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Q9Y6F1

- PARP3_HUMAN

UniProt

Q9Y6F1 - PARP3_HUMAN

Protein

Poly [ADP-ribose] polymerase 3

Gene

PARP3

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 141 (01 Oct 2014)
      Sequence version 3 (03 Mar 2009)
      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. May link the DNA damage surveillance network to the mitotic fidelity checkpoint. Negatively influences the G1/S cell cycle progression without interfering with centrosome duplication. Binds DNA. May be involved in the regulation of PRC2 and PRC3 complex-dependent gene silencing.1 Publication

    Catalytic activityi

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

    GO - Molecular functioni

    1. catalytic activity Source: ProtInc
    2. NAD+ ADP-ribosyltransferase activity Source: MGI

    GO - Biological processi

    1. DNA repair Source: ProtInc
    2. double-strand break repair Source: MGI
    3. positive regulation of DNA ligation Source: MGI
    4. protein ADP-ribosylation Source: MGI
    5. protein localization to site of double-strand break Source: MGI
    6. regulation of mitotic spindle organization Source: MGI
    7. telomere maintenance Source: MGI

    Keywords - Molecular functioni

    Glycosyltransferase, Transferase

    Keywords - Ligandi

    NAD

    Enzyme and pathway databases

    BRENDAi2.4.2.30. 2681.
    SignaLinkiQ9Y6F1.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Poly [ADP-ribose] polymerase 3 (EC:2.4.2.30)
    Short name:
    PARP-3
    Short name:
    hPARP-3
    Alternative name(s):
    ADP-ribosyltransferase diphtheria toxin-like 3
    Short name:
    ARTD3
    IRT1
    NAD(+) ADP-ribosyltransferase 3
    Short name:
    ADPRT-3
    Poly[ADP-ribose] synthase 3
    Short name:
    pADPRT-3
    Gene namesi
    Name:PARP3
    Synonyms:ADPRT3, ADPRTL3
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 3

    Organism-specific databases

    HGNCiHGNC:273. PARP3.

    Subcellular locationi

    Nucleus. Cytoplasmcytoskeletonmicrotubule organizing centercentrosome. Cytoplasmcytoskeletonmicrotubule organizing centercentrosomecentriole
    Note: Core component of the centrosome. Preferentially localized to the daughter centriole throughout the cell cycle. According to PubMed:16924674, it is almost exclusively localized in the nucleus and appears in numerous small foci and a small number of larger foci whereas a centrosomal location has not been detected.

    GO - Cellular componenti

    1. centriole Source: UniProtKB-SubCell
    2. nucleus Source: UniProtKB-SubCell
    3. site of double-strand break Source: MGI

    Keywords - Cellular componenti

    Cytoplasm, Cytoskeleton, Nucleus

    Pathology & Biotechi

    Organism-specific databases

    PharmGKBiPA24593.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 533533Poly [ADP-ribose] polymerase 3PRO_0000211329Add
    BLAST

    Post-translational modificationi

    Auto-poly(ADP)-ribosylation.

    Proteomic databases

    PaxDbiQ9Y6F1.
    PRIDEiQ9Y6F1.

    PTM databases

    PhosphoSiteiQ9Y6F1.

    Expressioni

    Tissue specificityi

    Widely expressed; the highest levels are in the kidney, skeletal muscle, liver, heart and spleen; also detected in pancreas, lung, placenta, brain, leukocytes, colon, small intestine, ovary, testis, prostate and thymus.

    Gene expression databases

    ArrayExpressiQ9Y6F1.
    BgeeiQ9Y6F1.
    CleanExiHS_PARP3.
    GenevestigatoriQ9Y6F1.

    Interactioni

    Subunit structurei

    Interacts with PRKDC and PARP1. Interacts with XRCC5; the interaction is dependent on nucleic acids. Interacts with XRCC6; the interaction is dependent on nucleic acids. Interacts with EZH2, HDAC1, HDAC2, SUZ12, YY1, LRIG3 and LIG4.2 Publications

    Protein-protein interaction databases

    BioGridi115351. 10 interactions.
    STRINGi9606.ENSP00000381740.

