Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Basket 0
(max 400 entries)x

Your basket is currently empty.

Select item(s) and click on "Add to basket" to create your own collection here
(400 entries max)

P09874

- PARP1_HUMAN

UniProt

P09874 - PARP1_HUMAN

Protein

Poly [ADP-ribose] polymerase 1

Gene

PARP1

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
    • BLAST
    • Align
    • Format
    • Add to basket
    • History
      Entry version 188 (01 Oct 2014)
      Sequence version 4 (23 Jan 2007)
      Previous versions | rss
    • Help video
    • Feedback
    • Comment

    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.5 Publications

    Catalytic activityi

    NAD+ + (ADP-D-ribosyl)(n)-acceptor = nicotinamide + (ADP-D-ribosyl)(n+1)-acceptor.1 PublicationPROSITE-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: ProtInc
    2. enzyme binding Source: UniProt
    3. identical protein binding Source: IntAct
    4. NAD+ ADP-ribosyltransferase activity Source: UniProtKB
    5. NAD binding Source: Ensembl
    6. poly(A) RNA binding Source: UniProtKB
    7. protein binding Source: UniProtKB
    8. protein N-terminus binding Source: UniProtKB
    9. transcription factor binding Source: BHF-UCL
    10. zinc ion binding Source: InterPro

    GO - Biological processi

    1. base-excision repair Source: Ensembl
    2. cellular response to insulin stimulus Source: BHF-UCL
    3. DNA damage response, detection of DNA damage Source: Ensembl
    4. DNA repair Source: UniProtKB
    5. double-strand break repair Source: UniProtKB
    6. gene expression Source: Reactome
    7. macrophage differentiation Source: UniProtKB
    8. negative regulation of transcription from RNA polymerase II promoter Source: Reactome
    9. positive regulation of SMAD protein import into nucleus Source: Ensembl
    10. positive regulation of transcription from RNA polymerase II promoter Source: Ensembl
    11. positive regulation of transcription regulatory region DNA binding Source: Ensembl
    12. protein ADP-ribosylation Source: UniProtKB
    13. protein autoprocessing Source: Ensembl
    14. protein poly-ADP-ribosylation Source: UniProtKB
    15. regulation of growth rate Source: Ensembl
    16. signal transduction involved in regulation of gene expression Source: Ensembl
    17. telomere maintenance Source: Ensembl
    18. transcription, DNA-templated Source: Reactome
    19. transcription from RNA polymerase II promoter Source: ProtInc
    20. transcription initiation from RNA polymerase II promoter Source: Reactome
    21. transforming growth factor beta receptor signaling pathway Source: Reactome

    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

    BRENDAi2.4.2.30. 2681.
    ReactomeiREACT_121111. Downregulation of SMAD2/3:SMAD4 transcriptional activity.
    SignaLinkiP09874.

    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, PPOL
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 1

    Organism-specific databases

    HGNCiHGNC:270. PARP1.

    Subcellular locationi

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

    GO - Cellular componenti

    1. membrane Source: UniProtKB
    2. nuclear envelope Source: UniProtKB
    3. nucleolus Source: UniProtKB
    4. nucleoplasm Source: Reactome
    5. nucleus Source: HPA
    6. transcription factor complex Source: BHF-UCL

    Keywords - Cellular componenti

    Nucleus

    Pathology & Biotechi

    Mutagenesis

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Mutagenesisi797 – 7971L → P: 1.5% of wild-type activity.
    Mutagenesisi868 – 8681N → S: 4% of wild-type activity.
    Mutagenesisi890 – 8901M → V: <0.5% of wild-type activity.
    Mutagenesisi893 – 8931K → I: Abolishes enzymatic activity.
    Mutagenesisi897 – 8971F → S: 10% of wild-type activity.
    Mutagenesisi899 – 8991D → N: 0.6% of wild-type activity.
    Mutagenesisi908 – 9081C → R: <0.5% of wild-type activity.
    Mutagenesisi926 – 9261L → F: 1.5% of wild-type activity.
    Mutagenesisi986 – 9861Y → H: 14% of wild-type activity and increased branching 15-fold.
    Mutagenesisi988 – 9881E → K: 1.25% of wild-type activity; only monomers are added.
    Mutagenesisi1003 – 10031L → P: 1.5% of wild-type activity.

    Organism-specific databases

    PharmGKBiPA32.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Initiator methioninei1 – 11Removed2 Publications
    Chaini2 – 10141013Poly [ADP-ribose] polymerase 1PRO_0000211320Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei2 – 21N-acetylalanine2 Publications
    Modified residuei41 – 411Phosphoserine1 Publication
    Modified residuei97 – 971N6-acetyllysine1 Publication
    Modified residuei105 – 1051N6-acetyllysine1 Publication
    Modified residuei131 – 1311N6-acetyllysine1 Publication
    Modified residuei179 – 1791Phosphoserine1 Publication
    Modified residuei368 – 3681Phosphothreonine1 Publication
    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 residuei471 – 4711PolyADP-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 residuei513 – 5131PolyADP-ribosyl glutamic acidSequence Analysis
    Modified residuei514 – 5141PolyADP-ribosyl glutamic acidSequence Analysis
    Modified residuei520 – 5201PolyADP-ribosyl glutamic acidSequence Analysis
    Modified residuei600 – 6001N6-acetyllysine1 Publication
    Modified residuei621 – 6211N6-acetyllysine1 Publication
    Modified residuei782 – 7821Phosphoserine4 Publications

    Post-translational modificationi

    Phosphorylated by PRKDC and TXK.7 Publications
    Poly-ADP-ribosylated by PARP2. Poly-ADP-ribosylation mediates the recruitment of CHD1L to DNA damage sites.
    S-nitrosylated, leading to inhibit transcription regulation activity.By similarity

    Keywords - PTMi

    Acetylation, ADP-ribosylation, Phosphoprotein

    Proteomic databases

    MaxQBiP09874.
    PaxDbiP09874.
    PeptideAtlasiP09874.
    PRIDEiP09874.

