ID RCAS1_HUMAN Reviewed; 213 AA. AC O00559; A8K3N6; Q5Y8C7; Q6IB20; Q9BS76; DT 01-DEC-2000, integrated into UniProtKB/Swiss-Prot. DT 01-JUL-1997, sequence version 1. DT 28-JAN-2026, entry version 188. DE RecName: Full=Receptor-binding cancer antigen expressed on SiSo cells; DE AltName: Full=Cancer-associated surface antigen RCAS1; DE AltName: Full=Estrogen receptor-binding fragment-associated gene 9 protein; GN Name=EBAG9; Synonyms=RCAS1; 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=Uterine adenocarcinoma; RX PubMed=10426319; DOI=10.1038/11383; RA Nakashima M., Sonoda K., Watanabe T.; RT "Inhibition of cell growth and induction of apoptotic cell death by the RT human tumor-associated antigen RCAS1."; RL Nat. Med. 5:938-942(1999). RN [2] RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1). RC TISSUE=Mammary cancer; RX PubMed=9418891; DOI=10.1128/mcb.18.1.442; RA Watanabe T., Inoue S., Hiroi H., Orimo A., Kawashima H., Muramatsu M.; RT "Isolation of estrogen-responsive genes with a CpG island library."; RL Mol. Cell. Biol. 18:442-449(1998). RN [3] RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2). RA Lo W.Y., Hsieh S.L.; RL Submitted (JUN-2004) to the EMBL/GenBank/DDBJ databases. RN [4] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1). RC TISSUE=Embryo; 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 [5] 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 [6] 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 [7] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1). RC TISSUE=Brain, Lung, and Placenta; 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 [8] RP ROLE IN CANCER. RX PubMed=12054692; DOI=10.1016/s0006-291x(02)00401-1; RA Rousseau J., Tetu B., Caron D., Malenfant P., Cattaruzzi P., Audette M., RA Doillon C., Tremblay J.P., Guerette B.; RT "RCAS1 is associated with ductal breast cancer progression."; RL Biochem. Biophys. Res. Commun. 293:1544-1549(2002). RN [9] RP ROLE IN CANCER. RX PubMed=12138241; DOI=10.1159/000065065; RA Oizumi S., Yamazaki K., Nakashima M., Watanabe T., Hommura F., Ogura S., RA Nishimura M., Dosaka-Akita H.; RT "RCAS1 expression: a potential prognostic marker for adenocarcinomas of the RT lung."; RL Oncology 62:333-339(2002). RN [10] RP FUNCTION, AND SUBCELLULAR LOCATION. RX PubMed=12672804; DOI=10.1074/jbc.m301361200; RA Engelsberg A., Hermosilla R., Karsten U., Schuelein R., Doerken B., RA Rehm A.; RT "The Golgi protein RCAS1 controls cell surface expression of tumor- RT associated O-linked glycan antigens."; RL J. Biol. Chem. 278:22998-23007(2003). RN [11] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-36 AND THR-41, AND RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Leukemic T-cell; RX PubMed=15144186; DOI=10.1021/ac035352d; RA Brill L.M., Salomon A.R., Ficarro S.B., Mukherji M., Stettler-Gill M., RA Peters E.C.; RT "Robust phosphoproteomic profiling of tyrosine phosphorylation sites from RT human T cells using immobilized metal affinity chromatography and tandem RT mass spectrometry."; RL Anal. Chem. 76:2763-2772(2004). RN [12] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-94, AND IDENTIFICATION BY RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RX PubMed=15592455; DOI=10.1038/nbt1046; RA Rush J., Moritz A., Lee K.A., Guo A., Goss V.L., Spek E.J., Zhang H., RA Zha X.-M., Polakiewicz R.D., Comb M.J.; RT "Immunoaffinity profiling of tyrosine phosphorylation in cancer cells."; RL Nat. Biotechnol. 