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P11103

- PARP1_MOUSE

UniProt

P11103 - PARP1_MOUSE

Protein

Poly [ADP-ribose] polymerase 1

Gene

Parp1

Organism
Mus musculus (Mouse)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 159 (01 Oct 2014)
      Sequence version 3 (23 Jan 2007)
      Previous versions | rss
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    Functioni

    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. 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. 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 – 372371Add
    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. NAD+ ADP-ribosyltransferase activity Source: MGI
    3. NAD binding Source: InterPro
    4. protein binding Source: IntAct
    5. zinc ion binding Source: InterPro

    GO - Biological processi

    1. base-excision repair Source: MGI
    2. cellular response to superoxide Source: MGI
    3. DNA metabolic process Source: MGI
    4. DNA repair Source: MGI
    5. double-strand break repair Source: UniProtKB
    6. protein ADP-ribosylation Source: InterPro
    7. regulation of growth rate Source: MGI
    8. regulation of transcription, DNA-templated Source: UniProtKB-KW
    9. telomere maintenance Source: MGI
    10. transcription, DNA-templated Source: UniProtKB-KW

    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
    Short name:
    msPARP
    Gene namesi
    Name:Parp1
    Synonyms:Adprp, Adprt, Adprt1
    OrganismiMus musculus (Mouse)
    Taxonomic identifieri10090 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
    ProteomesiUP000000589: Unplaced

    Organism-specific databases

    MGIiMGI:1340806. Parp1.

    Subcellular locationi

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

    GO - Cellular componenti

    1. cytoplasm Source: BHF-UCL
    2. nucleolus Source: MGI
    3. nucleoplasm Source: MGI
    4. nucleus Source: BHF-UCL
    5. protein complex Source: MGI

    Keywords - Cellular componenti

    Nucleus

    Pathology & Biotechi

    Disruption phenotypei

    Mice show a complete lack of nuclear poly(ADP-ribosyl)ation. Mice are however viable and fertile. Moreover, repair of UV and MNNG induced DNA damage are not affected. However, about 30% of the mutant mice developed pathological skin aberrations on a mixed 129/Sv x C57B1/6 genetic background.1 Publication

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Initiator methioninei1 – 11RemovedBy similarity
    Chaini2 – 10131012Poly [ADP-ribose] polymerase 1PRO_0000023259Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei2 – 21N-acetylalanineBy similarity
    Modified residuei41 – 411PhosphoserineBy similarity
    Modified residuei97 – 971N6-acetyllysine1 Publication
    Modified residuei105 – 1051N6-acetyllysineBy similarity
    Modified residuei131 – 1311N6-acetyllysineBy similarity
    Modified residuei179 – 1791PhosphoserineBy 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 residuei448 – 4481PolyADP-ribosyl glutamic acidSequence Analysis
    Modified residuei456 – 4561PolyADP-ribosyl glutamic acidSequence Analysis
    Modified residuei484 – 4841PolyADP-ribosyl glutamic acidSequence Analysis
    Modified residuei488 – 4881PolyADP-ribosyl glutamic acidSequence Analysis
    Modified residuei491 – 4911PolyADP-ribosyl glutamic acidSequence Analysis
    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
    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.1 Publication

    Keywords - PTMi

    Acetylation, ADP-ribosylation, Phosphoprotein, S-nitrosylation

    Proteomic databases

    MaxQBiP11103.
    PaxDbiP11103.
    PRIDEiP11103.

    PTM databases

    PhosphoSiteiP11103.

