Mol. Brain Res. 16:365-370(1992). RN [3] RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1). RC TISSUE=Hippocampus; RX PubMed=8300646; DOI=10.1016/s0021-9258(17)42054-0; RA Ren H., Stiles G.L.; RT "Characterization of the human A1 adenosine receptor gene. Evidence for RT alternative splicing."; RL J. Biol. Chem. 269:3104-3110(1994). RN [4] RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1). RC TISSUE=Brain; RA Salvatore C.A., Luneau C.J., Johnson R.G., Jacobson M.; RL Submitted (SEP-1992) to the EMBL/GenBank/DDBJ databases. RN [5] RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1). RC TISSUE=Heart; RA Hirabatake Y., Takao K., Hagiwara S., Kasanuki H., Hosoda S., Kokubun S.; RT "Complete nucleotide sequence of an adenosine A1-receptor from heart."; RL Submitted (JUN-1997) to the EMBL/GenBank/DDBJ databases. RN [6] RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2). RA Feng Y.-H., Cheng H., Qiu R.; RT "Identification of a 3TM adenosine receptor subtype 1 variant."; RL Submitted (OCT-2006) to the EMBL/GenBank/DDBJ databases. RN [7] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1). RC TISSUE=Brain, and Hippocampus; RX PubMed=14702039; DOI=10.1038/ng1285; RA Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., RA Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., RA Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S., RA Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., RA Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H., RA Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., RA Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., RA Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., RA Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., RA Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., RA Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., RA Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., RA Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., RA Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., RA Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., RA Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., RA Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., RA Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y., RA Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., RA Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., RA Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., RA Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., RA Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., RA Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., RA Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., RA Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., RA Isogai T., Sugano S.; RT "Complete sequencing and characterization of 21,243 full-length human RT cDNAs."; RL Nat. Genet. 36:40-45(2004). RN [8] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1). RC TISSUE=Brain; RA Puhl H.L. III, Ikeda S.R., Aronstam R.S.; RT "cDNA clones of human proteins involved in signal transduction sequenced by RT the Guthrie cDNA resource center (www.cdna.org)."; RL Submitted (JUL-2002) to the EMBL/GenBank/DDBJ databases. RN [9] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1). RA Kalnine N., Chen X., Rolfs A., Halleck A., Hines L., Eisenstein S., RA Koundinya M., Raphael J., Moreira D., Kelley T., LaBaer J., Lin Y., RA Phelan M., Farmer A.; RT "Cloning of human full-length CDSs in BD Creator(TM) system donor vector."; RL Submitted (MAY-2003) to the EMBL/GenBank/DDBJ databases. RN [10] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1). RA Ebert L., Schick M., Neubert P., Schatten R., Henze S., Korn B.; RT "Cloning of human full open reading frames in Gateway(TM) system entry RT vector (pDONR201)."; RL Submitted (JUN-2004) to the EMBL/GenBank/DDBJ databases. RN [11] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RX PubMed=16710414; DOI=10.1038/nature04727; RA Gregory S.G., Barlow K.F., McLay K.E., Kaul R., Swarbreck D., Dunham A., RA Scott C.E., Howe K.L., Woodfine K., Spencer C.C.A., Jones M.C., Gillson C., RA Searle S., Zhou Y., Kokocinski F., McDonald L., Evans R., Phillips K., RA Atkinson A., Cooper R., Jones C., Hall R.E., Andrews T.D., Lloyd C., RA Ainscough R., Almeida J.P., Ambrose K.D., Anderson F., Andrew R.W., RA Ashwell R.I.S., Aubin K., Babbage A.K., Bagguley C.L., Bailey J., RA Beasley H., Bethel G., Bird C.P., Bray-Allen S., Brown J.Y., Brown A.J., RA Buckley D., Burton J., Bye J., Carder C., Chapman J.C., Clark S.Y., RA Clarke G., Clee C., Cobley V., Collier R.E., Corby N., Coville G.J., RA Davies J., Deadman R., Dunn M., Earthrowl M., Ellington A.G., Errington H., RA Frankish A., Frankland J., French L., Garner P., Garnett J., Gay L., RA Ghori M.R.J., Gibson R., Gilby L.M., Gillett W., Glithero R.J., RA Grafham D.V., Griffiths C., Griffiths-Jones S., Grocock R., Hammond S., RA Harrison E.S.I., Hart E., Haugen E., Heath P.D., Holmes S., Holt K., RA Howden P.J., Hunt A.R., Hunt S.E., Hunter G., Isherwood J., James R., RA Johnson C., Johnson D., Joy A., Kay M., Kershaw J.K., Kibukawa M., RA Kimberley A.M., King A., Knights A.J., Lad H., Laird G., Lawlor S., RA Leongamornlert D.A., Lloyd D.M., Loveland J., Lovell J., Lush M.J., RA Lyne R., Martin S., Mashreghi-Mohammadi M., Matthews L., Matthews N.S.W., RA McLaren S., Milne S., Mistry S., Moore M.J.F., Nickerson T., O'Dell C.N., RA Oliver K., Palmeiri A., Palmer S.A., Parker A., Patel D., Pearce A.V., RA Peck A.I., Pelan S., Phelps K., Phillimore B.J., Plumb R., Rajan J., RA Raymond C., Rouse G., Saenphimmachak C., Sehra H.K., Sheridan E., RA Shownkeen R., Sims S., Skuce C.D., Smith M., Steward C., Subramanian S., RA Sycamore N., Tracey A., Tromans A., Van Helmond Z., Wall M., Wallis J.M., RA White S., Whitehead S.L., Wilkinson J.E., Willey D.L., Williams H., RA Wilming L., Wray P.W., Wu Z., Coulson A., Vaudin M., Sulston J.E., RA Durbin R.M., Hubbard T., Wooster R., Dunham I., Carter N.P., McVean G., RA Ross M.T., Harrow J., Olson M.V., Beck S., Rogers J., Bentley D.R.; RT "The DNA sequence and biological annotation of human chromosome 1."; RL Nature 441:315-321(2006). RN [12] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RA Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M., RA Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J., RA Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S., RA Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H., RA Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K., RA Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D., RA Hunkapiller M.W., Myers E.W., Venter J.C.; RL Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases. RN [13] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1), AND VARIANTS SER-43; RP PRO-50; HIS-105 AND GLN-261. RC TISSUE=Brain; RX PubMed=15489334; DOI=10.1101/gr.2596504; RG The MGC Project Team; RT "The status, quality, and expansion of the NIH full-length cDNA project: RT the Mammalian Gene Collection (MGC)."; RL Genome Res. 14:2121-2127(2004). RN [14] {ECO:0007744|PDB:6D9H} RP STRUCTURE BY ELECTRON MICROSCOPY (3.60 ANGSTROMS) OF 2-326 IN COMPLEX WITH RP ADENOSINE, DISULFIDE BONDS, FUNCTION, INTERACTION WITH GNAI2, AND TOPOLOGY. RX PubMed=29925945; DOI=10.1038/s41586-018-0236-6; RA Draper-Joyce C.J., Khoshouei M., Thal D.M., Liang Y.L., Nguyen A.T.N., RA Furness S.G.B., Venugopal H., Baltos J.A., Plitzko J.M., Danev R., RA Baumeister W., May L.T., Wootten D., Sexton P.M., Glukhova A., RA Christopoulos A.; RT "Structure of the adenosine-bound human adenosine A1 receptor-Gi complex."; RL Nature 558:559-563(2018). RN [15] RP VARIANT [LARGE SCALE ANALYSIS] LYS-170. RX PubMed=16959974; DOI=10.1126/science.1133427; RA Sjoeblom T., Jones S., Wood L.D., Parsons D.W., Lin J., Barber T.D., RA Mandelker D., Leary R.J., Ptak J., Silliman N., Szabo S., Buckhaults P., RA Farrell C., Meeh P., Markowitz S.D., Willis J., Dawson D., Willson J.K.V., RA Gazdar A.F., Hartigan J., Wu L., Liu C., Parmigiani G., Park B.H., RA Bachman K.E., Papadopoulos N., Vogelstein B., Kinzler K.W., RA Velculescu V.E.; RT "The consensus coding sequences of human breast and colorectal cancers."; RL Science 314:268-274(2006). RN [16] RP VARIANT SER-279, CHARACTERIZATION OF VARIANT SER-279, AND SUBCELLULAR RP LOCATION. RX PubMed=27134041; DOI=10.1002/mds.26627; RA Jaberi E., Rohani M., Shahidi G.A., Nafissi S., Arefian E., Soleimani M., RA Moghadam A., Arzenani M.K., Keramatian F., Klotzle B., Fan J.B., Turk C., RA Steemers F., Elahi E.; RT "Mutation in ADORA1 identified as likely cause of early-onset parkinsonism RT and cognitive dysfunction."; RL Mov. Disord. 31:1004-1011(2016). CC -!- FUNCTION: Receptor for adenosine (PubMed:29925945). The activity of CC this receptor is mediated by G proteins such as GNAI2 which inhibit CC adenylyl cyclase. {ECO:0000269|PubMed:29925945}. CC -!- SUBUNIT: Interacts with GNAI2. {ECO:0000269|PubMed:29925945}. CC -!- INTERACTION: CC P30542; P29274: ADORA2A; NbExp=4; IntAct=EBI-2903663, EBI-2902702; CC P30542; P08588: ADRB1; NbExp=5; IntAct=EBI-2903663, EBI-991009; CC P30542; P07550: ADRB2; NbExp=5; IntAct=EBI-2903663, EBI-491169; CC P30542; P16473: TSHR; NbExp=2; IntAct=EBI-2903663, EBI-13939599; CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:27134041}; CC Multi-pass membrane protein. CC -!- ALTERNATIVE PRODUCTS: CC Event=Alternative splicing; Named isoforms=2; CC Name=1; CC IsoId=P30542-1; Sequence=Displayed; CC Name=2; CC IsoId=P30542-2; Sequence=VSP_034401, VSP_034402; CC -!- SIMILARITY: Belongs to the G-protein coupled receptor 1 family. CC {ECO:0000255|PROSITE-ProRule:PRU00521}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; S45235; AAB23388.1; -; mRNA. DR EMBL; S56143; AAB25533.2; -; mRNA. DR EMBL; L22214; AAA17544.1; -; mRNA. DR EMBL; X68485; CAA48503.1; -; mRNA. DR EMBL; AB004662; BAA20433.1; -; mRNA. DR EMBL; EF057066; ABO25743.1; -; mRNA. DR EMBL; AK127752; BAG54566.1; -; mRNA. DR EMBL; AK289928; BAF82617.1; -; mRNA. DR EMBL; AY136746; AAN01272.1; -; mRNA. DR EMBL; BT019854; AAV38657.1; -; mRNA. DR EMBL; CR541749; CAG46549.1; -; mRNA. DR EMBL; AC105940; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; CH471067; EAW91465.1; -; Genomic_DNA. DR EMBL; BC026340; AAH26340.1; -; mRNA. DR CCDS; CCDS1434.1; -. [P30542-1] DR PIR; A53005; A53005. DR RefSeq; NP_000665.1; NM_000674.3. [P30542-1] DR RefSeq; NP_001041695.1; NM_001048230.2. [P30542-1] DR PDB; 5N2S; X-ray; 3.30 A; A=4-316. DR PDB; 5UEN; X-ray; 3.20 A; A/B=2-211, A/B=228-311. DR PDB; 6D9H; EM; 3.60 A; R=2-326. DR PDB; 7LD3; EM; 3.20 A; R=2-326. DR PDB; 7LD4; EM; 3.30 A; R=2-326. DR PDBsum; 5N2S; -. DR PDBsum; 5UEN; -. DR PDBsum; 6D9H; -. DR PDBsum; 7LD3; -. DR PDBsum; 7LD4; -. DR AlphaFoldDB; P30542; -. DR EMDB; EMD-23280; -. DR EMDB; EMD-23281; -. DR EMDB; EMD-7835; -. DR SMR; P30542; -. DR BioGRID; 106646; 17. DR CORUM; P30542; -. DR FunCoup; P30542; 889. DR IntAct; P30542; 12. DR MINT; P30542; -. DR STRING; 9606.ENSP00000356205; -. DR BindingDB; P30542; -. DR ChEMBL; CHEMBL226; -. DR DrugBank; DB07954; 3-isobutyl-1-methyl-7H-xanthine. DR DrugBank; DB08770; 4-{2-[(7-amino-2-furan-2-yl[1,2,4]triazolo[1,5-a][1,3,5]triazin-5-yl)amino]ethyl}phenol. DR DrugBank; DB02282; 5'-S-methyl-5'-thioadenosine. DR DrugBank; DB00640; Adenosine. DR DrugBank; DB01223; Aminophylline. DR DrugBank; DB14018; Bromotheophylline. DR DrugBank; DB00201; Caffeine. DR DrugBank; DB09061; Cannabidiol. DR DrugBank; DB16118; Capadenoson. DR DrugBank; DB04932; Defibrotide. DR DrugBank; DB12446; Derenofylline. DR DrugBank; DB12946; DPCPX. DR DrugBank; DB00651; Dyphylline. DR DrugBank; DB00824; Enprofylline. DR DrugBank; DB06484; FK352B. DR DrugBank; DB07776; Flavone. DR DrugBank; DB00996; Gabapentin. DR DrugBank; DB12760; GW-493838. DR DrugBank; DB11757; Istradefylline. DR DrugBank; DB00555; Lamotrigine. DR DrugBank; DB06471; Naxifylline. DR DrugBank; DB13138; Neladenoson bialanate. DR DrugBank; DB01303; Oxtriphylline. DR DrugBank; DB00806; Pentoxifylline. DR DrugBank; DB16288; Peoniflorin. DR DrugBank; DB12670; Rolofylline. DR DrugBank; DB08517; Sakuranetin. DR DrugBank; DB16325; Selodenoson. DR DrugBank; DB04954; Tecadenoson. DR DrugBank; DB01412; Theobromine. DR DrugBank; DB00277; Theophylline. DR DrugBank; DB12569; Tonapofylline. DR DrugBank; DB13122; Trabodenoson. DR DrugBank; DB00193; Tramadol. DR DrugCentral; P30542; -. DR GuidetoPHARMACOLOGY; 18; -. DR TCDB; 9.A.14.3.4; the g-protein-coupled receptor (gpcr) family. DR GlyConnect; 992; 6 N-Linked glycans (1 site). DR GlyCosmos; P30542; 1 site, 6 glycans. DR GlyGen; P30542; 1 site, 6 N-linked glycans (1 site). DR iPTMnet; P30542; -. DR PhosphoSitePlus; P30542; -. DR SwissPalm; P30542; -. DR BioMuta; ADORA1; -. DR DMDM; 231473; -. DR jPOST; P30542; -. DR MassIVE; P30542; -. DR PaxDb; 9606-ENSP00000356205; -. DR PeptideAtlas; P30542; -. DR ProteomicsDB; 54718; -. [P30542-1] DR Antibodypedia; 20660; 491 antibodies from 38 providers. DR DNASU; 134; -. DR Ensembl; ENST00000309502.7; ENSP00000308549.3; ENSG00000163485.19. [P30542-1] DR Ensembl; ENST00000337894.9; ENSP00000338435.4; ENSG00000163485.19. [P30542-1] DR Ensembl; ENST00000367235.1; ENSP00000356204.1; ENSG00000163485.19. [P30542-2] DR Ensembl; ENST00000367236.8; ENSP00000356205.4; ENSG00000163485.19. [P30542-1] DR GeneID; 134; -. DR KEGG; hsa:134; -. DR MANE-Select; ENST00000337894.9; ENSP00000338435.4; NM_000674.3; NP_000665.1. DR UCSC; uc001gze.1; human. [P30542-1] DR AGR; HGNC:262; -. DR ClinPGx; PA24583; -. DR CTD; 134; -. DR DisGeNET; 134; -. DR GeneCards; ADORA1; -. DR HGNC; HGNC:262; ADORA1. DR HPA; ENSG00000163485; Tissue enhanced (brain, testis). DR MalaCards; ADORA1; -. DR MIM; 102775; gene. DR OpenTargets; ENSG00000163485; -. DR VEuPathDB; HostDB:ENSG00000163485; -. DR eggNOG; KOG3656; Eukaryota. DR GeneTree; ENSGT01030000234555; -. DR HOGENOM; CLU_009579_11_5_1; -. DR InParanoid; P30542; -. DR OMA; FCCKDTP; -. DR OrthoDB; 5984709at2759; -. DR PAN-GO; P30542; 5 GO annotations based on evolutionary models. DR PhylomeDB; P30542; -. DR PathwayCommons; P30542; -. DR Reactome; R-HSA-417973; Adenosine P1 receptors. DR Reactome; R-HSA-418594; G alpha (i) signalling events. DR SignaLink; P30542; -. DR SIGNOR; P30542; -. DR Agora; ENSG00000163485; -. DR BioGRID-ORCS; 134; 13 hits in 1155 CRISPR screens. DR ChiTaRS; ADORA1; human. DR GeneWiki; Adenosine_A1_receptor; -. DR GenomeRNAi; 134; -. DR Pharos; P30542; Tclin. DR PRO; PR:P30542; -. DR Proteomes; UP000005640; Chromosome 1. DR RNAct; P30542; protein. DR Bgee; ENSG00000163485; Expressed in inferior vagus X ganglion and 180 other cell types or tissues. DR ExpressionAtlas; P30542; baseline and differential. DR GO; GO:0032279; C:asymmetric synapse; IEA:Ensembl. DR GO; GO:0030673; C:axolemma; IEA:Ensembl. DR GO; GO:0016323; C:basolateral plasma membrane; IEA:Ensembl. DR GO; GO:0044305; C:calyx of Held; IEA:Ensembl. DR GO; GO:0005929; C:cilium; IDA:HPA. DR GO; GO:0030425; C:dendrite; IBA:GO_Central. DR GO; GO:0043197; C:dendritic spine; IEA:Ensembl. DR GO; GO:0043025; C:neuronal cell body; IEA:Ensembl. DR GO; GO:0005886; C:plasma membrane; IDA:HPA. DR GO; GO:0045211; C:postsynaptic membrane; IEA:Ensembl. DR GO; GO:0048786; C:presynaptic active zone; IEA:Ensembl. DR GO; GO:0042734; C:presynaptic membrane; IEA:Ensembl. DR GO; GO:0045202; C:synapse; IBA:GO_Central. DR GO; GO:0043195; C:terminal bouton; IEA:Ensembl. DR GO; GO:0001609; F:G protein-coupled adenosine receptor activity; ISS:BHF-UCL. DR GO; GO:0001664; F:G protein-coupled receptor binding; ISS:BHF-UCL. DR GO; GO:0031683; F:G-protein beta/gamma-subunit complex binding; IEA:Ensembl. DR GO; GO:0031072; F:heat shock protein binding; IEA:Ensembl. DR GO; GO:0032795; F:heterotrimeric G-protein binding; IEA:Ensembl. DR GO; GO:0046982; F:protein heterodimerization activity; IEA:Ensembl. DR GO; GO:0001883; F:purine nucleoside binding; IEA:Ensembl. DR GO; GO:0007193; P:adenylate cyclase-inhibiting G protein-coupled receptor signaling pathway; IEA:Ensembl. DR GO; GO:0097190; P:apoptotic signaling pathway; TAS:ProtInc. DR GO; GO:0007267; P:cell-cell signaling; TAS:ProtInc. DR GO; GO:0050890; P:cognition; IEA:Ensembl. DR GO; GO:0050965; P:detection of temperature stimulus involved in sensory perception of pain; IEA:Ensembl. DR GO; GO:0060079; P:excitatory postsynaptic potential; IEA:Ensembl. DR GO; GO:0055089; P:fatty acid homeostasis; IEA:Ensembl. DR GO; GO:0035589; P:G protein-coupled purinergic nucleotide receptor signaling pathway; ISS:BHF-UCL. DR GO; GO:0007186; P:G protein-coupled receptor signaling pathway; IBA:GO_Central. DR GO; GO:0006954; P:inflammatory response; TAS:ProtInc. DR GO; GO:0050900; P:leukocyte migration; IEA:Ensembl. DR GO; GO:0016042; P:lipid catabolic process; IEA:Ensembl. DR GO; GO:0060292; P:long-term synaptic depression; IEA:Ensembl. DR GO; GO:0070254; P:mucus secretion; IEA:Ensembl. DR GO; GO:0002674; P:negative regulation of acute inflammatory response; IEA:Ensembl. DR GO; GO:0043066; P:negative regulation of apoptotic process; IEA:Ensembl. DR GO; GO:0008285; P:negative regulation of cell population proliferation; IEA:Ensembl. DR GO; GO:0042323; P:negative regulation of circadian sleep/wake cycle, non-REM sleep; IEA:Ensembl. DR GO; GO:0014050; P:negative regulation of glutamate secretion; IEA:Ensembl. DR GO; GO:0046888; P:negative regulation of hormone secretion; IEA:Ensembl. DR GO; GO:0002686; P:negative regulation of leukocyte migration; IEA:Ensembl. DR GO; GO:0050995; P:negative regulation of lipid catabolic process; IEA:Ensembl. DR GO; GO:1900453; P:negative regulation of long-term synaptic depression; IEA:Ensembl. DR GO; GO:1900272; P:negative regulation of long-term synaptic potentiation; IEA:Ensembl. DR GO; GO:0070256; P:negative regulation of mucus secretion; IEA:Ensembl. DR GO; GO:0032900; P:negative regulation of neurotrophin production; IEA:Ensembl. DR GO; GO:0032229; P:negative regulation of synaptic transmission, GABAergic; IEA:Ensembl. DR GO; GO:0051967; P:negative regulation of synaptic transmission, glutamatergic; IEA:Ensembl. DR GO; GO:0003085; P:negative regulation of systemic arterial blood pressure; IEA:Ensembl. DR GO; GO:0007399; P:nervous system development; TAS:ProtInc. DR GO; GO:0006909; P:phagocytosis; TAS:ProtInc. DR GO; GO:0035306; P:positive regulation of dephosphorylation; IEA:Ensembl. DR GO; GO:0050996; P:positive regulation of lipid catabolic process; IEA:Ensembl. DR GO; GO:0043410; P:positive regulation of MAPK cascade; IEA:Ensembl. DR GO; GO:0032244; P:positive regulation of nucleoside transport; IEA:Ensembl. DR GO; GO:0002793; P:positive regulation of peptide secretion; IEA:Ensembl. DR GO; GO:0043268; P:positive regulation of potassium ion transport; IEA:Ensembl. DR GO; GO:0003084; P:positive regulation of systemic arterial blood pressure; IEA:Ensembl. DR GO; GO:0006612; P:protein targeting to membrane; IEA:Ensembl. DR GO; GO:0086004; P:regulation of cardiac muscle cell contraction; IEA:Ensembl. DR GO; GO:0003093; P:regulation of glomerular filtration; IEA:Ensembl. DR GO; GO:0099509; P:regulation of presynaptic cytosolic calcium ion concentration; IEA:Ensembl. DR GO; GO:0002087; P:regulation of respiratory gaseous exchange by nervous system process; IEA:Ensembl. DR GO; GO:0051930; P:regulation of sensory perception of pain; IEA:Ensembl. DR GO; GO:0001666; P:response to hypoxia; IEA:Ensembl. DR GO; GO:0014074; P:response to purine-containing compound; IDA:MGI. DR GO; GO:0007165; P:signal transduction; TAS:ProtInc. DR GO; GO:0001659; P:temperature homeostasis; IEA:Ensembl. DR GO; GO:0070328; P:triglyceride homeostasis; IEA:Ensembl. DR GO; GO:0042311; P:vasodilation; IEA:Ensembl. DR CDD; cd15071; 7tmA_Adenosine_R_A1; 1. DR DisProt; DP02651; -. DR FunFam; 1.20.1070.10:FF:000061; Adenosine receptor A2; 1. DR Gene3D; 1.20.1070.10; Rhodopsin 7-helix transmembrane proteins; 1. DR InterPro; IPR001068; Adeno_A1_rcpt. DR InterPro; IPR001634; Adenosn_rcpt. DR InterPro; IPR000276; GPCR_Rhodpsn. DR InterPro; IPR017452; GPCR_Rhodpsn_7TM. DR PANTHER; PTHR24246:SF1; ADENOSINE RECEPTOR A1; 1. DR PANTHER; PTHR24246; OLFACTORY RECEPTOR AND ADENOSINE RECEPTOR; 1. DR Pfam; PF00001; 7tm_1; 1. DR PRINTS; PR00552; ADENOSINEA1R. DR PRINTS; PR00424; ADENOSINER. DR PRINTS; PR00237; GPCRRHODOPSN. DR SMART; SM01381; 7TM_GPCR_Srsx; 1. DR SUPFAM; SSF81321; Family A G protein-coupled receptor-like; 1. DR PROSITE; PS00237; G_PROTEIN_RECEP_F1_1; 1. DR PROSITE; PS50262; G_PROTEIN_RECEP_F1_2; 1. PE 1: Evidence at protein level; KW 3D-structure; Alternative splicing; Cell membrane; Disulfide bond; KW G-protein coupled receptor; Glycoprotein; Lipoprotein; Membrane; Palmitate; KW Proteomics identification; Receptor; Reference proteome; Transducer; KW Transmembrane; Transmembrane helix. FT CHAIN 1..326 FT /note="Adenosine receptor A1" FT /id="PRO_0000068991" FT TOPO_DOM 1..11 FT /note="Extracellular" FT /evidence="ECO:0000269|PubMed:29925945" FT TRANSMEM 12..32 FT /note="Helical; Name=1" FT /evidence="ECO:0000269|PubMed:29925945" FT TOPO_DOM 33..47 FT /note="Cytoplasmic" FT /evidence="ECO:0000269|PubMed:29925945" FT TRANSMEM 48..68 FT /note="Helical; Name=2" FT /evidence="ECO:0000269|PubMed:29925945" FT TOPO_DOM 69..77 FT /note="Extracellular" FT /evidence="ECO:0000269|PubMed:29925945" FT TRANSMEM 78..98 FT /note="Helical; Name=3" FT /evidence="ECO:0000269|PubMed:29925945" FT TOPO_DOM 99..127 FT /note="Cytoplasmic" FT /evidence="ECO:0000269|PubMed:29925945" FT TRANSMEM 128..147 FT /note="Helical; Name=4" FT /evidence="ECO:0000269|PubMed:29925945" FT TOPO_DOM 148..173 FT /note="Extracellular" FT /evidence="ECO:0000269|PubMed:29925945" FT TRANSMEM 174..196 FT /note="Helical; Name=5" FT /evidence="ECO:0000269|PubMed:29925945" FT TOPO_DOM 197..236 FT /note="Cytoplasmic" FT /evidence="ECO:0000269|PubMed:29925945" FT TRANSMEM 237..259 FT /note="Helical; Name=6" FT /evidence="ECO:0000269|PubMed:29925945" FT TOPO_DOM 260..267 FT /note="Extracellular" FT /evidence="ECO:0000269|PubMed:29925945" FT TRANSMEM 268..289 FT /note="Helical; Name=7" FT /evidence="ECO:0000269|PubMed:29925945" FT TOPO_DOM 290..326 FT /note="Cytoplasmic" FT /evidence="ECO:0000269|PubMed:29925945" FT LIPID 309 FT /note="S-palmitoyl cysteine" FT /evidence="ECO:0000255" FT CARBOHYD 159 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000255" FT DISULFID 80..169 FT /evidence="ECO:0000269|PubMed:29925945" FT DISULFID 260..263 FT /evidence="ECO:0000269|PubMed:29925945" FT VAR_SEQ 115..125 FT /note="YKMVVTPRRAA -> RISQCMASTKS (in isoform 2)" FT /evidence="ECO:0000303|Ref.6" FT /id="VSP_034401" FT VAR_SEQ 126..326 FT /note="Missing (in isoform 2)" FT /evidence="ECO:0000303|Ref.6" FT /id="VSP_034402" FT VARIANT 43 FT /note="A -> S (in dbSNP:rs11547175)" FT /evidence="ECO:0000269|PubMed:15489334" FT /id="VAR_044138" FT VARIANT 50 FT /note="S -> P (in dbSNP:rs11547174)" FT /evidence="ECO:0000269|PubMed:15489334" FT /id="VAR_044139" FT VARIANT 105 FT /note="R -> H (in dbSNP:rs11547176)" FT /evidence="ECO:0000269|PubMed:15489334" FT /id="VAR_044140" FT VARIANT 170 FT /note="E -> K (in a colorectal cancer sample; somatic FT mutation; dbSNP:rs899207013)" FT /evidence="ECO:0000269|PubMed:16959974" FT /id="VAR_035754" FT VARIANT 261 FT /note="P -> Q (in dbSNP:rs17852405)" FT /evidence="ECO:0000269|PubMed:15489334" FT /id="VAR_044141" FT VARIANT 279 FT /note="G -> S (found in a family with early-onset autosomal FT recessive parkinsonism and intellectual disability; FT uncertain significance; does not affect protein abundance; FT does not affect expression at the cell surface; FT dbSNP:rs748346254)" FT /evidence="ECO:0000269|PubMed:27134041" FT /id="VAR_078549" FT CONFLICT 312 FT /note="A -> T (in Ref. 7; BAF82617)" FT /evidence="ECO:0000305" FT HELIX 7..36 FT /evidence="ECO:0007829|PDB:5UEN" FT HELIX 38..40 FT /evidence="ECO:0007829|PDB:5UEN" FT HELIX 43..60 FT /evidence="ECO:0007829|PDB:5UEN" FT HELIX 62..71 FT /evidence="ECO:0007829|PDB:5UEN" FT STRAND 74..76 FT /evidence="ECO:0007829|PDB:7LD3" FT HELIX 77..110 FT /evidence="ECO:0007829|PDB:5UEN" FT TURN 112..114 FT /evidence="ECO:0007829|PDB:5UEN" FT HELIX 115..118 FT /evidence="ECO:0007829|PDB:5UEN" FT HELIX 121..140 FT /evidence="ECO:0007829|PDB:5UEN" FT HELIX 141..144 FT /evidence="ECO:0007829|PDB:5UEN" FT HELIX 149..159 FT /evidence="ECO:0007829|PDB:5UEN" FT STRAND 166..168 FT /evidence="ECO:0007829|PDB:7LD3" FT HELIX 171..174 FT /evidence="ECO:0007829|PDB:5UEN" FT HELIX 177..182 FT /evidence="ECO:0007829|PDB:5UEN" FT HELIX 184..188 FT /evidence="ECO:0007829|PDB:5UEN" FT HELIX 190..211 FT /evidence="ECO:0007829|PDB:5UEN" FT HELIX 228..259 FT /evidence="ECO:0007829|PDB:5UEN" FT HELIX 267..291 FT /evidence="ECO:0007829|PDB:5UEN" FT HELIX 293..306 FT /evidence="ECO:0007829|PDB:5UEN" SQ SEQUENCE 326 AA; 36512 MW; 1B555893BCDEC9A6 CRC64; MPPSISAFQA AYIGIEVLIA LVSVPGNVLV IWAVKVNQAL RDATFCFIVS LAVADVAVGA LVIPLAILIN IGPQTYFHTC LMVACPVLIL TQSSILALLA IAVDRYLRVK IPLRYKMVVT PRRAAVAIAG CWILSFVVGL TPMFGWNNLS AVERAWAANG SMGEPVIKCE FEKVISMEYM VYFNFFVWVL PPLLLMVLIY LEVFYLIRKQ LNKKVSASSG DPQKYYGKEL KIAKSLALIL FLFALSWLPL HILNCITLFC PSCHKPSILT YIAIFLTHGN SAMNPIVYAF RIQKFRVTFL KIWNDHFRCQ PAPPIDEDLP EERPDD // ID IF4G1_HUMAN Reviewed; 1599 AA. AC Q04637; D3DNT2; D3DNT4; D3DNT5; E9PFM1; G5E9S1; O43177; O95066; Q5HYG0; AC Q6ZN21; Q8N102; DT 01-FEB-1995, integrated into UniProtKB/Swiss-Prot. DT 20-APR-2010, sequence version 4. DT 28-JAN-2026, entry version 251. DE RecName: Full=Eukaryotic translation initiation factor 4 gamma 1; DE Short=eIF-4-gamma 1; DE Short=eIF-4G 1; DE Short=eIF-4G1; DE AltName: Full=p220; GN Name=EIF4G1; Synonyms=EIF4F, EIF4G, EIF4GI; OS Homo sapiens (Human). