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Protein

Poly [ADP-ribose] polymerase 1

Gene

PARP1

Organism
Cricetulus griseus (Chinese hamster) (Cricetulus barabensis griseus)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at transcript 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. Mediates the poly(ADP-ribosyl)ation of APLF and CHFR. Positively regulates the transcription of MTUS1 and negatively regulates the transcription of MTUS2/TIP150. With EEF1A1 and TXK, forms a complex that acts as a T-helper 1 (Th1) cell-specific transcription factor and binds the promoter of IFN-gamma to directly regulate its transcription, and is thus involved importantly in Th1 cytokine production (By similarity). Required for PARP9 and DTX3L recruitment to DNA damage sites. PARP1-dependent PARP9-DTX3L-mediated ubiquitination promotes the rapid and specific recruitment of 53BP1/TP53BP1, UIMC1/RAP80, and BRCA1 to DNA damage sites (By similarity).By similarity

Catalytic activityi

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

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
DNA bindingi2 – 372371By similarityAdd
BLAST
Zinc fingeri9 – 9385PARP-type 1PROSITE-ProRule annotationAdd
BLAST
Zinc fingeri113 – 20391PARP-type 2PROSITE-ProRule annotationAdd
BLAST

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Glycosyltransferase, Transferase

Keywords - Biological processi

DNA damage, DNA repair, Transcription, Transcription regulation

Keywords - Ligandi

DNA-binding, Metal-binding, NAD, Zinc

Names & Taxonomyi

Protein namesi
Recommended name:
Poly [ADP-ribose] polymerase 1 (EC:2.4.2.30)
Short name:
PARP-1
Alternative name(s):
ADP-ribosyltransferase diphtheria toxin-like 1
Short name:
ARTD1
NAD(+) ADP-ribosyltransferase 1
Short name:
ADPRT 1
Poly[ADP-ribose] synthase 1
Gene namesi
Name:PARP1
Synonyms:ADPRT
OrganismiCricetulus griseus (Chinese hamster) (Cricetulus barabensis griseus)
Taxonomic identifieri10029 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaCricetidaeCricetinaeCricetulus

Subcellular locationi

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Nucleus

Pathology & Biotechi

Chemistry

ChEMBLiCHEMBL2321638.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Initiator methionineiRemovedBy similarity
Chaini2 – 10131012Poly [ADP-ribose] polymerase 1PRO_0000211319Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei2 – 21N-acetylalanineBy similarity
Modified residuei41 – 411PhosphoserineBy similarity
Modified residuei97 – 971N6-acetyllysineBy similarity
Modified residuei105 – 1051N6-acetyllysineBy similarity
Modified residuei131 – 1311N6-acetyllysineBy similarity
Modified residuei179 – 1791PhosphoserineBy similarity
Cross-linki203 – 203Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)By similarity
Modified residuei407 – 4071PolyADP-ribosyl glutamic acidSequence analysis
Modified residuei413 – 4131PolyADP-ribosyl glutamic acidSequence analysis
Modified residuei435 – 4351PolyADP-ribosyl glutamic acidSequence analysis
Modified residuei437 – 4371PolyADP-ribosyl glutamic acidSequence analysis
Modified residuei444 – 4441PolyADP-ribosyl glutamic acidSequence analysis
Modified residuei445 – 4451PolyADP-ribosyl glutamic acidSequence analysis
Modified residuei456 – 4561PolyADP-ribosyl glutamic acidSequence analysis
Cross-linki467 – 467Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)By similarity
Modified residuei471 – 4711PolyADP-ribosyl glutamic acidSequence analysis
Modified residuei484 – 4841PolyADP-ribosyl glutamic acidSequence analysis
Cross-linki486 – 486Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)By similarity
Modified residuei488 – 4881PolyADP-ribosyl glutamic acidSequence analysis
Modified residuei491 – 4911PolyADP-ribosyl glutamic acidSequence analysis
Cross-linki511 – 511Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)By similarity
Modified residuei512 – 5121PolyADP-ribosyl glutamic acidSequence analysis
Modified residuei513 – 5131PolyADP-ribosyl glutamic acidSequence analysis
Modified residuei519 – 5191PolyADP-ribosyl glutamic acidSequence analysis
Modified residuei599 – 5991N6-acetyllysineBy similarity
Modified residuei620 – 6201N6-acetyllysineBy similarity
Cross-linki747 – 747Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)By similarity
Modified residuei781 – 7811PhosphoserineBy similarity

