Search Results
Overview
| Uniprot ID | P63010 |
|---|---|
| Protein Name | AP-2 complex subunit beta |
| Gene Name | AP2B1 |
| Organism | Homo sapiens |
Kla Sites from experimental identification
| Position | Flanking peptide |
|---|---|
| 117 | MGCIRVDKITEYLCE |
| 12 | KYFTTNKKGEIFELK |
| 139 | DEDPYVRKTAAVCVA |
| 26 | KAELNNEKKEKRKEA |
| 335 | YNDPIYVKLEKLDIM |
| 5 | ***MTDSKYFTTNKK |
| 721 | WLPAVKAKGLEISGT |
| 878 | NNVYTIAKRNVEGQD |
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
Protein Sequence
Gene Ontology
| Classification | GO ID | Description |
|---|---|---|
| Cellular Component | GO:0030122 | AP-2 adaptor complex |
| Cellular Component | GO:0030131 | clathrin adaptor complex |
| Cellular Component | GO:0045334 | clathrin-coated endocytic vesicle |
| Cellular Component | GO:0030669 | clathrin-coated endocytic vesicle membrane |
| Cellular Component | GO:0009898 | cytoplasmic side of plasma membrane |
| Cellular Component | GO:0005829 | cytosol |
| Cellular Component | GO:0030666 | endocytic vesicle membrane |
| Cellular Component | GO:0036020 | endolysosome membrane |
| Cellular Component | GO:0098894 | extrinsic component of presynaptic endocytic zone membrane |
| Cellular Component | GO:0098978 | glutamatergic synapse |
| Cellular Component | GO:0016020 | membrane |
| Cellular Component | GO:0005886 | plasma membrane |
| Cellular Component | GO:0098843 | postsynaptic endocytic zone |
| Cellular Component | GO:0008021 | synaptic vesicle |
| Molecular Function | GO:0030276 | clathrin binding |
| Molecular Function | GO:0044877 | protein-containing complex binding |
| Molecular Function | GO:0005048 | signal sequence binding |
| Biological Process | GO:0048268 | clathrin coat assembly |
| Biological Process | GO:0072583 | clathrin-dependent endocytosis |
| Biological Process | GO:0006886 | intracellular protein transport |
| Biological Process | GO:0007269 | neurotransmitter secretion |
| Biological Process | GO:0045807 | positive regulation of endocytosis |
| Biological Process | GO:1905477 | positive regulation of protein localization to membrane |
| Biological Process | GO:0098884 | postsynaptic neurotransmitter receptor internalization |
| Biological Process | GO:0048488 | synaptic vesicle endocytosis |
| Biological Process | GO:0016192 | vesicle-mediated transport |
Reference
[1] Yang D, Yin J, Shan L, Yi X, Zhang W et al.. Identification of lysine-lactylated substrates in gastric cancer cells.. iScience 25(7):104630. 2022 Jul 15. PMID: 35800753.
[2] Yang Z, Yan C, Ma J, Peng P, Ren X et al.. Lactylome analysis suggests lactylation-dependent mechanisms of metabolic adaptation in hepatocellular carcinoma.. Nat Metab 5(1):61-79. 2023 Jan. PMID: 36593272.
[3] Hong H, Chen X, Wang H, Gu X, Yuan Y et al.. Global profiling of protein lysine lactylation and potential target modified protein analysis in hepatocellular carcinoma.. Proteomics 23(9):e2200432. 2023 May. PMID: 36625413.
[4] Shi CM, Wang QC, Li XL, Yang YH, Tang XY et al.. Global Profiling of Protein Lactylation in Human Hippocampi.. Proteomics Clin Appl 19(2):e202400061. 2025 Mar. PMID: 39610256.
[5] Chao L, Xu Y, Yang Y, Ao X, Liang J. Identification of lactylation-related biomarkers for diagnosis, prognosis, and treatment responsiveness in triple-negative breast cancer.. World J Surg Oncol 24(1):77. 2026 Jan 22. PMID: 41566505.
[6] Wu Q, Li Z, Gong T, Zheng X, Zhou X et al.. Porphyromonas gingivalis infection induces lysine lactylation reprogramming in human umbilical vein endothelial cells.. Front Cell Infect Microbiol 16:1706727. 2026. PMID: 41696360.