CPLM 1.0 - Compendium of Protein Lysine Modification
TagContent
CPLM ID CPLM-041997
UniProt Accession
Genbank Protein ID
Genbank Nucleotide ID
Protein Name
 Poly (ADP-ribose) polymerase family, member 9, isoform CRA_b 
Protein Synonyms/Alias
 Poly [ADP-ribose] polymerase 9 
Gene Name
 PARP9 
Gene Synonyms/Alias
 hCG_17211 
Created Date
 July 27, 2013 
Organism
 Homo sapiens (Human) 
NCBI Taxa ID
 9606 
Lysine Modification
Position
Peptide
Type
References
30AFSSEMAKRSKMLSLubiquitination[1]
33SEMAKRSKMLSLNNYubiquitination[1]
177QWTIQQQKTQDEMKEubiquitination[1, 2]
183QKTQDEMKENIIFLKubiquitination[1]
204QELLDQKKQFEKCGLubiquitination[1]
208DQKKQFEKCGLQVLKubiquitination[1]
285GAGIYFTKNLKNLAEubiquitination[1, 2]
288IYFTKNLKNLAEKAKubiquitination[1]
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
Functional Description
  
Sequence Annotation
  
Keyword
 Complete proteome; Reference proteome. 
Sequence Source
 UniProt (SWISSPROT/TrEMBL); GenBank; EMBL 
Protein Length
 399 AA 
Protein Sequence
MDFSMVAGAA AYNEKSDLEI YKAFSSEMAK RSKMLSLNNY SVPQSTREEK RENGLEARSP 60
AINLMGFNVE EMYEAHAWIQ RILSLQNHHI IENNHILYLG RKEHDILSQL QKTSSVSITE 120
IISPGRTELE IEGARADLIE VVMNIEDMLC KVQEEMARKK ERGLWRSLGQ WTIQQQKTQD 180
EMKENIIFLK CPVPPTQELL DQKKQFEKCG LQVLKVEKID NEVLMAAFQR KKKMMEEKLH 240
RQPVSHRLFQ QVPYQFCNVV CRVGFQRMYS TPCDPKYGAG IYFTKNLKNL AEKAKKISAA 300
DKLIYVFEAE VLTGFFCQGH PLNIVPPPLS PGAIDGHDSV VDNVSSPETF VIFSGMQAIP 360
QYLWTCTQEY VQSQDYSSGP MRPFAQHPWR GFASGSPVD 399 
Gene Ontology
 GO:0003950; F:NAD+ ADP-ribosyltransferase activity; IEA:InterPro. 
Interpro
 IPR012317; Poly(ADP-ribose)pol_cat_dom. 
Pfam
  
SMART
  
PROSITE
 PS51059; PARP_CATALYTIC 
PRINTS