23:94-101(2005). RN [13] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-36, 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 [14] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-36, AND IDENTIFICATION BY RP 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 [15] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-36, AND IDENTIFICATION BY RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Cervix carcinoma; RX PubMed=18691976; DOI=10.1016/j.molcel.2008.07.007; RA Daub H., Olsen J.V., Bairlein M., Gnad F., Oppermann F.S., Korner R., RA Greff Z., Keri G., Stemmann O., Mann M.; RT "Kinase-selective enrichment enables quantitative phosphoproteomics of the RT kinome across the cell cycle."; RL Mol. Cell 31:438-448(2008). RN [16] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-36, AND IDENTIFICATION BY RP 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 [17] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-36, AND IDENTIFICATION BY RP 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 [18] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-36, 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 [19] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-36, 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 [20] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-36, AND IDENTIFICATION BY RP 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 [21] RP IDENTIFICATION 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 [22] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-36, AND IDENTIFICATION BY RP MASS SPECTROMETRY [LARGE SCALE 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 [23] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-36, 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). CC -!- FUNCTION: May participate in suppression of cell proliferation and CC induces apoptotic cell death through activation of interleukin-1-beta CC converting enzyme (ICE)-like proteases. {ECO:0000269|PubMed:12054692, CC ECO:0000269|PubMed:12138241, ECO:0000269|PubMed:12672804}. CC -!- SUBUNIT: Homodimer. CC -!- INTERACTION: CC O00559; Q9ULC5: ACSL5; NbExp=3; IntAct=EBI-8787095, EBI-2876927; CC O00559; Q9BQE5: APOL2; NbExp=3; IntAct=EBI-8787095, EBI-4290634; CC O00559; Q12983: BNIP3; NbExp=3; IntAct=EBI-8787095, EBI-749464; CC O00559; Q9BXR6: CFHR5; NbExp=3; IntAct=EBI-8787095, EBI-11579371; CC O00559; Q9H5X1: CIAO2A; NbExp=3; IntAct=EBI-8787095, EBI-752069; CC O00559; Q6UXB4: CLEC4G; NbExp=3; IntAct=EBI-8787095, EBI-2114729; CC O00559; Q9NWW5: CLN6; NbExp=3; IntAct=EBI-8787095, EBI-6165897; CC O00559; A0A0C4DFN3: MGLL; NbExp=3; IntAct=EBI-8787095, EBI-12866138; CC O00559; Q8N912: NRAC; NbExp=3; IntAct=EBI-8787095, EBI-12051377; CC O00559; Q8NH19: OR10AG1; NbExp=3; IntAct=EBI-8787095, EBI-13339917; CC O00559; Q9P0S3: ORMDL1; NbExp=3; IntAct=EBI-8787095, EBI-1054848; CC O00559; Q9Y5Y5: PEX16; NbExp=3; IntAct=EBI-8787095, EBI-981985; CC O00559; O60831: PRAF2; NbExp=3; IntAct=EBI-8787095, EBI-2506064; CC O00559; Q96HR9-2: REEP6; NbExp=3; IntAct=EBI-8787095, EBI-14065960; CC O00559; Q9BRI3: SLC30A2; NbExp=3; IntAct=EBI-8787095, EBI-8644112; CC O00559; P78382: SLC35A1; NbExp=3; IntAct=EBI-8787095, EBI-12870360; CC O00559; Q96G79: SLC35A4; NbExp=3; IntAct=EBI-8787095, EBI-12363689; CC O00559; Q969S0: SLC35B4; NbExp=3; IntAct=EBI-8787095, EBI-10281213; CC O00559; Q16623: STX1A; NbExp=3; IntAct=EBI-8787095, EBI-712466; CC O00559; P32856-2: STX2; NbExp=3; IntAct=EBI-8787095, EBI-11956649; CC O00559; Q13277: STX3; NbExp=3; IntAct=EBI-8787095, EBI-1394295; CC O00559; Q6UX40: TMEM107; NbExp=3; IntAct=EBI-8787095, EBI-12845616; CC O00559; Q6ZUI0: TPRG1; NbExp=3; IntAct=EBI-8787095, EBI-17249488; CC O00559; Q9Y228: TRAF3IP3; NbExp=3; IntAct=EBI-8787095, EBI-765817; CC O00559; Q9P0L0: VAPA; NbExp=3; IntAct=EBI-8787095, EBI-1059156; CC O00559; O95292: VAPB; NbExp=3; IntAct=EBI-8787095, EBI-1188298; CC -!- SUBCELLULAR LOCATION: Golgi apparatus membrane CC {ECO:0000269|PubMed:12672804}; Single-pass type III membrane protein CC {ECO:0000269|PubMed:12672804}. Note=According to PubMed:10426319, it CC also exists as a soluble form which has the same biological activities. CC The existence of such soluble form is however uncertain. CC -!