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UniProtKB/Swiss-Prot entry O00559


[Entry info] [Name and origin] [References] [Comments] [Cross-references] [Keywords] [Features] [Sequence] [Tools]

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Entry information
Entry name RCAS1_HUMAN
Primary accession number O00559
Secondary accession numbers Q6IB20 Q9BS76
Integrated into Swiss-Prot on December 1, 2000
Sequence was last modified on July 1, 1997 (Sequence version 1)
Annotations were last modified on    June 16, 2009 (Entry version 80)
Name and origin of the protein
Protein name Receptor-binding cancer antigen expressed on SiSo cells
Synonyms Cancer-associated surface antigen RCAS1
Estrogen receptor-binding fragment-associated gene 9 protein
Gene name
Name: EBAG9
Synonyms: RCAS1
From
Homo sapiens (Human) [TaxID: 9606] 
Taxonomy Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae; Homo.
Protein existence 1: Evidence at protein level;
References
[1]
NUCLEOTIDE SEQUENCE [MRNA].
TISSUE=Uterine adenocarcinoma;
DOI=10.1038/11383; PubMed=10426319 [NCBI, ExPASy, EBI, Israel, Japan]
Nakashima M., Sonoda K., Watanabe T.;
"Inhibition of cell growth and induction of apoptotic cell death by the human tumor-associated antigen RCAS1.";
Nat. Med. 5:938-942(1999).
[2]
NUCLEOTIDE SEQUENCE [MRNA].
TISSUE=Mammary cancer;
PubMed=9418891 [NCBI, ExPASy, EBI, Israel, Japan]
Watanabe T., Inoue S., Hiroi H., Orimo A., Kawashima H., Muramatsu M.;
"Isolation of estrogen-responsive genes with a CpG island library.";
Mol. Cell. Biol. 18:442-449(1998).
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Ebert L., Schick M., Neubert P., Schatten R., Henze S., Korn B.;
"Cloning of human full open reading frames in Gateway(TM) system entry vector (pDONR201).";
Submitted (JUN-2004) to the EMBL/GenBank/DDBJ databases.
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
TISSUE=Brain, Lung, and Placenta;
DOI=10.1101/gr.2596504; PubMed=15489334 [NCBI, ExPASy, EBI, Israel, Japan]
The MGC Project Team;
"The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC).";
Genome Res. 14:2121-2127(2004).
[5]
DISEASE.
DOI=10.1016/S0006-291X(02)00401-1; PubMed=12054692 [NCBI, ExPASy, EBI, Israel, Japan]
Rousseau J., Tetu B., Caron D., Malenfant P., Cattaruzzi P., Audette M., Doillon C., Tremblay J.P., Guerette B.;
"RCAS1 is associated with ductal breast cancer progression.";
Biochem. Biophys. Res. Commun. 293:1544-1549(2002).
[6]
DISEASE.
DOI=10.1159/000065065; PubMed=12138241 [NCBI, ExPASy, EBI, Israel, Japan]
Oizumi S., Yamazaki K., Nakashima M., Watanabe T., Hommura F., Ogura S., Nishimura M., Dosaka-Akita H.;
"RCAS1 expression: a potential prognostic marker for adenocarcinomas of the lung.";
Oncology 62:333-339(2002).
[7]
FUNCTION, AND SUBCELLULAR LOCATION.
DOI=10.1074/jbc.M301361200; PubMed=12672804 [NCBI, ExPASy, EBI, Israel, Japan]
Engelsberg A., Hermosilla R., Karsten U., Schuelein R., Doerken B., Rehm A.;
"The Golgi protein RCAS1 controls cell surface expression of tumor-associated O-linked glycan antigens.";
J. Biol. Chem. 278:22998-23007(2003).
[8]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-36; THR-41 AND TYR-48, AND MASS SPECTROMETRY.
TISSUE=T-cell;
DOI=10.1021/ac035352d; PubMed=15144186 [NCBI, ExPASy, EBI, Israel, Japan]
Brill L.M., Salomon A.R., Ficarro S.B., Mukherji M., Stettler-Gill M., Peters E.C.;
"Robust phosphoproteomic profiling of tyrosine phosphorylation sites from human T cells using immobilized metal affinity chromatography and tandem mass spectrometry.";
Anal. Chem. 76:2763-2772(2004).
[9]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-94, AND MASS SPECTROMETRY.
DOI=10.1038/nbt1046; PubMed=15592455 [NCBI, ExPASy, EBI, Israel, Japan]
Rush J., Moritz A., Lee K.A., Guo A., Goss V.L., Spek E.J., Zhang H., Zha X.-M., Polakiewicz R.D., Comb M.J.;
"Immunoaffinity profiling of tyrosine phosphorylation in cancer cells.";
Nat. Biotechnol. 23:94-101(2005).
[10]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-36, AND MASS SPECTROMETRY.