Post-translational modificationi

Phosphorylated by PRKDC and TXK.
Poly-ADP-ribosylated by PARP2. Poly-ADP-ribosylation mediates the recruitment of CHD1L to DNA damage sites (By similarity).By similarity
S-nitrosylated, leading to inhibit transcription regulation activity.By similarity

Keywords - PTMi

Acetylation, ADP-ribosylation, Isopeptide bond, Phosphoprotein, Ubl conjugation

Proteomic databases

PRIDEiQ9R152.

Interactioni

Subunit structurei

Component of a base excision repair (BER) complex, containing at least XRCC1, PARP2, POLB and LRIG3. Homo- and heterodimer with PARP2. Interacts with PARP3 and APTX. The SWAP complex consists of NPM1, NCL, PARP1, SWAP70 and SRY. Interacts with TIAM2 and ZNF423. Interacts (when poly-ADP-ribosylated) with CHD1L. Interacts with EEF1A1, RNF4 and TXK. Interacts with RNF146. Interacts with SNAI1 (via zinc fingers); the interaction requires SNAI1 to be poly-ADP-ribosylated and non-phosphorylated (active) by GSK3B. Interacts (when poly-ADP-ribosylated) with PARP9. Interacts with NR4A3; activates PARP1 by improving acetylation of PARP1 and suppressing the interaction between PARP1 and SIRT1. Interacts (via catalytic domain) with PUM3; the interaction inhibits the poly(ADP-ribosyl)ation activity of PARP1 and the degradation of PARP1 by CASP3 following genotoxic stress.By similarity

Structurei

3D structure databases

ProteinModelPortaliQ9R152.
SMRiQ9R152. Positions 1-93, 105-359, 381-489, 519-642, 661-1010.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini385 – 47692BRCTPROSITE-ProRule annotationAdd
BLAST
Domaini661 – 778118PARP alpha-helicalPROSITE-ProRule annotationAdd
BLAST
Domaini787 – 1013227PARP catalyticPROSITE-ProRule annotationAdd
BLAST

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni373 – 523151Automodification domainBy similarityAdd
BLAST

Motif

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Motifi207 – 2093Nuclear localization signalSequence analysis
Motifi221 – 2266Nuclear localization signalSequence analysis

Sequence similaritiesi

Contains 1 BRCT domain.PROSITE-ProRule annotation
Contains 1 PARP alpha-helical domain.PROSITE-ProRule annotation
Contains 1 PARP catalytic domain.PROSITE-ProRule annotation
Contains 2 PARP-type zinc fingers.PROSITE-ProRule annotation

Zinc finger

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Zinc fingeri9 – 9385PARP-type 1PROSITE-ProRule annotationAdd
BLAST
Zinc fingeri113 – 20391PARP-type 2PROSITE-ProRule annotationAdd
BLAST

Keywords - Domaini

Repeat, Zinc-finger

Phylogenomic databases

HOVERGENiHBG053513.
KOiK10798.

