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Protein

Poly [ADP-ribose] polymerase 3

Gene

PARP3

Organism
Homo sapiens (Human)
Status
Reviewed-Annotation score: -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
  • negative regulation of telomerase RNA reverse transcriptase activity Source: BHF-UCL
  • 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

Keywordsi

Molecular functionGlycosyltransferase, Transferase
LigandNAD

Enzyme and pathway databases

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

EuPathDBiHostDB:ENSG00000041880.14
HGNCiHGNC:273 PARP3
MIMi607726 gene
neXtProtiNX_Q9Y6F1

Subcellular locationi

Extracellular region or secreted Cytosol Plasma membrane Cytoskeleton Lysosome Endosome Peroxisome ER Golgi apparatus Nucleus Mitochondrion Manual annotation Automatic computational assertionGraphics by Christian Stolte; Source: COMPARTMENTS

Keywords - Cellular componenti

Cytoplasm, Cytoskeleton, Nucleus

Pathology & Biotechi

Organism-specific databases

DisGeNETi10039
OpenTargetsiENSG00000041880
PharmGKBiPA24593

Chemistry databases

ChEMBLiCHEMBL5083
DrugBankiDB09074 Olaparib
DB12332 Rucaparib
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

EPDiQ9Y6F1
PaxDbiQ9Y6F1
PeptideAtlasiQ9Y6F1
PRIDEiQ9Y6F1
ProteomicsDBi86661
86662 [Q9Y6F1-2]

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, 13 interactors
IntActiQ9Y6F1, 5 interactors
STRINGi9606.ENSP00000381740

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

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.

Phylogenomic databases

eggNOGiKOG1037 Eukaryota
ENOG410XP18 LUCA
GeneTreeiENSGT00390000017341
HOGENOMiHOG000173055
HOVERGENiHBG053514
InParanoidiQ9Y6F1
KOiK10798
OMAiLIYQESQ
OrthoDBiEOG091G06SC
PhylomeDBiQ9Y6F1
TreeFamiTF315407

Family and domain databases

Gene3Di1.20.142.10, 1 hit
2.20.140.10, 1 hit
InterProiView protein in InterPro
IPR031275 PARP3
IPR012317 Poly(ADP-ribose)pol_cat_dom
IPR004102 Poly(ADP-ribose)pol_reg_dom
IPR036616 Poly(ADP-ribose)pol_reg_dom_sf
IPR036930 WGR_dom_sf
IPR008893 WGR_domain
PANTHERiPTHR10459:SF66 PTHR10459:SF66, 1 hit
PfamiView protein in Pfam
PF00644 PARP, 1 hit
PF02877 PARP_reg, 1 hit
PF05406 WGR, 1 hit
SMARTiView protein in SMART
SM00773 WGR, 1 hit
SUPFAMiSSF142921 SSF142921, 1 hit
SSF47587 SSF47587, 1 hit
PROSITEiView protein in PROSITE
PS51060 PARP_ALPHA_HD, 1 hit
PS51059 PARP_CATALYTIC, 1 hit

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 SNRFFTCWNR
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 isoform.1 Publication
Length:533
Mass (Da):60,089
Last modified:September 27, 2017 - v4
Checksum:i6296A0E439CC7767
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):60,865
Checksum:i728CF4D3E119DC86
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 dbSNP:rs34224216Ensembl.1
Natural variantiVAR_054622100R → H. Corresponds to variant dbSNP:rs28547534Ensembl.1
Natural variantiVAR_056644269Q → R. Corresponds to variant dbSNP:rs323870Ensembl.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 [Q9Y6F1-2]
NP_005476.4, NM_005485.5 [Q9Y6F1-1]
XP_005264836.2, XM_005264779.4 [Q9Y6F1-1]
XP_016860979.1, XM_017005490.1 [Q9Y6F1-1]
UniGeneiHs.271742

Genome annotation databases

EnsembliENST00000398755; ENSP00000381740; ENSG00000041880 [Q9Y6F1-2]
ENST00000417220; ENSP00000395951; ENSG00000041880 [Q9Y6F1-1]
ENST00000431474; ENSP00000401511; ENSG00000041880 [Q9Y6F1-1]
GeneIDi10039
KEGGihsa:10039
UCSCiuc003dbz.4 human [Q9Y6F1-1]

Keywords - Coding sequence diversityi

Alternative splicing, Polymorphism

Similar proteinsi

Entry informationi

Entry nameiPARP3_HUMAN
AccessioniPrimary (citable) accession number: Q9Y6F1
Secondary accession number(s): Q8NER9, Q96CG2, Q9UG81
Entry historyiIntegrated into UniProtKB/Swiss-Prot: September 26, 2001
Last sequence update: September 27, 2017
Last modified: July 18, 2018
This is version 177 of the entry and version 4 of the sequence. See 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

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