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P27008 (PARP1_RAT) Reviewed, UniProtKB/Swiss-Prot

Last modified May 14, 2014. Version 143. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Poly [ADP-ribose] polymerase 1

Short name=PARP-1
EC=2.4.2.30
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 names
Name:Parp1
Synonyms:Adprt
OrganismRattus norvegicus (Rat) [Reference proteome]
Taxonomic identifier10116 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeRattus

Protein attributes

Sequence length1014 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
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. 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.

Catalytic activity

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

Subunit structure

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.

Subcellular location

Nucleus By similarity. Nucleusnucleolus By similarity. Note: Localizes at sites of DNA damage By similarity.

Post-translational modification

Phosphorylated by PRKDC and TXK.

Poly-ADP-ribosylated by PARP2. Poly-ADP-ribosylation mediates the recruitment of CHD1L to DNA damage sites By similarity.

S-nitrosylated, leading to inhibit transcription regulation activity By similarity.

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.

Sequence similarities

Contains 1 BRCT domain.

Contains 1 PARP alpha-helical domain.

Contains 1 PARP catalytic domain.

Contains 2 PARP-type zinc fingers.

Sequence caution

The sequence CAA46478.1 differs from that shown. Reason: Erroneous initiation.

Ontologies

Keywords
   Biological processDNA damage
DNA repair
Transcription
Transcription regulation
   Cellular componentNucleus
   DomainRepeat
Zinc-finger
   LigandDNA-binding
Metal-binding
NAD
Zinc
   Molecular functionGlycosyltransferase
Transferase
   PTMAcetylation
ADP-ribosylation
Phosphoprotein
   Technical term3D-structure
Complete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processDNA damage response, detection of DNA damage

Inferred from direct assay PubMed 15857403. Source: RGD

base-excision repair

Inferred from electronic annotation. Source: Ensembl

cellular response to insulin stimulus

Inferred from electronic annotation. Source: Ensembl

double-strand break repair

Inferred from sequence or structural similarity. Source: UniProtKB

positive regulation of SMAD protein import into nucleus

Inferred from mutant phenotype PubMed 22073128. Source: BHF-UCL

positive regulation of transcription from RNA polymerase II promoter

Inferred from mutant phenotype PubMed 22073128. Source: BHF-UCL

positive regulation of transcription regulatory region DNA binding

Inferred from mutant phenotype PubMed 22073128. Source: BHF-UCL

protein ADP-ribosylation

Inferred from direct assay PubMed 15857403PubMed 16093393. Source: RGD

protein autoprocessing

Inferred from direct assay PubMed 16093393. Source: RGD

protein poly-ADP-ribosylation

Inferred from mutant phenotype PubMed 22073128. Source: BHF-UCL

regulation of growth rate

Inferred from electronic annotation. Source: Ensembl

signal transduction involved in regulation of gene expression

Inferred from mutant phenotype PubMed 22073128. Source: BHF-UCL

telomere maintenance

Inferred from electronic annotation. Source: Ensembl

transcription, DNA-templated

Inferred from electronic annotation. Source: UniProtKB-KW

transforming growth factor beta receptor signaling pathway

Inferred from mutant phenotype PubMed 22073128. Source: BHF-UCL

   Cellular_componentnuclear envelope

Inferred from electronic annotation. Source: Ensembl

nucleolus

Inferred from electronic annotation. Source: UniProtKB-SubCell

nucleoplasm

Inferred from electronic annotation. Source: Ensembl

nucleus

Inferred from direct assay PubMed 22073128. Source: BHF-UCL

transcription factor complex

Inferred from electronic annotation. Source: Ensembl

   Molecular_functionDNA binding

Inferred from electronic annotation. Source: UniProtKB-KW

NAD binding

Inferred from direct assay PubMed 15857403PubMed 16302026. Source: RGD

NAD+ ADP-ribosyltransferase activity

Inferred from mutant phenotype PubMed 22073128. Source: BHF-UCL

R-SMAD binding

Inferred from physical interaction PubMed 22073128. Source: BHF-UCL

enzyme binding

Inferred from physical interaction PubMed 19470756. Source: BHF-UCL

transferase activity, transferring pentosyl groups

Non-traceable author statement Ref.1. Source: RGD

zinc ion binding

Inferred from electronic annotation. Source: InterPro

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Initiator methionine11Removed By similarity
Chain2 – 10141013Poly [ADP-ribose] polymerase 1
PRO_0000211321