Family and domain databases

Gene3Di1.20.142.10. 1 hit.
2.20.140.10. 1 hit.
3.30.1740.10. 2 hits.
3.40.50.10190. 1 hit.
3.90.228.10. 1 hit.
InterProiIPR001357. BRCT_dom.
IPR012982. PADR1.
IPR008288. PARP.
IPR012317. Poly(ADP-ribose)pol_cat_dom.
IPR004102. Poly(ADP-ribose)pol_reg_dom.
IPR008893. WGR_domain.
IPR001510. Znf_PARP.
[Graphical view]
PfamiPF00533. BRCT. 1 hit.
PF08063. PADR1. 1 hit.
PF00644. PARP. 1 hit.
PF02877. PARP_reg. 1 hit.
PF05406. WGR. 1 hit.
PF00645. zf-PARP. 2 hits.
[Graphical view]
PIRSFiPIRSF000489. NAD_ADPRT. 1 hit.
SMARTiSM00292. BRCT. 1 hit.
SM01335. PADR1. 1 hit.
SM00773. WGR. 1 hit.
SM01336. zf-PARP. 2 hits.
[Graphical view]
SUPFAMiSSF142921. SSF142921. 1 hit.
SSF47587. SSF47587. 1 hit.
SSF52113. SSF52113. 1 hit.
PROSITEiPS50172. BRCT. 1 hit.
PS51060. PARP_ALPHA_HD. 1 hit.
PS51059. PARP_CATALYTIC. 1 hit.
PS00347. PARP_ZN_FINGER_1. 2 hits.
PS50064. PARP_ZN_FINGER_2. 2 hits.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

Q9R152-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MAEASERLYR VEYAKSGRAS CKKCSESIPK DSLRMAIMVQ SPMFDGKVPH
60 70 80 90 100
WYHFSCFWKV GHSIRQPDVE VDGFSELRWD DQQKVKKTAE AGGVAGKGQD
110 120 130 140 150
GSGGKSEKTL GDFAAEYAKS NRSTCKGCME KIEKGQVRLS KKMLDPEKPQ
160 170 180 190 200
LGMIDRWYHP TCFVKNREEL GFRPEYSASQ LKGFSLLSAE DKEVLKKQLP
210 220 230 240 250
GVKSEGKRKG DEVDGADEVA KKKSKKGKDK DSKLEKALKA QNDLIWNIKD
260 270 280 290 300
ELKKACSTSD LKELLIFNQQ QVPSGESAIL DRVADGMAFG ALLPCKECSG
310 320 330 340 350
QLVFKSDAYY CTGDVTAWTK CMVKTQTPSR KEWVTPKEFR EISYLKKLKV
360 370 380 390 400
KKQDRIFPPE TSAPAPPHLP PSVTSAPTAV NSSCPADKPL SNMKILTLGK
410 420 430 440 450
LSQSKDEAKA TIEKLGGKLT GSANNASLCI STKKEVEKMG KKMEEVQAAN
460 470 480 490 500
VRVVCEDFLQ DVAASTKSLQ ELLSAHSLSS WGAEVKVEPV EVAAPKGKSA
510 520 530 540 550
APSKKSKGLY KEEGVNKSEK RMKLTLKGGA AVDPDSGLEH SAHVLEKGGK
560 570 580 590 600
VFSATLGLVD IVKGTNSYYK LQLLEDDKES RYWIFRSWGR VGTVIGSNKL
610 620 630 640 650
EQMPSKEDAV EHFMKLYEEK TGNAWHSKNF TKYPKKFYPL EIDYGQDEEA
660 670 680 690 700
VKKLTVKPGT KSKLPKAVQE LVGMIFDVES MKKALVEYEI DLQKMPLGKL
710 720 730 740 750
SKRQIQAAYS ILSEVQQAVS QGSSDSQILD LSNRFYTLIP HDFGMKKPPL
760 770 780 790 800
LNNADSVQAK VEMLDNLLDI EVAYSLLRGG SDDSSKDPID VNYEKLKTDI
810 820 830 840 850
KVVDRDSEEA EVIRKYVKNT HATTHNAYDL EVMDIFKIER EGESQRYKPF
860 870 880 890 900
KQLHNRRLLW HGSRTTNFAG ILSQGLRIAP PEAPVTGYMF GKGIYFADMV
910 920 930 940 950
SKSANYCHTS QGDPIGLILL GEVALGNMYE LKHASHISKL PKGKHSVKGL
960 970 980 990 1000
GKTTPDPSAS ITLEGVEVPL GTGIPSGVND TCLLYNEYIV YDIAQVNLKY
1010
LLKLKFNFKT SLW
Length:1,013
Mass (Da):112,532
Last modified:January 23, 2007 - v3
Checksum:i90617C4DB91C9DEC
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF168781 mRNA. Translation: AAD45817.1.
RefSeqiNP_001233650.1. NM_001246721.1.

