Skip Header

 
Contribute Send feedback
Read comments (0) or add your own

Reviewed, UniProtKB/Swiss-Prot O00559 (RCAS1_HUMAN)

Last modified October 13, 2009. Version 85. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data | Customize display text xml rdf/xml gff fasta
Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Web resources · Cross-references · Entry information · Relevant documents

Names and origin

Protein namesRecommended name:
    Receptor-binding cancer antigen expressed on SiSo cells
Alternative name(s):
    Cancer-associated surface antigen RCAS1
    Estrogen receptor-binding fragment-associated gene 9 protein
Gene names
Name: EBAG9
Synonyms: RCAS1
OrganismHomo sapiens (Human) [Complete proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length213 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is not processed.
Protein existenceEvidence at protein level.

General annotation (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. Ref.7

Subunit structure

Homodimer.

Subcellular location

Golgi apparatus membrane; Single-pass type III membrane protein. Note: According to Ref.1, it also exists as a soluble form which has the same biological activities. The existence of such soluble form is however uncertain. Ref.7

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.

Involvement in 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 Ref.7, 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. Ref.5 Ref.6

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, Ref.7 showed that it does not bind any receptor.

Ontologies

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 213213Receptor-binding cancer antigen expressed on SiSo cells
PRO_0000097195

Regions

Topological domain1 – 66Extracellular Potential
Transmembrane7 – 2721Signal-anchor for type III membrane protein Potential
Topological domain28 – 213186Cytoplasmic Potential
Coiled coil163 – 21149 Potential
Compositional bias160 – 1634Poly-Glu

Amino acid modifications

Modified residue361Phosphoserine Ref.8 Ref.10 Ref.11 Ref.12 Ref.13 Ref.14 Ref.15
Modified residue411Phosphothreonine Ref.8
Modified residue481Phosphotyrosine Ref.8
Modified residue941Phosphotyrosine Ref.9

Experimental info

Sequence conflict1831K → E in AAH05249. Ref.4

Sequences

Sequence LengthMass (Da)Tools
O00559-1 [UniParc].

Last modified July 1, 1997. Version 1.
Checksum: B115E741E23891C5

FASTA21324,377
        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 

« Hide

References

« Hide 'large scale' references
[1]"Inhibition of cell growth and induction of apoptotic cell death by the human tumor-associated antigen RCAS1."
Nakashima M., Sonoda K., Watanabe T.
Nat. Med. 5:938-942(1999) [PubMed: 10426319] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
Tissue: Uterine adenocarcinoma.
[2]"Isolation of estrogen-responsive genes with a CpG island library."
Watanabe T., Inoue S., Hiroi H., Orimo A., Kawashima H., Muramatsu M.
Mol. Cell. Biol. 18:442-449(1998) [PubMed: 9418891] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
Tissue: Mammary cancer.
[3]"Cloning of human full open reading frames in Gateway(TM) system entry vector (pDONR201)."
Ebert L., Schick M., Neubert P., Schatten R., Henze S., Korn B.
Submitted (JUN-2004) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
[4]"The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
The MGC Project Team
Genome Res. 14:2121-2127(2004) [PubMed: 15489334] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Tissue: Brain, Lung and Placenta.
[5]"RCAS1 is associated with ductal breast cancer progression."
Rousseau J., Tetu B., Caron D., Malenfant P., Cattaruzzi P., Audette M., Doillon C., Tremblay J.P., Guerette B.
Biochem. Biophys. Res. Commun. 293:1544-1549(2002) [PubMed: 12054692] [Abstract]
Cited for: DISEASE.
[6]"RCAS1 expression: a potential prognostic marker for adenocarcinomas of the lung."
Oizumi S., Yamazaki K., Nakashima M., Watanabe T., Hommura F., Ogura S., Nishimura M., Dosaka-Akita H.
Oncology 62:333-339(2002) [PubMed: 12138241] [Abstract]
Cited for: DISEASE.
[7]"The Golgi protein RCAS1 controls cell surface expression of tumor-associated O-linked glycan antigens."
Engelsberg A., Hermosilla R., Karsten U., Schuelein R., Doerken B., Rehm A.
J. Biol. Chem. 278:22998-23007(2003) [PubMed: 12672804] [Abstract]
Cited for: FUNCTION, SUBCELLULAR LOCATION.
[8]"Robust phosphoproteomic profiling of tyrosine phosphorylation sites from human T cells using immobilized metal affinity chromatography and tandem mass spectrometry."
Brill L.M., Salomon A.R., Ficarro S.B., Mukherji M., Stettler-Gill M., Peters E.C.
Anal. Chem. 76:2763-2772(2004) [PubMed: 15144186] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-36; THR-41 AND TYR-48, MASS SPECTROMETRY.
Tissue: T-cell.
[9]"Immunoaffinity profiling of tyrosine phosphorylation in cancer cells."
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.
Nat. Biotechnol. 23:94-101(2005) [PubMed: 15592455] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-94, MASS SPECTROMETRY.
[10]"Global, in vivo, and site-specific phosphorylation dynamics in signaling networks."
Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P., Mann M.
Cell 127:635-648(2006) [PubMed: 17081983] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-36, MASS SPECTROMETRY.
Tissue: Epithelium.
[11]"Toward a global characterization of the phosphoproteome in prostate cancer cells: identification of phosphoproteins in the LNCaP cell line."
Giorgianni F., Zhao Y., Desiderio D.M., Beranova-Giorgianni S.
Electrophoresis 28:2027-2034(2007) [PubMed: 17487921] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-36, MASS SPECTROMETRY.
[12]"Automated phosphoproteome analysis for cultured cancer cells by two-dimensional nanoLC-MS using a calcined titania/C18 biphasic column."
Imami K., Sugiyama N., Kyono Y., Tomita M., Ishihama Y.
Anal. Sci. 24:161-166(2008) [PubMed: 18187866] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-36, MASS SPECTROMETRY.
[13]"Phosphoproteome of resting human platelets."
Zahedi R.P., Lewandrowski U., Wiesner J., Wortelkamp S., Moebius J., Schuetz C., Walter U., Gambaryan S., Sickmann A.
J. Proteome Res. 7:526-534(2008) [PubMed: 18088087] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-36, MASS SPECTROMETRY.
Tissue: Platelet.
[14]"Kinase-selective enrichment enables quantitative phosphoproteomics of the kinome across the cell cycle."
Daub H., Olsen J.V., Bairlein M., Gnad F., Oppermann F.S., Korner R., Greff Z., Keri G., Stemmann O., Mann M.
Mol. Cell 31:438-448(2008) [PubMed: 18691976] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-36, MASS SPECTROMETRY.
[15]"A quantitative atlas of mitotic phosphorylation."
Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E., Elledge S.J., Gygi S.P.
Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008) [PubMed: 18669648] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-36, MASS SPECTROMETRY.
+Additional computationally mapped references.

