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Protein

Poly [ADP-ribose] polymerase 1

Gene

Parp1

Organism
Rattus norvegicus (Rat)
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. 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. 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. Mediates the poly(ADP-ribosyl)ation of histones in a HPF1-dependent manner. Involved in the synthesis of ATP in the nucleus, together with NMNAT1, PARG and NUDT5. Nuclear ATP generation is required for extensive chromatin remodeling events that are energy-consuming.By similarity

Catalytic activityi

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

Regions

Feature keyPosition(s)DescriptionActionsGraphical viewLength
DNA bindingi2 – 373Add BLAST372
Zinc fingeri9 – 93PARP-type 1PROSITE-ProRule annotationAdd BLAST85
Zinc fingeri113 – 203PARP-type 2PROSITE-ProRule annotationAdd BLAST91

GO - Molecular functioni

  • DNA binding Source: UniProtKB-KW
  • DNA ligase (ATP) activity Source: GO_Central
  • enzyme binding Source: BHF-UCL
  • estrogen receptor binding Source: RGD
  • histone deacetylase binding Source: RGD
  • NAD+ ADP-ribosyltransferase activity Source: BHF-UCL
  • NAD binding Source: RGD
  • poly(A) RNA binding Source: Ensembl
  • R-SMAD binding Source: BHF-UCL
  • SMAD binding Source: RGD
  • transferase activity, transferring pentosyl groups Source: RGD
  • zinc ion binding Source: InterPro

GO - Biological processi

  • ATP generation from poly-ADP-D-ribose Source: UniProtKB
  • cellular response to beta-amyloid Source: RGD
  • cellular response to insulin stimulus Source: Ensembl
  • cellular response to oxidative stress Source: Ensembl
  • cellular response to transforming growth factor beta stimulus Source: RGD
  • cellular response to zinc ion Source: RGD
  • DNA damage response, detection of DNA damage Source: RGD
  • DNA ligation involved in DNA repair Source: GO_Central
  • double-strand break repair Source: UniProtKB
  • lagging strand elongation Source: GO_Central
  • mitochondrial DNA repair Source: Ensembl
  • positive regulation of cardiac muscle hypertrophy Source: UniProtKB
  • positive regulation of intracellular estrogen receptor signaling pathway Source: RGD
  • positive regulation of mitochondrial depolarization Source: RGD
  • positive regulation of myofibroblast differentiation Source: RGD
  • positive regulation of neuron death Source: RGD
  • positive regulation of protein localization to nucleus Source: RGD
  • positive regulation of SMAD protein import into nucleus Source: BHF-UCL
  • positive regulation of transcription from RNA polymerase II promoter Source: BHF-UCL
  • positive regulation of transcription regulatory region DNA binding Source: BHF-UCL
  • protein ADP-ribosylation Source: RGD
  • protein autoprocessing Source: RGD
  • protein poly-ADP-ribosylation Source: BHF-UCL
  • regulation of DNA methylation Source: RGD
  • regulation of oxidative stress-induced neuron intrinsic apoptotic signaling pathway Source: RGD
  • regulation of SMAD protein complex assembly Source: RGD
  • response to aldosterone Source: RGD
  • response to gamma radiation Source: RGD
  • signal transduction involved in regulation of gene expression Source: BHF-UCL
  • transcription, DNA-templated Source: UniProtKB-KW
  • transforming growth factor beta receptor signaling pathway Source: BHF-UCL
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

Enzyme and pathway databases

ReactomeiR-RNO-110362. POLB-Dependent Long Patch Base Excision Repair.
R-RNO-2173795. Downregulation of SMAD2/3:SMAD4 transcriptional activity.
R-RNO-3108214. SUMOylation of DNA damage response and repair proteins.
R-RNO-5685939. HDR through MMEJ (alt-NHEJ).
R-RNO-5696394. DNA Damage Recognition in GG-NER.
R-RNO-5696395. Formation of Incision Complex in GG-NER.
R-RNO-5696400. Dual Incision in GG-NER.

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
OrganismiRattus norvegicus (Rat)
Taxonomic identifieri10116 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeRattus
Proteomesi
  • UP000002494 Componenti: Chromosome 13

Organism-specific databases

RGDi2053. Parp1.

