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P27008

- PARP1_RAT

UniProt

P27008 - PARP1_RAT

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
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    • History
      Entry version 145 (01 Oct 2014)
      Sequence version 4 (23 Jan 2007)
      Previous versions | rss
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    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. R-SMAD binding Source: BHF-UCL
    6. transferase activity, transferring pentosyl groups Source: RGD
    7. 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

    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: UniProtKB-SubCell
    3. nucleoplasm Source: Ensembl
    4. nucleus Source: BHF-UCL
    5. transcription factor complex Source: Ensembl

    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

    MAEATERLYR VEYAKSGRAS CKKCSESIPK DSLRMAIMVQ SPMFDGKVPH     50
    WYHFSCFWKV GHSIRQPDTE VDGFSELRWD DQQKVKKTAE AGGVAGKGQH 100
    GGGGKAEKTL GDFAAEYAKS NRSTCKGCME KIEKGQMRLS KKMLDPEKPQ 150
    LGMIDRWYHP TCFVKNRDEL GFRPEYSASQ LKGFSLLSAE DKEALKKQLP 200
    AVKSEGKRKC DEVDGIDEVA KKKSKKGKDK ESSKLEKALK AQNELVWNIK 250
    DELKKACSTN DLKELLIFNQ QQVPSGESAI LDRVADGMAF GALLPCKECS 300
    GQLVFKSDAY YCTGDVTAWT KCMVKTQNPS RKEWVTPKEF REISYLKKLK 350
    IKKQDRLFPP ESSAPAPPAP PVSITSAPTA VNSSAPADKP LSNMKILTLG 400
    KLSQNKDEAK AMIEKLGGKL TGSANKASLC ISTKKEVEKM SKKMEEVKAA 450
    NVRVVCEDFL QDVSASAKSL QELLSAHSLS SWGAEVKVEP GEVVVPKGKS 500
    AAPSKKSKGA VKEEGVNKSE KRMKLTLKGG AAVDPDSGLE HSAHVLEKGG 550
    KVFSATLGLV DIVKGTNSYY KLQLLESDKE SRYWIFRSWG RVGTVIGSNK 600
    LEQMPSKEDA VEHFMKLYEE KTGNAWHSKN FTKYPKKFYP LEIDYGQDEE 650
    AVKKLAVKPG TKSKLPKPVQ ELVGMIFDVE SMKKALVEYE IDLQKMPLGK 700
    LSRRQIQAAY SILSEVQQAV SQGSSESQIL DLSNRFYTLI PHDFGMKKPP 750
    LLNNTDSVQA KVEMLDNLLD IEVAYSLLRG GSDDSSKDPI DVNYEKLKTD 800
    IKVVDRDSEE AEVIRKYVKN THATTHNAYD LEVIDIFKIE REGESQRYKP 850
    FRQLHNRRLL WHGSRTTNFA GILSQGLRIA PPEAPVTGYM FGKGIYFADM 900
    VSKSANYCHT SQGDPIGLIL LGEVALGNMY ELKHASHISK LPKGKHSVKG 950
    LGKTAPDPSA SITLDGVEVP LGTGIPSGVN DTCLLYNEYI VYDIAQVNLK 1000
    YLLKLKFNFK TSLW 1014
    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

    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 1, 2014
    This is version 145 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