CPLM 1.0 - Compendium of Protein Lysine Modification
TagContent
CPLM ID CPLM-001118
UniProt Accession
Genbank Protein ID
Genbank Nucleotide ID
Protein Name
 Copine-3 
Protein Synonyms/Alias
 Copine III 
Gene Name
 CPNE3 
Gene Synonyms/Alias
 CPN3; KIAA0636 
Created Date
 July 27, 2013 
Organism
 Homo sapiens (Human) 
NCBI Taxa ID
 9606 
Lysine Modification
Position
Peptide
Type
References
61CLNPQFSKTFIIDYYubiquitination[1]
76FEVVQKLKFGVYDIDubiquitination[2]
125KTGRPAGKGSITISAubiquitination[1, 3]
136TISAEEIKDNRVVLFubiquitination[1]
158DNKDLFGKSDPYLEFubiquitination[1, 2, 3, 4]
167DPYLEFHKQTSDGNWubiquitination[1, 2, 3, 4, 5]
184VHRTEVVKNNLNPVWubiquitination[2, 4]
262RQKKKSYKNSGVISVubiquitination[1, 2, 3]
390RSCLPQIKLYGPTNFubiquitination[5, 6]
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] 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] 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] 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]
 [6] 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
Functional Description
 May function in membrane trafficking. Exhibits calcium- dependent phospholipid binding properties (By similarity). 
Sequence Annotation
 DOMAIN 2 99 C2 1.
 DOMAIN 125 230 C2 2.
 DOMAIN 291 513 VWFA.
 MOD_RES 242 242 Phosphoserine (By similarity).  
Keyword
 Complete proteome; Direct protein sequencing; Phosphoprotein; Polymorphism; Reference proteome; Repeat. 
Sequence Source
 UniProt (SWISSPROT/TrEMBL); GenBank; EMBL 
Protein Length
 537 AA 
Protein Sequence
MAAQCVTKVA LNVSCANLLD KDIGSKSDPL CVLFLNTSGQ QWYEVERTER IKNCLNPQFS 60
KTFIIDYYFE VVQKLKFGVY DIDNKTIELS DDDFLGECEC TLGQIVSSKK LTRPLVMKTG 120
RPAGKGSITI SAEEIKDNRV VLFEMEARKL DNKDLFGKSD PYLEFHKQTS DGNWLMVHRT 180
EVVKNNLNPV WRPFKISLNS LCYGDMDKTI KVECYDYDND GSHDLIGTFQ TTMTKLKEAS 240
RSSPVEFECI NEKKRQKKKS YKNSGVISVK QCEITVECTF LDYIMGGCQL NFTVGVDFTG 300
SNGDPRSPDS LHYISPNGVN EYLTALWSVG LVIQDYDADK MFPAFGFGAQ IPPQWQVSHE 360
FPMNFNPSNP YCNGIQGIVE AYRSCLPQIK LYGPTNFSPI INHVARFAAA ATQQQTASQY 420
FVLLIITDGV ITDLDETRQA IVNASRLPMS IIIVGVGGAD FSAMEFLDGD GGSLRSPLGE 480
VAIRDIVQFV PFRQFQNAPK EALAQCVLAE IPQQVVGYFN TYKLLPPKNP ATKQQKQ 537 
Gene Ontology
 GO:0005829; C:cytosol; IDA:UniProtKB.
 GO:0005544; F:calcium-dependent phospholipid binding; TAS:UniProtKB.
 GO:0004674; F:protein serine/threonine kinase activity; IDA:UniProtKB.
 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