CPLM 1.0 - Compendium of Protein Lysine Modification
TagContent
CPLM ID CPLM-019802
UniProt Accession
Genbank Protein ID
Genbank Nucleotide ID
Protein Name
 Copine-1 
Protein Synonyms/Alias
 Copine I 
Gene Name
 CPNE1 
Gene Synonyms/Alias
 CPN1 
Created Date
 July 27, 2013 
Organism
 Homo sapiens (Human) 
NCBI Taxa ID
 9606 
Lysine Modification
Position
Peptide
Type
References
20SCDHLIDKDIGSKSDubiquitination[1]
25IDKDIGSKSDPLCVLubiquitination[1]
60CSSPEFSKTLQLEYRubiquitination[1, 2, 3]
73YRFETVQKLRFGIYDubiquitination[1, 2, 3, 4, 5]
84GIYDIDNKTPELRDDubiquitination[1, 4, 5]
135TVSAQELKDNRVVTMacetylation[6]
135TVSAQELKDNRVVTMubiquitination[1, 4, 5]
151VEARNLDKKDFLGKSubiquitination[1]
152EARNLDKKDFLGKSDubiquitination[1]
157DKKDFLGKSDPFLEFubiquitination[1, 3, 4, 5]
171FFRQGDGKWHLVYRSacetylation[7]
171FFRQGDGKWHLVYRSubiquitination[1]
182VYRSEVIKNNLNPTWubiquitination[1, 2, 4, 5]
190NNLNPTWKRFSVPVQubiquitination[1, 4, 5]
256QQKKKSYKNSGTIRVubiquitination[1]
522AQGWAPLKPLPPSAKubiquitination[1, 2, 4, 5]
529KPLPPSAKDPAQAPQubiquitination[1, 4, 5]
Reference
 [1] 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]
 [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] 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]
 [6] Regulation of cellular metabolism by protein lysine acetylation.
 Zhao S, Xu W, Jiang W, Yu W, Lin Y, Zhang T, Yao J, Zhou L, Zeng Y, Li H, Li Y, Shi J, An W, Hancock SM, He F, Qin L, Chin J, Yang P, Chen X, Lei Q, Xiong Y, Guan KL.
 Science. 2010 Feb 19;327(5968):1000-4. [PMID: 20167786]
 [7] 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
Functional Description
 May function in membrane trafficking. Exhibits calcium- dependent phospholipid binding properties. 
Sequence Annotation
 DOMAIN 1 98 C2 1.
 DOMAIN 144 228 C2 2.
 DOMAIN 285 505 VWFA.
 MOD_RES 171 171 N6-acetyllysine.  
Keyword
 Acetylation; Complete proteome; Polymorphism; Reference proteome; Repeat. 
Sequence Source
 UniProt (SWISSPROT/TrEMBL); GenBank; EMBL 
Protein Length
 537 AA 
Protein Sequence
MAHCVTLVQL SISCDHLIDK DIGSKSDPLC VLLQDVGGGS WAELGRTERV RNCSSPEFSK 60
TLQLEYRFET VQKLRFGIYD IDNKTPELRD DDFLGGAECS LGQIVSSQVL TLPLMLKPGK 120
PAGRGTITVS AQELKDNRVV TMEVEARNLD KKDFLGKSDP FLEFFRQGDG KWHLVYRSEV 180
IKNNLNPTWK RFSVPVQHFC GGNPSTPIQV QCSDYDSDGS HDLIGTFHTS LAQLQAVPAE 240
FECIHPEKQQ KKKSYKNSGT IRVKICRVET EYSFLDYVMG GCQINFTVGV DFTGSNGDPS 300
SPDSLHYLSP TGVNEYLMAL WSVGSVVQDY DSDKLFPAFG FGAQVPPDWQ VSHEFALNFN 360
PSNPYCAGIQ GIVDAYRQAL PQVRLYGPTN FAPIINHVAR FAAQAAHQGT ASQYFMLLLL 420
TDGAVTDVEA TREAVVRASN LPMSVIIVGV GGADFEAMEQ LDADGGPLHT RSGQAAARDI 480
VQFVPYRRFQ NAPREALAQT VLAEVPTQLV SYFRAQGWAP LKPLPPSAKD PAQAPQA 537 
Gene Ontology
 GO:0005634; C:nucleus; IDA:HPA.
 GO:0005544; F:calcium-dependent phospholipid binding; TAS:ProtInc.
 GO:0001786; F:phosphatidylserine binding; IDA:MGI.
 GO:0005215; F:transporter activity; TAS:ProtInc.
 GO:0006629; P:lipid metabolic process; TAS:ProtInc.
 GO:0016192; P:vesicle-mediated transport; TAS:ProtInc. 
Interpro
 IPR000008; C2_Ca-dep.
 IPR008973; C2_Ca/lipid-bd_dom_CaLB.
 IPR018029; C2_membr_targeting.
 IPR010734; Copine.
 IPR002035; VWF_A. 
Pfam
 PF00168; C2
 PF07002; Copine 
SMART
 SM00239; C2
 SM00327; VWA 
PROSITE
 PS50004; C2
 PS50234; VWFA 
PRINTS