    2D gel databases

    SWISS-2DPAGEP09874.

    PTM databases

    PhosphoSiteiP09874.

    Miscellaneous databases

    PMAP-CutDBP09874.

    Expressioni

    Gene expression databases

    ArrayExpressiP09874.
    BgeeiP09874.
    CleanExiHS_PARP1.
    GenevestigatoriP09874.

    Organism-specific databases

    HPAiCAB000147.
    CAB003839.
    CAB003840.
    HPA045168.

    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. The SWAP complex consists of NPM1, NCL, PARP1 and SWAP70. Interacts with TIAM2 By similarity. 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 ZNF423. 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 similarity11 Publications

    Binary interactionsi

    WithEntry#Exp.IntActNotes
    itself3EBI-355676,EBI-355676
    APLFQ8IW193EBI-355676,EBI-1256044
    APTXQ7Z2E38EBI-355676,EBI-847814
    CEBPAP497152EBI-355676,EBI-1172054
    E2F1Q010942EBI-355676,EBI-448924
    ERGP113087EBI-355676,EBI-79704
    OARD1Q9Y5305EBI-355676,EBI-8502288
    PIAS4Q8N2W95EBI-355676,EBI-473160
    SNAI1O9586310EBI-355676,EBI-1045459
    Snai1Q020853EBI-355676,EBI-6049807From a different organism.
    SUMO1P631652EBI-355676,EBI-80140
    TP53P046373EBI-355676,EBI-366083
    UBCP0CG482EBI-355676,EBI-3390054
    WRNQ141918EBI-355676,EBI-368417
    XRCC1P188875EBI-355676,EBI-947466
    ZNF423Q2M1K92EBI-355676,EBI-950016

    Protein-protein interaction databases

    BioGridi106652. 191 interactions.
    DIPiDIP-38N.
    IntActiP09874. 65 interactions.
    MINTiMINT-104344.
    STRINGi9606.ENSP00000355759.

    Structurei

    Secondary structure

    1
    1014
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Turni2 – 54
    Beta strandi8 – 136
    Beta strandi15 – 173
    Turni22 – 243
    Beta strandi25 – 273
    Beta strandi32 – 409
    Beta strandi42 – 5312
    Helixi54 – 596
    Helixi67 – 704
    Helixi74 – 763
    Helixi79 – 9012
    Beta strandi113 – 1175
    Beta strandi119 – 1213
    Turni126 – 1283
    Beta strandi137 – 1459
    Beta strandi148 – 15811
    Helixi160 – 1656
    Helixi167 – 1704
    Turni174 – 1763
    Helixi177 – 1804
    Helixi184 – 1863
    Helixi189 – 19810
    Turni204 – 2063
    Helixi226 – 25530
    Helixi258 – 26710
    Turni273 – 2753
    Helixi276 – 28914
    Turni296 – 2983
    Beta strandi302 – 3054
    Beta strandi308 – 3114
    Beta strandi314 – 3163
    Beta strandi324 – 3274
    Helixi337 – 3404
    Helixi342 – 3476
    Beta strandi389 – 3924
    Beta strandi394 – 3974
    Helixi405 – 41410
    Beta strandi418 – 4214
    Beta strandi427 – 4304
    Helixi433 – 4386
    Helixi441 – 4488
    Helixi457 – 4637
    Helixi469 – 4757
    Helixi535 – 5373
    Turni540 – 5423
    Beta strandi543 – 5453
    Beta strandi551 – 56010
    Turni562 – 5643
    Beta strandi567 – 5737
    Turni578 – 5814
    Beta strandi585 – 5917
    Beta strandi597 – 6026
    Helixi608 – 62215
    Beta strandi639 – 6413
    Helixi667 – 67610
    Helixi679 – 68810
    Turni693 – 6953
    Helixi698 – 7003
    Helixi703 – 72119
    Helixi726 – 73914
    Beta strandi745 – 7473
    Beta strandi752 – 7543
    Helixi755 – 77925
    Beta strandi785 – 7873
    Helixi789 – 7968
    Beta strandi799 – 8035
    Beta strandi806 – 8083
    Helixi809 – 82012
    Helixi824 – 8263
    Beta strandi829 – 84113
    Helixi844 – 8485
    Helixi849 – 8513
    Beta strandi855 – 86410
    Helixi866 – 8683
    Helixi869 – 8757
    Beta strandi882 – 8843
    Helixi886 – 8883
    Beta strandi889 – 8913
    Beta strandi893 – 9008
    Helixi901 – 9055
    Helixi906 – 9083
    Beta strandi912 – 9143
    Beta strandi916 – 92510
    Beta strandi928 – 9347
    Beta strandi947 – 9504
    Beta strandi952 – 9565
    Helixi958 – 9603
    Beta strandi962 – 9643
    Beta strandi967 – 9693
    Beta strandi974 – 9763
    Beta strandi983 – 9864
    Beta strandi988 – 9925
    Helixi994 – 9963
    Beta strandi997 – 100913

