AP2B1
entrez
163
canonical
uniprot
P63010
canonical
ensembl
ENSG00000006125
resolver
ensp
ENSP00000478115
resolver
ensp
ENSP00000478471
resolver
ensp
ENSP00000479691
resolver
ensp
ENSP00000482315
resolver
ensp
ENSP00000482835
resolver
ensp
ENSP00000483185
resolver
ensp
ENSP00000549078
resolver
ensp
ENSP00000549080
resolver
ensp
ENSP00000549084
resolver
ensp
ENSP00000608815
resolver
genesymbol
AP2B1
resolver
genesymbol_syn
ADTB2
resolver
genesymbol_syn
CLAPB1
resolver
hgnc
HGNC:563
resolver
uniprot
A0A140VJE8
resolver
uniprot
A6NJP3
resolver
uniprot
P21851
resolver
uniprot
Q7Z451
resolver
uniprot
Q96EL6
resolver
uniprot
Q96J19
resolver
uniprot_entry
A0A140VJE8_HUMAN
resolver
uniprot_entry
AP2B1_HUMAN
resolver
uniprot_entry
Q96EL6_HUMAN
resolver
uniprot_sec
A6NJP3
resolver
uniprot_sec
P21851
resolver
uniprot_sec
Q7Z451
resolver
uniprot_sec
Q96J19
resolver
amino_acid_sequence
MTDSKYFTTNKKGEIFELKAELNNEKKEKRKEAVKKVIAAMTVGKDVSSLFPDVVNCMQTDNLELKKLVYLYLMNYAKSQPDMAIMAVNSFVKDCEDPNPLIRALAVRTMGCIRVDKITEYLCEPLRKCLKDEDPYVRKTAAVCVAKLHDINAQMVEDQGFLDSLRDLIADSNPMVVANAVAALSEISESHPNSNLLDLNPQNINKLLTALNECTEWGQIFILDCLSNYNPKDDREAQSICERVTPRLSHANSAVVLSAVKVLMKFLELLPKDSDYYNMLLKKLAPPLVTLLSGEPEVQYVALRNINLIVQKRPEILKQEIKVFFVKYNDPIYVKLEKLDIMIRLASQANIAQVLAELKEYATEVDVDFVRKAVRAIGRCAIKVEQSAERCVSTLLDLIQTKVNYVVQEAIVVIRDIFRKYPNKYESIIATLCENLDSLDEPDARAAMIWIVGEYAERIDNADELLESFLEGFHDESTQVQLTLLTAIVKLFLKKPSETQELVQQVLSLATQDSDNPDLRDRGYIYWRLLSTDPVTAKEVVLSEKPLISEETDLIEPTLLDELICHIGSLASVYHKPPNAFVEGSHGIHRKHLPIHHGSTDAGDSPVGTTTATNLEQPQVIPSQGDLLGDLLNLDLGPPVNVPQVSSMQMGAVDLLGGGLDSLVGQSFIPSSVPATFAPSPTPAVVSSGLNDLFELSTGIGMAPGGYVAPKAVWLPAVKAKGLEISGTFTHRQGHIYMEMNFTNKALQHMTDFAIQFNKNSFGVIPSTPLAIHTPLMPNQSIDVSLPLNTLGPVMKMEPLNNLQVAVKNNIDVFYFSCLIPLNVLFVEDGKMERQVFLATWKDIPNENELQFQIKECHLNADTVSSKLQNNNVYTIAKRNVEGQDMLYQSLKLTNGIWILAELRIQPGNPNYTLSLKCRAPEVSQYIYQVYDSILKN
uniprot
proteins
function
FUNCTION: Component of the adaptor protein complex 2 (AP-2). Adaptor protein complexes function in protein transport via transport vesicles in different membrane traffic pathways. Adaptor protein complexes are vesicle coat components and appear to be involved in cargo selection and vesicle formation. AP-2 is involved in clathrin-dependent endocytosis in which cargo proteins are incorporated into vesicles surrounded by clathrin (clathrin-coated vesicles, CCVs) which are destined for fusion with the early endosome. The clathrin lattice serves as a mechanical scaffold but is itself unable to bind directly to membrane components. Clathrin-associated adaptor protein (AP) complexes which can bind directly to both the clathrin lattice and to the lipid and protein components of membranes are considered to be the major clathrin adaptors contributing the CCV formation. AP-2 also serves as a cargo receptor to selectively sort the membrane proteins involved in receptor-mediated endocytosis. AP-2 seems to play a role in the recycling of synaptic vesicle membranes from the presynaptic surface. AP-2 recognizes Y-X-X-[FILMV] (Y-X-X-Phi) and [ED]-X-X-X-L-[LI] endocytosis signal motifs within the cytosolic tails of transmembrane cargo molecules. AP-2 may also play a role in maintaining normal post-endocytic trafficking through the ARF6-regulated, non-clathrin pathway. During long-term potentiation in hippocampal neurons, AP-2 is responsible for the endocytosis of ADAM10 (PubMed:23676497). The AP-2 beta subunit acts via its C-terminal appendage domain as a scaffolding platform for endocytic accessory proteins; at least some clathrin-associated sorting proteins (CLASPs) are recognized by their [DE]-X(1,2)-F-X-X-[FL]-X-X-X-R motif. The AP-2 beta subunit binds to clathrin heavy chain, promoting clathrin lattice assembly; clathrin displaces at least some CLASPs from AP2B1 which probably then can be positioned for further coat assembly. {ECO:0000269|PubMed:14745134, ECO:0000269|PubMed:14985334, ECO:0000269|PubMed:15473838, ECO:0000269|PubMed:19033387, ECO:0000269|PubMed:23676497}.