Genome annotation databases

GeneIDi100689463.
KEGGicge:100689463.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF168781 mRNA. Translation: AAD45817.1.
RefSeqiNP_001233650.1. NM_001246721.1.

3D structure databases

ProteinModelPortaliQ9R152.
SMRiQ9R152. Positions 1-93, 105-359, 381-489, 519-642, 661-1010.
ModBaseiSearch...
MobiDBiSearch...

Chemistry

ChEMBLiCHEMBL2321638.

Proteomic databases

PRIDEiQ9R152.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

GeneIDi100689463.
KEGGicge:100689463.

Organism-specific databases

CTDi142.

Phylogenomic databases

HOVERGENiHBG053513.
KOiK10798.

Miscellaneous databases

PROiQ9R152.

Family and domain databases

Gene3Di1.20.142.10. 1 hit.
2.20.140.10. 1 hit.
3.30.1740.10. 2 hits.
3.40.50.10190. 1 hit.
3.90.228.10. 1 hit.
InterProiIPR001357. BRCT_dom.
IPR012982. PADR1.
IPR008288. PARP.
IPR012317. Poly(ADP-ribose)pol_cat_dom.
IPR004102. Poly(ADP-ribose)pol_reg_dom.
IPR008893. WGR_domain.
IPR001510. Znf_PARP.
[Graphical view]
PfamiPF00533. BRCT. 1 hit.
PF08063. PADR1. 1 hit.
PF00644. PARP. 1 hit.
PF02877. PARP_reg. 1 hit.
PF05406. WGR. 1 hit.
PF00645. zf-PARP. 2 hits.
[Graphical view]
PIRSFiPIRSF000489. NAD_ADPRT. 1 hit.
SMARTiSM00292. BRCT. 1 hit.
SM01335. PADR1. 1 hit.
SM00773. WGR. 1 hit.
SM01336. zf-PARP. 2 hits.
[Graphical view]
SUPFAMiSSF142921. SSF142921. 1 hit.
SSF47587. SSF47587. 1 hit.
SSF52113. SSF52113. 1 hit.
PROSITEiPS50172. BRCT. 1 hit.
PS51060. PARP_ALPHA_HD. 1 hit.
PS51059. PARP_CATALYTIC. 1 hit.
PS00347. PARP_ZN_FINGER_1. 2 hits.
PS50064. PARP_ZN_FINGER_2. 2 hits.
[Graphical view]
ProtoNetiSearch...

Publicationsi

  1. "Suppression of the radiation-sensitive phenotype of hamster irs1 and irs2 strains selected for resistance to 3-aminobenzamide."
    Ganesh A., Phillips E., Thacker J., Meuth M.
    Int. J. Radiat. Biol. 77:609-616(2001) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].

Entry informationi

Entry nameiPARP1_CRIGR
AccessioniPrimary (citable) accession number: Q9R152
Entry historyi
Integrated into UniProtKB/Swiss-Prot: September 26, 2001
Last sequence update: January 23, 2007
Last modified: June 8, 2016
This is version 123 of the entry and version 3 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Miscellaneous

The ADP-D-ribosyl group of NAD+ is transferred to an acceptor carboxyl group on a histone or the enzyme itself, and further ADP-ribosyl groups are transferred to the 2'-position of the terminal adenosine moiety, building up a polymer with an average chain length of 20-30 units.

Documents

  1. 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.