    Structurei

    Secondary structure

    1
    533
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Beta strandi50 – 534
    Turni54 – 563
    Beta strandi61 – 7414
    Turni75 – 784
    Beta strandi79 – 8911
    Beta strandi95 – 1006
    Beta strandi111 – 1177
    Helixi118 – 13316
    Helixi140 – 1423
    Beta strandi147 – 1493
    Beta strandi151 – 1533
    Helixi187 – 19610
    Helixi199 – 20810
    Turni213 – 2153
    Turni218 – 2203
    Helixi223 – 24018
    Beta strandi246 – 2483
    Helixi250 – 26011
    Beta strandi265 – 2684
    Helixi276 – 29823
    Helixi303 – 3075
    Beta strandi309 – 3113
    Helixi314 – 3218
    Beta strandi325 – 3284
    Helixi336 – 34611
    Beta strandi349 – 3513
    Beta strandi354 – 3629
    Turni364 – 3663
    Helixi367 – 3715
    Turni372 – 3754
    Beta strandi379 – 3857
    Helixi388 – 3903
    Helixi391 – 3977
    Beta strandi411 – 4188
    Helixi419 – 4235
    Beta strandi429 – 4313
    Beta strandi434 – 44512
    Beta strandi448 – 4547
    Beta strandi467 – 4715
    Beta strandi473 – 4775
    Helixi479 – 4813
    Beta strandi483 – 4875
    Beta strandi490 – 4945
    Beta strandi499 – 5013
    Helixi503 – 5053
    Beta strandi509 – 5124
    Beta strandi514 – 5196
    Helixi520 – 5223
    Beta strandi523 – 53210

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    2EOCNMR-A41-157[»]
    3C49X-ray2.80A178-532[»]
    3C4HX-ray2.10A178-532[»]
    3CE0X-ray2.80A178-532[»]
    3FHBX-ray2.30A178-532[»]
    4GV0X-ray1.90A178-532[»]
    4GV2X-ray1.80A178-532[»]
    4GV4X-ray1.80A178-532[»]
    4L6ZX-ray2.00A178-532[»]
    4L70X-ray2.00A178-532[»]
    4L7LX-ray2.10A178-532[»]
    4L7NX-ray1.80A178-532[»]
    4L7OX-ray2.00A178-532[»]
    4L7PX-ray2.30A178-532[»]
    4L7RX-ray2.20A178-532[»]
    4L7UX-ray2.80A178-532[»]
    ProteinModelPortaliQ9Y6F1.
    SMRiQ9Y6F1. Positions 41-157, 178-532.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiQ9Y6F1.

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini182 – 300119PARP alpha-helicalPROSITE-ProRule annotationAdd
    BLAST
    Domaini313 – 533221PARP catalyticPROSITE-ProRule annotationAdd
    BLAST

    Motif

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Motifi14 – 207Nuclear localization signalSequence Analysis

    Domaini

    According to PubMed:10329013, the N-terminal domain (54 amino acids) of isoform 2 is responsible for its centrosomal localization. The C-terminal region contains the catalytic domain.

    Sequence similaritiesi

    Contains 1 PARP alpha-helical domain.PROSITE-ProRule annotation
    Contains 1 PARP catalytic domain.PROSITE-ProRule annotation

    Phylogenomic databases

    eggNOGiNOG243963.
    HOGENOMiHOG000173055.
    HOVERGENiHBG053514.
    InParanoidiQ9Y6F1.
    KOiK10798.
    OMAiFSKEMFK.
    OrthoDBiEOG7RV9G0.
    PhylomeDBiQ9Y6F1.
    TreeFamiTF315407.

    Family and domain databases

    Gene3Di1.20.142.10. 1 hit.
    2.20.140.10. 1 hit.
    3.90.228.10. 1 hit.
    InterProiIPR012317. Poly(ADP-ribose)pol_cat_dom.
    IPR004102. Poly(ADP-ribose)pol_reg_dom.
    IPR008893. WGR_domain.
    [Graphical view]
    PfamiPF00644. PARP. 1 hit.
    PF02877. PARP_reg. 1 hit.
    PF05406. WGR. 1 hit.
    [Graphical view]
    SMARTiSM00773. WGR. 1 hit.
    [Graphical view]
    SUPFAMiSSF142921. SSF142921. 1 hit.
    SSF47587. SSF47587. 1 hit.
    PROSITEiPS51060. PARP_ALPHA_HD. 1 hit.
    PS51059. PARP_CATALYTIC. 1 hit.
    [Graphical view]

    Sequences (2)i

    Sequence statusi: Complete.

