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Protein

Poly [ADP-ribose] polymerase 3

Gene

PARP3

Organism
Homo sapiens (Human)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

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.1 Publication

Catalytic activityi

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

GO - Molecular functioni

  • catalytic activity Source: ProtInc
  • DNA ligase (ATP) activity Source: GO_Central
  • NAD+ ADP-ribosyltransferase activity Source: MGI

GO - Biological processi

  • DNA ligation involved in DNA repair Source: GO_Central
  • DNA repair Source: ProtInc
  • double-strand break repair Source: MGI
  • lagging strand elongation Source: GO_Central
  • positive regulation of DNA ligation Source: MGI
  • protein ADP-ribosylation Source: MGI
  • protein localization to site of double-strand break Source: MGI
  • regulation of mitotic spindle organization Source: MGI
  • telomere maintenance Source: MGI
Complete GO annotation...

Keywords - Molecular functioni

Glycosyltransferase, Transferase

Keywords - Ligandi

NAD

Enzyme and pathway databases

BioCyciZFISH:HS00555-MONOMER.
BRENDAi2.4.2.30. 2681.
SignaLinkiQ9Y6F1.

Names & Taxonomyi

Protein namesi
Recommended name:
Poly [ADP-ribose] polymerase 3 (EC:2.4.2.30)
Short name:
PARP-3
Short name:
hPARP-3
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 namesi
Name:PARP3
Synonyms:ADPRT3, ADPRTL3
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
Proteomesi
  • UP000005640 Componenti: Chromosome 3

Organism-specific databases

HGNCiHGNC:273. PARP3.

Subcellular locationi

GO - Cellular componenti

  • centriole Source: UniProtKB-SubCell
  • cytoplasm Source: GO_Central
  • nucleus Source: UniProtKB-SubCell
  • site of double-strand break Source: MGI
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm, Cytoskeleton, Nucleus

Pathology & Biotechi

Organism-specific databases

DisGeNETi10039.
PharmGKBiPA24593.

Chemistry databases

ChEMBLiCHEMBL5083.
DrugBankiDB09074. Olaparib.
GuidetoPHARMACOLOGYi2864.

Polymorphism and mutation databases

BioMutaiPARP3.
DMDMi224471880.

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00002113291 – 533Poly [ADP-ribose] polymerase 3Add BLAST533

Post-translational modificationi

Auto-poly(ADP)-ribosylation.

Proteomic databases

PaxDbiQ9Y6F1.
PeptideAtlasiQ9Y6F1.
PRIDEiQ9Y6F1.

PTM databases

iPTMnetiQ9Y6F1.
PhosphoSitePlusiQ9Y6F1.

Expressioni

Tissue specificityi

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.

Gene expression databases

BgeeiENSG00000041880.
CleanExiHS_PARP3.
ExpressionAtlasiQ9Y6F1. baseline and differential.
GenevisibleiQ9Y6F1. HS.

Organism-specific databases

HPAiHPA067657.

Interactioni

Subunit structurei

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 LIG4.2 Publications

Protein-protein interaction databases

BioGridi115351. 8 interactors.
STRINGi9606.ENSP00000381740.

Chemistry databases

BindingDBiQ9Y6F1.

Structurei

Secondary structure

1533
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Beta strandi50 – 53Combined sources4
Turni54 – 56Combined sources3
Beta strandi61 – 74Combined sources14
Turni75 – 78Combined sources4
Beta strandi79 – 89Combined sources11
Beta strandi95 – 100Combined sources6
Beta strandi111 – 117Combined sources7
Helixi118 – 133Combined sources16
Helixi140 – 142Combined sources3
Beta strandi147 – 149Combined sources3
Beta strandi151 – 153Combined sources3
Helixi187 – 196Combined sources10
Helixi199 – 208Combined sources10
Turni213 – 215Combined sources3
Turni218 – 220Combined sources3
Helixi223 – 240Combined sources18
Beta strandi246 – 248Combined sources3
Helixi250 – 260Combined sources11
Beta strandi265 – 268Combined sources4
Helixi276 – 298Combined sources23
Helixi303 – 307Combined sources5
Beta strandi309 – 311Combined sources3
Helixi314 – 321Combined sources8
Beta strandi325 – 328Combined sources4
Helixi336 – 346Combined sources11
Beta strandi349 – 351Combined sources3
Beta strandi354 – 362Combined sources9
Turni364 – 366Combined sources3
Helixi367 – 371Combined sources5
Turni372 – 375Combined sources4
Beta strandi379 – 385Combined sources7
Helixi388 – 390Combined sources3
Helixi391 – 397Combined sources7
Beta strandi411 – 418Combined sources8
Helixi419 – 423Combined sources5
Beta strandi429 – 431Combined sources3
Beta strandi434 – 445Combined sources12
Beta strandi448 – 454Combined sources7
Beta strandi467 – 471Combined sources5
Beta strandi473 – 477Combined sources5
Helixi479 – 481Combined sources3
Beta strandi483 – 487Combined sources5
Beta strandi490 – 494Combined sources5
Beta strandi499 – 501Combined sources3
Helixi503 – 505Combined sources3
Beta strandi509 – 512Combined sources4
Beta strandi514 – 519Combined sources6
Helixi520 – 522Combined sources3
Beta strandi523 – 532Combined sources10

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB 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[»]
ProteinModelPortaliQ9Y6F1.
SMRiQ9Y6F1.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiQ9Y6F1.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Domaini182 – 300PARP alpha-helicalPROSITE-ProRule annotationAdd BLAST119
Domaini313 – 533PARP catalyticPROSITE-ProRule annotationAdd BLAST221

Motif

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Motifi14 – 20Nuclear localization signalSequence analysis7

Domaini

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.