TISSUE=Epithelium;
DOI=10.1016/j.cell.2006.09.026; PubMed=17081983 [NCBI, ExPASy, EBI, Israel, Japan]
Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P., Mann M.;
"Global, in vivo, and site-specific phosphorylation dynamics in signaling networks.";
Cell 127:635-648(2006).
[11]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-36, AND MASS SPECTROMETRY.
DOI=10.1002/elps.200600782; PubMed=17487921 [NCBI, ExPASy, EBI, Israel, Japan]
Giorgianni F., Zhao Y., Desiderio D.M., Beranova-Giorgianni S.;
"Toward a global characterization of the phosphoproteome in prostate cancer cells: identification of phosphoproteins in the LNCaP cell line.";
Electrophoresis 28:2027-2034(2007).
[12]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-36, AND MASS SPECTROMETRY.
DOI=10.2116/analsci.24.161; PubMed=18187866 [NCBI, ExPASy, EBI, Israel, Japan]
Imami K., Sugiyama N., Kyono Y., Tomita M., Ishihama Y.;
"Automated phosphoproteome analysis for cultured cancer cells by two-dimensional nanoLC-MS using a calcined titania/C18 biphasic column.";
Anal. Sci. 24:161-166(2008).
[13]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-36, AND MASS SPECTROMETRY.
TISSUE=Platelet;
DOI=10.1021/pr0704130; PubMed=18088087 [NCBI, ExPASy, EBI, Israel, Japan]
Zahedi R.P., Lewandrowski U., Wiesner J., Wortelkamp S., Moebius J., Schuetz C., Walter U., Gambaryan S., Sickmann A.;
"Phosphoproteome of resting human platelets.";
J. Proteome Res. 7:526-534(2008).
[14]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-36, AND MASS SPECTROMETRY.
DOI=10.1016/j.molcel.2008.07.007; PubMed=18691976 [NCBI, ExPASy, EBI, Israel, Japan]
Daub H., Olsen J.V., Bairlein M., Gnad F., Oppermann F.S., Korner R., Greff Z., Keri G., Stemmann O., Mann M.;
"Kinase-selective enrichment enables quantitative phosphoproteomics of the kinome across the cell cycle.";
Mol. Cell 31:438-448(2008).
[15]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-36, AND MASS SPECTROMETRY.
DOI=10.1073/pnas.0805139105; PubMed=18669648 [NCBI, ExPASy, EBI, Israel, Japan]
Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E., Elledge S.J., Gygi S.P.;
"A quantitative atlas of mitotic phosphorylation.";
Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008).
Comments
  • FUNCTION: May participate in suppression of cell proliferation and induces apoptotic cell death through activation of interleukin-1-beta converting enzyme (ICE)-like proteases.
  • SUBUNIT: Homodimer.
  • SUBCELLULAR LOCATION: Golgi apparatus membrane; Single-pass type III membrane protein. Note=According to PubMed:10426319, it also exists as a soluble form which has the same biological activities. The existence of such soluble form is however uncertain.
  • TISSUE SPECIFICITY: Widely expressed. Expressed in ovary, testis, prostate, thymus, muscle and heart, but not in small intestine, colon, lymph nodes, or peripherical blood lymphocytes. The protein is not detected in any of the above organs.
  • INDUCTION: By estrogen.
  • DOMAIN: The coiled coil domain is necessary for the homodimerization.
  • DISEASE: Defects in EBAG9 may be a cause of breast cancers and adenocarcinomas of the lung. It is present and overexpressed in many patients suffering from breast carcinomas, its level of expression correlates with tumor grade, suggesting that it may be involved in cancer immune escape. According to PubMed:12672804, it is however not directly a tumor-associated antigen, but it rather modulates surface expression of tumor-associated O-linked glycan Tn when it is overexpressed, suggesting that it contributes indirectly to the antigenicity of tumor cells.
  • MISCELLANEOUS: May serve as a prognostic marker for cancers such as adenocarcinomas of the lung and breast cancers.
  • CAUTION: It was initially reported to be a ligand for some putative receptor present on T-, B-, natural killer (NK) cells and various human cell lines. However, PubMed:12672804 showed that it does not bind any receptor.