Cross-references

Sequence databases

AF006265 mRNA. Translation: AAB61617.1.
AB007619 mRNA. Translation: BAA22572.1.
CR456984 mRNA. Translation: CAG33265.1.
BC005249 mRNA. Translation: AAH05249.1.
BC017729 mRNA. Translation: AAH17729.1.
BC022506 mRNA. Translation: AAH22506.1.
IPIIPI00299076.
RefSeqNP_004206.1.
NP_936056.1.
UniGeneHs.409368

3D structure databases

ModBaseSearch...

Protein-protein interaction databases

STRINGO00559.

PTM databases

PhosphoSiteO00559.

Proteomic databases

PRIDEO00559.

Genome annotation databases

EnsemblENST00000276658; ENSP00000276658; ENSG00000147654; Homo sapiens. [Genome view]
ENST00000337573; ENSP00000337675; ENSG00000147654; Homo sapiens. [Genome view]
ENST00000395785; ENSP00000379131; ENSG00000147654; Homo sapiens. [Genome view]
GeneID9166.
KEGGhsa:9166.
UCSCuc003ynf.1. human.

Organism-specific databases

CTD9166.
GeneCardsGC08P110621.
H-InvDBHIX0007729.
HGNCHGNC:3123. EBAG9.
HPAHPA021153.
HPA021154.
MIM605772. gene.
PharmGKBPA27581.
GenAtlasSearch...

Phylogenomic databases

HOVERGENO00559.

Gene expression databases

ArrayExpressO00559.
BgeeO00559.
CleanExHS_EBAG9.
GenevestigatorO00559.
GermOnlineENSG00000147654. Homo sapiens.

Family and domain databases

InterProIPR017025. Cancer-assoc_antigen_RCAS1.
[Graphical view]
PIRSFPIRSF034247. RCAS1. 1 hit.
ProtoNetSearch...

Other Resources

NextBio34373.
SOURCESearch...

Entry information

Entry nameRCAS1_HUMAN
AccessionPrimary (citable) accession number: O00559
Secondary accession number(s): Q6IB20, Q9BS76
Entry history
Integrated into UniProtKB/Swiss-Prot: December 1, 2000
Last sequence update: July 1, 1997
Last modified: October 13, 2009
This is version 85 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation projectHPI (Human Proteome Initiative)
DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

Relevant documents

Human chromosome 8

Human chromosome 8: entries, gene names and cross-references to MIM

MIM cross-references

Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot

Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Web resources · Cross-references · Entry information · Relevant documents