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    1UK0X-ray3.00A/B662-1011[»]
    1UK1X-ray3.00A/B662-1011[»]
    1WOKX-ray3.00A/B/C/D662-1011[»]
    2COKNMR-A387-486[»]
    2CR9NMR-A518-643[»]
    2CS2NMR-A103-223[»]
    2DMJNMR-A1-93[»]
    2JVNNMR-A233-358[»]
    2L30NMR-A1-108[»]
    2L31NMR-A103-214[»]
    2RCWX-ray2.80A662-1011[»]
    2RD6X-ray2.30A662-1011[»]
    2RIQX-ray1.70A216-366[»]
    3GJWX-ray2.30A662-1011[»]
    3GN7X-ray2.50A662-1011[»]
    3L3LX-ray2.50A662-1011[»]
    3L3MX-ray2.50A662-1011[»]
    3OD8X-ray2.40A/B/C/D/E/F/G/H2-96[»]
    3ODAX-ray2.64A/B/C/D/E/F/G/H2-96[»]
    3ODCX-ray2.80A/B105-206[»]
    3ODEX-ray2.95A/B105-206[»]
    4AV1X-ray3.10A/B/C/D5-202[»]
    4DQYX-ray3.25A/D1-96[»]
    B/E216-366[»]
    C/F518-1014[»]
    4GV7X-ray2.89A/B/C/D662-1011[»]
    4HHYX-ray2.36A/B/C/D660-1011[»]
    4HHZX-ray2.72A/B/C/D660-1011[»]
    4L6SX-ray2.20A/B662-1011[»]
    ProteinModelPortaliP09874.
    SMRiP09874. Positions 1-359, 381-489, 520-1011.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiP09874.

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini385 – 47692BRCTPROSITE-ProRule annotationAdd
    BLAST
    Domaini662 – 779118PARP alpha-helicalPROSITE-ProRule annotationAdd
    BLAST
    Domaini788 – 1014227PARP catalyticPROSITE-ProRule annotationAdd
    BLAST

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni373 – 524152Automodification domainAdd
    BLAST

    Motif

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Motifi207 – 2093Nuclear localization signal1 Publication
    Motifi221 – 2266Nuclear localization signal1 Publication

    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.
    HOGENOMiHOG000030402.
    HOVERGENiHBG053513.
    InParanoidiP09874.
    KOiK10798.
    OMAiITAWTKC.
    OrthoDBiEOG7KM5S0.
    PhylomeDBiP09874.
    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.

    P09874-1 [UniParc]FASTAAdd to Basket

    « Hide

    MAESSDKLYR VEYAKSGRAS CKKCSESIPK DSLRMAIMVQ SPMFDGKVPH     50
    WYHFSCFWKV GHSIRHPDVE VDGFSELRWD DQQKVKKTAE AGGVTGKGQD 100
    GIGSKAEKTL GDFAAEYAKS NRSTCKGCME KIEKGQVRLS KKMVDPEKPQ 150
    LGMIDRWYHP GCFVKNREEL GFRPEYSASQ LKGFSLLATE DKEALKKQLP 200
    GVKSEGKRKG DEVDGVDEVA KKKSKKEKDK DSKLEKALKA QNDLIWNIKD 250
    ELKKVCSTND LKELLIFNKQ QVPSGESAIL DRVADGMVFG ALLPCEECSG 300
    QLVFKSDAYY CTGDVTAWTK CMVKTQTPNR KEWVTPKEFR EISYLKKLKV 350
    KKQDRIFPPE TSASVAATPP PSTASAPAAV NSSASADKPL SNMKILTLGK 400
    LSRNKDEVKA MIEKLGGKLT GTANKASLCI STKKEVEKMN KKMEEVKEAN 450
    IRVVSEDFLQ DVSASTKSLQ ELFLAHILSP WGAEVKAEPV EVVAPRGKSG 500
    AALSKKSKGQ VKEEGINKSE KRMKLTLKGG AAVDPDSGLE HSAHVLEKGG 550
    KVFSATLGLV DIVKGTNSYY KLQLLEDDKE NRYWIFRSWG RVGTVIGSNK 600
    LEQMPSKEDA IEHFMKLYEE KTGNAWHSKN FTKYPKKFYP LEIDYGQDEE 650
    AVKKLTVNPG TKSKLPKPVQ DLIKMIFDVE SMKKAMVEYE IDLQKMPLGK 700
    LSKRQIQAAY SILSEVQQAV SQGSSDSQIL DLSNRFYTLI PHDFGMKKPP 750
    LLNNADSVQA KVEMLDNLLD IEVAYSLLRG GSDDSSKDPI DVNYEKLKTD 800
    IKVVDRDSEE AEIIRKYVKN THATTHNAYD LEVIDIFKIE REGECQRYKP 850
    FKQLHNRRLL WHGSRTTNFA GILSQGLRIA PPEAPVTGYM FGKGIYFADM 900
    VSKSANYCHT SQGDPIGLIL LGEVALGNMY ELKHASHISK LPKGKHSVKG 950
    LGKTTPDPSA NISLDGVDVP LGTGISSGVN DTSLLYNEYI VYDIAQVNLK 1000
    YLLKLKFNFK TSLW 1014
    Length:1,014
    Mass (Da):113,084
    Last modified:January 23, 2007 - v4
    Checksum:i6A5FC01EB91C046B
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti17 – 171G → E in AAB59447. (PubMed:2824474)Curated
    Sequence conflicti70 – 701E → Q in AAA60137. (PubMed:3120710)Curated
    Sequence conflicti212 – 2121E → K in AAB59447. (PubMed:2824474)Curated
    Sequence conflicti613 – 6131H → Q in AAA60155. (PubMed:2891139)Curated
    Sequence conflicti827 – 8271N → S in AAA60155. (PubMed:2891139)Curated
    Sequence conflicti908 – 9081C → Y in AAA60155. (PubMed:2891139)Curated
    Sequence conflicti980 – 9801N → I in AAA60155. (PubMed:2891139)Curated

