CPLM 1.0 - Compendium of Protein Lysine Modification
TagContent
CPLM ID CPLM-008717
UniProt Accession
Genbank Protein ID
Genbank Nucleotide ID
Protein Name
 Coatomer subunit beta 
Protein Synonyms/Alias
 Beta-coat protein; Beta-COP 
Gene Name
 COPB1 
Gene Synonyms/Alias
 COPB; MSTP026 
Created Date
 July 27, 2013 
Organism
 Homo sapiens (Human) 
NCBI Taxa ID
 9606 
Lysine Modification
Position
Peptide
Type
References
107LVCDAYRKDLQHPNEubiquitination[1, 2, 3, 4]
126STLRFLCKLKEAELLubiquitination[3]
128LRFLCKLKEAELLEPubiquitination[3]
298KESDNNVKLIVLDRLubiquitination[3]
309LDRLIELKEHPAHERubiquitination[3]
362ELVIVLKKEVIKTNNubiquitination[3]
378SEHEDTDKYRQLLVRubiquitination[3]
501KKEAGELKPEEEITVubiquitination[3, 5, 6]
534LSSSRPTKKEEDRPPubiquitination[1, 4]
603GKSSLPKKPITDDDVubiquitination[6]
633LMNDIFNKECRQSLSubiquitination[3, 6, 7, 8]
655EEEKLSQKKESEKRNubiquitination[3]
679SFMQLTAKNEMNCKEubiquitination[3]
685AKNEMNCKEDQFQLSubiquitination[3, 7]
703AMGNTQRKEAADPLAubiquitination[3]
712AADPLASKLNKVTQLubiquitination[3, 7]
771GDLKLVEKPSPLTLAubiquitination[1, 3, 4]
786PHDFANIKANVKVASubiquitination[1, 3, 4, 7]
871DYLQHILKSTNMKCLubiquitination[7]
876ILKSTNMKCLTPEKAubiquitination[3, 6, 7]
882MKCLTPEKALSGYCGubiquitination[3, 7]
913LANVSIEKPIHQGPDubiquitination[1, 3, 4]
943MALSLGDKINLSQKKubiquitination[1, 4]
950KINLSQKKTSI****ubiquitination[3]
Reference
 [1] 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]
 [2] 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]
 [3] 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]
 [4] hCKSAAP_UbSite: improved prediction of human ubiquitination sites by exploiting amino acid pattern and properties.
 Chen Z, Zhou Y, Song J, Zhang Z.
 Biochim Biophys Acta. 2013 Aug;1834(8):1461-7. [PMID: 23603789]
 [5] 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]
 [6] Integrated proteomic analysis of post-translational modifications by serial enrichment.
 Mertins P, Qiao JW, Patel J, Udeshi ND, Clauser KR, Mani DR, Burgess MW, Gillette MA, Jaffe JD, Carr SA.
 Nat Methods. 2013 Jul;10(7):634-7. [PMID: 23749302]
 [7] Global identification of modular cullin-RING ligase substrates.
 Emanuele MJ, Elia AE, Xu Q, Thoma CR, Izhar L, Leng Y, Guo A, Chen YN, Rush J, Hsu PW, Yen HC, Elledge SJ.
 Cell. 2011 Oct 14;147(2):459-74. [PMID: 21963094]
 [8] 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] 
Functional Description
 The coatomer is a cytosolic protein complex that binds to dilysine motifs and reversibly associates with Golgi non- clathrin-coated vesicles, which further mediate biosynthetic protein transport from the ER, via the Golgi up to the trans Golgi network. Coatomer complex is required for budding from Golgi membranes, and is essential for the retrograde Golgi-to-ER transport of dilysine-tagged proteins. In mammals, the coatomer can only be recruited by membranes associated to ADP-ribosylation factors (ARFs), which are small GTP-binding proteins; the complex also influences the Golgi structural integrity, as well as the processing, activity, and endocytic recycling of LDL receptors. Plays a functional role in facilitating the transport of kappa- type opioid receptor mRNAs into axons and enhances translation of these proteins. Required for limiting lipid storage in lipid droplets. Involved in lipid homeostasis by regulating the presence of perilipin family members PLIN2 and PLIN3 at the lipid droplet surface and promoting the association of adipocyte surface triglyceride lipase (PNPLA2) with the lipid droplet to mediate lipolysis (By similarity). Involved in the Golgi disassembly and reassembly processes during cell cycle. Involved in autophagy by playing a role in early endosome function. Plays a role in organellar compartmentalization of secretory compartments including endoplasmic reticulum (ER)-Golgi intermediate compartment (ERGIC), Golgi, trans-Golgi network (TGN) and recycling endosomes, and in biosynthetic transport of CAV1. Promotes degradation of Nef cellular targets CD4 and MHC class I antigens by facilitating their trafficking to degradative compartments. 