- ALTERNATIVE PRODUCTS: CC Event=Alternative splicing; Named isoforms=2; CC Name=1; CC IsoId=O00559-1; Sequence=Displayed; CC Name=2; CC IsoId=O00559-2; Sequence=VSP_055503; CC -!- TISSUE SPECIFICITY: Widely expressed. Expressed in ovary, testis, CC prostate, thymus, muscle and heart, but not in small intestine, colon, CC lymph nodes, or peripherical blood lymphocytes. The protein is not CC detected in any of the above organs. CC -!- INDUCTION: By estrogen. CC -!- DOMAIN: The coiled coil domain is necessary for the homodimerization. CC -!- MISCELLANEOUS: May serve as a prognostic marker for cancers such as CC adenocarcinomas of the lung and breast cancers. It is present and CC overexpressed in many patients suffering from breast carcinomas, its CC level of expression correlates with tumor grade, suggesting that it may CC be involved in cancer immune escape. According to PubMed:12672804, it CC is however not directly a tumor-associated antigen, but it rather CC modulates surface expression of tumor-associated O-linked glycan Tn CC when it is overexpressed, suggesting that it contributes indirectly to CC the antigenicity of tumor cells. CC -!- CAUTION: It was initially reported to be a ligand for some putative CC receptor present on T-, B-, natural killer (NK) cells and various human CC cell lines. However, PubMed:12672804 showed that it does not bind any CC receptor. {ECO:0000305}. CC -!- WEB RESOURCE: Name=Atlas of Genetics and Cytogenetics in Oncology and CC Haematology; CC URL="https://atlasgeneticsoncology.org/gene/40393/EBAG9"; 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; AF006265; AAB61617.1; -; mRNA. DR EMBL; AB007619; BAA22572.1; -; mRNA. DR EMBL; AY653072; AAU85838.1; -; mRNA. DR EMBL; AK290651; BAF83340.1; -; mRNA. DR EMBL; CR456984; CAG33265.1; -; mRNA. DR EMBL; AC079061; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; AP000427; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; BC005249; AAH05249.1; -; mRNA. DR EMBL; BC017729; AAH17729.1; -; mRNA. DR EMBL; BC022506; AAH22506.1; -; mRNA. DR CCDS; CCDS6313.1; -. [O00559-1] DR RefSeq; NP_001265867.1; NM_001278938.2. [O00559-1] DR RefSeq; NP_004206.1; NM_004215.5. [O00559-1] DR RefSeq; NP_936056.1; NM_198120.3. [O00559-1] DR RefSeq; XP_016869449.1; XM_017013960.2. [O00559-1] DR RefSeq; XP_047278368.1; XM_047422412.1. [O00559-1] DR RefSeq; XP_047278369.1; XM_047422413.1. [O00559-1] DR RefSeq; XP_054217468.1; XM_054361493.1. [O00559-1] DR RefSeq; XP_054217469.1; XM_054361494.1. [O00559-1] DR AlphaFoldDB; O00559; -. DR SMR; O00559; -. DR BioGRID; 114607; 313. DR FunCoup; O00559; 1234. DR IntAct; O00559; 33. DR STRING; 9606.ENSP00000337675; -. DR iPTMnet; O00559; -. DR PhosphoSitePlus; O00559; -. DR SwissPalm; O00559; -. DR BioMuta; EBAG9; -. DR jPOST; O00559; -. DR MassIVE; O00559; -. DR PaxDb; 9606-ENSP00000337675; -. DR PeptideAtlas; O00559; -. DR ProteomicsDB; 47973; -. [O00559-1] DR ProteomicsDB; 65861; -. DR Pumba; O00559; -. DR Antibodypedia; 13458; 429 antibodies from 38 providers. DR CPTC; O00559; 3 antibodies. DR DNASU; 9166; -. DR Ensembl; ENST00000337573.10; ENSP00000337675.5; ENSG00000147654.17. [O00559-1] DR Ensembl; ENST00000395785.7; ENSP00000379131.2; ENSG00000147654.17. [O00559-1] DR Ensembl; ENST00000531677.5; ENSP00000432082.1; ENSG00000147654.17. [O00559-2] DR Ensembl; ENST00000614147.1; ENSP00000477734.1; ENSG00000147654.17. [O00559-2] DR Ensembl; ENST00000620557.4; ENSP00000477645.1; ENSG00000147654.17. [O00559-1] DR Ensembl; ENST00000699338.1; ENSP00000514313.1; ENSG00000147654.17. [O00559-1] DR GeneID; 9166; -. DR KEGG; hsa:9166; -. DR MANE-Select; ENST00000337573.10; ENSP00000337675.5; NM_004215.5; NP_004206.1. DR UCSC; uc003ynf.5; human. [O00559-1] DR AGR; HGNC:3123; -. DR