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Q9Y6F1 (PARP3_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 138. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (6) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Alt products·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Poly [ADP-ribose] polymerase 3

Short name=PARP-3
Short name=hPARP-3
EC=2.4.2.30
Alternative name(s):
ADP-ribosyltransferase diphtheria toxin-like 3
Short name=ARTD3
IRT1
NAD(+) ADP-ribosyltransferase 3
Short name=ADPRT-3
Poly[ADP-ribose] synthase 3
Short name=pADPRT-3
Gene names
Name:PARP3
Synonyms:ADPRT3, ADPRTL3
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length533 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (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. Ref.7

Catalytic activity

NAD+ + (ADP-D-ribosyl)(n)-acceptor = nicotinamide + (ADP-D-ribosyl)(n+1)-acceptor.

Subunit structure

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, LRIG3 and LIG4. Ref.7

Subcellular location

Nucleus. Cytoplasmcytoskeletonmicrotubule organizing centercentrosome. Cytoplasmcytoskeletonmicrotubule organizing centercentrosomecentriole. Note: Core component of the centrosome. Preferentially localized to the daughter centriole throughout the cell cycle. According to Ref.7, it 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. Ref.3 Ref.7

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 Ref.2, the N-terminal domain (54 amino acids) of isoform 2 is responsible for its centrosomal localization. The C-terminal region contains the catalytic domain.

Post-translational modification

Auto-poly(ADP)-ribosylation.

Sequence similarities

Contains 1 PARP alpha-helical domain.

Contains 1 PARP catalytic domain.

Alternative products

This entry describes 2 isoforms produced by alternative splicing. [Align] [Select]
Isoform 1 (identifier: Q9Y6F1-1)

Also known as: Short;

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.
Note: More abundant according to PubMed:16924674.
Isoform 2 (identifier: Q9Y6F1-2)

Also known as: Long;

The sequence of this isoform differs from the canonical sequence as follows:
     1-1: M → MSLLFLAM

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 533533Poly [ADP-ribose] polymerase 3
PRO_0000211329

Regions

Domain182 – 300119PARP alpha-helical
Domain313 – 533221PARP catalytic
Motif14 – 207Nuclear localization signal Potential

Natural variations

Alternative sequence11M → MSLLFLAM in isoform 2.
VSP_007863
Natural variant911S → N.
Corresponds to variant rs34224216 [ dbSNP | Ensembl ].
VAR_056643
Natural variant1001H → R. Ref.1 Ref.2 Ref.3 Ref.5 Ref.6
Corresponds to variant rs28547534 [ dbSNP | Ensembl ].
VAR_054622
Natural variant2691Q → R.
Corresponds to variant rs323870 [ dbSNP | Ensembl ].
VAR_056644

Experimental info

Sequence conflict801N → K in AAD29855. Ref.2
Sequence conflict1711G → A in AAD29855. Ref.2
Sequence conflict4111K → E in CAB43246. Ref.6

Secondary structure

......................................................................................... 533
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
Isoform 1 (Short) [UniParc].

Last modified March 3, 2009. Version 3.
Checksum: BF728C3D88722029

FASTA53360,070
        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 

« Hide

Isoform 2 (Long) [UniParc].

Checksum: AF68D80A50A78BC8
Show »

FASTA54060,846

References

« Hide 'large scale' references
[1]Koch-Nolte F.
Submitted (MAR-1998) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2), VARIANT ARG-100.
[2]"A human poly(ADP-ribose) polymerase gene family (ADPRTL): cDNA cloning of two novel poly(ADP-ribose) polymerase homologues."
Johansson M.
Genomics 57:442-445(1999) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), VARIANT ARG-100.
Tissue: Fetal brain.
[3]"PARP-3 localizes preferentially to the daughter centriole and interferes with the G1/S cell cycle progression."
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.
J. Cell Sci. 116:1551-1562(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2), VARIANT ARG-100, SUBCELLULAR LOCATION.
Tissue: Frontal cortex.
[4]"The DNA sequence, annotation and analysis of human chromosome 3."
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. expand/collapse author list , 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.
Nature 440:1194-1198(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[5]"The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
The MGC Project Team
Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1), VARIANT ARG-100.
Tissue: B-cell.
[6]"The full-ORF clone resource of the German cDNA consortium."
Bechtel S., Rosenfelder H., Duda A., Schmidt C.P., Ernst U., Wellenreuther R., Mehrle A., Schuster C., Bahr A., Bloecker H., Heubner D., Hoerlein A., Michel G., Wedler H., Koehrer K., Ottenwaelder B., Poustka A., Wiemann S., Schupp I.
BMC Genomics 8:399-399(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 75-533 (ISOFORM 1), VARIANT ARG-100.
Tissue: Kidney.
[7]"PARP-3 associates with polycomb group bodies and with components of the DNA damage repair machinery."
Rouleau M., McDonald D., Gagne P., Ouellet M.E., Droit A., Hunter J.M., Dutertre S., Prigent C., Hendzel M.J., Poirier G.G.
J. Cell. Biochem. 100:385-401(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, SUBCELLULAR LOCATION, INTERACTION WITH PRKDC; PARP1; EZH2; HDAC1; HDAC2; SUZ12; YY1; LRIG3 AND LIG4.
[8]"Toward a unified nomenclature for mammalian ADP-ribosyltransferases."
Hottiger M.O., Hassa P.O., Luscher B., Schuler H., Koch-Nolte F.
Trends Biochem. Sci. 35:208-219(2010) [PubMed] [Europe PMC] [Abstract]
Cited for: NOMENCLATURE.
[9]"Human poly(ADP-ribose) polymerase 3, catalytic fragment in complex with an inhibitor 3-aminobenzoic acid."
Structural genomics consortium (SGC)
Submitted (APR-2007) to the PDB data bank
Cited for: X-RAY CRYSTALLOGRAPHY (2.3 ANGSTROMS) OF 178-532 IN COMPLEX WITH THE INHIBITOR 3-AMINOBENZOIC ACID.
[10]"Solution structure of the WGR domain from human poly [ADP-ribose] polymerase-3."
RIKEN structural genomics initiative (RSGI)
Submitted (APR-2008) to the PDB data bank
Cited for: STRUCTURE BY NMR OF 41-157.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
Y16836 mRNA. Translation: CAC79988.1.
AF083068 mRNA. Translation: AAD29855.1.
AY126341 mRNA. Translation: AAM95460.1.
AC115284 Genomic DNA. No translation available.
BC014260 mRNA. Translation: AAH14260.1.
AL050034 mRNA. Translation: CAB43246.1.
PIRT08713.
RefSeqNP_001003931.2. NM_001003931.2.
NP_005476.3. NM_005485.4.
XP_005264836.2. XM_005264779.2.
UniGeneHs.271742.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
2EOCNMR-A41-157[»]
3C49X-ray2.80A178-532[»]
3C4HX-ray2.10A178-532[»]
3CE0X-ray2.80A178-532[»]
3FHBX-ray2.30A178-532[»]
4GV0X-ray1.90A178-532[»]
4GV2X-ray1.80A178-532[»]
4GV4X-ray1.80A178-532[»]
4L6ZX-ray2.00A178-532[»]
4L70X-ray2.00A178-532[»]
4L7LX-ray2.10A178-532[»]
4L7NX-ray1.80A178-532[»]
4L7OX-ray2.00A178-532[»]
4L7PX-ray2.30A178-532[»]
4L7RX-ray2.20A178-532[»]
4L7UX-ray2.80A178-532[»]
ProteinModelPortalQ9Y6F1.
SMRQ9Y6F1. Positions 41-157, 178-532.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid115351. 10 interactions.
STRING9606.ENSP00000381740.