    Natural variant

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti54 – 541F → L.
    Corresponds to variant rs3738708 [ dbSNP | Ensembl ].
    VAR_050460
    Natural varianti188 – 1881A → T.1 Publication
    Corresponds to variant rs1805409 [ dbSNP | Ensembl ].
    VAR_014714
    Natural varianti334 – 3341V → I.1 Publication
    Corresponds to variant rs3219057 [ dbSNP | Ensembl ].
    VAR_019171
    Natural varianti377 – 3771P → S.
    Corresponds to variant rs2230484 [ dbSNP | Ensembl ].
    VAR_050461
    Natural varianti383 – 3831S → Y.1 Publication
    Corresponds to variant rs3219062 [ dbSNP | Ensembl ].
    VAR_019172
    Natural varianti488 – 4881E → V in a breast cancer sample; somatic mutation. 1 Publication
    VAR_035852
    Natural varianti762 – 7621V → A.2 Publications
    Corresponds to variant rs1136410 [ dbSNP | Ensembl ].
    VAR_014715
    Natural varianti940 – 9401K → R.2 Publications
    Corresponds to variant rs3219145 [ dbSNP | Ensembl ].
    VAR_019173

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    M18112 mRNA. Translation: AAA60137.1.
    J03473 mRNA. Translation: AAB59447.1.
    M32721 mRNA. Translation: AAA60155.1.
    M29786
    , M29545, M29766, M29767, M29768, M29769, M29770, M29771, M29772, M29773, M29774, M29775, M29776, M29777, M29778, M29779, M29780, M29781, M29783, M29784, M29785, M29544, M29782 Genomic DNA. Translation: AAA51663.1.
    AF524947 Genomic DNA. Translation: AAM75364.1.
    AL359704, AL359742 Genomic DNA. Translation: CAH70215.1.
    AL359742, AL359704 Genomic DNA. Translation: CAI12102.1.
    CH471098 Genomic DNA. Translation: EAW69783.1.
    BC037545 mRNA. Translation: AAH37545.1.
    X56140, X56141 Genomic DNA. Translation: CAA39606.1.
    X16674 Genomic DNA. Translation: CAA34663.1.
    M60436 Genomic DNA. Translation: AAA60000.1.
    M17081 mRNA. Translation: AAA51599.1. Sequence problems.
    CCDSiCCDS1554.1.
    PIRiA29725.
    RefSeqiNP_001609.2. NM_001618.3.
    UniGeneiHs.177766.

    Genome annotation databases

    EnsembliENST00000366794; ENSP00000355759; ENSG00000143799.
    GeneIDi142.
    KEGGihsa:142.
    UCSCiuc001hqd.4. human.

    Polymorphism databases

    DMDMi130781.