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia; OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae; OC Homo. OX NCBI_TaxID=9606; RN [1] RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 7), AND VARIANT VAL-432. RC TISSUE=Brain; RX PubMed=1429670; DOI=10.1016/s0021-9258(18)50080-6; RA Yan R., Rychlik W., Etchison D., Rhoads R.E.; RT "Amino acid sequence of the human protein synthesis initiation factor eIF-4 RT gamma."; RL J. Biol. Chem. 267:23226-23231(1992). RN [2] RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM B), AND INTERACTION WITH PABPC1. RX PubMed=9857202; DOI=10.1093/emboj/17.24.7480; RA Imataka H., Gradi A., Sonenberg N.; RT "A newly identified N-terminal amino acid sequence of human eIF4G binds RT poly(A)-binding protein and functions in poly(A)-dependent translation."; RL EMBO J. 17:7480-7489(1998). RN [3] RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM C). RX PubMed=9418880; DOI=10.1128/mcb.18.1.334; RA Gradi A., Imataka H., Svitkin Y.V., Rom E., Raught B., Morino S., RA Sonenberg N.; RT "A novel functional human eukaryotic translation initiation factor 4G."; RL Mol. Cell. Biol. 18:334-342(1998). RN [4] RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 8), VARIANTS ALA-161 AND VAL-432, AND RP ALTERNATIVE INITIATION. RX PubMed=12052860; DOI=10.1128/mcb.22.13.4499-4511.2002; RA Byrd M.P., Zamora M., Lloyd R.E.; RT "Generation of multiple isoforms of eukaryotic translation initiation RT factor 4GI by use of alternate translation initiation codons."; RL Mol. Cell. Biol. 22:4499-4511(2002). RN [5] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM A). RX PubMed=14702039; DOI=10.1038/ng1285; RA Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., RA Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., RA Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S., RA Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., RA Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H., RA Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., RA Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., RA Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., RA Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., RA Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., RA Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., RA Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., RA Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., RA Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., RA Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., RA Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., RA Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., RA Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y., RA Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., RA Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., RA Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., RA Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., RA Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., RA Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., RA Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., RA Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., RA Isogai T., Sugano S.; RT "Complete sequencing and characterization of 21,243 full-length human RT cDNAs."; RL Nat. Genet. 36:40-45(2004). RN [6] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM A), AND VARIANT ALA-161. RC TISSUE=Endometrial tumor; RX PubMed=17974005; DOI=10.1186/1471-2164-8-399; RA Bechtel S., Rosenfelder H., Duda A., Schmidt C.P., Ernst U., RA Wellenreuther R., Mehrle A., Schuster C., Bahr A., Bloecker H., Heubner D., RA Hoerlein A., Michel G., Wedler H., Koehrer K., Ottenwaelder B., Poustka A., RA Wiemann S., Schupp I.; RT "The full-ORF clone resource of the German cDNA consortium."; RL BMC Genomics 8:399-399(2007). RN [7] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RX PubMed=16641997; DOI=10.1038/nature04728; RA Muzny D.M., Scherer S.E., Kaul R., Wang J., Yu J., Sudbrak R., Buhay C.J., RA Chen R., Cree A., Ding Y., Dugan-Rocha S., Gill R., Gunaratne P., RA Harris R.A., Hawes A.C., Hernandez J., Hodgson A.V., Hume J., Jackson A., RA Khan Z.M., Kovar-Smith C., Lewis L.R., Lozado R.J., Metzker M.L., RA Milosavljevic A., Miner G.R., Morgan M.B., Nazareth L.V., Scott G., RA Sodergren E., Song X.-Z., Steffen D., Wei S., Wheeler D.A., Wright M.W., RA Worley K.C., Yuan Y., Zhang Z., Adams C.Q., Ansari-Lari M.A., Ayele M., RA Brown M.J., Chen G., Chen Z., Clendenning J., Clerc-Blankenburg K.P., RA Chen R., Chen Z., Davis C., Delgado O., Dinh H.H., Dong W., Draper H., RA Ernst S., Fu G., Gonzalez-Garay M.L., Garcia D.K., Gillett W., Gu J., RA Hao B., Haugen E., Havlak P., He X., Hennig S., Hu S., Huang W., RA Jackson L.R., Jacob L.S., Kelly S.H., Kube M., Levy R., Li Z., Liu B., RA Liu J., Liu W., Lu J., Maheshwari M., Nguyen B.-V., Okwuonu G.O., RA Palmeiri A., Pasternak S., Perez L.M., Phelps K.A., Plopper F.J., Qiang B., RA Raymond C., Rodriguez R., Saenphimmachak C., Santibanez J., Shen H., RA Shen Y., Subramanian S., Tabor P.E., Verduzco D., Waldron L., Wang J., RA Wang J., Wang Q., Williams G.A., Wong G.K.-S., Yao Z., Zhang J., Zhang X., RA Zhao G., Zhou J., Zhou Y., Nelson D., Lehrach H., Reinhardt R., RA Naylor S.L., Yang H., Olson M., Weinstock G., Gibbs R.A.; RT "The DNA sequence, annotation and analysis of human chromosome 3."; RL Nature 440:1194-1198(2006). RN [8] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RA Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M., RA Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J., RA Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S., RA Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H., RA Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K., RA Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D., RA Hunkapiller M.W., Myers E.W., Venter J.C.; RL Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases. RN [9] RP NUCLEOTIDE SEQUENCE [MRNA] OF 30-206, NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF RP 180-234, VARIANT ALA-161, AND INTERACTION WITH ROTAVIRAL NSP3. RX PubMed=9755181; DOI=10.1093/emboj/17.19.5811; RA Piron M., Vende P., Cohen J., Poncet D.; RT "Rotavirus RNA binding protein NSP3, interacts with eIF-4GI and evicts the RT poly(A) binding protein from eIF4F."; RL EMBO J. 17:5811-5821(1998). RN [10] RP NUCLEOTIDE SEQUENCE [MRNA] OF 37-1599 (ISOFORM 8), INTERACTION WITH EIF4A, RP VARIANTS ALA-161 AND VAL-432, AND MUTAGENESIS OF LEU-768; LEU-771; PHE-776; RP 842-LEU-LEU-843; 851-PHE-GLU-852; LEU-896; ILE-902; LEU-905; ARG-974; RP PHE-977; LEU-985 AND TRP-990. RX PubMed=9372926; DOI=10.1128/mcb.17.12.6940; RA Imataka H., Sonenberg N.; RT "Human eukaryotic translation initiation factor 4G (eIF4G) possesses two RT separate and independent binding sites for eIF4A."; RL Mol. Cell. Biol. 17:6940-6947(1997). RN [11] RP NUCLEOTIDE SEQUENCE [MRNA] OF 605-721, INTERACTION WITH EIF4E, AND RP MUTAGENESIS OF TYR-612 AND 617-LEU-LEU-618. RX PubMed=7651417; DOI=10.1128/mcb.15.9.4990; RA Mader S., Lee H., Pause A., Sonenberg N.; RT "The translation initiation factor eIF-4E binds to a common motif shared by RT the translation factor eIF-4 gamma and the translational repressors 4E- RT binding proteins."; RL Mol. Cell. Biol. 15:4990-4997(1995). RN [12] RP NUCLEOTIDE SEQUENCE [MRNA] OF 682-912 (ISOFORM 8). RA De Gregorio E.; RL Submitted (AUG-1997) to the EMBL/GenBank/DDBJ databases. RN [13] RP CLEAVAGE BY RHINOVIRUS AND COXSACKIEVIRUS PROTEASE. RX PubMed=8396129; DOI=10.1016/s0021-9258(19)36499-3; RA Lamphear B.J., Yan R., Yang F., Waters D., Liebig H.-D., Klump H., RA Kuechler E., Skern T., Rhoads R.E.; RT "Mapping the cleavage site in protein synthesis initiation factor eIF-4 RT gamma of the 2A proteases from human Coxsackievirus and rhinovirus."; RL J. Biol. Chem. 268:19200-19203(1993). RN [14] RP INTERACTION WITH EIF4E. RC TISSUE=Placenta; RX PubMed=7935836; DOI=10.1038/371762a0; RA Pause A., Belsham G.J., Gingras A.-C., Donze O., Lin T.-A., RA Lawrence J.C. Jr., Sonenberg N.; RT "Insulin-dependent stimulation of protein synthesis by phosphorylation of a RT regulator of 5'-cap function."; RL Nature 371:762-767(1994). RN [15] RP INTERACTION WITH EIF4E AND EIF4EBP1. RX PubMed=8521827; DOI=10.1002/j.1460-2075.1995.tb00257.x; RA Haghighat A., Mader S., Pause A., Sonenberg N.; RT "Repression of cap-dependent translation by 4E-binding protein 1: RT competition with p220 for binding to eukaryotic initiation factor-4E."; RL EMBO J. 14:5701-5709(1995). RN [16] RP MUTAGENESIS OF GLY-682. RX PubMed=8961935; DOI=10.1021/bi961864t; RA Lamphear B.J., Rhoads R.E.; RT "A single amino acid change in protein synthesis initiation factor 4G RT renders cap-dependent translation resistant to picornaviral 2A proteases."; RL Biochemistry 35:15726-15733(1996). RN [17] RP CLEAVAGE BY POLIOVIRUS. RX PubMed=9755863; DOI=10.1016/s0014-5793(98)01027-8; RA Ventoso I., MacMillan S.E., Hershey J.W., Carrasco L.; RT "Poliovirus 2A proteinase cleaves directly the eIF-4G subunit of eIF-4F RT complex."; RL FEBS Lett. 435:79-83(1998). RN [18] RP REVIEW. RX PubMed=10872469; DOI=10.1146/annurev.biochem.68.1.913; RA Gingras A.-C., Raught B., Sonenberg N.; RT "eIF4 initiation factors: effectors of mRNA recruitment to ribosomes and RT regulators of translation."; RL Annu. Rev. Biochem. 68:913-963(1999). RN [19] RP INTERACTION WITH MKNK1. RX PubMed=9878069; DOI=10.1093/emboj/18.1.270; RA Pyronnet S., Imataka H., Gingras A.-C., Fukunaga R., Hunter T., RA Sonenberg N.; RT "Human eukaryotic translation initiation factor 4G (eIF4G) recruits mnk1 to RT phosphorylate eIF4E."; RL EMBO J. 18:270-279(1999). RN [20] RP INTERACTION WITH PABPC1, AND MUTAGENESIS OF 174-LYS--LYS-178 AND RP 184-ASP--GLN-197. RX PubMed=10996799; DOI=10.1016/s0960-9822(00)00701-6; RA Wakiyama M., Imataka H., Sonenberg N.; RT "Interaction of eIF4G with poly(A)-binding protein stimulates translation RT and is critical for Xenopus oocyte maturation."; RL Curr. Biol. 10:1147-1150(2000). RN [21] RP INTERACTION WITH PABPC1. RX PubMed=10970864; DOI=10.1093/emboj/19.17.4723; RA Gray N.K., Coller J.M., Dickson K.S., Wickens M.; RT "Multiple portions of poly(A)-binding protein stimulate translation in RT vivo."; RL EMBO J. 19:4723-4733(2000). RN [22] RP CLEAVAGE BY FMDV AND HRV-2. RX PubMed=11034318; DOI=10.1016/s0014-5793(00)01928-1; RA Glaser W., Skern T.; RT "Extremely efficient cleavage of eIF4G by picornaviral proteinases L and 2A RT in vitro."; RL FEBS Lett. 480:151-155(2000). RN [23] RP INTERACTION WITH MKNK2. RX PubMed=11154262; DOI=10.1128/mcb.21.3.743-754.2001; RA Scheper G.C., Morrice N.A., Kleijn M., Proud C.G.; RT "The mitogen-activated protein kinase signal-integrating kinase Mnk2 is a RT eukaryotic initiation factor 4E kinase with high levels of basal activity RT in mammalian cells."; RL Mol. Cell. Biol. 21:743-754(2001). RN [24] RP INTERACTION WITH HADV5 100K PROTEIN (MICROBIAL INFECTION). RX PubMed=15314025; DOI=10.1101/gad.1212504; RA Xi Q., Cuesta R., Schneider R.J.; RT "Tethering of eIF4G to adenoviral mRNAs by viral 100k protein drives RT ribosome shunting."; RL Genes Dev. 18:1997-2009(2004). RN [25] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1231, AND IDENTIFICATION BY RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Cervix carcinoma; RX PubMed=17081983; DOI=10.1016/j.cell.2006.09.026; RA Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P., Mann M.; RT "Global, in vivo, and site-specific phosphorylation dynamics in signaling RT networks."; RL Cell 127:635-648(2006). RN [26] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1231, AND IDENTIFICATION BY RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Cervix carcinoma; RX PubMed=16964243; DOI=10.1038/nbt1240; RA Beausoleil S.A., Villen J., Gerber S.A., Rush J., Gygi S.P.; RT "A probability-based approach for high-throughput protein phosphorylation RT analysis and site localization."; RL Nat. Biotechnol. 24:1285-1292(2006). RN [27] RP INTERACTION WITH CIRBP. RX PubMed=16513844; DOI=10.1093/nar/gkj519; RA Yang R., Weber D.J., Carrier F.; RT "Post-transcriptional regulation of thioredoxin by the stress inducible RT heterogeneous ribonucleoprotein A18."; RL Nucleic Acids Res. 34:1224-1236(2006). RN [28] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1092, AND IDENTIFICATION BY RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Cervix carcinoma; RX PubMed=17924679; DOI=10.1021/pr070152u; RA Yu L.R., Zhu Z., Chan K.C., Issaq H.J., Dimitrov D.S., Veenstra T.D.; RT "Improved titanium dioxide enrichment of phosphopeptides from HeLa cells RT and high confident phosphopeptide identification by cross-validation of RT MS/MS and MS/MS/MS spectra."; RL J. Proteome Res. 6:4150-4162(2007). RN [29] RP INTERACTION WITH RBM4. RX PubMed=17284590; DOI=10.1073/pnas.0611015104; RA Lin J.C., Hsu M., Tarn W.Y.; RT "Cell stress modulates the function of splicing regulatory protein RBM4 in RT translation control."; RL Proc. Natl. Acad. Sci. U.S.A. 104:2235-2240(2007). RN [30] RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Platelet; RX PubMed=18088087; DOI=10.1021/pr0704130; RA Zahedi R.P., Lewandrowski U., Wiesner J., Wortelkamp S., Moebius J., RA Schuetz C., Walter U., Gambaryan S., Sickmann A.; RT "Phosphoproteome of resting human platelets."; RL J. Proteome Res. 7:526-534(2008). RN [31] RP INTERACTION WITH ROTAVIRUS A NSP3 (MICROBIAL INFECTION). RX PubMed=18799579; DOI=10.1128/jvi.00872-08; RA Harb M., Becker M.M., Vitour D., Baron C.H., Vende P., Brown S.C., RA Bolte S., Arold S.T., Poncet D.; RT "Nuclear localization of cytoplasmic poly(A)-binding protein upon rotavirus RT infection involves the interaction of NSP3 with eIF4G and RoXaN."; RL J. Virol. 82:11283-11293(2008). RN [32] RP INTERACTION WITH DAZAP2, AND SUBCELLULAR LOCATION. RX PubMed=17984221; DOI=10.1128/mcb.01226-07; RA Kim J.E., Ryu I., Kim W.J., Song O.K., Ryu J., Kwon M.Y., Kim J.H., RA Jang S.K.; RT "Proline-rich transcript in brain protein induces stress granule RT formation."; RL Mol. Cell. Biol. 28:803-813(2008). RN [33] RP INTERACTION WITH MIF4GD. RX PubMed=18025107; DOI=10.1128/mcb.01500-07; RA Cakmakci N.G., Lerner R.S., Wagner E.J., Zheng L., Marzluff W.F.; RT "SLIP1, a factor required for activation of histone mRNA translation by the RT stem-loop binding protein."; RL Mol. Cell. Biol. 28:1182-1194(2008). RN [34] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-207; THR-223; THR-647; RP SER-1092 AND SER-1209, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE RP ANALYSIS]. RC TISSUE=Cervix carcinoma; RX PubMed=18669648; DOI=10.1073/pnas.0805139105; RA Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E., RA Elledge S.J., Gygi S.P.; RT "A quantitative atlas of mitotic phosphorylation."; RL Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008). RN [35] RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RX PubMed=19369195; DOI=10.1074/mcp.m800588-mcp200; RA Oppermann F.S., Gnad F., Olsen J.V., Hornberger R., Greff Z., Keri G., RA Mann M., Daub H.; RT "Large-scale proteomics analysis of the human kinome."; RL Mol. Cell. Proteomics 8:1751-1764(2009). RN [36] RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Leukemic T-cell; RX PubMed=19690332; DOI=10.1126/scisignal.2000007; RA Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K., RA Rodionov V., Han D.K.; RT "Quantitative phosphoproteomic analysis of T cell receptor signaling RT reveals system-wide modulation of protein-protein interactions."; RL Sci. Signal. 2:RA46-RA46(2009). RN [37] RP ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-1095, AND IDENTIFICATION BY MASS RP SPECTROMETRY [LARGE SCALE ANALYSIS]. RX PubMed=19608861; DOI=10.1126/science.1175371; RA Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T.C., RA Olsen J.V., Mann M.; RT "Lysine acetylation targets protein complexes and co-regulates major RT cellular functions."; RL Science 325:834-840(2009). RN [38] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1028; SER-1092; SER-1185; RP SER-1187; SER-1209; THR-1211; SER-1231 AND SER-1596, AND IDENTIFICATION BY RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Cervix carcinoma; RX PubMed=20068231; DOI=10.1126/scisignal.2000475; RA Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L., RA Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S., Mann M.; RT "Quantitative phosphoproteomics reveals widespread full phosphorylation RT site occupancy during mitosis."; RL Sci. Signal. 3:RA3-RA3(2010). RN [39] RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RX PubMed=21269460; DOI=10.1186/1752-0509-5-17; RA Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T., RA Bennett K.L., Superti-Furga G., Colinge J.; RT "Initial characterization of the human central proteome."; RL BMC Syst. Biol. 5:17-17(2011). RN [40] RP PHOSPHORYLATION AT SER-1185. RX PubMed=21576361; DOI=10.1128/mcb.05589-11; RA Dobrikov M., Dobrikova E., Shveygert M., Gromeier M.; RT "Phosphorylation of eukaryotic translation initiation factor 4G1 (eIF4G1) RT by protein kinase C{alpha} regulates eIF4G1 binding to Mnk1."; RL Mol. Cell. Biol. 31:2947-2959(2011). RN [41] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1028; SER-1092; SER-1145; RP SER-1147; SER-1185; SER-1187; SER-1209; THR-1211; SER-1231 AND SER-1596, RP AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RX PubMed=21406692; DOI=10.1126/scisignal.2001570; RA Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J., Johansen P.T., RA Kratchmarova I., Kassem M., Mann M., Olsen J.V., Blagoev B.; RT "System-wide temporal characterization of the proteome and phosphoproteome RT of human embryonic stem cell differentiation."; RL Sci. Signal. 4:RS3-RS3(2011). RN [42] RP INTERACTION WITH DDX3X, AND SUBCELLULAR LOCATION. RX PubMed=22872150; DOI=10.1038/emboj.2012.220; RA Soto-Rifo R., Rubilar P.S., Limousin T., de Breyne S., Decimo D., RA Ohlmann T.; RT "DEAD-box protein DDX3 associates with eIF4F to promote translation of RT selected mRNAs."; RL EMBO J. 31:3745-3756(2012). RN [43] RP ACETYLATION [LARGE SCALE ANALYSIS] AT MET-2 (ISOFORM C), CLEAVAGE OF RP INITIATOR METHIONINE [LARGE SCALE ANALYSIS] (ISOFORM C), AND IDENTIFICATION RP BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RX PubMed=22814378; DOI=10.1073/pnas.1210303109; RA Van Damme P., Lasa M., Polevoda B., Gazquez C., Elosegui-Artola A., RA Kim D.S., De Juan-Pardo E., Demeyer K., Hole K., Larrea E., Timmerman E., RA Prieto J., Arnesen T., Sherman F., Gevaert K., Aldabe R.; RT "N-terminal acetylome analyses and functional insights of the N-terminal RT acetyltransferase NatB."; RL Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012). RN [44] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-207; THR-647; SER-1028; RP SER-1077; SER-1092; SER-1145; SER-1147; SER-1185; SER-1187; SER-1194; RP SER-1209; SER-1231; SER-1238 AND SER-1596, PHOSPHORYLATION [LARGE SCALE RP ANALYSIS] AT SER-509 (ISOFORM 7), PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT RP SER-705 (ISOFORM 8), AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE RP ANALYSIS]. RC TISSUE=Cervix carcinoma, and Erythroleukemia; RX PubMed=23186163; DOI=10.1021/pr300630k; RA Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J., RA Mohammed S.; RT "Toward a comprehensive characterization of a human cancer cell RT phosphoproteome."; RL J. Proteome Res. 12:260-271(2013). RN [45] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-314, AND IDENTIFICATION BY RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Liver; RX PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014; RA Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., Wang L., RA Ye M., Zou H.; RT "An enzyme assisted RP-RPLC approach for in-depth analysis of human liver RT phosphoproteome."; RL J. Proteomics 96:253-262(2014). RN [46] RP METHYLATION [LARGE SCALE ANALYSIS] AT ARG-73; ARG-110; ARG-685; ARG-694; RP ARG-1032 AND ARG-1042, METHYLATION [LARGE SCALE ANALYSIS] AT ARG-489 AND RP ARG-498 (ISOFORM 7), METHYLATION [LARGE SCALE ANALYSIS] AT ARG-685 AND RP ARG-694 (ISOFORM 8), AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE RP ANALYSIS]. RC TISSUE=Colon carcinoma; RX PubMed=24129315; DOI=10.1074/mcp.o113.027870; RA Guo A., Gu H., Zhou J., Mulhern D., Wang Y., Lee K.A., Yang V., Aguiar M., RA Kornhauser J., Jia X., Ren J., Beausoleil S.A., Silva J.C., Vemulapalli V., RA Bedford M.T., Comb M.J.; RT "Immunoaffinity enrichment and mass spectrometry analysis of protein RT methylation."; RL Mol. Cell. Proteomics 13:372-387(2014). RN [47] RP INTERACTION WITH HNRNPD, AND RNA-BINDING. RX PubMed=24423872; DOI=10.1093/nar/gkt1379; RA Lee K.H., Kim S.H., Kim H.J., Kim W., Lee H.R., Jung Y., Choi J.H., RA Hong K.Y., Jang S.K., Kim K.T.; RT "AUF1 contributes to Cryptochrome1 mRNA degradation and rhythmic RT translation."; RL Nucleic Acids Res. 42:3590-3606(2014). RN [48] RP FUNCTION. RX PubMed=29062139; DOI=10.1038/s41598-017-14262-7; RA Adjibade P., Grenier St-Sauveur V., Bergeman J., Huot M.E., Khandjian E.W., RA Mazroui R.; RT "DDX3 regulates endoplasmic reticulum stress-induced ATF4 expression."; RL Sci. Rep. 7:13832-13832(2017). RN [49] RP FUNCTION, AND INTERACTION WITH EIF1 AND EIF4E. RX PubMed=29987188; DOI=10.1128/mcb.00139-18; RA Haimov O., Sehrawat U., Tamarkin-Ben Harush A., Bahat A., Uzonyi A., RA Will A., Hiraishi H., Asano K., Dikstein R.; RT "Dynamic interaction of eukaryotic initiation factor 4G1 (eIF4G1) with RT eIF4E and eIF1 underlies scanning-dependent and -independent translation."; RL Mol. Cell. Biol. 38:0-0(2018). RN [50] RP INTERACTION WITH HUMAN NOROVIRUS VIRAL GENOME-LINKED PROTEIN (MICROBIAL RP INFECTION). RX PubMed=31403400; DOI=10.7554/elife.46681; RA Hosmillo M., Lu J., McAllaster M.R., Eaglesham J.B., Wang X., Emmott E., RA Domingues P., Chaudhry Y., Fitzmaurice T.J., Tung M.K., Panas M.D., RA McInerney G., Locker N., Wilen C.B., Goodfellow I.G.; RT "Noroviruses subvert the core stress granule component G3BP1 to promote RT viral VPg-dependent translation."; RL Elife 8:0-0(2019). RN [51] RP VARIANT [LARGE SCALE ANALYSIS] VAL-432, AND IDENTIFICATION BY MASS RP SPECTROMETRY [LARGE SCALE ANALYSIS]. RX PubMed=19413330; DOI=10.1021/ac9004309; RA Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J., Mohammed S.; RT "Lys-N and trypsin cover complementary parts of the phosphoproteome in a RT refined SCX-based approach."; RL Anal. Chem. 81:4493-4501(2009). RN [52] RP VARIANT HIS-201. RX PubMed=26740508; DOI=10.1136/jmedgenet-2015-103568; RA Lopes F., Barbosa M., Ameur A., Soares G., de Sa J., Dias A.I., RA Oliveira G., Cabral P., Temudo T., Calado E., Cruz I.F., Vieira J.P., RA Oliveira R., Esteves S., Sauer S., Jonasson I., Syvaenen A.C., RA Gyllensten U., Pinto D., Maciel P.; RT "Identification of novel genetic causes of Rett syndrome-like phenotypes."; RL J. Med. Genet. 