    Expressioni

    Tissue specificityi

    Widely expressed. Expression is correlated with proliferation, with higher levels occurring during early fetal development and organogenesis and in the highly proliferative cell compartments of adult. Expressed in B-cells that have been induced to switch to various Ig isotypes.1 Publication

    Developmental stagei

    At stage E12.5, expressed at high level in the developing liver and kidneys. Expressed at higher level in the genital ridge and the spinal ganglia. At E18.5, preferentially expressed in the thymus and in regions of the nervous system. Within the developing trunk, preferential expression persisted in the liver and became restricted to the cortical region of the kidney, spleen, adrenal gland, and to stomach and intestinal epithelia. From E14.5 to E18.5, as well as in the adult, expressed at the highest level in thymus. Expression is particularly high in the subcapsular zone of the thymus where immature lymphocytes proliferate. Expressed at high level in the seminiferous tubules of the developing testis.1 Publication

    Gene expression databases

    CleanExiMM_PARP1.
    GenevestigatoriP11103.

    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, APTX and SRY 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 By similarity. The SWAP complex consists of NPM1, NCL, PARP1 and SWAP70. Interacts with TIAM2 and ZNF423. Interacts with RNF4. Interacts with EEF1A1 and TXK By similarity. Interacts with RNF146 By similarity. 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 By similarity.By similarity

    Binary interactionsi

    WithEntry#Exp.IntActNotes
    P030872EBI-642213,EBI-1555770From a different organism.
    ArntlQ9WTL87EBI-642213,EBI-644534
    Casp3P706773EBI-642213,EBI-1790419
    Casp7P978643EBI-642213,EBI-5307197
    Pou5f1P202632EBI-642213,EBI-1606219

    Protein-protein interaction databases

    DIPiDIP-39371N.
    IntActiP11103. 12 interactions.
    MINTiMINT-237428.

    Structurei

    3D structure databases

    ProteinModelPortaliP11103.
    SMRiP11103. Positions 5-94, 108-200, 234-359, 388-486, 519-1010.
    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 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.
    HOVERGENiHBG053513.
    InParanoidiP11103.
    PhylomeDBiP11103.

    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]

    Sequences (2)i

    Sequence statusi: Complete.

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

    This entry describes 2 isoformsi produced by alternative initiation. Align

    Isoform 1 (identifier: P11103-1) [UniParc]FASTAAdd to Basket

    Also known as: Long

    This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

    « Hide

    MAEASERLYR VQYAKSGRAS CKKCSESIPK DSLRMAIMVQ SPMFDGKVPH     50
    WYHFSCFWKV GQSIRHPDVE VDGFSELRWD DQQKVKKTAE AGGVAGKGQD 100
    GSGGKAEKTL GDFAAEYAKS NRSMCKGCLE KIEKGQMRLS KKMVDPEKPQ 150
    LGMIDRWYHP TCFVKKRDEL GFRPEYSASQ LKGFSLLSAE DKEALKKQLP 200
    AIKNEGKRKG DEVDGTDEVA KKKSRKETDK YSKLEKALKA QNELIWNIKD 250
    ELKKACSTND LKELLIFNQQ QVPSGESAIL DRVADGMAFG ALLPCKECSG 300
    QLVFKSDAYY CTGDVTAWTK CMVKTQNPSR KEWVTPKEFR EISYLKKLKV 350
    KKQDRIFPPE SSAPITVHWP LSVTSAPTAV NSSAPADKPL SNMKILTLGK 400
    LSQNKDEAKA VIEKLGGKLT GSANKASLCI SIKKEVEKMN KKMEEVKEAN 450
    IRVVSEDFLQ DVSASTKSLQ DLLSAHSLSP WGAEVKAEPG EVVAPRGKSA 500
    APSKKSKGCF KEEGVNKSEK RMKLTLKGGA AVDPDSGLEH SAHVLEKGGK 550
    VFSATLGLVD IVKGTNSYYK LQLLEDDKES RYWIFRSWGR LGTVIGSNKL 600
    EQMPSKEEAV EQFMKLYEEK TGNAWHSKNF TKYPKKFYPL EIDYGQDEEA 650
    VKKLTVKPGT KSKLPKPVQE LVGMIFDVDS MKKALVEYEI DLQKMPLGKL 700
    SRRQIQAAYS ILSEVQQPVS QGSSESQILD LSNRFYTLIP HDFGMKKPPL 750
    LNNADSVQAK VEMLDNLLDI EVAYSLLRGG SDDSSKDPID VNYEKLKTDI 800
    KVVDRDSEEA EVIRKYVKNT HATTHNAYDL EVIDIFKIER EGESQRYKPF 850
    RQLHNRRLLW HGSRTTNFAG ILSQGLRIAP PEAPVTGYMF GKGIYFADMV 900
    SKSANYCHTS QGDPIGLIML GEVALGNMYE LKHASHISKL PKGKHSVKGL 950
    GKTTPDPSAS ITLEGVEVPL GTGIPSGVND TALLYNEYIV YDIAQVNLKY 1000
    LLKLKFNFKT SLW 1013
    Length:1,013
    Mass (Da):113,100
    Last modified:January 23, 2007 - v3
    Checksum:i5E54C3E5F60BB922
    GO
    Isoform 2 (identifier: P11103-2) [UniParc]FASTAAdd to Basket