    Keywords - Coding sequence diversityi

    Polymorphism

    Cross-referencesi

    Web resourcesi

    NIEHS-SNPs

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    M18112 mRNA. Translation: AAA60137.1 .
    J03473 mRNA. Translation: AAB59447.1 .
    M32721 mRNA. Translation: AAA60155.1 .
    M29786
    , M29545 , M29766 , M29767 , M29768 , M29769 , M29770 , M29771 , M29772 , M29773 , M29774 , M29775 , M29776 , M29777 , M29778 , M29779 , M29780 , M29781 , M29783 , M29784 , M29785 , M29544 , M29782 Genomic DNA. Translation: AAA51663.1 .
    AF524947 Genomic DNA. Translation: AAM75364.1 .
    AL359704 , AL359742 Genomic DNA. Translation: CAH70215.1 .
    AL359742 , AL359704 Genomic DNA. Translation: CAI12102.1 .
    CH471098 Genomic DNA. Translation: EAW69783.1 .
    BC037545 mRNA. Translation: AAH37545.1 .
    X56140 , X56141 Genomic DNA. Translation: CAA39606.1 .
    X16674 Genomic DNA. Translation: CAA34663.1 .
    M60436 Genomic DNA. Translation: AAA60000.1 .
    M17081 mRNA. Translation: AAA51599.1 . Sequence problems.
    CCDSi CCDS1554.1.
    PIRi A29725.
    RefSeqi NP_001609.2. NM_001618.3.
    UniGenei Hs.177766.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    1UK0 X-ray 3.00 A/B 662-1011 [» ]
    1UK1 X-ray 3.00 A/B 662-1011 [» ]
    1WOK X-ray 3.00 A/B/C/D 662-1011 [» ]
    2COK NMR - A 387-486 [» ]
    2CR9 NMR - A 518-643 [» ]
    2CS2 NMR - A 103-223 [» ]
    2DMJ NMR - A 1-93 [» ]
    2JVN NMR - A 233-358 [» ]
    2L30 NMR - A 1-108 [» ]
    2L31 NMR - A 103-214 [» ]
    2RCW X-ray 2.80 A 662-1011 [» ]
    2RD6 X-ray 2.30 A 662-1011 [» ]
    2RIQ X-ray 1.70 A 216-366 [» ]
    3GJW X-ray 2.30 A 662-1011 [» ]
    3GN7 X-ray 2.50 A 662-1011 [» ]
    3L3L X-ray 2.50 A 662-1011 [» ]
    3L3M X-ray 2.50 A 662-1011 [» ]
    3OD8 X-ray 2.40 A/B/C/D/E/F/G/H 2-96 [» ]
    3ODA X-ray 2.64 A/B/C/D/E/F/G/H 2-96 [» ]
    3ODC X-ray 2.80 A/B 105-206 [» ]
    3ODE X-ray 2.95 A/B 105-206 [» ]
    4AV1 X-ray 3.10 A/B/C/D 5-202 [» ]
    4DQY X-ray 3.25 A/D 1-96 [» ]
    B/E 216-366 [» ]
    C/F 518-1014 [» ]
    4GV7 X-ray 2.89 A/B/C/D 662-1011 [» ]
    4HHY X-ray 2.36 A/B/C/D 660-1011 [» ]
    4HHZ X-ray 2.72 A/B/C/D 660-1011 [» ]
    4L6S X-ray 2.20 A/B 662-1011 [» ]
    ProteinModelPortali P09874.
    SMRi P09874. Positions 1-359, 381-489, 520-1011.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 106652. 191 interactions.
    DIPi DIP-38N.
    IntActi P09874. 65 interactions.
    MINTi MINT-104344.
    STRINGi 9606.ENSP00000355759.

    Chemistry

    BindingDBi P09874.
    ChEMBLi CHEMBL3105.
    GuidetoPHARMACOLOGYi 2771.

    PTM databases

    PhosphoSitei P09874.

    Polymorphism databases

    DMDMi 130781.

    2D gel databases

    SWISS-2DPAGE P09874.

    Proteomic databases

    MaxQBi P09874.
    PaxDbi P09874.
    PeptideAtlasi P09874.
    PRIDEi P09874.

    Protocols and materials databases

    DNASUi 142.
    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000366794 ; ENSP00000355759 ; ENSG00000143799 .
    GeneIDi 142.
    KEGGi hsa:142.
    UCSCi uc001hqd.4. human.

    Organism-specific databases

    CTDi 142.
    GeneCardsi GC01M226548.
    H-InvDB HIX0023551.
    HGNCi HGNC:270. PARP1.
    HPAi CAB000147.
    CAB003839.
    CAB003840.
    HPA045168.
    MIMi 173870. gene.
    neXtProti NX_P09874.
    PharmGKBi PA32.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi NOG243963.
    HOGENOMi HOG000030402.
    HOVERGENi HBG053513.
    InParanoidi P09874.
    KOi K10798.
    OMAi ITAWTKC.
    OrthoDBi EOG7KM5S0.
    PhylomeDBi P09874.
    TreeFami TF316616.

    Enzyme and pathway databases

    BRENDAi 2.4.2.30. 2681.
    Reactomei REACT_121111. Downregulation of SMAD2/3:SMAD4 transcriptional activity.
    SignaLinki P09874.

    Miscellaneous databases

    ChiTaRSi PARP1. human.
    EvolutionaryTracei P09874.
    GeneWikii PARP1.
    GenomeRNAii 142.
    NextBioi 565.
    PMAP-CutDB P09874.
    PROi P09874.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi P09874.
    Bgeei P09874.
    CleanExi HS_PARP1.
    Genevestigatori P09874.

