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Protein

Receptor-binding cancer antigen expressed on SiSo cells

Gene

EBAG9

Organism
Homo sapiens (Human)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

May participate in suppression of cell proliferation and induces apoptotic cell death through activation of interleukin-1-beta converting enzyme (ICE)-like proteases.3 Publications

GO - Molecular functioni

  • peptidase activator activity involved in apoptotic process Source: UniProtKB

GO - Biological processi

  • regulation of cell growth Source: UniProtKB
Complete GO annotation...

Keywords - Biological processi

Apoptosis

Names & Taxonomyi

Protein namesi
Recommended 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 namesi
Name:EBAG9
Synonyms:RCAS1
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
Proteomesi
  • UP000005640 Componenti: Chromosome 8

Organism-specific databases

HGNCiHGNC:3123. EBAG9.

Subcellular locationi

Topology

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Topological domaini1 – 66ExtracellularSequence analysis
Transmembranei7 – 2721Helical; Signal-anchor for type III membrane proteinSequence analysisAdd
BLAST
Topological domaini28 – 213186CytoplasmicSequence analysisAdd
BLAST

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Golgi apparatus, Membrane

Pathology & Biotechi

Organism-specific databases

PharmGKBiPA27581.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 213213Receptor-binding cancer antigen expressed on SiSo cellsPRO_0000097195Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei36 – 361PhosphoserineCombined sources
Modified residuei41 – 411PhosphothreonineCombined sources
Modified residuei94 – 941PhosphotyrosineCombined sources

Keywords - PTMi

Phosphoprotein

Proteomic databases

EPDiO00559.
MaxQBiO00559.
PaxDbiO00559.
PeptideAtlasiO00559.
PRIDEiO00559.

PTM databases

iPTMnetiO00559.
PhosphoSiteiO00559.
SwissPalmiO00559.

Expressioni

Tissue specificityi

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.

Inductioni

By estrogen.

Gene expression databases

BgeeiO00559.
CleanExiHS_EBAG9.
ExpressionAtlasiO00559. baseline and differential.
GenevisibleiO00559. HS.

Organism-specific databases

HPAiCAB072810.
HPA021153.
HPA021154.

Interactioni

Subunit structurei

Homodimer.

Protein-protein interaction databases

BioGridi114607. 3 interactions.
IntActiO00559. 3 interactions.
STRINGi9606.ENSP00000337675.

Structurei

3D structure databases

ProteinModelPortaliO00559.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Coiled coil

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Coiled coili163 – 21149Sequence analysisAdd
BLAST

Compositional bias

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Compositional biasi160 – 1634Poly-Glu

Domaini

The coiled coil domain is necessary for the homodimerization.

Keywords - Domaini

Coiled coil, Signal-anchor, Transmembrane, Transmembrane helix

Phylogenomic databases

eggNOGiENOG410IE57. Eukaryota.
ENOG41101KS. LUCA.
GeneTreeiENSGT00390000004040.
HOGENOMiHOG000073537.
HOVERGENiHBG059707.
InParanoidiO00559.
OMAiFRLFKIC.
OrthoDBiEOG7RJPSJ.
PhylomeDBiO00559.
TreeFamiTF326584.

Family and domain databases

InterProiIPR017025. Cancer-assoc_antigen_RCAS1.
[Graphical view]
PANTHERiPTHR15208. PTHR15208. 1 hit.
PIRSFiPIRSF034247. RCAS1. 1 hit.

Sequences (2)i

Sequence statusi: Complete.

This entry describes 2 isoformsi produced by alternative splicing. AlignAdd to basket

Isoform 1 (identifier: O00559-1) [UniParc]FASTAAdd to basket

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

« Hide

        10         20         30         40         50
MAITQFRLFK FCTCLATVFS FLKRLICRSG RGRKLSGDQI TLPTTVDYSS
60 70 80 90 100
VPKQTDVEEW TSWDEDAPTS VKIEGGNGNV ATQQNSLEQL EPDYFKDMTP
110 120 130 140 150
TIRKTQKIVI KKREPLNFGI PDGSTGFSSR LAATQDLPFI HQSSELGDLD
160 170 180 190 200
TWQENTNAWE EEEDAAWQAE EVLRQQKLAD REKRAAEQQR KKMEKEAQRL
210
MKKEQNKIGV KLS
Length:213
Mass (Da):24,377
Last modified:July 1, 1997 - v1
Checksum:iB115E741E23891C5
GO
Isoform 2 (identifier: O00559-2) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     174-174: R → RSRTNVCLLCSLLFHHPTPTSTPYINQSVKIERVSLGQWSYGKSKE

