CPLM 1.0 - Compendium of Protein Lysine Modification
TagContent
CPLM ID CPLM-021752
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 
Created Date
 July 27, 2013 
Organism
 Mus musculus (Mouse) 
NCBI Taxa ID
 10090 
Lysine Modification
Position
Peptide
Type
References
128LRFLCKLKEAELLEPacetylation[1]
128LRFLCKLKEAELLEPubiquitination[2]
298KESDNNVKLIVLDRLubiquitination[2]
494PIVESEIKKEAGELKacetylation[3]
534LSSSRPTKKEEDRPPubiquitination[2]
603GKSSLPKKPITDDDVubiquitination[2]
786PHDFANIKANVKVASubiquitination[2]
Reference
 [1] Quantitative acetylome analysis reveals the roles of SIRT1 in regulating diverse substrates and cellular pathways.
 Chen Y, Zhao W, Yang JS, Cheng Z, Luo H, Lu Z, Tan M, Gu W, Zhao Y.
 Mol Cell Proteomics. 2012 Oct;11(10):1048-62. [PMID: 22826441]
 [2] Proteomic analyses reveal divergent ubiquitylation site patterns in murine tissues.
 Wagner SA, Beli P, Weinert BT, Schölz C, Kelstrup CD, Young C, Nielsen ML, Olsen JV, Brakebusch C, Choudhary C.
 Mol Cell Proteomics. 2012 Dec;11(12):1578-85. [PMID: 22790023]
 [3] SIRT5-Mediated Lysine Desuccinylation Impacts Diverse Metabolic Pathways.
 Park J, Chen Y, Tishkoff DX, Peng C, Tan M, Dai L, Xie Z, Zhang Y, Zwaans BM, Skinner ME, Lombard DB, Zhao Y.
 Mol Cell. 2013 Jun 27;50(6):919-30. [PMID: 23806337] 
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. 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 (By similarity). Plays a functional role in facilitating the transport of kappa-type opioid receptor mRNAs into axons and enhances translation of these proteins in cortical neurons. 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 triglyceride lipase (PNPLA2) with the lipid droplet surface to mediate lipolysis. 
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 (By similarity).  
Keyword
 Acetylation; Cell membrane; Complete proteome; Cytoplasm; Cytoplasmic vesicle; ER-Golgi transport; Golgi apparatus; 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
VLDRLVELKE HPAHERVLQD LVMDILRVLS TPDLEVRKKT LQLALDLVSS RNVEELVIVL 360
KKEVIKTNNV SEHEDTDKYR QLLVRTLHSC SVRFPDMAAN VIPVLMEFLS DSNEAAAADV 420
LEFVREAIQR FDNLRMLIVE KMLEVFHAIK SVKIYRGALW ILGEYCSTKE DIQSVMTEVR 480
RSLGEIPIVE SEIKKEAGEL KPEEEITVGP VQKLVTEMGT YATQSALSSS RPTKKEEDRP 540
PLRGFLLDGD FFVAASLATT LTKIALRYVA LVQEKKKQNS FVAEAMLLMA TILHLGKSSL 600
PKKPITDDDV DRISLCLKVL SECSPLMNDI FNKECRQSLS QMLSAKLEEE KLSQKKESEK 660
RNVTVQPDDP ISFMQLTAKN EMNCKEDQFQ LSLLAAMGNT QRKEAADPLA SKLNKVTQLT 720
GFSDPVYAEA YVHVNQYDIV LDVLVVNQTS DTLQNCTLEL ATLGDLKLVE KPSPLTLAPH 780
DFANIKANVK VASTENGIIF GNIVYDVSGA ASDRNCVVLS DIHIDIMDYI QPATCTDAEF 840
RQMWAEFEWE NKVTVNTNMT DLNDYLQHIL KSTNMKCLTP EKALSGYCGF MAANLYARSI 900
FGEDALANVS IEKPVHQGPD AAVTGHIRIR AKSQGMALSL GDKINLSQKK TSL 953 
Gene Ontology
 GO:0030126; C:COPI vesicle coat; IEA:Compara.
 GO:0030137; C:COPI-coated vesicle; IDA:MGI.
 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:0006891; P:intra-Golgi vesicle-mediated transport; IEA:Compara.
 GO:0006886; P:intracellular protein transport; IEA:InterPro. 
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