    This entry describes 2 isoformsi produced by alternative splicing. Align

    Isoform 1 (identifier: Q9Y6F1-1) [UniParc]FASTAAdd to Basket

    Also known as: Short

    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

    MAPKPKPWVQ TEGPEKKKGR QAGREEDPFR STAEALKAIP AEKRIIRVDP    50
    TCPLSSNPGT QVYEDYNCTL NQTNIENNNN KFYIIQLLQD SNRFFTCWNH 100
    WGRVGEVGQS KINHFTRLED AKKDFEKKFR EKTKNNWAER DHFVSHPGKY 150
    TLIEVQAEDE AQEAVVKVDR GPVRTVTKRV QPCSLDPATQ KLITNIFSKE 200
    MFKNTMALMD LDVKKMPLGK LSKQQIARGF EALEALEEAL KGPTDGGQSL 250
    EELSSHFYTV IPHNFGHSQP PPINSPELLQ AKKDMLLVLA DIELAQALQA 300
    VSEQEKTVEE VPHPLDRDYQ LLKCQLQLLD SGAPEYKVIQ TYLEQTGSNH 350
    RCPTLQHIWK VNQEGEEDRF QAHSKLGNRK LLWHGTNMAV VAAILTSGLR 400
    IMPHSGGRVG KGIYFASENS KSAGYVIGMK CGAHHVGYMF LGEVALGREH 450
    HINTDNPSLK SPPPGFDSVI ARGHTEPDPT QDTELELDGQ QVVVPQGQPV 500
    PCPEFSSSTF SQSEYLIYQE SQCRLRYLLE VHL 533

    Note: More abundant according to PubMed:16924674.

    Length:533
    Mass (Da):60,070
    Last modified:March 3, 2009 - v3
    Checksum:iBF728C3D88722029
    GO
    Isoform 2 (identifier: Q9Y6F1-2) [UniParc]FASTAAdd to Basket

    Also known as: Long

    The sequence of this isoform differs from the canonical sequence as follows:
         1-1: M → MSLLFLAM

    Show »
    Length:540
    Mass (Da):60,846
    Checksum:iAF68D80A50A78BC8
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti80 – 801N → K in AAD29855. (PubMed:10329013)Curated
    Sequence conflicti171 – 1711G → A in AAD29855. (PubMed:10329013)Curated
    Sequence conflicti411 – 4111K → E in CAB43246. (PubMed:17974005)Curated

    Natural variant

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti91 – 911S → N.
    Corresponds to variant rs34224216 [ dbSNP | Ensembl ].
    VAR_056643
    Natural varianti100 – 1001H → R.5 Publications
    Corresponds to variant rs28547534 [ dbSNP | Ensembl ].
    VAR_054622
    Natural varianti269 – 2691Q → R.
    Corresponds to variant rs323870 [ dbSNP | Ensembl ].
    VAR_056644

    Alternative sequence

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Alternative sequencei1 – 11M → MSLLFLAM in isoform 2. 2 PublicationsVSP_007863

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    Y16836 mRNA. Translation: CAC79988.1.
    AF083068 mRNA. Translation: AAD29855.1.
    AY126341 mRNA. Translation: AAM95460.1.
    AC115284 Genomic DNA. No translation available.
    BC014260 mRNA. Translation: AAH14260.1.
    AL050034 mRNA. Translation: CAB43246.1.
    CCDSiCCDS43097.1. [Q9Y6F1-1]
    CCDS46839.1. [Q9Y6F1-2]
    PIRiT08713.
    RefSeqiNP_001003931.2. NM_001003931.2. [Q9Y6F1-2]
    NP_005476.3. NM_005485.4. [Q9Y6F1-1]
    XP_005264836.2. XM_005264779.2.
    XP_006712977.1. XM_006712914.1.
    UniGeneiHs.271742.

