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Protein

Receptor-binding cancer antigen expressed on SiSo cells

Gene

Ebag9

Organism
Mus musculus (Mouse)
Status
Reviewed-Annotation score: Annotation score: 3 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.By similarity

GO - Biological processi

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
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
Proteomesi
  • UP000000589 Componenti: Chromosome 15

Organism-specific databases

MGIiMGI:1859920. Ebag9.

Subcellular locationi

Topology

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Topological domaini1 – 77ExtracellularSequence analysis
Transmembranei8 – 2720Helical; 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

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 213213Receptor-binding cancer antigen expressed on SiSo cellsPRO_0000097196Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei36 – 361PhosphoserineCombined sources
Modified residuei41 – 411PhosphothreonineBy similarity
Modified residuei94 – 941PhosphotyrosineBy similarity

Keywords - PTMi

Phosphoprotein

Proteomic databases

EPDiQ9D0V7.
MaxQBiQ9D0V7.
PaxDbiQ9D0V7.
PRIDEiQ9D0V7.

PTM databases

iPTMnetiQ9D0V7.
PhosphoSiteiQ9D0V7.
SwissPalmiQ9D0V7.

Expressioni

Tissue specificityi

Widely expressed. Expressed in heart, brain, spleen, liver, kidney and testis.1 Publication

Developmental stagei

Expressed in the developing embryo.1 Publication

Inductioni

By 17-beta-estradiol (E2).1 Publication

Gene expression databases

BgeeiQ9D0V7.
GenevisibleiQ9D0V7. MM.

Interactioni

Subunit structurei

Homodimer.By similarity

Protein-protein interaction databases

STRINGi10090.ENSMUSP00000022964.

Structurei

3D structure databases

ProteinModelPortaliQ9D0V7.
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.By similarity

Keywords - Domaini

Coiled coil, Signal-anchor, Transmembrane, Transmembrane helix

Phylogenomic databases

eggNOGiENOG410IE57. Eukaryota.
ENOG41101KS. LUCA.
GeneTreeiENSGT00390000004040.
HOGENOMiHOG000073537.
HOVERGENiHBG059707.
InParanoidiQ9D0V7.
OMAiFRLFKIC.
OrthoDBiEOG7RJPSJ.
PhylomeDBiQ9D0V7.
TreeFamiTF326584.

Family and domain databases

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

Sequencei

Sequence statusi: Complete.

Q9D0V7-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MAITQFRLFK VCTCLATVFS FLKRLICRSG RGRKLSGDQI TLPTTVDYSS
60 70 80 90 100
VPKQTDVEEW TSWDEDAPTS VKIEGGNGNV ATQQNSLEQL EPDYFKDMTP
110 120 130 140 150
TIRKTQKIVI KKREPLNFGV PDGSTGFSSR LAATQDMPFI HQSSELGDLD
160 170 180 190 200
TWQENSNAWE EEEDAAWQAE EVLRQQKIAD REKRAAEQQR KKMEKEAQRL
210
MKKEQNKIGV KLS
Length:213
Mass (Da):24,319
Last modified:September 26, 2003 - v2
Checksum:i349FAD1E2AEFF529
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti11 – 111V → G in AAF23857 (PubMed:16141072).Curated
Sequence conflicti115 – 1151P → A in AAF23857 (PubMed:16141072).Curated
Sequence conflicti150 – 1501D → G in BAE35132 (PubMed:16141072).Curated
Sequence conflicti157 – 1571N → S in AAF23857 (PubMed:16141072).Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AY009091 mRNA. Translation: AAG41054.1.
AF076524 mRNA. Translation: AAF23857.1.
AK004366 mRNA. Translation: BAB23277.1.
AK159499 mRNA. Translation: BAE35132.1.
AK160149 mRNA. Translation: BAE35657.1.
BC108397 mRNA. Translation: AAI08398.1.
BC119118 mRNA. Translation: AAI19119.1.
BC119120 mRNA. Translation: AAI19121.1.
BC144740 mRNA. Translation: AAI44741.1.
CCDSiCCDS27457.1.
PIRiJC7696.
RefSeqiNP_062353.3. NM_019480.4.
XP_006521256.1. XM_006521193.1.
XP_006521257.1. XM_006521194.2.
XP_006521258.1. XM_006521195.2.
UniGeneiMm.287896.

