O00559 (RCAS1_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

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 names

Name:	EBAG9
Synonyms:	RCAS1

Organism

Homo sapiens (Human)

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Primates › Haplorrhini › Catarrhini › Hominidae › Homo

Protein attributes

Sequence length	213 AA.
Sequence status	Complete.
Protein existence	Evidence 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.5 Ref.6 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.
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 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.
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

Keywords
Biological process	Apoptosis
Cellular component	Golgi apparatus Membrane
Domain	Coiled coil Signal-anchor Transmembrane Transmembrane helix
PTM	Phosphoprotein
Technical term	Complete proteome Reference proteome
Gene Ontology (GO)
Biological process	apoptotic process Inferred from electronic annotation. Source: UniProtKB-KW regulation of cell growth Non-traceable author statement Ref.1. Source: UniProtKB
Cellular component	Golgi membrane Inferred from electronic annotation. Source: UniProtKB-SubCell focal adhesion Inferred from direct assay. Source: HPA integral to membrane Non-traceable author statement. Source: UniProtKB soluble fraction Non-traceable author statement. Source: UniProtKB
Molecular function	apoptotic protease activator activity Non-traceable author statement Ref.1. Source: UniProtKB
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 213	213	Receptor-binding cancer antigen expressed on SiSo cells		PRO_0000097195
Regions
	Topological domain	1 – 6	6	Extracellular Potential
	Transmembrane	7 – 27	21	Helical; Signal-anchor for type III membrane protein; Potential
	Topological domain	28 – 213	186	Cytoplasmic Potential
	Coiled coil	163 – 211	49	Potential
	Compositional bias	160 – 163	4	Poly-Glu
Amino acid modifications
	Modified residue	36	1	Phosphoserine Ref.8 Ref.10 Ref.11 Ref.12 Ref.13 Ref.14 Ref.15 Ref.16 Ref.17 Ref.18
	Modified residue	41	1	Phosphothreonine Ref.8
	Modified residue	48	1	Phosphotyrosine Ref.8
	Modified residue	86	1	Phosphoserine Ref.16
	Modified residue	94	1	Phosphotyrosine Ref.9
Experimental info
	Sequence conflict	183	1	K → E in AAH05249. Ref.4

Sequences

	Sequence		Length	Mass (Da)
	O00559 [UniParc]. Last modified July 1, 1997. Version 1. Checksum: B115E741E23891C5	FASTA	213	24,377
	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

References

	« Hide 'large scale' referencesShow '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: ROLE IN CANCER.
[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: ROLE IN CANCER.
[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: Leukemic 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: Cervix carcinoma.
[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. Tissue: Prostate cancer.
[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. Tissue: Cervix carcinoma.
[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. Tissue: Cervix carcinoma.
[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. Tissue: Cervix carcinoma.
[16]	"Lys-N and trypsin cover complementary parts of the phosphoproteome in a refined SCX-based approach." Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J., Mohammed S. Anal. Chem. 81:4493-4501(2009) [PubMed: 19413330] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-36 AND SER-86, MASS SPECTROMETRY. Tissue: Embryonic kidney.
[17]	"Large-scale proteomics analysis of the human kinome." Oppermann F.S., Gnad F., Olsen J.V., Hornberger R., Greff Z., Keri G., Mann M., Daub H. Mol. Cell. Proteomics 8:1751-1764(2009) [PubMed: 19369195] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-36, MASS SPECTROMETRY.
[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: 19690332] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-36, MASS SPECTROMETRY. Tissue: Leukemic T-cell.
+	Additional computationally mapped references.

Web resources

Atlas of Genetics and Cytogenetics in Oncology and Haematology

Cross-references

Sequence databases
EMBL GenBank DDBJ	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.
IPI	IPI00299076.
RefSeq	NP_004206.1. NM_004215.3. NP_936056.1. NM_198120.1.
UniGene	Hs.409368.
3D structure databases
ProteinModelPortal	O00559.
ModBase	Search...
Protein-protein interaction databases
STRING	O00559.
PTM databases
PhosphoSite	O00559.
Proteomic databases
PRIDE	O00559.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
Ensembl	ENST00000337573; ENSP00000337675; ENSG00000147654. ENST00000395785; ENSP00000379131; ENSG00000147654.
GeneID	9166.
KEGG	hsa:9166.
UCSC	uc003ynf.1. human.
Organism-specific databases
CTD	9166.
GeneCards	GC08P110621.
H-InvDB	HIX0007729.
HGNC	HGNC:3123. EBAG9.
HPA	HPA021153. HPA021154.
MIM	605772. gene.
neXtProt	NX_O00559.
PharmGKB	PA27581.
GenAtlas	Search...
Phylogenomic databases
eggNOG	prNOG08413.
HOVERGEN	HBG059707.
OrthoDB	EOG4XPQGZ.
PhylomeDB	O00559.
Gene expression databases
ArrayExpress	O00559.
Bgee	O00559.
CleanEx	HS_EBAG9.
Genevestigator	O00559.
GermOnline	ENSG00000147654. Homo sapiens.
Family and domain databases
InterPro	IPR017025. Cancer-assoc_antigen_RCAS1. [Graphical view]
PIRSF	PIRSF034247. RCAS1. 1 hit.
ProtoNet	Search...
Other
NextBio	34373.
SOURCE	Search...

Entry information

Entry name

RCAS1_HUMAN

Accession

Primary (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:	January 25, 2012
This is version 100 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program

Disclaimer

Any 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.