53:190-199(2016). RN [53] RP X-RAY CRYSTALLOGRAPHY (2.38 ANGSTROMS) OF 172-199 IN COMPLEX WITH ROTAVIRAL RP NSP3, INTERACTION WITH PABPC1, AND MUTAGENESIS OF ILE-180; ILE-182; ILE-192 RP AND ILE-196. RX PubMed=12086624; DOI=10.1016/s1097-2765(02)00555-5; RA Groft C.M., Burley S.K.; RT "Recognition of eIF4G by rotavirus NSP3 reveals a basis for mRNA RT circularization."; RL Mol. Cell 9:1273-1283(2002). RN [54] RP X-RAY CRYSTALLOGRAPHY (2.24 ANGSTROMS) OF 1234-1571. RX PubMed=16698552; DOI=10.1016/j.str.2006.03.012; RA Bellsolell L., Cho-Park P.F., Poulin F., Sonenberg N., Burley S.K.; RT "Two structurally atypical HEAT domains in the C-terminal portion of human RT eIF4G support binding to eIF4A and Mnk1."; RL Structure 14:913-923(2006). RN [55] RP VARIANT [LARGE SCALE ANALYSIS] LEU-696. RX PubMed=16959974; DOI=10.1126/science.1133427; RA Sjoeblom T., Jones S., Wood L.D., Parsons D.W., Lin J., Barber T.D., RA Mandelker D., Leary R.J., Ptak J., Silliman N., Szabo S., Buckhaults P., RA Farrell C., Meeh P., Markowitz S.D., Willis J., Dawson D., Willson J.K.V., RA Gazdar A.F., Hartigan J., Wu L., Liu C., Parmigiani G., Park B.H., RA Bachman K.E., Papadopoulos N., Vogelstein B., Kinzler K.W., RA Velculescu V.E.; RT "The consensus coding sequences of human breast and colorectal cancers."; RL Science 314:268-274(2006). RN [56] RP VARIANTS PARK18 VAL-502 AND HIS-1205, AND VARIANTS SER-71; ALA-161; RP CYS-311; VAL-432; 466-GLY--ALA-468 DEL; CYS-686; VAL-806; SER-829; RP ARG-1164; TRP-1197; ALA-1229; PRO-1233 AND SER-1257. RX PubMed=21907011; DOI=10.1016/j.ajhg.2011.08.009; RA Chartier-Harlin M.C., Dachsel J.C., Vilarino-Guell C., Lincoln S.J., RA Lepretre F., Hulihan M.M., Kachergus J., Milnerwood A.J., Tapia L., RA Song M.S., Le Rhun E., Mutez E., Larvor L., Duflot A., RA Vanbesien-Mailliot C., Kreisler A., Ross O.A., Nishioka K., RA Soto-Ortolaza A.I., Cobb S.A., Melrose H.L., Behrouz B., Keeling B.H., RA Bacon J.A., Hentati E., Williams L., Yanagiya A., Sonenberg N., RA Lockhart P.J., Zubair A.C., Uitti R.J., Aasly J.O., Krygowska-Wajs A., RA Opala G., Wszolek Z.K., Frigerio R., Maraganore D.M., Gosal D., Lynch T., RA Hutchinson M., Bentivoglio A.R., Valente E.M., Nichols W.C., Pankratz N., RA Foroud T., Gibson R.A., Hentati F., Dickson D.W., Destee A., Farrer M.J.; RT "Translation initiator EIF4G1 mutations in familial Parkinson disease."; RL Am. J. Hum. Genet. 89:398-406(2011). CC -!- FUNCTION: Component of the protein complex eIF4F, which is involved in CC the recognition of the mRNA cap, ATP-dependent unwinding of 5'-terminal CC secondary structure and recruitment of mRNA to the ribosome CC (PubMed:29987188). Exists in two complexes, either with EIF1 or with CC EIF4E (mutually exclusive) (PubMed:29987188). Together with EIF1, is CC required for leaky scanning, in particular for avoiding cap-proximal CC start codon (PubMed:29987188). Together with EIF4E, antagonizes the CC scanning promoted by EIF1-EIF4G1 and locates the start codon (through a CC TISU element) without scanning (PubMed:29987188). As a member of the CC eIF4F complex, required for endoplasmic reticulum stress-induced ATF4 CC mRNA translation (PubMed:29062139). {ECO:0000269|PubMed:29062139, CC ECO:0000269|PubMed:29987188}. CC -!- SUBUNIT: eIF4F is a multi-subunit complex, the composition of which CC varies with external and internal environmental conditions. It is CC composed of at least EIF4A, EIF4E (cap-binding) and EIF4G1/EIF4G3 CC (PubMed:7651417, PubMed:7935836, PubMed:9372926). Interacts with eIF3 CC complex, mutually exclusive with EIF4A1 or EIF4A2, EIF4E and through CC its N-terminus with PABPC1 (PubMed:10970864, PubMed:10996799, CC PubMed:12086624, PubMed:16698552, PubMed:7651417, PubMed:7935836, CC PubMed:9372926, PubMed:9857202). Interacts with EIF4E or with EIF1 CC (mutually exclusive) through a common binding site (PubMed:29987188). CC Interacts through its C-terminus with the serine/threonine kinases CC MKNK1, and with MKNK2 (PubMed:11154262, PubMed:9878069). Appears to act CC as a scaffold protein, holding these enzymes in place to phosphorylate CC EIF4E (PubMed:11154262, PubMed:9878069). Non-phosphorylated EIF4EBP1 CC competes with EIF4G1/EIF4G3 to interact with EIF4E; insulin stimulated CC MAP-kinase (MAPK1 and MAPK3) phosphorylation of EIF4EBP1 causes CC dissociation of the complex allowing EIF4G1/EIF4G3 to bind and CC consequent initiation of translation (PubMed:8521827). EIF4G1/EIF4G3 CC interacts with PABPC1 to bring about circularization of the mRNA CC (PubMed:10970864, PubMed:10996799, PubMed:12086624, PubMed:9857202). CC Interacts with EIF4E3 (By similarity). Interacts with CIRBP and MIF4GD CC (PubMed:10970864, PubMed:10996799, PubMed:16513844, PubMed:18025107). CC Interacts with RBM4 (PubMed:17284590). Interacts with HNRNPD/AUF1; the CC interaction requires RNA (PubMed:24423872). Interacts with DDX3X; the CC interaction requires RNA (PubMed:22872150). Interacts with DAZAP2 CC (PubMed:17984221). {ECO:0000250|UniProtKB:Q6NZJ6, CC ECO:0000269|PubMed:10970864, ECO:0000269|PubMed:10996799, CC ECO:0000269|PubMed:11154262, ECO:0000269|PubMed:12086624, CC ECO:0000269|PubMed:16513844, ECO:0000269|PubMed:17284590, CC ECO:0000269|PubMed:17984221, ECO:0000269|PubMed:18025107, CC ECO:0000269|PubMed:22872150, ECO:0000269|PubMed:24423872, CC ECO:0000269|PubMed:29987188, ECO:0000269|PubMed:7651417, CC ECO:0000269|PubMed:7935836, ECO:0000269|PubMed:8521827, CC ECO:0000269|PubMed:9372926, ECO:0000269|PubMed:9857202, CC ECO:0000269|PubMed:9878069}. CC -!- SUBUNIT: (Microbial infection) Interacts with rotavirus A NSP3; in this CC interaction, NSP3 takes the place of PABPC1 thereby inducing shutoff of CC host protein synthesis. {ECO:0000269|PubMed:18799579, CC ECO:0000269|PubMed:9755181}. CC -!- SUBUNIT: (Microbial infection) Interacts with human adenovirus 5 CC protein 100K; this interaction promotes translational shunt in presence CC of polysomes containing viral tripartite leader mRNAs. CC {ECO:0000269|PubMed:15314025}. CC -!- SUBUNIT: (Microbial infection) Interacts with viral genome-linked CC protein (via c-terminus); this interaction plays a role in the CC translation of viral proteins. {ECO:0000269|PubMed:31403400}. CC -!- INTERACTION: CC Q04637; O00571: DDX3X; NbExp=3; IntAct=EBI-73711, EBI-353779; CC Q04637; P55884: EIF3B; NbExp=2; IntAct=EBI-73711, EBI-366696; CC Q04637; O75822: EIF3J; NbExp=2; IntAct=EBI-73711, EBI-366647; CC Q04637; P60842: EIF4A1; NbExp=18; IntAct=EBI-73711, EBI-73449; CC Q04637; Q14240: EIF4A2; NbExp=4; IntAct=EBI-73711, EBI-73473; CC Q04637; P06730: EIF4E; NbExp=15; IntAct=EBI-73711, EBI-73440; CC Q04637; Q14103-4: HNRNPD; NbExp=3; IntAct=EBI-73711, EBI-432545; CC Q04637; Q9BUB5: MKNK1; NbExp=3; IntAct=EBI-73711, EBI-73837; CC Q04637; P11940: PABPC1; NbExp=6; IntAct=EBI-73711, EBI-81531; CC Q04637; Q9BWF3-1: RBM4; NbExp=4; IntAct=EBI-73711, EBI-15621561; CC Q04637; Q9UGR2: ZC3H7B; NbExp=3; IntAct=EBI-73711, EBI-948845; CC Q04637; Q9J0X9: UL54; Xeno; NbExp=3; IntAct=EBI-73711, EBI-7967856; CC Q04637-1; P60842: EIF4A1; NbExp=2; IntAct=EBI-5456295, EBI-73449; CC Q04637-9; Q9NQ94: A1CF; NbExp=3; IntAct=EBI-12012124, EBI-2809489; CC Q04637-9; Q8N5M1: ATPAF2; NbExp=3; IntAct=EBI-12012124, EBI-1166928; CC Q04637-9; Q2TAC2-2: CCDC57; NbExp=3; IntAct=EBI-12012124, EBI-10961624; CC Q04637-9; P55273: CDKN2D; NbExp=3; IntAct=EBI-12012124, EBI-745859; CC Q04637-9; Q99828: CIB1; NbExp=7; IntAct=EBI-12012124, EBI-372594; CC Q04637-9; P56545-3: CTBP2; NbExp=3; IntAct=EBI-12012124, EBI-10171902; CC Q04637-9; Q86UW9: DTX2; NbExp=3; IntAct=EBI-12012124, EBI-740376; CC Q04637-9; Q9H0I2: ENKD1; NbExp=3; IntAct=EBI-12012124, EBI-744099; CC Q04637-9; P51116: FXR2; NbExp=3; IntAct=EBI-12012124, EBI-740459; CC Q04637-9; Q15323: KRT31; NbExp=3; IntAct=EBI-12012124, EBI-948001; CC Q04637-9; O76011: KRT34; NbExp=3; IntAct=EBI-12012124, EBI-1047093; CC Q04637-9; Q96HA8: NTAQ1; NbExp=3; IntAct=EBI-12012124, EBI-741158; CC Q04637-9; Q9UBV8: PEF1; NbExp=3; IntAct=EBI-12012124, EBI-724639; CC Q04637-9; Q96GM5: SMARCD1; NbExp=3; IntAct=EBI-12012124, EBI-358489; CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:17984221}. Nucleus CC {ECO:0000269|PubMed:17984221}. Cytoplasm, Stress granule CC {ECO:0000269|PubMed:22872150}. CC -!- ALTERNATIVE PRODUCTS: CC Event=Alternative splicing, Alternative initiation; Named isoforms=8; CC Name=A; CC IsoId=Q04637-1; Sequence=Displayed; CC Name=B; CC IsoId=Q04637-3; Sequence=VSP_018720; CC Name=C; CC IsoId=Q04637-4; Sequence=VSP_018721; CC Name=D; CC IsoId=Q04637-5; Sequence=VSP_018722; CC Name=E; CC IsoId=Q04637-6; Sequence=VSP_018723; CC Name=7; CC IsoId=Q04637-7; Sequence=VSP_018723, VSP_047397; CC Name=8; CC IsoId=Q04637-8; Sequence=VSP_047397; CC Name=9; CC IsoId=Q04637-9; Sequence=VSP_047396; CC -!- PTM: Phosphorylated at multiple sites in vivo. Phosphorylation at Ser- CC 1185 by PRKCA induces binding to MKNK1. {ECO:0000269|PubMed:21576361}. CC -!- PTM: Following infection by certain enteroviruses, rhinoviruses and CC aphthoviruses, EIF4G1 is cleaved by the viral protease 2A, or the CC leader protease in the case of aphthoviruses. This shuts down the CC capped cellular mRNA transcription. {ECO:0000269|PubMed:11034318, CC ECO:0000269|PubMed:8396129, ECO:0000269|PubMed:9755863}. CC -!- DISEASE: Parkinson disease 18 (PARK18) [MIM:614251]: An autosomal CC dominant, late-onset form of Parkinson disease. Parkinson disease is a CC complex neurodegenerative disorder characterized by bradykinesia, CC resting tremor, muscular rigidity and postural instability, as well as CC by a clinically significant response to treatment with levodopa. The CC pathology involves the loss of dopaminergic neurons in the substantia CC nigra and the presence of Lewy bodies (intraneuronal accumulations of CC aggregated proteins), in surviving neurons in various areas of the CC brain. {ECO:0000269|PubMed:21907011}. Note=The disease is caused by CC variants affecting the gene represented in this entry. CC -!- MISCELLANEOUS: [Isoform B]: Produced by alternative initiation at Met- CC 41 of isoform A. {ECO:0000305}. CC -!- MISCELLANEOUS: [Isoform C]: Produced by alternative initiation at Met- CC 88 of isoform A. {ECO:0000305}. CC -!- MISCELLANEOUS: [Isoform D]: Produced by alternative initiation at Met- CC 165 of isoform A. {ECO:0000305}. CC -!- MISCELLANEOUS: [Isoform E]: Produced by alternative initiation at Met- CC 197 of isoform A. {ECO:0000305}. CC -!- MISCELLANEOUS: [Isoform 7]: Produced by alternative splicing. CC {ECO:0000305}. CC -!- MISCELLANEOUS: [Isoform 8]: Produced by alternative splicing. CC {ECO:0000305}. CC -!- MISCELLANEOUS: [Isoform 9]: Produced by alternative splicing. CC {ECO:0000305}. CC -!- SIMILARITY: Belongs to the eukaryotic initiation factor 4G family. CC {ECO:0000305}. CC -!- SEQUENCE CAUTION: CC Sequence=AAC78444.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305}; CC Sequence=AAC82471.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305}; CC Sequence=BAA02185.1; Type=Frameshift; Evidence={ECO:0000305}; CC Sequence=BAD18554.1; Type=Miscellaneous discrepancy; Note=Aberrant splicing.; Evidence={ECO:0000305}; CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; D12686; BAA02185.1; ALT_FRAME; mRNA. DR EMBL; AY082886; AAL92872.1; -; mRNA. DR EMBL; AF281070; AAM69365.1; -; mRNA. DR EMBL; AK131407; BAD18554.1; ALT_SEQ; mRNA. DR EMBL; BX647812; CAI46013.1; -; mRNA. DR EMBL; AC078797; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; CH471052; EAW78257.1; -; Genomic_DNA. DR EMBL; CH471052; EAW78259.1; -; Genomic_DNA. DR EMBL; CH471052; EAW78262.1; -; Genomic_DNA. DR EMBL; CH471052; EAW78263.1; -; Genomic_DNA. DR EMBL; CH471052; EAW78264.1; -; Genomic_DNA. DR EMBL; CH471052; EAW78265.1; -; Genomic_DNA. DR EMBL; CH471052; EAW78266.1; -; Genomic_DNA. DR EMBL; CH471052; EAW78267.1; -; Genomic_DNA. DR EMBL; AF002816; AAC78443.1; -; mRNA. DR EMBL; AF004836; AAC78444.1; ALT_INIT; Genomic_DNA. DR EMBL; AF104913; AAC82471.1; ALT_INIT; mRNA. DR EMBL; AJ001046; CAA04500.1; -; mRNA. DR CCDS; CCDS3259.1; -. [Q04637-1] DR CCDS; CCDS3260.1; -. [Q04637-4] DR CCDS; CCDS3261.1; -. [Q04637-5] DR CCDS; CCDS46970.2; -. [Q04637-7] DR CCDS; CCDS54687.1; -. [Q04637-9] DR CCDS; CCDS54688.1; -. [Q04637-8] DR CCDS; CCDS77866.1; -. [Q04637-3] DR PIR; A44453; A44453. DR RefSeq; NP_001181875.2; NM_001194946.2. [Q04637-9] DR RefSeq; NP_001181876.2; NM_001194947.2. [Q04637-9] DR RefSeq; NP_001278086.2; NM_001291157.2. [Q04637-3] DR RefSeq; NP_004944.3; NM_004953.4. [Q04637-7] DR RefSeq; NP_886553.3; NM_182917.4. DR RefSeq; NP_937884.2; NM_198241.3. [Q04637-1] DR RefSeq; NP_937885.1; NM_198242.3. [Q04637-5] DR RefSeq; NP_937887.2; NM_198244.3. [Q04637-4] DR PDB; 1LJ2; X-ray; 2.38 A; C/D=172-199. DR PDB; 1UG3; X-ray; 2.24 A; A/B=1233-1571. DR PDB; 2W97; X-ray; 2.29 A; E/F=609-622. DR PDB; 4AZA; X-ray; 2.16 A; B/D=609-620. DR PDB; 4F02; X-ray; 2.00 A; C/F=178-203. DR PDB; 5EHC; X-ray; 2.40 A; B=609-622. DR PDB; 5EI3; X-ray; 1.71 A; B=609-622. DR PDB; 5EIR; X-ray; 2.69 A; B=609-622. DR PDB; 5T46; X-ray; 1.53 A; B/D=592-653. DR PDB; 5ZK5; X-ray; 2.25 A; B=609-623. DR PDB; 6ZMW; EM; 3.70 A; g=290-1599. DR PDB; 8HUJ; EM; 3.76 A; B=746-992. DR PDB; 8J7R; EM; 3.70 A; B=746-992. DR PDB; 8OZ0; EM; 3.50 A; 2=197-1599. DR PDBsum; 1LJ2; -. DR PDBsum; 1UG3; -. DR PDBsum; 2W97; -. DR PDBsum; 4AZA; -. DR PDBsum; 4F02; -. DR PDBsum; 5EHC; -. DR PDBsum; 5EI3; -. DR PDBsum; 5EIR; -. DR PDBsum; 5T46; -. DR PDBsum; 5ZK5; -. DR PDBsum; 6ZMW; -. DR PDBsum; 8HUJ; -. DR PDBsum; 8J7R; -. DR PDBsum; 8OZ0; -. DR AlphaFoldDB; Q04637; -. DR BMRB; Q04637; -. DR EMDB; EMD-11302; -. DR EMDB; EMD-17297; -. DR EMDB; EMD-35041; -. DR EMDB; EMD-36046; -. DR SMR; Q04637; -. DR BioGRID; 108296; 468. DR ComplexPortal; CPX-2666; Eukaryotic translation initiation factor 4F, EIF4A1 and EIF4G1 variant. DR ComplexPortal; CPX-5634; Eukaryotic translation initiation factor 4F, EIF4A2 and EIF4G1 variant. DR CORUM; Q04637; -. DR DIP; DIP-1161N; -. DR ELM; Q04637; -. DR FunCoup; Q04637; 2647. DR IntAct; Q04637; 183. DR MINT; Q04637; -. DR STRING; 9606.ENSP00000416255; -. DR BindingDB; Q04637; -. DR ChEMBL; CHEMBL4523621; -. DR MoonProt; Q04637; -. DR GlyConnect; 2847; 1 O-GlcNAc glycan (1 site). DR GlyCosmos; Q04637; 6 sites, 1 glycan. DR GlyGen; Q04637; 24 sites, 1 N-linked glycan (1 site), 1 O-linked glycan (19 sites). DR iPTMnet; Q04637; -. DR MetOSite; Q04637; -. DR PhosphoSitePlus; Q04637; -. DR SwissPalm; Q04637; -. DR BioMuta; EIF4G1; -. DR DMDM; 294862538; -. DR jPOST; Q04637; -. DR MassIVE; Q04637; -. DR PaxDb; 9606-ENSP00000416255; -. DR PeptideAtlas; Q04637; -. DR ProteomicsDB; 20132; -. DR ProteomicsDB; 34026; -. DR ProteomicsDB; 58250; -. [Q04637-1] DR ProteomicsDB; 58251; -. [Q04637-3] DR ProteomicsDB; 58252; -. [Q04637-4] DR ProteomicsDB; 58253; -. [Q04637-5] DR ProteomicsDB; 58254; -. [Q04637-6] DR Pumba; Q04637; -. DR Antibodypedia; 3406; 617 antibodies from 40 providers. DR DNASU; 1981; -. DR Ensembl; ENST00000342981.8; ENSP00000343450.4; ENSG00000114867.23. [Q04637-8] DR Ensembl; ENST00000346169.7; ENSP00000316879.5; ENSG00000114867.23. [Q04637-1] DR Ensembl; ENST00000350481.9; ENSP00000317600.8; ENSG00000114867.23. [Q04637-5] DR Ensembl; ENST00000352767.7; ENSP00000338020.4; ENSG00000114867.23. [Q04637-9] DR Ensembl; ENST00000382330.7; ENSP00000371767.3; ENSG00000114867.23. [Q04637-9] DR Ensembl; ENST00000392537.6; ENSP00000376320.2; ENSG00000114867.23. [Q04637-4] DR Ensembl; ENST00000414031.5; ENSP00000391935.1; ENSG00000114867.23. [Q04637-3] DR Ensembl; ENST00000424196.5; ENSP00000416255.1; ENSG00000114867.23. [Q04637-9] DR Ensembl; ENST00000434061.6; ENSP00000411826.2; ENSG00000114867.23. [Q04637-7] DR GeneID; 1981; -. DR KEGG; hsa:1981; -. DR MANE-Select; ENST00000346169.7; ENSP00000316879.5; NM_198241.3; NP_937884.2. DR UCSC; uc003fnp.4; human. [Q04637-1] DR AGR; HGNC:3296; -. DR ClinPGx; PA27722; -. DR CTD; 1981; -. DR DisGeNET; 1981; -. DR GeneCards; EIF4G1; -. DR HGNC; HGNC:3296; EIF4G1. DR HPA; ENSG00000114867; Tissue enhanced (skeletal). DR MalaCards; EIF4G1; -. DR MIM; 600495; gene. DR MIM; 614251; phenotype. DR OpenTargets; ENSG00000114867; -. DR Orphanet; 411602; Hereditary late-onset Parkinson disease. DR VEuPathDB; HostDB:ENSG00000114867; -. DR eggNOG; KOG0401; Eukaryota. DR GeneTree; ENSGT00940000154648; -. DR HOGENOM; CLU_001519_2_0_1; -. DR InParanoid; Q04637; -. DR OMA; PRGGPNM; -. DR OrthoDB; 514777at2759; -. DR PAN-GO; Q04637; 3 GO annotations based on evolutionary models. DR PhylomeDB; Q04637; -. DR PathwayCommons; Q04637; -. DR Reactome; R-HSA-1169408; ISG15 antiviral mechanism. DR Reactome; R-HSA-156827; L13a-mediated translational silencing of Ceruloplasmin expression. DR Reactome; R-HSA-166208; mTORC1-mediated signalling. DR Reactome; R-HSA-429947; Deadenylation of mRNA. DR Reactome; R-HSA-450408; AUF1 (hnRNP D0) binds and destabilizes mRNA. DR Reactome; R-HSA-72649; Translation initiation complex formation. DR Reactome; R-HSA-72662; Activation of the mRNA upon binding of the cap-binding complex and eIFs, and subsequent binding to 43S. DR Reactome; R-HSA-72702; Ribosomal scanning and start codon recognition. DR Reactome; R-HSA-72706; GTP hydrolysis and joining of the 60S ribosomal subunit. DR Reactome; R-HSA-9010553; Regulation of expression of SLITs and ROBOs. DR Reactome; R-HSA-975956; Nonsense Mediated Decay (NMD) independent of the Exon Junction Complex (EJC). DR Reactome; R-HSA-975957; Nonsense Mediated Decay (NMD) enhanced by the Exon Junction Complex (EJC). DR Reactome; R-HSA-9820841; M-decay: degradation of maternal mRNAs by maternally stored factors. DR Reactome; R-HSA-9820865; Z-decay: degradation of maternal mRNAs by zygotically expressed factors. DR SignaLink; Q04637; -. DR SIGNOR; Q04637; -. DR Agora; ENSG00000114867; -. DR BioGRID-ORCS; 1981; 612 hits in 1167 CRISPR screens. DR CD-CODE; 232F8A39; P-body. DR CD-CODE; DEE660B4; Stress granule. DR CD-CODE; E1879998; Synthetic Condensate 000375. DR CD-CODE; FB4E32DD; Presynaptic clusters and postsynaptic densities. DR ChiTaRS; EIF4G1; human. DR EvolutionaryTrace; Q04637; -. DR GeneWiki; Eukaryotic_translation_initiation_factor_4_gamma; -. DR GenomeRNAi; 1981; -. DR Pharos; Q04637; Tbio. DR PRO; PR:Q04637; -. DR Proteomes; UP000005640; Chromosome 3. DR RNAct; Q04637; protein. DR Bgee; ENSG00000114867; Expressed in gastrocnemius and 206 other cell types or tissues. DR ExpressionAtlas; Q04637; baseline and differential. DR GO; GO:0005737; C:cytoplasm; IDA:AgBase. DR GO; GO:0010494; C:cytoplasmic stress granule; IDA:UniProtKB. DR GO; GO:0005829; C:cytosol; IDA:HPA. DR GO; GO:0016281; C:eukaryotic translation initiation factor 4F complex; IDA:ParkinsonsUK-UCL. DR GO; GO:0016020; C:membrane; HDA:UniProtKB. DR GO; GO:0005634; C:nucleus; IDA:UniProtKB. DR GO; GO:0005840; C:ribosome; IMP:ParkinsonsUK-UCL. DR GO; GO:0005524; F:ATP binding; IDA:ParkinsonsUK-UCL. DR GO; GO:0008190; F:eukaryotic initiation factor 4E binding; IDA:AgBase. DR GO; GO:0060090; F:molecular adaptor activity; TAS:ParkinsonsUK-UCL. DR GO; GO:0003729; F:mRNA binding; IDA:ParkinsonsUK-UCL. DR GO; GO:0003723; F:RNA binding; HDA:UniProtKB. DR GO; GO:0008135; F:translation factor activity, RNA binding; IMP:ParkinsonsUK-UCL. DR GO; GO:0003743; F:translation initiation factor activity; IDA:UniProtKB. DR GO; GO:0031369; F:translation initiation factor binding; TAS:ParkinsonsUK-UCL. DR GO; GO:0001662; P:behavioral fear response; IEA:Ensembl. DR GO; GO:0002191; P:cap-dependent translational initiation; TAS:ParkinsonsUK-UCL. DR GO; GO:0031669; P:cellular response to nutrient levels; IMP:ParkinsonsUK-UCL. DR GO; GO:0097009; P:energy homeostasis; IMP:ParkinsonsUK-UCL. DR GO; GO:0035278; P:miRNA-mediated gene silencing by inhibition of translation; IDA:ParkinsonsUK-UCL. DR GO; GO:0010507; P:negative regulation of autophagy; IMP:ParkinsonsUK-UCL. DR GO; GO:0030182; P:neuron differentiation; IEA:Ensembl. DR GO; GO:0030307; P:positive regulation of cell growth; IMP:ParkinsonsUK-UCL. DR GO; GO:1905537; P:positive regulation of eukaryotic translation initiation factor 4F complex assembly; IMP:ParkinsonsUK-UCL. DR GO; GO:1900087; P:positive regulation of G1/S transition of mitotic cell cycle; IMP:ParkinsonsUK-UCL. DR GO; GO:0045666; P:positive regulation of neuron differentiation; IEA:Ensembl. DR GO; GO:1904377; P:positive regulation of protein localization to cell periphery; IGI:ParkinsonsUK-UCL. DR GO; GO:0051247; P:positive regulation of protein metabolic process; IMP:ParkinsonsUK-UCL. DR GO; GO:0036493; P:positive regulation of translation in response to endoplasmic reticulum stress; IMP:UniProtKB. DR GO; GO:0080135; P:regulation of cellular response to stress; TAS:ParkinsonsUK-UCL. DR GO; GO:1905606; P:regulation of presynapse assembly; IGI:ARUK-UCL. DR GO; GO:0006446; P:regulation of translational initiation; IMP:UniProtKB. DR GO; GO:0006412; P:translation; IMP:ParkinsonsUK-UCL. DR GO; GO:0006413; P:translational initiation; IDA:UniProtKB. DR CDD; cd11559; W2_eIF4G1_like; 1. DR DisProt; DP02398; -. DR DisProt; DP03499; -. [Q04637-8] DR FunFam; 1.25.40.180:FF:000001; Eukaryotic translation initiation factor 4 gamma, 3, putative; 1. DR FunFam; 1.25.40.180:FF:000002; Eukaryotic translation initiation factor 4 gamma, 3, putative; 1. DR FunFam; 1.25.40.180:FF:000003; Putative eukaryotic translation initiation factor 4 gamma 1; 1. DR Gene3D; 1.25.40.180; -; 3. DR InterPro; IPR016024; ARM-type_fold. DR InterPro; IPR003891; Initiation_fac_eIF4g_MI. DR InterPro; IPR003890; MIF4G-like_typ-3. DR InterPro; IPR003307; W2_domain. DR PANTHER; PTHR23253; EUKARYOTIC TRANSLATION INITIATION FACTOR 4 GAMMA; 1. DR PANTHER; PTHR23253:SF10; EUKARYOTIC TRANSLATION INITIATION FACTOR 4 GAMMA 1; 1. DR Pfam; PF02847; MA3; 1. DR Pfam; PF02854; MIF4G; 1. DR Pfam; PF02020; W2; 1. DR SMART; SM00515; eIF5C; 1. DR SMART; SM00544; MA3; 1. DR SMART; SM00543; MIF4G; 1. DR SUPFAM; SSF48371; ARM repeat; 3. DR PROSITE; PS51366; MI; 1. DR PROSITE; PS51363; W2; 1. PE 1: Evidence at protein level; KW 3D-structure; Acetylation; Alternative initiation; Alternative splicing; KW Cytoplasm; Disease variant; Host-virus interaction; Initiation factor; KW Methylation; Neurodegeneration; Nucleus; Parkinson disease; Parkinsonism; KW Phosphoprotein; Protein biosynthesis; Proteomics identification; KW Reference proteome; RNA-binding; Translation regulation; KW Translational shunt. FT CHAIN 1..1599 FT /note="Eukaryotic translation initiation factor 4 gamma 1" FT /id="PRO_0000007786" FT DOMAIN 565..792 FT /note="MIF4G" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00698" FT DOMAIN 1241..1363 FT /note="MI" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00698" FT DOMAIN 1433..1599 FT /note="W2" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00695" FT REGION 1..77 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 166..222 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 172..200 FT /note="PABPC1-binding" FT REGION 239..319 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 332..600 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 607..618 FT /note="EIF4E-binding" FT REGION 667..713 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 682..1085 FT /note="eIF3/EIF4A-binding" FT REGION 731..757 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 1024..1227 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 1450..1599 FT /note="EIF4A-binding" FT REGION 1585..1599 FT /note="Necessary but not sufficient for MKNK1-binding" FT COMPBIAS 8..24 FT /note="Pro residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 34..48 FT /note="Polar residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 53..72 FT /note="Low complexity" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 249..260 FT /note="Low complexity" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 261..271 FT /note="Pro residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 289..304 FT /note="Polar residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 429..452 FT /note="Low complexity" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 453..474 FT /note="Acidic residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 519..535 FT /note="Basic and acidic residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 548..563 FT /note="Low complexity" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 574..583 FT /note="Basic and acidic residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 674..683 FT /note="Low complexity" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 693..703 FT /note="Low complexity" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 741..757 FT /note="Basic and acidic residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 1116..1134 FT /note="Polar residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 1146..1178 FT /note="Basic and acidic residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 1186..1225 FT /note="Basic and acidic residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT SITE 674..675 FT /note="Cleavage; by foot-and-mouth disease virus leader FT protease" FT SITE 681..682 FT /note="Cleavage; by enterovirus/rhinovirus protease 2A" FT MOD_RES 15 FT /note="Phosphoserine" FT /evidence="ECO:0000250|UniProtKB:Q6NZJ6" FT MOD_RES 73 FT /note="Omega-N-methylarginine" FT /evidence="ECO:0007744|PubMed:24129315" FT MOD_RES 110 FT /note="Omega-N-methylarginine" FT /evidence="ECO:0007744|PubMed:24129315" FT MOD_RES 207 FT /note="Phosphothreonine" FT /evidence="ECO:0007744|PubMed:18669648, FT ECO:0007744|PubMed:23186163" FT MOD_RES 223 FT /note="Phosphothreonine" FT /evidence="ECO:0007744|PubMed:18669648" FT MOD_RES 314 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:24275569" FT MOD_RES 602 FT /note="N6-acetyllysine" FT /evidence="ECO:0000250|UniProtKB:Q6NZJ6" FT MOD_RES 647 FT /note="Phosphothreonine" FT /evidence="ECO:0007744|PubMed:18669648, FT ECO:0007744|PubMed:23186163" FT MOD_RES 685 FT /note="Omega-N-methylarginine" FT /evidence="ECO:0007744|PubMed:24129315" FT MOD_RES 694 FT /note="Omega-N-methylarginine" FT /evidence="ECO:0007744|PubMed:24129315" FT MOD_RES 1028 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:20068231, FT ECO:0007744|PubMed:21406692, ECO:0007744|PubMed:23186163" FT MOD_RES 1032 FT /note="Omega-N-methylarginine" FT /evidence="ECO:0007744|PubMed:24129315" FT MOD_RES 1042 FT /note="Omega-N-methylarginine" FT /evidence="ECO:0007744|PubMed:24129315" FT MOD_RES 1077 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:23186163" FT MOD_RES 1092 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:17924679, FT ECO:0007744|PubMed:18669648, ECO:0007744|PubMed:20068231, FT ECO:0007744|PubMed:21406692, ECO:0007744|PubMed:23186163" FT MOD_RES 1095 FT /note="N6-acetyllysine" FT /evidence="ECO:0007744|PubMed:19608861" FT MOD_RES 1145 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:21406692, FT ECO:0007744|PubMed:23186163" FT MOD_RES 1147 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:21406692, FT ECO:0007744|PubMed:23186163" FT MOD_RES 1185 FT /note="Phosphoserine; by PKC/PRKCA" FT /evidence="ECO:0000269|PubMed:21576361, FT ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:21406692, FT ECO:0007744|PubMed:23186163" FT MOD_RES 1187 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:20068231, FT ECO:0007744|PubMed:21406692, ECO:0007744|PubMed:23186163" FT MOD_RES 1194 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:23186163" FT MOD_RES 1209 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:18669648, FT ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:21406692, FT ECO:0007744|PubMed:23186163" FT MOD_RES 1211 FT /note="Phosphothreonine" FT /evidence="ECO:0007744|PubMed:20068231, FT ECO:0007744|PubMed:21406692" FT MOD_RES 1231 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:16964243, FT ECO:0007744|PubMed:17081983, ECO:0007744|PubMed:20068231, FT ECO:0007744|PubMed:21406692, ECO:0007744|PubMed:23186163" FT MOD_RES 1238 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:23186163" FT MOD_RES 1596 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:20068231, FT ECO:0007744|PubMed:21406692, ECO:0007744|PubMed:23186163" FT VAR_SEQ 1..196 FT /note="Missing (in isoform E and isoform 7)" FT /evidence="ECO:0000303|PubMed:1429670" FT /id="VSP_018723" FT VAR_SEQ 1..164 FT /note="Missing (in isoform D)" FT /evidence="ECO:0000305" FT /id="VSP_018722" FT VAR_SEQ 1..87 FT /note="Missing (in isoform C)" FT /evidence="ECO:0000303|PubMed:9418880" FT /id="VSP_018721" FT VAR_SEQ 1..40 FT /note="Missing (in isoform B)" FT /evidence="ECO:0000303|PubMed:9857202" FT /id="VSP_018720" FT VAR_SEQ 48 FT /note="R -> RQGGFRSL (in isoform 9)" FT /evidence="ECO:0000305" FT /id="VSP_047396" FT VAR_SEQ 696 FT /note="P -> PQ (in isoform 7 and isoform 8)" FT /evidence="ECO:0000303|PubMed:12052860, FT ECO:0000303|PubMed:1429670, ECO:0000303|PubMed:9372926, FT ECO:0000303|Ref.12" FT /id="VSP_047397" FT VARIANT 71 FT /note="P -> S (in dbSNP:rs113810947)" FT /evidence="ECO:0000269|PubMed:21907011" FT /id="VAR_066571" FT VARIANT 161 FT /note="T -> A (in dbSNP:rs13319149)" FT /evidence="ECO:0000269|PubMed:12052860, FT ECO:0000269|PubMed:17974005, ECO:0000269|PubMed:21907011, FT ECO:0000269|PubMed:9372926, ECO:0000269|PubMed:9755181" FT /id="VAR_061147" FT VARIANT 201 FT /note="R -> H (found in a patient with Rett syndrome-like FT phenotype; uncertain significance; dbSNP:rs34838305)" FT /evidence="ECO:0000269|PubMed:26740508" FT /id="VAR_079031" FT VARIANT 311 FT /note="Y -> C (in dbSNP:rs16858632)" FT /evidence="ECO:0000269|PubMed:21907011" FT /id="VAR_055704" FT VARIANT 432 FT /note="M -> V (in dbSNP:rs2178403)" FT /evidence="ECO:0000269|PubMed:12052860, FT ECO:0000269|PubMed:1429670, ECO:0000269|PubMed:21907011, FT ECO:0000269|PubMed:9372926, ECO:0007744|PubMed:19413330" FT /id="VAR_063040" FT VARIANT 466..468 FT /note="Missing" FT /evidence="ECO:0000269|PubMed:21907011" FT /id="VAR_066572" FT VARIANT 502 FT /note="A -> V (in PARK18; dbSNP:rs111290936)" FT /evidence="ECO:0000269|PubMed:21907011" FT /id="VAR_066573" FT VARIANT 686 FT /note="G -> C (found in patients with Parkinson disease; FT uncertain significance; dbSNP:rs112019125)" FT /evidence="ECO:0000269|PubMed:21907011" FT /id="VAR_066574" FT VARIANT 696 FT /note="P -> L (in a colorectal cancer sample; somatic FT mutation; dbSNP:rs754755344)" FT /evidence="ECO:0000269|PubMed:16959974" FT /id="VAR_036117" FT VARIANT 806 FT /note="I -> V (in dbSNP:rs62287499)" FT /evidence="ECO:0000269|PubMed:21907011" FT /id="VAR_066575" FT VARIANT 829 FT /note="T -> S (in dbSNP:rs111500185)" FT /evidence="ECO:0000269|PubMed:21907011" FT /id="VAR_066576" FT VARIANT 1164 FT /note="S -> R (found in a patient with Parkinson disease; FT uncertain significance; dbSNP:rs113169049)" FT /evidence="ECO:0000269|PubMed:21907011" FT /id="VAR_066577" FT VARIANT 1197 FT /note="R -> W (found in a patient with Parkinson disease; FT uncertain significance; dbSNP:rs113388242)" FT /evidence="ECO:0000269|PubMed:21907011" FT /id="VAR_066578" FT VARIANT 1205 FT /note="R -> H (in PARK18; dbSNP:rs112176450)" FT /evidence="ECO:0000269|PubMed:21907011" FT /id="VAR_066579" FT VARIANT 1229 FT /note="P -> A (in dbSNP:rs35629949)" FT /evidence="ECO:0000269|PubMed:21907011" FT /id="VAR_061148" FT VARIANT 1233 FT /note="L -> P (in dbSNP:rs2230570)" FT /evidence="ECO:0000269|PubMed:21907011" FT /id="VAR_055705" FT VARIANT 1257 FT /note="N -> S (in dbSNP:rs73053766)" FT /evidence="ECO:0000269|PubMed:21907011" FT /id="VAR_066580" FT MUTAGEN 174..178 FT /note="KRERK->AAAAA: Loss of PABPC1 binding; when FT associated with 184-AAAA-187." FT /evidence="ECO:0000269|PubMed:10996799" FT MUTAGEN 180 FT /note="I->A: Loss of PABPC1 binding." FT /evidence="ECO:0000269|PubMed:12086624" FT MUTAGEN 182 FT /note="I->A: Loss of PABPC1 binding." FT /evidence="ECO:0000269|PubMed:12086624" FT MUTAGEN 184..187 FT /note="DPNQ->AAAA: Loss of PABPC1 binding; when associated FT with 174-AAAAA-178." FT MUTAGEN 192 FT /note="I->A: Loss of PABPC1 binding." FT /evidence="ECO:0000269|PubMed:12086624" FT MUTAGEN 196 FT /note="I->A: Loss of PABPC1 binding." FT /evidence="ECO:0000269|PubMed:12086624" FT MUTAGEN 612 FT /note="Y->A,F: Abolishes binding to EIF4E." FT /evidence="ECO:0000269|PubMed:7651417" FT MUTAGEN 617..618 FT /note="LL->AA: Abolishes binding to EIF4E." FT /evidence="ECO:0000269|PubMed:7651417" FT MUTAGEN 682 FT /note="G->A,V,W,R,E: Reduced cleavage by protease 2A from FT human rhinovirus 2." FT /evidence="ECO:0000269|PubMed:8961935" FT MUTAGEN 768 FT /note="L->A: Abolishes binding to EIF4A; when associated FT with A-770 and A-775." FT /evidence="ECO:0000269|PubMed:9372926" FT MUTAGEN 771 FT /note="L->A: Abolishes binding to EIF4A; when associated FT with A-767 and A-775." FT /evidence="ECO:0000269|PubMed:9372926" FT MUTAGEN 776 FT /note="F->A: Abolishes binding to EIF4A; when associated FT with A-767 and A-770." FT /evidence="ECO:0000269|PubMed:9372926" FT MUTAGEN 842..843 FT /note="LL->AA: Abolishes binding to EIF4A; when associated FT with A-850 and K-851." FT /evidence="ECO:0000269|PubMed:9372926" FT MUTAGEN 851..852 FT /note="FE->AK: Abolishes binding to EIF4A; when associated FT with A-841 and A-842." FT /evidence="ECO:0000269|PubMed:9372926" FT MUTAGEN 896 FT /note="L->A: Abolishes binding to EIF4A; when associated FT with A-92 and A-95." FT /evidence="ECO:0000269|PubMed:9372926" FT MUTAGEN 902 FT /note="I->A: Abolishes binding to EIF4A; when associated FT with A-895 and A-95." FT /evidence="ECO:0000269|PubMed:9372926" FT MUTAGEN 905 FT /note="L->A: Abolishes binding to EIF4A; when associated FT with A-895 and A-92." FT /evidence="ECO:0000269|PubMed:9372926" FT MUTAGEN 974 FT /note="R->A: Abolishes binding to EIF4A; when associated FT with A-976." FT /evidence="ECO:0000269|PubMed:9372926" FT MUTAGEN 977 FT /note="F->A: Abolishes binding to EIF4A; when associated FT with A-973." FT /evidence="ECO:0000269|PubMed:9372926" FT MUTAGEN 985 FT /note="L->A: Slightly reduced binding to EIF4A; when FT associated with A-989." FT /evidence="ECO:0000269|PubMed:9372926" FT MUTAGEN 990 FT /note="W->A: Slightly reduced binding to EIF4A; when FT associated with A-984." FT /evidence="ECO:0000269|PubMed:9372926" FT CONFLICT 30 FT /note="P -> R (in Ref. 9; AAC78443)" FT /evidence="ECO:0000305" FT CONFLICT 138 FT /note="F -> L (in Ref. 5; AAL92872/AAM69365)" FT /evidence="ECO:0000305" FT CONFLICT 149 FT /note="Q -> R (in Ref. 5; AAL92872/AAM69365)" FT /evidence="ECO:0000305" FT CONFLICT 214 FT /note="G -> S (in Ref. 1; BAA02185)" FT /evidence="ECO:0000305" FT CONFLICT 462 FT /note="E -> D (in Ref. 1; BAA02185)" FT /evidence="ECO:0000305" FT CONFLICT 468 FT /note="A -> V (in Ref. 1; BAA02185)" FT /evidence="ECO:0000305" FT CONFLICT 474 FT /note="A -> G (in Ref. 1; BAA02185)" FT /evidence="ECO:0000305" FT CONFLICT 479 FT /note="G -> R (in Ref. 1; BAA02185)" FT /evidence="ECO:0000305" FT CONFLICT 604 FT /note="L -> P (in Ref. 1; BAA02185, 5; AAL92872/AAM69365 FT and 10; AAC82471)" FT /evidence="ECO:0000305" FT CONFLICT 625..626 FT /note="AS -> CQ (in Ref. 1; BAA02185)" FT /evidence="ECO:0000305" FT CONFLICT 693 FT /note="P -> A (in Ref. 1; BAA02185)" FT /evidence="ECO:0000305" FT CONFLICT 696 FT /note="P -> A (in Ref. 1; BAA02185)" FT /evidence="ECO:0000305" FT CONFLICT 764 FT /note="V -> W (in Ref. 1; BAA02185)" FT /evidence="ECO:0000305" FT CONFLICT 878 FT /note="G -> E (in Ref. 1; BAA02185)" FT /evidence="ECO:0000305" FT CONFLICT 894 FT /note="R -> C (in Ref. 1; BAA02185)" FT /evidence="ECO:0000305" FT CONFLICT 1104 FT /note="K -> Q (in Ref. 1; BAA02185)" FT /evidence="ECO:0000305" FT CONFLICT 1121 FT /note="N -> I (in Ref. 1; BAA02185)" FT /evidence="ECO:0000305" FT CONFLICT 1185 FT /note="S -> T (in Ref. 1; BAA02185)" FT /evidence="ECO:0000305" FT CONFLICT 1384 FT /note="C -> Y (in Ref. 6; CAI46013)" FT /evidence="ECO:0000305" FT CONFLICT 1472 FT /note="Missing (in Ref. 1; BAA02185)" FT /evidence="ECO:0000305" FT STRAND 181..183 FT /evidence="ECO:0007829|PDB:1LJ2" FT HELIX 185..187 FT /evidence="ECO:0007829|PDB:4F02" FT HELIX 193..197 FT /evidence="ECO:0007829|PDB:4F02" FT HELIX 614..618 FT /evidence="ECO:0007829|PDB:5T46" FT TURN 619..622 FT /evidence="ECO:0007829|PDB:5T46" FT HELIX 624..627 FT /evidence="ECO:0007829|PDB:5T46" FT TURN 637..639 FT /evidence="ECO:0007829|PDB:5T46" FT HELIX 1234..1256 FT /evidence="ECO:0007829|PDB:1UG3" FT HELIX 1259..1267 FT /evidence="ECO:0007829|PDB:1UG3" FT HELIX 1272..1274 FT /evidence="ECO:0007829|PDB:1UG3" FT HELIX 1275..1286 FT /evidence="ECO:0007829|PDB:1UG3" FT TURN 1287..1289 FT /evidence="ECO:0007829|PDB:1UG3" FT HELIX 1291..1306 FT /evidence="ECO:0007829|PDB:1UG3" FT HELIX 1312..1329 FT /evidence="ECO:0007829|PDB:1UG3" FT TURN 1330..1332 FT /evidence="ECO:0007829|PDB:1UG3" FT HELIX 1336..1344 FT /evidence="ECO:0007829|PDB:1UG3" FT HELIX 1345..1348 FT /evidence="ECO:0007829|PDB:1UG3" FT HELIX 1355..1362 FT /evidence="ECO:0007829|PDB:1UG3" FT TURN 1363..1365 FT /evidence="ECO:0007829|PDB:1UG3" FT HELIX 1366..1369 FT /evidence="ECO:0007829|PDB:1UG3" FT HELIX 1372..1387 FT /evidence="ECO:0007829|PDB:1UG3" FT HELIX 1389..1398 FT /evidence="ECO:0007829|PDB:1UG3" FT HELIX 1403..1405 FT /evidence="ECO:0007829|PDB:1UG3" FT HELIX 1413..1419 FT /evidence="ECO:0007829|PDB:1UG3" FT HELIX 1423..1425 FT /evidence="ECO:0007829|PDB:1UG3" FT HELIX 1439..1452 FT /evidence="ECO:0007829|PDB:1UG3" FT HELIX 1457..1467 FT /evidence="ECO:0007829|PDB:1UG3" FT HELIX 1470..1473 FT /evidence="ECO:0007829|PDB:1UG3" FT HELIX 1476..1489 FT /evidence="ECO:0007829|PDB:1UG3" FT STRAND 1494..1496 FT /evidence="ECO:0007829|PDB:1UG3" FT HELIX 1501..1514 FT /evidence="ECO:0007829|PDB:1UG3" FT HELIX 1518..1534 FT /evidence="ECO:0007829|PDB:1UG3" FT HELIX 1541..1551 FT /evidence="ECO:0007829|PDB:1UG3" FT HELIX 1557..1563 FT /evidence="ECO:0007829|PDB:1UG3" FT INIT_MET Q04637-4:1 FT /note="Removed" FT /evidence="ECO:0007744|PubMed:22814378" FT MOD_RES Q04637-4:2 FT /note="N-acetylmethionine" FT /evidence="ECO:0007744|PubMed:22814378" FT MOD_RES Q04637-7:489 FT /note="Omega-N-methylarginine" FT /evidence="ECO:0007744|PubMed:24129315" FT MOD_RES Q04637-7:498 FT /note="Omega-N-methylarginine" FT /evidence="ECO:0007744|PubMed:24129315" FT MOD_RES Q04637-7:509 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:23186163" FT MOD_RES Q04637-8:685 FT /note="Omega-N-methylarginine" FT /evidence="ECO:0007744|PubMed:24129315" FT MOD_RES Q04637-8:694 FT /note="Omega-N-methylarginine" FT /evidence="ECO:0007744|PubMed:24129315" FT MOD_RES Q04637-8:705 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:23186163" SQ SEQUENCE 1599 AA; 175491 MW; 324088B60863DA34 CRC64; MNKAPQSTGP PPAPSPGLPQ PAFPPGQTAP VVFSTPQATQ MNTPSQPRQH FYPSRAQPPS SAASRVQSAA PARPGPAAHV YPAGSQVMMI PSQISYPASQ GAYYIPGQGR STYVVPTQQY PVQPGAPGFY PGASPTEFGT YAGAYYPAQG VQQFPTGVAP TPVLMNQPPQ IAPKRERKTI RIRDPNQGGK DITEEIMSGA RTASTPTPPQ TGGGLEPQAN GETPQVAVIV RPDDRSQGAI IADRPGLPGP EHSPSESQPS SPSPTPSPSP VLEPGSEPNL AVLSIPGDTM TTIQMSVEES TPISRETGEP YRLSPEPTPL AEPILEVEVT LSKPVPESEF SSSPLQAPTP LASHTVEIHE PNGMVPSEDL EPEVESSPEL APPPACPSES PVPIAPTAQP EELLNGAPSP PAVDLSPVSE PEEQAKEVTA SMAPPTIPSA TPATAPSATS PAQEEEMEEE EEEEEGEAGE AGEAESEKGG EELLPPESTP IPANLSQNLE AAAATQVAVS VPKRRRKIKE LNKKEAVGDL LDAFKEANPA VPEVENQPPA GSNPGPESEG SGVPPRPEEA DETWDSKEDK IHNAENIQPG EQKYEYKSDQ WKPLNLEEKK RYDREFLLGF QFIFASMQKP EGLPHISDVV LDKANKTPLR PLDPTRLQGI NCGPDFTPSF ANLGRTTLST RGPPRGGPGG ELPRGPAGLG PRRSQQGPRK EPRKIIATVL MTEDIKLNKA EKAWKPSSKR TAADKDRGEE DADGSKTQDL FRRVRSILNK LTPQMFQQLM KQVTQLAIDT EERLKGVIDL IFEKAISEPN FSVAYANMCR CLMALKVPTT EKPTVTVNFR KLLLNRCQKE FEKDKDDDEV FEKKQKEMDE AATAEERGRL KEELEEARDI ARRRSLGNIK FIGELFKLKM LTEAIMHDCV VKLLKNHDEE SLECLCRLLT TIGKDLDFEK AKPRMDQYFN QMEKIIKEKK TSSRIRFMLQ DVLDLRGSNW VPRRGDQGPK TIDQIHKEAE MEEHREHIKV QQLMAKGSDK RRGGPPGPPI SRGLPLVDDG GWNTVPISKG SRPIDTSRLT KITKPGSIDS NNQLFAPGGR LSWGKGSSGG SGAKPSDAAS EAARPATSTL NRFSALQQAV PTESTDNRRV VQRSSLSRER GEKAGDRGDR LERSERGGDR GDRLDRARTP ATKRSFSKEV EERSRERPSQ PEGLRKAASL TEDRDRGRDA VKREAALPPV SPLKAALSEE ELEKKSKAII EEYLHLNDMK EAVQCVQELA SPSLLFIFVR HGVESTLERS AIAREHMGQL LHQLLCAGHL STAQYYQGLY EILELAEDME IDIPHVWLYL AELVTPILQE GGVPMGELFR EITKPLRPLG KAASLLLEIL GLLCKSMGPK KVGTLWREAG LSWKEFLPEG QDIGAFVAEQ KVEYTLGEES EAPGQRALPS EELNRQLEKL LKEGSSNQRV FDWIEANLSE QQIVSNTLVR ALMTAVCYSA IIFETPLRVD VAVLKARAKL LQKYLCDEQK ELQALYALQA LVVTLEQPPN LLRMFFDALY DEDVVKEDAF YSWESSKDPA EQQGKGVALK SVTAFFKWLR EAEEESDHN // ID NDUA1_HUMAN Reviewed; 70 AA. AC O15239; DT 15-JUL-1998, integrated into UniProtKB/Swiss-Prot. DT 01-JAN-1998, sequence version 1. DT 28-JAN-2026, entry version 197. DE RecName: Full=NADH dehydrogenase [ubiquinone] 1 alpha subcomplex subunit 1; DE AltName: Full=Complex I-MWFE; DE Short=CI-MWFE; DE AltName: Full=NADH-ubiquinone oxidoreductase MWFE subunit; GN Name=NDUFA1; OS Homo sapiens (Human). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia; OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae; OC Homo. OX NCBI_TaxID=9606; RN [1] RP NUCLEOTIDE SEQUENCE [MRNA]. RX PubMed=8938439; DOI=10.1006/geno.1996.0561; RA Zhuchenko O., Wehnert M., Bailey J., Sun Z.S., Lee C.C.; RT "Isolation, mapping, and genomic structure of an X-linked gene for a RT subunit of human mitochondrial complex I."; RL Genomics 37:281-288(1996). RN [2] RP NUCLEOTIDE SEQUENCE [MRNA]. RC TISSUE=Liver; RX PubMed=9224902; DOI=10.1016/s0378-1119(97)00108-x; RA Frattini A., Faranda S., Bagnasco L., Patrosso C., Nulli P., Zucchi I., RA Vezzoni P.; RT "Identification of a new member (ZNF183) of the Ring finger gene family in RT Xq24-25."; RL Gene 192:291-298(1997). RN [3] RP NUCLEOTIDE SEQUENCE [MRNA]. RA Zhuchenko O.P., Wehnert M., Bailey J., Sun Z.S., Lee C.C.; RT "hMWFE gene -- component of human mitochondrial complex I."; RL Submitted (APR-1996) to the EMBL/GenBank/DDBJ databases. RN [4] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. RC TISSUE=Eye; RX PubMed=15489334; DOI=10.1101/gr.2596504; RG The MGC Project Team; RT "The status, quality, and expansion of the NIH full-length cDNA project: RT the Mammalian Gene Collection (MGC)."; RL Genome Res. 14:2121-2127(2004). RN [5] RP IDENTIFICATION IN THE NADH-UBIQUINONE OXIDOREDUCTASE COMPLEX, AND RP IDENTIFICATION BY MASS SPECTROMETRY. RX PubMed=12611891; DOI=10.1074/jbc.c300064200; RA Murray J., Zhang B., Taylor S.W., Oglesbee D., Fahy E., Marusich M.F., RA Ghosh S.S., Capaldi R.A.; RT "The subunit composition of the human NADH dehydrogenase obtained by rapid RT one-step immunopurification."; RL J. Biol. Chem. 278:13619-13622(2003). RN [6] RP FUNCTION, AND IDENTIFICATION IN THE NADH-UBIQUINONE OXIDOREDUCTASE COMPLEX. RX PubMed=27626371; DOI=10.1038/nature19754; RA Stroud D.A., Surgenor E.E., Formosa L.E., Reljic B., Frazier A.E., RA Dibley M.G., Osellame L.D., Stait T., Beilharz T.H., Thorburn D.R., RA Salim A., Ryan M.T.; RT "Accessory subunits are integral for assembly and function of human RT mitochondrial complex I."; RL Nature 538:123-126(2016). RN [7] RP VARIANT [LARGE SCALE ANALYSIS] CYS-53. RX PubMed=16959974; DOI=10.1126/science.1133427; RA Sjoeblom T., Jones S., Wood L.D., Parsons D.W., Lin J., Barber T.D., RA Mandelker D., Leary R.J., Ptak J., Silliman N., Szabo S., Buckhaults P., RA Farrell C., Meeh P., Markowitz S.D., Willis J., Dawson D., Willson J.K.V., RA Gazdar A.F., Hartigan J., Wu L., Liu C., Parmigiani G., Park B.H., RA Bachman K.E., Papadopoulos N., Vogelstein B., Kinzler K.W., RA Velculescu V.E.; RT "The consensus coding sequences of human breast and colorectal cancers."; RL Science 314:268-274(2006). RN [8] RP VARIANTS MC1DN12 ARG-8 AND SER-37. RX PubMed=17262856; DOI=10.1002/ana.21036; RA Fernandez-Moreira D., Ugalde C., Smeets R., Rodenburg R.J.T., RA Lopez-Laso E., Ruiz-Falco M.L., Briones P., Martin M.A., Smeitink J.A.M., RA Arenas J.; RT "X-linked NDUFA1 gene mutations associated with mitochondrial RT encephalomyopathy."; RL Ann. Neurol. 61:73-83(2007). CC -!- FUNCTION: Accessory subunit of the mitochondrial membrane respiratory CC chain NADH dehydrogenase (Complex I), that is believed not to be CC involved in catalysis. Complex I functions in the transfer of electrons CC from NADH to the respiratory chain. The immediate electron acceptor for CC the enzyme is believed to be ubiquinone. {ECO:0000269|PubMed:27626371}. CC -!- SUBUNIT: Complex I is composed of 45 different subunits. CC {ECO:0000269|PubMed:12611891, ECO:0000269|PubMed:27626371}. CC -!- SUBCELLULAR LOCATION: Mitochondrion inner membrane CC {ECO:0000305|PubMed:12611891}; Single-pass membrane protein CC {ECO:0000255}; Matrix side {ECO:0000305}. CC -!- TISSUE SPECIFICITY: Primarily expressed in heart and skeletal muscle. CC -!- DISEASE: Mitochondrial complex I deficiency, nuclear type 12 (MC1DN12) CC [MIM:301020]: A form of mitochondrial complex I deficiency, the most CC common biochemical signature of mitochondrial disorders, a group of CC highly heterogeneous conditions characterized by defective oxidative CC phosphorylation, which collectively affects 1 in 5-10000 live births. CC Clinical disorders have variable severity, ranging from lethal neonatal CC disease to adult-onset neurodegenerative disorders. Phenotypes include CC macrocephaly with progressive leukodystrophy, non-specific CC encephalopathy, cardiomyopathy, myopathy, liver disease, Leigh CC syndrome, Leber hereditary optic neuropathy, and some forms of CC Parkinson disease. {ECO:0000269|PubMed:17262856}. Note=The disease is CC caused by variants affecting the gene represented in this entry. CC -!- SIMILARITY: Belongs to the complex I NDUFA1 subunit family. CC {ECO:0000305}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; X81900; CAA57489.1; -; mRNA. DR EMBL; U54993; AAD00084.1; -; mRNA. DR EMBL; BC000266; AAH00266.1; -; mRNA. DR CCDS; CCDS14590.1; -. DR RefSeq; NP_004532.1; NM_004541.4. DR PDB; 5XTC; EM; 3.70 A; S=1-70. DR PDB; 5XTD; EM; 3.70 A; S=1-70. DR PDB; 5XTH; EM; 3.90 A; S=1-70. DR PDB; 5XTI; EM; 17.40 A; BS/S=1-70. DR PDB; 9CWT; EM; 3.44 A; S=1-70. DR PDBsum; 5XTC; -. DR PDBsum; 5XTD; -. DR PDBsum; 5XTH; -. DR PDBsum; 5XTI; -. DR PDBsum; 9CWT; -. DR AlphaFoldDB; O15239; -. DR EMDB; EMD-45974; -. DR SMR; O15239; -. DR BioGRID; 110774; 45. DR ComplexPortal; CPX-577; Mitochondrial respiratory chain complex I. DR CORUM; O15239; -. DR FunCoup; O15239; 444. DR IntAct; O15239; 42. DR MINT; O15239; -. DR STRING; 9606.ENSP00000360492; -. DR BindingDB; O15239; -. DR ChEMBL; CHEMBL2363065; -. DR DrugBank; DB00157; NADH. DR DrugCentral; O15239; -. DR GlyGen; O15239; 1 site, 1 O-linked glycan (1 site). DR iPTMnet; O15239; -. DR PhosphoSitePlus; O15239; -. DR BioMuta; NDUFA1; -. DR jPOST; O15239; -. DR MassIVE; O15239; -. DR PaxDb; 9606-ENSP00000360492; -. DR PeptideAtlas; O15239; -. DR ProteomicsDB; 48530; -. DR Pumba; O15239; -. DR TopDownProteomics; O15239; -. DR Antibodypedia; 29846; 230 antibodies from 28 providers. DR DNASU; 4694; -. DR Ensembl; ENST00000371437.5; ENSP00000360492.4; ENSG00000125356.8. DR GeneID; 4694; -. DR KEGG; hsa:4694; -. DR MANE-Select; ENST00000371437.5; ENSP00000360492.4; NM_004541.4; NP_004532.1. DR AGR; HGNC:7683; -. DR ClinPGx; PA31489; -. DR CTD; 4694; -. DR DisGeNET; 4694; -. DR GeneCards; NDUFA1; -. DR GeneReviews; NDUFA1; -. DR HGNC; HGNC:7683; NDUFA1. DR HPA; ENSG00000125356; Low tissue specificity. DR MalaCards; NDUFA1; -. DR MIM; 300078; gene. DR MIM; 301020; phenotype. DR OpenTargets; ENSG00000125356; -. DR Orphanet; 2609; Isolated complex I deficiency. DR VEuPathDB; HostDB:ENSG00000125356; -. DR eggNOG; ENOG502S3S5; Eukaryota. DR GeneTree; ENSGT00390000007560; -. DR HOGENOM; CLU_185502_2_0_1; -. DR InParanoid; O15239; -. DR OMA; WALMERD; -. DR OrthoDB; 1920692at2759; -. DR PAN-GO; O15239; 1 GO annotation based on evolutionary models. DR PhylomeDB; O15239; -. DR BioCyc; MetaCyc:HS04875-MONOMER; -. DR PathwayCommons; O15239; -. DR Reactome; R-HSA-611105; Respiratory electron transport. DR Reactome; R-HSA-6799198; Complex I biogenesis. DR SignaLink; O15239; -. DR SIGNOR; O15239; -. DR Agora; ENSG00000125356; -. DR BioGRID-ORCS; 4694; 126 hits in 779 CRISPR screens. DR ChiTaRS; NDUFA1; human. DR GeneWiki; NADH_dehydrogenase_(ubiquinone),_alpha_1; -. DR GenomeRNAi; 4694; -. DR Pharos; O15239; Tclin. DR PRO; PR:O15239; -. DR Proteomes; UP000005640; Chromosome X. DR RNAct; O15239; protein. DR Bgee; ENSG00000125356; Expressed in left ventricle myocardium and 206 other cell types or tissues. DR ExpressionAtlas; O15239; baseline and differential. DR GO; GO:0005743; C:mitochondrial inner membrane; IDA:ComplexPortal. DR GO; GO:0031966; C:mitochondrial membrane; IDA:UniProtKB. DR GO; GO:0005739; C:mitochondrion; IDA:MGI. DR GO; GO:0045271; C:respiratory chain complex I; IDA:UniProtKB. DR GO; GO:0008137; F:NADH dehydrogenase (ubiquinone) activity; TAS:ProtInc. DR GO; GO:0009060; P:aerobic respiration; NAS:ComplexPortal. DR GO; GO:0006120; P:mitochondrial electron transport, NADH to ubiquinone; NAS:UniProtKB. DR GO; GO:0042776; P:proton motive force-driven mitochondrial ATP synthesis; NAS:ComplexPortal. DR InterPro; IPR017384; NADH_Ub_cplx-1_asu_su-1. DR PANTHER; PTHR17098:SF2; NADH DEHYDROGENASE [UBIQUINONE] 1 ALPHA SUBCOMPLEX SUBUNIT 1; 1. DR PANTHER; PTHR17098; NADH-UBIQUINONE OXIDOREDUCTASE MWFE SUBUNIT; 1. DR Pfam; PF15879; MWFE; 1. DR PIRSF; PIRSF038095; NDUA1; 1. PE 1: Evidence at protein level; KW 3D-structure; Disease variant; Electron transport; Membrane; Mitochondrion; KW Mitochondrion inner membrane; Primary mitochondrial disease; KW Proteomics identification; Reference proteome; Respiratory chain; KW Transmembrane; Transmembrane helix; Transport. FT CHAIN 1..70 FT /note="NADH dehydrogenase [ubiquinone] 1 alpha subcomplex FT subunit 1" FT /id="PRO_0000118817" FT TRANSMEM 1..21 FT /note="Helical" FT /evidence="ECO:0000255" FT VARIANT 8 FT /note="G -> R (in MC1DN12; dbSNP:rs104894884)" FT /evidence="ECO:0000269|PubMed:17262856" FT /id="VAR_035099" FT VARIANT 32 FT /note="G -> R (in dbSNP:rs1801316)" FT /id="VAR_014485" FT VARIANT 37 FT /note="R -> S (in MC1DN12; dbSNP:rs104894885)" FT /evidence="ECO:0000269|PubMed:17262856" FT /id="VAR_035100" FT VARIANT 53 FT /note="R -> C (in a colorectal cancer sample; somatic FT mutation; dbSNP:rs1257734702)" FT /evidence="ECO:0000269|PubMed:16959974" FT /id="VAR_036173" SQ SEQUENCE 70 AA; 8072 MW; E4004A62117BF253 CRC64; MWFEILPGLS VMGVCLLIPG LATAYIHRFT NGGKEKRVAH FGYHWSLMER DRRISGVDRY YVSKGLENID // ID RIR2B_HUMAN Reviewed; 351 AA. AC Q7LG56; B4E2N4; Q17R22; Q75PQ6; Q75PQ7; Q75PY8; Q75PY9; Q86YE3; Q9NPD6; AC Q9NTD8; Q9NUW3; DT 21-MAR-2006, integrated into UniProtKB/Swiss-Prot. DT 05-JUL-2004, sequence version 1. DT 28-JAN-2026, entry version 197. DE RecName: Full=Ribonucleoside-diphosphate reductase subunit M2 B; DE EC=1.17.4.1; DE AltName: Full=TP53-inducible ribonucleotide reductase M2 B; DE AltName: Full=p53-inducible ribonucleotide reductase small subunit 2-like protein; DE Short=p53R2; GN Name=RRM2B; Synonyms=P53R2; OS Homo sapiens (Human). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia; OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae; OC Homo. OX NCBI_TaxID=9606; RN [1] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA] (ISOFORM 1), FUNCTION, AND RP INDUCTION. RX PubMed=10716435; DOI=10.1038/35003506; RA Tanaka H., Arakawa H., Yamaguchi T., Shiraishi K., Fukuda S., Matsui K., RA Takei Y., Nakamura Y.; RT "A ribonucleotide reductase gene involved in a p53-dependent cell-cycle RT checkpoint for DNA damage."; RL Nature 404:42-49(2000). RN [2] RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1; 2; 3; 4 AND 5). RA Ugai H., Yokoyama K.K.; RT "Homo sapiens p53-inducible ribonucleotide reductase small subunit 2 RT splicing variants."; RL Submitted (MAR-2004) to the EMBL/GenBank/DDBJ databases. RN [3] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1), AND NUCLEOTIDE SEQUENCE RP [LARGE SCALE MRNA] OF 1-351 (ISOFORM 6). RC TISSUE=Placenta, and Trachea; RX PubMed=14702039; DOI=10.1038/ng1285; RA Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., RA Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., RA Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S., RA Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., RA Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H., RA Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., RA Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., RA Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., RA Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., RA Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., RA Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., RA Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., RA Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., RA Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., RA Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., RA Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., RA Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., RA Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y., RA Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., RA Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., RA Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., RA Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., RA Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., RA Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., RA Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., RA Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., RA Isogai T., Sugano S.; RT "Complete sequencing and characterization of 21,243 full-length human RT cDNAs."; RL Nat. Genet. 36:40-45(2004). RN [4] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1). RC TISSUE=Amygdala; RX PubMed=17974005; DOI=10.1186/1471-2164-8-399; RA Bechtel S., Rosenfelder H., Duda A., Schmidt C.P., Ernst U., RA Wellenreuther R., Mehrle A., Schuster C., Bahr A., Bloecker H., Heubner D., RA Hoerlein A., Michel G., Wedler H., Koehrer K., Ottenwaelder B., Poustka A., RA Wiemann S., Schupp I.; RT "The full-ORF clone resource of the German cDNA consortium."; RL BMC Genomics 8:399-399(2007). RN [5] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RX PubMed=16421571; DOI=10.1038/nature04406; RA Nusbaum C., Mikkelsen T.S., Zody M.C., Asakawa S., Taudien S., Garber M., RA Kodira C.D., Schueler M.G., Shimizu A., Whittaker C.A., Chang J.L., RA Cuomo C.A., Dewar K., FitzGerald M.G., Yang X., Allen N.R., Anderson S., RA Asakawa T., Blechschmidt K., Bloom T., Borowsky M.L., Butler J., Cook A., RA Corum B., DeArellano K., DeCaprio D., Dooley K.T., Dorris L. III, RA Engels R., Gloeckner G., Hafez N., Hagopian D.S., Hall J.L., Ishikawa S.K., RA Jaffe D.B., Kamat A., Kudoh J., Lehmann R., Lokitsang T., Macdonald P., RA Major J.E., Matthews C.D., Mauceli E., Menzel U., Mihalev A.H., RA Minoshima S., Murayama Y., Naylor J.W., Nicol R., Nguyen C., O'Leary S.B., RA O'Neill K., Parker S.C.J., Polley A., Raymond C.K., Reichwald K., RA Rodriguez J., Sasaki T., Schilhabel M., Siddiqui R., Smith C.L., RA Sneddon T.P., Talamas J.A., Tenzin P., Topham K., Venkataraman V., Wen G., RA Yamazaki S., Young S.K., Zeng Q., Zimmer A.R., Rosenthal A., Birren B.W., RA Platzer M., Shimizu N., Lander E.S.; RT "DNA sequence and analysis of human chromosome 8."; RL Nature 439:331-335(2006). RN [6] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RA Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M., RA Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J., RA Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S., RA Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H., RA Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K., RA Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D., RA Hunkapiller M.W., Myers E.W., Venter J.C.; RL Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases. RN [7] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA]. RG NIEHS SNPs program; RL Submitted (MAY-2005) to the EMBL/GenBank/DDBJ databases. RN [8] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1). RC TISSUE=Brain, and Eye; RX PubMed=15489334; DOI=10.1101/gr.2596504; RG The MGC Project Team; RT "The status, quality, and expansion of the NIH full-length cDNA project: RT the Mammalian Gene Collection (MGC)."; RL Genome Res. 14:2121-2127(2004). RN [9] RP FUNCTION, AND SUBUNIT. RX PubMed=11517226; DOI=10.1074/jbc.m106088200; RA Guittet O., Haakansson P., Voevodskaya N., Fridd S., Graeslund A., RA Arakawa H., Nakamura Y., Thelander L.; RT "Mammalian p53R2 protein forms an active ribonucleotide reductase in vitro RT with the R1 protein, which is expressed both in resting cells in response RT to DNA damage and in proliferating cells."; RL J. Biol. Chem. 276:40647-40651(2001). RN [10] RP FUNCTION, SUBCELLULAR LOCATION, AND VARIANT LEU-115. RX PubMed=11719458; RA Yamaguchi T., Matsuda K., Sagiya Y., Iwadate M., Fujino M.A., Nakamura Y., RA Arakawa H.; RT "p53R2-dependent pathway for DNA synthesis in a p53-regulated cell cycle RT checkpoint."; RL Cancer Res. 61:8256-8262(2001). RN [11] RP SUBCELLULAR LOCATION, AND INTERACTION WITH TP53 AND RRM1. RX PubMed=12615712; RA Xue L., Zhou B., Liu X., Qiu W., Jin Z., Yen Y.; RT "Wild-type p53 regulates human ribonucleotide reductase by protein-protein RT interaction with p53R2 as well as hRRM2 subunits."; RL Cancer Res. 63:980-986(2003). RN [12] RP TISSUE SPECIFICITY. RX PubMed=14583450; RA Zhou B., Liu X., Mo X., Xue L., Darwish D., Qiu W., Shih J., Hwu E.B., RA Luh F., Yen Y.; RT "The human ribonucleotide reductase subunit hRRM2 complements p53R2 in RT response to UV-induced DNA repair in cells with mutant p53."; RL Cancer Res. 63:6583-6594(2003). RN [13] RP CATALYTIC ACTIVITY, AND SUBUNIT. RX PubMed=16376858; DOI=10.1016/j.bbrc.2005.12.019; RA Qiu W., Zhou B., Darwish D., Shao J., Yen Y.; RT "Characterization of enzymatic properties of human ribonucleotide reductase RT holoenzyme reconstituted in vitro from hRRM1, hRRM2, and p53R2 subunits."; RL Biochem. Biophys. Res. Commun. 340:428-434(2006). RN [14] RP INVOLVEMENT IN PEOA5. RX PubMed=19664747; DOI=10.1016/j.ajhg.2009.07.009; RA Tyynismaa H., Ylikallio E., Patel M., Molnar M.J., Haller R.G., RA Suomalainen A.; RT "A heterozygous truncating mutation in RRM2B causes autosomal-dominant RT progressive external ophthalmoplegia with multiple mtDNA deletions."; RL Am. J. Hum. Genet. 85:290-295(2009). RN [15] RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RX PubMed=21269460; DOI=10.1186/1752-0509-5-17; RA Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T., RA Bennett K.L., Superti-Furga G., Colinge J.; RT "Initial characterization of the human central proteome."; RL BMC Syst. Biol. 5:17-17(2011). RN [16] RP X-RAY CRYSTALLOGRAPHY (2.6 ANGSTROMS) IN COMPLEX WITH IRON IONS, AND RP COFACTOR. RX PubMed=19728742; DOI=10.1021/bi9001425; RA Smith P., Zhou B., Ho N., Yuan Y.C., Su L., Tsai S.C., Yen Y.; RT "2.6 A X-ray crystal structure of human p53R2, a p53-inducible RT ribonucleotide reductase."; RL Biochemistry 48:11134-11141(2009). RN [17] RP X-RAY CRYSTALLOGRAPHY (2.8 ANGSTROMS) OF 20-322 IN COMPLEX WITH IRON IONS. RG Structural genomics consortium (SGC); RT "Human ribonucleotide reductase, subunit M2 B."; RL Submitted (FEB-2009) to the PDB data bank. RN [18] RP VARIANTS MTDPS8A ARG-64; GLU-85 DEL; GLY-194; LYS-194 AND PHE-236. RX PubMed=17486094; DOI=10.1038/ng2040; RA Bourdon A., Minai L., Serre V., Jais J.-P., Sarzi E., Aubert S., RA Chretien D., de Lonlay P., Paquis-Flucklinger V., Arakawa H., Nakamura Y., RA Munnich A., Roetig A.; RT "Mutation of RRM2B, encoding p53-controlled ribonucleotide reductase RT (p53R2), causes severe mitochondrial DNA depletion."; RL Nat. Genet. 39:776-780(2007). RN [19] RP VARIANTS MTDPS8A SER-224; ILE-282 AND VAL-317. RX PubMed=18504129; DOI=10.1016/j.nmd.2008.04.006; RA Bornstein B., Area E., Flanigan K.M., Ganesh J., Jayakar P., Swoboda K.J., RA Coku J., Naini A., Shanske S., Tanji K., Hirano M., DiMauro S.; RT "Mitochondrial DNA depletion syndrome due to mutations in the RRM2B gene."; RL Neuromuscul. Disord. 18:453-459(2008). RN [20] RP VARIANTS MTDPS8B HIS-110 AND HIS-121. RX PubMed=19667227; DOI=10.1001/archneurol.2009.139; RA Shaibani A., Shchelochkov O.A., Zhang S., Katsonis P., Lichtarge O., RA Wong L.J., Shinawi M.; RT "Mitochondrial neurogastrointestinal encephalopathy due to mutations in RT RRM2B."; RL Arch. Neurol. 66:1028-1032(2009). RN [21] RP VARIANT SER-33. RX PubMed=26741492; DOI=10.1371/journal.pgen.1005679; RA Kohda M., Tokuzawa Y., Kishita Y., Nyuzuki H., Moriyama Y., Mizuno Y., RA Hirata T., Yatsuka Y., Yamashita-Sugahara Y., Nakachi Y., Kato H., RA Okuda A., Tamaru S., Borna N.N., Banshoya K., Aigaki T., Sato-Miyata Y., RA Ohnuma K., Suzuki T., Nagao A., Maehata H., Matsuda F., Higasa K., RA Nagasaki M., Yasuda J., Yamamoto M., Fushimi T., Shimura M., RA Kaiho-Ichimoto K., Harashima H., Yamazaki T., Mori M., Murayama K., RA Ohtake A., Okazaki Y.; RT "A comprehensive genomic analysis reveals the genetic landscape of RT mitochondrial respiratory chain complex deficiencies."; RL PLoS Genet. 12:E1005679-E1005679(2016). RN [22] RP VARIANT RCDFRD ASP-262, AND INVOLVEMENT IN RCDFRD. RX PubMed=32827185; DOI=10.1002/humu.24094; RA Roberts L., Julius S., Dawlat S., Yildiz S., Rebello G., Meldau S., RA Pillay K., Esterhuizen A., Vorster A., Benefeld G., da Rocha J., RA Beighton P., Sellars S.L., Thandrayen K., Pettifor J.M., Ramesar R.S.; RT "Renal dysfunction, rod-cone dystrophy, and sensorineural hearing loss RT caused by a mutation in RRM2B."; RL Hum. Mutat. 41:1871-1876(2020). CC -!- FUNCTION: Plays a pivotal role in cell survival by repairing damaged CC DNA in a p53/TP53-dependent manner. Supplies deoxyribonucleotides for CC DNA repair in cells arrested at G1 or G2. Contains an iron-tyrosyl free CC radical center required for catalysis. Forms an active ribonucleotide CC reductase (RNR) complex with RRM1 which is expressed both in resting CC and proliferating cells in response to DNA damage. CC {ECO:0000269|PubMed:10716435, ECO:0000269|PubMed:11517226, CC ECO:0000269|PubMed:11719458}. CC -!- CATALYTIC ACTIVITY: CC Reaction=a 2'-deoxyribonucleoside 5'-diphosphate + [thioredoxin]- CC disulfide + H2O = a ribonucleoside 5'-diphosphate + [thioredoxin]- CC dithiol; Xref=Rhea:RHEA:23252, Rhea:RHEA-COMP:10698, Rhea:RHEA- CC COMP:10700, ChEBI:CHEBI:15377, ChEBI:CHEBI:29950, ChEBI:CHEBI:50058, CC ChEBI:CHEBI:57930, ChEBI:CHEBI:73316; EC=1.17.4.1; CC Evidence={ECO:0000255|PROSITE-ProRule:PRU10014, CC ECO:0000269|PubMed:16376858}; CC -!- COFACTOR: CC Name=Fe cation; Xref=ChEBI:CHEBI:24875; CC Evidence={ECO:0000269|PubMed:19728742}; CC Note=Binds 2 iron ions per subunit. {ECO:0000269|PubMed:19728742}; CC -!- SUBUNIT: Heterotetramer with large (RRM1) subunit. Interacts with CC p53/TP53. Interacts with RRM1 in response to DNA damage. CC {ECO:0000269|PubMed:11517226, ECO:0000269|PubMed:12615712, CC ECO:0000269|PubMed:16376858, ECO:0000269|PubMed:19728742, CC ECO:0000269|Ref.17}. CC -!- INTERACTION: CC Q7LG56; Q13315: ATM; NbExp=3; IntAct=EBI-9009083, EBI-495465; CC Q7LG56; Q00987: MDM2; NbExp=2; IntAct=EBI-9009083, EBI-389668; CC Q7LG56; O43929: ORC4; NbExp=4; IntAct=EBI-9009083, EBI-374889; CC Q7LG56; Q9H4P4: RNF41; NbExp=3; IntAct=EBI-9009083, EBI-2130266; CC Q7LG56; Q7LG56: RRM2B; NbExp=3; IntAct=EBI-9009083, EBI-9009083; CC Q7LG56-1; Q00987: MDM2; NbExp=2; IntAct=EBI-15741413, EBI-389668; CC -!- SUBCELLULAR LOCATION: Cytoplasm. Nucleus. Note=Translocates from CC cytoplasm to nucleus in response to DNA damage. CC -!- ALTERNATIVE PRODUCTS: CC Event=Alternative splicing; Named isoforms=6; CC Name=1; CC IsoId=Q7LG56-1; Sequence=Displayed; CC Name=2; Synonyms=Long form; CC IsoId=Q7LG56-2; Sequence=VSP_017670; CC Name=3; Synonyms=Short form gamma; CC IsoId=Q7LG56-3; Sequence=VSP_017669; CC Name=4; Synonyms=Short form beta; CC IsoId=Q7LG56-4; Sequence=VSP_017668; CC Name=5; Synonyms=Short form; CC IsoId=Q7LG56-5; Sequence=VSP_017671, VSP_017672; CC Name=6; CC IsoId=Q7LG56-6; Sequence=VSP_053585; CC -!- TISSUE SPECIFICITY: Widely expressed at a high level in skeletal muscle CC and at a weak level in thymus. Expressed in epithelial dysplasias and CC squamous cell carcinoma. {ECO:0000269|PubMed:14583450}. CC -!- INDUCTION: In response to DNA damage in a wild-type p53/TP53-dependent CC manner. {ECO:0000269|PubMed:10716435}. CC -!- DISEASE: Mitochondrial DNA depletion syndrome 8A (MTDPS8A) CC [MIM:612075]: A disorder due to mitochondrial dysfunction characterized CC by various combinations of neonatal hypotonia, neurological CC deterioration, respiratory distress, lactic acidosis, and renal CC tubulopathy. {ECO:0000269|PubMed:17486094, CC ECO:0000269|PubMed:18504129}. Note=The disease is caused by variants CC affecting the gene represented in this entry. CC -!- DISEASE: Mitochondrial DNA depletion syndrome 8B (MTDPS8B) CC [MIM:612075]: A disease due to mitochondrial dysfunction and CC characterized by ophthalmoplegia, ptosis, gastrointestinal dysmotility, CC cachexia, peripheral neuropathy. {ECO:0000269|PubMed:19667227}. CC Note=The disease is caused by variants affecting the gene represented CC in this entry. CC -!- DISEASE: Progressive external ophthalmoplegia with mitochondrial DNA CC deletions, autosomal dominant, 5 (PEOA5) [MIM:613077]: A disorder CC characterized by progressive weakness of ocular muscles and levator CC muscle of the upper eyelid. In a minority of cases, it is associated CC with skeletal myopathy, which predominantly involves axial or proximal CC muscles and which causes abnormal fatigability and even permanent CC muscle weakness. Ragged-red fibers and atrophy are found on muscle CC biopsy. A large proportion of chronic ophthalmoplegias are associated CC with other symptoms, leading to a multisystemic pattern of this CC disease. Additional symptoms are variable, and may include cataracts, CC hearing loss, sensory axonal neuropathy, ataxia, depression, CC hypogonadism, and parkinsonism. {ECO:0000269|PubMed:19664747}. Note=The CC disease is caused by variants affecting the gene represented in this CC entry. CC -!- DISEASE: Rod-cone dystrophy, sensorineural deafness, and Fanconi-type CC renal dysfunction (RCDFRD) [MIM:268315]: An autosomal recessive disease CC characterized by visual impairment due to rod-cone dystrophy, CC sensorineural hearing loss, and Fanconi-type renal dysfunction CC resulting in rickets-like skeletal changes. Death may occur in CC childhood or young adulthood due to renal failure. Disease onset is CC before age 5 years. {ECO:0000269|PubMed:32827185}. Note=The disease is CC caused by variants affecting the gene represented in this entry. CC -!- MISCELLANEOUS: [Isoform 5]: May be produced at very low levels due to a CC premature stop codon in the mRNA, leading to nonsense-mediated mRNA CC decay. {ECO:0000305}. CC -!- SIMILARITY: Belongs to the ribonucleoside diphosphate reductase small CC chain family. {ECO:0000305}. CC -!- SEQUENCE CAUTION: CC Sequence=BAG65196.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305}; CC Sequence=EAW91842.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305}; CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; AB036063; BAA92434.1; -; mRNA. DR EMBL; AB036532; BAA92493.1; -; Genomic_DNA. DR EMBL; AB163437; BAD11774.1; -; mRNA. DR EMBL; AB163438; BAD11775.1; -; mRNA. DR EMBL; AB166669; BAD12265.1; -; mRNA. DR EMBL; AB166670; BAD12266.1; -; mRNA. DR EMBL; AB166671; BAD12267.1; -; mRNA. DR EMBL; AK001965; BAA92005.1; -; mRNA. DR EMBL; AK304354; BAG65196.1; ALT_INIT; mRNA. DR EMBL; DC308409; -; NOT_ANNOTATED_CDS; mRNA. DR EMBL; AL137348; CAB70703.2; -; mRNA. DR EMBL; DQ027001; AAY29059.1; -; Genomic_DNA. DR EMBL; AP001328; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; AP002907; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; CH471060; EAW91842.1; ALT_SEQ; Genomic_DNA. DR EMBL; BC042468; AAH42468.1; -; mRNA. DR EMBL; BC108261; AAI08262.1; -; mRNA. DR EMBL; BC117496; AAI17497.1; -; mRNA. DR EMBL; BC130628; AAI30629.1; -; mRNA. DR CCDS; CCDS34932.1; -. [Q7LG56-1] DR CCDS; CCDS55267.1; -. [Q7LG56-2] DR PIR; T46249; T46249. DR RefSeq; NP_001165948.1; NM_001172477.1. [Q7LG56-6] DR RefSeq; NP_001165949.1; NM_001172478.2. [Q7LG56-2] DR RefSeq; NP_056528.2; NM_015713.4. [Q7LG56-1] DR PDB; 2VUX; X-ray; 2.80 A; A/B=20-322. DR PDB; 3HF1; X-ray; 2.60 A; A/B=1-351. DR PDB; 4DJN; X-ray; 2.20 A; A/B=13-322. DR PDBsum; 2VUX; -. DR PDBsum; 3HF1; -. DR PDBsum; 4DJN; -. DR AlphaFoldDB; Q7LG56; -. DR SMR; Q7LG56; -. DR BioGRID; 119071; 74. DR ComplexPortal; CPX-369; Ribonucleoside-diphosphate reductase RR1 complex, RRM2B variant. DR CORUM; Q7LG56; -. DR DIP; DIP-24264N; -. DR DIP; DIP-48627N; -. DR FunCoup; Q7LG56; 2091. DR IntAct; Q7LG56; 34. DR STRING; 9606.ENSP00000251810; -. DR BindingDB; Q7LG56; -. DR ChEMBL; CHEMBL3301398; -. DR DrugBank; DB00242; Cladribine. DR DrugBank; DB00631; Clofarabine. DR DrugBank; DB12948; Didox. DR GlyGen; Q7LG56; 1 site, 1 O-linked glycan (1 site). DR iPTMnet; Q7LG56; -. DR PhosphoSitePlus; Q7LG56; -. DR BioMuta; RRM2B; -. DR DMDM; 74727333; -. DR jPOST; Q7LG56; -. DR MassIVE; Q7LG56; -. DR PaxDb; 9606-ENSP00000251810; -. DR PeptideAtlas; Q7LG56; -. DR ProteomicsDB; 5837; -. DR ProteomicsDB; 68860; -. [Q7LG56-1] DR ProteomicsDB; 68861; -. [Q7LG56-2] DR ProteomicsDB; 68862; -. [Q7LG56-3] DR ProteomicsDB; 68863; -. [Q7LG56-4] DR ProteomicsDB; 68864; -. [Q7LG56-5] DR Pumba; Q7LG56; -. DR Antibodypedia; 3483; 343 antibodies from 38 providers. DR DNASU; 50484; -. DR Ensembl; ENST00000251810.8; ENSP00000251810.3; ENSG00000048392.14. [Q7LG56-1] DR Ensembl; ENST00000395912.6; ENSP00000379248.2; ENSG00000048392.14. [Q7LG56-2] DR Ensembl; ENST00000519317.5; ENSP00000430641.1; ENSG00000048392.14. [Q7LG56-3] DR Ensembl; ENST00000519962.5; ENSP00000429140.1; ENSG00000048392.14. [Q7LG56-4] DR Ensembl; ENST00000522394.1; ENSP00000429578.1; ENSG00000048392.14. [Q7LG56-5] DR GeneID; 50484; -. DR KEGG; hsa:50484; -. DR MANE-Select; ENST00000251810.8; ENSP00000251810.3; NM_015713.5; NP_056528.2. DR UCSC; uc003ykn.4; human. [Q7LG56-1] DR AGR; HGNC:17296; -. DR ClinPGx; PA34866; -. DR CTD; 50484; -. DR DisGeNET; 50484; -. DR GeneCards; RRM2B; -. DR GeneReviews; RRM2B; -. DR HGNC; HGNC:17296; RRM2B. DR HPA; ENSG00000048392; Low tissue specificity. DR MalaCards; RRM2B; -. DR MIM; 268315; phenotype. DR MIM; 604712; gene. DR MIM; 612075; phenotype. DR MIM; 613077; phenotype. DR OpenTargets; ENSG00000048392; -. DR Orphanet; 329336; Adult-onset chronic progressive external ophthalmoplegia with mitochondrial myopathy. DR Orphanet; 254892; Autosomal dominant progressive external ophthalmoplegia. DR Orphanet; 480; Kearns-Sayre syndrome. DR Orphanet; 255235; Mitochondrial DNA depletion syndrome, encephalomyopathic form with renal tubulopathy. DR Orphanet; 298; Mitochondrial neurogastrointestinal encephalomyopathy. DR VEuPathDB; HostDB:ENSG00000048392; -. DR eggNOG; KOG1567; Eukaryota. DR GeneTree; ENSGT00390000013305; -. DR HOGENOM; CLU_035339_2_0_1; -. DR InParanoid; Q7LG56; -. DR OMA; LEPMFLG; -. DR OrthoDB; 10248373at2759; -. DR PAN-GO; Q7LG56; 3 GO annotations based on evolutionary models. DR PhylomeDB; Q7LG56; -. DR BRENDA; 1.17.4.1; 2681. DR PathwayCommons; Q7LG56; -. DR Reactome; R-HSA-499943; Interconversion of nucleotide di- and triphosphates. DR Reactome; R-HSA-5628897; TP53 Regulates Metabolic Genes. DR SignaLink; Q7LG56; -. DR SIGNOR; Q7LG56; -. DR Agora; ENSG00000048392; Agora Nominated Target for Alzheimer's Disease. DR BioGRID-ORCS; 50484; 17 hits in 1170 CRISPR screens. DR ChiTaRS; RRM2B; human. DR EvolutionaryTrace; Q7LG56; -. DR GeneWiki; RRM2B; -. DR GenomeRNAi; 50484; -. DR Pharos; Q7LG56; Tbio. DR PRO; PR:Q7LG56; -. DR Proteomes; UP000005640; Chromosome 8. DR RNAct; Q7LG56; protein. DR Bgee; ENSG00000048392; Expressed in secondary oocyte and 188 other cell types or tissues. DR ExpressionAtlas; Q7LG56; baseline and differential. DR GO; GO:0005829; C:cytosol; IDA:HPA. DR GO; GO:0005739; C:mitochondrion; IEA:GOC. DR GO; GO:0005654; C:nucleoplasm; IDA:HPA. DR GO; GO:0005971; C:ribonucleoside-diphosphate reductase complex; ISS:ComplexPortal. DR GO; GO:0042802; F:identical protein binding; IPI:IntAct. DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW. DR GO; GO:0004748; F:ribonucleoside-diphosphate reductase activity, thioredoxin disulfide as acceptor; IBA:GO_Central. DR GO; GO:0009265; P:2'-deoxyribonucleotide biosynthetic process; IDA:ComplexPortal. DR GO; GO:0009200; P:deoxyribonucleoside triphosphate metabolic process; IEA:Ensembl. DR GO; GO:0009263; P:deoxyribonucleotide biosynthetic process; IBA:GO_Central. DR GO; GO:0006281; P:DNA repair; IDA:ComplexPortal. DR GO; GO:0000731; P:DNA synthesis involved in DNA repair; NAS:ComplexPortal. DR GO; GO:0001822; P:kidney development; IEA:Ensembl. DR GO; GO:0006264; P:mitochondrial DNA replication; IMP:ComplexPortal. DR GO; GO:1902254; P:negative regulation of intrinsic apoptotic signaling pathway by p53 class mediator; IEA:Ensembl. DR GO; GO:0070318; P:positive regulation of G0 to G1 transition; IDA:ComplexPortal. DR GO; GO:0010971; P:positive regulation of G2/M transition of mitotic cell cycle; IDA:ComplexPortal. DR GO; GO:0003014; P:renal system process; IEA:Ensembl. DR GO; GO:0014075; P:response to amine; IEA:Ensembl. DR GO; GO:0006979; P:response to oxidative stress; IEA:Ensembl. DR GO; GO:0009185; P:ribonucleoside diphosphate metabolic process; IDA:ComplexPortal. DR CDD; cd01049; RNRR2; 1. DR FunFam; 1.10.620.20:FF:000004; Ribonucleoside-diphosphate reductase subunit M2 B; 1. DR Gene3D; 1.10.620.20; Ribonucleotide Reductase, subunit A; 1. DR InterPro; IPR009078; Ferritin-like_SF. DR InterPro; IPR012348; RNR-like. DR InterPro; IPR033909; RNR_small. DR InterPro; IPR030475; RNR_small_AS. DR InterPro; IPR000358; RNR_small_fam. DR PANTHER; PTHR23409; RIBONUCLEOSIDE-DIPHOSPHATE REDUCTASE SMALL CHAIN; 1. DR PANTHER; PTHR23409:SF19; RIBONUCLEOSIDE-DIPHOSPHATE REDUCTASE SUBUNIT M2 B; 1. DR Pfam; PF00268; Ribonuc_red_sm; 1. DR SUPFAM; SSF47240; Ferritin-like; 1. DR PROSITE; PS00368; RIBORED_SMALL; 1. PE 1: Evidence at protein level; KW 3D-structure; Alternative splicing; Cytoplasm; Deafness; KW Deoxyribonucleotide synthesis; Disease variant; DNA damage; DNA repair; KW Iron; Metal-binding; Neuropathy; Nucleus; Oxidoreductase; KW Primary mitochondrial disease; Progressive external ophthalmoplegia; KW Proteomics identification; Reference proteome. FT CHAIN 1..351 FT /note="Ribonucleoside-diphosphate reductase subunit M2 B" FT /id="PRO_0000228150" FT REGION 1..32 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT ACT_SITE 138 FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10014" FT BINDING 100 FT /ligand="Fe cation" FT /ligand_id="ChEBI:CHEBI:24875" FT /ligand_label="1" FT BINDING 131 FT /ligand="Fe cation" FT /ligand_id="ChEBI:CHEBI:24875" FT /ligand_label="1" FT BINDING 131 FT /ligand="Fe cation" FT /ligand_id="ChEBI:CHEBI:24875" FT /ligand_label="2" FT BINDING 134 FT /ligand="Fe cation" FT /ligand_id="ChEBI:CHEBI:24875" FT /ligand_label="1" FT BINDING 194 FT /ligand="Fe cation" FT /ligand_id="ChEBI:CHEBI:24875" FT /ligand_label="2" FT BINDING 228 FT /ligand="Fe cation" FT /ligand_id="ChEBI:CHEBI:24875" FT /ligand_label="2" FT BINDING 231 FT /ligand="Fe cation" FT /ligand_id="ChEBI:CHEBI:24875" FT /ligand_label="2" FT VAR_SEQ 1..16 FT /note="MGDPERPEAAGLDQDE -> MLLLRLPPHRSHASPLDCKLQDRCRKCYSPRS FT GQACPPALAAAWLRRCERRGGRPRGGRRKELTLGLRPARCSAPGPAKDDAWRPQAG FT (in isoform 6)" FT /evidence="ECO:0000303|PubMed:14702039" FT /id="VSP_053585" FT VAR_SEQ 17..301 FT /note="Missing (in isoform 4)" FT /evidence="ECO:0000303|Ref.2" FT /id="VSP_017668" FT VAR_SEQ 17..228 FT /note="Missing (in isoform 3)" FT /evidence="ECO:0000303|Ref.2" FT /id="VSP_017669" FT VAR_SEQ 17..68 FT /note="Missing (in isoform 2)" FT /evidence="ECO:0000303|Ref.2" FT /id="VSP_017670" FT VAR_SEQ 42..43 FT /note="FV -> SF (in isoform 5)" FT /evidence="ECO:0000303|Ref.2" FT /id="VSP_017671" FT VAR_SEQ 44..351 FT /note="Missing (in isoform 5)" FT /evidence="ECO:0000303|Ref.2" FT /id="VSP_017672" FT VARIANT 33 FT /note="P -> S (found in a patient with combined respiratory FT complex deficiencies, muscle weakness and hearing loss; FT uncertain significance; dbSNP:rs387906892)" FT /evidence="ECO:0000269|PubMed:26741492" FT /id="VAR_076280" FT VARIANT 64 FT /note="W -> R (in MTDPS8A; dbSNP:rs515726182)" FT /evidence="ECO:0000269|PubMed:17486094" FT /id="VAR_046217" FT VARIANT 85 FT /note="Missing (in MTDPS8A; dbSNP:rs515726184)" FT /evidence="ECO:0000269|PubMed:17486094" FT /id="VAR_046218" FT VARIANT 110 FT /note="R -> H (in MTDPS8B; dbSNP:rs267607025)" FT /evidence="ECO:0000269|PubMed:19667227" FT /id="VAR_065122" FT VARIANT 115 FT /note="V -> L (in colorectal adenocarcinomas cell line; FT loss of ribonucleotide reductase activity)" FT /evidence="ECO:0000269|PubMed:11719458" FT /id="VAR_025699" FT VARIANT 121 FT /note="R -> H (in MTDPS8B; dbSNP:rs267607024)" FT /evidence="ECO:0000269|PubMed:19667227" FT /id="VAR_065123" FT VARIANT 194 FT /note="E -> G (in MTDPS8A; dbSNP:rs515726191)" FT /evidence="ECO:0000269|PubMed:17486094" FT /id="VAR_046219" FT VARIANT 194 FT /note="E -> K (in MTDPS8A; dbSNP:rs121918308)" FT /evidence="ECO:0000269|PubMed:17486094" FT /id="VAR_046220" FT VARIANT 224 FT /note="I -> S (in MTDPS8A; without tubulopathy; FT dbSNP:rs515726196)" FT /evidence="ECO:0000269|PubMed:18504129" FT /id="VAR_046221" FT VARIANT 236 FT /note="C -> F (in MTDPS8A; dbSNP:rs121918309)" FT /evidence="ECO:0000269|PubMed:17486094" FT /id="VAR_046222" FT VARIANT 262 FT /note="E -> D (in RCDFRD; dbSNP:rs1810682433)" FT /evidence="ECO:0000269|PubMed:32827185" FT /id="VAR_086956" FT VARIANT 282 FT /note="M -> I (in MTDPS8A; without tubulopathy; FT dbSNP:rs182614164)" FT /evidence="ECO:0000269|PubMed:18504129" FT /id="VAR_046223" FT VARIANT 317 FT /note="L -> V (in MTDPS8A; without tubulopathy; FT dbSNP:rs515726198)" FT /evidence="ECO:0000269|PubMed:18504129" FT /id="VAR_046224" FT CONFLICT 277 FT /note="M -> V (in Ref. 3; BAA92005)" FT /evidence="ECO:0000305" FT HELIX 29..31 FT /evidence="ECO:0007829|PDB:4DJN" FT TURN 33..35 FT /evidence="ECO:0007829|PDB:4DJN" FT HELIX 37..39 FT /evidence="ECO:0007829|PDB:4DJN" FT STRAND 42..44 FT /evidence="ECO:0007829|PDB:4DJN" FT HELIX 50..61 FT /evidence="ECO:0007829|PDB:4DJN" FT HELIX 66..68 FT /evidence="ECO:0007829|PDB:4DJN" FT HELIX 74..78 FT /evidence="ECO:0007829|PDB:4DJN" FT HELIX 83..109 FT /evidence="ECO:0007829|PDB:4DJN" FT HELIX 111..114 FT /evidence="ECO:0007829|PDB:4DJN" FT HELIX 118..145 FT /evidence="ECO:0007829|PDB:4DJN" FT HELIX 149..156 FT /evidence="ECO:0007829|PDB:4DJN" FT HELIX 158..161 FT /evidence="ECO:0007829|PDB:4DJN" FT HELIX 163..177 FT /evidence="ECO:0007829|PDB:4DJN" FT STRAND 179..181 FT /evidence="ECO:0007829|PDB:4DJN" FT HELIX 183..195 FT /evidence="ECO:0007829|PDB:4DJN" FT TURN 196..198 FT /evidence="ECO:0007829|PDB:4DJN" FT HELIX 199..210 FT /evidence="ECO:0007829|PDB:4DJN" FT HELIX 215..240 FT /evidence="ECO:0007829|PDB:4DJN" FT HELIX 248..267 FT /evidence="ECO:0007829|PDB:4DJN" FT HELIX 272..275 FT /evidence="ECO:0007829|PDB:4DJN" FT HELIX 279..296 FT /evidence="ECO:0007829|PDB:4DJN" FT HELIX 310..312 FT /evidence="ECO:0007829|PDB:4DJN" SQ SEQUENCE 351 AA; 40737 MW; 6D008687EEF40994 CRC64; MGDPERPEAA GLDQDERSSS DTNESEIKSN EEPLLRKSSR RFVIFPIQYP DIWKMYKQAQ ASFWTAEEVD LSKDLPHWNK LKADEKYFIS HILAFFAASD GIVNENLVER FSQEVQVPEA RCFYGFQILI ENVHSEMYSL LIDTYIRDPK KREFLFNAIE TMPYVKKKAD WALRWIADRK STFGERVVAF AAVEGVFFSG SFAAIFWLKK RGLMPGLTFS NELISRDEGL HCDFACLMFQ YLVNKPSEER VREIIVDAVK IEQEFLTEAL PVGLIGMNCI LMKQYIEFVA DRLLVELGFS KVFQAENPFD FMENISLEGK TNFFEKRVSE YQRFAVMAET TDNVFTLDAD F // ID TAF1_HUMAN Reviewed; 1893 AA. AC P21675; A5CVC8; A5CVC9; A5CVD0; A5CVD1; B1Q2X3; Q59FZ3; Q6IUZ1; Q70Q86; AC Q70Q87; Q70T00; Q70T01; Q70T02; Q70T03; DT 01-MAY-1991, integrated into UniProtKB/Swiss-Prot. DT 08-NOV-2023, sequence version 3. DT 28-JAN-2026, entry version 249. DE RecName: Full=Transcription initiation factor TFIID subunit 1 {ECO:0000305}; DE EC=2.3.1.48 {ECO:0000269|PubMed:15870300}; DE EC=2.7.11.1; DE AltName: Full=Cell cycle gene 1 protein; DE AltName: Full=TBP-associated factor 250 kDa; DE Short=p250; DE AltName: Full=Transcription initiation factor TFIID 250 kDa subunit; DE Short=TAF(II)250; DE Short=TAFII-250; DE Short=TAFII250; GN Name=TAF1 {ECO:0000312|HGNC:HGNC:11535}; Synonyms=BA2R, CCG1, CCGS, TAF2A; OS Homo sapiens (Human). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia; OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae; OC Homo. OX NCBI_TaxID=9606; RN [1] RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), FUNCTION, AND SUBCELLULAR LOCATION. RC TISSUE=Laryngeal carcinoma; RX PubMed=2038334; DOI=10.1128/mcb.11.6.3317-3325.1991; RA Sekiguchi T., Nohiro Y., Nakamura Y., Hisamoto N., Nishimoto T.; RT "The human CCG1 gene, essential for progression of the G1 phase, encodes a RT 210-kilodalton nuclear DNA-binding protein."; RL Mol. Cell. Biol. 11:3317-3325(1991). RN [2] RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), AND INTERACTION WITH TBP AND TAFS. RX PubMed=7680771; DOI=10.1038/362175a0; RA Ruppert S., Wang E.H., Tjian R.; RT "Cloning and expression of human TAFII250: a TBP-associated factor RT implicated in cell-cycle regulation."; RL Nature 362:175-179(1993). RN [3] RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM N-TAF1), AND INVOLVEMENT IN DYT3. RC TISSUE=Brain; RX PubMed=17273961; DOI=10.1086/512129; RA Makino S., Kaji R., Ando S., Tomizawa M., Yasuno K., Goto S., Matsumoto S., RA Tabuena M.D., Maranon E., Dantes M., Lee L.V., Ogasawara K., Tooyama I., RA Akatsu H., Nishimura M., Tamiya G.; RT "Reduced neuron-specific expression of the TAF1 gene is associated with X- RT linked dystonia-parkinsonism."; RL Am. J. Hum. Genet. 80:393-406(2007). RN [4] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] (ISOFORM 2), AND VARIANT VAL-290. RG NIEHS SNPs program; RL Submitted (MAY-2004) to the EMBL/GenBank/DDBJ databases. RN [5] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RX PubMed=15772651; DOI=10.1038/nature03440; RA Ross M.T., Grafham D.V., Coffey A.J., Scherer S., McLay K., Muzny D., RA Platzer M., Howell G.R., Burrows C., Bird C.P., Frankish A., Lovell F.L., RA Howe K.L., Ashurst J.L., Fulton R.S., Sudbrak R., Wen G., Jones M.C., RA Hurles M.E., Andrews T.D., Scott C.E., Searle S., Ramser J., Whittaker A., RA Deadman R., Carter N.P., Hunt S.E., Chen R., Cree A., Gunaratne P., RA Havlak P., Hodgson A., Metzker M.L., Richards S., Scott G., Steffen D., RA Sodergren E., Wheeler D.A., Worley K.C., Ainscough R., Ambrose K.D., RA Ansari-Lari M.A., Aradhya S., Ashwell R.I., Babbage A.K., Bagguley C.L., RA Ballabio A., Banerjee R., Barker G.E., Barlow K.F., Barrett I.P., RA Bates K.N., Beare D.M., Beasley H., Beasley O., Beck A., Bethel G., RA Blechschmidt K., Brady N., Bray-Allen S., Bridgeman A.M., Brown A.J., RA Brown M.J., Bonnin D., Bruford E.A., Buhay C., Burch P., Burford D., RA Burgess J., Burrill W., Burton J., Bye J.M., Carder C., Carrel L., RA Chako J., Chapman J.C., Chavez D., Chen E., Chen G., Chen Y., Chen Z., RA Chinault C., Ciccodicola A., Clark S.Y., Clarke G., Clee C.M., Clegg S., RA Clerc-Blankenburg K., Clifford K., Cobley V., Cole C.G., Conquer J.S., RA Corby N., Connor R.E., David R., Davies J., Davis C., Davis J., Delgado O., RA Deshazo D., Dhami P., Ding Y., Dinh H., Dodsworth S., Draper H., RA Dugan-Rocha S., Dunham A., Dunn M., Durbin K.J., Dutta I., Eades T., RA Ellwood M., Emery-Cohen A., Errington H., Evans K.L., Faulkner L., RA Francis F., Frankland J., Fraser A.E., Galgoczy P., Gilbert J., Gill R., RA Gloeckner G., Gregory S.G., Gribble S., Griffiths C., Grocock R., Gu Y., RA Gwilliam R., Hamilton C., Hart E.A., Hawes A., Heath P.D., Heitmann K., RA Hennig S., Hernandez J., Hinzmann B., Ho S., Hoffs M., Howden P.J., RA Huckle E.J., Hume J., Hunt P.J., Hunt A.R., Isherwood J., Jacob L., RA Johnson D., Jones S., de Jong P.J., Joseph S.S., Keenan S., Kelly S., RA Kershaw J.K., Khan Z., Kioschis P., Klages S., Knights A.J., Kosiura A., RA Kovar-Smith C., Laird G.K., Langford C., Lawlor S., Leversha M., Lewis L., RA Liu W., Lloyd C., Lloyd D.M., Loulseged H., Loveland J.E., Lovell J.D., RA Lozado R., Lu J., Lyne R., Ma J., Maheshwari M., Matthews L.H., RA McDowall J., McLaren S., McMurray A., Meidl P., Meitinger T., Milne S., RA Miner G., Mistry S.L., Morgan M., Morris S., Mueller I., Mullikin J.C., RA Nguyen N., Nordsiek G., Nyakatura G., O'dell C.N., Okwuonu G., Palmer S., RA Pandian R., Parker D., Parrish J., Pasternak S., Patel D., Pearce A.V., RA Pearson D.M., Pelan S.E., Perez L., Porter K.M., Ramsey Y., Reichwald K., RA Rhodes S., Ridler K.A., Schlessinger D., Schueler M.G., Sehra H.K., RA Shaw-Smith C., Shen H., Sheridan E.M., Shownkeen R., Skuce C.D., RA Smith M.L., Sotheran E.C., Steingruber H.E., Steward C.A., Storey R., RA Swann R.M., Swarbreck D., Tabor P.E., Taudien S., Taylor T., Teague B., RA Thomas K., Thorpe A., Timms K., Tracey A., Trevanion S., Tromans A.C., RA d'Urso M., Verduzco D., Villasana D., Waldron L., Wall M., Wang Q., RA Warren J., Warry G.L., Wei X., West A., Whitehead S.L., Whiteley M.N., RA Wilkinson J.E., Willey D.L., Williams G., Williams L., Williamson A., RA Williamson H., Wilming L., Woodmansey R.L., Wray P.W., Yen J., Zhang J., RA Zhou J., Zoghbi H., Zorilla S., Buck D., Reinhardt R., Poustka A., RA Rosenthal A., Lehrach H., Meindl A., Minx P.J., Hillier L.W., Willard H.F., RA Wilson R.K., Waterston R.H., Rice C.M., Vaudin M., Coulson A., Nelson D.L., RA Weinstock G., Sulston J.E., Durbin R.M., Hubbard T., Gibbs R.A., Beck S., RA Rogers J., Bentley D.R.; RT "The DNA sequence of the human X chromosome."; RL Nature 434:325-337(2005). RN [6] RP NUCLEOTIDE SEQUENCE [MRNA] OF 61-1604 (ISOFORM 1). RX PubMed=3169001; DOI=10.1002/j.1460-2075.1988.tb02996.x; RA Sekiguchi T., Miyata T., Nishimoto T.; RT "Molecular cloning of the cDNA of human X chromosomal gene (CCG1) which RT complements the temperature-sensitive G1 mutants, tsBN462 and ts13, of the RT BHK cell line."; RL EMBO J. 7:1683-1687(1988). RN [7] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 858-1893 (ISOFORM 4). RC TISSUE=Brain; RA Totoki Y., Toyoda A., Takeda T., Sakaki Y., Tanaka A., Yokoyama S., RA Ohara O., Nagase T., Kikuno R.F.; RL Submitted (MAR-2005) to the EMBL/GenBank/DDBJ databases. RN [8] RP NUCLEOTIDE SEQUENCE [MRNA] OF 1368-1893 (ISOFORMS 2A; 2C; 2D AND 2E), RP NUCLEOTIDE SEQUENCE [MRNA] OF 1519-1893 (ISOFORM 16), NUCLEOTIDE SEQUENCE RP [MRNA] OF 1749-1893 (ISOFORM 15), AND INVOLVEMENT IN DYT3. RC TISSUE=Fetal brain; RX PubMed=12928496; DOI=10.1073/pnas.1831949100; RA Nolte D., Niemann S., Muller U.; RT "Specific sequence changes in multiple transcript system DYT3 are RT associated with X-linked dystonia parkinsonism."; RL Proc. Natl. Acad. Sci. U.S.A. 100:10347-10352(2003). RN [9] RP SEQUENCE REVISION (ISOFORMS 2A; 2C; 2D AND 2E), NUCLEOTIDE SEQUENCE [MRNA] RP OF 1368-1893 (ISOFORMS 2E; 2G; 2H AND 2I), AND ALTERNATIVE SPLICING. RX PubMed=17952504; DOI=10.1007/s00335-007-9063-z; RA Herzfeld T., Nolte D., Muller U.; RT "Structural and functional analysis of the human TAF1/DYT3 multiple RT transcript system."; RL Mamm. Genome 18:787-795(2007). RN [10] RP FUNCTION. RX PubMed=8450888; DOI=10.1038/362179a0; RA Hisatake K., Hasegawa S., Takada R., Nakatani Y., Horikoshi M., RA Roeder R.G.; RT "The p250 subunit of native TATA box-binding factor TFIID is the cell-cycle RT regulatory protein CCG1."; RL Nature 362:179-181(1993). RN [11] RP FUNCTION, ACTIVITY REGULATION, PHOSPHORYLATION AT SER-137 AND SER-328, AND RP ATP-BINDING. RX PubMed=8625415; DOI=10.1016/s0092-8674(00)81055-7; RA Dikstein R., Ruppert S., Tjian R.; RT "TAFII250 is a bipartite protein kinase that phosphorylates the base RT transcription factor RAP74."; RL Cell 84:781-790(1996). RN [12] RP INTERACTION WITH SV40 LARGE T ANTIGEN (MICROBIAL INFECTION). RX PubMed=8647434; DOI=10.1101/gad.10.11.1369; RA Damania B., Alwine J.C.; RT "TAF-like function of SV40 large T antigen."; RL Genes Dev. 10:1369-1381(1996). RN [13] RP INTERACTION WITH HERPES SIMPLEX VIRUS 1 ICP4 (MICROBIAL INFECTION). RX PubMed=8649420; DOI=10.1128/mcb.16.6.3085; RA Carrozza M.J., DeLuca N.A.; RT "Interaction of the viral activator protein ICP4 with TFIID through RT TAF250."; RL Mol. Cell. Biol. 16:3085-3093(1996). RN [14] RP FUNCTION, AND MUTAGENESIS. RX PubMed=9660973; DOI=10.1016/s1097-2765(00)80089-1; RA O'Brien T., Tjian R.; RT "Functional analysis of the human TAFII250 N-terminal kinase domain."; RL Mol. Cell 1:905-911(1998). RN [15] RP FUNCTION, ACTIVITY REGULATION, INTERACTION WITH RB1, AND ATP-BINDING. RX PubMed=9858607; DOI=10.1128/mcb.19.1.846; RA Siegert J.L., Robbins P.D.; RT "Rb inhibits the intrinsic kinase activity of TATA-binding protein- RT associated factor TAFII250."; RL Mol. Cell. Biol. 19:846-854(1999). RN [16] RP INTERACTION WITH ASF1A. RX PubMed=10759893; DOI=10.1046/j.1365-2443.2000.00319.x; RA Munakata T., Adachi N., Yokoyama N., Kuzuhara T., Horikoshi M.; RT "A human homologue of yeast anti-silencing factor has histone chaperone RT activity."; RL Genes Cells 5:221-233(2000). RN [17] RP FUNCTION. RX PubMed=11278496; DOI=10.1074/jbc.m009385200; RA Solow S., Salunek M., Ryan R., Lieberman P.M.; RT "Taf(II) 250 phosphorylates human transcription factor IIA on serine RT residues important for TBP binding and transcription activity."; RL J. Biol. Chem. 276:15886-15892(2001). RN [18] RP ACTIVITY REGULATION, AND INTERACTION WITH TAF7. RX PubMed=11592977; DOI=10.1073/pnas.211444798; RA Gegonne A., Weissman J.D., Singer D.S.; RT "TAFII55 binding to TAFII250 inhibits its acetyltransferase activity."; RL Proc. Natl. Acad. Sci. U.S.A. 98:12432-12437(2001). RN [19] RP INTERACTION WITH ASF1A. RX PubMed=12093919; DOI=10.1073/pnas.142627899; RA Chimura T., Kuzuhara T., Horikoshi M.; RT "Identification and characterization of CIA/ASF1 as an interactor of RT bromodomains associated with TFIID."; RL Proc. Natl. Acad. Sci. U.S.A. 99:9334-9339(2002). RN [20] RP INTERACTION WITH ASF1A AND ASF1B. RX PubMed=12842904; DOI=10.1074/jbc.m303549200; RA Umehara T., Horikoshi M.; RT "Transcription initiation factor IID-interactive histone chaperone CIA-II RT implicated in mammalian spermatogenesis."; RL J. Biol. Chem. 278:35660-35667(2003). RN [21] RP FUNCTION, AND INTERACTION WITH TP53. RX PubMed=15053879; DOI=10.1016/s1097-2765(04)00123-6; RA Li H.-H., Li A.G., Sheppard H.M., Liu X.; RT "Phosphorylation on Thr-55 by TAF1 mediates degradation of p53: a role for RT TAF1 in cell G1 progression."; RL Mol. Cell 13:867-878(2004). RN [22] RP IDENTIFICATION IN THE MLL1/MLL COMPLEX. RX PubMed=15960975; DOI=10.1016/j.cell.2005.04.031; RA Dou Y., Milne T.A., Tackett A.J., Smith E.R., Fukuda A., Wysocka J., RA Allis C.D., Chait B.T., Hess J.L., Roeder R.G.; RT "Physical association and coordinate function of the H3 K4 RT methyltransferase MLL1 and the H4 K16 acetyltransferase MOF."; RL Cell 121:873-885(2005). RN [23] RP HISTONE ACETYLTRANSFERASE ACTIVITY, AND MUTAGENESIS OF GLU-742 AND RP 848-MET--ASP-850. RX PubMed=15870300; DOI=10.1128/mcb.25.10.4321-4332.2005; RA Hilton T.L., Li Y., Dunphy E.L., Wang E.H.; RT "TAF1 histone acetyltransferase activity in Sp1 activation of the cyclin D1 RT promoter."; RL Mol. Cell. Biol. 25:4321-4332(2005). RN [24] RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Cervix carcinoma; RX PubMed=18669648; DOI=10.1073/pnas.0805139105; RA Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E., RA Elledge S.J., Gygi S.P.; RT "A quantitative atlas of mitotic phosphorylation."; RL Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008). RN [25] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1847, AND IDENTIFICATION BY RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Leukemic T-cell; RX PubMed=19690332; DOI=10.1126/scisignal.2000007; RA Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K., RA Rodionov V., Han D.K.; RT "Quantitative phosphoproteomic analysis of T cell receptor signaling RT reveals system-wide modulation of protein-protein interactions."; RL Sci. Signal. 2:RA46-RA46(2009). RN [26] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1721 (ISOFORMS 2A AND 4), RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1723 (ISOFORM 2G), RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1718 (ISOFORM 16), AND RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Cervix carcinoma; RX PubMed=20068231; DOI=10.1126/scisignal.2000475; RA Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L., RA Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S., Mann M.; RT "Quantitative phosphoproteomics reveals widespread full phosphorylation RT site occupancy during mitosis."; RL Sci. Signal. 3:RA3-RA3(2010). RN [27] RP ACTIVITY REGULATION. RX PubMed=22711989; DOI=10.1128/mcb.00416-12; RA Kloet S.L., Whiting J.L., Gafken P., Ranish J., Wang E.H.; RT "Phosphorylation-dependent regulation of cyclin D1 and cyclin A gene RT transcription by TFIID subunits TAF1 and TAF7."; RL Mol. Cell. Biol. 32:3358-3369(2012). RN [28] RP MISCELLANEOUS. RX PubMed=23184149; DOI=10.1093/hmg/dds499; RA Herzfeld T., Nolte D., Grznarova M., Hofmann A., Schultze J.L., Muller U.; RT "X-linked dystonia parkinsonism syndrome (XDP, lubag): disease-specific RT sequence change DSC3 in TAF1/DYT3 affects genes in vesicular transport and RT dopamine metabolism."; RL Hum. Mol. Genet. 22:941-951(2013). RN [29] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-328, AND IDENTIFICATION BY RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Liver; RX PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014; RA Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., Wang L., RA Ye M., Zou H.; RT "An enzyme assisted RP-RPLC approach for in-depth analysis of human liver RT phosphoproteome."; RL J. Proteomics 96:253-262(2014). RN [30] RP SUBCELLULAR LOCATION. RX PubMed=25593309; DOI=10.1101/gad.252189.114; RA Gong F., Chiu L.Y., Cox B., Aymard F., Clouaire T., Leung J.W., RA Cammarata M., Perez M., Agarwal P., Brodbelt J.S., Legube G., Miller K.M.; RT "Screen identifies bromodomain protein ZMYND8 in chromatin recognition of RT transcription-associated DNA damage that promotes homologous RT recombination."; RL Genes Dev. 29:197-211(2015). RN [31] RP SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-570 AND LYS-583, AND RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RX PubMed=28112733; DOI=10.1038/nsmb.3366; RA Hendriks I.A., Lyon D., Young C., Jensen L.J., Vertegaal A.C., RA Nielsen M.L.; RT "Site-specific mapping of the human SUMO proteome reveals co-modification RT with phosphorylation."; RL Nat. Struct. Mol. Biol. 24:325-336(2017). RN [32] RP X-RAY CRYSTALLOGRAPHY (2.1 ANGSTROMS) OF 1380-1659. RX PubMed=10827952; DOI=10.1126/science.288.5470.1422; RA Jacobson R.H., Ladurner A.G., King D.S., Tjian R.; RT "Structure and function of a human TAFII250 double bromodomain module."; RL Science 288:1422-1425(2000). RN [33] RP X-RAY CRYSTALLOGRAPHY (1.89 ANGSTROMS) OF 1522-1656, AND SUBUNIT. RX PubMed=22464331; DOI=10.1016/j.cell.2012.02.013; RA Filippakopoulos P., Picaud S., Mangos M., Keates T., Lambert J.P., RA Barsyte-Lovejoy D., Felletar I., Volkmer R., Muller S., Pawson T., RA Gingras A.C., Arrowsmith C.H., Knapp S.; RT "Histone recognition and large-scale structural analysis of the human RT bromodomain family."; RL Cell 149:214-231(2012). RN [34] RP X-RAY CRYSTALLOGRAPHY (2.30 ANGSTROMS) OF 600-1236 IN COMPLEX WITH TAF7, RP FUNCTION, AND INTERACTION WITH TAF7. RX PubMed=25412659; DOI=10.1038/cr.2014.148; RA Wang H., Curran E.C., Hinds T.R., Wang E.H., Zheng N.; RT "Crystal structure of a TAF1-TAF7 complex in human transcription factor IID RT reveals a promoter binding module."; RL Cell Res. 24:1433-1444(2014). RN [35] RP X-RAY CRYSTALLOGRAPHY (1.50 ANGSTROMS) OF 1518-1659 IN COMPLEX WITH RP CROTONYLATED OR BUTYRYLATED HISTONE H4. RX PubMed=26365797; DOI=10.1016/j.str.2015.08.004; RA Flynn E.M., Huang O.W., Poy F., Oppikofer M., Bellon S.F., Tang Y., RA Cochran A.G.; RT "A subset of human bromodomains recognizes butyryllysine and crotonyllysine RT histone peptide modifications."; RL Structure 23:1801-1814(2015). RN [36] RP STRUCTURE BY ELECTRON MICROSCOPY (8.50 ANGSTROMS), AND SUBCELLULAR RP LOCATION. RX PubMed=27007846; DOI=10.1038/nature17394; RA Louder R.K., He Y., Lopez-Blanco J.R., Fang J., Chacon P., Nogales E.; RT "Structure of promoter-bound TFIID and model of human pre-initiation RT complex assembly."; RL Nature 531:604-609(2016). RN [37] {ECO:0007744|PDB:6FIC} RP X-RAY CRYSTALLOGRAPHY (2.18 ANGSTROMS) OF 1380-1659. RA Mathea S., Suh J.L., Salah E., Tallant C., Siejka P., Pike A.C.W., RA von Delft F., Arrowsmith C.H., Edwards A.M., Bountra C., James L.I., RA Frye S.V., Knapp S.; RT "Bivalent Inhibitor UNC4512 Bound to the TAF1 Bromodomain Tandem."; RL Submitted (JAN-2018) to the PDB data bank. RN [38] {ECO:0007744|PDB:6P39, ECO:0007744|PDB:6P3A} RP X-RAY CRYSTALLOGRAPHY (2.94 ANGSTROMS) OF 1521-1656. RA Seo H.