Show »
Length:258
Mass (Da):29,466
Checksum:i98ECCBCEA9BA1B9C
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti183 – 1831K → E in AAH05249 (PubMed:15489334).Curated
Sequence conflicti199 – 1991R → Q in BAF83340 (PubMed:14702039).Curated

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei174 – 1741R → RSRTNVCLLCSLLFHHPTPT STPYINQSVKIERVSLGQWS YGKSKE in isoform 2. 1 PublicationVSP_055503

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF006265 mRNA. Translation: AAB61617.1.
AB007619 mRNA. Translation: BAA22572.1.
AY653072 mRNA. Translation: AAU85838.1.
AK290651 mRNA. Translation: BAF83340.1.
CR456984 mRNA. Translation: CAG33265.1.
AC079061 Genomic DNA. No translation available.
AP000427 Genomic DNA. No translation available.
BC005249 mRNA. Translation: AAH05249.1.
BC017729 mRNA. Translation: AAH17729.1.
BC022506 mRNA. Translation: AAH22506.1.
CCDSiCCDS6313.1. [O00559-1]
RefSeqiNP_001265867.1. NM_001278938.1. [O00559-1]
NP_004206.1. NM_004215.4. [O00559-1]
NP_936056.1. NM_198120.2. [O00559-1]
UniGeneiHs.409368.
Hs.632960.

Genome annotation databases

EnsembliENST00000337573; ENSP00000337675; ENSG00000147654. [O00559-1]
ENST00000395785; ENSP00000379131; ENSG00000147654. [O00559-1]
ENST00000531677; ENSP00000432082; ENSG00000147654. [O00559-2]
ENST00000614147; ENSP00000477734; ENSG00000147654. [O00559-2]
ENST00000620557; ENSP00000477645; ENSG00000147654. [O00559-1]
GeneIDi9166.
KEGGihsa:9166.
UCSCiuc003ynf.5. human. [O00559-1]

Keywords - Coding sequence diversityi

Alternative splicing

Cross-referencesi

Web resourcesi

Atlas of Genetics and Cytogenetics in Oncology and Haematology

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF006265 mRNA. Translation: AAB61617.1.
AB007619 mRNA. Translation: BAA22572.1.
AY653072 mRNA. Translation: AAU85838.1.
AK290651 mRNA. Translation: BAF83340.1.
CR456984 mRNA. Translation: CAG33265.1.
AC079061 Genomic DNA. No translation available.
AP000427 Genomic DNA. No translation available.
BC005249 mRNA. Translation: AAH05249.1.
BC017729 mRNA. Translation: AAH17729.1.
BC022506 mRNA. Translation: AAH22506.1.
CCDSiCCDS6313.1. [O00559-1]
RefSeqiNP_001265867.1. NM_001278938.1. [O00559-1]
NP_004206.1. NM_004215.4. [O00559-1]
NP_936056.1. NM_198120.2. [O00559-1]
UniGeneiHs.409368.
Hs.632960.

3D structure databases

ProteinModelPortaliO00559.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi114607. 3 interactions.
IntActiO00559. 3 interactions.
STRINGi9606.ENSP00000337675.

PTM databases

iPTMnetiO00559.
PhosphoSiteiO00559.
SwissPalmiO00559.

Proteomic databases

EPDiO00559.
MaxQBiO00559.
PaxDbiO00559.
PeptideAtlasiO00559.
PRIDEiO00559.

Protocols and materials databases

DNASUi9166.
Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000337573; ENSP00000337675; ENSG00000147654. [O00559-1]
ENST00000395785; ENSP00000379131; ENSG00000147654. [O00559-1]
ENST00000531677; ENSP00000432082; ENSG00000147654. [O00559-2]
ENST00000614147; ENSP00000477734; ENSG00000147654. [O00559-2]
ENST00000620557; ENSP00000477645; ENSG00000147654. [O00559-1]
GeneIDi9166.
KEGGihsa:9166.
UCSCiuc003ynf.5. human. [O00559-1]

Organism-specific databases

CTDi9166.
GeneCardsiEBAG9.
HGNCiHGNC:3123. EBAG9.
HPAiCAB072810.
HPA021153.
HPA021154.
MIMi605772. gene.
neXtProtiNX_O00559.
PharmGKBiPA27581.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiENOG410IE57. Eukaryota.
ENOG41101KS. LUCA.
GeneTreeiENSGT00390000004040.
HOGENOMiHOG000073537.
HOVERGENiHBG059707.
InParanoidiO00559.
OMAiFRLFKIC.
OrthoDBiEOG7RJPSJ.
PhylomeDBiO00559.
TreeFamiTF326584.

Miscellaneous databases

ChiTaRSiEBAG9. human.
GeneWikiiEBAG9.
GenomeRNAii9166.
PROiO00559.
SOURCEiSearch...