Sequence Annotation
 REPEAT 96 131 HEAT 1.
 REPEAT 132 168 HEAT 2.
 REPEAT 240 276 HEAT 3.
 REPEAT 277 314 HEAT 4.
 REPEAT 316 353 HEAT 5.
 REPEAT 396 433 HEAT 6.
 MOD_RES 2 2 N-acetylthreonine.  
Keyword
 Acetylation; Cell membrane; Complete proteome; Cytoplasm; Cytoplasmic vesicle; ER-Golgi transport; Golgi apparatus; Host-virus interaction; Membrane; Protein transport; Reference proteome; Repeat; Transport. 
Sequence Source
 UniProt (SWISSPROT/TrEMBL); GenBank; EMBL 
Protein Length
 953 AA 
Protein Sequence
MTAAENVCYT LINVPMDSEP PSEISLKNDL EKGDVKSKTE ALKKVIIMIL NGEKLPGLLM 60
TIIRFVLPLQ DHTIKKLLLV FWEIVPKTTP DGRLLHEMIL VCDAYRKDLQ HPNEFIRGST 120
LRFLCKLKEA ELLEPLMPAI RACLEHRHSY VRRNAVLAIY TIYRNFEHLI PDAPELIHDF 180
LVNEKDASCK RNAFMMLIHA DQDRALDYLS TCIDQVQTFG DILQLVIVEL IYKVCHANPS 240
ERARFIRCIY NLLQSSSPAV KYEAAGTLVT LSSAPTAIKA AAQCYIDLII KESDNNVKLI 300
VLDRLIELKE HPAHERVLQD LVMDILRVLS TPDLEVRKKT LQLALDLVSS RNVEELVIVL 360
KKEVIKTNNV SEHEDTDKYR QLLVRTLHSC SVRFPDMAAN VIPVLMEFLS DNNEAAAADV 420
LEFVREAIQR FDNLRMLIVE KMLEVFHAIK SVKIYRGALW ILGEYCSTKE DIQSVMTEIR 480
RSLGEIPIVE SEIKKEAGEL KPEEEITVGP VQKLVTEMGT YATQSALSSS RPTKKEEDRP 540
PLRGFLLDGD FFVAASLATT LTKIALRYVA LVQEKKKQNS FVAEAMLLMA TILHLGKSSL 600
PKKPITDDDV DRISLCLKVL SECSPLMNDI FNKECRQSLS HMLSAKLEEE KLSQKKESEK 660
RNVTVQPDDP ISFMQLTAKN EMNCKEDQFQ LSLLAAMGNT QRKEAADPLA SKLNKVTQLT 720
GFSDPVYAEA YVHVNQYDIV LDVLVVNQTS DTLQNCTLEL ATLGDLKLVE KPSPLTLAPH 780
DFANIKANVK VASTENGIIF GNIVYDVSGA ASDRNCVVLS DIHIDIMDYI QPATCTDAEF 840
RQMWAEFEWE NKVTVNTNMV DLNDYLQHIL KSTNMKCLTP EKALSGYCGF MAANLYARSI 900
FGEDALANVS IEKPIHQGPD AAVTGHIRIR AKSQGMALSL GDKINLSQKK TSI 953 
Gene Ontology
 GO:0030126; C:COPI vesicle coat; ISS:UniProtKB.
 GO:0005829; C:cytosol; TAS:Reactome.
 GO:0005793; C:endoplasmic reticulum-Golgi intermediate compartment; IEA:UniProtKB-SubCell.
 GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
 GO:0005198; F:structural molecule activity; IEA:InterPro.
 GO:0048205; P:COPI coating of Golgi vesicle; TAS:Reactome.
 GO:0006891; P:intra-Golgi vesicle-mediated transport; ISS:UniProtKB.
 GO:0006886; P:intracellular protein transport; IEA:InterPro.
 GO:0006890; P:retrograde vesicle-mediated transport, Golgi to ER; TAS:Reactome.
 GO:0019048; P:virus-host interaction; IEA:UniProtKB-KW. 
Interpro
 IPR011989; ARM-like.
 IPR016024; ARM-type_fold.
 IPR002553; Clathrin/coatomer_adapt-like_N.
 IPR011710; Coatomer_bsu_C.
 IPR016460; COPB1. 
Pfam
 PF01602; Adaptin_N
 PF07718; Coatamer_beta_C 
SMART
  
PROSITE
 PS50077; HEAT_REPEAT 
PRINTS