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P27008

- PARP1_RAT

UniProt

P27008 - PARP1_RAT

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Protein

Poly [ADP-ribose] polymerase 1

Gene

Parp1

Organism
Rattus norvegicus (Rat)
Status
Reviewed - 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 (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 – 373372Add
BLAST
Zinc fingeri9 – 9385PARP-type 1PROSITE-ProRule annotationAdd
BLAST
Zinc fingeri113 – 20391PARP-type 2PROSITE-ProRule annotationAdd
BLAST

GO - Molecular functioni

  1. DNA binding Source: UniProtKB-KW
  2. enzyme binding Source: BHF-UCL
  3. NAD+ ADP-ribosyltransferase activity Source: BHF-UCL
  4. NAD binding Source: RGD
  5. poly(A) RNA binding Source: Ensembl
  6. R-SMAD binding Source: BHF-UCL
  7. transferase activity, transferring pentosyl groups Source: RGD
  8. zinc ion binding Source: InterPro

GO - Biological processi

  1. base-excision repair Source: Ensembl
  2. cellular response to insulin stimulus Source: Ensembl
  3. DNA damage response, detection of DNA damage Source: RGD
  4. double-strand break repair Source: UniProtKB
  5. positive regulation of SMAD protein import into nucleus Source: BHF-UCL
  6. positive regulation of transcription from RNA polymerase II promoter Source: BHF-UCL
  7. positive regulation of transcription regulatory region DNA binding Source: BHF-UCL
  8. protein ADP-ribosylation Source: RGD
  9. protein autoprocessing Source: RGD
  10. protein poly-ADP-ribosylation Source: BHF-UCL
  11. regulation of growth rate Source: Ensembl
  12. signal transduction involved in regulation of gene expression Source: BHF-UCL
  13. telomere maintenance Source: Ensembl
  14. transcription, DNA-templated Source: UniProtKB-KW
  15. 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

ReactomeiREACT_194639. Downregulation of SMAD2/3:SMAD4 transcriptional activity.

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
ProteomesiUP000002494: 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

  1. nuclear envelope Source: Ensembl
  2. nucleolus Source: Ensembl
  3. nucleoplasm Source: Ensembl
  4. nucleus Source: BHF-UCL
  5. transcription factor complex Source: Ensembl
Complete GO annotation...

Keywords - Cellular componenti

Nucleus

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Initiator methioninei1 – 11RemovedBy similarity
Chaini2 – 10141013Poly [ADP-ribose] polymerase 1PRO_0000211321Add
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
Modified residuei408 – 4081PolyADP-ribosyl glutamic acidSequence Analysis
Modified residuei414 – 4141PolyADP-ribosyl glutamic acidSequence Analysis
Modified residuei436 – 4361PolyADP-ribosyl glutamic acidSequence Analysis
Modified residuei438 – 4381PolyADP-ribosyl glutamic acidSequence Analysis
Modified residuei445 – 4451PolyADP-ribosyl glutamic acidSequence Analysis
Modified residuei446 – 4461PolyADP-ribosyl glutamic acidSequence Analysis
Modified residuei457 – 4571PolyADP-ribosyl glutamic acidSequence Analysis
Modified residuei485 – 4851PolyADP-ribosyl glutamic acidSequence Analysis
Modified residuei489 – 4891PolyADP-ribosyl glutamic acidSequence Analysis
Modified residuei492 – 4921PolyADP-ribosyl glutamic acidSequence Analysis
Modified residuei513 – 5131PolyADP-ribosyl glutamic acidSequence Analysis
Modified residuei514 – 5141PolyADP-ribosyl glutamic acidSequence Analysis
Modified residuei520 – 5201PolyADP-ribosyl glutamic acidSequence Analysis
Modified residuei600 – 6001N6-acetyllysineBy similarity
Modified residuei621 – 6211N6-acetyllysineBy similarity
Modified residuei782 – 7821PhosphoserineBy 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, Phosphoprotein

Proteomic databases

PaxDbiP27008.
PRIDEiP27008.