Chemistry

BindingDBQ9Y6F1.
ChEMBLCHEMBL5083.

PTM databases

PhosphoSiteQ9Y6F1.

Polymorphism databases

DMDM224471880.

Proteomic databases

PaxDbQ9Y6F1.
PRIDEQ9Y6F1.

Protocols and materials databases

DNASU10039.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000398755; ENSP00000381740; ENSG00000041880. [Q9Y6F1-2]
ENST00000417220; ENSP00000395951; ENSG00000041880. [Q9Y6F1-1]
ENST00000431474; ENSP00000401511; ENSG00000041880. [Q9Y6F1-1]
GeneID10039.
KEGGhsa:10039.
UCSCuc003dby.3. human. [Q9Y6F1-1]
uc003dbz.3. human. [Q9Y6F1-2]

Organism-specific databases

CTD10039.
GeneCardsGC03P051951.
HGNCHGNC:273. PARP3.
MIM607726. gene.
neXtProtNX_Q9Y6F1.
PharmGKBPA24593.
GenAtlasSearch...

Phylogenomic databases

eggNOGNOG243963.
HOGENOMHOG000173055.
HOVERGENHBG053514.
InParanoidQ9Y6F1.
KOK10798.
OMAFSKEMFK.
OrthoDBEOG7RV9G0.
PhylomeDBQ9Y6F1.
TreeFamTF315407.

Enzyme and pathway databases

BRENDA2.4.2.30. 2681.
SignaLinkQ9Y6F1.

Gene expression databases

ArrayExpressQ9Y6F1.
BgeeQ9Y6F1.
CleanExHS_PARP3.
GenevestigatorQ9Y6F1.

Family and domain databases

Gene3D1.20.142.10. 1 hit.
2.20.140.10. 1 hit.
3.90.228.10. 1 hit.
InterProIPR012317. Poly(ADP-ribose)pol_cat_dom.
IPR004102. Poly(ADP-ribose)pol_reg_dom.
IPR008893. WGR_domain.
[Graphical view]
PfamPF00644. PARP. 1 hit.
PF02877. PARP_reg. 1 hit.
PF05406. WGR. 1 hit.
[Graphical view]
SMARTSM00773. WGR. 1 hit.
[Graphical view]
SUPFAMSSF142921. SSF142921. 1 hit.
SSF47587. SSF47587. 1 hit.
PROSITEPS51060. PARP_ALPHA_HD. 1 hit.
PS51059. PARP_CATALYTIC. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

EvolutionaryTraceQ9Y6F1.
GeneWikiPARP3.
GenomeRNAi10039.
NextBio37913.
PROQ9Y6F1.
SOURCESearch...

Entry information

Entry namePARP3_HUMAN
AccessionPrimary (citable) accession number: Q9Y6F1
Secondary accession number(s): Q8NER9, Q96CG2, Q9UG81
Entry history
Integrated into UniProtKB/Swiss-Prot: September 26, 2001
Last sequence update: March 3, 2009
Last modified: April 16, 2014
This is version 138 of the entry and version 3 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

Relevant documents

SIMILARITY comments

Index of protein domains and families

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

MIM cross-references

Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot

Human polymorphisms and disease mutations

Index of human polymorphisms and disease mutations

Human entries with polymorphisms or disease mutations

List of human entries with polymorphisms or disease mutations

Human chromosome 3

Human chromosome 3: entries, gene names and cross-references to MIM