Gene expression databases

BgeeiO00559.
CleanExiHS_EBAG9.
ExpressionAtlasiO00559. baseline and differential.
GenevisibleiO00559. HS.

Family and domain databases

InterProiIPR017025. Cancer-assoc_antigen_RCAS1.
[Graphical view]
PANTHERiPTHR15208. PTHR15208. 1 hit.
PIRSFiPIRSF034247. RCAS1. 1 hit.
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  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] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
    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] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
    Tissue: Mammary cancer.
  3. Lo W.Y., Hsieh S.L.
    Submitted (JUN-2004) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2).
  4. "Complete sequencing and characterization of 21,243 full-length human cDNAs."
    Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.
    , Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.
    Nat. Genet. 36:40-45(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
    Tissue: Embryo.
  5. "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] (ISOFORM 1).
  6. "DNA sequence and analysis of human chromosome 8."
    Nusbaum C., Mikkelsen T.S., Zody M.C., Asakawa S., Taudien S., Garber M., Kodira C.D., Schueler M.G., Shimizu A., Whittaker C.A., Chang J.L., Cuomo C.A., Dewar K., FitzGerald M.G., Yang X., Allen N.R., Anderson S., Asakawa T.
    , Blechschmidt K., Bloom T., Borowsky M.L., Butler J., Cook A., Corum B., DeArellano K., DeCaprio D., Dooley K.T., Dorris L. III, Engels R., Gloeckner G., Hafez N., Hagopian D.S., Hall J.L., Ishikawa S.K., Jaffe D.B., Kamat A., Kudoh J., Lehmann R., Lokitsang T., Macdonald P., Major J.E., Matthews C.D., Mauceli E., Menzel U., Mihalev A.H., Minoshima S., Murayama Y., Naylor J.W., Nicol R., Nguyen C., O'Leary S.B., O'Neill K., Parker S.C.J., Polley A., Raymond C.K., Reichwald K., Rodriguez J., Sasaki T., Schilhabel M., Siddiqui R., Smith C.L., Sneddon T.P., Talamas J.A., Tenzin P., Topham K., Venkataraman V., Wen G., Yamazaki S., Young S.K., Zeng Q., Zimmer A.R., Rosenthal A., Birren B.W., Platzer M., Shimizu N., Lander E.S.
    Nature 439:331-335(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  7. "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] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
    Tissue: Brain, Lung and Placenta.
  8. Cited for: ROLE IN CANCER.
  9. "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] [Europe PMC] [Abstract]
    Cited for: ROLE IN CANCER.
  10. "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] [Europe PMC] [Abstract]
    Cited for: FUNCTION, SUBCELLULAR LOCATION.
  11. "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] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-36 AND THR-41, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Leukemic T-cell.
  12. "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] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-94, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  13. "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] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-36, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  14. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-36, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Platelet.
  15. "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] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-36, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  16. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-36, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  17. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-36, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  18. "Quantitative phosphoproteomic analysis of T cell receptor signaling reveals system-wide modulation of protein-protein interactions."
    Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K., Rodionov V., Han D.K.
    Sci. Signal. 2:RA46-RA46(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-36, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Leukemic T-cell.
  19. "Quantitative phosphoproteomics reveals widespread full phosphorylation site occupancy during mitosis."
    Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L., Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S., Mann M.
    Sci. Signal. 3:RA3-RA3(2010) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-36, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  20. "System-wide temporal characterization of the proteome and phosphoproteome of human embryonic stem cell differentiation."
    Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J., Johansen P.T., Kratchmarova I., Kassem M., Mann M., Olsen J.V., Blagoev B.
    Sci. Signal. 4:RS3-RS3(2011) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-36, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  21. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  22. "Toward a comprehensive characterization of a human cancer cell phosphoproteome."
    Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J., Mohammed S.
    J. Proteome Res. 12:260-271(2013) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-36, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma and Erythroleukemia.
  23. "An enzyme assisted RP-RPLC approach for in-depth analysis of human liver phosphoproteome."
    Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., Wang L., Ye M., Zou H.
    J. Proteomics 96:253-262(2014) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-36, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Liver.

Entry informationi

Entry nameiRCAS1_HUMAN
AccessioniPrimary (citable) accession number: O00559
Secondary accession number(s): A8K3N6
, Q5Y8C7, Q6IB20, Q9BS76
Entry historyi
Integrated into UniProtKB/Swiss-Prot: December 1, 2000
Last sequence update: July 1, 1997
Last modified: July 6, 2016
This is version 140 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
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.

Miscellaneousi

Miscellaneous

May serve as a prognostic marker for cancers such as adenocarcinomas of the lung and breast cancers. 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.

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.Curated

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. Human chromosome 8
    Human chromosome 8: entries, gene names and cross-references to MIM
  2. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.