CPLM 1.0 - Compendium of Protein Lysine Modification
TagContent
CPLM ID CPLM-013450
UniProt Accession
Genbank Protein ID
Genbank Nucleotide ID
Protein Name
 Poly [ADP-ribose] polymerase 10 
Protein Synonyms/Alias
 PARP-10; ADP-ribosyltransferase diphtheria toxin-like 10; ARTD10 
Gene Name
 PARP10 
Gene Synonyms/Alias
  
Created Date
 July 27, 2013 
Organism
 Homo sapiens (Human) 
NCBI Taxa ID
 9606 
Lysine Modification
Position
Peptide
Type
References
916RNATVYGKGVYFARRacetylation[1]
916RNATVYGKGVYFARRubiquitination[2, 3]
Reference
 [1] 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]
 [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] 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] 
Functional Description
 May play a role in cell proliferation. May be required for the maintenance of cell cycle progression. 
Sequence Annotation
 DOMAIN 806 1025 PARP catalytic.
 REGION 700 907 Myc binding.
 MOTIF 650 667 Ubiquitin-interacting.
 MOTIF 673 690 Ubiquitin-interacting.
 MOD_RES 101 101 Phosphothreonine.
 MOD_RES 916 916 N6-acetyllysine.  
Keyword
 3D-structure; Acetylation; Complete proteome; Cytoplasm; Glycosyltransferase; NAD; Nucleus; Phosphoprotein; Polymorphism; Reference proteome; Transferase. 
Sequence Source
 UniProt (SWISSPROT/TrEMBL); GenBank; EMBL 
Protein Length
 1025 AA 
Protein Sequence
MVAMAEAEAG VAVEVRGLPP AVPDELLTLY FENRRRSGGG PVLSWQRLGC GGVLTFREPA 60
DAERVLAQAD HELHGAQLSL RPAPPRAPAR LLLQGLPPGT TPQRLEQHVQ ALLRASGLPV 120
QPCCALASPR PDRALVQLPK PLSEADVRVL EEQAQNLGLE GTLVSLARVP QARAVRVVGD 180
GASVDLLLLE LYLENERRSG GGPLEDLQRL PGPLGTVASF QQWQVAERVL QQEHRLQGSE 240
LSLVPHYDIL EPEELAENTS GGDHPSTQGP RATKHALLRT GGLVTALQGA GTVTMGSGEE 300
PGQSGASLRT GPMVQGRGIM TTGSGQEPGQ SGTSLRTGPM GSLGQAEQVS SMPMGSLEHE 360
GLVSLRPVGL QEQEGPMSLG PVGSAGPVET SKGLLGQEGL VEIAMDSPEQ EGLVGPMEIT 420
MGSLEKAGPV SPGCVKLAGQ EGLVEMVLLM EPGAMRFLQL YHEDLLAGLG DVALLPLEGP 480
DMTGFRLCGA QASCQAAEEF LRSLLGSISC HVLCLEHPGS ARFLLGPEGQ HLLQGLEAQF 540
QCVFGTERLA TATLDTGLEE VDPTEALPVL PGNAHTLWTP DSTGGDQEDV SLEEVRELLA 600
TLEGLDLDGE DWLPRELEEE GPQEQPEEEV TPGHEEEEPV APSTVAPRWL EEEAALQLAL 660
HRSLEPQGQV AEQEEAAALR QALTLSLLEQ PPLEAEEPPD GGTDGKAQLV VHSAFEQDVE 720
ELDRALRAAL EVHVQEETVG PWRRTLPAEL RARLERCHGV SVALRGDCTI LRGFGAHPAR 780
AARHLVALLA GPWDQSLAFP LAASGPTLAG QTLKGPWNNL ERLAENTGEF QEVVRAFYDT 840
LDAARSSIRV VRVERVSHPL LQQQYELYRE RLLQRCERRP VEQVLYHGTT APAVPDICAH 900
GFNRSFCGRN ATVYGKGVYF ARRASLSVQD RYSPPNADGH KAVFVARVLT GDYGQGRRGL 960
RAPPLRGPGH VLLRYDSAVD CICQPSIFVI FHDTQALPTH LITCEHVPRA SPDDPSGLPG 1020
RSPDT 1025 
Gene Ontology
 GO:0005794; C:Golgi apparatus; IDA:HPA.
 GO:0005634; C:nucleus; IDA:UniProtKB.
 GO:0003950; F:NAD+ ADP-ribosyltransferase activity; IEA:EC.
 GO:0048147; P:negative regulation of fibroblast proliferation; IDA:UniProtKB.
 GO:0070212; P:protein poly-ADP-ribosylation; IDA:UniProtKB.
 GO:0010847; P:regulation of chromatin assembly; IDA:UniProtKB. 
Interpro
 IPR012317; Poly(ADP-ribose)pol_cat_dom.
 IPR003903; Ubiquitin-int_motif. 
Pfam
 PF00644; PARP 
SMART
 SM00726; UIM 
PROSITE
 PS51059; PARP_CATALYTIC 
PRINTS