Regions

Domain386 – 47792BRCT
Domain662 – 779118PARP alpha-helical
Domain788 – 1014227PARP catalytic
DNA binding2 – 373372
Zinc finger9 – 9385PARP-type 1
Zinc finger113 – 20391PARP-type 2
Region374 – 524151Automodification domain
Motif207 – 2093Nuclear localization signal
Motif221 – 2266Nuclear localization signal

Amino acid modifications

Modified residue21N-acetylalanine By similarity
Modified residue411Phosphoserine By similarity
Modified residue971N6-acetyllysine By similarity
Modified residue1051N6-acetyllysine By similarity
Modified residue1311N6-acetyllysine By similarity
Modified residue1791Phosphoserine By similarity
Modified residue4081PolyADP-ribosyl glutamic acid Potential
Modified residue4141PolyADP-ribosyl glutamic acid Potential
Modified residue4361PolyADP-ribosyl glutamic acid Potential
Modified residue4381PolyADP-ribosyl glutamic acid Potential
Modified residue4451PolyADP-ribosyl glutamic acid Potential
Modified residue4461PolyADP-ribosyl glutamic acid Potential
Modified residue4571PolyADP-ribosyl glutamic acid Potential
Modified residue4851PolyADP-ribosyl glutamic acid Potential
Modified residue4891PolyADP-ribosyl glutamic acid Potential
Modified residue4921PolyADP-ribosyl glutamic acid Potential
Modified residue5131PolyADP-ribosyl glutamic acid Potential
Modified residue5141PolyADP-ribosyl glutamic acid Potential
Modified residue5201PolyADP-ribosyl glutamic acid Potential
Modified residue6001N6-acetyllysine By similarity
Modified residue6211N6-acetyllysine By similarity
Modified residue7821Phosphoserine By similarity

Experimental info

Sequence conflict6391Y → H in CAA46478. Ref.5
Sequence conflict6421E → A in CAA46478. Ref.5
Sequence conflict7531N → D in CAA46478. Ref.5

Secondary structure

................... 1014
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
P27008 [UniParc].

Last modified January 23, 2007. Version 4.
Checksum: BE1B6F2B29B887ED

FASTA1,014112,660
        10         20         30         40         50         60 
MAEATERLYR VEYAKSGRAS CKKCSESIPK DSLRMAIMVQ SPMFDGKVPH WYHFSCFWKV 

        70         80         90        100        110        120 
GHSIRQPDTE VDGFSELRWD DQQKVKKTAE AGGVAGKGQH GGGGKAEKTL GDFAAEYAKS 

       130        140        150        160        170        180 
NRSTCKGCME KIEKGQMRLS KKMLDPEKPQ LGMIDRWYHP TCFVKNRDEL GFRPEYSASQ 

       190        200        210        220        230        240 
LKGFSLLSAE DKEALKKQLP AVKSEGKRKC DEVDGIDEVA KKKSKKGKDK ESSKLEKALK 

       250        260        270        280        290        300 
AQNELVWNIK DELKKACSTN DLKELLIFNQ QQVPSGESAI LDRVADGMAF GALLPCKECS 

       310        320        330        340        350        360 
GQLVFKSDAY YCTGDVTAWT KCMVKTQNPS RKEWVTPKEF REISYLKKLK IKKQDRLFPP 

       370        380        390        400        410        420 
ESSAPAPPAP PVSITSAPTA VNSSAPADKP LSNMKILTLG KLSQNKDEAK AMIEKLGGKL 

       430        440        450        460        470        480 
TGSANKASLC ISTKKEVEKM SKKMEEVKAA NVRVVCEDFL QDVSASAKSL QELLSAHSLS 

       490        500        510        520        530        540 
SWGAEVKVEP GEVVVPKGKS AAPSKKSKGA VKEEGVNKSE KRMKLTLKGG AAVDPDSGLE 

       550        560        570        580        590        600 
HSAHVLEKGG KVFSATLGLV DIVKGTNSYY KLQLLESDKE SRYWIFRSWG RVGTVIGSNK 

       610        620        630        640        650        660 
LEQMPSKEDA VEHFMKLYEE KTGNAWHSKN FTKYPKKFYP LEIDYGQDEE AVKKLAVKPG 

       670        680        690        700        710        720 
TKSKLPKPVQ ELVGMIFDVE SMKKALVEYE IDLQKMPLGK LSRRQIQAAY SILSEVQQAV 

       730        740        750        760        770        780 
SQGSSESQIL DLSNRFYTLI PHDFGMKKPP LLNNTDSVQA KVEMLDNLLD IEVAYSLLRG 

       790        800        810        820        830        840 
GSDDSSKDPI DVNYEKLKTD IKVVDRDSEE AEVIRKYVKN THATTHNAYD LEVIDIFKIE 

