CPLM 1.0 - Compendium of Protein Lysine Modification
TagContent
CPLM ID CPLM-023971
UniProt Accession
Genbank Protein ID
Genbank Nucleotide ID
Protein Name
 Coatomer subunit gamma-1 
Protein Synonyms/Alias
 Gamma-1-coat protein; Gamma-1-COP 
Gene Name
 COPG1 
Gene Synonyms/Alias
 COPG 
Created Date
 July 27, 2013 
Organism
 Homo sapiens (Human) 
NCBI Taxa ID
 9606 
Lysine Modification
Position
Peptide
Type
References
24NPFQHLEKSAVLQEAubiquitination[1]
116LTKDMTGKEDNYRGPubiquitination[1]
145QAIERYMKQAIVDKVubiquitination[1]
213NDRLAVNKMISKVTRubiquitination[2]
238MMIRVASKQLEEEDGubiquitination[1, 3]
300QLFCSSPKAALRYAAubiquitination[2]
350LAITTLLKTGSESSIubiquitination[3]
465LLGQEGPKTTNPSKYubiquitination[1, 2]
471PKTTNPSKYIRFIYNubiquitination[1, 2, 3]
514PSILVLLKRCVMDDDubiquitination[1, 2, 3]
538YLNVLEQKQKALNAGubiquitination[1, 2, 3]
540NVLEQKQKALNAGYIubiquitination[2, 4, 5]
572YTLEPSEKPFDLKSVubiquitination[1, 2, 3, 4, 5, 6, 7]
577SEKPFDLKSVPLATAubiquitination[1, 2, 3]
600STPITAVKQPEKVAAubiquitination[1, 2, 7]
631RGLGPLFKSSPEPVAubiquitination[1, 2, 3]
806EAVGNIVKFLGMHPCubiquitination[1]
818HPCERSDKVPDNKNTubiquitination[2]
Reference
 [1] 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]
 [2] 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]
 [3] Landscape of the PARKIN-dependent ubiquitylome in response to mitochondrial depolarization.
 Sarraf SA, Raman M, Guarani-Pereira V, Sowa ME, Huttlin EL, Gygi SP, Harper JW.
 Nature. 2013 Apr 18;496(7445):372-6. [PMID: 23503661]
 [4] 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]
 [5] 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]
 [6] 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]
 [7] 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] 
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. 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 (By similarity). 
Sequence Annotation
 REPEAT 64 101 HEAT 1.
 REPEAT 283 320 HEAT 2.
 REPEAT 322 355 HEAT 3.
 REPEAT 356 392 HEAT 4.
 REGION 609 874 Interaction with ZNF289/ARFGAP2.  
Keyword
 3D-structure; Complete proteome; Cytoplasm; Cytoplasmic vesicle; ER-Golgi transport; Golgi apparatus; Membrane; Polymorphism; Protein transport; Reference proteome; Repeat; Transport. 
Sequence Source
 UniProt (SWISSPROT/TrEMBL); GenBank; EMBL 
Protein Length
 874 AA 
Protein Sequence
MLKKFDKKDE ESGGGSNPFQ HLEKSAVLQE ARVFNETPIN PRKCAHILTK ILYLINQGEH 60
LGTTEATEAF FAMTKLFQSN DPTLRRMCYL TIKEMSCIAE DVIIVTSSLT KDMTGKEDNY 120
RGPAVRALCQ ITDSTMLQAI ERYMKQAIVD KVPSVSSSAL VSSLHLLKCS FDVVKRWVNE 180
AQEAASSDNI MVQYHALGLL YHVRKNDRLA VNKMISKVTR HGLKSPFAYC MMIRVASKQL 240
EEEDGSRDSP LFDFIESCLR NKHEMVVYEA ASAIVNLPGC SAKELAPAVS VLQLFCSSPK 300
AALRYAAVRT LNKVAMKHPS AVTACNLDLE NLVTDSNRSI ATLAITTLLK TGSESSIDRL 360
MKQISSFMSE ISDEFKVVVV QAISALCQKY PRKHAVLMNF LFTMLREEGG FEYKRAIVDC 420
IISIIEENSE SKETGLSHLC EFIEDCEFTV LATRILHLLG QEGPKTTNPS KYIRFIYNRV 480
VLEHEEVRAG AVSALAKFGA QNEEMLPSIL VLLKRCVMDD DNEVRDRATF YLNVLEQKQK 540
ALNAGYILNG LTVSIPGLER ALQQYTLEPS EKPFDLKSVP LATAPMAEQR TESTPITAVK 600
QPEKVAATRQ EIFQEQLAAV PEFRGLGPLF KSSPEPVALT ESETEYVIRC TKHTFTNHMV 660
FQFDCTNTLN DQTLENVTVQ MEPTEAYEVL CYVPARSLPY NQPGTCYTLV ALPKEDPTAV 720
ACTFSCMMKF TVKDCDPTTG ETDDEGYEDE YVLEDLEVTV ADHIQKVMKL NFEAAWDEVG 780
DEFEKEETFT LSTIKTLEEA VGNIVKFLGM HPCERSDKVP DNKNTHTLLL AGVFRGGHDI 840
LVRSRLLLLD TVTMQVTARS LEELPVDIIL ASVG 874 
Gene Ontology
 GO:0030126; C:COPI vesicle coat; ISS:UniProtKB.
 GO:0005829; C:cytosol; TAS:Reactome.
 GO:0005634; C:nucleus; IDA:HPA.
 GO:0005198; F:structural molecule activity; IEA:InterPro.
 GO:0048205; P:COPI coating of Golgi vesicle; TAS:Reactome.
 GO:0051683; P:establishment of Golgi localization; ISS:BHF-UCL.
 GO:0006886; P:intracellular protein transport; IEA:InterPro.
 GO:0072384; P:organelle transport along microtubule; ISS:BHF-UCL.
 GO:0006890; P:retrograde vesicle-mediated transport, Golgi to ER; TAS:Reactome. 
Interpro
 IPR011989; ARM-like.
 IPR016024; ARM-type_fold.
 IPR002553; Clathrin/coatomer_adapt-like_N.
 IPR015873; Clathrin_a/coatomer_app_sub_C.
 IPR009028; Coatomer/calthrin_app_sub_C.
 IPR013041; Coatomer/clathrin_app_Ig-like.
 IPR017106; Coatomer_gsu.
 IPR014863; Coatomer_gsu_app.
 IPR013040; Coatomer_gsu_app_Ig-like-sub. 
Pfam
 PF01602; Adaptin_N
 PF08752; Gamma-COP 
SMART
  
PROSITE
 PS50077; HEAT_REPEAT 
PRINTS