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UniProtKB/Swiss-Prot entry Q9Y6F1


[Entry info] [Name and origin] [References] [Comments] [Cross-references] [Keywords] [Features] [Sequence] [Tools]

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Entry information
Entry name PARP3_HUMAN
Primary accession number Q9Y6F1
Secondary accession numbers Q8NER9 Q96CG2 Q9UG81
Integrated into Swiss-Prot on September 26, 2001
Sequence was last modified on March 3, 2009 (Sequence version 3)
Annotations were last modified on    June 16, 2009 (Entry version 91)
Name and origin of the protein
Protein name Poly [ADP-ribose] polymerase 3
Synonyms PARP-3
EC 2.4.2.30
NAD(+) ADP-ribosyltransferase 3
Poly[ADP-ribose] synthetase 3
pADPRT-3
hPARP-3
IRT1
Gene name
Name: PARP3
Synonyms: ADPRT3, ADPRTL3
From
Homo sapiens (Human) [TaxID: 9606] 
Taxonomy Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae; Homo.
Protein existence 1: Evidence at protein level;
References
[1]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2), AND VARIANT ARG-100.
Koch-Nolte F.;
Submitted (MAR-1998) to the EMBL/GenBank/DDBJ databases.
[2]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), AND VARIANT ARG-100.
TISSUE=Fetal brain;
DOI=10.1006/geno.1999.5799; PubMed=10329013 [NCBI, ExPASy, EBI, Israel, Japan]
Johansson M.;
"A human poly(ADP-ribose) polymerase gene family (ADPRTL): cDNA cloning of two novel poly(ADP-ribose) polymerase homologues.";
Genomics 57:442-445(1999).
[3]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2), VARIANT ARG-100, AND SUBCELLULAR LOCATION.
TISSUE=Frontal cortex;
DOI=10.1242/jcs.00341; PubMed=12640039 [NCBI, ExPASy, EBI, Israel, Japan]
Augustin A., Spenlehauer C., Dumond H., Menissier-de Murcia J., Piel M., Schmit A.-C., Apiou F., Vonesch J.-L., Kock M., Bornens M., de Murcia G.M.;
"PARP-3 localizes preferentially to the daughter centriole and interferes with the G1/S cell cycle progression.";
J. Cell Sci. 116:1551-1562(2003).
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
DOI=10.1038/nature04728; PubMed=16641997 [NCBI, ExPASy, EBI, Israel, Japan]
Muzny D.M., Scherer S.E., Kaul R., Wang J., Yu J., Sudbrak R., Buhay C.J., Chen R., Cree A., Ding Y., Dugan-Rocha S., Gill R., Gunaratne P., Harris R.A., Hawes A.C., Hernandez J., Hodgson A.V., Hume J., Jackson A., Khan Z.M., Kovar-Smith C., Lewis L.R., Lozado R.J., Metzker M.L., Milosavljevic A., Miner G.R., Morgan M.B., Nazareth L.V., Scott G., Sodergren E., Song X.-Z., Steffen D., Wei S., Wheeler D.A., Wright M.W., Worley K.C., Yuan Y., Zhang Z., Adams C.Q., Ansari-Lari M.A., Ayele M., Brown M.J., Chen G., Chen Z., Clendenning J., Clerc-Blankenburg K.P., Chen R., Chen Z., Davis C., Delgado O., Dinh H.H., Dong W., Draper H., Ernst S., Fu G., Gonzalez-Garay M.L., Garcia D.K., Gillett W., Gu J., Hao B., Haugen E., Havlak P., He X., Hennig S., Hu S., Huang W., Jackson L.R., Jacob L.S., Kelly S.H., Kube M., Levy R., Li Z., Liu B., Liu J., Liu W., Lu J., Maheshwari M., Nguyen B.-V., Okwuonu G.O., Palmeiri A., Pasternak S., Perez L.M., Phelps K.A., Plopper F.J., Qiang B., Raymond C., Rodriguez R., Saenphimmachak C., Santibanez J., Shen H., Shen Y., Subramanian S., Tabor P.E., Verduzco D., Waldron L., Wang J., Wang J., Wang Q., Williams G.A., Wong G.K.-S., Yao Z., Zhang J., Zhang X., Zhao G., Zhou J., Zhou Y., Nelson D., Lehrach H., Reinhardt R., Naylor S.L., Yang H., Olson M., Weinstock G., Gibbs R.A.;
"The DNA sequence, annotation and analysis of human chromosome 3.";
Nature 440:1194-1198(2006).
[5]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1), AND VARIANT ARG-100.
TISSUE=B-cell;
DOI=10.1101/gr.2596504; PubMed=15489334 [NCBI, ExPASy, EBI, Israel, Japan]
The MGC Project Team;
"The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC).";
Genome Res. 14:2121-2127(2004).
[6]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 75-533 (ISOFORM 1), AND VARIANT ARG-100.
TISSUE=Kidney;
DOI=10.1186/1471-2164-8-399; PubMed=17974005 [NCBI, ExPASy, EBI, Israel, Japan]
Bechtel S., Rosenfelder H., Duda A., Schmidt C.P., Ernst U., Wellenreuther R., Mehrle A., Schuster C., Bahr A., Blocker H., Heubner D., Hoerlein A., Michel G., Wedler H., Kohrer K., Ottenwalder B., Poustka A., Wiemann S., Schupp I.;
"The full-ORF clone resource of the German cDNA consortium.";
BMC Genomics 8:399-399(2007).
[7]
FUNCTION, SUBCELLULAR LOCATION, AND INTERACTION WITH PRKDC; PARP1; EZH2; HDAC1; HDAC2; SUZ12; YY1; LIG3 AND LIG4.
