AP2A2

Protein-coding gene in the species Homo sapiens
AP2A2
Available structures
PDBOrtholog search: PDBe RCSB
List of PDB id codes

1B9K, 1KY6, 1KY7, 1KYD, 1KYF, 1KYU, 1QTP, 1QTS, 1W80, 2JKR, 2JKT, 2VJ0, 3HS8

Identifiers
AliasesAP2A2, ADTAB, CLAPA2, HIP-9, HIP9, HYPJ, adaptor related protein complex 2 alpha 2 subunit, adaptor related protein complex 2 subunit alpha 2
External IDsOMIM: 607242; MGI: 101920; HomoloGene: 5335; GeneCards: AP2A2; OMA:AP2A2 - orthologs
Gene location (Human)
Chromosome 11 (human)
Chr.Chromosome 11 (human)[1]
Chromosome 11 (human)
Genomic location for AP2A2
Genomic location for AP2A2
Band11p15.5Start924,881 bp[1]
End1,012,245 bp[1]
Gene location (Mouse)
Chromosome 7 (mouse)
Chr.Chromosome 7 (mouse)[2]
Chromosome 7 (mouse)
Genomic location for AP2A2
Genomic location for AP2A2
Band7|7 F5Start141,142,086 bp[2]
End141,212,924 bp[2]
RNA expression pattern
Bgee
HumanMouse (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
SpeciesHumanMouse
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 MbChr 7: 141.14 – 141.21 Mb
PubMed search[3][4]
Wikidata
View/Edit HumanView/Edit Mouse

AP-2 complex subunit alpha-2 is a protein that in humans is encoded by the AP2A2 gene.[5][6][7]

Interactions

AP2A2 has been shown to interact with EPN1[8] and SHC1.[9]

References

  1. ^ a b c ENSG00000280759, ENSG00000183020 GRCh38: Ensembl release 89: ENSG00000281385, ENSG00000280759, ENSG00000183020 – Ensembl, May 2017
  2. ^ a b c GRCm38: Ensembl release 89: ENSMUSG00000002957 – Ensembl, May 2017
  3. ^ "Human PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
  4. ^ "Mouse PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
  5. ^ Faber PW, Barnes GT, Srinidhi J, Chen J, Gusella JF, MacDonald ME (Sep 1998). "Huntingtin interacts with a family of WW domain proteins". Human Molecular Genetics. 7 (9): 1463–74. doi:10.1093/hmg/7.9.1463. PMID 9700202.
  6. ^ Robinson MS (Mar 1989). "Cloning of cDNAs encoding two related 100-kD coated vesicle proteins (alpha-adaptins)". The Journal of Cell Biology. 108 (3): 833–42. doi:10.1083/jcb.108.3.833. PMC 2115374. PMID 2564002.
  7. ^ "Entrez Gene: AP2A2 adaptor-related protein complex 2, alpha 2 subunit".
  8. ^ 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.
  9. ^ 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.

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

  • v
  • t
  • e
  • 1b9k: ALPHA-ADAPTIN APPENDAGE DOMAIN, FROM CLATHRIN ADAPTOR AP2
    1b9k: ALPHA-ADAPTIN APPENDAGE DOMAIN, FROM CLATHRIN ADAPTOR AP2
  • 1gw5:
    1gw5:
  • 1ky6: AP-2 CLATHRIN ADAPTOR ALPHA-APPENDAGE IN COMPLEX WITH EPSIN DPW PEPTIDE
    1ky6: AP-2 CLATHRIN ADAPTOR ALPHA-APPENDAGE IN COMPLEX WITH EPSIN DPW PEPTIDE
  • 1ky7: THE AP-2 CLATHRIN ADAPTOR ALPHA-APPENDAGE IN COMPLEX WITH AMPHIPHYSIN FXDXF
    1ky7: THE AP-2 CLATHRIN ADAPTOR ALPHA-APPENDAGE IN COMPLEX WITH AMPHIPHYSIN FXDXF
  • 1kyd: AP-2 CLATHRIN ADAPTOR ALPHA-APPENDAGE IN COMPLEX WITH EPSIN DPW PEPTIDE
    1kyd: AP-2 CLATHRIN ADAPTOR ALPHA-APPENDAGE IN COMPLEX WITH EPSIN DPW PEPTIDE
  • 1kyf: AP-2 CLATHRIN ADAPTOR ALPHA-APPENDAGE IN COMPLEX WITH EPS15 DPF PEPTIDE
    1kyf: AP-2 CLATHRIN ADAPTOR ALPHA-APPENDAGE IN COMPLEX WITH EPS15 DPF PEPTIDE
  • 1kyu: AP-2 CLATHRIN ADAPTOR ALPHA-APPENDAGE IN COMPLEX WITH EPS15 DPF PEPTIDE
    1kyu: AP-2 CLATHRIN ADAPTOR ALPHA-APPENDAGE IN COMPLEX WITH EPS15 DPF PEPTIDE
  • 1qtp: CRYSTAL STRUCTURE OF THE AP-2 CLATHRIN ADAPTOR ALPHA-APPENDAGE
    1qtp: CRYSTAL STRUCTURE OF THE AP-2 CLATHRIN ADAPTOR ALPHA-APPENDAGE
  • 1qts: CRYSTAL STRUCTURE OF THE AP-2 CLATHRIN ADAPTOR ALPHA-APPENDAGE
    1qts: CRYSTAL STRUCTURE OF THE AP-2 CLATHRIN ADAPTOR ALPHA-APPENDAGE
  • 1w80: CRYSTAL STRUCTURE OF THE ALPHA-ADAPTIN APPENDAGE DOMAIN, FROM THE AP2 ADAPTOR COMPLEX, BOUND TO 2 PEPTIDES FROM SYNAPTOJANIN170
    1w80: CRYSTAL STRUCTURE OF THE ALPHA-ADAPTIN APPENDAGE DOMAIN, FROM THE AP2 ADAPTOR COMPLEX, BOUND TO 2 PEPTIDES FROM SYNAPTOJANIN170


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