Genome annotation databases

EnsembliENSMUST00000022964; ENSMUSP00000022964; ENSMUSG00000022339.
GeneIDi55960.
KEGGimmu:55960.
UCSCiuc007vpz.1. mouse.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AY009091 mRNA. Translation: AAG41054.1.
AF076524 mRNA. Translation: AAF23857.1.
AK004366 mRNA. Translation: BAB23277.1.
AK159499 mRNA. Translation: BAE35132.1.
AK160149 mRNA. Translation: BAE35657.1.
BC108397 mRNA. Translation: AAI08398.1.
BC119118 mRNA. Translation: AAI19119.1.
BC119120 mRNA. Translation: AAI19121.1.
BC144740 mRNA. Translation: AAI44741.1.
CCDSiCCDS27457.1.
PIRiJC7696.
RefSeqiNP_062353.3. NM_019480.4.
XP_006521256.1. XM_006521193.1.
XP_006521257.1. XM_006521194.2.
XP_006521258.1. XM_006521195.2.
UniGeneiMm.287896.

3D structure databases

ProteinModelPortaliQ9D0V7.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi10090.ENSMUSP00000022964.

PTM databases

iPTMnetiQ9D0V7.
PhosphoSiteiQ9D0V7.
SwissPalmiQ9D0V7.

Proteomic databases

EPDiQ9D0V7.
MaxQBiQ9D0V7.
PaxDbiQ9D0V7.
PRIDEiQ9D0V7.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSMUST00000022964; ENSMUSP00000022964; ENSMUSG00000022339.
GeneIDi55960.
KEGGimmu:55960.
UCSCiuc007vpz.1. mouse.

Organism-specific databases

CTDi9166.
MGIiMGI:1859920. Ebag9.

Phylogenomic databases

eggNOGiENOG410IE57. Eukaryota.
ENOG41101KS. LUCA.
GeneTreeiENSGT00390000004040.
HOGENOMiHOG000073537.
HOVERGENiHBG059707.
InParanoidiQ9D0V7.
OMAiFRLFKIC.
OrthoDBiEOG7RJPSJ.
PhylomeDBiQ9D0V7.
TreeFamiTF326584.

Miscellaneous databases

NextBioi311658.
PROiQ9D0V7.
SOURCEiSearch...

Gene expression databases

BgeeiQ9D0V7.
GenevisibleiQ9D0V7. MM.

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. "Molecular cloning and characterization of mouse EBAG9, homolog of a human cancer associated surface antigen: expression and regulation by estrogen."
    Tsuchiya F., Ikeda K., Tsutsumi O., Hiroi H., Momoeda M., Taketani Y., Muramatsu M., Inoue S.
    Biochem. Biophys. Res. Commun. 284:2-10(2001) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA], TISSUE SPECIFICITY, DEVELOPMENTAL STAGE, INDUCTION.
    Tissue: Brain.
  2. "Human type II receptor like cancer associated surface antigen (RCAS1)."
    Nakashima M., Sonoda K., Watanabe T.
    Submitted (JAN-2000) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
    Strain: C57BL/6J.
  3. "The transcriptional landscape of the mammalian genome."
    Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.
    , Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.
    Science 309:1559-1563(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Strain: C57BL/6J.
    Tissue: Embryo and Testis.
  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] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Strain: C57BL/6J.
    Tissue: Brain and Embryo.
  5. "Qualitative and quantitative analyses of protein phosphorylation in naive and stimulated mouse synaptosomal preparations."
    Munton R.P., Tweedie-Cullen R., Livingstone-Zatchej M., Weinandy F., Waidelich M., Longo D., Gehrig P., Potthast F., Rutishauser D., Gerrits B., Panse C., Schlapbach R., Mansuy I.M.
    Mol. Cell. Proteomics 6:283-293(2007) [PubMed] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Brain cortex.
  6. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-36, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Liver.
  7. "Specific phosphopeptide enrichment with immobilized titanium ion affinity chromatography adsorbent for phosphoproteome analysis."
    Zhou H., Ye M., Dong J., Han G., Jiang X., Wu R., Zou H.
    J. Proteome Res. 7:3957-3967(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-36, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Liver.
  8. "The phagosomal proteome in interferon-gamma-activated macrophages."
    Trost M., English L., Lemieux S., Courcelles M., Desjardins M., Thibault P.
    Immunity 30:143-154(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-36, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  9. "Large scale localization of protein phosphorylation by use of electron capture dissociation mass spectrometry."
    Sweet S.M., Bailey C.M., Cunningham D.L., Heath J.K., Cooper H.J.
    Mol. Cell. Proteomics 8:904-912(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Embryonic fibroblast.
  10. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-36, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Brain, Brown adipose tissue, Heart, Kidney, Liver, Lung, Pancreas, Spleen and Testis.

Entry informationi

Entry nameiRCAS1_MOUSE
AccessioniPrimary (citable) accession number: Q9D0V7
Secondary accession number(s): Q0VET4
, Q3TVG2, Q3TWY4, Q9QYD0
Entry historyi
Integrated into UniProtKB/Swiss-Prot: September 26, 2003
Last sequence update: September 26, 2003
Last modified: May 11, 2016
This is version 106 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. MGD cross-references
    Mouse Genome Database (MGD) 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.