SEC61B

Sec61 beta subunit, also known as SEC61B, is a human gene.

PBB_Summary
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summary_text = The Sec61 complex is the central component of the protein translocation apparatus of the endoplasmic reticulum (ER) membrane. Oligomers of the Sec61 complex form a transmembrane channel where proteins are translocated across and integrated into the ER membrane. This complex consists of three membrane proteins- alpha, beta, and gamma. This gene encodes the beta-subunit protein. The Sec61 subunits are also observed in the post-ER compartment, suggesting that these proteins can escape the ER and recycle back. There is evidence for multiple polyadenylated sites for this transcript.cite web | title = Entrez Gene: SEC61B Sec61 beta subunit| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=10952| accessdate = ]

References

Further reading

PBB_Further_reading
citations =
*cite journal | author=Hartmann E, Sommer T, Prehn S, "et al." |title=Evolutionary conservation of components of the protein translocation complex. |journal=Nature |volume=367 |issue= 6464 |pages= 654–7 |year= 1994 |pmid= 8107851 |doi= 10.1038/367654a0
*cite journal | author=Maruyama K, Sugano S |title=Oligo-capping: a simple method to replace the cap structure of eukaryotic mRNAs with oligoribonucleotides. |journal=Gene |volume=138 |issue= 1-2 |pages= 171–4 |year= 1994 |pmid= 8125298 |doi=10.1016/0378-1119(94)90802-8
*cite journal | author=Wiertz EJ, Tortorella D, Bogyo M, "et al." |title=Sec61-mediated transfer of a membrane protein from the endoplasmic reticulum to the proteasome for destruction. |journal=Nature |volume=384 |issue= 6608 |pages= 432–8 |year= 1997 |pmid= 8945469 |doi= 10.1038/384432a0
*cite journal | author=Suzuki Y, Yoshitomo-Nakagawa K, Maruyama K, "et al." |title=Construction and characterization of a full length-enriched and a 5'-end-enriched cDNA library. |journal=Gene |volume=200 |issue= 1-2 |pages= 149–56 |year= 1997 |pmid= 9373149 |doi=10.1016/S0378-1119(97)00411-3
*cite journal | author=Knight BC, High S |title=Membrane integration of Sec61alpha: a core component of the endoplasmic reticulum translocation complex. |journal=Biochem. J. |volume=331 ( Pt 1) |issue= |pages= 161–7 |year= 1998 |pmid= 9512475 |doi=
*cite journal | author=Chen Y, Le Cahérec F, Chuck SL |title=Calnexin and other factors that alter translocation affect the rapid binding of ubiquitin to apoB in the Sec61 complex. |journal=J. Biol. Chem. |volume=273 |issue= 19 |pages= 11887–94 |year= 1998 |pmid= 9565615 |doi=10.1074/jbc.273.19.11887
*cite journal | author=Kalies KU, Rapoport TA, Hartmann E |title=The beta subunit of the Sec61 complex facilitates cotranslational protein transport and interacts with the signal peptidase during translocation. |journal=J. Cell Biol. |volume=141 |issue= 4 |pages= 887–94 |year= 1998 |pmid= 9585408 |doi=10.1083/jcb.141.4.887
*cite journal | author=Bebök Z, Mazzochi C, King SA, "et al." |title=The mechanism underlying cystic fibrosis transmembrane conductance regulator transport from the endoplasmic reticulum to the proteasome includes Sec61beta and a cytosolic, deglycosylated intermediary. |journal=J. Biol. Chem. |volume=273 |issue= 45 |pages= 29873–8 |year= 1998 |pmid= 9792704 |doi=10.1074/jbc.273.45.29873
*cite journal | author=Greenfield JJ, High S |title=The Sec61 complex is located in both the ER and the ER-Golgi intermediate compartment. |journal=J. Cell. Sci. |volume=112 ( Pt 10) |issue= |pages= 1477–86 |year= 1999 |pmid= 10212142 |doi=
*cite journal | author=Ingley E, Williams JH, Walker CE, "et al." |title=A novel ADP-ribosylation like factor (ARL-6), interacts with the protein-conducting channel SEC61beta subunit. |journal=FEBS Lett. |volume=459 |issue= 1 |pages= 69–74 |year= 1999 |pmid= 10508919 |doi=10.1016/S0014-5793(99)01188-6
*cite journal | author=Yamaguchi A, Hori O, Stern DM, "et al." |title=Stress-associated endoplasmic reticulum protein 1 (SERP1)/Ribosome-associated membrane protein 4 (RAMP4) stabilizes membrane proteins during stress and facilitates subsequent glycosylation. |journal=J. Cell Biol. |volume=147 |issue= 6 |pages= 1195–204 |year= 2000 |pmid= 10601334 |doi=10.1083/jcb.147.6.1195
*cite journal | author=Meyer HA, Grau H, Kraft R, "et al." |title=Mammalian Sec61 is associated with Sec62 and Sec63. |journal=J. Biol. Chem. |volume=275 |issue= 19 |pages= 14550–7 |year= 2000 |pmid= 10799540 |doi=10.1074/jbc.275.19.14550
*cite journal | author=Strausberg RL, Feingold EA, Grouse LH, "et al." |title=Generation and initial analysis of more than 15,000 full-length human and mouse cDNA sequences. |journal=Proc. Natl. Acad. Sci. U.S.A. |volume=99 |issue= 26 |pages= 16899–903 |year= 2003 |pmid= 12477932 |doi= 10.1073/pnas.242603899
*cite journal | author=Humphray SJ, Oliver K, Hunt AR, "et al." |title=DNA sequence and analysis of human chromosome 9. |journal=Nature |volume=429 |issue= 6990 |pages= 369–74 |year= 2004 |pmid= 15164053 |doi= 10.1038/nature02465
*cite journal | author=Gerhard DS, Wagner L, Feingold EA, "et al." |title=The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC). |journal=Genome Res. |volume=14 |issue= 10B |pages= 2121–7 |year= 2004 |pmid= 15489334 |doi= 10.1101/gr.2596504
*cite journal | author=Besemer J, Harant H, Wang S, "et al." |title=Selective inhibition of cotranslational translocation of vascular cell adhesion molecule 1. |journal=Nature |volume=436 |issue= 7048 |pages= 290–3 |year= 2005 |pmid= 16015337 |doi= 10.1038/nature03670
*cite journal | author=Kim JE, Tannenbaum SR, White FM |title=Global phosphoproteome of HT-29 human colon adenocarcinoma cells. |journal=J. Proteome Res. |volume=4 |issue= 4 |pages= 1339–46 |year= 2005 |pmid= 16083285 |doi= 10.1021/pr050048h
*cite journal | author=Olsen JV, Blagoev B, Gnad F, "et al." |title=Global, in vivo, and site-specific phosphorylation dynamics in signaling networks. |journal=Cell |volume=127 |issue= 3 |pages= 635–48 |year= 2006 |pmid= 17081983 |doi= 10.1016/j.cell.2006.09.026
*cite journal | author=Liao HJ, Carpenter G |title=Role of the Sec61 translocon in EGF receptor trafficking to the nucleus and gene expression. |journal=Mol. Biol. Cell |volume=18 |issue= 3 |pages= 1064–72 |year= 2007 |pmid= 17215517 |doi= 10.1091/mbc.E06-09-0802

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