CPLM 1.0 - Compendium of Protein Lysine Modification
TagContent
CPLM ID CPLM-011727
UniProt Accession
Genbank Protein ID
Genbank Nucleotide ID
Protein Name
 AP-1 complex subunit beta-1 
Protein Synonyms/Alias
 Adapter-related protein complex 1 subunit beta-1; Adaptor protein complex AP-1 subunit beta-1; Beta-1-adaptin; Beta-adaptin 1; Clathrin assembly protein complex 1 beta large chain; Golgi adaptor HA1/AP1 adaptin beta subunit 
Gene Name
 AP1B1 
Gene Synonyms/Alias
 ADTB1; BAM22; CLAPB2 
Created Date
 July 27, 2013 
Organism
 Homo sapiens (Human) 
NCBI Taxa ID
 9606 
Lysine Modification
Position
Peptide
Type
References
5***MTDSKYFTTTKKubiquitination[1]
117MGCIRVDKITEYLCEubiquitination[2]
131EPLRKCLKDEDPYVRubiquitination[3]
272KFMEMLSKDLDYYGTubiquitination[4]
282DYYGTLLKKLAPPLVubiquitination[2]
318QKRPEILKHEMKVFFacetylation[5]
335YNDPIYVKLEKLDIMubiquitination[4]
591GGRGVVHKSLPPRTAubiquitination[1]
876NAEAASSKLQSSNIFubiquitination[6]
887SNIFTVAKRNVEGQDubiquitination[2, 6]
Reference
 [1] Systems-wide analysis of ubiquitylation dynamics reveals a key role for PAF15 ubiquitylation in DNA-damage bypass.
 Povlsen LK, Beli P, Wagner SA, Poulsen SL, Sylvestersen KB, Poulsen JW, Nielsen ML, Bekker-Jensen S, Mailand N, Choudhary C.
 Nat Cell Biol. 2012 Oct;14(10):1089-98. [PMID: 23000965]
 [2] A proteome-wide, quantitative survey of in vivo ubiquitylation sites reveals widespread regulatory roles.
 Wagner SA, Beli P, Weinert BT, Nielsen ML, Cox J, Mann M, Choudhary C.
 Mol Cell Proteomics. 2011 Oct;10(10):M111.013284. [PMID: 21890473]
 [3] Ubiquitin ligase substrate identification through quantitative proteomics at both the protein and peptide levels.
 Lee KA, Hammerle LP, Andrews PS, Stokes MP, Mustelin T, Silva JC, Black RA, Doedens JR.
 J Biol Chem. 2011 Dec 2;286(48):41530-8. [PMID: 21987572]
 [4] Systematic and quantitative assessment of the ubiquitin-modified proteome.
 Kim W, Bennett EJ, Huttlin EL, Guo A, Li J, Possemato A, Sowa ME, Rad R, Rush J, Comb MJ, Harper JW, Gygi SP.
 Mol Cell. 2011 Oct 21;44(2):325-40. [PMID: 21906983]
 [5] Lysine acetylation targets protein complexes and co-regulates major cellular functions.
 Choudhary C, Kumar C, Gnad F, Nielsen ML, Rehman M, Walther TC, Olsen JV, Mann M.
 Science. 2009 Aug 14;325(5942):834-40. [PMID: 19608861]
 [6] Refined preparation and use of anti-diglycine remnant (K-ε-GG) antibody enables routine quantification of 10,000s of ubiquitination sites in single proteomics experiments.
 Udeshi ND, Svinkina T, Mertins P, Kuhn E, Mani DR, Qiao JW, Carr SA.
 Mol Cell Proteomics. 2013 Mar;12(3):825-31. [PMID: 23266961] 
Functional Description
 Subunit of clathrin-associated adaptor protein complex 1 that plays a role in protein sorting in the late-Golgi/trans-Golgi network (TGN) and/or endosomes. The AP complexes mediate both the recruitment of clathrin to membranes and the recognition of sorting signals within the cytosolic tails of transmembrane cargo molecules. 
Sequence Annotation
 MOD_RES 318 318 N6-acetyllysine.
 MOD_RES 574 574 Nitrated tyrosine (By similarity).  
