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Adaptor-related protein complex 2, beta 1 subunit
Protein AP2B1 PDB 1e42.png
PDB rendering based on 1e42.
Available structures
PDB Ortholog search: PDBe, RCSB
Symbols AP2B1 ; ADTB2; AP105B; AP2-BETA; CLAPB1
External IDs OMIM601025 MGI1919020 HomoloGene68176 GeneCards: AP2B1 Gene
RNA expression pattern
PBB GE AP2B1 200615 s at tn.png
More reference expression data
Species Human Mouse
Entrez 163 71770
Ensembl ENSG00000006125 ENSMUSG00000035152
UniProt P63010 Q9DBG3
RefSeq (mRNA) NM_001030006 NM_001035854
RefSeq (protein) NP_001025177 NP_001030931
Location (UCSC) Chr 17:
33.91 – 34.05 Mb
Chr 11:
83.3 – 83.41 Mb
PubMed search [1] [2]

AP-2 complex subunit beta is a protein that in humans is encoded by the AP2B1 gene.[1][2][3]

The protein encoded by this gene is one of two large chain components of the assembly protein complex 2, which serves to link clathrin to receptors in coated vesicles. The encoded protein is found on the cytoplasmic face of coated vesicles in the plasma membrane. Two transcript variants encoding different isoforms have been found for this gene.[3]


AP2B1 has been shown to interact with TGF beta receptor 2,[4] AP1M2,[5] BUB1B,[6] LDLRAP1[5][7] and Arrestin beta 2.[8][9]


  1. ^ Gallusser A, Kirchhausen T (January 1994). "The beta 1 and beta 2 subunits of the AP complexes are the clathrin coat assembly components". EMBO J 12 (13): 5237–44. PMC 413789. PMID 8262066. 
  2. ^ Druck T, Gu Y, Prabhala G, Cannizzaro LA, Park SH, Huebner K, Keen JH (April 1996). "Chromosome localization of human genes for clathrin adaptor polypeptides AP2 beta and AP50 and the clathrin-binding protein, VCP". Genomics 30 (1): 94–7. doi:10.1006/geno.1995.0016. PMID 8595912. 
  3. ^ a b "Entrez Gene: AP2B1 adaptor-related protein complex 2, beta 1 subunit". 
  4. ^ Yao, Diying; Ehrlich Marcelo; Henis Yoav I; Leof Edward B (November 2002). "Transforming growth factor-beta receptors interact with AP2 by direct binding to beta2 subunit". Mol. Biol. Cell (United States) 13 (11): 4001–12. doi:10.1091/mbc.02-07-0104. ISSN 1059-1524. PMC 133610. PMID 12429842. 
  5. ^ a b Rual, Jean-François; Venkatesan Kavitha, Hao Tong, Hirozane-Kishikawa Tomoko, Dricot Amélie, Li Ning, Berriz Gabriel F, Gibbons Francis D, Dreze Matija, Ayivi-Guedehoussou Nono, Klitgord Niels, Simon Christophe, Boxem Mike, Milstein Stuart, Rosenberg Jennifer, Goldberg Debra S, Zhang Lan V, Wong Sharyl L, Franklin Giovanni, Li Siming, Albala Joanna S, Lim Janghoo, Fraughton Carlene, Llamosas Estelle, Cevik Sebiha, Bex Camille, Lamesch Philippe, Sikorski Robert S, Vandenhaute Jean, Zoghbi Huda Y, Smolyar Alex, Bosak Stephanie, Sequerra Reynaldo, Doucette-Stamm Lynn, Cusick Michael E, Hill David E, Roth Frederick P, Vidal Marc (October 2005). "Towards a proteome-scale map of the human protein-protein interaction network". Nature (England) 437 (7062): 1173–8. doi:10.1038/nature04209. PMID 16189514. 
  6. ^ Cayrol, Corinne; Cougoule Céline; Wright Michel (November 2002). "The beta2-adaptin clathrin adaptor interacts with the mitotic checkpoint kinase BubR1". Biochem. Biophys. Res. Commun. (United States) 298 (5): 720–30. doi:10.1016/S0006-291X(02)02522-6. ISSN 0006-291X. PMID 12419313. 
  7. ^ He, Guocheng; Gupta Sarita; Yi Ming; Michaely Peter; Hobbs Helen H; Cohen Jonathan C (November 2002). "ARH is a modular adaptor protein that interacts with the LDL receptor, clathrin, and AP-2". J. Biol. Chem. (United States) 277 (46): 44044–9. doi:10.1074/jbc.M208539200. ISSN 0021-9258. PMID 12221107. 
  8. ^ Laporte, S A; Oakley R H; Zhang J; Holt J A; Ferguson S S; Caron M G; Barak L S (March 1999). "The beta2-adrenergic receptor/betaarrestin complex recruits the clathrin adaptor AP-2 during endocytosis". Proc. Natl. Acad. Sci. U.S.A. (UNITED STATES) 96 (7): 3712–7. doi:10.1073/pnas.96.7.3712. ISSN 0027-8424. PMC 22359. PMID 10097102. 
  9. ^ Kim, You-Me; Benovic Jeffrey L (August 2002). "Differential roles of arrestin-2 interaction with clathrin and adaptor protein 2 in G protein-coupled receptor trafficking". J. Biol. Chem. (United States) 277 (34): 30760–8. doi:10.1074/jbc.M204528200. ISSN 0021-9258. PMID 12070169. 

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