AP2A2

AP-2 complex subunit alpha-2 is a protein that in humans is encoded by the AP2A2 gene.

AP2A2
Available structures PDB Ortholog search: PDBe RCSB List of PDB id codes 1B9K, 1KY6, 1KY7, 1KYD, 1KYF, 1KYU, 1QTP, 1QTS, 1W80, 2JKR, 2JKT, 2VJ0, 3HS8
Identifiers
Aliases	AP2A2, ADTAB, CLAPA2, HIP-9, HIP9, HYPJ, adaptor related protein complex 2 alpha 2 subunit, adaptor related protein complex 2 subunit alpha 2
External IDs	OMIM: 607242 MGI: 101920 HomoloGene: 5335 GeneCards: AP2A2
Gene location (Human) Chr. Chromosome 11 (human) Band 11p15.5 Start 924,881 bp End 1,012,245 bp
Gene location (Mouse) Chr. Chromosome 7 (mouse) Band 7|7 F5 Start 141,142,086 bp End 141,212,924 bp
RNA expression pattern Bgee Human Mouse (ortholog) Top expressed in spleen superior frontal gyrus sural nerve subcutaneous adipose tissue prefrontal cortex canal of the cervix pituitary gland ganglionic eminence upper lobe of left lung kidney Top expressed in entorhinal cortex medullary collecting duct superior frontal gyrus cerebellar cortex habenula hippocampus proper supraoptic nucleus Region I of hippocampus proper amygdala dorsomedial hypothalamic nucleus More reference expression data BioGPS More reference expression data
Gene ontology Molecular function clathrin adaptor activity protein binding protein kinase binding lipid binding protein domain specific binding disordered domain specific binding molecular function Cellular component endocytic vesicle membrane cytosol clathrin-coated endocytic vesicle membrane membrane plasma membrane endolysosome membrane membrane coat clathrin-coated pit AP-2 adaptor complex clathrin adaptor complex secretory granule membrane cytoplasmic vesicle ficolin-1-rich granule membrane clathrin-coated endocytic vesicle Biological process endocytosis antigen processing and presentation of exogenous peptide antigen via MHC class II ephrin receptor signaling pathway mitigation of host defenses by virus clathrin-dependent endocytosis protein transport intracellular protein transport vesicle-mediated transport microtubule-based movement Wnt signaling pathway, planar cell polarity pathway neutrophil degranulation membrane organization low-density lipoprotein particle receptor catabolic process low-density lipoprotein particle clearance transport Sources:Amigo / QuickGO
Orthologs Species Human Mouse Entrez 161 11772 Ensembl ENSG00000281385 ENSG00000280759 ENSG00000183020 ENSMUSG00000002957 UniProt O94973 P17427 RefSeq (mRNA) NM_001242837 NM_012305 NM_007459 NM_001357068 RefSeq (protein) NP_001229766 NP_036437 NP_031485 NP_001343997 Location (UCSC) Chr 11: 0.92 – 1.01 Mb Chr 7: 141.14 – 141.21 Mb PubMed search
Wikidata
View/Edit Human View/Edit Mouse

Interactions

AP2A2 has been shown to interact with EPN1 and SHC1.