    Also known as: Short, sPARP-1

    The sequence of this isoform differs from the canonical sequence as follows:
         2-521: Missing.

    Note: No experimental confirmation available.

    Show »
    Length:493
    Mass (Da):55,368
    Checksum:iFBD0D37BA9E04DC7
    GO

    Sequence cautioni

    The sequence AAF61293.1 differs from that shown. Reason: Erroneous initiation.

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti114 – 1141A → L AA sequence (PubMed:9642267)Curated
    Sequence conflicti591 – 5911L → V in AAF61293. (PubMed:10809783)Curated
    Sequence conflicti608 – 6081E → D in AAF61293. (PubMed:10809783)Curated
    Sequence conflicti612 – 6121Q → H in AAF61293. (PubMed:10809783)Curated
    Sequence conflicti629 – 6291N → D in AAF61293. (PubMed:10809783)Curated
    Sequence conflicti679 – 6791D → E in AAF61293. (PubMed:10809783)Curated
    Sequence conflicti717 – 7171Q → E in AAF61293. (PubMed:10809783)Curated
    Sequence conflicti758 – 7581Q → L in AAF61293. (PubMed:10809783)Curated
    Sequence conflicti982 – 9821A → C in AAF61293. (PubMed:10809783)Curated

    Alternative sequence

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Alternative sequencei2 – 521520Missing in isoform 2. 1 PublicationVSP_018970Add
    BLAST

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    X14206 mRNA. Translation: CAA32421.1.
    AF126717 mRNA. Translation: AAF61293.1. Different initiation.
    PIRiS04200.
    UniGeneiMm.277779.

    Keywords - Coding sequence diversityi

    Alternative initiation

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    X14206 mRNA. Translation: CAA32421.1 .
    AF126717 mRNA. Translation: AAF61293.1 . Different initiation.
    PIRi S04200.
    UniGenei Mm.277779.

    3D structure databases

    ProteinModelPortali P11103.
    SMRi P11103. Positions 5-94, 108-200, 234-359, 388-486, 519-1010.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    DIPi DIP-39371N.
    IntActi P11103. 12 interactions.
    MINTi MINT-237428.

    Chemistry

    BindingDBi P11103.
    ChEMBLi CHEMBL3740.

    PTM databases

    PhosphoSitei P11103.

    Proteomic databases

    MaxQBi P11103.
    PaxDbi P11103.
    PRIDEi P11103.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Organism-specific databases

    MGIi MGI:1340806. Parp1.

    Phylogenomic databases

    eggNOGi NOG243963.
    HOVERGENi HBG053513.
    InParanoidi P11103.
    PhylomeDBi P11103.

    Miscellaneous databases

    PROi P11103.
    SOURCEi Search...

    Gene expression databases

    CleanExi MM_PARP1.
    Genevestigatori P11103.