Sequence similaritiesi

Contains 1 PARP alpha-helical domain.PROSITE-ProRule annotation
Contains 1 PARP catalytic domain.PROSITE-ProRule annotation

Phylogenomic databases

eggNOGiKOG1037. Eukaryota.
ENOG410XP18. LUCA.
HOGENOMiHOG000173055.
HOVERGENiHBG053514.
InParanoidiQ9Y6F1.
KOiK10798.
OrthoDBiEOG091G06SC.
PhylomeDBiQ9Y6F1.
TreeFamiTF315407.

Family and domain databases

Gene3Di1.20.142.10. 1 hit.
2.20.140.10. 1 hit.
3.90.228.10. 1 hit.
InterProiIPR031275. PARP3.
IPR012317. Poly(ADP-ribose)pol_cat_dom.
IPR004102. Poly(ADP-ribose)pol_reg_dom.
IPR008893. WGR_domain.
[Graphical view]
PANTHERiPTHR10459:SF66. PTHR10459:SF66. 1 hit.
PfamiPF00644. PARP. 1 hit.
PF02877. PARP_reg. 1 hit.
PF05406. WGR. 1 hit.
[Graphical view]
SMARTiSM00773. WGR. 1 hit.
[Graphical view]
SUPFAMiSSF142921. SSF142921. 1 hit.
SSF47587. SSF47587. 1 hit.
PROSITEiPS51060. PARP_ALPHA_HD. 1 hit.
PS51059. PARP_CATALYTIC. 1 hit.
[Graphical view]

Sequences (2)i

Sequence statusi: Complete.

This entry describes 2 isoformsi produced by alternative splicing. AlignAdd to basket

Isoform 1 (identifier: Q9Y6F1-1) [UniParc]FASTAAdd to basket
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.

« Hide

        10         20         30         40         50
MAPKPKPWVQ TEGPEKKKGR QAGREEDPFR STAEALKAIP AEKRIIRVDP
60 70 80 90 100
TCPLSSNPGT QVYEDYNCTL NQTNIENNNN KFYIIQLLQD SNRFFTCWNH
110 120 130 140 150
WGRVGEVGQS KINHFTRLED AKKDFEKKFR EKTKNNWAER DHFVSHPGKY
160 170 180 190 200
TLIEVQAEDE AQEAVVKVDR GPVRTVTKRV QPCSLDPATQ KLITNIFSKE
210 220 230 240 250
MFKNTMALMD LDVKKMPLGK LSKQQIARGF EALEALEEAL KGPTDGGQSL
260 270 280 290 300
EELSSHFYTV IPHNFGHSQP PPINSPELLQ AKKDMLLVLA DIELAQALQA
310 320 330 340 350
VSEQEKTVEE VPHPLDRDYQ LLKCQLQLLD SGAPEYKVIQ TYLEQTGSNH
360 370 380 390 400
RCPTLQHIWK VNQEGEEDRF QAHSKLGNRK LLWHGTNMAV VAAILTSGLR
410 420 430 440 450
IMPHSGGRVG KGIYFASENS KSAGYVIGMK CGAHHVGYMF LGEVALGREH
460 470 480 490 500
HINTDNPSLK SPPPGFDSVI ARGHTEPDPT QDTELELDGQ QVVVPQGQPV
510 520 530
PCPEFSSSTF SQSEYLIYQE SQCRLRYLLE VHL
Note: More abundant according to PubMed:16924674.
Length:533
Mass (Da):60,070
Last modified:March 3, 2009 - v3
Checksum:iBF728C3D88722029
GO
Isoform 2 (identifier: Q9Y6F1-2) [UniParc]FASTAAdd to basket
Also known as: Long

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

Show »
Length:540
Mass (Da):60,846
Checksum:iAF68D80A50A78BC8
GO

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sequence conflicti80N → K in AAD29855 (PubMed:10329013).Curated1
Sequence conflicti171G → A in AAD29855 (PubMed:10329013).Curated1
Sequence conflicti411K → E in CAB43246 (PubMed:17974005).Curated1

Natural variant

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Natural variantiVAR_05664391S → N.Corresponds to variant rs34224216dbSNPEnsembl.1
Natural variantiVAR_054622100H → R.5 PublicationsCorresponds to variant rs28547534dbSNPEnsembl.1
Natural variantiVAR_056644269Q → R.Corresponds to variant rs323870dbSNPEnsembl.1

Alternative sequence

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Alternative sequenceiVSP_0078631M → MSLLFLAM in isoform 2. 2 Publications1

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
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.
CCDSiCCDS43097.1. [Q9Y6F1-1]
CCDS46839.1. [Q9Y6F1-2]
PIRiT08713.
RefSeqiNP_001003931.3. NM_001003931.3.
NP_005476.4. NM_005485.5.
XP_005264836.2. XM_005264779.4.
XP_016860979.1. XM_017005490.1.
UniGeneiHs.271742.

