Ap2a2
entrez
11772
canonical
uniprot
P17427
canonical
ensembl
ENSMUSG00000002957
resolver
ensp
ENSMUSP00000003038
resolver
ensp
ENSMUSP00000245029
resolver
enst
ENSMUST00000003038
resolver
genesymbol
Ap2a2
resolver
genesymbol_syn
Adtab
resolver
genesymbol_syn
mKIAA0899
resolver
uniprot
Q69ZW4
resolver
uniprot
Q6PEE6
resolver
uniprot
Q8C2J5
resolver
uniprot
Q921V0
resolver
uniprot_entry
AP2A2_MOUSE
resolver
uniprot_entry
Q69ZW4_MOUSE
resolver
uniprot_entry
Q6PEE6_MOUSE
resolver
uniprot_sec
Q8C2J5
resolver
uniprot_sec
Q921V0
resolver
amino_acid_sequence
MPAVSKGDGMRGLAVFISDIRNCKSKEAEIKRINKELANIRSKFKGDKALDGYSKKKYVCKLLFIFLLGHDIDFGHMEAVNLLSSNRYTEKQIGYLFISVLVNSNSELIRLINNAIKNDLASRNPTFMGLALHCIANVGSREMAEAFAGEIPKILVAGDTMDSVKQSAALCLLRLYRTSPDLVPMGDWTSRVVHLLNDQHLGVVTAATSLITTLAQKNPEEFKTSVSLAVSRLSRIVTSASTDLQDYTYYFVPAPWLSVKLLRLLQCYPPPDPAVRGRLTECLETILNKAQEPPKSKKVQHSNAKNAVLFEAISLIIHHDSEPNLLVRACNQLGQFLQHRETNLRYLALESMCTLASSEFSHEAVKTHIETVINALKTERDVSVRQRAVDLLYAMCDRSNAQQIVAEMLSYLETADYSIREEIVLKVAILAEKYAVDYTWYVDTILNLIRIAGDYVSEEVWYRVIQIVINRDDVQGYAAKTVFEALQAPACHENLVKVGGYILGEFGNLIAGDPRSSPLIQFNLLHSKFHLCSVPTRALLLSTYIKFVNLFPEVKATIQDVLRSDSQLKNADVELQQRAVEYLRLSTVASTDILATVLEEMPPFPERESSILAKLKKKKGPSTVTDLEETKRERSIDVNGGPEPVPASTSAASTPSPSADLLGLGAVPPAPTGPPPSSGGGLLVDVFSDSASAVAPLAPGSEDNFARFVCKNNGVLFENQLLQIGLKSEFRQNLGRMFIFYGNKTSTQFLNFTPTLICADDLQTNLNLQTKPVDPTVDGGAQVQQVVNIECISDFTEAPVLNIQFRYGGTFQNVSVKLPITLNKFFQPTEMASQDFFQRWKQLSNPQQEVQNIFKAKHPMDTEITKAKIIGFGSALLEEVDPNPANFVGAGIIHTKTTQIGCLLRLEPNLQAQMYRLTLRTSKDTVSQRLCELLSEQF
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 alpha subunit binds polyphosphoinositide-containing lipids, positioning AP-2 on the membrane. The AP-2 alpha subunit acts via its C-terminal appendage domain as a scaffolding platform for endocytic accessory proteins. The AP-2 alpha and AP-2 sigma subunits are thought to contribute to the recognition of the [ED]-X-X-X-L-[LI] motif. {ECO:0000269|PubMed:10459011, ECO:0000269|PubMed:14745134, ECO:0000269|PubMed:15473838, ECO:0000269|PubMed:23676497}.