uniprot
proteins
mass_dalton
104553
uniprot
proteins
mutagenesis
MUTAGEN 815; /note="Y->A: Strongly reduces interaction with SNAP91, EPS15, AMPH and BIN1 and clathrin heavy chain."; /evidence="ECO:0000269|PubMed:16516836, ECO:0000269|PubMed:16903783"; MUTAGEN 841; /note="W->A: Abolishes interaction with LDLRAP1 and ARRB1. Greatly reduces DENND1B-binding."; /evidence="ECO:0000269|PubMed:15728179, ECO:0000269|PubMed:16516836, ECO:0000269|PubMed:16903783, ECO:0000269|PubMed:20154091"; MUTAGEN 842; /note="K->E: Strongly reduces interaction with ARRB1."; /evidence="ECO:0000269|PubMed:16903783"; MUTAGEN 849; /note="E->A: Strongly reduces interaction with LDLRAP1, ARRB1 and EPN1. No effect on DENND1B-binding."; /evidence="ECO:0000269|PubMed:11777907, ECO:0000269|PubMed:16516836, ECO:0000269|PubMed:20154091"; MUTAGEN 851; /note="Q->A: Strongly reduces interaction with ARRB1."; /evidence="ECO:0000269|PubMed:16903783"; MUTAGEN 879; /note="R->A: No effect on interaction with ARRB1."; /evidence="ECO:0000269|PubMed:10944104, ECO:0000269|PubMed:16903783"; MUTAGEN 879; /note="R->E: Strongly reduces interaction with EPN1. Reduces interaction with SNAP91 and clathrin. No effect on EPS15 binding."; /evidence="ECO:0000269|PubMed:10944104, ECO:0000269|PubMed:16903783"; MUTAGEN 888; /note="Y->V: Strongly reduces interaction with SNAP91, EPN1 and clathrin. No effect on EPS15 binding. Abolishes interaction with ARRB1 and with DENND1B."; /evidence="ECO:0000269|PubMed:10944104, ECO:0000269|PubMed:15728179, ECO:0000269|PubMed:16516836, ECO:0000269|PubMed:16903783, ECO:0000269|PubMed:20154091"; MUTAGEN 902; /note="E->A: Strongly reduces interaction with LDLRAP1 and ARRB1. No effect on DENND1B-binding."; /evidence="ECO:0000269|PubMed:11777907, ECO:0000269|PubMed:16516836, ECO:0000269|PubMed:20154091"; MUTAGEN 917; /note="K->Q: Strongly reduces interaction with LDLRAP1. SNAP91 and clathrin. Reduces interaction with EPN1. No effect on EPS15 binding."; /evidence="ECO:0000269|PubMed:10944104
uniprot
proteins
post_translational_modification
PTM: Phosphorylation at Tyr-737 by SRC occurs at the plasma membrane in clathrin-coated vesicles (CCVs). {ECO:0000269|PubMed:17456551, ECO:0000269|PubMed:18938240}.
uniprot
proteins
protein_family
Adaptor complexes large subunit family
uniprot
proteins
pubmed
10944104
uniprot
proteins
pubmed
11777907
uniprot
proteins
pubmed
12086608
uniprot
proteins
pubmed
12429842
uniprot
proteins
pubmed
14530274
uniprot
proteins
pubmed
14745134
uniprot
proteins
pubmed
14985334
uniprot
proteins
pubmed
15473838
uniprot
proteins
pubmed
15489334
uniprot
proteins
pubmed
15728179
uniprot
proteins
pubmed
15897975
uniprot
proteins
pubmed
16516836
uniprot
proteins
pubmed
16625196
uniprot
proteins
pubmed
16723738
uniprot
proteins
pubmed
16903783
uniprot
proteins
pubmed
17456551
uniprot
proteins
pubmed
17719203
uniprot
proteins
pubmed
18691976
uniprot
proteins
pubmed
18938240
uniprot
proteins
pubmed
19033387
uniprot
proteins
pubmed
19140243
uniprot
proteins
pubmed
19608861
uniprot
proteins
pubmed
1969413
uniprot
proteins
pubmed
20154091
uniprot
proteins
pubmed
21269460
uniprot
proteins
pubmed
22484487
uniprot
proteins
pubmed
22814378
uniprot
proteins
pubmed
23186163
uniprot
proteins
pubmed
23676497
uniprot
proteins
pubmed
24275569
uniprot
proteins
pubmed
25944712
uniprot
proteins
pubmed
27022195
uniprot
proteins
pubmed
29262337
uniprot
proteins
sequence_length
937
uniprot
proteins
subcellular_location
SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:14530274}. Membrane, coated pit {ECO:0000269|PubMed:14530274}; Peripheral membrane protein {ECO:0000269|PubMed:14530274}; Cytoplasmic side {ECO:0000269|PubMed:14530274}. Note=AP-2 appears to be excluded from internalizing CCVs and to disengage from sites of endocytosis seconds before internalization of the nascent CCV.
uniprot
proteins