Subcellular locationi

  • Nucleus PROSITE-ProRule annotation
  • Nucleusnucleolus By similarity

  • Note: Localizes at sites of DNA damage.By similarity

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Nucleus

Pathology & Biotechi

Chemistry databases

ChEMBLiCHEMBL4664.

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Initiator methionineiRemovedBy similarity
ChainiPRO_00002113212 – 1014Poly [ADP-ribose] polymerase 1Add BLAST1013

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei2N-acetylalanineBy similarity1
Modified residuei41PhosphoserineBy similarity1
Modified residuei97N6-acetyllysineBy similarity1
Modified residuei105N6-acetyllysineBy similarity1
Modified residuei131N6-acetyllysineBy similarity1
Modified residuei177PhosphoserineBy similarity1
Modified residuei179PhosphoserineBy similarity1
Modified residuei185PhosphoserineBy similarity1
Cross-linki203Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO1)By similarity
Cross-linki203Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)By similarity
Modified residuei275PhosphoserineBy similarity1
Modified residuei278PhosphoserineBy similarity1
Modified residuei408PolyADP-ribosyl glutamic acidSequence analysis1
Modified residuei414PolyADP-ribosyl glutamic acidSequence analysis1
Modified residuei436PolyADP-ribosyl glutamic acidSequence analysis1
Modified residuei438PolyADP-ribosyl glutamic acidSequence analysis1
Modified residuei445PolyADP-ribosyl glutamic acidSequence analysis1
Modified residuei446PolyADP-ribosyl glutamic acidSequence analysis1
Modified residuei457PolyADP-ribosyl glutamic acidSequence analysis1
Cross-linki468Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)By similarity
Modified residuei485PolyADP-ribosyl glutamic acidSequence analysis1
Cross-linki487Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO1)By similarity
Cross-linki487Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)By similarity
Modified residuei489PolyADP-ribosyl glutamic acidSequence analysis1
Modified residuei492PolyADP-ribosyl glutamic acidSequence analysis1
Cross-linki512Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)By similarity
Modified residuei513PolyADP-ribosyl glutamic acidSequence analysis1
Modified residuei514PolyADP-ribosyl glutamic acidSequence analysis1
Modified residuei520PolyADP-ribosyl glutamic acidSequence analysis1
Modified residuei600N6-acetyllysineBy similarity1
Modified residuei621N6-acetyllysineBy similarity1
Cross-linki748Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO1)By similarity
Cross-linki748Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)By similarity
Modified residuei782PhosphoserineBy similarity1
Modified residuei786PhosphoserineBy similarity1

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

PaxDbiP27008.
PRIDEiP27008.

PTM databases

iPTMnetiP27008.
PhosphoSitePlusiP27008.

Expressioni

Gene expression databases

BgeeiENSRNOG00000003084.
GenevisibleiP27008. RN.

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 the DNA polymerase alpha catalytic subunit POLA1; this interaction functions as part of the control of replication fork progression. 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 (By similarity). Interacts (when poly-ADP-ribosylated) with PARP9 (By similarity). Interacts with NR4A3; activates PARP1 by improving acetylation of PARP1 and suppressing the interaction between PARP1 and SIRT1 (PubMed:25625556). 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. Interacts (via the PARP catalytic domain) with HPF1 (By similarity).By similarity1 Publication

GO - Molecular functioni

  • enzyme binding Source: BHF-UCL
  • estrogen receptor binding Source: RGD
  • histone deacetylase binding Source: RGD
  • R-SMAD binding Source: BHF-UCL
  • SMAD binding Source: RGD

Protein-protein interaction databases

BioGridi247621. 16 interactors.
STRINGi10116.ENSRNOP00000004232.

Chemistry databases

BindingDBiP27008.

