ID RB39B_HUMAN Reviewed; 213 AA. AC Q96DA2; Q5JT79; Q8NEX3; DT 10-JAN-2003, integrated into UniProtKB/Swiss-Prot. DT 01-DEC-2001, sequence version 1. DT 07-APR-2021, entry version 167. DE RecName: Full=Ras-related protein Rab-39B; GN Name=RAB39B; 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]. RC TISSUE=Fetal brain; RX PubMed=12438742; DOI=10.1159/000064047; RA Cheng H., Ma Y., Ni X., Jiang M., Guo L., Ying K., Xie Y., Mao Y.; RT "Isolation and characterization of a human novel RAB (RAB39B) gene."; RL Cytogenet. Genome Res. 97:72-75(2002). RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. RC TISSUE=Brain; 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 [3] 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 [4] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. RC TISSUE=Pancreas; 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 SUBCELLULAR LOCATION, TISSUE SPECIFICITY, AND INVOLVEMENT IN MRX72. RX PubMed=20159109; DOI=10.1016/j.ajhg.2010.01.011; RA Giannandrea M., Bianchi V., Mignogna M.L., Sirri A., Carrabino S., RA D'Elia E., Vecellio M., Russo S., Cogliati F., Larizza L., Ropers H.H., RA Tzschach A., Kalscheuer V., Oehl-Jaschkowitz B., Skinner C., Schwartz C.E., RA Gecz J., Van Esch H., Raynaud M., Chelly J., de Brouwer A.P., Toniolo D., RA D'Adamo P.; RT "Mutations in the small GTPase gene RAB39B are responsible for X-linked RT mental retardation associated with autism, epilepsy, and macrocephaly."; RL Am. J. Hum. Genet. 86:185-195(2010). RN [6] RP SUBCELLULAR LOCATION. RX PubMed=24349490; DOI=10.1371/journal.pone.0083324; RA Seto S., Sugaya K., Tsujimura K., Nagata T., Horii T., Koide Y.; RT "Rab39a interacts with phosphatidylinositol 3-kinase and negatively RT regulates autophagy induced by lipopolysaccharide stimulation in RT macrophages."; RL PLoS ONE 8:E83324-E83324(2013). RN [7] RP INTERACTION WITH PICK1. RX PubMed=25784538; DOI=10.1038/ncomms7504; RA Mignogna M.L., Giannandrea M., Gurgone A., Fanelli F., Raimondi F., RA Mapelli L., Bassani S., Fang H., Van Anken E., Alessio M., Passafaro M., RA Gatti S., Esteban J.A., Huganir R., D'Adamo P.; RT "The intellectual disability protein RAB39B selectively regulates GluA2 RT trafficking to determine synaptic AMPAR composition."; RL Nat. Commun. 6:6504-6504(2015). RN [8] RP INVOLVEMENT IN WSMN, VARIANT WSMN LYS-168, AND CHARACTERIZATION OF VARIANT RP WSMN LYS-168. RX PubMed=25434005; DOI=10.1016/j.ajhg.2014.10.015; RA Wilson G.R., Sim J.C., McLean C., Giannandrea M., Galea C.A., Riseley J.R., RA Stephenson S.E., Fitzpatrick E., Haas S.A., Pope K., Hogan K.J., RA Gregg R.G., Bromhead C.J., Wargowski D.S., Lawrence C.H., James P.A., RA Churchyard A., Gao Y., Phelan D.G., Gillies G., Salce N., Stanford L., RA Marsh A.P., Mignogna M.L., Hayflick S.J., Leventer R.J., Delatycki M.B., RA Mellick G.D., Kalscheuer V.M., D'Adamo P., Bahlo M., Amor D.J., RA Lockhart P.J.; RT "Mutations in RAB39B cause X-linked intellectual disability and early-onset RT Parkinson disease with alpha-synuclein pathology."; RL Am. J. Hum. Genet. 