Translocon-associated protein subunit beta (SSR2)

The protein contains 183 amino acids for an estimated molecular weight of 20135 Da.

 

TRAP proteins are part of a complex whose function is to bind calcium to the ER membrane and thereby regulate the retention of ER resident proteins. (updated: Oct. 10, 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.

This protein is predicted to be membranous by TOPCONS.


Interpro domains
Total structural coverage: 0%
Model score: 40

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The reference OMIM entry for this protein is 600867

Signal sequence receptor, beta; ssr2
Translocon-associated protein, beta
Trap-beta

DESCRIPTION

In order to translocate membrane or secretory proteins across the endoplasmic reticulum (ER) membrane, the signal sequence of a nascent peptide is recognized by a signal recognition particle (SRP), by which the nascent peptide associated with a ribosome can bind to the ER membrane receptor (or docking protein). The SRP is released from both the ribosome and the signal sequence; the latter lies near an integral, glycosylated ER membrane protein referred to as the signal sequence receptor (SSR). The SSR consists of 2 subunits: a 34-kD glycoprotein, alpha-SSR (SSR1; 600868), and a 22-kD glycoprotein, beta-SSR (SSR2) (summary by Chinen et al., 1995).

CLONING

Chinen et al. (1995) isolated a human cDNA clone homologous to the canine beta-SSR gene. Northern blot analysis revealed ubiquitous expression of beta-SSR in all organs examined.

MAPPING

By FISH, Chinen et al. (1995) mapped the SSR2 gene to chromosome 1q21-q23. ... 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 600867 was added.

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