AP2S1

{{Short description|Protein-coding gene in the species Homo sapiens}}

{{Infobox_gene}}

AP-2 complex subunit sigma is a protein that in humans is encoded by the AP2S1 gene.{{cite journal |vauthors=Winterpacht A, Endele S, Enklaar T, Fuhry M, Zabel B | title = Human CLAPS2 encoding AP17, a small chain of the clathrin-associated protein complex: cDNA cloning and chromosomal assignment to 19q13.2→q13.3 | journal = Cytogenet Cell Genet | volume = 75 | issue = 2–3 | pages = 132–5 |date=Mar 1997 | pmid = 9040778 | doi = 10.1159/000134463}}{{cite journal |vauthors=Holzmann K, Poltl A, Sauermann G | title = A novel spliced transcript of human CLAPS2 encoding a protein alternative to clathrin adaptor protein AP17 | journal = Gene | volume = 220 | issue = 1–2 | pages = 39–44 |date=Nov 1998 | pmid = 9767099 | doi =10.1016/S0378-1119(98)00406-5 }}{{cite web | title = Entrez Gene: AP2S1 adaptor-related protein complex 2, sigma 1 subunit| url = https://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=1175}}

One of two major clathrin-associated adaptor complexes, AP-2, is a heterotetramer which is associated with the plasma membrane. This complex is composed of two large chains, a medium chain, and a small chain. This gene encodes the small chain of this complex. Alternative splicing has been observed in this gene and results in two known transcripts.

References

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Further reading

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  • {{cite journal |vauthors=Pearse BM, Smith CJ, Owen DJ |title=Clathrin coat construction in endocytosis |journal=Curr. Opin. Struct. Biol. |volume=10 |issue= 2 |pages= 220–8 |year= 2000 |pmid= 10753805 |doi=10.1016/S0959-440X(00)00071-3 }}
  • {{cite journal |vauthors=Ewing RM, Chu P, Elisma F |title=Large-scale mapping of human protein–protein interactions by mass spectrometry |journal=Mol. Syst. Biol. |volume=3 |issue= 1|pages= 89 |year= 2007 |pmid= 17353931 |doi= 10.1038/msb4100134 | pmc=1847948 |display-authors=etal}}
  • {{cite journal |vauthors=Byland R, Vance PJ, Hoxie JA, Marsh M |title=A Conserved Dileucine Motif Mediates Clathrin and AP-2–dependent Endocytosis of the HIV-1 Envelope Protein |journal=Mol. Biol. Cell |volume=18 |issue= 2 |pages= 414–25 |year= 2007 |pmid= 17108326 |doi= 10.1091/mbc.E06-06-0535 | pmc=1783771 }}
  • {{cite journal |vauthors=Rual JF, Venkatesan K, Hao T |title=Towards a proteome-scale map of the human protein-protein interaction network |journal=Nature |volume=437 |issue= 7062 |pages= 1173–8 |year= 2005 |pmid= 16189514 |doi= 10.1038/nature04209 |display-authors=etal |bibcode=2005Natur.437.1173R|s2cid=4427026 }}
  • {{cite journal |vauthors=Batonick M, Favre M, Boge M |title=Interaction of HIV-1 Gag with the clathrin-associated adaptor AP-2 |journal=Virology |volume=342 |issue= 2 |pages= 190–200 |year= 2006 |pmid= 16139856 |doi= 10.1016/j.virol.2005.08.001 |display-authors=etal|doi-access=free }}
  • {{cite journal |vauthors=Gerhard DS, Wagner L, Feingold EA |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 | pmc=528928 |display-authors=etal}}
  • {{cite journal |vauthors=Vendeville A, Rayne F, Bonhoure A |title=HIV-1 Tat Enters T Cells Using Coated Pits before Translocating from Acidified Endosomes and Eliciting Biological Responses |journal=Mol. Biol. Cell |volume=15 |issue= 5 |pages= 2347–60 |year= 2005 |pmid= 15020715 |doi= 10.1091/mbc.E03-12-0921 | pmc=404028 |display-authors=etal}}
  • {{cite journal |vauthors=Strausberg RL, Feingold EA, Grouse LH |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 | pmc=139241 |display-authors=etal |bibcode=2002PNAS...9916899M|doi-access=free }}
  • {{cite journal |vauthors=Collins BM, McCoy AJ, Kent HM |title=Molecular architecture and functional model of the endocytic AP2 complex |journal=Cell |volume=109 |issue= 4 |pages= 523–35 |year= 2002 |pmid= 12086608 |doi=10.1016/S0092-8674(02)00735-3 |s2cid=483953 |display-authors=etal|doi-access=free }}
  • {{cite journal |vauthors=Berlioz-Torrent C, Shacklett BL, Erdtmann L |title=Interactions of the Cytoplasmic Domains of Human and Simian Retroviral Transmembrane Proteins with Components of the Clathrin Adaptor Complexes Modulate Intracellular and Cell Surface Expression of Envelope Glycoproteins |journal=J. Virol. |volume=73 |issue= 2 |pages= 1350–61 |year= 1999 |pmid= 9882340 |doi= 10.1128/JVI.73.2.1350-1361.1999| pmc=103959 |display-authors=etal}}
  • {{cite journal |vauthors=Page LJ, Robinson MS |title=Targeting signals and subunit interactions in coated vesicle adaptor complexes |journal=J. Cell Biol. |volume=131 |issue= 3 |pages= 619–30 |year= 1995 |pmid= 7593184 |doi=10.1083/jcb.131.3.619 | pmc=2120623 }}
  • {{cite journal |vauthors=Kirchhausen T, Nathanson KL, Matsui W |title=Structural and functional division into two domains of the large (100- to 115-kDa) chains of the clathrin-associated protein complex AP-2 |journal=Proc. Natl. Acad. Sci. U.S.A. |volume=86 |issue= 8 |pages= 2612–6 |year= 1989 |pmid= 2495531 |doi=10.1073/pnas.86.8.2612 | pmc=286967 |bibcode=1989PNAS...86.2612K |display-authors=etal|doi-access=free }}
  • {{cite journal |vauthors=Kirchhausen T, Davis AC, Frucht S |title=AP17 and AP19, the mammalian small chains of the clathrin-associated protein complexes show homology to Yap17p, their putative homolog in yeast |journal=J. Biol. Chem. |volume=266 |issue= 17 |pages= 11153–7 |year= 1991 |doi=10.1016/S0021-9258(18)99141-6 |pmid= 2040623 |display-authors=etal|doi-access=free }}

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