95:729-735(2014). RN [9] RP FUNCTION, AND MUTAGENESIS OF SER-22 AND GLN-68. RX PubMed=27103069; DOI=10.15252/embj.201593350; RA Sellier C., Campanari M.L., Julie Corbier C., Gaucherot A., RA Kolb-Cheynel I., Oulad-Abdelghani M., Ruffenach F., Page A., Ciura S., RA Kabashi E., Charlet-Berguerand N.; RT "Loss of C9ORF72 impairs autophagy and synergizes with polyQ Ataxin-2 to RT induce motor neuron dysfunction and cell death."; RL EMBO J. 35:1276-1297(2016). RN [10] RP DISCUSSION ON INVOLVEMENT IN WSMN. RX PubMed=27459931; DOI=10.1016/j.neurobiolaging.2016.03.021; RA Hodges K., Brewer S.S., Labbe C., Soto-Ortolaza A.I., Walton R.L., RA Strongosky A.J., Uitti R.J., van Gerpen J.A., Ertekin-Taner N., RA Kantarci K., Lowe V.J., Parisi J.E., Savica R., Graff-Radford J., RA Jones D.T., Knopman D.S., Petersen R.C., Murray M.E., Graff-Radford N.R., RA Ferman T.J., Dickson D.W., Wszolek Z.K., Boeve B.F., Ross O.A., RA Lorenzo-Betancor O.; RT "RAB39B gene mutations are not a common cause of Parkinson's disease or RT dementia with Lewy bodies."; RL Neurobiol. Aging 45:107-108(2016). RN [11] RP DISCUSSION ON INVOLVEMENT IN WSMN. RX PubMed=26739247; DOI=10.1016/j.parkreldis.2015.12.014; RA Loechte T., Brueggemann N., Vollstedt E.J., Krause P., Domingo A., RA Rosales R., Lee L.V., Hopfner F., Westenberger A., Kuehn A., Klein C., RA Lohmann K.; RT "RAB39B mutations are a rare finding in Parkinson disease patients."; RL Parkinsonism Relat. Disord. 23:116-117(2016). RN [12] RP VARIANT WSMN ARG-192, AND SUBCELLULAR LOCATION. RX PubMed=26399558; DOI=10.1186/s13024-015-0045-4; RA Mata I.F., Jang Y., Kim C.H., Hanna D.S., Dorschner M.O., Samii A., RA Agarwal P., Roberts J.W., Klepitskaya O., Shprecher D.R., Chung K.A., RA Factor S.A., Espay A.J., Revilla F.J., Higgins D.S., Litvan I., RA Leverenz J.B., Yearout D., Inca-Martinez M., Martinez E., Thompson T.R., RA Cholerton B.A., Hu S.C., Edwards K.L., Kim K.S., Zabetian C.P.; RT "The RAB39B p.G192R mutation causes X-linked dominant Parkinson's RT disease."; RL Mol. Neurodegener. 10:50-50(2015). RN [13] RP VARIANT WSMN 186-TRP--CYS-213 DEL. RX PubMed=27066548; DOI=10.1212/nxg.0000000000000009; RG French Parkinson's Disease Genetics Study Group (PDG) and the International Parkinson's Disease Genomics Consortium (IPDGC); RA Lesage S., Bras J., Cormier-Dequaire F., Condroyer C., Nicolas A., RA Darwent L., Guerreiro R., Majounie E., Federoff M., Heutink P., Wood N.W., RA Gasser T., Hardy J., Tison F., Singleton A., Brice A.; RT "Loss-of-function mutations in RAB39B are associated with typical early- RT onset Parkinson disease."; RL Neurol. Genet. 1:E9-E9(2015). CC -!- FUNCTION: Small GTPases Rab involved in autophagy (PubMed:27103069). CC The small GTPases Rab are key regulators of intracellular membrane CC trafficking, from the formation of transport vesicles to their fusion CC with membranes. Rabs cycle between an inactive GDP-bound form and an CC active GTP-bound form that is able to recruit to membranes different CC sets of downstream effectors directly responsible for vesicle CC formation, movement, tethering and fusion (PubMed:27103069). May CC regulate the homeostasis of SNCA/alpha-synuclein. Together with PICK1 CC proposed to ensure selectively GRIA2 exit from the endoplasmic CC reticulum to the Golgi and to regulate AMPAR compostion at the post- CC synapses and thus synaptic transmission (By similarity). CC {ECO:0000250|UniProtKB:Q8BHC1, ECO:0000269|PubMed:27103069}. CC -!