Structurei

Secondary structure

11014
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Beta strandi394 – 398Combined sources5
Helixi406 – 416Combined sources11
Beta strandi422 – 424Combined sources3
Beta strandi427 – 431Combined sources5
Helixi434 – 439Combined sources6
Helixi442 – 449Combined sources8
Beta strandi453 – 455Combined sources3
Helixi458 – 465Combined sources8
Helixi470 – 476Combined sources7

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
2LE0NMR-A389-487[»]
ProteinModelPortaliP27008.
SMRiP27008.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Domaini386 – 477BRCTPROSITE-ProRule annotationAdd BLAST92
Domaini662 – 779PARP alpha-helicalPROSITE-ProRule annotationAdd BLAST118
Domaini788 – 1014PARP catalyticPROSITE-ProRule annotationAdd BLAST227

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni374 – 524Automodification domainAdd BLAST151

Motif

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Motifi207 – 209Nuclear localization signal3
Motifi221 – 226Nuclear localization signal6

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)DescriptionActionsGraphical viewLength
Zinc fingeri9 – 93PARP-type 1PROSITE-ProRule annotationAdd BLAST85
Zinc fingeri113 – 203PARP-type 2PROSITE-ProRule annotationAdd BLAST91

Keywords - Domaini

Repeat, Zinc-finger

Phylogenomic databases

eggNOGiKOG1037. Eukaryota.
ENOG410XP18. LUCA.
GeneTreeiENSGT00390000017341.
HOGENOMiHOG000030402.
HOVERGENiHBG053513.
InParanoidiP27008.
KOiK10798.
OMAiEIEVAYN.
OrthoDBiEOG091G13H1.
PhylomeDBiP27008.
TreeFamiTF316616.

Family and domain databases

CDDicd00027. BRCT. 1 hit.
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.

P27008-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MAEATERLYR VEYAKSGRAS CKKCSESIPK DSLRMAIMVQ SPMFDGKVPH
60 70 80 90 100
WYHFSCFWKV GHSIRQPDTE VDGFSELRWD DQQKVKKTAE AGGVAGKGQH
110 120 130 140 150
GGGGKAEKTL GDFAAEYAKS NRSTCKGCME KIEKGQMRLS KKMLDPEKPQ
160 170 180 190 200
LGMIDRWYHP TCFVKNRDEL GFRPEYSASQ LKGFSLLSAE DKEALKKQLP
210 220 230 240 250
AVKSEGKRKC DEVDGIDEVA KKKSKKGKDK ESSKLEKALK AQNELVWNIK
260 270 280 290 300
DELKKACSTN DLKELLIFNQ QQVPSGESAI LDRVADGMAF GALLPCKECS
310 320 330 340 350
GQLVFKSDAY YCTGDVTAWT KCMVKTQNPS RKEWVTPKEF REISYLKKLK
360 370 380 390 400
IKKQDRLFPP ESSAPAPPAP PVSITSAPTA VNSSAPADKP LSNMKILTLG
410 420 430 440 450
KLSQNKDEAK AMIEKLGGKL TGSANKASLC ISTKKEVEKM SKKMEEVKAA
460 470 480 490 500
NVRVVCEDFL QDVSASAKSL QELLSAHSLS SWGAEVKVEP GEVVVPKGKS
510 520 530 540 550
AAPSKKSKGA VKEEGVNKSE KRMKLTLKGG AAVDPDSGLE HSAHVLEKGG
560 570 580 590 600
KVFSATLGLV DIVKGTNSYY KLQLLESDKE SRYWIFRSWG RVGTVIGSNK
610 620 630 640 650
LEQMPSKEDA VEHFMKLYEE KTGNAWHSKN FTKYPKKFYP LEIDYGQDEE
660 670 680 690 700
AVKKLAVKPG TKSKLPKPVQ ELVGMIFDVE SMKKALVEYE IDLQKMPLGK
710 720 730 740 750
LSRRQIQAAY SILSEVQQAV SQGSSESQIL DLSNRFYTLI PHDFGMKKPP
760 770 780 790 800
LLNNTDSVQA KVEMLDNLLD IEVAYSLLRG GSDDSSKDPI DVNYEKLKTD
810 820 830 840 850
IKVVDRDSEE AEVIRKYVKN THATTHNAYD LEVIDIFKIE REGESQRYKP
860 870 880 890 900
FRQLHNRRLL WHGSRTTNFA GILSQGLRIA PPEAPVTGYM FGKGIYFADM
910 920 930 940 950
VSKSANYCHT SQGDPIGLIL LGEVALGNMY ELKHASHISK LPKGKHSVKG
960 970 980 990 1000
LGKTAPDPSA SITLDGVEVP LGTGIPSGVN DTCLLYNEYI VYDIAQVNLK
1010
YLLKLKFNFK TSLW
Length:1,014
Mass (Da):112,660
Last modified:January 23, 2007 - v4
Checksum:iBE1B6F2B29B887ED
GO

