Features Interactions Isoform Disease Linear motifs Fingerprint Network All partners

AP2B1_HUMAN

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). 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. [View more on UniProt]

0100200300400500600700800900
Transmembrane
Phase separation
ELM
Phosphorylation
PFAM
Coiled coil
Anchor
Disordered
Interacting regions
Sequence
LOADING 73%

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0100200300400500600700800900
AP2B1_HUMAN
LOADING 67%
01002003004005006007008009001,0001,1001,200
AP2B1_HUMAN
LOADING 67%
02004006008001,0001,2001,4001,600
AP2B1_HUMAN
LOADING 67%
0100200300400500600700800900
AP2B1_HUMAN
LOADING 67%
0100200300400500600700800900
AP2B1_HUMAN
LOADING 67%
0100200300400500600700800900
AP2B1_HUMAN
LOADING 67%
0100200300400500600700800900
AP2B1_HUMAN
LOADING 67%
0100200300400500600700800900
AP2B1_HUMAN
LOADING 67%
0100200300400500600700800900
AP2B1_HUMAN
LOADING 67%
0100200300400500600700800900
AP2B1_HUMAN
LOADING 67%
Download full PS network for entry.
0100200300400500600700800900
Interacting regions
Canonical [AP2B1_HUMAN]
Isoform [K7EJ01] alignment
Isoform [K7EJX1] alignment
Isoform [K7EKZ5] alignment
Isoform [K7EMN7] alignment
Isoform [K7EN71] alignment
Isoform [K7ERB2] alignment
Isoform [A0A087X253] alignment
Isoform [A0A087WU93] alignment
Isoform [A0A087WXS3] alignment
Isoform [A0A087WYD1] alignment
Isoform [A0A087WZQ6] alignment
Isoform [P63010-2] alignment
Isoform [P63010-3] alignment
LOADING 28%

No data found.

No annotated instance was found. To search for linear motifs, use the ELM prediction server.

Molecular function

Biological process

Disease

No data found.

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