    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. "Nucleotide sequence of a full-length cDNA for human fibroblast poly(ADP-ribose) polymerase."
      Uchida K., Morita T., Sato T., Ogura T., Yamashita R., Noguchi S., Suzuki H., Nyunoya H., Miwa M., Sugimura T.
      Biochem. Biophys. Res. Commun. 148:617-622(1987) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA].
      Tissue: Fibroblast.
    2. "Primary structure of human poly(ADP-ribose) synthetase as deduced from cDNA sequence."
      Kurosaki T., Ushiro H., Mitsuuchi Y., Suzuki S., Matsuda M., Matsuda Y., Katunuma N., Kangawa K., Matsuo H., Hirose T., Inayama S., Shizuta Y.
      J. Biol. Chem. 262:15990-15997(1987) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA].
      Tissue: Fibroblast.
    3. "cDNA sequence, protein structure, and chromosomal location of the human gene for poly(ADP-ribose) polymerase."
      Cherney B.W., McBride O.W., Chen D., Alkhatib H., Bhatia K., Hensley P., Smulson M.E.
      Proc. Natl. Acad. Sci. U.S.A. 84:8370-8374(1987) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA], VARIANT ARG-940.
    4. "Human nuclear NAD+ ADP-ribosyltransferase(polymerizing): organization of the gene."
      Auer B., Nagl U., Herzog H., Schneider R., Schweiger M.
      DNA 8:575-580(1989) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    5. NIEHS SNPs program
      Submitted (JUN-2002) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], VARIANTS THR-188; ILE-334; TYR-383; ALA-762 AND ARG-940.
    6. "The DNA sequence and biological annotation of human chromosome 1."
      Gregory S.G., Barlow K.F., McLay K.E., Kaul R., Swarbreck D., Dunham A., Scott C.E., Howe K.L., Woodfine K., Spencer C.C.A., Jones M.C., Gillson C., Searle S., Zhou Y., Kokocinski F., McDonald L., Evans R., Phillips K.
      , Atkinson A., Cooper R., Jones C., Hall R.E., Andrews T.D., Lloyd C., Ainscough R., Almeida J.P., Ambrose K.D., Anderson F., Andrew R.W., Ashwell R.I.S., Aubin K., Babbage A.K., Bagguley C.L., Bailey J., Beasley H., Bethel G., Bird C.P., Bray-Allen S., Brown J.Y., Brown A.J., Buckley D., Burton J., Bye J., Carder C., Chapman J.C., Clark S.Y., Clarke G., Clee C., Cobley V., Collier R.E., Corby N., Coville G.J., Davies J., Deadman R., Dunn M., Earthrowl M., Ellington A.G., Errington H., Frankish A., Frankland J., French L., Garner P., Garnett J., Gay L., Ghori M.R.J., Gibson R., Gilby L.M., Gillett W., Glithero R.J., Grafham D.V., Griffiths C., Griffiths-Jones S., Grocock R., Hammond S., Harrison E.S.I., Hart E., Haugen E., Heath P.D., Holmes S., Holt K., Howden P.J., Hunt A.R., Hunt S.E., Hunter G., Isherwood J., James R., Johnson C., Johnson D., Joy A., Kay M., Kershaw J.K., Kibukawa M., Kimberley A.M., King A., Knights A.J., Lad H., Laird G., Lawlor S., Leongamornlert D.A., Lloyd D.M., Loveland J., Lovell J., Lush M.J., Lyne R., Martin S., Mashreghi-Mohammadi M., Matthews L., Matthews N.S.W., McLaren S., Milne S., Mistry S., Moore M.J.F., Nickerson T., O'Dell C.N., Oliver K., Palmeiri A., Palmer S.A., Parker A., Patel D., Pearce A.V., Peck A.I., Pelan S., Phelps K., Phillimore B.J., Plumb R., Rajan J., Raymond C., Rouse G., Saenphimmachak C., Sehra H.K., Sheridan E., Shownkeen R., Sims S., Skuce C.D., Smith M., Steward C., Subramanian S., Sycamore N., Tracey A., Tromans A., Van Helmond Z., Wall M., Wallis J.M., White S., Whitehead S.L., Wilkinson J.E., Willey D.L., Williams H., Wilming L., Wray P.W., Wu Z., Coulson A., Vaudin M., Sulston J.E., Durbin R.M., Hubbard T., Wooster R., Dunham I., Carter N.P., McVean G., Ross M.T., Harrow J., Olson M.V., Beck S., Rogers J., Bentley D.R.
      Nature 441:315-321(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    7. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    8. "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], VARIANT ALA-762.
      Tissue: Brain.
    9. Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-95.
    10. "Characterization of a putative promoter region of the human poly(ADP-ribose) polymerase gene: structural similarity to that of the DNA polymerase beta gene."
      Ogura T., Nyunoya H., Takahashi-Masutani M., Miwa M., Sugimura T., Esumi H.
      Biochem. Biophys. Res. Commun. 167:701-710(1990) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-40.
    11. "Human pADPRT is involved in the regulation of its own gene."
      Herzog H., Schneider R., Hirsch-Kauffmann M., Schnitzer D., Schweiger M.
      Submitted (JUL-1991) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-40.
    12. Cited for: PROTEIN SEQUENCE OF 2-10; 35-47; 66-78; 109-119; 183-197; 209-221; 263-282; 453-467; 487-496; 529-548; 552-564; 572-582; 637-654; 668-695; 748-761; 780-796; 803-816 AND 859-903, CLEAVAGE OF INITIATOR METHIONINE, ACETYLATION AT ALA-2, IDENTIFICATION BY MASS SPECTROMETRY.
      Tissue: Colon carcinoma and Ovarian carcinoma.
    13. "Txk, a member of the non-receptor tyrosine kinase of the Tec family, forms a complex with poly(ADP-ribose) polymerase 1 and elongation factor 1alpha and regulates interferon-gamma gene transcription in Th1 cells."
      Maruyama T., Nara K., Yoshikawa H., Suzuki N.
      Clin. Exp. Immunol. 147:164-175(2007) [PubMed] [Europe PMC] [Abstract]
      Cited for: PROTEIN SEQUENCE OF 166-177 AND 356-367, INTERACTION WITH EEF1A1 AND TXK, PHOSPHORYLATION BY TXK, SUBCELLULAR LOCATION, FUNCTION AS A TRANSCRIPTION FACTOR.