ClinPGx; PA27581; -. DR CTD; 9166; -. DR DisGeNET; 9166; -. DR GeneCards; EBAG9; -. DR HGNC; HGNC:3123; EBAG9. DR HPA; ENSG00000147654; Low tissue specificity. DR MIM; 605772; gene. DR OpenTargets; ENSG00000147654; -. DR VEuPathDB; HostDB:ENSG00000147654; -. DR eggNOG; ENOG502QSN4; Eukaryota. DR GeneTree; ENSGT00390000004040; -. DR HOGENOM; CLU_094995_0_0_1; -. DR InParanoid; O00559; -. DR OMA; LGEMENW; -. DR OrthoDB; 10017216at2759; -. DR PAN-GO; O00559; 1 GO annotation based on evolutionary models. DR PhylomeDB; O00559; -. DR PathwayCommons; O00559; -. DR Reactome; R-HSA-9018519; Estrogen-dependent gene expression. DR SignaLink; O00559; -. DR Agora; ENSG00000147654; -. DR BioGRID-ORCS; 9166; 19 hits in 1151 CRISPR screens. DR ChiTaRS; EBAG9; human. DR GeneWiki; EBAG9; -. DR GenomeRNAi; 9166; -. DR Pharos; O00559; Tbio. DR PRO; PR:O00559; -. DR Proteomes; UP000005640; Chromosome 8. DR RNAct; O00559; protein. DR Bgee; ENSG00000147654; Expressed in parotid gland and 212 other cell types or tissues. DR ExpressionAtlas; O00559; baseline and differential. DR GO; GO:0000139; C:Golgi membrane; TAS:Reactome. DR GO; GO:0030141; C:secretory granule; IBA:GO_Central. DR GO; GO:0016505; F:peptidase activator activity involved in apoptotic process; NAS:UniProtKB. DR GO; GO:0090717; P:adaptive immune memory response involving T cells and B cells; IEA:Ensembl. DR GO; GO:0001558; P:regulation of cell growth; NAS:UniProtKB. DR GO; GO:0001913; P:T cell mediated cytotoxicity; IEA:Ensembl. DR InterPro; IPR017025; Cancer-assoc_antigen_RCAS1. DR PANTHER; PTHR15208:SF2; RECEPTOR-BINDING CANCER ANTIGEN EXPRESSED ON SISO CELLS; 1. DR PANTHER; PTHR15208; RECEPTOR-BINDING CANCER ANTIGEN EXPRESSED ON SISO CELLS CANCER ASSOCIATED SURFACE ANTIGEN RCAS1 ESTROGEN RECEPTOR-BINDING FRAGMENT- ASSOCIATED GENE 9 PROTEIN; 1. DR PIRSF; PIRSF034247; RCAS1; 1. PE 1: Evidence at protein level; KW Alternative splicing; Apoptosis; Coiled coil; Golgi apparatus; Membrane; KW Phosphoprotein; Proteomics identification; Reference proteome; KW Signal-anchor; Transmembrane; Transmembrane helix. FT CHAIN 1..213 FT /note="Receptor-binding cancer antigen expressed on SiSo FT cells" FT /id="PRO_0000097195" FT TOPO_DOM 1..6 FT /note="Extracellular" FT /evidence="ECO:0000255" FT TRANSMEM 7..27 FT /note="Helical; Signal-anchor for type III membrane FT protein" FT /evidence="ECO:0000255" FT TOPO_DOM 28..213 FT /note="Cytoplasmic" FT /evidence="ECO:0000255" FT REGION 178..213 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COILED 163..211 FT /evidence="ECO:0000255" FT COMPBIAS 178..206 FT /note="Basic and acidic residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT MOD_RES 36 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:15144186, FT ECO:0007744|PubMed:17081983, ECO:0007744|PubMed:18088087, FT ECO:0007744|PubMed:18669648, ECO:0007744|PubMed:18691976, FT ECO:0007744|PubMed:19369195, ECO:0007744|PubMed:19690332, FT ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:21406692, FT ECO:0007744|PubMed:23186163, ECO:0007744|PubMed:24275569" FT MOD_RES 41 FT /note="Phosphothreonine" FT /evidence="ECO:0007744|PubMed:15144186" FT MOD_RES 94 FT /note="Phosphotyrosine" FT /evidence="ECO:0007744|PubMed:15592455" FT VAR_SEQ 174 FT /note="R -> RSRTNVCLLCSLLFHHPTPTSTPYINQSVKIERVSLGQWSYGKSKE FT (in isoform 2)" FT /evidence="ECO:0000303|Ref.3" FT /id="VSP_055503" FT CONFLICT 183 FT /note="K -> E (in Ref. 7; AAH05249)" FT /evidence="ECO:0000305" FT CONFLICT 199 FT /note="R -> Q (in Ref. 4; BAF83340)" FT /evidence="ECO:0000305" SQ SEQUENCE 213 AA; 24377 MW; B115E741E23891C5 CRC64; MAITQFRLFK FCTCLATVFS FLKRLICRSG RGRKLSGDQI TLPTTVDYSS VPKQTDVEEW TSWDEDAPTS VKIEGGNGNV ATQQNSLEQL EPDYFKDMTP TIRKTQKIVI KKREPLNFGI PDGSTGFSSR LAATQDLPFI HQSSELGDLD TWQENTNAWE EEEDAAWQAE EVLRQQKLAD REKRAAEQQR KKMEKEAQRL MKKEQNKIGV KLS //