  • WEB RESOURCE: Name=Atlas of Genetics and Cytogenetics in Oncology and Haematology; URL="http://atlasgeneticsoncology.org/Genes/EBAG9ID40393ch8q23.html";.
Copyright
Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms. Distributed under the Creative Commons Attribution-NoDerivs License.
Cross-references
Sequence databases
EMBL
AF006265; AAB61617.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AB007619; BAA22572.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
CR456984; CAG33265.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
BC005249; AAH05249.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
BC017729; AAH17729.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
BC022506; AAH22506.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
IPI IPI00299076; -.
RefSeq NP_004206.1; -.
NP_936056.1; -.
UniGene Hs.409368
3D structure databases
ModBase O00559.
PTM databases
PhosphoSite O00559; -.
Organism-specific databases
GeneCards GC08P110621; -.
H-InvDB HIX0007729; -.
HGNC HGNC:3123; EBAG9.
GenAtlas EBAG9.
MIM 605772; gene. [NCBI / EBI]
PharmGKB PA27581; -.
Gene expression databases
ArrayExpress O00559; -.
Bgee O00559; -.
CleanEx HS_EBAG9; -.
GermOnline ENSG00000147654; Homo sapiens.
Ontologies
GO
GO:0000139; Cellular component: Golgi membrane (inferred from electronic annotation from UniProtKB-SubCell).
GO:0016021; Cellular component: integral to membrane (non-traceable author statement from UniProtKB).
GO:0005625; Cellular component: soluble fraction (non-traceable author statement from UniProtKB).
GO:0016505; Molecular function: apoptotic protease activator activity (non-traceable author statement from UniProtKB).
GO:0006915; Biological process: apoptosis (inferred from electronic annotation from UniProtKB-KW).
GO:0001558; Biological process: regulation of cell growth (non-traceable author statement from UniProtKB).
QuickGo view.
Family and domain databases
InterPro IPR017025; Cancer-assoc_antigen_RCAS1.
Graphical view of domain structure.
PIRSF PIRSF034247; RCAS1; 1.
Proteomic databases
PRIDE O00559; -.
Genome annotation databases
Ensembl ENSG00000147654; Homo sapiens. [Contig view]
GeneID 9166; -.
KEGG hsa:9166; -.
Phylogenomic databases
HOVERGEN O00559; -.
Other
NextBio 34373; -.
SOURCE EBAG9; Homo sapiens.
ProtoNet O00559.
UniRef View cluster of proteins with at least 50% / 90% / 100% identity.
Keywords
Apoptosis; Coiled coil; Golgi apparatus; Membrane; Phosphoprotein; Signal-anchor; Transmembrane.
Features
SEVIEWER logo Feature table viewer FT aligner logo Feature aligner
KeyFrom   To Length Description FTId
CHAIN   1   213  213     Receptor-binding cancer antigen expressed on SiSo cells. PRO_0000097195
TOPO_DOM   1     6  6     Extracellular (Potential). 
TRANSMEM   7    27  21     Signal-anchor for type III membrane protein (Potential). 
TOPO_DOM   28   213  186     Cytoplasmic (Potential). 
COILED   163   211  49     Potential. 
COMPBIAS   160   163  4     Poly-Glu. 
MOD_RES   36    36        Phosphoserine. 
MOD_RES   41    41        Phosphothreonine. 
MOD_RES   48    48        Phosphotyrosine. 
MOD_RES   94    94        Phosphotyrosine. 
CONFLICT   183   183        K -> E (in Ref. 4; AAH05249). 
Sequence information
Length: 213 AA [This is the length of the unprocessed precursor] Molecular weight: 24377 Da [This is the MW of the unprocessed precursor] CRC64: B115E741E23891C5 [This is a checksum on the sequence]
        10         20         30         40         50         60 
MAITQFRLFK FCTCLATVFS FLKRLICRSG RGRKLSGDQI TLPTTVDYSS VPKQTDVEEW 

        70         80         90        100        110        120 
TSWDEDAPTS VKIEGGNGNV ATQQNSLEQL EPDYFKDMTP TIRKTQKIVI KKREPLNFGI 

       130        140        150        160        170        180 
PDGSTGFSSR LAATQDLPFI HQSSELGDLD TWQENTNAWE EEEDAAWQAE EVLRQQKLAD 

       190        200        210 
REKRAAEQQR KKMEKEAQRL MKKEQNKIGV KLS 

O00559 in FASTA format

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