    14. "Isolation of a cDNA clone for human NAD+: protein ADP-ribosyltransferase."
      Schneider R., Auer B., Kuhne C., Herzog H., Klocker H., Burtscher H.J., Hirsch-Kauffmann M., Wintersberger U., Schweiger M.
      Eur. J. Cell Biol. 44:302-307(1987) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 381-420 AND 682-710.
    15. "Molecular cloning of cDNA for human poly(ADP-ribose) polymerase and expression of its gene during HL-60 cell differentiation."
      Suzuki H., Uchida K., Shima H., Sato T., Okamoto T., Kimura T., Miwa M.
      Biochem. Biophys. Res. Commun. 146:403-409(1987) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 441-1014.
    16. Erratum
      Suzuki H., Uchida K., Shima H., Sato T., Okamoto T., Kimura T., Miwa M.
      Biochem. Biophys. Res. Commun. 148:1549-1550(1987)
    17. "The second zinc-finger domain of poly(ADP-ribose) polymerase determines specificity for single-stranded breaks in DNA."
      Gradwohl G., Menissier-de Murcia J., Molinete M., Simonin F., Koken M.H.M., Hoeijmakers J.H.J., de Murcia G.M.
      Proc. Natl. Acad. Sci. U.S.A. 87:2990-2994(1990) [PubMed] [Europe PMC] [Abstract]
      Cited for: ANALYSIS OF ZINC-FINGERS.
    18. "The zinc fingers of human poly(ADP-ribose) polymerase are differentially required for the recognition of DNA breaks and nicks and the consequent enzyme activation. Other structures recognize intact DNA."
      Ikelima M., Noguchi S., Yamashita R., Ogura T., Sugimura T., Gill D.M., Miwa M.
      J. Biol. Chem. 265:21907-21913(1990) [PubMed] [Europe PMC] [Abstract]
      Cited for: ANALYSIS OF ZINC-FINGERS.
    19. "Expression and site-directed mutagenesis of the catalytic domain of human poly(ADP-ribose)polymerase in Escherichia coli. Lysine 893 is critical for activity."
      Simonin F., Menissier-de Murcia J., Poch O., Muller S., Gradwohl G., Molinete M., Penning C., Keith G., de Murcia G.M.
      J. Biol. Chem. 265:19249-19256(1990) [PubMed] [Europe PMC] [Abstract]
      Cited for: MUTAGENESIS OF CATALYTIC DOMAIN.
    20. "The human poly(ADP-ribose) polymerase nuclear localization signal is a bipartite element functionally separate from DNA binding and catalytic activity."
      Schreiber V., Molinete M., Boeuf H., de Murcia G.M., Menissier-de Murcia J.
      EMBO J. 11:3263-3269(1992) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEAR LOCALIZATION SIGNAL.
    21. "Random mutagenesis of the poly(ADP-ribose) polymerase catalytic domain reveals amino acids involved in polymer branching."
      Rolli V., O'Farrell M., Menissier-de Murcia J., de Murcia G.M.
      Biochemistry 36:12147-12154(1997) [PubMed] [Europe PMC] [Abstract]
      Cited for: MUTAGENESIS OF CATALYTIC DOMAIN.
    22. "Functional association of poly(ADP-ribose) polymerase with DNA polymerase alpha-primase complex: a link between DNA strand break detection and DNA replication."
      Dantzer F., Nasheuer H.P., Vonesch J.L., de Murcia G., Menissier-de Murcia J.
      Nucleic Acids Res. 26:1891-1898(1998) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH POLA1.
    23. "Suppression of the poly(ADP-ribose) polymerase activity by DNA-dependent protein kinase in vitro."
      Ariumi Y., Masutani M., Copeland T.D., Mimori T., Sugimura T., Shimotohno K., Ueda K., Hatanaka M., Noda M.
      Oncogene 18:4616-4625(1999) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION.
    24. Cited for: INTERACTION WITH APTX.
    25. "The poly(ADP-ribose) polymerase 1 interacts with Sry and modulates its biological functions."
      Li Y., Oh H.J., Lau Y.-F.C.
      Mol. Cell. Endocrinol. 257:35-46(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH SRY.
    26. "A novel human AP endonuclease with conserved zinc-finger-like motifs involved in DNA strand break responses."
      Kanno S., Kuzuoka H., Sasao S., Hong Z., Lan L., Nakajima S., Yasui A.
      EMBO J. 26:2094-2103(2007) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH APLF.
    27. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-179, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Embryonic kidney.
    28. "Poly(ADP-ribose)-binding zinc finger motifs in DNA repair/checkpoint proteins."
      Ahel I., Ahel D., Matsusaka T., Clark A.J., Pines J., Boulton S.J., West S.C.
      Nature 451:81-85(2008) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, CATALYTIC ACTIVITY.
    29. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-368 AND SER-782, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    30. "Poly(ADP-ribose) polymerase-1 (PARP-1) transcriptionally regulates angiotensin AT2 receptor (AT2R) and AT2R binding protein (ATBP) genes."
      Reinemund J., Seidel K., Steckelings U.M., Zaade D., Klare S., Rompe F., Katerbaum M., Schacherl J., Li Y., Menk M., Schefe J.H., Goldin-Lang P., Szabo C., Olah G., Unger T., Funke-Kaiser H.
      Biochem. Pharmacol. 77:1795-1805(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION.
    31. "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.
    32. "Quantitative phosphoproteomic analysis of T cell receptor signaling reveals system-wide modulation of protein-protein interactions."
      Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K., Rodionov V., Han D.K.
      Sci. Signal. 2:RA46-RA46(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-782, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Leukemic T-cell.
    33. "Poly(ADP-ribose)-dependent regulation of DNA repair by the chromatin remodeling enzyme ALC1."
