SSR1: Difference between revisions

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{{Underlinked|date=March 2014}}
{{Infobox_gene}}
{{Infobox_gene}}
'''Translocon-associated protein subunit alpha''' is a [[protein]] that in humans is encoded by the ''SSR1'' [[gene]].<ref name="entrez">{{cite web | title = Entrez Gene: SSR1 signal sequence receptor, alpha (translocon-associated protein alpha)| url = https://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=6745| accessdate = }}</ref>
'''Translocon-associated protein subunit alpha''' is a [[protein]] that in humans is encoded by the ''SSR1'' [[gene]].<ref name="entrez">{{cite web | title = Entrez Gene: SSR1 signal sequence receptor, alpha (translocon-associated protein alpha)| url = https://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=6745| accessdate = }}</ref>
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{{PBB_Summary
{{PBB_Summary
| section_title =  
| section_title =  
| summary_text = 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 encoded by this gene and a 22-kD glycoprotein. This gene generates several mRNA species as a result of complex alternative polyadenylation. This gene is unusual in that it utilizes arrays of polyA signal sequences that are exclusively non-canonical.<ref name="entrez"/>
| summary_text = 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]] encoded by this gene and a 22-kD glycoprotein. This gene generates several [[mRNA]] species as a result of complex alternative [[polyadenylation]]. This gene is unusual in that it utilizes arrays of polyA signal sequences that are exclusively non-canonical.<ref name="entrez"/>
}}
}}


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*{{cite journal  | vauthors=Wei ML, Cresswell P |title=HLA-A2 molecules in an antigen-processing mutant cell contain signal sequence-derived peptides. |journal=Nature |volume=356 |issue= 6368 |pages= 443–6 |year= 1992 |pmid= 1557127 |doi= 10.1038/356443a0 }}
*{{cite journal  | vauthors=Wei ML, Cresswell P |title=HLA-A2 molecules in an antigen-processing mutant cell contain signal sequence-derived peptides. |journal=Nature |volume=356 |issue= 6368 |pages= 443–6 |year= 1992 |pmid= 1557127 |doi= 10.1038/356443a0 }}
*{{cite journal  | vauthors=Vogel F, Hartmann E, Görlich D, Rapoport TA |title=Segregation of the signal sequence receptor protein in the rough endoplasmic reticulum membrane. |journal=Eur. J. Cell Biol. |volume=53 |issue= 2 |pages= 197–202 |year= 1991 |pmid= 1964414 |doi=  }}
*{{cite journal  | vauthors=Vogel F, Hartmann E, Görlich D, Rapoport TA |title=Segregation of the signal sequence receptor protein in the rough endoplasmic reticulum membrane. |journal=Eur. J. Cell Biol. |volume=53 |issue= 2 |pages= 197–202 |year= 1991 |pmid= 1964414 |doi=  }}
*{{cite journal  |vauthors=Hartmann E, Görlich D, Kostka S, etal |title=A tetrameric complex of membrane proteins in the endoplasmic reticulum. |journal=Eur. J. Biochem. |volume=214 |issue= 2 |pages= 375–81 |year= 1993 |pmid= 7916687 |doi=10.1111/j.1432-1033.1993.tb17933.x  }}
*{{cite journal  |vauthors=Hartmann E, Görlich D, Kostka S, etal |title=A tetrameric complex of membrane proteins in the endoplasmic reticulum. |journal=Eur. J. Biochem. |volume=214 |issue= 2 |pages= 375–81 |year= 1993 |pmid= 7916687 |doi=10.1111/j.1432-1033.1993.tb17933.x  |url=http://pubman.mpdl.mpg.de/pubman/item/escidoc:1922630/component/escidoc:1922631/1922630.pdf }}
*{{cite journal  | vauthors=Hartmann E, Prehn S |title=The N-terminal region of the alpha-subunit of the TRAP complex has a conserved cluster of negative charges. |journal=FEBS Lett. |volume=349 |issue= 3 |pages= 324–6 |year= 1994 |pmid= 8050590 |doi=10.1016/0014-5793(94)00693-8  }}
*{{cite journal  | vauthors=Hartmann E, Prehn S |title=The N-terminal region of the alpha-subunit of the TRAP complex has a conserved cluster of negative charges. |journal=FEBS Lett. |volume=349 |issue= 3 |pages= 324–6 |year= 1994 |pmid= 8050590 |doi=10.1016/0014-5793(94)00693-8  }}
*{{cite journal  | vauthors=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  | vauthors=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  }}

Latest revision as of 01:39, 25 October 2018

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Identifiers
Aliases
External IDsGeneCards: [1]
Orthologs
SpeciesHumanMouse
Entrez
Ensembl
UniProt
RefSeq (mRNA)

n/a

n/a

RefSeq (protein)

n/a

n/a

Location (UCSC)n/an/a
PubMed searchn/an/a
Wikidata
View/Edit Human

Translocon-associated protein subunit alpha is a protein that in humans is encoded by the SSR1 gene.[1]

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 encoded by this gene and a 22-kD glycoprotein. This gene generates several mRNA species as a result of complex alternative polyadenylation. This gene is unusual in that it utilizes arrays of polyA signal sequences that are exclusively non-canonical.[1]

References

  1. 1.0 1.1 "Entrez Gene: SSR1 signal sequence receptor, alpha (translocon-associated protein alpha)".

Further reading