       850        860        870        880        890        900 
REGESQRYKP FRQLHNRRLL WHGSRTTNFA GILSQGLRIA PPEAPVTGYM FGKGIYFADM 

       910        920        930        940        950        960 
VSKSANYCHT SQGDPIGLIL LGEVALGNMY ELKHASHISK LPKGKHSVKG LGKTAPDPSA 

       970        980        990       1000       1010 
SITLDGVEVP LGTGIPSGVN DTCLLYNEYI VYDIAQVNLK YLLKLKFNFK TSLW 

« Hide

References

« Hide 'large scale' references
[1]"Isolation of cDNA encoding full-length rat (Rattus norvegicus) poly (ADP-ribose) polymerase."
Beneke S., Meyer R., Buerkle A.
Biochem. Mol. Biol. Int. 43:755-761(1997) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
Strain: Sprague-Dawley.
Tissue: Monocyte.
[2]Beneke S., Meyer R., Buerkle A.
Submitted (FEB-1998) to the EMBL/GenBank/DDBJ databases
Cited for: SEQUENCE REVISION TO 812.
[3]"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].
Tissue: Kidney.
[4]"Structural analysis of the putative regulatory region of the rat gene encoding poly(ADP-ribose) polymerase."
Potvin F., Thibodeau J., Kirkland J.B., Dandenault B., Duchaine C., Poirier G.G.
FEBS Lett. 302:269-273(1992) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-12.
Strain: Sprague-Dawley.
Tissue: Prostate.
[5]"Cloning of rodent cDNA coding the poly(ADP-ribose) polymerase catalytic domain and analysis of mRNA levels during the cell cycle."
Thibodeau J., Gradwohl G., Dumas C., Clairoux-Moreau S., Brunet G.
Biochem. Cell Biol. 67:653-660(1989) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 515-1014.
Strain: Sprague-Dawley.
Tissue: Prostate.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
U94340 mRNA. Translation: AAC53544.1.
BC085765 mRNA. Translation: AAH85765.1.
X65496 Genomic DNA. Translation: CAA46477.1.
X65497 Genomic DNA. Translation: CAA46478.1. Different initiation.
PIRS21163.
S26057.
RefSeqNP_037195.1. NM_013063.2.
UniGeneRn.11327.

3D structure databases

PDBe
RCSB-PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
2LE0NMR-A389-487[»]
ProteinModelPortalP27008.
SMRP27008. Positions 1-93, 105-360, 382-490, 520-643, 662-1011.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid247621. 16 interactions.

Chemistry

BindingDBP27008.
ChEMBLCHEMBL4664.

PTM databases

PhosphoSiteP27008.

Proteomic databases

PaxDbP27008.
PRIDEP27008.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENSRNOT00000004232; ENSRNOP00000004232; ENSRNOG00000003084.
GeneID25591.
KEGGrno:25591.
UCSCRGD:2053. rat.

Organism-specific databases

CTD142.
RGD2053. Parp1.

Phylogenomic databases

eggNOGNOG243963.
GeneTreeENSGT00390000017341.
HOGENOMHOG000030402.
HOVERGENHBG053513.
InParanoidP27008.
KOK10798.
OMAITAWTKC.
OrthoDBEOG7KM5S0.
PhylomeDBP27008.
TreeFamTF316616.

Gene expression databases

GenevestigatorP27008.

Family and domain databases

Gene3D1.20.142.10. 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.
InterProIPR001357. BRCT_dom.
IPR008288. NAD_ADPRT.
IPR012982. PADR1.
IPR012317. Poly(ADP-ribose)pol_cat_dom.
IPR004102. Poly(ADP-ribose)pol_reg_dom.
IPR008893. WGR_domain.
IPR001510. Znf_PARP.
[Graphical view]
PfamPF00533. 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]
PIRSFPIRSF000489. NAD_ADPRT. 1 hit.
SMARTSM00292. BRCT. 1 hit.
SM00773. WGR. 1 hit.
[Graphical view]
SUPFAMSSF142921. SSF142921. 1 hit.
SSF47587. SSF47587. 1 hit.
SSF52113. SSF52113. 1 hit.
PROSITEPS50172. 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]
ProtoNetSearch...

Other

NextBio607267.
PROP27008.

Entry information

Entry namePARP1_RAT
AccessionPrimary (citable) accession number: P27008
Secondary accession number(s): O35937
Entry history
Integrated into UniProtKB/Swiss-Prot: August 1, 1992
Last sequence update: January 23, 2007
Last modified: May 14, 2014
This is version 143 of the entry and version 4 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

PDB cross-references

Index of Protein Data Bank (PDB) cross-references