Keyword
 3D-structure; Acetylation; Alternative splicing; Complete proteome; Cytoplasmic vesicle; Endocytosis; Golgi apparatus; Membrane; Nitration; Polymorphism; Protein transport; Reference proteome; Transport. 
Sequence Source
 UniProt (SWISSPROT/TrEMBL); GenBank; EMBL 
Protein Length
 949 AA 
Protein Sequence
MTDSKYFTTT KKGEIFELKA ELNSDKKEKK KEAVKKVIAS MTVGKDVSAL FPDVVNCMQT 60
DNLELKKLVY LYLMNYAKSQ PDMAIMAVNT FVKDCEDPNP LIRALAVRTM GCIRVDKITE 120
YLCEPLRKCL KDEDPYVRKT AAVCVAKLHD INAQLVEDQG FLDTLKDLIS DSNPMVVANA 180
VAALSEIAES HPSSNLLDLN PQSINKLLTA LNECTEWGQI FILDCLANYM PKDDREAQSI 240
CERVTPRLSH ANSAVVLSAV KVLMKFMEML SKDLDYYGTL LKKLAPPLVT LLSAEPELQY 300
VALRNINLIV QKRPEILKHE MKVFFVKYND PIYVKLEKLD IMIRLASQAN IAQVLAELKE 360
YATEVDVDFV RKAVRAIGRC AIKVEQSAER CVSTLLDLIQ TKVNYVVQEA IVVIKDIFRK 420
YPNKYESVIA TLCENLDSLD EPEARAAMIW IVGEYAERID NADELLESFL EGFHDESTQV 480
QLQLLTAIVK LFLKKPTETQ ELVQQVLSLA TQDSDNPDLR DRGYIYWRLL STDPVAAKEV 540
VLAEKPLISE ETDLIEPTLL DELICYIGTL ASVYHKPPSA FVEGGRGVVH KSLPPRTASS 600
ESAESPETAP TGAPPGEQPD VIPAQGDLLG DLLNLDLGPP VSGPPLATSS VQMGAVDLLG 660
GGLDSLMGDE PEGIGGTNFV APPTAAVPAN LGAPIGSGLS DLFDLTSGVG TLSGSYVAPK 720
AVWLPAMKAK GLEISGTFTR QVGSISMDLQ LTNKALQVMT DFAIQFNRNS FGLAPATPLQ 780
VHAPLSPNQT VEISLPLSTV GSVMKMEPLN NLQVAVKNNI DVFYFSTLYP LHILFVEDGK 840
MDRQMFLATW KDIPNENEAQ FQIRDCPLNA EAASSKLQSS NIFTVAKRNV EGQDMLYQSL 900
KLTNGIWVLA ELRIQPGNPS CTDLELSLKC RAPEVSQHVY QAYETILKN 949 
Gene Ontology
 GO:0030131; C:clathrin adaptor complex; IEA:InterPro.
 GO:0030665; C:clathrin-coated vesicle membrane; IEA:UniProtKB-SubCell.
 GO:0030659; C:cytoplasmic vesicle membrane; TAS:Reactome.
 GO:0005829; C:cytosol; TAS:Reactome.
 GO:0000139; C:Golgi membrane; TAS:Reactome.
 GO:0005765; C:lysosomal membrane; TAS:Reactome.
 GO:0032588; C:trans-Golgi network membrane; TAS:Reactome.
 GO:0008565; F:protein transporter activity; IEA:InterPro.
 GO:0005215; F:transporter activity; TAS:ProtInc.
 GO:0019886; P:antigen processing and presentation of exogenous peptide antigen via MHC class II; TAS:Reactome.
 GO:0016044; P:cellular membrane organization; TAS:Reactome.
 GO:0006897; P:endocytosis; IEA:UniProtKB-KW.
 GO:0006886; P:intracellular protein transport; IEA:InterPro.
 GO:0006892; P:post-Golgi vesicle-mediated transport; TAS:Reactome.
 GO:0050690; P:regulation of defense response to virus by virus; TAS:Reactome.
 GO:0016032; P:viral reproduction; TAS:Reactome. 
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