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Overview

Uniprot ID	P62944
Protein Name	AP-2 complex subunit beta
Gene Name	Ap2b1
Organism	Rattus norvegicus

Kla Sites from experimental identification

Position	Flanking peptide
11	SKYFTTNKKGEIFEL
117	MGCIRVDKITEYLCE
12	KYFTTNKKGEIFELK
139	DEDPYVRKTAAVCVA
26	KAELNNEKKEKRKEA
265	SAVKVLMKFLELLPK
282	DYYNMLLKKLAPPLV
312	NINLIVQKRPEILKQ
335	YNDPIYVKLEKLDIM
36	KRKEAVKKVIAAMTV
5	***MTDSKYFTTNKK
719	AVWLPAVKAKGLEIS
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 (By similarity). 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 (By similarity)

Protein Sequence

10 MTDSKYFTTN 20 KKGEIFELKA 30 ELNNEKKEKR 40 KEAVKKVIAA 50 MTVGKDVSSL 60 FPDVVNCMQT 70 DNLELKKLVY 80 LYLMNYAKSQ 90 PDMAIMAVNS 100 FVKDCEDPNP 110 LIRALAVRTM 120 GCIRVDKITE 130 YLCEPLRKCL 140 KDEDPYVRKT 150 AAVCVAKLHD 160 INAQMVEDQG 170 FLDSLRDLIA 180 DSNPMVVANA 190 VAALSEISES 200 HPNSNLLDLN 210 PQNINKLLTA 220 LNECTEWGQI 230 FILDCLSNYN 240 PKDDREAQSI 250 CERVTPRLSH 260 ANSAVVLSAV 270 KVLMKFLELL 280 PKDSDYYNML 290 LKKLAPPLVT 300 LLSGEPEVQY 310 VALRNINLIV 320 QKRPEILKQE 330 IKVFFVKYND 340 PIYVKLEKLD 350 IMIRLASQAN 360 IAQVLAELKE 370 YATEVDVDFV 380 RKAVRAIGRC 390 AIKVEQSAER 400 CVSTLLDLIQ 410 TKVNYVVQEA 420 IVVIRDIFRK 430 YPNKYESIIA 440 TLCENLDSLD 450 EPDARAAMIW 460 IVGEYAERID 470 NADELLESFL 480 EGFHDESTQV 490 QLTLLTAIVK 500 LFLKKPSETQ 510 ELVQQVLSLA 520 TQDSDNPDLR 530 DRGYIYWRLL 540 STDPVTAKEV 550 VLSEKPLISE 560 ETDLIEPTLL 570 DELICHIGSL 580 ASVYHKPPNA 590 FVEGSHGIHR 600 KHLPIHHGST 610 DAGDSPVGTT 620 TATNLEQPQV 630 IPSQGDLLGD 640 LLNLDLGPPV 650 NVPQVSSMQM 660 GAVDLLGGGL 670 DSLVGQSFIP 680 SSVPATFAPS 690 PTPAVVSSGL 700 NDLFELSTGI 710 GMAPGGYVAP 720 KAVWLPAVKA 730 KGLEISGTFT 740 HRQGHIYMEM 750 NFTNKALQHM 760 TDFAIQFNKN 770 SFGVIPSTPL 780 AIHTPLMPNQ 790 SIDVSLPLNT 800 LGPVMKMEPL 810 NNLQVAVKNN 820 IDVFYFSCLI 830 PLNVLFVEDG 840 KMERQVFLAT 850 WKDIPNENEL 860 QFQIKECHLN 870 ADTVSSKLQN 880 NNVYTIAKRN 890 VEGQDMLYQS 900 LKLTNGIWIL 910 AELRIQPGNP 920 NYTLSLKCRA 930 PEVSQYIYQV YDSILKN

Gene Ontology

Classification	GO ID	Description
Cellular Component	GO:0030122	AP-2 adaptor complex
Cellular Component	GO:0030119	AP-type membrane coat adaptor complex
Cellular Component	GO:0030131	clathrin adaptor complex
Cellular Component	GO:0030118	clathrin coat
Cellular Component	GO:0098894	extrinsic component of presynaptic endocytic zone membrane
Cellular Component	GO:0098978	glutamatergic synapse
Cellular Component	GO:0098843	postsynaptic endocytic zone
Cellular Component	GO:0045202	synapse
Cellular Component	GO:0008021	synaptic vesicle
Molecular Function	GO:0030276	clathrin binding
Molecular Function	GO:0044877	protein-containing complex binding
Biological Process	GO:0035904	aorta development
Biological Process	GO:0003279	cardiac septum development
Biological Process	GO:0048268	clathrin coat assembly
Biological Process	GO:0072583	clathrin-dependent endocytosis
Biological Process	GO:0060976	coronary vasculature development
Biological Process	GO:0007507	heart development
Biological Process	GO:0006886	intracellular protein transport
Biological Process	GO:0001822	kidney development
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:0003281	ventricular septum development
Biological Process	GO:0016192	vesicle-mediated transport

Reference

[1] Yao Y, Bade R, Li G, Zhang A, Zhao H et al.. Global-Scale Profiling of Differential Expressed Lysine-Lactylated Proteins in the Cerebral Endothelium of Cerebral Ischemia-Reperfusion Injury Rats.. Cell Mol Neurobiol 43(5):1989-2004. 2023 Jul. PMID: 36030297.

[2] Sheng L, Xu H, Wang Y, Ni J, Xiang T et al.. Systematic analysis of lysine lactylation in nucleus pulposus cells.. iScience 27(11):111157. 2024 Nov 15. PMID: 39524337.

[3] Chen Y, Sun W, Sun Z, Zhao H, Wu T et al.. Effect of electroacupuncture on hippocampal protein lactylation in a rat model of vascular dementia.. Front Neurol 16:1629474. 2025. PMID: 40963935.