DOI=10.1002/jcb.21051; PubMed=16924674 [NCBI, ExPASy, EBI, Israel, Japan]
Rouleau M., McDonald D., Gagne P., Ouellet M.E., Droit A., Hunter J.M., Dutertre S., Prigent C., Hendzel M.J., Poirier G.G.;
"PARP-3 associates with polycomb group bodies and with components of the DNA damage repair machinery.";
J. Cell. Biochem. 100:385-401(2007).
[8]
X-RAY CRYSTALLOGRAPHY (2.3 ANGSTROMS) OF 178-532 IN COMPLEX WITH THE INHIBITOR 3-AMINOBENZOIC ACID.
Structural genomics consortium (SGC);
"Human poly(ADP-ribose) polymerase 3, catalytic fragment in complex with an inhibitor 3-aminobenzoic acid.";
Submitted (APR-2007) to the PDB data bank.
[9]
STRUCTURE BY NMR OF 41-157.
RIKEN structural genomics initiative (RSGI);
"Solution structure of the WGR domain from human poly [ADP-ribose] polymerase-3.";
Submitted (APR-2008) to the PDB data bank.
Comments
  • FUNCTION: Involved in the base excision repair (BER) pathway, by catalyzing the poly(ADP-ribosyl)ation of a limited number of acceptor proteins involved in chromatin architecture and in DNA metabolism. This modification follows DNA damages and appears as an obligatory step in a detection/signaling pathway leading to the reparation of DNA strand breaks. May link the DNA damage surveillance network to the mitotic fidelity checkpoint. Negatively influences the G1/S cell cycle progression without interfering with centrosome duplication. Binds DNA. May be involved in the regulation of PRC2 and PRC3 complex-dependent gene silencing.
  • CATALYTIC ACTIVITY: NAD+ + (ADP-D-ribosyl)(n)-acceptor = nicotinamide + (ADP-D-ribosyl)(n+1)-acceptor.
  • SUBUNIT: Interacts with PRKDC and PARP1. Interacts with XRCC5; the interaction is dependent on nucleic acids. Interacts with XRCC6; the interaction is dependent on nucleic acids. Interacts with EZH2, HDAC1, HDAC2, SUZ12, YY1, LIG3 and LIG4.
  • INTERACTION:
    Q16778:HIST2H2BE; NbExp=1; IntAct=EBI-1045281, EBI-1056125;
    Q71DI3:HIST2H3A; NbExp=1; IntAct=EBI-1045281, EBI-750650;
  • SUBCELLULAR LOCATION: Nucleus. Centrosome. Centrosome, centriole. Note=Core component of the centrosome. Preferentially localized to the daughter centriole throughout the cell cycle. According PubMed:16924674 is almost exclusively localized in the nucleus and appears in numerous small foci and a small number of larger foci whereas a centrosomal location has not been detected.
  • ALTERNATIVE PRODUCTS: 2 named isoforms [FASTA] produced by alternative splicing.
    Name1
    SynonymsShort
    Isoform IDQ9Y6F1-1
    Note: More abundant according to PubMed:16924674.
    This is the isoform sequence displayed in this entry.
    Name2
    SynonymsLong
    Isoform IDQ9Y6F1-2
    Features which should be applied to build the isoform sequence: VSP_007863.
  • TISSUE SPECIFICITY: Widely expressed; the highest levels are in the kidney, skeletal muscle, liver, heart and spleen; also detected in pancreas, lung, placenta, brain, leukocytes, colon, small intestine, ovary, testis, prostate and thymus.
  • DOMAIN: According to PubMed:10329013 the N-terminal domain (54 amino acids) of isoform 2 is responsible for its centrosomal localization. The C-terminal region contains the catalytic domain.
  • PTM: Auto-poly(ADP)-ribosylation.
  • SIMILARITY: Contains 1 PARP alpha-helical domain.
  • SIMILARITY: Contains 1 PARP catalytic domain.
Copyright
Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms. Distributed under the Creative Commons Attribution-NoDerivs License.
Cross-references
Sequence databases
EMBL
Y16836; CAC79988.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AF083068; AAD29855.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AY126341; AAM95460.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AC115284; -; NOT_ANNOTATED_CDS; Genomic_DNA.[EMBL / GenBank / DDBJ]
BC014260; AAH14260.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AL050034; CAB43246.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
IPI IPI00023184; -.
IPI00333507; -.
PIR T08713; T08713.
RefSeq NP_001003931.2; -.
NP_005476.3; -.
UniGene Hs.271742
3D structure databases
PDB
2EOC; NMR; -; A=41-157.[ExPASy / RCSB / EBI]
3C49; X-ray; 2.80 A; A=178-532.[ExPASy / RCSB / EBI]
3C4H; X-ray; 2.10 A; A=178-532.[ExPASy / RCSB / EBI]
3CE0; X-ray; 2.80 A; A=178-532.[ExPASy / RCSB / EBI]
3FHB; X-ray; 2.30 A; A=178-532.[ExPASy / RCSB / EBI]
Detailed list of linked structures.
PDBsum 2EOC; -.
3C49; -.
3C4H; -.
3CE0; -.
3FHB; -.