-S., Dhe-Paganon S.; RT "Crystal Structure Analysis of TAF1 Bromodomain."; RL Submitted (MAY-2019) to the PDB data bank. RN [39] {ECO:0007744|PDB:7JJG} RP X-RAY CRYSTALLOGRAPHY (1.60 ANGSTROMS) OF 1522-1656. RA Karim M.R., Schonbrunn E.; RT "Crystal structure of the second bromodomain (BD2) of human TAF1 bound to RT ATR kinase inhibitor AZ20."; RL Submitted (JUL-2020) to the PDB data bank. RN [40] {ECO:0007744|PDB:7JJH} RP X-RAY CRYSTALLOGRAPHY (2.10 ANGSTROMS) OF 1394-1656. RA Karim M.R., Schonbrunn E.; RT "Crystal structure of the unliganded tandem bromodomain (BD1, BD2) of human RT TAF1."; RL Submitted (JUL-2020) to the PDB data bank. RN [41] {ECO:0007744|PDB:7JSP} RP X-RAY CRYSTALLOGRAPHY (1.70 ANGSTROMS) OF 1522-1656. RA Karim M.R., Schonbrunn E.; RT "Crystal structure of the second bromodomain (BD2) of human TAF1 bound to RT the ATR kinase inhibitor AZD6738."; RL Submitted (AUG-2020) to the PDB data bank. RN [42] {ECO:0007744|PDB:7JTC} RP X-RAY CRYSTALLOGRAPHY (2.05 ANGSTROMS) OF 1522-1656. RA Karim M.R., Schonbrunn E.; RT "Crystal structure of the second bromodomain (BD2) of human TAF1 bound to RT ZS1-322."; RL Submitted (AUG-2020) to the PDB data bank. RN [43] {ECO:0007744|PDB:7K03} RP X-RAY CRYSTALLOGRAPHY (1.60 ANGSTROMS) OF 1394-1656. RA Karim M.R., Schonbrunn E.; RT "Crystal structure of the tandem bromodomain (BD1 and BD2) of human TAF1 RT bound to ATR kinase inhibitor AZD6738."; RL Submitted (SEP-2020) to the PDB data bank. RN [44] {ECO:0007744|PDB:7K0D} RP X-RAY CRYSTALLOGRAPHY (2.20 ANGSTROMS) OF 1394-1656. RA Karim M.R., Schonbrunn E.; RT "Crystal structure of the tandem bromodomain (BD1, BD2) of human TAF1 bound RT to mTORC1/2 inhibitor AZD3147."; RL Submitted (SEP-2020) to the PDB data bank. RN [45] {ECO:0007744|PDB:7K0U} RP X-RAY CRYSTALLOGRAPHY (2.52 ANGSTROMS) OF 1522-1656. RA Karim M.R., Schonbrunn E.; RT "Crystal structure of the second bromodomain (BD2) of human TAF1 bound to RT PLK1 kinase inhibitor BI2536."; RL Submitted (SEP-2020) to the PDB data bank. RN [46] {ECO:0007744|PDB:7K1P} RP X-RAY CRYSTALLOGRAPHY (2.45 ANGSTROMS) OF 1522-1656. RA Karim M.R., Schonbrunn E.; RT "Crystal structure of the second bromodomain (BD2) of human TAF1 bound to RT bromosporine."; RL Submitted (SEP-2020) to the PDB data bank. RN [47] {ECO:0007744|PDB:7K27} RP X-RAY CRYSTALLOGRAPHY (1.50 ANGSTROMS) OF 1394-1656. RA Karim M.R., Schonbrunn E.; RT "Crystal structure of the tandem bromodomain (BD1, BD2) of human TAF1 bound RT to ATR inhibitor AZ20."; RL Submitted (SEP-2020) to the PDB data bank. RN [48] {ECO:0007744|PDB:7K3O} RP X-RAY CRYSTALLOGRAPHY (1.70 ANGSTROMS) OF 1522-1656. RA Karim M.R., Schonbrunn E.; RT "Crystal structure of the unliganded second bromodomain (BD2) of human RT TAF1."; RL Submitted (SEP-2020) to the PDB data bank. RN [49] {ECO:0007744|PDB:7K42} RP X-RAY CRYSTALLOGRAPHY (1.70 ANGSTROMS) OF 1522-1656. RA Karim M.R., Schonbrunn E.; RT "Crystal structure of the second bromodomain (BD2) of human TAF1 bound to RT dioxane."; RL Submitted (SEP-2020) to the PDB data bank. RN [50] {ECO:0007744|PDB:7K6F} RP X-RAY CRYSTALLOGRAPHY (1.86 ANGSTROMS) OF 1394-1656. RA Karim M.R., Bikowitz M.J., Schonbrunn E.; RT "Crystal structure of the tandem bromodomain (BD1, BD2) of human TAF1 in RT complex with MES (2-(N-morpholino)ethanesulfonic acid)."; RL Submitted (SEP-2020) to the PDB data bank. RN [51] {ECO:0007744|PDB:7L6X} RP X-RAY CRYSTALLOGRAPHY (2.75 ANGSTROMS) OF 1394-1656. RA Karim M.R., Schonbrunn E.; RT "Crystal structure of the tandem bromodomain (BD1, BD2) of human TAF1 bound RT to GNE-371."; RL Submitted (DEC-2020) to the PDB data bank. RN [52] {ECO:0007744|PDB:7LB0} RP X-RAY CRYSTALLOGRAPHY (2.33 ANGSTROMS) OF 1394-1656. RA Karim M.R., Schonbrunn E.; RT "Crystal structure of the tandem bromodomain (BD1, BD2) of human TAF1 bound RT to ZS1-295."; RL Submitted (JAN-2021) to the PDB data bank. RN [53] {ECO:0007744|PDB:7LB1} RP X-RAY CRYSTALLOGRAPHY (1.35 ANGSTROMS) OF 1394-1656. RA Karim M.R., Schonbrunn E.; RT "Crystal structure of the tandem bromodomain (BD1, BD2) of human TAF1 bound RT to ZS1-585."; RL Submitted (JAN-2021) to the PDB data bank. RN [54] {ECO:0007744|PDB:7LB2} RP X-RAY CRYSTALLOGRAPHY (1.70 ANGSTROMS) OF 1394-1656. RA Karim M.R., Schonbrunn E.; RT "Crystal structure of the tandem bromodomain (BD1, BD2) of human TAF1 bound RT to ZS1-589."; RL Submitted (JAN-2021) to the PDB data bank. RN [55] {ECO:0007744|PDB:7N42} RP X-RAY CRYSTALLOGRAPHY (1.90 ANGSTROMS) OF 1394-1656. RA Karim M.R., Schonbrunn E.; RT "Crystal structure of the tandem bromodomain of human TAF1 (TAF1-T) bound RT to ZS1-681."; RL Submitted (JUN-2021) to the PDB data bank. RN [56] {ECO:0007744|PDB:7EDX, ECO:0007744|PDB:7EG7, ECO:0007744|PDB:7EG8, ECO:0007744|PDB:7EG9, ECO:0007744|PDB:7EGA, ECO:0007744|PDB:7EGB, ECO:0007744|PDB:7EGC, ECO:0007744|PDB:7EGD, ECO:0007744|PDB:7EGE, ECO:0007744|PDB:7EGH} RP STRUCTURE BY ELECTRON MICROSCOPY (3.04 ANGSTROMS), FUNCTION, IDENTIFICATION RP IN THE TFIID COMPLEX, AND SUBUNIT. RX PubMed=33795473; DOI=10.1126/science.aba8490; RA Chen X., Qi Y., Wu Z., Wang X., Li J., Zhao D., Hou H., Li Y., Yu Z., RA Liu W., Wang M., Ren Y., Li Z., Yang H., Xu Y.; RT "Structural insights into preinitiation complex assembly on core RT promoters."; RL Science 372:0-0(2021). RN [57] RP VARIANTS [LARGE SCALE ANALYSIS] VAL-290; GLY-318; ASP-474; LYS-672 AND RP ILE-712. RX PubMed=17344846; DOI=10.1038/nature05610; RA Greenman C., Stephens P., Smith R., Dalgliesh G.L., Hunter C., Bignell G., RA Davies H., Teague J., Butler A., Stevens C., Edkins S., O'Meara S., RA Vastrik I., Schmidt E.E., Avis T., Barthorpe S., Bhamra G., Buck G., RA Choudhury B., Clements J., Cole J., Dicks E., Forbes S., Gray K., RA Halliday K., Harrison R., Hills K., Hinton J., Jenkinson A., Jones D., RA Menzies A., Mironenko T., Perry J., Raine K., Richardson D., Shepherd R., RA Small A., Tofts C., Varian J., Webb T., West S., Widaa S., Yates A., RA Cahill D.P., Louis D.N., Goldstraw P., Nicholson A.G., Brasseur F., RA Looijenga L., Weber B.L., Chiew Y.-E., DeFazio A., Greaves M.F., RA Green A.R., Campbell P., Birney E., Easton D.F., Chenevix-Trench G., RA Tan M.-H., Khoo S.K., Teh B.T., Yuen S.T., Leung S.Y., Wooster R., RA Futreal P.A., Stratton M.R.; RT "Patterns of somatic mutation in human cancer genomes."; RL Nature 446:153-158(2007). RN [58] RP INVOLVEMENT IN MRXS33, AND VARIANTS MRXS33 SER-596; ARG-807; HIS-976; RP TRP-1246; THR-1337; HIS-1452 AND HIS-1517. RX PubMed=26637982; DOI=10.1016/j.ajhg.2015.11.005; RA O'Rawe J.A., Wu Y., Doerfel M.J., Rope A.F., Au P.Y., Parboosingh J.S., RA Moon S., Kousi M., Kosma K., Smith C.S., Tzetis M., Schuette J.L., RA Hufnagel R.B., Prada C.E., Martinez F., Orellana C., Crain J., RA Caro-Llopis A., Oltra S., Monfort S., Jimenez-Barron L.T., Swensen J., RA Ellingwood S., Smith R., Fang H., Ospina S., Stegmann S., Den Hollander N., RA Mittelman D., Highnam G., Robison R., Yang E., Faivre L., Roubertie A., RA Riviere J.B., Monaghan K.G., Wang K., Davis E.E., Katsanis N., RA Kalscheuer V.M., Wang E.H., Metcalfe K., Kleefstra T., Innes A.M., RA Kitsiou-Tzeli S., Rosello M., Keegan C.E., Lyon G.J.; RT "TAF1 Variants Are Associated with Dysmorphic Features, Intellectual RT Disability, and Neurological Manifestations."; RL Am. J. Hum. Genet. 97:922-932(2015). RN [59] RP VARIANTS ASP-493 AND CYS-1190. RX PubMed=25644381; DOI=10.1038/mp.2014.193; RA Hu H., Haas S.A., Chelly J., Van Esch H., Raynaud M., de Brouwer A.P., RA Weinert S., Froyen G., Frints S.G., Laumonnier F., Zemojtel T., Love M.I., RA Richard H., Emde A.K., Bienek M., Jensen C., Hambrock M., Fischer U., RA Langnick C., Feldkamp M., Wissink-Lindhout W., Lebrun N., Castelnau L., RA Rucci J., Montjean R., Dorseuil O., Billuart P., Stuhlmann T., Shaw M., RA Corbett M.A., Gardner A., Willis-Owen S., Tan C., Friend K.L., Belet S., RA van Roozendaal K.E., Jimenez-Pocquet M., Moizard M.P., Ronce N., Sun R., RA O'Keeffe S., Chenna R., van Boemmel A., Goeke J., Hackett A., Field M., RA Christie L., Boyle J., Haan E., Nelson J., Turner G., Baynam G., RA Gillessen-Kaesbach G., Mueller U., Steinberger D., Budny B., RA Badura-Stronka M., Latos-Bielenska A., Ousager L.B., Wieacker P., RA Rodriguez Criado G., Bondeson M.L., Anneren G., Dufke A., Cohen M., RA Van Maldergem L., Vincent-Delorme C., Echenne B., Simon-Bouy B., RA Kleefstra T., Willemsen M., Fryns J.P., Devriendt K., Ullmann R., RA Vingron M., Wrogemann K., Wienker T.F., Tzschach A., van Bokhoven H., RA Gecz J., Jentsch T.J., Chen W., Ropers H.H., Kalscheuer V.M.; RT "X-exome sequencing of 405 unresolved families identifies seven novel RT intellectual disability genes."; RL Mol. Psychiatry 21:133-148(2016). CC -!- FUNCTION: The TFIID basal transcription factor complex plays a major CC role in the initiation of RNA polymerase II (Pol II)-dependent CC transcription (PubMed:33795473). TFIID recognizes and binds promoters CC with or without a TATA box via its subunit TBP, a TATA-box-binding CC protein, and promotes assembly of the pre-initiation complex (PIC) CC (PubMed:33795473). The TFIID complex consists of TBP and TBP-associated CC factors (TAFs), including TAF1, TAF2, TAF3, TAF4, TAF5, TAF6, TAF7, CC TAF8, TAF9, TAF10, TAF11, TAF12 and TAF13 (PubMed:33795473). TAF1 is CC the largest component and core scaffold of the TFIID complex, involved CC in nucleating complex assembly (PubMed:25412659, PubMed:27007846, CC PubMed:33795473). TAF1 forms a promoter DNA binding subcomplex of CC TFIID, together with TAF7 and TAF2 (PubMed:33795473). Contains novel CC N- and C-terminal Ser/Thr kinase domains which can autophosphorylate or CC transphosphorylate other transcription factors (PubMed:25412659, CC PubMed:8625415). Phosphorylates TP53 on 'Thr-55' which leads to MDM2- CC mediated degradation of TP53 (PubMed:25412659). Phosphorylates GTF2A1 CC and GTF2F1 on Ser residues (PubMed:25412659). Possesses DNA-binding CC activity (PubMed:25412659). Essential for progression of the G1 phase CC of the cell cycle (PubMed:11278496, PubMed:15053879, PubMed:2038334, CC PubMed:8450888, PubMed:8625415, PubMed:9660973, PubMed:9858607). CC Exhibits histone acetyltransferase activity towards histones H3 and H4 CC (PubMed:15870300). {ECO:0000269|PubMed:11278496, CC ECO:0000269|PubMed:15053879, ECO:0000269|PubMed:15870300, CC ECO:0000269|PubMed:2038334, ECO:0000269|PubMed:25412659, CC ECO:0000269|PubMed:27007846, ECO:0000269|PubMed:33795473, CC ECO:0000269|PubMed:8450888, ECO:0000269|PubMed:8625415, CC ECO:0000269|PubMed:9660973, ECO:0000269|PubMed:9858607}. CC -!- CATALYTIC ACTIVITY: CC Reaction=L-seryl-[protein] + ATP = O-phospho-L-seryl-[protein] + ADP + CC H(+); Xref=Rhea:RHEA:17989, Rhea:RHEA-COMP:9863, Rhea:RHEA- CC COMP:11604, ChEBI:CHEBI:15378, ChEBI:CHEBI:29999, ChEBI:CHEBI:30616, CC ChEBI:CHEBI:83421, ChEBI:CHEBI:456216; EC=2.7.11.1; CC -!- CATALYTIC ACTIVITY: CC Reaction=L-threonyl-[protein] + ATP = O-phospho-L-threonyl-[protein] + CC ADP + H(+); Xref=Rhea:RHEA:46608, Rhea:RHEA-COMP:11060, Rhea:RHEA- CC COMP:11605, ChEBI:CHEBI:15378, ChEBI:CHEBI:30013, ChEBI:CHEBI:30616, CC ChEBI:CHEBI:61977, ChEBI:CHEBI:456216; EC=2.7.11.1; CC -!- CATALYTIC ACTIVITY: CC Reaction=L-lysyl-[protein] + acetyl-CoA = N(6)-acetyl-L-lysyl-[protein] CC + CoA + H(+); Xref=Rhea:RHEA:45948, Rhea:RHEA-COMP:9752, Rhea:RHEA- CC COMP:10731, ChEBI:CHEBI:15378, ChEBI:CHEBI:29969, ChEBI:CHEBI:57287, CC ChEBI:CHEBI:57288, ChEBI:CHEBI:61930; EC=2.3.1.48; CC Evidence={ECO:0000269|PubMed:15870300}; CC -!- COFACTOR: CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420; CC -!- ACTIVITY REGULATION: Autophosphorylates on Ser residues CC (PubMed:8625415). Inhibited by retinoblastoma tumor suppressor protein, CC RB1 (PubMed:9858607). Binding to TAF7 or CIITA inhibits the histone CC acetyltransferase activity (PubMed:11592977, PubMed:22711989). CC {ECO:0000269|PubMed:11592977, ECO:0000269|PubMed:22711989, CC ECO:0000269|PubMed:8625415, ECO:0000269|PubMed:9858607}. CC -!- SUBUNIT: Component of the TFIID basal transcription factor complex, CC composed of TATA-box-binding protein TBP, and a number of TBP- CC associated factors (TAFs), including TAF1, TAF2, TAF3, TAF4, TAF5, CC TAF6, TAF7, TAF8, TAF9, TAF10, TAF11, TAF12 and TAF13 (PubMed:33795473, CC PubMed:7680771). Interacts with TAF7; the interaction is direct CC (PubMed:11592977, PubMed:25412659). TAF1, when part of the TFIID CC complex, interacts with C-terminus of TP53 (PubMed:15053879). Part of a CC TFIID-containing RNA polymerase II pre-initiation complex that is CC composed of TBP and at least GTF2A1, GTF2A2, GTF2E1, GTF2E2, GTF2F1, CC GTF2H2, GTF2H3, GTF2H4, GTF2H5, GTF2B, TCEA1, ERCC2, ERCC3, TAF1, TAF2, CC TAF3, TAF4, TAF5, TAF6, TAF7, TAF8, TAF9, TAF10, TAF11, TAF12 and TAF13 CC (PubMed:27007846). Component of some MLL1/MLL complex, at least CC composed of the core components KMT2A/MLL1, ASH2L, HCFC1/HCF1, WDR5 and CC RBBP5, as well as the facultative components BACC1, CHD8, E2F6, HSP70, CC INO80C, KANSL1, LAS1L, MAX, MCRS1, MGA, KAT8/MOF, PELP1, PHF20, PRP31, CC RING2, RUVB1/TIP49A, RUVB2/TIP49B, SENP3, TAF1, TAF4, TAF6, TAF7, TAF9 CC and TEX10 (PubMed:15960975). RB1 interacts with the N-terminal domain CC of TAF1 (PubMed:9858607). Interacts with ASF1A and ASF1B CC (PubMed:10759893, PubMed:12093919, PubMed:12842904). Interacts (via CC bromo domains) with acetylated lysine residues on the N-terminus of CC histone H1.4, H2A, H2B, H3 and H4 (in vitro) (PubMed:22464331). CC {ECO:0000269|PubMed:10759893, ECO:0000269|PubMed:11592977, CC ECO:0000269|PubMed:12093919, ECO:0000269|PubMed:12842904, CC ECO:0000269|PubMed:15053879, ECO:0000269|PubMed:15960975, CC ECO:0000269|PubMed:22464331, ECO:0000269|PubMed:25412659, CC ECO:0000269|PubMed:27007846, ECO:0000269|PubMed:33795473, CC ECO:0000269|PubMed:7680771, ECO:0000269|PubMed:9858607}. CC -!- SUBUNIT: (Microbial infection) Interacts with SV40 Large T antigen. CC {ECO:0000269|PubMed:8647434}. CC -!- SUBUNIT: (Microbial infection) Interacts with herpes simplex virus 1 CC ICP4. {ECO:0000269|PubMed:8649420}. CC -!- INTERACTION: CC P21675; P35269: GTF2F1; NbExp=3; IntAct=EBI-491289, EBI-457886; CC P21675; P20226: TBP; NbExp=11; IntAct=EBI-491289, EBI-355371; CC P21675; P03255; Xeno; NbExp=3; IntAct=EBI-491289, EBI-2603114; CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:2038334, CC ECO:0000269|PubMed:25593309, ECO:0000269|PubMed:27007846}. CC -!- ALTERNATIVE PRODUCTS: CC Event=Alternative splicing, Alternative initiation; Named isoforms=15; CC Comment=the TAF1/DYT3 multiple transcript system is composed of 38 CC evolutionary conserved exons plus 5 downstream exons referred to as CC exons d1-d5 that are primate-specific. Multiple highly polymorphic CC variants can be generated by splicing exons d3 and d4 to various CC combinations of exons 1-37. {ECO:0000305|PubMed:17952504}; CC Name=2; CC IsoId=P21675-2; Sequence=Displayed; CC Name=1; CC IsoId=P21675-1; Sequence=VSP_061988; CC Name=13; CC IsoId=P21675-13; Sequence=VSP_061987, VSP_061988; CC Name=14; CC IsoId=P21675-14; Sequence=VSP_061987; CC Name=15; CC IsoId=P21675-15; Sequence=VSP_061999, VSP_062000; CC Name=16; CC IsoId=P21675-16; Sequence=VSP_061996, VSP_061998; CC Name=N-TAF1; Synonyms=TA14-391; CC IsoId=P21675-17; Sequence=VSP_061995; CC Name=2a; CC IsoId=P21675-18; Sequence=VSP_061997, VSP_061998; CC Name=2c; CC IsoId=P21675-19; Sequence=VSP_061998; CC Name=2d; CC IsoId=P21675-20; Sequence=VSP_061995, VSP_061998; CC Name=2e; CC IsoId=P21675-21; Sequence=VSP_061993, VSP_061994; CC Name=2g; CC IsoId=P21675-22; Sequence=VSP_061995, VSP_061997, VSP_061998; CC Name=2h; CC IsoId=P21675-23; Sequence=VSP_061990, VSP_061991; CC Name=2i; CC IsoId=P21675-24; Sequence=VSP_061989, VSP_061992; CC Name=4; CC IsoId=P21675-25; Sequence=VSP_061997; CC -!- DOMAIN: The Bromo domain mediates interaction with histones that have CC acetylated lysine residues at specific positions (PubMed:22464331). The CC second domain also recognizes and binds histones that are butyrylated CC and crotonylated (PubMed:26365797). {ECO:0000269|PubMed:22464331, CC ECO:0000269|PubMed:26365797}. CC -!- PTM: Phosphorylated by casein kinase II in vitro. CC {ECO:0000269|PubMed:8625415}. CC -!- DISEASE: Dystonia 3, torsion, X-linked (DYT3) [MIM:314250]: An X-linked CC dystonia-parkinsonism disorder. Dystonia is defined by the presence of CC sustained involuntary muscle contractions, often leading to abnormal CC postures. DYT3 is characterized by severe progressive torsion dystonia CC followed by parkinsonism. It has a well-defined pathology of extensive CC neuronal loss and mosaic gliosis in the striatum (caudate nucleus and CC putamen) which appears to resemble that in Huntington disease. CC {ECO:0000269|PubMed:12928496, ECO:0000269|PubMed:17273961}. Note=The CC disease is caused by variants affecting the gene represented in this CC entry. CC -!- DISEASE: Intellectual developmental disorder, X-linked, syndromic 33 CC (MRXS33) [MIM:300966]: A syndrome characterized by intellectual CC deficit, delayed psychomotor development, delayed speech and language, CC and characteristic facial features. {ECO:0000269|PubMed:26637982}. CC Note=The disease is caused by variants affecting the gene represented CC in this entry. CC -!- MISCELLANEOUS: [Isoform 16]: May be produced at very low levels due to CC a premature stop CC codon in the mRNA, leading to nonsense-mediated CC mRNA decay. {ECO:0000305}. CC -!- MISCELLANEOUS: [Isoform 2a]: May be produced at very low levels due to CC a premature stop CC codon in the mRNA, leading to nonsense-mediated CC mRNA decay (Probable). Includes a downstream (d) exon and is CC preferentially expressed in brain (Probable). May play a role in the CC regulation of genes involved in dopamine processing and transport CC (Probable). {ECO:0000305, ECO:0000305|PubMed:17952504}. CC -!- MISCELLANEOUS: [Isoform 2c]: May be produced at very low levels due to CC a premature stop CC codon in the mRNA, leading to nonsense-mediated CC mRNA decay (Probable). Includes a downstream (d) exon and is CC preferentially expressed in brain (Probable). May play a role in the CC regulation of genes involved in dopamine processing and transport CC (Probable). {ECO:0000305, ECO:0000305|PubMed:17952504}. CC -!- MISCELLANEOUS: [Isoform 2d]: May be produced at very low levels due to CC a premature stop CC codon in the mRNA, leading to nonsense-mediated CC mRNA decay (Probable). Includes a downstream (d) exon and is CC preferentially expressed in brain (Probable). May play a role in the CC regulation of genes involved in dopamine processing and transport CC (Probable). {ECO:0000305, ECO:0000305|PubMed:17952504}. CC -!- MISCELLANEOUS: [Isoform 2e]: May be produced at very low levels due to CC a premature stop CC codon in the mRNA, leading to nonsense-mediated CC mRNA decay (Probable). Includes a downstream (d) exon and is CC preferentially expressed in brain (Probable). May play a role in the CC regulation of genes involved in dopamine processing and transport CC (Probable). {ECO:0000305, ECO:0000305|PubMed:17952504}. CC -!- MISCELLANEOUS: [Isoform 2h]: May be produced at very low levels due to CC a premature stop CC codon in the mRNA, leading to nonsense-mediated CC mRNA decay (Probable). Includes a downstream (d) exon and is CC preferentially expressed in brain (Probable). May play a role in the CC regulation of genes involved in dopamine processing and transport CC (Probable). {ECO:0000305, ECO:0000305|PubMed:17952504}. CC -!- MISCELLANEOUS: [Isoform 2i]: May be produced at very low levels due to CC a premature stop CC codon in the mRNA, leading to nonsense-mediated CC mRNA decay (Probable). Includes a downstream (d) exon and is CC preferentially expressed in brain (Probable). May play a role in the CC regulation of genes involved in dopamine processing and transport CC (Probable). {ECO:0000305, ECO:0000305|PubMed:17952504}. CC -!- MISCELLANEOUS: [Isoform 2g]: Includes a downstream (d) exon and is CC preferentially expressed in brain (Probable). May play a role in the CC regulation of genes involved in dopamine processing and transport CC (Probable). {ECO:0000305|PubMed:17952504}. CC -!- MISCELLANEOUS: [Isoform 15]: May be produced at very low levels due to CC a premature stop CC codon in the mRNA, leading to nonsense-mediated CC mRNA decay. {ECO:0000305}. CC -!- MISCELLANEOUS: [Isoform N-TAF1]: Only detected in brain, highest CC expression in the caudate nucleus. {ECO:0000305}. CC -!- SIMILARITY: Belongs to the TAF1 family. {ECO:0000305}. CC -!- SEQUENCE CAUTION: CC Sequence=CAA30073.1; Type=Miscellaneous discrepancy; Note=Contaminating sequence. Sequence of unknown origin in the N-terminal and C-terminal part.; Evidence={ECO:0000305}; CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; D90359; BAA14374.1; -; mRNA. DR EMBL; AB300418; BAG15901.1; -; mRNA. DR EMBL; AY623109; AAT38105.1; -; Genomic_DNA. DR EMBL; AL590762; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; AL590763; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; X07024; CAA30073.1; ALT_SEQ; mRNA. DR EMBL; AB209316; BAD92553.1; -; mRNA. DR EMBL; AJ549247; CAD70490.1; -; mRNA. DR EMBL; AJ549248; CAD70491.3; -; mRNA. DR EMBL; AJ549249; CAD70492.2; -; mRNA. DR EMBL; AJ549250; CAD70493.3; -; mRNA. DR EMBL; AJ555148; CAD87527.2; -; mRNA. DR EMBL; AJ555149; CAD87528.2; -; mRNA. DR EMBL; AM711892; CAM98555.1; -; mRNA. DR EMBL; AM711893; CAM98556.1; -; mRNA. DR EMBL; AM711894; CAM98557.1; -; mRNA. DR EMBL; AM711895; CAM98558.1; -; mRNA. DR CCDS; CCDS14412.2; -. [P21675-14] DR CCDS; CCDS35325.2; -. [P21675-13] DR PIR; A40262; A40262. DR RefSeq; NP_620278.2; NM_138923.4. [P21675-13] DR RefSeq; XP_047298351.1; XM_047442395.1. [P21675-14] DR RefSeq; XP_047298355.1; XM_047442399.1. [P21675-13] DR RefSeq; XP_054183607.1; XM_054327632.1. [P21675-14] DR RefSeq; XP_054183611.1; XM_054327636.1. [P21675-13] DR PDB; 1EQF; X-ray; 2.10 A; A=1380-1659. DR PDB; 3AAD; X-ray; 3.30 A; A=1363-1650. DR PDB; 3UV4; X-ray; 1.89 A; A/B=1522-1656. DR PDB; 3UV5; X-ray; 2.03 A; A=1394-1656. DR PDB; 4RGW; X-ray; 2.30 A; A=600-1236. DR PDB; 4YYM; X-ray; 1.50 A; A/B=1518-1659. DR PDB; 4YYN; X-ray; 1.85 A; A/B=1518-1659. DR PDB; 5FUR; EM; 8.50 A; G=1-1893. DR PDB; 5I1Q; X-ray; 1.50 A; A=1518-1659. DR PDB; 5I29; X-ray; 1.21 A; A=1518-1659. DR PDB; 5MG2; X-ray; 1.75 A; A=1522-1656. DR PDB; 6BQD; X-ray; 2.14 A; A/B=1522-1651. DR PDB; 6FIC; X-ray; 2.18 A; T=1380-1659. DR PDB; 6MZD; EM; 9.80 A; A=21-1893. DR PDB; 6MZL; EM; 23.00 A; A=1-1893. DR PDB; 6MZM; EM; 7.50 A; A=609-1104. DR PDB; 6P38; X-ray; 2.80 A; A=1522-1656. DR PDB; 6P39; X-ray; 2.94 A; A=1521-1656. DR PDB; 6P3A; X-ray; 2.99 A; A/B=1522-1656. DR PDB; 7EDX; EM; 4.50 A; A=1-1893. DR PDB; 7EG7; EM; 6.20 A; A=1-1893. DR PDB; 7EG8; EM; 7.40 A; A=1-1893. DR PDB; 7EG9; EM; 3.70 A; A=1-1893. DR PDB; 7EGA; EM; 4.10 A; A=1-1893. DR PDB; 7EGB; EM; 3.30 A; A=1-1893. DR PDB; 7EGC; EM; 3.90 A; A=1-1893. DR PDB; 7EGD; EM; 6.75 A; A=1-1893. DR PDB; 7EGE; EM; 9.00 A; A=1-1893. DR PDB; 7EGH; EM; 3.04 A; A=1-1893. DR PDB; 7EGI; EM; 9.82 A; A=1-1893. DR PDB; 7EGJ; EM; 8.64 A; A=1-1893. DR PDB; 7ENA; EM; 4.07 A; DA=1-1893. DR PDB; 7ENC; EM; 4.13 A; DA=1-1893. DR PDB; 7JJG; X-ray; 1.60 A; A=1522-1656. DR PDB; 7JJH; X-ray; 2.10 A; A=1394-1656. DR PDB; 7JSP; X-ray; 1.70 A; A=1522-1656. DR PDB; 7JTC; X-ray; 2.05 A; A=1522-1656. DR PDB; 7K03; X-ray; 1.60 A; A=1394-1656. DR PDB; 7K0D; X-ray; 2.20 A; A=1394-1656. DR PDB; 7K0U; X-ray; 2.52 A; A/B=1522-1656. DR PDB; 7K1P; X-ray; 2.45 A; A=1522-1656. DR PDB; 7K27; X-ray; 1.50 A; A=1394-1656. DR PDB; 7K3O; X-ray; 1.70 A; A/B=1522-1656. DR PDB; 7K42; X-ray; 1.70 A; A/B=1522-1656. DR PDB; 7K6F; X-ray; 1.86 A; A=1394-1656. DR PDB; 7L6X; X-ray; 2.75 A; A=1394-1656. DR PDB; 7LB0; X-ray; 2.33 A; A=1394-1656. DR PDB; 7LB1; X-ray; 1.35 A; A=1394-1656. DR PDB; 7LB2; X-ray; 1.70 A; A=1394-1656. DR PDB; 7LB3; X-ray; 1.90 A; A=1522-1656. DR PDB; 7N42; X-ray; 1.90 A; A=1394-1656. DR PDB; 7P4S; X-ray; 2.17 A; A=1522-1656. DR PDB; 7T2I; X-ray; 1.89 A; A=1394-1656. DR PDB; 7T36; X-ray; 1.65 A; A=1394-1656. DR PDB; 8GXQ; EM; 5.04 A; DA=1-1893. DR PDB; 8GXS; EM; 4.16 A; DA=1-1893. DR PDB; 8WAK; EM; 5.47 A; A=1-1872. DR PDB; 8WAL; EM; 8.52 A; A=1-1872. DR PDB; 8WAN; EM; 6.07 A; A=1-1872. DR PDB; 8WAO; EM; 6.40 A; A=1-1872. DR PDB; 8WAP; EM; 5.85 A; A=1-1872. DR PDB; 8WAQ; EM; 6.29 A; A=1-1872. DR PDB; 8WAR; EM; 7.20 A; A=1-1872. DR PDB; 8WAS; EM; 6.13 A; A=1-1872. DR PDBsum; 1EQF; -. DR PDBsum; 3AAD; -. DR PDBsum; 3UV4; -. DR PDBsum; 3UV5; -. DR PDBsum; 4RGW; -. DR PDBsum; 4YYM; -. DR PDBsum; 4YYN; -. DR PDBsum; 5FUR; -. DR PDBsum; 5I1Q; -. DR PDBsum; 5I29; -. DR PDBsum; 5MG2; -. DR PDBsum; 6BQD; -. DR PDBsum; 6FIC; -. DR PDBsum; 6MZD; -. DR PDBsum; 6MZL; -. DR PDBsum; 6MZM; -. DR PDBsum; 6P38; -. DR PDBsum; 6P39; -. DR PDBsum; 6P3A; -. DR PDBsum; 7EDX; -. DR PDBsum; 7EG7; -. DR PDBsum; 7EG8; -. DR PDBsum; 7EG9; -. DR PDBsum; 7EGA; -. DR PDBsum; 7EGB; -. DR PDBsum; 7EGC; -. DR PDBsum; 7EGD; -. DR PDBsum; 7EGE; -. DR PDBsum; 7EGH; -. DR PDBsum; 7EGI; -. DR PDBsum; 7EGJ; -. DR PDBsum; 7ENA; -. DR PDBsum; 7ENC; -. DR PDBsum; 7JJG; -. DR PDBsum; 7JJH; -. DR PDBsum; 7JSP; -. DR PDBsum; 7JTC; -. DR PDBsum; 7K03; -. DR PDBsum; 7K0D; -. DR PDBsum; 7K0U; -. DR PDBsum; 7K1P; -. DR PDBsum; 7K27; -. DR PDBsum; 7K3O; -. DR PDBsum; 7K42; -. DR PDBsum; 7K6F; -. DR PDBsum; 7L6X; -. DR PDBsum; 7LB0; -. DR PDBsum; 7LB1; -. DR PDBsum; 7LB2; -. DR PDBsum; 7LB3; -. DR PDBsum; 7N42; -. DR PDBsum; 7P4S; -. DR PDBsum; 7T2I; -. DR PDBsum; 7T36; -. DR PDBsum; 8GXQ; -. DR PDBsum; 8GXS; -. DR PDBsum; 8WAK; -. DR PDBsum; 8WAL; -. DR PDBsum; 8WAN; -. DR PDBsum; 8WAO; -. DR PDBsum; 8WAP; -. DR PDBsum; 8WAQ; -. DR PDBsum; 8WAR; -. DR PDBsum; 8WAS; -. DR AlphaFoldDB; P21675; -. DR EMDB; EMD-31075; -. DR EMDB; EMD-31107; -. DR EMDB; EMD-31108; -. DR EMDB; EMD-31109; -. DR EMDB; EMD-31110; -. DR EMDB; EMD-31111; -. DR EMDB; EMD-31112; -. DR EMDB; EMD-31113; -. DR EMDB; EMD-31114; -. DR EMDB; EMD-31117; -. DR EMDB; EMD-31118; -. DR EMDB; EMD-31119; -. DR EMDB; EMD-31204; -. DR EMDB; EMD-31207; -. DR EMDB; EMD-34359; -. DR EMDB; EMD-34360; -. DR EMDB; EMD-37395; -. DR EMDB; EMD-37396; -. DR EMDB; EMD-37398; -. DR EMDB; EMD-37399; -. DR EMDB; EMD-37400; -. DR EMDB; EMD-37401; -. DR EMDB; EMD-37402; -. DR EMDB; EMD-37403; -. DR EMDB; EMD-9302; -. DR EMDB; EMD-9305; -. DR EMDB; EMD-9306; -. DR SASBDB; P21675; -. DR SMR; P21675; -. DR BioGRID; 112735; 258. DR ComplexPortal; CPX-915; General transcription factor complex TFIID. DR ComplexPortal; CPX-930; General transcription factor complex TFIID, TAF4B variant. DR CORUM; P21675; -. DR DIP; DIP-147N; -. DR FunCoup; P21675; 3231. DR IntAct; P21675; 83. DR MINT; P21675; -. DR STRING; 9606.ENSP00000406549; -. DR BindingDB; P21675; -. DR ChEMBL; CHEMBL3217390; -. DR GuidetoPHARMACOLOGY; 2231; -. DR GlyCosmos; P21675; 1 site, 1 glycan. DR GlyGen; P21675; 1 site, 1 O-linked glycan (1 site). DR iPTMnet; P21675; -. DR PhosphoSitePlus; P21675; -. DR BioMuta; TAF1; -. DR DMDM; 115942; -. DR jPOST; P21675; -. DR MassIVE; P21675; -. DR PaxDb; 9606-ENSP00000406549; -. DR PeptideAtlas; P21675; -. DR ProteomicsDB; 3401; -. DR ProteomicsDB; 53886; -. [P21675-1] DR ProteomicsDB; 53887; -. [P21675-2] DR Pumba; P21675; -. DR ABCD; P21675; 1 sequenced antibody. DR Antibodypedia; 346; 301 antibodies from 39 providers. DR DNASU; 6872; -. DR Ensembl; ENST00000373790.9; ENSP00000362895.5; ENSG00000147133.19. [P21675-13] DR Ensembl; ENST00000423759.6; ENSP00000406549.2; ENSG00000147133.19. [P21675-14] DR Ensembl; ENST00000715246.1; ENSP00000520427.1; ENSG00000147133.19. [P21675-2] DR GeneID; 6872; -. DR KEGG; hsa:6872; -. DR MANE-Select; ENST00000423759.6; ENSP00000406549.2; NM_004606.5; NP_004597.3. [P21675-14] DR