Search Results
Overview
| Uniprot ID | Q96CW1 |
|---|---|
| Protein Name | AP-2 complex subunit mu |
| Gene Name | AP2M1 |
| Organism | Homo sapiens |
Kla Sites from experimental identification
| Position | Flanking peptide |
|---|---|
| 145 | IKSQHQTKEEQSQIT |
| 224 | NDKIVIEKQGKGTAD |
| 238 | DETSKSGKQSIAIDD |
| 256 | HQCVRLSKFDSERSI |
| 410 | YLKVFEPKLNYSDHD |
| 59 | RTSFFHVKRSNIWLA |
Function
Component of the adaptor protein complex 2 (AP-2) (PubMed:12694563, PubMed:12952941, PubMed:14745134, PubMed:14985334, PubMed:15473838, PubMed:31104773). Adaptor protein complexes function in protein transport via transport vesicles in different membrane traffic pathways (PubMed:12694563, PubMed:12952941, PubMed:14745134, PubMed:14985334, PubMed:15473838, PubMed:31104773). Adaptor protein complexes are vesicle coat components and appear to be involved in cargo selection and vesicle formation (PubMed:12694563, PubMed:12952941, PubMed:14745134, PubMed:14985334, PubMed:15473838, PubMed:31104773). 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 (PubMed:12694563, PubMed:12952941, PubMed:14745134, PubMed:14985334, PubMed:15473838, PubMed:31104773). The clathrin lattice serves as a mechanical scaffold but is itself unable to bind directly to membrane components (PubMed:12694563, PubMed:12952941, PubMed:14745134, PubMed:14985334, PubMed:15473838, PubMed:31104773). 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 (PubMed:12694563, PubMed:12952941, PubMed:14745134, PubMed:14985334, PubMed:15473838, PubMed:31104773). AP-2 also serves as a cargo receptor to selectively sort the membrane proteins involved in receptor-mediated endocytosis (PubMed:16581796). AP-2 seems to play a role in the recycling of synaptic vesicle membranes from the presynaptic surface (PubMed:12694563, PubMed:12952941, PubMed:14745134, PubMed:14985334, PubMed:15473838, PubMed:31104773). 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 (By similarity). AP-2 may also play a role in maintaining normal post-endocytic trafficking through the ARF6-regulated, non-clathrin pathway (PubMed:19033387). During long-term potentiation in hippocampal neurons, AP-2 is responsible for the endocytosis of ADAM10 (PubMed:23676497). The AP-2 mu subunit binds to transmembrane cargo proteins; it recognizes the Y-X-X-Phi motifs (By similarity). The surface region interacting with to the Y-X-X-Phi motif is inaccessible in cytosolic AP-2, but becomes accessible through a conformational change following phosphorylation of AP-2 mu subunit at Thr-156 in membrane-associated AP-2 (PubMed:11877457). The membrane-specific phosphorylation event appears to involve assembled clathrin which activates the AP-2 mu kinase AAK1 (PubMed:11877457). Plays a role in endocytosis of frizzled family members upon Wnt signaling (By similarity)
Protein Sequence
Gene Ontology
| Classification | GO ID | Description |
|---|---|---|
| Molecular Function | GO:0005048 | signal sequence binding |
| Cellular Component | GO:0030121 | AP-1 adaptor complex |
| Cellular Component | GO:0030122 | AP-2 adaptor complex |
| Cellular Component | GO:0045334 | clathrin-coated endocytic vesicle |
| Cellular Component | GO:0030669 | clathrin-coated endocytic vesicle membrane |
| Cellular Component | GO:0005905 | clathrin-coated pit |
| 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:0070062 | extracellular exosome |
| Cellular Component | GO:0098894 | extrinsic component of presynaptic endocytic zone membrane |
| Cellular Component | GO:0098978 | glutamatergic synapse |
| Cellular Component | GO:0005765 | lysosomal membrane |
| Cellular Component | GO:0005886 | plasma membrane |
| Cellular Component | GO:0098794 | postsynapse |
| Cellular Component | GO:0008021 | synaptic vesicle |
| Molecular Function | GO:0035615 | clathrin adaptor activity |
| Molecular Function | GO:0097718 | disordered domain specific binding |
| Molecular Function | GO:0008289 | lipid binding |
| Molecular Function | GO:0050750 | low-density lipoprotein particle receptor binding |
| Molecular Function | GO:0044325 | transmembrane transporter binding |
| Biological Process | GO:0072583 | clathrin-dependent endocytosis |
| Biological Process | GO:0006896 | Golgi to vacuole transport |
| Biological Process | GO:0006886 | intracellular protein transport |
| Biological Process | GO:1903077 | negative regulation of protein localization to plasma membrane |
| Biological Process | GO:0002092 | positive regulation of receptor internalization |
| Biological Process | GO:1900244 | positive regulation of synaptic vesicle endocytosis |
| Biological Process | GO:0098884 | postsynaptic neurotransmitter receptor internalization |
| Biological Process | GO:0065003 | protein-containing complex assembly |
| Biological Process | GO:0031623 | receptor internalization |
| Biological Process | GO:0097494 | regulation of vesicle size |
| Biological Process | GO:0048488 | synaptic vesicle endocytosis |
| Biological Process | GO:0006900 | vesicle budding from membrane |
| Biological Process | GO:0016192 | vesicle-mediated transport |
Reference
[1] 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.
[2] 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.
[3] 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.