      Ahel D., Horejsi Z., Wiechens N., Polo S.E., Garcia-Wilson E., Ahel I., Flynn H., Skehel M., West S.C., Jackson S.P., Owen-Hughes T., Boulton S.J.
      Science 325:1240-1243(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, POLY-ADP-RIBOSYLATION, INTERACTION WITH CHD1L.
    34. "Lysine acetylation targets protein complexes and co-regulates major cellular functions."
      Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T.C., Olsen J.V., Mann M.
      Science 325:834-840(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-97; LYS-105; LYS-131; LYS-600 AND LYS-621, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    35. "Quantitative phosphoproteomics reveals widespread full phosphorylation site occupancy during mitosis."
      Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L., Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S., Mann M.
      Sci. Signal. 3:RA3-RA3(2010) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-41 AND SER-782, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    36. "Toward a unified nomenclature for mammalian ADP-ribosyltransferases."
      Hottiger M.O., Hassa P.O., Luscher B., Schuler H., Koch-Nolte F.
      Trends Biochem. Sci. 35:208-219(2010) [PubMed] [Europe PMC] [Abstract]
      Cited for: NOMENCLATURE.
    37. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    38. "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.
    39. Cited for: INTERACTION WITH RNF146, SUBCELLULAR LOCATION.
    40. "System-wide temporal characterization of the proteome and phosphoproteome of human embryonic stem cell differentiation."
      Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J., Johansen P.T., Kratchmarova I., Kassem M., Mann M., Olsen J.V., Blagoev B.
      Sci. Signal. 4:RS3-RS3(2011) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-782, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    41. "Exome capture reveals ZNF423 and CEP164 mutations, linking renal ciliopathies to DNA damage response signaling."
      Chaki M., Airik R., Ghosh A.K., Giles R.H., Chen R., Slaats G.G., Wang H., Hurd T.W., Zhou W., Cluckey A., Gee H.Y., Ramaswami G., Hong C.J., Hamilton B.A., Cervenka I., Ganji R.S., Bryja V., Arts H.H.
      , van Reeuwijk J., Oud M.M., Letteboer S.J., Roepman R., Husson H., Ibraghimov-Beskrovnaya O., Yasunaga T., Walz G., Eley L., Sayer J.A., Schermer B., Liebau M.C., Benzing T., Le Corre S., Drummond I., Janssen S., Allen S.J., Natarajan S., O'Toole J.F., Attanasio M., Saunier S., Antignac C., Koenekoop R.K., Ren H., Lopez I., Nayir A., Stoetzel C., Dollfus H., Massoudi R., Gleeson J.G., Andreoli S.P., Doherty D.G., Lindstrad A., Golzio C., Katsanis N., Pape L., Abboud E.B., Al-Rajhi A.A., Lewis R.A., Omran H., Lee E.Y., Wang S., Sekiguchi J.M., Saunders R., Johnson C.A., Garner E., Vanselow K., Andersen J.S., Shlomai J., Nurnberg G., Nurnberg P., Levy S., Smogorzewska A., Otto E.A., Hildebrandt F.
      Cell 150:533-548(2012) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH ZNF423.
    42. "Systematic analysis of protein pools, isoforms, and modifications affecting turnover and subcellular localization."
      Ahmad Y., Boisvert F.M., Lundberg E., Uhlen M., Lamond A.I.
      Mol. Cell. Proteomics 11:M111.013680.01-M111.013680.15(2012) [PubMed] [Europe PMC] [Abstract]
      Cited for: SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
    43. Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    44. "BAL1 and its partner E3 ligase, BBAP, link Poly(ADP-ribose) activation, ubiquitylation, and double-strand DNA repair independent of ATM, MDC1, and RNF8."
      Yan Q., Xu R., Zhu L., Cheng X., Wang Z., Manis J., Shipp M.A.
      Mol. Cell. Biol. 33:845-857(2013) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, SUBCELLULAR LOCATION, INTERACTION WITH PARP9.
    45. "Solution structure of the first ZF-PARP domain, of the BRCT domain and of the WGR domain of human poly(ADP-ribose)polymerase-1."
      RIKEN structural genomics initiative (RSGI)
      Submitted (APR-2007) to the PDB data bank
      Cited for: STRUCTURE BY NMR OF 1-93 AND 385-643.
    46. Cited for: VARIANT [LARGE SCALE ANALYSIS] VAL-488.

    Entry informationi

    Entry nameiPARP1_HUMAN
    AccessioniPrimary (citable) accession number: P09874
    Secondary accession number(s): B1ANJ4, Q8IUZ9
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: July 1, 1989
    Last sequence update: January 23, 2007
    Last modified: October 1, 2014
    This is version 188 of the entry and version 4 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programChordata Protein Annotation Program
    DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

    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, Direct protein sequencing, Reference proteome

    Documents

    1. Human chromosome 1
      Human chromosome 1: entries, gene names and cross-references to MIM
    2. Human entries with polymorphisms or disease mutations
      List of human entries with polymorphisms or disease mutations
    3. Human polymorphisms and disease mutations
      Index of human polymorphisms and disease mutations
    4. MIM cross-references
      Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
    5. PDB cross-references
      Index of Protein Data Bank (PDB) cross-references
    6. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3