UCSC; uc004dzt.6; human. [P21675-2] DR AGR; HGNC:11535; -. DR ClinPGx; PA36310; -. DR CTD; 6872; -. DR DisGeNET; 6872; -. DR GeneCards; TAF1; -. DR GeneReviews; TAF1; -. DR HGNC; HGNC:11535; TAF1. DR HPA; ENSG00000147133; Low tissue specificity. DR MalaCards; TAF1; -. DR MIM; 300966; phenotype. DR MIM; 313650; gene. DR MIM; 314250; phenotype. DR OpenTargets; ENSG00000147133; -. DR Orphanet; 53351; X-linked dystonia-parkinsonism. DR Orphanet; 480907; X-linked intellectual disability-global development delay-facial dysmorphism-sacral caudal remnant syndrome. DR VEuPathDB; HostDB:ENSG00000147133; -. DR eggNOG; KOG0008; Eukaryota. DR GeneTree; ENSGT00940000155242; -. DR HOGENOM; CLU_000572_3_0_1; -. DR InParanoid; P21675; -. DR OMA; PARIWYD; -. DR OrthoDB; 5752at2759; -. DR PAN-GO; P21675; 4 GO annotations based on evolutionary models. DR PhylomeDB; P21675; -. DR BRENDA; 2.3.1.48; 2681. DR PathwayCommons; P21675; -. DR Reactome; R-HSA-167161; HIV Transcription Initiation. DR Reactome; R-HSA-167162; RNA Polymerase II HIV Promoter Escape. DR Reactome; R-HSA-167172; Transcription of the HIV genome. DR Reactome; R-HSA-674695; RNA Polymerase II Pre-transcription Events. DR Reactome; R-HSA-6804756; Regulation of TP53 Activity through Phosphorylation. DR Reactome; R-HSA-73776; RNA Polymerase II Promoter Escape. DR Reactome; R-HSA-73779; RNA Polymerase II Transcription Pre-Initiation And Promoter Opening. DR Reactome; R-HSA-75953; RNA Polymerase II Transcription Initiation. DR Reactome; R-HSA-76042; RNA Polymerase II Transcription Initiation And Promoter Clearance. DR SignaLink; P21675; -. DR SIGNOR; P21675; -. DR Agora; ENSG00000147133; -. DR BioGRID-ORCS; 6872; 343 hits in 821 CRISPR screens. DR ChiTaRS; TAF1; human. DR EvolutionaryTrace; P21675; -. DR GeneWiki; TAF1; -. DR GenomeRNAi; 6872; -. DR Pharos; P21675; Tchem. DR PRO; PR:P21675; -. DR Proteomes; UP000005640; Chromosome X. DR RNAct; P21675; protein. DR Bgee; ENSG00000147133; Expressed in sural nerve and 182 other cell types or tissues. DR ExpressionAtlas; P21675; baseline and differential. DR GO; GO:0000785; C:chromatin; IDA:ParkinsonsUK-UCL. DR GO; GO:0071339; C:MLL1 complex; IDA:UniProtKB. DR GO; GO:0005654; C:nucleoplasm; IDA:HPA. DR GO; GO:0005634; C:nucleus; IDA:UniProtKB. DR GO; GO:0005669; C:transcription factor TFIID complex; IDA:UniProtKB. DR GO; GO:0005667; C:transcription regulator complex; IPI:ParkinsonsUK-UCL. DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW. DR GO; GO:0004402; F:histone acetyltransferase activity; IDA:UniProtKB. DR GO; GO:0140046; F:histone H4K16ac reader activity; IDA:BHF-UCL. DR GO; GO:0016301; F:kinase activity; IDA:ParkinsonsUK-UCL. DR GO; GO:0016922; F:nuclear receptor binding; IPI:ParkinsonsUK-UCL. DR GO; GO:0002039; F:p53 binding; IPI:BHF-UCL. DR GO; GO:0046982; F:protein heterodimerization activity; IPI:ParkinsonsUK-UCL. DR GO; GO:0004672; F:protein kinase activity; IDA:ParkinsonsUK-UCL. DR GO; GO:0106310; F:protein serine kinase activity; IEA:RHEA. DR GO; GO:0004674; F:protein serine/threonine kinase activity; IDA:UniProtKB. DR GO; GO:0001181; F:RNA polymerase I general transcription initiation factor activity; IDA:ARUK-UCL. DR GO; GO:0000979; F:RNA polymerase II core promoter sequence-specific DNA binding; IMP:ParkinsonsUK-UCL. DR GO; GO:0016251; F:RNA polymerase II general transcription initiation factor activity; IDA:BHF-UCL. DR GO; GO:0001091; F:RNA polymerase II general transcription initiation factor binding; IPI:BHF-UCL. DR GO; GO:0061629; F:RNA polymerase II-specific DNA-binding transcription factor binding; IPI:ParkinsonsUK-UCL. DR GO; GO:0043565; F:sequence-specific DNA binding; ISS:BHF-UCL. DR GO; GO:0017025; F:TBP-class protein binding; IPI:BHF-UCL. DR GO; GO:0140416; F:transcription regulator inhibitor activity; IDA:ParkinsonsUK-UCL. DR GO; GO:0061631; F:ubiquitin conjugating enzyme activity; IDA:ParkinsonsUK-UCL. DR GO; GO:0071318; P:cellular response to ATP; IDA:ParkinsonsUK-UCL. DR GO; GO:0034644; P:cellular response to UV; IDA:ParkinsonsUK-UCL. DR GO; GO:0006974; P:DNA damage response; IDA:ParkinsonsUK-UCL. DR GO; GO:0030901; P:midbrain development; IGI:ParkinsonsUK-UCL. DR GO; GO:0042789; P:mRNA transcription by RNA polymerase II; IDA:ComplexPortal. DR GO; GO:0010629; P:negative regulation of gene expression; IMP:ParkinsonsUK-UCL. DR GO; GO:1905524; P:negative regulation of protein autoubiquitination; IDA:ParkinsonsUK-UCL. DR GO; GO:1901797; P:negative regulation of signal transduction by p53 class mediator; IDA:ParkinsonsUK-UCL. DR GO; GO:0000122; P:negative regulation of transcription by RNA polymerase II; IMP:ParkinsonsUK-UCL. DR GO; GO:2000059; P:negative regulation of ubiquitin-dependent protein catabolic process; IMP:ParkinsonsUK-UCL. DR GO; GO:0160207; P:positive regulation of androgen receptor signaling pathway; IDA:ParkinsonsUK-UCL. DR GO; GO:0032436; P:positive regulation of proteasomal ubiquitin-dependent protein catabolic process; IDA:BHF-UCL. DR GO; GO:0045944; P:positive regulation of transcription by RNA polymerase II; IDA:ParkinsonsUK-UCL. DR GO; GO:0060261; P:positive regulation of transcription initiation by RNA polymerase II; IDA:ComplexPortal. DR GO; GO:0046777; P:protein autophosphorylation; TAS:UniProtKB. DR GO; GO:0000209; P:protein polyubiquitination; IDA:ParkinsonsUK-UCL. DR GO; GO:0050821; P:protein stabilization; IDA:ParkinsonsUK-UCL. DR GO; GO:1902806; P:regulation of cell cycle G1/S phase transition; TAS:ParkinsonsUK-UCL. DR GO; GO:1901796; P:regulation of signal transduction by p53 class mediator; TAS:Reactome. DR GO; GO:0051123; P:RNA polymerase II preinitiation complex assembly; IPI:ComplexPortal. DR GO; GO:0006366; P:transcription by RNA polymerase II; IGI:BHF-UCL. DR GO; GO:0006361; P:transcription initiation at RNA polymerase I promoter; IGI:ParkinsonsUK-UCL. DR GO; GO:0006367; P:transcription initiation at RNA polymerase II promoter; IDA:BHF-UCL. DR GO; GO:0006511; P:ubiquitin-dependent protein catabolic process; IDA:ParkinsonsUK-UCL. DR CDD; cd05511; Bromo_TFIID; 2. DR DisProt; DP03451; -. [P21675-1] DR FunFam; 1.10.1100.10:FF:000001; Transcription initiation factor TFIID subunit; 1. DR FunFam; 1.20.920.10:FF:000019; Transcription initiation factor TFIID subunit; 1. DR FunFam; 1.20.920.10:FF:000020; Transcription initiation factor TFIID subunit; 1. DR Gene3D; 1.20.920.10; Bromodomain-like; 2. DR Gene3D; 1.10.1100.10; TAFII-230 TBP-binding domain; 1. DR IDEAL; IID00545; -. DR InterPro; IPR001487; Bromodomain. DR InterPro; IPR036427; Bromodomain-like_sf. DR InterPro; IPR018359; Bromodomain_CS. DR InterPro; IPR040240; TAF1. DR InterPro; IPR011177; TAF1_animal. DR InterPro; IPR022591; TAF1_HAT_dom. DR InterPro; IPR009067; TAF_II_230-bd. DR InterPro; IPR036741; TAFII-230_TBP-bd_sf. DR InterPro; IPR041670; Znf-CCHC_6. DR PANTHER; PTHR13900; TRANSCRIPTION INITIATION FACTOR TFIID; 1. DR PANTHER; PTHR13900:SF0; TRANSCRIPTION INITIATION FACTOR TFIID SUBUNIT 1; 1. DR Pfam; PF00439; Bromodomain; 2. DR Pfam; PF12157; DUF3591; 1. DR Pfam; PF09247; TBP-binding; 1. DR Pfam; PF15288; zf-CCHC_6; 1. DR PIRSF; PIRSF003047; TAF1_animal; 1. DR PRINTS; PR00503; BROMODOMAIN. DR SMART; SM00297; BROMO; 2. DR SUPFAM; SSF47370; Bromodomain; 2. DR SUPFAM; SSF47055; TAF(II)230 TBP-binding fragment; 1. DR PROSITE; PS00633; BROMODOMAIN_1; 2. DR PROSITE; PS50014; BROMODOMAIN_2; 2. PE 1: Evidence at protein level; KW 3D-structure; Acetylation; Acyltransferase; Alternative initiation; KW Alternative splicing; ATP-binding; Bromodomain; Cell cycle; KW Disease variant; DNA-binding; Dystonia; Host-virus interaction; KW Intellectual disability; Isopeptide bond; Kinase; Nucleotide-binding; KW Nucleus; Parkinsonism; Phosphoprotein; Proteomics identification; KW Reference proteome; Repeat; Serine/threonine-protein kinase; Transcription; KW Transcription regulation; Transferase; Ubl conjugation. FT CHAIN 1..1893 FT /note="Transcription initiation factor TFIID subunit 1" FT /id="PRO_0000211215" FT DOMAIN 1..435 FT /note="Protein kinase 1" FT DOMAIN 1397..1505 FT /note="Bromo 1" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00035" FT DOMAIN 1446..1893 FT /note="Protein kinase 2" FT DOMAIN 1519..1628 FT /note="Bromo 2" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00035" FT DNA_BIND 1216..1294 FT /note="HMG box; involved in promoter binding" FT /evidence="ECO:0007744|PDB:7EDX, ECO:0007744|PDB:7EG7, FT ECO:0007744|PDB:7EG8, ECO:0007744|PDB:7EG9, FT ECO:0007744|PDB:7EGA, ECO:0007744|PDB:7EGB, FT ECO:0007744|PDB:7EGC, ECO:0007744|PDB:7EGD, FT ECO:0007744|PDB:7EGE, ECO:0007744|PDB:7EGH, FT ECO:0007744|PDB:7EGI, ECO:0007744|PDB:7EGJ" FT REGION 155..184 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 197..224 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 534..557 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 538..997 FT /note="Histone acetyltransferase (HAT)" FT REGION 990..1009 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 1128..1148 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 1158..1177 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 1254..1278 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 1363..1650 FT /note="Interaction with ASF1A and ASF1B" FT /evidence="ECO:0000269|PubMed:12842904" FT REGION 1651..1676 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 1696..1893 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT MOTIF 1372..1379 FT /note="Nuclear localization signal" FT /evidence="ECO:0000255" FT COMPBIAS 156..165 FT /note="Pro residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 197..208 FT /note="Low complexity" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 995..1004 FT /note="Basic and acidic residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 1139..1148 FT /note="Basic and acidic residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 1254..1270 FT /note="Basic and acidic residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 1659..1668 FT /note="Pro residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 1709..1723 FT /note="Acidic residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 1741..1756 FT /note="Acidic residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 1830..1840 FT /note="Polar residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 1846..1857 FT /note="Acidic residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 1860..1869 FT /note="Polar residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT MOD_RES 137 FT /note="Phosphoserine; by autocatalysis" FT /evidence="ECO:0000269|PubMed:8625415" FT MOD_RES 328 FT /note="Phosphoserine; by autocatalysis" FT /evidence="ECO:0000269|PubMed:8625415, FT ECO:0007744|PubMed:24275569" FT MOD_RES 565 FT /note="N6-acetyllysine" FT /evidence="ECO:0000250|UniProtKB:Q80UV9" FT MOD_RES 1690 FT /note="Phosphoserine" FT /evidence="ECO:0000250|UniProtKB:Q80UV9" FT MOD_RES 1693 FT /note="Phosphoserine" FT /evidence="ECO:0000250|UniProtKB:Q80UV9" FT MOD_RES 1799 FT /note="Phosphoserine" FT /evidence="ECO:0000250|UniProtKB:Q80UV9" FT MOD_RES 1802 FT /note="Phosphoserine" FT /evidence="ECO:0000250|UniProtKB:Q80UV9" FT MOD_RES 1820 FT /note="Phosphoserine" FT /evidence="ECO:0000250|UniProtKB:Q80UV9" FT MOD_RES 1847 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:19690332" FT CROSSLNK 570 FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with FT G-Cter in SUMO2)" FT /evidence="ECO:0007744|PubMed:28112733" FT CROSSLNK 583 FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with FT G-Cter in SUMO2)" FT /evidence="ECO:0007744|PubMed:28112733" FT VAR_SEQ 1..20 FT /note="Missing (in isoform 13 and isoform 14)" FT /id="VSP_061987" FT VAR_SEQ 178..198 FT /note="Missing (in isoform 1 and isoform 13)" FT /id="VSP_061988" FT VAR_SEQ 1546..1561 FT /note="SWPFHHPVNKKFVPDY -> VSCLCAKYFLAISSPS (in isoform FT 2i)" FT /evidence="ECO:0000303|PubMed:17952504" FT /id="VSP_061989" FT VAR_SEQ 1546..1549 FT /note="SWPF -> IITK (in isoform 2h)" FT /evidence="ECO:0000303|PubMed:17952504" FT /id="VSP_061990" FT VAR_SEQ 1550..1893 FT /note="Missing (in isoform 2h)" FT /evidence="ECO:0000303|PubMed:17952504" FT /id="VSP_061991" FT VAR_SEQ 1562..1893 FT /note="Missing (in isoform 2i)" FT /evidence="ECO:0000303|PubMed:17952504" FT /id="VSP_061992" FT VAR_SEQ 1606..1613 FT /note="PESQYTKT -> YMCTTCRT (in isoform 2e)" FT /evidence="ECO:0000303|PubMed:12928496, FT ECO:0000303|PubMed:17952504" FT /id="VSP_061993" FT VAR_SEQ 1614..1893 FT /note="Missing (in isoform 2e)" FT /evidence="ECO:0000303|PubMed:12928496, FT ECO:0000303|PubMed:17952504" FT /id="VSP_061994" FT VAR_SEQ 1666 FT /note="Q -> QAK (in isoform N-TAF1, isoform 2d and isoform FT 2g)" FT /evidence="ECO:0000303|PubMed:12928496, FT ECO:0000303|PubMed:17273961, ECO:0000303|PubMed:17952504" FT /id="VSP_061995" FT VAR_SEQ 1706..1708 FT /note="VTQ -> MRQGRGRLGEEDSDVDIEGYDDEEEDGKPKTPAP (in FT isoform 16)" FT /evidence="ECO:0000303|PubMed:12928496" FT /id="VSP_061996" FT VAR_SEQ 1708 FT /note="Q -> QMRQGRGRLGEEDSDVDIEGYDDEEEDGKPKTPAP (in isoform FT 4, isoform 2a and isoform 2g)" FT /evidence="ECO:0000303|PubMed:12928496, FT ECO:0000303|PubMed:17952504, ECO:0000303|Ref.7" FT /id="VSP_061997" FT VAR_SEQ 1820..1893 FT /note="SYGSYEEPDPKSNTQDTSFSSIGGYEVSEEEEDEEEEEQRSGPSVLSQVHLS FT EDEEDSEDFHSIAGDSDLDSDE -> RYQ (in isoform 2a, isoform 16, FT isoform 2c, isoform 2d and isoform 2g)" FT /evidence="ECO:0000303|PubMed:12928496, FT ECO:0000303|PubMed:17952504" FT /id="VSP_061998" FT VAR_SEQ 1820 FT /note="S -> R (in isoform 15)" FT /id="VSP_061999" FT VAR_SEQ 1821..1893 FT /note="Missing (in isoform 15)" FT /id="VSP_062000" FT VARIANT 290 FT /note="L -> V (in dbSNP:rs28382158)" FT /evidence="ECO:0000269|PubMed:17344846, ECO:0000269|Ref.4" FT /id="VAR_020678" FT VARIANT 318 FT /note="A -> G (in dbSNP:rs35317750)" FT /evidence="ECO:0000269|PubMed:17344846" FT /id="VAR_041930" FT VARIANT 474 FT /note="G -> D (in a colorectal adenocarcinoma sample; FT somatic mutation)" FT /evidence="ECO:0000269|PubMed:17344846" FT /id="VAR_041931" FT VARIANT 493 FT /note="N -> D (found in a patient with X-linked FT intellectual disability; uncertain significance; FT dbSNP:rs200177996)" FT /evidence="ECO:0000269|PubMed:25644381" FT /id="VAR_077838" FT VARIANT 596 FT /note="P -> S (in MRXS33; dbSNP:rs864321630)" FT /evidence="ECO:0000269|PubMed:26637982" FT /id="VAR_076394" FT VARIANT 672 FT /note="E -> K (in a metastatic melanoma sample; somatic FT mutation)" FT /evidence="ECO:0000269|PubMed:17344846" FT /id="VAR_041932" FT VARIANT 712 FT /note="M -> I (in a lung bronchoalveolar carcinoma sample; FT somatic mutation; dbSNP:rs2148297629)" FT /evidence="ECO:0000269|PubMed:17344846" FT /id="VAR_041933" FT VARIANT 807 FT /note="C -> R (in MRXS33; dbSNP:rs864321628)" FT /evidence="ECO:0000269|PubMed:26637982" FT /id="VAR_076395" FT VARIANT 976 FT /note="D -> H (in MRXS33; dbSNP:rs864321631)" FT /evidence="ECO:0000269|PubMed:26637982" FT /id="VAR_076396" FT VARIANT 1190 FT /note="R -> C (found in a patient with X-linked FT intellectual disability; uncertain significance; FT dbSNP:rs1569301036)" FT /evidence="ECO:0000269|PubMed:25644381" FT /id="VAR_077839" FT VARIANT 1246 FT /note="R -> W (in MRXS33; dbSNP:rs864321629)" FT /evidence="ECO:0000269|PubMed:26637982" FT /id="VAR_076397" FT VARIANT 1337 FT /note="I -> T (in MRXS33; dbSNP:rs864321627)" FT /evidence="ECO:0000269|PubMed:26637982" FT /id="VAR_076398" FT VARIANT 1404 FT /note="V -> I (in dbSNP:rs7050748)" FT /id="VAR_048433" FT VARIANT 1452 FT /note="R -> H (in MRXS33; uncertain significance; FT dbSNP:rs2148488251)" FT /evidence="ECO:0000269|PubMed:26637982" FT /id="VAR_076399" FT VARIANT 1517 FT /note="N -> H (in MRXS33; uncertain significance; FT dbSNP:rs1602624914)" FT /evidence="ECO:0000269|PubMed:26637982" FT /id="VAR_076400" FT MUTAGEN 137 FT /note="S->A: No decrease in kinase activity." FT /evidence="ECO:0000269|PubMed:9660973" FT MUTAGEN 145 FT /note="D->A: Reduces kinase activity; when associated with FT A-147; A-149; A-150; A-152 and A-154." FT /evidence="ECO:0000269|PubMed:9660973" FT MUTAGEN 147 FT /note="D->A: Reduces kinase activity; when associated with FT A-145; A-149; A-150; A-152 and A-154." FT /evidence="ECO:0000269|PubMed:9660973" FT MUTAGEN 149 FT /note="E->A: Reduces kinase activity; when associated with FT A-145; A-147; A-150; A-152 and A-154." FT /evidence="ECO:0000269|PubMed:9660973" FT MUTAGEN 150 FT /note="D->A: Reduces kinase activity; when associated with FT A-145; A-147; A-149; A-152 and A-154." FT /evidence="ECO:0000269|PubMed:9660973" FT MUTAGEN 152 FT /note="D->A: Reduces kinase activity; when associated with FT A-145; A-147; A-149; A-150 and A-154." FT /evidence="ECO:0000269|PubMed:9660973" FT MUTAGEN 154 FT /note="K->A: Reduces kinase activity; when associated with FT A-145; A-147; A-149; A-150 and A-152." FT /evidence="ECO:0000269|PubMed:9660973" FT MUTAGEN 326 FT /note="C->A: Reduces kinase activity; when associated with FT A-328; A-329; A-330 and A-331." FT /evidence="ECO:0000269|PubMed:9660973" FT MUTAGEN 328 FT /note="S->A: Reduces kinase activity; when associated with FT A-326; A-329; A-330 and A-331." FT /evidence="ECO:0000269|PubMed:9660973" FT MUTAGEN 329 FT /note="D->A: Reduces kinase activity; when associated with FT A-326; A-328; A-330 and A-331." FT /evidence="ECO:0000269|PubMed:9660973" FT MUTAGEN 330 FT /note="D->A: Reduces kinase activity; when associated with FT A-326; A-328; A-329 and A-331." FT /evidence="ECO:0000269|PubMed:9660973" FT MUTAGEN 331 FT /note="E->A: Reduces kinase activity; when associated with FT A-326; A-328; A-329 and A-330." FT /evidence="ECO:0000269|PubMed:9660973" FT MUTAGEN 742 FT /note="E->Q: 25% decrease in histone acetylation." FT /evidence="ECO:0000269|PubMed:15870300" FT MUTAGEN 848..850 FT /note="Missing: Dramatic decrease in histone acetylation." FT /evidence="ECO:0000269|PubMed:15870300" FT STRAND 363..365 FT /evidence="ECO:0007829|PDB:7EGH" FT HELIX 368..374 FT /evidence="ECO:0007829|PDB:7EGH" FT HELIX 420..423 FT /evidence="ECO:0007829|PDB:7EGH" FT STRAND 427..429 FT /evidence="ECO:0007829|PDB:7EGH" FT HELIX 431..434 FT /evidence="ECO:0007829|PDB:7EGH" FT HELIX 494..498 FT /evidence="ECO:0007829|PDB:7EGH" FT HELIX 501..504 FT /evidence="ECO:0007829|PDB:7EGH" FT STRAND 509..511 FT /evidence="ECO:0007829|PDB:7EGH" FT STRAND 525..527 FT /evidence="ECO:0007829|PDB:7EGH" FT HELIX 591..594 FT /evidence="ECO:0007829|PDB:7EGH" FT HELIX 614..617 FT /evidence="ECO:0007829|PDB:4RGW" FT TURN 621..623 FT /evidence="ECO:0007829|PDB:4RGW" FT HELIX 630..634 FT /evidence="ECO:0007829|PDB:4RGW" FT TURN 635..637 FT /evidence="ECO:0007829|PDB:4RGW" FT STRAND 645..647 FT /evidence="ECO:0007829|PDB:4RGW" FT HELIX 648..650 FT /evidence="ECO:0007829|PDB:4RGW" FT STRAND 651..653 FT /evidence="ECO:0007829|PDB:4RGW" FT STRAND 655..659 FT /evidence="ECO:0007829|PDB:4RGW" FT HELIX 661..676 FT /evidence="ECO:0007829|PDB:4RGW" FT TURN 677..679 FT /evidence="ECO:0007829|PDB:4RGW" FT HELIX 689..692 FT /evidence="ECO:0007829|PDB:4RGW" FT STRAND 696..706 FT /evidence="ECO:0007829|PDB:4RGW" FT STRAND 718..725 FT /evidence="ECO:0007829|PDB:4RGW" FT STRAND 729..731 FT /evidence="ECO:0007829|PDB:4RGW" FT STRAND 739..745 FT /evidence="ECO:0007829|PDB:4RGW" FT STRAND 750..753 FT /evidence="ECO:0007829|PDB:4RGW" FT STRAND 760..777 FT /evidence="ECO:0007829|PDB:4RGW" FT STRAND 782..788 FT /evidence="ECO:0007829|PDB:4RGW" FT STRAND 791..795 FT /evidence="ECO:0007829|PDB:4RGW" FT STRAND 799..803 FT /evidence="ECO:0007829|PDB:4RGW" FT HELIX 818..838 FT /evidence="ECO:0007829|PDB:4RGW" FT STRAND 841..843 FT /evidence="ECO:0007829|PDB:4RGW" FT STRAND 845..847 FT /evidence="ECO:0007829|PDB:4RGW" FT HELIX 848..854 FT /evidence="ECO:0007829|PDB:4RGW" FT HELIX 860..868 FT /evidence="ECO:0007829|PDB:4RGW" FT STRAND 871..874 FT /evidence="ECO:0007829|PDB:4RGW" FT STRAND 877..879 FT /evidence="ECO:0007829|PDB:4RGW" FT STRAND 882..885 FT /evidence="ECO:0007829|PDB:4RGW" FT HELIX 894..900 FT /evidence="ECO:0007829|PDB:4RGW" FT HELIX 903..921 FT /evidence="ECO:0007829|PDB:4RGW" FT HELIX 926..928 FT /evidence="ECO:0007829|PDB:4RGW" FT HELIX 946..949 FT /evidence="ECO:0007829|PDB:4RGW" FT HELIX 952..963 FT /evidence="ECO:0007829|PDB:4RGW" FT STRAND 968..973 FT /evidence="ECO:0007829|PDB:4RGW" FT STRAND 979..983 FT /evidence="ECO:0007829|PDB:4RGW" FT STRAND 985..989 FT /evidence="ECO:0007829|PDB:4RGW" FT HELIX 1014..1018 FT /evidence="ECO:0007829|PDB:7EGH" FT HELIX 1020..1031 FT /evidence="ECO:0007829|PDB:7EGH" FT HELIX 1035..1039 FT /evidence="ECO:0007829|PDB:7EGH" FT HELIX 1043..1055 FT /evidence="ECO:0007829|PDB:7EGH" FT HELIX 1076..1099 FT /evidence="ECO:0007829|PDB:4RGW" FT STRAND 1186..1191 FT /evidence="ECO:0007829|PDB:7EGH" FT TURN 1195..1197 FT /evidence="ECO:0007829|PDB:7EGH" FT STRAND 1201..1206 FT /evidence="ECO:0007829|PDB:7EGH" FT HELIX 1209..1224 FT /evidence="ECO:0007829|PDB:7EGH" FT HELIX 1238..1262 FT /evidence="ECO:0007829|PDB:7EGH" FT HELIX 1402..1418 FT /evidence="ECO:0007829|PDB:7LB1" FT HELIX 1424..1426 FT /evidence="ECO:0007829|PDB:7LB1" FT STRAND 1427..1429 FT /evidence="ECO:0007829|PDB:3AAD" FT TURN 1432..1434 FT /evidence="ECO:0007829|PDB:7LB1" FT HELIX 1438..1441 FT /evidence="ECO:0007829|PDB:7LB1" FT HELIX 1448..1456 FT /evidence="ECO:0007829|PDB:7LB1" FT HELIX 1463..1480 FT /evidence="ECO:0007829|PDB:7LB1" FT STRAND 1483..1485 FT /evidence="ECO:0007829|PDB:3AAD" FT HELIX 1486..1504 FT /evidence="ECO:0007829|PDB:7LB1" FT HELIX 1506..1516 FT /evidence="ECO:0007829|PDB:7LB1" FT HELIX 1518..1521 FT /evidence="ECO:0007829|PDB:7LB1" FT HELIX 1523..1538 FT /evidence="ECO:0007829|PDB:5I29" FT TURN 1539..1542 FT /evidence="ECO:0007829|PDB:5I29" FT HELIX 1547..1549 FT /evidence="ECO:0007829|PDB:5I29" FT TURN 1555..1557 FT /evidence="ECO:0007829|PDB:5I29" FT STRAND 1558..1560 FT /evidence="ECO:0007829|PDB:6P3A" FT HELIX 1561..1564 FT /evidence="ECO:0007829|PDB:5I29" FT STRAND 1565..1567 FT /evidence="ECO:0007829|PDB:6P3A" FT HELIX 1571..1579 FT /evidence="ECO:0007829|PDB:5I29" FT HELIX 1586..1604 FT /evidence="ECO:0007829|PDB:5I29" FT STRAND 1606..1608 FT /evidence="ECO:0007829|PDB:7K6F" FT HELIX 1609..1627 FT /evidence="ECO:0007829|PDB:5I29" FT HELIX 1629..1655 FT /evidence="ECO:0007829|PDB:5I29" FT MOD_RES P21675-16:1718 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:20068231" FT MOD_RES P21675-18:1721 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:20068231" FT MOD_RES P21675-22:1723 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:20068231" FT MOD_RES P21675-25:1721 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:20068231" SQ SEQUENCE 1893 AA; 214714 MW; AE148C222B418BB4 CRC64; MGPGCDLLLR TAATITAAAI MSDTDSDEDS AGGGPFSLAG FLFGNINGAG QLEGESVLDD ECKKHLAGLG ALGLGSLITE LTANEELTGT DGALVNDEGW VRSTEDAVDY SDINEVAEDE SRRYQQTMGS LQPLCHSDYD EDDYDADCED IDCKLMPPPP PPPGPMKKDK DQDSITGVSE NGEGIILPSI IAPSSLASEK VDFSSSSDSE SEMGPQEATQ AESEDGKLTL PLAGIMQHDA TKLLPSVTEL FPEFRPGKVL RFLRLFGPGK NVPSVWRSAR RKRKKKHREL IQEEQIQEVE CSVESEVSQK SLWNYDYAPP PPPEQCLSDD EITMMAPVES KFSQSTGDID KVTDTKPRVA EWRYGPARLW YDMLGVPEDG SGFDYGFKLR KTEHEPVIKS RMIEEFRKLE ENNGTDLLAD ENFLMVTQLH WEDDIIWDGE DVKHKGTKPQ RASLAGWLPS SMTRNAMAYN VQQGFAATLD DDKPWYSIFP IDNEDLVYGR WEDNIIWDAQ AMPRLLEPPV LTLDPNDENL ILEIPDEKEE ATSNSPSKES KKESSLKKSR ILLGKTGVIK EEPQQNMSQP EVKDPWNLSN DEYYYPKQQG LRGTFGGNII QHSIPAVELR QPFFPTHMGP IKLRQFHRPP LKKYSFGALS QPGPHSVQPL LKHIKKKAKM REQERQASGG GEMFFMRTPQ DLTGKDGDLI LAEYSEENGP LMMQVGMATK IKNYYKRKPG KDPGAPDCKY GETVYCHTSP FLGSLHPGQL LQAFENNLFR APIYLHKMPE TDFLIIRTRQ GYYIRELVDI FVVGQQCPLF EVPGPNSKRA NTHIRDFLQV FIYRLFWKSK DRPRRIRMED IKKAFPSHSE SSIRKRLKLC ADFKRTGMDS NWWVLKSDFR LPTEEEIRAM VSPEQCCAYY SMIAAEQRLK DAGYGEKSFF APEEENEEDF QMKIDDEVRT APWNTTRAFI AAMKGKCLLE VTGVADPTGC GEGFSYVKIP NKPTQQKDDK EPQPVKKTVT GTDADLRRLS LKNAKQLLRK FGVPEEEIKK LSRWEVIDVV RTMSTEQARS GEGPMSKFAR GSRFSVAEHQ ERYKEECQRI FDLQNKVLSS TEVLSTDTDS SSAEDSDFEE MGKNIENMLQ NKKTSSQLSR EREEQERKEL QRMLLAAGSA ASGNNHRDDD TASVTSLNSS ATGRCLKIYR TFRDEEGKEY VRCETVRKPA VIDAYVRIRT TKDEEFIRKF ALFDEQHREE MRKERRRIQE QLRRLKRNQE KEKLKGPPEK KPKKMKERPD LKLKCGACGA IGHMRTNKFC PLYYQTNAPP SNPVAMTEEQ EEELEKTVIH NDNEELIKVE GTKIVLGKQL IESADEVRRK SLVLKFPKQQ LPPKKKRRVG TTVHCDYLNR PHKSIHRRRT DPMVTLSSIL ESIINDMRDL PNTYPFHTPV NAKVVKDYYK IITRPMDLQT LRENVRKRLY PSREEFREHL ELIVKNSATY NGPKHSLTQI SQSMLDLCDE KLKEKEDKLA RLEKAINPLL DDDDQVAFSF ILDNIVTQKM MAVPDSWPFH HPVNKKFVPD YYKVIVNPMD LETIRKNISK HKYQSRESFL DDVNLILANS VKYNGPESQY TKTAQEIVNV CYQTLTEYDE HLTQLEKDIC TAKEAALEEA ELESLDPMTP GPYTPQPPDL YDTNTSLSMS RDASVFQDES NMSVLDIPSA TPEKQVTQEG EDGDGDLADE EEGTVQQPQA SVLYEDLLMS EGEDDEEDAG SDEEGDNPFS AIQLSESGSD SDVGSGGIRP KQPRMLQENT RMDMENEESM MSYEGDGGEA SHGLEDSNIS YGSYEEPDPK SNTQDTSFSS IGGYEVSEEE EDEEEEEQRS GPSVLSQVHL SEDEEDSEDF HSIAGDSDLD SDE //