Sequence cautioni

The sequence CAA46478 differs from that shown. Reason: Erroneous initiation.Curated

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sequence conflicti639Y → H in CAA46478 (PubMed:2508731).Curated1
Sequence conflicti642E → A in CAA46478 (PubMed:2508731).Curated1
Sequence conflicti753N → D in CAA46478 (PubMed:2508731).Curated1

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U94340 mRNA. Translation: AAC53544.1.
BC085765 mRNA. Translation: AAH85765.1.
X65496 Genomic DNA. Translation: CAA46477.1.
X65497 Genomic DNA. Translation: CAA46478.1. Different initiation.
PIRiS21163.
S26057.
RefSeqiNP_037195.1. NM_013063.2.
UniGeneiRn.11327.

Genome annotation databases

EnsembliENSRNOT00000004232; ENSRNOP00000004232; ENSRNOG00000003084.
GeneIDi25591.
KEGGirno:25591.
UCSCiRGD:2053. rat.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U94340 mRNA. Translation: AAC53544.1.
BC085765 mRNA. Translation: AAH85765.1.
X65496 Genomic DNA. Translation: CAA46477.1.
X65497 Genomic DNA. Translation: CAA46478.1. Different initiation.
PIRiS21163.
S26057.
RefSeqiNP_037195.1. NM_013063.2.
UniGeneiRn.11327.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
2LE0NMR-A389-487[»]
ProteinModelPortaliP27008.
SMRiP27008.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi247621. 16 interactors.
STRINGi10116.ENSRNOP00000004232.

Chemistry databases

BindingDBiP27008.
ChEMBLiCHEMBL4664.

PTM databases

iPTMnetiP27008.
PhosphoSitePlusiP27008.

Proteomic databases

PaxDbiP27008.
PRIDEiP27008.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSRNOT00000004232; ENSRNOP00000004232; ENSRNOG00000003084.
GeneIDi25591.
KEGGirno:25591.
UCSCiRGD:2053. rat.

Organism-specific databases

CTDi142.
RGDi2053. Parp1.

Phylogenomic databases

eggNOGiKOG1037. Eukaryota.
ENOG410XP18. LUCA.
GeneTreeiENSGT00390000017341.
HOGENOMiHOG000030402.
HOVERGENiHBG053513.
InParanoidiP27008.
KOiK10798.
OMAiEIEVAYN.
OrthoDBiEOG091G13H1.
PhylomeDBiP27008.
TreeFamiTF316616.

Enzyme and pathway databases

ReactomeiR-RNO-110362. POLB-Dependent Long Patch Base Excision Repair.
R-RNO-2173795. Downregulation of SMAD2/3:SMAD4 transcriptional activity.
R-RNO-3108214. SUMOylation of DNA damage response and repair proteins.
R-RNO-5685939. HDR through MMEJ (alt-NHEJ).
R-RNO-5696394. DNA Damage Recognition in GG-NER.
R-RNO-5696395. Formation of Incision Complex in GG-NER.
R-RNO-5696400. Dual Incision in GG-NER.

Miscellaneous databases

PROiP27008.

Gene expression databases

BgeeiENSRNOG00000003084.
GenevisibleiP27008. RN.

Family and domain databases

CDDicd00027. BRCT. 1 hit.
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...

Entry informationi

Entry nameiPARP1_RAT
AccessioniPrimary (citable) accession number: P27008
Secondary accession number(s): O35937
Entry historyi
Integrated into UniProtKB/Swiss-Prot: August 1, 1992
Last sequence update: January 23, 2007
Last modified: November 30, 2016
This is version 166 of the entry and version 4 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.

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

Documents

  1. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  2. 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.