- SUBUNIT: Interacts (in GTP-bound form) with PICK1 (via PDZ domain); a CC PICK1 homodimer may allow simultaneous association of RAB39B and GRIA2 CC to PICK1 which is involved in GRIA2 trafficking. CC {ECO:0000269|PubMed:25784538}. CC -!- INTERACTION: CC Q96DA2; Q08379: GOLGA2; NbExp=4; IntAct=EBI-9089467, EBI-618309; CC Q96DA2; Q96T51: RUFY1; NbExp=4; IntAct=EBI-9089467, EBI-3941207; CC Q96DA2; O14972: VPS26C; NbExp=3; IntAct=EBI-9089467, EBI-7207091; CC Q96DA2; Q8IUH5: ZDHHC17; NbExp=3; IntAct=EBI-9089467, EBI-524753; CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000305}; Lipid-anchor CC {ECO:0000305}; Cytoplasmic side {ECO:0000305}. Cytoplasmic vesicle CC membrane {ECO:0000269|PubMed:26399558}; Lipid-anchor {ECO:0000305}; CC Cytoplasmic side {ECO:0000305}. Golgi apparatus CC {ECO:0000269|PubMed:20159109, ECO:0000269|PubMed:24349490}. CC Note=Partial colocalization with markers that cycle from the cell CC surface to the trans-Golgi network. {ECO:0000250|UniProtKB:Q8BHC1}. CC -!- TISSUE SPECIFICITY: Highly expressed in the brain. CC {ECO:0000269|PubMed:20159109}. CC -!- DISEASE: Mental retardation, X-linked 72 (MRX72) [MIM:300271]: A CC disorder characterized by significantly below average general CC intellectual functioning associated with impairments in adaptive CC behavior and manifested during the developmental period. Intellectual CC deficiency is the only primary symptom of non-syndromic X-linked mental CC retardation, while syndromic mental retardation presents with CC associated physical, neurological and/or psychiatric manifestations. CC MRX72 patients can manifest autism spectrum disorder, seizures and CC macrocephaly as additional features. {ECO:0000269|PubMed:20159109}. CC Note=The disease is caused by variants affecting the gene represented CC in this entry. CC -!- DISEASE: Waisman syndrome (WSMN) [MIM:311510]: A neurologic disorder CC characterized by delayed psychomotor development, intellectual CC disability, and early-onset Parkinson disease. CC {ECO:0000269|PubMed:25434005, ECO:0000269|PubMed:26399558, CC ECO:0000269|PubMed:27066548}. Note=The disease is caused by variants CC affecting the gene represented in this entry. Its association with CC Parkinson disease is however unclear (PubMed:26739247, CC PubMed:27459931). According to a number of studies, variations CC affecting this gene are not a frequent cause of Parkinson disease, CC suggesting that RAB39B does not play a major role in Parkinson disease CC etiology (PubMed:26739247, PubMed:27459931). CC {ECO:0000269|PubMed:26739247, ECO:0000269|PubMed:27459931}. CC -!