ModBase Q9Y6F1.
Protein-protein interaction databases
IntAct Q9Y6F1; 4.
PTM databases
PhosphoSite Q9Y6F1; -.
Enzyme and pathway databases
BRENDA 2.4.2.30; 247.
Organism-specific databases
GeneCards GC03P051951; -.
H-InvDB HIX0003336; -.
HGNC HGNC:273; PARP3.
GenAtlas PARP3.
MIM 607726; gene. [NCBI / EBI]
PharmGKB PA24593; -.
Gene expression databases
ArrayExpress Q9Y6F1; -.
Bgee Q9Y6F1; -.
CleanEx HS_PARP3; -.
GermOnline ENSG00000041880; Homo sapiens.
Ontologies
GO
GO:0005814; Cellular component: centriole (inferred from electronic annotation from UniProtKB-SubCell).
GO:0005634; Cellular component: nucleus (inferred from electronic annotation from UniProtKB-SubCell).
GO:0003950; Molecular function: NAD+ ADP-ribosyltransferase activity (inferred from electronic annotation from EC).
GO:0005515; Molecular function: protein binding (inferred from physical interaction from IntAct).
GO:0006281; Biological process: DNA repair (traceable author statement from ProtInc).
GO:0006471; Biological process: protein amino acid ADP-ribosylation (traceable author statement from ProtInc).
QuickGo view.
Family and domain databases
InterPro IPR012317; PARP_catalytic.
IPR004102; PARP_reg.
IPR008893; WGR.
Graphical view of domain structure.
Gene3D G3DSA:1.20.142.10; PARP_reg; 1.
Pfam PF00644; PARP; 1.
PF02877; PARP_reg; 1.
PF05406; WGR; 1.
Pfam graphical view of domain structure.
SMART SM00773; WGR; 1.
SMART graphical view of domain structure.
PROSITE PS51060; PARP_ALPHA_HD; 1.
PS51059; PARP_CATALYTIC; 1.
PROSITE graphical view of domain structure (profiles).
Proteomic databases
PRIDE Q9Y6F1; -.
Genome annotation databases
Ensembl ENSG00000041880; Homo sapiens. [Contig view]
GeneID 10039; -.
KEGG hsa:10039; -.
Phylogenomic databases
HOVERGEN Q9Y6F1; -.
OMA Q9Y6F1; YQLLKCQ.
Other
NextBio 37913; -.
SOURCE PARP3; Homo sapiens.
ProtoNet Q9Y6F1.
UniRef View cluster of proteins with at least 50% / 90% / 100% identity.
Keywords
3D-structure; Alternative splicing; Glycosyltransferase; NAD; Nucleus; Polymorphism; Transferase.
Features
SEVIEWER logo Feature table viewer FT aligner logo Feature aligner
KeyFrom   To Length Description FTId
CHAIN   1   533  533     Poly [ADP-ribose] polymerase 3. PRO_0000211329
DOMAIN   182   300  119     PARP alpha-helical. 
DOMAIN   313   533  221     PARP catalytic. 
MOTIF   14    20  7     Nuclear localization signal (Potential). 
VAR_SEQ   1     1        M -> MSLLFLAM (in isoform 2). VSP_007863
VARIANT   91    91  1     S -> N (in dbSNP:rs34224216 [NCBI]). VAR_056643 
VARIANT   100   100  1     H -> R (in dbSNP:rs28547534 [NCBI]). VAR_054622 
VARIANT   269   269  1     Q -> R (in dbSNP:rs323870 [NCBI]). VAR_056644 
CONFLICT   80    80        N -> K (in Ref. 2; AAD29855). 
CONFLICT   171   171        G -> A (in Ref. 2; AAD29855). 
CONFLICT   411   411        K -> E (in Ref. 6; CAB43246). 
STRAND   50    53  4      
TURN   54    56  3      
STRAND   61    74  14      
TURN   75    78  4      
STRAND   79    89  11      
STRAND   95   100  6      
STRAND   111   117  7      
HELIX   118   133  16      
HELIX   140   142  3      
STRAND   147   149  3      
STRAND   151   153  3      
HELIX   187   197  11      
HELIX   199   207  9      
TURN   208   210  3      
TURN   213   215  3      
TURN   218   220  3      
HELIX   223   241  19      
HELIX   250   260  11      
HELIX   276   298  23      
HELIX   303   307  5      
STRAND   309   311  3      
HELIX   314   321  8      
STRAND   324   328  5      
HELIX   336   346  11      
STRAND   349   351  3      
STRAND   354   363  10      
HELIX   366   370  5      
HELIX   371   373  3      
STRAND   379   385  7      
HELIX   388   390  3      
HELIX   391   397  7      
STRAND   411   418  8      
HELIX   419   423  5      
STRAND   430   445  16      
STRAND   448   454  7      
STRAND   467   471  5      
STRAND   474   477  4      
HELIX   479   481  3      
STRAND   483   487  5      
STRAND   490   494  5      
STRAND   499   501  3      
HELIX   503   505  3      
STRAND   514   519  6      
HELIX   520   522  3      
STRAND   523   532  10      
Sequence information
Length: 533 AA [This is the length of the unprocessed precursor] Molecular weight: 60070 Da [This is the MW of the unprocessed precursor] CRC64: BF728C3D88722029 [This is a checksum on the sequence]
        10         20         30         40         50         60 
MAPKPKPWVQ TEGPEKKKGR QAGREEDPFR STAEALKAIP AEKRIIRVDP TCPLSSNPGT 

