Search Results

Overview

Uniprot IDO95782
Protein NameAP-2 complex subunit alpha-1
Gene NameAP2A1
OrganismHomo sapiens

Kla Sites from experimental identification

Position Flanking peptide
177 LCLLRLYKASPDLVP
48 RSKFKGDKALDGYSK
6 **MPAVSKGDGMRGL
620 LAKLKRKKGPGAGSA
810 TQLAVQTKRVAAQVD
962 RLTLRTSKEPVSRHL

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 (By similarity)

Protein Sequence

10 MPAVSKGDGM 20 RGLAVFISDI 30 RNCKSKEAEI 40 KRINKELANI 50 RSKFKGDKAL 60 DGYSKKKYVC 70 KLLFIFLLGH 80 DIDFGHMEAV 90 NLLSSNKYTE 100 KQIGYLFISV 110 LVNSNSELIR 120 LINNAIKNDL 130 ASRNPTFMCL 140 ALHCIANVGS 150 REMGEAFAAD 160 IPRILVAGDS 170 MDSVKQSAAL 180 CLLRLYKASP 190 DLVPMGEWTA 200 RVVHLLNDQH 210 MGVVTAAVSL 220 ITCLCKKNPD 230 DFKTCVSLAV 240 SRLSRIVSSA 250 STDLQDYTYY 260 FVPAPWLSVK 270 LLRLLQCYPP 280 PEDAAVKGRL 290 VECLETVLNK 300 AQEPPKSKKV 310 QHSNAKNAIL 320 FETISLIIHY 330 DSEPNLLVRA 340 CNQLGQFLQH 350 RETNLRYLAL 360 ESMCTLASSE 370 FSHEAVKTHI 380 DTVINALKTE 390 RDVSVRQRAA 400 DLLYAMCDRS 410 NAKQIVSEML 420 RYLETADYAI 430 REEIVLKVAI 440 LAEKYAVDYS 450 WYVDTILNLI 460 RIAGDYVSEE 470 VWYRVLQIVT 480 NRDDVQGYAA 490 KTVFEALQAP 500 ACHENMVKVG 510 GYILGEFGNL 520 IAGDPRSSPP 530 VQFSLLHSKF 540 HLCSVATRAL 550 LLSTYIKFIN 560 LFPETKATIQ 570 GVLRAGSQLR 580 NADVELQQRA 590 VEYLTLSSVA 600 STDVLATVLE 610 EMPPFPERES 620 SILAKLKRKK 630 GPGAGSALDD 640 GRRDPSSNDI 650 NGGMEPTPST 660 VSTPSPSADL 670 LGLRAAPPPA 680 APPASAGAGN 690 LLVDVFDGPA 700 AQPSLGPTPE 710 EAFLSELEPP 720 APESPMALLA 730 DPAPAADPGP 740 EDIGPPIPEA 750 DELLNKFVCK 760 NNGVLFENQL 770 LQIGVKSEFR 780 QNLGRMYLFY 790 GNKTSVQFQN 800 FSPTVVHPGD 810 LQTQLAVQTK 820 RVAAQVDGGA 830 QVQQVLNIEC 840 LRDFLTPPLL 850 SVRFRYGGAP 860 QALTLKLPVT 870 INKFFQPTEM 880 AAQDFFQRWK 890 QLSLPQQEAQ 900 KIFKANHPMD 910 AEVTKAKLLG 920 FGSALLDNVD 930 PNPENFVGAG 940 IIQTKALQVG 950 CLLRLEPNAQ 960 AQMYRLTLRT 970 SKEPVSRHLC ELLAQQF

Gene Ontology

Classification GO ID Description
Molecular Function GO:0019901 protein kinase binding
Cellular Component GO:0030122 AP-2 adaptor complex
Cellular Component GO:0016324 apical plasma membrane
Cellular Component GO:0016323 basolateral plasma membrane
Cellular Component GO:0030130 clathrin coat of trans-Golgi network vesicle
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:0032433 filopodium tip
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:0035615 clathrin adaptor activity
Molecular Function GO:0050750 low-density lipoprotein particle receptor binding
Molecular Function GO:0044877 protein-containing complex binding
Biological Process GO:0072583 clathrin-dependent endocytosis
Biological Process GO:0006897 endocytosis
Biological Process GO:0006895 Golgi to endosome transport
Biological Process GO:0006886 intracellular protein transport
Biological Process GO:1900126 negative regulation of hyaluronan biosynthetic process
Biological Process GO:0010976 positive regulation of neuron projection development
Biological Process GO:0048260 positive regulation of receptor-mediated endocytosis
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 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] 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.

[3] 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.

[4] He J, Lai T, Zhou Z, Yang H, Lei Z et al.. Multiomics profiling reveals the involvement of protein lactylation in nonhomologous end joining pathway conferring radioresistance in lung adenocarcinoma cell.. Sci Rep 15(1):24651. 2025 Jul 9. PMID: 40634431.

[5] Yan M, Tu H, Tang S, Gai Z, Shi Q et al.. Lactylated Proteomic Analysis Reveals Functional Implications of Lysine Lactylation In Asthenozoospermia.. Mol Cell Proteomics 24(12):101439. 2025 Dec. PMID: 41192556.

[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.