Receptor-binding cancer antigen expressed on SiSo cells (EBAG9)

The protein contains 213 amino acids for an estimated molecular weight of 24377 Da.

 

May participate in suppression of cell proliferation and induces apoptotic cell death through activation of interleukin-1-beta converting enzyme (ICE)-like proteases. (updated: Sept. 12, 2018)

Protein identification was indicated in the following studies:

  1. Bryk and co-workers. (2017) Quantitative Analysis of Human Red Blood Cell Proteome. J Proteome Res. 16(8), 2752-2761.

Methods

The following articles were analysed to gather the proteome content of erythrocytes.

The gene or protein list provided in the studies were processed using the ID mapping API of Uniprot in September 2018. The number of proteins identified and mapped without ambiguity in these studies is indicated below.
Only Swiss-Prot entries (reviewed) were considered for protein evidence assignation.

PublicationIdentification 1Uniprot mapping 2Not mapped /
Obsolete
TrEMBLSwiss-Prot
Goodman (2013)2289 (gene list)227853205992269
Lange (2014)123412347281224
Hegedus (2015)2638262202352387
Wilson (2016)165815281702911068
d'Alessandro (2017)18261817201815
Bryk (2017)20902060101081942
Chu (2018)18531804553621387

1 as available in the article and/or in supplementary material
2 uniprot mapping returns all protein isoforms as one entry

The compilation of older studies can be retrieved from the Red Blood Cell Collection database.

The data and differentiation stages presented below come from the proteomic study and analysis performed by our partners of the GReX consortium, more details are available in their published work.

No sequence conservation computed yet.

Interpro domains
Total structural coverage: 0%
Model score: 41

(right-click above to access to more options from the contextual menu)

No binding partner found

The reference OMIM entry for this protein is 605772

Estrogen receptor-binding site-associated antigen, 9; ebag9
Rcas1
Eb9

Estrogen is essential for the growth, development, differentiation, and function of female organs as well as other nonreproductive organ systems. Estrogen action is mediated by estrogen receptors (ESR) which bind to estrogen-responsive elements (ERE) that exist in the enhancer regions of target genes, directly regulating their transcription. Watanabe et al. (1998) used the CpG-GBS (genomic binding site) method to isolate novel estrogen-responsive genes. By screening a breast cancer cDNA library with the ESR-binding fragments isolated from the CpG island library, they isolated cDNAs encoding EBAG9, GRIN2D (602717), and COX7A2L (605771), which the authors termed EB9, EB11, and EB1 (or COX7RP), respectively. EBAG9 encodes a deduced 214-amino acid protein. Northern blot analysis revealed expression of a 1.8-kb transcript in endometrial carcinoma and breast cancer cell lines and, to a lesser extent, in an osteosarcoma cell line. Gel mobility shift analysis confirmed that the ERE of EBAG9 binds to ESR. Northern blot analysis detected an upregulation of EBAG9 after estrogen treatment of a breast cancer cell line. Ikeda et al. (2000) noted that EBAG9 is identical with RCAS1, a human cancer cell surface antigen isolated by Nakashima et al. (1999). Ikeda et al. (2000) determined that the 5-prime flanking region of EBAG9 is 65% GC-rich, lacks a TATA motif, and contains a perfect palindromic ERE element at -60 to -48 upstream of the transcription initiation site. Promoter analysis revealed that the ERE-containing region can respond to estrogen in a breast cancer cell line. Electrophoretic mobility shift and supershift analysis demonstrated that ESR1 (133430) is involved in binding to the ERE element. Using FISH, Ikeda et al. (2000) mapped the EBAG9 gene to chromosome 8q23, a region that is frequently amplified in tumors. ... More on the omim web site

Subscribe to this protein entry history

Dec. 10, 2018: Protein entry updated
Automatic update: model status changed

Oct. 20, 2018: Protein entry updated
Automatic update: OMIM entry 605772 was added.

Oct. 19, 2018: Additional information
Initial protein addition to the database. This entry was referenced in Bryk and co-workers. (2017).