        70         80         90        100        110        120 
QVYEDYNCTL NQTNIENNNN KFYIIQLLQD SNRFFTCWNH WGRVGEVGQS KINHFTRLED 

       130        140        150        160        170        180 
AKKDFEKKFR EKTKNNWAER DHFVSHPGKY TLIEVQAEDE AQEAVVKVDR GPVRTVTKRV 

       190        200        210        220        230        240 
QPCSLDPATQ KLITNIFSKE MFKNTMALMD LDVKKMPLGK LSKQQIARGF EALEALEEAL 

       250        260        270        280        290        300 
KGPTDGGQSL EELSSHFYTV IPHNFGHSQP PPINSPELLQ AKKDMLLVLA DIELAQALQA 

       310        320        330        340        350        360 
VSEQEKTVEE VPHPLDRDYQ LLKCQLQLLD SGAPEYKVIQ TYLEQTGSNH RCPTLQHIWK 

       370        380        390        400        410        420 
VNQEGEEDRF QAHSKLGNRK LLWHGTNMAV VAAILTSGLR IMPHSGGRVG KGIYFASENS 

       430        440        450        460        470        480 
KSAGYVIGMK CGAHHVGYMF LGEVALGREH HINTDNPSLK SPPPGFDSVI ARGHTEPDPT 

       490        500        510        520        530 
QDTELELDGQ QVVVPQGQPV PCPEFSSSTF SQSEYLIYQE SQCRLRYLLE VHL 

Q9Y6F1 in FASTA format

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