Genome annotation databases

EnsembliENST00000398755; ENSP00000381740; ENSG00000041880.
GeneIDi10039.
KEGGihsa:10039.
UCSCiuc003dbz.4. human. [Q9Y6F1-1]

Keywords - Coding sequence diversityi

Alternative splicing, Polymorphism

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
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.
CCDSiCCDS43097.1. [Q9Y6F1-1]
CCDS46839.1. [Q9Y6F1-2]
PIRiT08713.
RefSeqiNP_001003931.3. NM_001003931.3.
NP_005476.4. NM_005485.5.
XP_005264836.2. XM_005264779.4.
XP_016860979.1. XM_017005490.1.
UniGeneiHs.271742.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB 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[»]
ProteinModelPortaliQ9Y6F1.
SMRiQ9Y6F1.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi115351. 8 interactors.
STRINGi9606.ENSP00000381740.

Chemistry databases

BindingDBiQ9Y6F1.
ChEMBLiCHEMBL5083.
DrugBankiDB09074. Olaparib.
GuidetoPHARMACOLOGYi2864.

PTM databases

iPTMnetiQ9Y6F1.
PhosphoSitePlusiQ9Y6F1.

Polymorphism and mutation databases

BioMutaiPARP3.
DMDMi224471880.

Proteomic databases

PaxDbiQ9Y6F1.
PeptideAtlasiQ9Y6F1.
PRIDEiQ9Y6F1.

Protocols and materials databases

DNASUi10039.
Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000398755; ENSP00000381740; ENSG00000041880.
GeneIDi10039.
KEGGihsa:10039.
UCSCiuc003dbz.4. human. [Q9Y6F1-1]

Organism-specific databases

CTDi10039.
DisGeNETi10039.
GeneCardsiPARP3.
HGNCiHGNC:273. PARP3.
HPAiHPA067657.
MIMi607726. gene.
neXtProtiNX_Q9Y6F1.
PharmGKBiPA24593.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiKOG1037. Eukaryota.
ENOG410XP18. LUCA.
HOGENOMiHOG000173055.
HOVERGENiHBG053514.
InParanoidiQ9Y6F1.
KOiK10798.
OrthoDBiEOG091G06SC.
PhylomeDBiQ9Y6F1.
TreeFamiTF315407.

Enzyme and pathway databases

BioCyciZFISH:HS00555-MONOMER.
BRENDAi2.4.2.30. 2681.
SignaLinkiQ9Y6F1.

Miscellaneous databases

EvolutionaryTraceiQ9Y6F1.
GeneWikiiPARP3.
GenomeRNAii10039.
PROiQ9Y6F1.
SOURCEiSearch...

Gene expression databases

BgeeiENSG00000041880.
CleanExiHS_PARP3.
ExpressionAtlasiQ9Y6F1. baseline and differential.
GenevisibleiQ9Y6F1. HS.

Family and domain databases

Gene3Di1.20.142.10. 1 hit.
2.20.140.10. 1 hit.
3.90.228.10. 1 hit.
InterProiIPR031275. PARP3.
IPR012317. Poly(ADP-ribose)pol_cat_dom.
IPR004102. Poly(ADP-ribose)pol_reg_dom.
IPR008893. WGR_domain.
[Graphical view]
PANTHERiPTHR10459:SF66. PTHR10459:SF66. 1 hit.
PfamiPF00644. PARP. 1 hit.
PF02877. PARP_reg. 1 hit.
PF05406. WGR. 1 hit.
[Graphical view]
SMARTiSM00773. WGR. 1 hit.
[Graphical view]
SUPFAMiSSF142921. SSF142921. 1 hit.
SSF47587. SSF47587. 1 hit.
PROSITEiPS51060. PARP_ALPHA_HD. 1 hit.
PS51059. PARP_CATALYTIC. 1 hit.
[Graphical view]
ProtoNetiSearch...

Entry informationi

Entry nameiPARP3_HUMAN
AccessioniPrimary (citable) accession number: Q9Y6F1
Secondary accession number(s): Q8NER9, Q96CG2, Q9UG81
Entry historyi
Integrated into UniProtKB/Swiss-Prot: September 26, 2001
Last sequence update: March 3, 2009
Last modified: November 2, 2016
This is version 163 of the entry and version 3 of the sequence. [Complete history]
Entry statusiReviewed (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.

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

Documents

  1. Human chromosome 3
    Human chromosome 3: entries, gene names and cross-references to MIM
  2. Human entries with polymorphisms or disease mutations
    List of human entries with polymorphisms or disease mutations
  3. Human polymorphisms and disease mutations
    Index of human polymorphisms and disease mutations
  4. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  5. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  6. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.