CPLM 1.0 - Compendium of Protein Lysine Modification
TagContent
CPLM ID CPLM-009631
UniProt Accession
Genbank Protein ID
Genbank Nucleotide ID
Protein Name
 AP-2 complex subunit beta 
Protein Synonyms/Alias
 AP105B; Adapter-related protein complex 2 beta subunit; Adaptor protein complex AP-2 subunit beta; Beta-2-adaptin; Beta-adaptin; Clathrin assembly protein complex 2 beta large chain; Plasma membrane adaptor HA2/AP2 adaptin beta subunit 
Gene Name
 Ap2b1 
Gene Synonyms/Alias
 Clapb1 
Created Date
 July 27, 2013 
Organism
 Rattus norvegicus (Rat) 
NCBI Taxa ID
 10116 
Lysine Modification
Position
Peptide
Type
References
5***MTDSKYFTTNKKacetylation[1]
5***MTDSKYFTTNKKubiquitination[2]
12KYFTTNKKGEIFELKubiquitination[2]
272KFLELLPKDSDYYNMacetylation[1]
282DYYNMLLKKLAPPLVacetylation[1]
318QKRPEILKQEIKVFFacetylation[1]
Reference
 [1] Proteomic analysis of lysine acetylation sites in rat tissues reveals organ specificity and subcellular patterns.
 Lundby A, Lage K, Weinert BT, Bekker-Jensen DB, Secher A, Skovgaard T, Kelstrup CD, Dmytriyev A, Choudhary C, Lundby C, Olsen JV.
 Cell Rep. 2012 Aug 30;2(2):419-31. [PMID: 22902405]
 [2] Synaptic protein ubiquitination in rat brain revealed by antibody-based ubiquitome analysis.
 Na CH, Jones DR, Yang Y, Wang X, Xu Y, Peng J.
 J Proteome Res. 2012 Sep 7;11(9):4722-32. [PMID: 22871113] 
Functional Description
 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. 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). 
Sequence Annotation
 MOD_RES 265 265 N6-acetyllysine (By similarity).
 MOD_RES 737 737 Phosphotyrosine (By similarity).
 MOD_RES 888 888 Phosphotyrosine (By similarity).  
Keyword
 3D-structure; Acetylation; Alternative splicing; Cell membrane; Coated pit; Complete proteome; Membrane; Phosphoprotein; Protein transport; Reference proteome; Transport. 
Sequence Source
 UniProt (SWISSPROT/TrEMBL); GenBank; EMBL 
Protein Length
 937 AA 
Protein Sequence
MTDSKYFTTN KKGEIFELKA ELNNEKKEKR KEAVKKVIAA MTVGKDVSSL FPDVVNCMQT 60
DNLELKKLVY LYLMNYAKSQ PDMAIMAVNS FVKDCEDPNP LIRALAVRTM GCIRVDKITE 120
YLCEPLRKCL KDEDPYVRKT AAVCVAKLHD INAQMVEDQG FLDSLRDLIA DSNPMVVANA 180
VAALSEISES HPNSNLLDLN PQNINKLLTA LNECTEWGQI FILDCLSNYN PKDDREAQSI 240
CERVTPRLSH ANSAVVLSAV KVLMKFLELL PKDSDYYNML LKKLAPPLVT LLSGEPEVQY 300
VALRNINLIV QKRPEILKQE IKVFFVKYND PIYVKLEKLD IMIRLASQAN IAQVLAELKE 360
YATEVDVDFV RKAVRAIGRC AIKVEQSAER CVSTLLDLIQ TKVNYVVQEA IVVIRDIFRK 420
YPNKYESIIA TLCENLDSLD EPDARAAMIW IVGEYAERID NADELLESFL EGFHDESTQV 480
QLTLLTAIVK LFLKKPSETQ ELVQQVLSLA TQDSDNPDLR DRGYIYWRLL STDPVTAKEV 540
VLSEKPLISE ETDLIEPTLL DELICHIGSL ASVYHKPPNA FVEGSHGIHR KHLPIHHGST 600
DAGDSPVGTT TATNLEQPQV IPSQGDLLGD LLNLDLGPPV NVPQVSSMQM GAVDLLGGGL 660
DSLVGQSFIP SSVPATFAPS PTPAVVSSGL NDLFELSTGI GMAPGGYVAP KAVWLPAVKA 720
KGLEISGTFT HRQGHIYMEM NFTNKALQHM TDFAIQFNKN SFGVIPSTPL AIHTPLMPNQ 780
SIDVSLPLNT LGPVMKMEPL NNLQVAVKNN IDVFYFSCLI PLNVLFVEDG KMERQVFLAT 840
WKDIPNENEL QFQIKECHLN ADTVSSKLQN NNVYTIAKRN VEGQDMLYQS LKLTNGIWIL 900
AELRIQPGNP NYTLSLKCRA PEVSQYIYQV YDSILKN 937 
Gene Ontology
 GO:0030119; C:AP-type membrane coat adaptor complex; TAS:ProtInc.
 GO:0030131; C:clathrin adaptor complex; IEA:InterPro.
 GO:0030118; C:clathrin coat; IDA:BHF-UCL.
 GO:0005905; C:coated pit; IEA:UniProtKB-SubCell.
 GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
 GO:0005802; C:trans-Golgi network; IDA:RGD.
 GO:0030276; F:clathrin binding; IDA:BHF-UCL.
 GO:0032403; F:protein complex binding; IMP:RGD.
 GO:0008565; F:protein transporter activity; IEA:InterPro.
 GO:0048268; P:clathrin coat assembly; IDA:BHF-UCL.
 GO:0006886; P:intracellular protein transport; IEA:InterPro. 
Interpro
 IPR026739; AP_beta.
 IPR016342; AP_complex_bsu_1_2_4.
 IPR011989; ARM-like.
 IPR016024; ARM-type_fold.
 IPR015151; B-adaptin_app_sub_C.
 IPR012295; Beta2_adaptin/TBP_C_dom.
 IPR002553; Clathrin/coatomer_adapt-like_N.
 IPR008152; Clathrin_a/b/g-adaptin_app_Ig.
 IPR013037; Clathrin_b-adaptin_app_Ig-like.
 IPR009028; Coatomer/calthrin_app_sub_C.
 IPR013041; Coatomer/clathrin_app_Ig-like. 
Pfam
 PF01602; Adaptin_N
 PF02883; Alpha_adaptinC2
 PF09066; B2-adapt-app_C 
SMART
 SM00809; Alpha_adaptinC2
 SM01020; B2-adapt-app_C 
PROSITE
  
PRINTS