CPLM 1.0 - Compendium of Protein Lysine Modification
TagContent
CPLM ID CPLM-021231
UniProt Accession
Genbank Protein ID
Genbank Nucleotide ID
Protein Name
 Poly [ADP-ribose] polymerase 12 
Protein Synonyms/Alias
 PARP-12; ADP-ribosyltransferase diphtheria toxin-like 12; ARTD12; Zinc finger CCCH domain-containing protein 1 
Gene Name
 PARP12 
Gene Synonyms/Alias
 ZC3HDC1 
Created Date
 July 27, 2013 
Organism
 Homo sapiens (Human) 
NCBI Taxa ID
 9606 
Lysine Modification
Position
Peptide
Type
References
209SNSENLEKLEKLGMSubiquitination[1, 2]
212ENLEKLEKLGMSSDLubiquitination[2]
256PQGTSERKDSSGSVSubiquitination[2]
289KSCSFQDKCHRVHFHubiquitination[2]
326EEAYCNPKIERILCSubiquitination[2]
410VSSSDVEKAYLAYCTubiquitination[2]
428DGQAATLKFQAGKHNubiquitination[2]
433TLKFQAGKHNYELDFubiquitination[2, 3]
441HNYELDFKAFVQKNLubiquitination[2, 3]
455LVYGTTKKVCRRPKYubiquitination[2]
477TMQTCNTKFPGPKSIubiquitination[1, 2]
482NTKFPGPKSIPDYWDubiquitination[3, 4]
512SSSEEYQKVWNLFNRubiquitination[2]
528LPFYFVQKIERVQNLubiquitination[2]
545WEVYQWQKGQMQKQNubiquitination[2]
593VHGTSYGKGSYFARDubiquitination[2]
Reference
 [1] Methods for quantification of in vivo changes in protein ubiquitination following proteasome and deubiquitinase inhibition.
 Udeshi ND, Mani DR, Eisenhaure T, Mertins P, Jaffe JD, Clauser KR, Hacohen N, Carr SA.
 Mol Cell Proteomics. 2012 May;11(5):148-59. [PMID: 22505724]
 [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] 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]
 [4] 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
  
Sequence Annotation
 DOMAIN 298 361 WWE 1.
 DOMAIN 364 458 WWE 2.
 DOMAIN 484 698 PARP catalytic.
 ZN_FING 94 119 C3H1-type 1.
 ZN_FING 150 179 C3H1-type 2.
 ZN_FING 180 202 C3H1-type 3.
 ZN_FING 270 297 C3H1-type 4.
 ZN_FING 271 296 C3H1-type 3.  
Keyword
 3D-structure; Complete proteome; Metal-binding; NAD; Nucleus; Polymorphism; Reference proteome; Repeat; Transferase; Zinc; Zinc-finger. 
Sequence Source
 UniProt (SWISSPROT/TrEMBL); GenBank; EMBL 
Protein Length
 701 AA 
Protein Sequence
MAQAGVVGEV TQVLCAAGGA LELPELRRRL RMGLSADALE RLLRQRGRFV VAVRAGGAAA 60
APERVVLAAS PLRLCRAHQG SKPGCVGLCA QLHLCRFMVY GACKFLRAGK NCRNSHSLTT 120
EHNLSVLRTH GVDHLSYNEL CQLLFQNDPW LLPEICQHYN KGDGPHGSCA FQKQCIKLHI 180
CQYFLQGECK FGTSCKRSHD FSNSENLEKL EKLGMSSDLV SRLPTIYRNA HDIKNKSSAP 240
SRVPPLFVPQ GTSERKDSSG SVSPNTLSQE EGDQICLYHI RKSCSFQDKC HRVHFHLPYR 300
WQFLDRGKWE DLDNMELIEE AYCNPKIERI LCSESASTFH SHCLNFNAMT YGATQARRLS 360
TASSVTKPPH FILTTDWIWY WSDEFGSWQE YGRQGTVHPV TTVSSSDVEK AYLAYCTPGS 420
DGQAATLKFQ AGKHNYELDF KAFVQKNLVY GTTKKVCRRP KYVSPQDVTT MQTCNTKFPG 480
PKSIPDYWDS SALPDPGFQK ITLSSSSEEY QKVWNLFNRT LPFYFVQKIE RVQNLALWEV 540
YQWQKGQMQK QNGGKAVDER QLFHGTSAIF VDAICQQNFD WRVCGVHGTS YGKGSYFARD 600
AAYSHHYSKS DTQTHTMFLA RVLVGEFVRG NASFVRPPAK EGWSNAFYDS CVNSVSDPSI 660
FVIFEKHQVY PEYVIQYTTS SKPSVTPSIL LALGSLFSSR Q 701 
Gene Ontology
 GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
 GO:0003950; F:NAD+ ADP-ribosyltransferase activity; IEA:EC.
 GO:0003676; F:nucleic acid binding; IEA:InterPro.
 GO:0008270; F:zinc ion binding; IEA:InterPro. 
Interpro
 IPR012317; Poly(ADP-ribose)pol_cat_dom.
 IPR004170; WWE-dom.
 IPR000571; Znf_CCCH. 
Pfam
 PF00644; PARP
 PF00642; zf-CCCH 
SMART
 SM00356; ZnF_C3H1 
PROSITE
 PS51059; PARP_CATALYTIC
 PS50918; WWE
 PS50103; ZF_C3H1 
PRINTS