- SIMILARITY: Belongs to the small GTPase superfamily. Rab 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; AY052478; AAL12244.1; -; mRNA. DR EMBL; AL834460; CAD39120.1; -; mRNA. DR EMBL; AL356738; CAI41468.1; -; Genomic_DNA. DR EMBL; BC009714; AAH09714.1; -; mRNA. DR CCDS; CCDS14766.1; -. DR RefSeq; NP_741995.1; NM_171998.3. DR PDB; 6S5F; X-ray; 1.70 A; A=1-207. DR PDBsum; 6S5F; -. DR SMR; Q96DA2; -. DR BioGRID; 125507; 33. DR IntAct; Q96DA2; 22. DR STRING; 9606.ENSP00000358466; -. DR iPTMnet; Q96DA2; -. DR PhosphoSitePlus; Q96DA2; -. DR BioMuta; RAB39B; -. DR DMDM; 27734447; -. DR EPD; Q96DA2; -. DR jPOST; Q96DA2; -. DR MassIVE; Q96DA2; -. DR MaxQB; Q96DA2; -. DR PaxDb; Q96DA2; -. DR PeptideAtlas; Q96DA2; -. DR PRIDE; Q96DA2; -. DR ProteomicsDB; 76264; -. DR Antibodypedia; 350; 183 antibodies. DR DNASU; 116442; -. DR Ensembl; ENST00000369454; ENSP00000358466; ENSG00000155961. DR GeneID; 116442; -. DR KEGG; hsa:116442; -. DR UCSC; uc004fne.5; human. DR CTD; 116442; -. DR DisGeNET; 116442; -. DR GeneCards; RAB39B; -. DR GeneReviews; RAB39B; -. DR HGNC; HGNC:16499; RAB39B. DR HPA; ENSG00000155961; Tissue enhanced (brain). DR MalaCards; RAB39B; -. DR MIM; 300271; phenotype. DR MIM; 300774; gene. DR MIM; 311510; phenotype. DR neXtProt; NX_Q96DA2; -. DR OpenTargets; ENSG00000155961; -. DR Orphanet; 2379; Early-onset parkinsonism-intellectual disability syndrome. DR Orphanet; 106; NON RARE IN EUROPE: Autism. DR Orphanet; 777; X-linked non-syndromic intellectual disability. DR PharmGKB; PA34131; -. DR VEuPathDB; HostDB:ENSG00000155961.4; -. DR eggNOG; KOG0091; Eukaryota. DR GeneTree; ENSGT00940000158132; -. DR HOGENOM; CLU_041217_23_1_1; -. DR InParanoid; Q96DA2; -. DR OMA; XSITRAY; -. DR OrthoDB; 172471at2759; -. DR PhylomeDB; Q96DA2; -. DR TreeFam; TF300032; -. DR PathwayCommons; Q96DA2; -. DR Reactome; R-HSA-8873719; RAB geranylgeranylation. DR Reactome; R-HSA-8876198; RAB GEFs exchange GTP for GDP on RABs. DR BioGRID-ORCS; 116442; 4 hits in 611 CRISPR screens. DR GeneWiki; RAB39B; -. DR GenomeRNAi; 116442; -. DR Pharos; Q96DA2; Tbio. DR PRO; PR:Q96DA2; -. DR Proteomes; UP000005640; Chromosome X. DR RNAct; Q96DA2; protein. DR Bgee; ENSG00000155961; Expressed in endothelial cell and 142 other tissues. DR Genevisible; Q96DA2; HS. DR GO; GO:0030659; C:cytoplasmic vesicle membrane; IEA:UniProtKB-SubCell. DR GO; GO:0005794; C:Golgi apparatus; IDA:UniProtKB. DR GO; GO:0000139; C:Golgi membrane; IBA:GO_Central. DR GO; GO:0043005; C:neuron projection; IDA:UniProtKB. DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell. DR GO; GO:0031982; C:vesicle; IDA:UniProtKB. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-KW. DR GO; GO:0003924; F:GTPase activity; IEA:InterPro. DR GO; GO:0031489; F:myosin V binding; IPI:UniProtKB. DR GO; GO:0006914; P:autophagy; IEA:UniProtKB-KW. DR GO; GO:0015031; P:protein transport; IEA:UniProtKB-KW. DR GO; GO:0032482; P:Rab protein signal transduction; IEA:InterPro. DR GO; GO:0010506; P:regulation of autophagy; IMP:UniProtKB. DR GO; GO:0050808; P:synapse organization; ISS:UniProtKB. DR GO; GO:0016192; P:vesicle-mediated transport; ISS:UniProtKB. DR CDD; cd04111; Rab39; 1. DR InterPro; IPR027417; P-loop_NTPase. DR InterPro; IPR041818; Rab39. DR InterPro; IPR005225; Small_GTP-bd_dom. DR InterPro; IPR001806; Small_GTPase. DR Pfam; PF00071; Ras; 1. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR00231; small_GTP; 1. DR PROSITE; PS51419; RAB; 1. PE 1: Evidence at protein level; KW 3D-structure; Autism spectrum disorder; Autophagy; Cell membrane; KW Cytoplasmic vesicle; Disease variant; Golgi apparatus; GTP-binding; KW Lipoprotein; Membrane; Mental retardation; Methylation; Nucleotide-binding; KW Parkinson disease; Phosphoprotein; Prenylation; Protein transport; KW Reference proteome; Transport. FT CHAIN 1..213 FT /note="Ras-related protein Rab-39B" FT /id="PRO_0000121255" FT NP_BIND 15..22 FT /note="GTP" FT /evidence="ECO:0000250" FT NP_BIND 64..68 FT /note="GTP" FT /evidence="ECO:0000250" FT NP_BIND 123..126 FT /note="GTP" FT /evidence="ECO:0000250" FT MOTIF 37..45 FT /note="Effector region" FT /evidence="ECO:0000250" FT MOD_RES 201 FT /note="Phosphoserine" FT /evidence="ECO:0000250|UniProtKB:Q8BHC1" FT MOD_RES 213 FT /note="Cysteine methyl ester" FT /evidence="ECO:0000250" FT LIPID 211 FT /note="S-geranylgeranyl cysteine" FT /evidence="ECO:0000250" FT LIPID 213 FT /note="S-geranylgeranyl cysteine" FT /evidence="ECO:0000250" FT VARIANT 168 FT /note="T -> K (in WSMN; loss of function mutation; FT expression of the mutation in neuroblastoma cells results FT in low levels of the mutant protein; dbSNP:rs587777874)" FT /evidence="ECO:0000269|PubMed:25434005" FT /id="VAR_073264" FT VARIANT 186..213 FT /note="Missing (in WSMN)" FT /evidence="ECO:0000269|PubMed:27066548" FT /id="VAR_078514" FT VARIANT 192 FT /note="G -> R (in WSMN; impaired localization to FT cytoplasmic vesicles; dbSNP:rs864309527)" FT /evidence="ECO:0000269|PubMed:26399558" FT /id="VAR_078515" FT MUTAGEN 22 FT /note="S->N: Dominant negative mutant." FT /evidence="ECO:0000269|PubMed:27103069" FT MUTAGEN 68 FT /note="Q->L: Constitutively active mutant locked in the FT active GTP-bound form." FT /evidence="ECO:0000269|PubMed:27103069" FT CONFLICT 57 FT /note="R -> T (in Ref. 1; AAL12244)" FT /evidence="ECO:0000305" FT STRAND 6..14 FT /evidence="ECO:0007744|PDB:6S5F" FT HELIX 21..30 FT /evidence="ECO:0007744|PDB:6S5F" FT STRAND 42..53 FT /evidence="ECO:0007744|PDB:6S5F" FT STRAND 56..65 FT /evidence="ECO:0007744|PDB:6S5F" FT HELIX 69..71 FT /evidence="ECO:0007744|PDB:6S5F" FT HELIX 72..76 FT /evidence="ECO:0007744|PDB:6S5F" FT STRAND 83..90 FT /evidence="ECO:0007744|PDB:6S5F" FT HELIX 94..98 FT /evidence="ECO:0007744|PDB:6S5F" FT HELIX 100..107 FT /evidence="ECO:0007744|PDB:6S5F" FT STRAND 112..114 FT /evidence="ECO:0007744|PDB:6S5F" FT STRAND 117..123 FT /evidence="ECO:0007744|PDB:6S5F" FT HELIX 128..130 FT /evidence="ECO:0007744|PDB:6S5F" FT HELIX 135..144 FT /evidence="ECO:0007744|PDB:6S5F" FT STRAND 149..153 FT /evidence="ECO:0007744|PDB:6S5F" FT TURN 154..157 FT /evidence="ECO:0007744|PDB:6S5F" FT HELIX 160..176 FT /evidence="ECO:0007744|PDB:6S5F" FT STRAND 188..191 FT /evidence="ECO:0007744|PDB:6S5F" SQ SEQUENCE 213 AA; 24622 MW; 2B2C5B35C61FA88E CRC64; MEAIWLYQFR LIVIGDSTVG KSCLIRRFTE GRFAQVSDPT VGVDFFSRLV EIEPGKRIKL QIWDTAGQER FRSITRAYYR NSVGGLLLFD ITNRRSFQNV HEWLEETKVH VQPYQIVFVL VGHKCDLDTQ RQVTRHEAEK LAAAYGMKYI ETSARDAINV EKAFTDLTRD IYELVKRGEI TIQEGWEGVK SGFVPNVVHS SEEVVKSERR CLC //