uniprot
proteins
mass_dalton
104017
uniprot
proteins
mutagenesis
MUTAGEN 21; /note="R->E: Reduces interaction with CD4 endocytosis signal motif; when associated with AP2S1 S-15."; /evidence="ECO:0000269|PubMed:19140243"; MUTAGEN 31; /note="K->Q: Reduces phosphatidylinositol binding."; /evidence="ECO:0000269|PubMed:10459011"; MUTAGEN 32; /note="R->Q: Reduces phosphatidylinositol binding."; /evidence="ECO:0000269|PubMed:10459011"; MUTAGEN 35; /note="K->Q: Reduces phosphatidylinositol binding."; /evidence="ECO:0000269|PubMed:10459011"; MUTAGEN 45; /note="K->Q: Reduces phosphatidylinositol binding."; /evidence="ECO:0000269|PubMed:10459011"; MUTAGEN 55; /note="K->Q: Strongly reduces phosphatidylinositol binding. Abolishes phosphatidylinositol binding; when associated with Q-56 and Q-57."; /evidence="ECO:0000269|PubMed:10459011"; MUTAGEN 56; /note="K->E: Strongly reduces phosphatidylinositol binding."; /evidence="ECO:0000269|PubMed:10459011"; MUTAGEN 56; /note="K->Q: Strongly reduces phosphatidylinositol binding. Abolishes phosphatidylinositol binding; when associated with Q-55 and Q-57."; /evidence="ECO:0000269|PubMed:10459011"; MUTAGEN 57; /note="K->Q: Strongly reduces phosphatidylinositol binding. Abolishes phosphatidylinositol binding; when associated with Q-55 and Q-56."; /evidence="ECO:0000269|PubMed:10459011"; MUTAGEN 61; /note="K->Q: Reduces phosphatidylinositol binding."; /evidence="ECO:0000269|PubMed:10459011"; MUTAGEN 727; /note="K->A: No effect on DENND1A-,DENND1B- nor DENND1C-binding."; MUTAGEN 782; /note="Q->A: Reduces DENND1A- and DENND1C-binding."; /evidence="ECO:0000269|PubMed:20154091"; MUTAGEN 837; /note="F->A: Reduces SNAP91, AMPH and BIN1 binding. Abolishes AMPH and SNAP91 binding; when associated with A-916. Abolishes EPN1 and EPS15 binding; when associated with A-905."; /evidence="ECO:0000269|PubMed:10380931, ECO:0000269|PubMed:10430869"; MUTAGEN 840; /note="W->A: Abolishes AMPH, BIN1, DGKD, EPS15, EPN1, auxilin and SNAP91 binding."; /evidence="ECO:0000269|PubMed:10380931, ECO:0000269|PubMed:17880279"; MUTAGEN 849; /note="E->A: No effect."; /evidence="ECO:0000269|PubMed:10380931"; MUTAGEN 905; /note="R->A: Strongly reduces AMPH, SNAP91, auxilin and BIN1 binding. Abolishes EPN1 and EPS15 binding; when associated with A-837."; /evidence="ECO:0000269|PubMed:10380931, ECO:0000269|PubMed:10430869"; MUTAGEN 907; /note="E->A: Strongly reduces AMPH, SNAP91 and BIN1 binding. Slightly reduces EPS15 and auxilin binding."; /evidence="ECO:0000269|PubMed:10380931"; MUTAGEN 916; /note="R->A: Strongly reduces AMPH and SNAP91 binding. Abolishes DENND1B-binding; no effect on DENND1A-, nor DENND1C-binding. Abolishes AMPH and SNAP91 binding; when associated with A-837."; /evidence="ECO:0000269|PubMed:10430869, ECO:0000269|PubMed:20154091"; MUTAGEN 920; /note="R->A: Abolishes AMPH and BIN1 binding. Reduces EPS15, SNAP91 and auxilin binding."; /evidence="ECO:0000269|PubMed:10380931
uniprot
proteins
protein_family
Adaptor complexes large subunit family
uniprot
proteins
pubmed
10380931
uniprot
proteins
pubmed
10430869
uniprot
proteins
pubmed
10459011
uniprot
proteins
pubmed
11247302
uniprot
proteins
pubmed
11470803
uniprot
proteins
pubmed
12057195
uniprot
proteins
pubmed
14530274
uniprot
proteins
pubmed
14745134
uniprot
proteins
pubmed
15473838
uniprot
proteins
pubmed
15489334
uniprot
proteins
pubmed
16141072
uniprot
proteins
pubmed
17035303
uniprot
proteins
pubmed
17880279
uniprot
proteins
pubmed
19140243
uniprot
proteins
pubmed
19468303
uniprot
proteins
pubmed
20154091
uniprot
proteins
pubmed
21183079
uniprot
proteins
pubmed
22484487
uniprot
proteins
pubmed
23676497
uniprot
proteins
pubmed
24097348
uniprot
proteins
pubmed
2564002
uniprot
proteins
pubmed
29262337
uniprot
proteins
pubmed
29288152
uniprot
proteins
pubmed
9618202
uniprot
proteins
sequence_length
938
uniprot
proteins
subcellular_location
SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:14530274, ECO:0000269|PubMed:17035303}; Peripheral membrane protein {ECO:0000305}; Cytoplasmic side {ECO:0000305}. Membrane, coated pit {ECO:0000269|PubMed:17035303}; Peripheral membrane protein {ECO:0000305}; Cytoplasmic side {ECO:0000305}. Note=AP-2 appears to be excluded from internalizing CCVs and to disengage from sites of endocytosis seconds before internalization of the nascent CCV. {ECO:0000269|PubMed:17035303}.
uniprot
proteins