    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. "Sequence and organization of the mouse poly (ADP-ribose) polymerase gene."
      Huppi K., Bhatia K., Siwarski D., Klinman D., Cherney B., Smulson M.
      Nucleic Acids Res. 17:3387-3401(1989) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
      Strain: BXSB.
    2. "Characterization of sPARP-1. An alternative product of PARP-1 gene with poly(ADP-ribose) polymerase activity independent of DNA strand breaks."
      Sallmann F.R., Vodenicharov M.D., Wang Z.-Q., Poirier G.G.
      J. Biol. Chem. 275:15504-15511(2000) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2), CHARACTERIZATION.
      Strain: C57BL/6 X 129/Sv.
      Tissue: Fibroblast.
    3. Cited for: PROTEIN SEQUENCE OF 109-119 AND 865-875, SUBUNIT, TISSUE SPECIFICITY.
      Strain: C57BL/6.
      Tissue: Spleen.
    4. "On the biological role of the nuclear polymerizing NAD+: protein(ADP-ribosyl) transferase (ADPRT): ADPRT from Dictyostelium discoideum and inactivation of the ADPRT gene in the mouse."
      Auer B., Flick K., Wang Z.Q., Haidacher D., Jaeger S., Berghammer H., Kofler B., Schweiger M., Wagner E.F.
      Biochimie 77:444-449(1995) [PubMed] [Europe PMC] [Abstract]
      Cited for: DISRUPTION PHENOTYPE.
    5. "Poly(ADP-ribose) polymerase-2 (PARP-2) is required for efficient base excision DNA repair in association with PARP-1 and XRCC1."
      Schreiber V., Ame J.-C., Dolle P., Schultz I., Rinaldi B., Fraulob V., Menissier-de Murcia J., de Murcia G.M.
      J. Biol. Chem. 277:23028-23036(2002) [PubMed] [Europe PMC] [Abstract]
      Cited for: DEVELOPMENTAL STAGE.
    6. "Poly(ADP-ribose) polymerase 1 interacts with OAZ and regulates BMP-target genes."
      Ku M.-C., Stewart S., Hata A.
      Biochem. Biophys. Res. Commun. 311:702-707(2003) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH ZNF423.
    7. "Nitric oxide-dependent negative feedback of PARP-1 trans-activation of the inducible nitric-oxide synthase gene."
      Yu Z., Kuncewicz T., Dubinsky W.P., Kone B.C.
      J. Biol. Chem. 281:9101-9109(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: S-NITROSYLATION.
    8. Cited for: INTERACTION WITH TIAM2.
    9. "PARP-1 transcriptional activity is regulated by sumoylation upon heat shock."
      Martin N., Schwamborn K., Schreiber V., Werner A., Guillier C., Zhang X.D., Bischof O., Seeler J.S., Dejean A.
      EMBO J. 28:3534-3548(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH RNF4.
    10. "Poly(ADP-ribose)-dependent regulation of Snail1 protein stability."
      Rodriguez M.I., Gonzalez-Flores A., Dantzer F., Collard J., de Herreros A.G., Oliver F.J.
      Oncogene 30:4365-4372(2011) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH SNAI1.
    11. "SIRT5-mediated lysine desuccinylation impacts diverse metabolic pathways."
      Park J., Chen Y., Tishkoff D.X., Peng C., Tan M., Dai L., Xie Z., Zhang Y., Zwaans B.M., Skinner M.E., Lombard D.B., Zhao Y.
      Mol. Cell 50:919-930(2013) [PubMed] [Europe PMC] [Abstract]
      Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-97, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Embryonic fibroblast.

    Entry informationi

    Entry nameiPARP1_MOUSE
    AccessioniPrimary (citable) accession number: P11103
    Secondary accession number(s): Q9JLX4, Q9QVQ3
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: July 1, 1989
    Last sequence update: January 23, 2007
    Last modified: October 1, 2014
    This is version 159 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.

    Keywords - Technical termi

    Complete proteome, Direct protein sequencing, Reference proteome

    Documents

    1. MGD cross-references
      Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
    2. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3