SSR2

Translocon-associated protein subunit beta also known as TRAP-beta is a protein that in humans is encoded by the SSR2 gene.

SSR2
Identifiers
Aliases	SSR2, TLAP, TRAP-BETA, TRAPB, HSD25, signal sequence receptor subunit 2
External IDs	OMIM: 600867 MGI: 1913506 HomoloGene: 2369 GeneCards: SSR2
Gene location (Human) Chr. Chromosome 1 (human) Band 1q22 Start 156,009,048 bp End 156,020,951 bp
Gene location (Mouse) Chr. Chromosome 3 (mouse) Band 3|3 F1 Start 88,575,876 bp End 88,588,419 bp
RNA expression pattern Bgee Human Mouse (ortholog) Top expressed in body of pancreas islet of Langerhans stromal cell of endometrium ganglionic eminence canal of the cervix left adrenal gland right adrenal gland gallbladder rectum smooth muscle tissue Top expressed in yolk sac seminal vesicula lip molar islet of Langerhans spermatocyte duodenum dermis parotid gland otic placode More reference expression data BioGPS More reference expression data
Gene ontology Molecular function protein binding Cellular component integral component of membrane endoplasmic reticulum membrane endoplasmic reticulum membrane Biological process cotranslational protein targeting to membrane Sources:Amigo / QuickGO
Orthologs Species Human Mouse Entrez 6746 66256 Ensembl ENSG00000163479 ENSMUSG00000041355 UniProt P43308 Q9CPW5 RefSeq (mRNA) NM_003145 NM_025448 RefSeq (protein) NP_003136 NP_079724 NP_001343245 NP_001343246 NP_001343247 NP_001343248 Location (UCSC) Chr 1: 156.01 – 156.02 Mb Chr 3: 88.58 – 88.59 Mb PubMed search
Wikidata
View/Edit Human View/Edit Mouse

Function

The signal sequence receptor (SSR) is a glycosylated endoplasmic reticulum (ER) membrane receptor associated with protein translocation across the ER membrane. The SSR consists of 2 subunits, a 34-kD glycoprotein (alpha-SSR or SSR1) and a 22-kD glycoprotein (beta-SSR or SSR2). The human beta-signal sequence receptor gene (SSR2) maps to chromosome bands 1q21-q23.

Further reading

• Tajima S, Lauffer L, Rath VL, Walter P (October 1986). "The signal recognition particle receptor is a complex that contains two distinct polypeptide chains". The Journal of Cell Biology. 103 (4): 1167–78. doi:10.1083/jcb.103.4.1167. PMC 2114348. PMID 3021779.
• Hartmann E, Görlich D, Kostka S, Otto A, Kraft R, Knespel S, Bürger E, Rapoport TA, Prehn S (June 1993). "A tetrameric complex of membrane proteins in the endoplasmic reticulum". European Journal of Biochemistry. 214 (2): 375–81. doi:10.1111/j.1432-1033.1993.tb17933.x. hdl:11858/00-001M-0000-0015-3BD2-F. PMID 7916687.
• Maruyama K, Sugano S (January 1994). "Oligo-capping: a simple method to replace the cap structure of eukaryotic mRNAs with oligoribonucleotides". Gene. 138 (1–2): 171–4. doi:10.1016/0378-1119(94)90802-8. PMID 8125298.
• Bodescot M, Brison O (January 1994). "Cloning and sequence analysis of the beta subunit of the human translocon-associated protein". Biochimica et Biophysica Acta (BBA) - Gene Structure and Expression. 1217 (1): 101–2. doi:10.1016/0167-4781(94)90131-7. PMID 8286409.
• Suzuki Y, Yoshitomo-Nakagawa K, Maruyama K, Suyama A, Sugano S (October 1997). "Construction and characterization of a full length-enriched and a 5'-end-enriched cDNA library". Gene. 200 (1–2): 149–56. doi:10.1016/S0378-1119(97)00411-3. PMID 9373149.
• Wang L, Dobberstein B (September 1999). "Oligomeric complexes involved in translocation of proteins across the membrane of the endoplasmic reticulum". FEBS Letters. 457 (3): 316–22. doi:10.1016/S0014-5793(99)01075-3. PMID 10471800.
• Zhang H, Li XJ, Martin DB, Aebersold R (June 2003). "Identification and quantification of N-linked glycoproteins using hydrazide chemistry, stable isotope labeling and mass spectrometry". Nature Biotechnology. 21 (6): 660–6. doi:10.1038/nbt827. PMID 12754519. S2CID 581283.
• Suzuki Y, Yamashita R, Shirota M, Sakakibara Y, Chiba J, Mizushima-Sugano J, Nakai K, Sugano S (September 2004). "Sequence comparison of human and mouse genes reveals a homologous block structure in the promoter regions". Genome Research. 14 (9): 1711–8. doi:10.1101/gr.2435604. PMC 515316. PMID 15342556.