RCAS1_HUMAN
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 03-AUG-2022, entry version 171.
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="http://atlasgeneticsoncology.org/Genes/EBAG9ID40393ch8q23.html";
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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_001278938.1. [O00559-1]
DR RefSeq; NP_004206.1; NM_004215.4. [O00559-1]
DR RefSeq; NP_936056.1; NM_198120.2. [O00559-1]
DR RefSeq; XP_016869449.1; XM_017013960.1. [O00559-1]
DR AlphaFoldDB; O00559; -.
DR SMR; O00559; -.
DR BioGRID; 114607; 304.
DR IntAct; O00559; 30.
DR STRING; 9606.ENSP00000337675; -.
DR iPTMnet; O00559; -.
DR PhosphoSitePlus; O00559; -.
DR SwissPalm; O00559; -.
DR BioMuta; EBAG9; -.
DR EPD; O00559; -.
DR jPOST; O00559; -.
DR MassIVE; O00559; -.
DR MaxQB; O00559; -.
DR PaxDb; O00559; -.
DR PeptideAtlas; O00559; -.
DR PRIDE; O00559; -.
DR ProteomicsDB; 47973; -. [O00559-1]
DR ProteomicsDB; 65861; -.
DR Antibodypedia; 13458; 424 antibodies from 39 providers.
DR CPTC; O00559; 3 antibodies.
DR DNASU; 9166; -.
DR Ensembl; ENST00000337573.10; ENSP00000337675.5; ENSG00000147654.15. [O00559-1]
DR Ensembl; ENST00000395785.6; ENSP00000379131.2; ENSG00000147654.15. [O00559-1]
DR Ensembl; ENST00000531677.5; ENSP00000432082.1; ENSG00000147654.15. [O00559-2]
DR Ensembl; ENST00000614147.1; ENSP00000477734.1; ENSG00000147654.15. [O00559-2]
DR Ensembl; ENST00000620557.4; ENSP00000477645.1; ENSG00000147654.15. [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 CTD; 9166; -.
DR DisGeNET; 9166; -.
DR GeneCards; EBAG9; -.
DR HGNC; HGNC:3123; EBAG9.
DR HPA; ENSG00000147654; Low tissue specificity.
DR MIM; 605772; gene.
DR neXtProt; NX_O00559; -.
DR OpenTargets; ENSG00000147654; -.
DR PharmGKB; PA27581; -.
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 PhylomeDB; O00559; -.
DR TreeFam; TF326584; -.
DR PathwayCommons; O00559; -.
DR Reactome; R-HSA-9018519; Estrogen-dependent gene expression.
DR SignaLink; O00559; -.
DR BioGRID-ORCS; 9166; 19 hits in 1075 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 210 other tissues.
DR ExpressionAtlas; O00559; baseline and differential.
DR Genevisible; O00559; HS.
DR GO; GO:0000139; C:Golgi membrane; TAS:Reactome.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
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:0001558; P:regulation of cell growth; NAS:UniProtKB.
DR InterPro; IPR017025; Cancer-assoc_antigen_RCAS1.
DR PANTHER; PTHR15208; PTHR15208; 1.
DR PIRSF; PIRSF034247; RCAS1; 1.
PE 1: Evidence at protein level;
KW Alternative splicing; Apoptosis; Coiled coil; Golgi apparatus; Membrane;
KW Phosphoprotein; Reference proteome; Signal-anchor; Transmembrane;
KW 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 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