PTM databases

PhosphoSiteiP27008.

Expressioni

Gene expression databases

GenevestigatoriP27008.

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).By similarity

Protein-protein interaction databases

BioGridi247621. 16 interactions.

Structurei

Secondary structure

1
1014
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi394 – 3985
Helixi406 – 41611
Beta strandi422 – 4243
Beta strandi427 – 4315
Helixi434 – 4396
Helixi442 – 4498
Beta strandi453 – 4553
Helixi458 – 4658
Helixi470 – 4767

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
2LE0NMR-A389-487[»]
ProteinModelPortaliP27008.
SMRiP27008. Positions 1-93, 105-360, 382-490, 520-643, 662-1011.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini386 – 47792BRCTPROSITE-ProRule annotationAdd
BLAST
Domaini662 – 779118PARP alpha-helicalPROSITE-ProRule annotationAdd
BLAST
Domaini788 – 1014227PARP catalyticPROSITE-ProRule annotationAdd
BLAST

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni374 – 524151Automodification domainAdd
BLAST

Motif

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

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

eggNOGiNOG243963.
GeneTreeiENSGT00390000017341.
HOGENOMiHOG000030402.
HOVERGENiHBG053513.
InParanoidiP27008.
KOiK10798.
OMAiITAWTKC.
OrthoDBiEOG7KM5S0.
PhylomeDBiP27008.
TreeFamiTF316616.

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.
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]
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.
SM00773. WGR. 1 hit.
[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 CAA46478.1 differs from that shown. Reason: Erroneous initiation.

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti639 – 6391Y → H in CAA46478. (PubMed:2508731)Curated
Sequence conflicti642 – 6421E → A in CAA46478. (PubMed:2508731)Curated
Sequence conflicti753 – 7531N → D in CAA46478. (PubMed:2508731)Curated

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
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:
EMBL
GenBank
DDBJ
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.
PIRi S21163.
S26057.
RefSeqi NP_037195.1. NM_013063.2.
UniGenei Rn.11327.

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
2LE0 NMR - A 389-487 [» ]
ProteinModelPortali P27008.
SMRi P27008. Positions 1-93, 105-360, 382-490, 520-643, 662-1011.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 247621. 16 interactions.

Chemistry

BindingDBi P27008.
ChEMBLi CHEMBL4664.

PTM databases

PhosphoSitei P27008.

Proteomic databases

PaxDbi P27008.
PRIDEi P27008.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENSRNOT00000004232 ; ENSRNOP00000004232 ; ENSRNOG00000003084 .
GeneIDi 25591.
KEGGi rno:25591.
UCSCi RGD:2053. rat.

Organism-specific databases

CTDi 142.
RGDi 2053. Parp1.

Phylogenomic databases

eggNOGi NOG243963.
GeneTreei ENSGT00390000017341.
HOGENOMi HOG000030402.
HOVERGENi HBG053513.
InParanoidi P27008.
KOi K10798.
OMAi ITAWTKC.
OrthoDBi EOG7KM5S0.
PhylomeDBi P27008.
TreeFami TF316616.

Enzyme and pathway databases

Reactomei REACT_194639. Downregulation of SMAD2/3:SMAD4 transcriptional activity.

Miscellaneous databases

NextBioi 607267.
PROi P27008.

Gene expression databases

Genevestigatori P27008.

Family and domain databases

Gene3Di 1.20.142.10. 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.
InterProi IPR001357. 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 ]
Pfami PF00533. 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 ]
PIRSFi PIRSF000489. NAD_ADPRT. 1 hit.
SMARTi SM00292. BRCT. 1 hit.
SM00773. WGR. 1 hit.
[Graphical view ]
SUPFAMi SSF142921. SSF142921. 1 hit.
SSF47587. SSF47587. 1 hit.
SSF52113. SSF52113. 1 hit.
PROSITEi PS50172. 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 ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  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.

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: October 29, 2014
This is version 146 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

External Data

Dasty 3