Further reading

• Kirchhausen T (2000). "Clathrin". Annual Review of Biochemistry. 69: 699–727. doi:10.1146/annurev.biochem.69.1.699. PMID 10966473.
• Nakajima D, Okazaki N, Yamakawa H, Kikuno R, Ohara O, Nagase T (Jun 2002). "Construction of expression-ready cDNA clones for KIAA genes: manual curation of 330 KIAA cDNA clones". DNA Research. 9 (3): 99–106. CiteSeerX 10.1.1.500.923. doi:10.1093/dnares/9.3.99. PMID 12168954.
• Maruyama K, Sugano S (Jan 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.
• David C, McPherson PS, Mundigl O, de Camilli P (Jan 1996). "A role of amphiphysin in synaptic vesicle endocytosis suggested by its binding to dynamin in nerve terminals". Proceedings of the National Academy of Sciences of the United States of America. 93 (1): 331–5. Bibcode:1996PNAS...93..331D. doi:10.1073/pnas.93.1.331. PMC 40232. PMID 8552632.
• Okabayashi Y, Sugimoto Y, Totty NF, Hsuan J, Kido Y, Sakaguchi K, Gout I, Waterfield MD, Kasuga M (Mar 1996). "Interaction of Shc with adaptor protein adaptins". The Journal of Biological Chemistry. 271 (9): 5265–9. doi:10.1074/jbc.271.9.5265. PMID 8617812.
• Benmerah A, Bégue B, Dautry-Varsat A, Cerf-Bensussan N (May 1996). "The ear of alpha-adaptin interacts with the COOH-terminal domain of the Eps 15 protein". The Journal of Biological Chemistry. 271 (20): 12111–6. doi:10.1074/jbc.271.20.12111. PMID 8662627.
• van Delft S, Schumacher C, Hage W, Verkleij AJ, van Bergen en Henegouwen PM (Feb 1997). "Association and colocalization of Eps15 with adaptor protein-2 and clathrin". The Journal of Cell Biology. 136 (4): 811–21. doi:10.1083/jcb.136.4.811. PMC 2132490. PMID 9049247.
• Ramjaun AR, Micheva KD, Bouchelet I, McPherson PS (Jun 1997). "Identification and characterization of a nerve terminal-enriched amphiphysin isoform". The Journal of Biological Chemistry. 272 (26): 16700–6. doi:10.1074/jbc.272.26.16700. PMID 9195986.
• Suzuki Y, Yoshitomo-Nakagawa K, Maruyama K, Suyama A, Sugano S (Oct 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.
• Chen H, Fre S, Slepnev VI, Capua MR, Takei K, Butler MH, Di Fiore PP, De Camilli P (Aug 1998). "Epsin is an EH-domain-binding protein implicated in clathrin-mediated endocytosis". Nature. 394 (6695): 793–7. Bibcode:1998Natur.394..793C. doi:10.1038/29555. PMID 9723620. S2CID 4430975.
• Berlioz-Torrent C, Shacklett BL, Erdtmann L, Delamarre L, Bouchaert I, Sonigo P, Dokhelar MC, Benarous R (Feb 1999). "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 of Virology. 73 (2): 1350–61. doi:10.1128/JVI.73.2.1350-1361.1999. PMC 103959. PMID 9882340.
• Nagase T, Ishikawa K, Suyama M, Kikuno R, Hirosawa M, Miyajima N, Tanaka A, Kotani H, Nomura N, Ohara O (Dec 1998). "Prediction of the coding sequences of unidentified human genes. XII. The complete sequences of 100 new cDNA clones from brain which code for large proteins in vitro". DNA Research. 5 (6): 355–64. doi:10.1093/dnares/5.6.355. PMID 10048485.
• Traub LM, Downs MA, Westrich JL, Fremont DH (Aug 1999). "Crystal structure of the alpha appendage of AP-2 reveals a recruitment platform for clathrin-coat assembly". Proceedings of the National Academy of Sciences of the United States of America. 96 (16): 8907–12. Bibcode:1999PNAS...96.8907T. doi:10.1073/pnas.96.16.8907. PMC 17706. PMID 10430869.
• Page LJ, Sowerby PJ, Lui WW, Robinson MS (Sep 1999). "Gamma-synergin: an EH domain-containing protein that interacts with gamma-adaptin". The Journal of Cell Biology. 146 (5): 993–1004. doi:10.1083/jcb.146.5.993. PMC 2169493. PMID 10477754.
• Kim ST, Lim DS, Canman CE, Kastan MB (Dec 1999). "Substrate specificities and identification of putative substrates of ATM kinase family members". The Journal of Biological Chemistry. 274 (53): 37538–43. doi:10.1074/jbc.274.53.37538. PMID 10608806.
• Slepnev VI, Ochoa GC, Butler MH, De Camilli P (Jun 2000). "Tandem arrangement of the clathrin and AP-2 binding domains in amphiphysin 1 and disruption of clathrin coat function by amphiphysin fragments comprising these sites". The Journal of Biological Chemistry. 275 (23): 17583–9. doi:10.1074/jbc.M910430199. PMID 10748223.
• Jullien-Flores V, Mahé Y, Mirey G, Leprince C, Meunier-Bisceuil B, Sorkin A, Camonis JH (Aug 2000). "RLIP76, an effector of the GTPase Ral, interacts with the AP2 complex: involvement of the Ral pathway in receptor endocytosis" (PDF). Journal of Cell Science. 113 (16): 2837–44. doi:10.1242/jcs.113.16.2837. PMID 10910768.

External links

• Human AP2A2 genome location and AP2A2 gene details page in the UCSC Genome Browser.