    Genome annotation databases

    EnsembliENST00000398755; ENSP00000381740; ENSG00000041880. [Q9Y6F1-2]
    ENST00000417220; ENSP00000395951; ENSG00000041880. [Q9Y6F1-1]
    ENST00000431474; ENSP00000401511; ENSG00000041880. [Q9Y6F1-1]
    GeneIDi10039.
    KEGGihsa:10039.
    UCSCiuc003dby.3. human. [Q9Y6F1-1]
    uc003dbz.3. human. [Q9Y6F1-2]

    Polymorphism databases

    DMDMi224471880.

    Keywords - Coding sequence diversityi

    Alternative splicing, Polymorphism

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    Y16836 mRNA. Translation: CAC79988.1 .
    AF083068 mRNA. Translation: AAD29855.1 .
    AY126341 mRNA. Translation: AAM95460.1 .
    AC115284 Genomic DNA. No translation available.
    BC014260 mRNA. Translation: AAH14260.1 .
    AL050034 mRNA. Translation: CAB43246.1 .
    CCDSi CCDS43097.1. [Q9Y6F1-1 ]
    CCDS46839.1. [Q9Y6F1-2 ]
    PIRi T08713.
    RefSeqi NP_001003931.2. NM_001003931.2. [Q9Y6F1-2 ]
    NP_005476.3. NM_005485.4. [Q9Y6F1-1 ]
    XP_005264836.2. XM_005264779.2.
    XP_006712977.1. XM_006712914.1.
    UniGenei Hs.271742.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    2EOC NMR - A 41-157 [» ]
    3C49 X-ray 2.80 A 178-532 [» ]
    3C4H X-ray 2.10 A 178-532 [» ]
    3CE0 X-ray 2.80 A 178-532 [» ]
    3FHB X-ray 2.30 A 178-532 [» ]
    4GV0 X-ray 1.90 A 178-532 [» ]
    4GV2 X-ray 1.80 A 178-532 [» ]
    4GV4 X-ray 1.80 A 178-532 [» ]
    4L6Z X-ray 2.00 A 178-532 [» ]
    4L70 X-ray 2.00 A 178-532 [» ]
    4L7L X-ray 2.10 A 178-532 [» ]
    4L7N X-ray 1.80 A 178-532 [» ]
    4L7O X-ray 2.00 A 178-532 [» ]
    4L7P X-ray 2.30 A 178-532 [» ]
    4L7R X-ray 2.20 A 178-532 [» ]
    4L7U X-ray 2.80 A 178-532 [» ]
    ProteinModelPortali Q9Y6F1.
    SMRi Q9Y6F1. Positions 41-157, 178-532.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 115351. 10 interactions.
    STRINGi 9606.ENSP00000381740.

    Chemistry

    BindingDBi Q9Y6F1.
    ChEMBLi CHEMBL5083.

    PTM databases

    PhosphoSitei Q9Y6F1.

    Polymorphism databases

    DMDMi 224471880.

    Proteomic databases

    PaxDbi Q9Y6F1.
    PRIDEi Q9Y6F1.

    Protocols and materials databases

    DNASUi 10039.
    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000398755 ; ENSP00000381740 ; ENSG00000041880 . [Q9Y6F1-2 ]
    ENST00000417220 ; ENSP00000395951 ; ENSG00000041880 . [Q9Y6F1-1 ]
    ENST00000431474 ; ENSP00000401511 ; ENSG00000041880 . [Q9Y6F1-1 ]
    GeneIDi 10039.
    KEGGi hsa:10039.
    UCSCi uc003dby.3. human. [Q9Y6F1-1 ]
    uc003dbz.3. human. [Q9Y6F1-2 ]

    Organism-specific databases

    CTDi 10039.
    GeneCardsi GC03P051951.
    HGNCi HGNC:273. PARP3.
    MIMi 607726. gene.
    neXtProti NX_Q9Y6F1.
    PharmGKBi PA24593.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi NOG243963.
    HOGENOMi HOG000173055.
    HOVERGENi HBG053514.
    InParanoidi Q9Y6F1.
    KOi K10798.
    OMAi FSKEMFK.
    OrthoDBi EOG7RV9G0.
    PhylomeDBi Q9Y6F1.
    TreeFami TF315407.

    Enzyme and pathway databases

    BRENDAi 2.4.2.30. 2681.
    SignaLinki Q9Y6F1.

    Miscellaneous databases

    EvolutionaryTracei Q9Y6F1.
    GeneWikii PARP3.
    GenomeRNAii 10039.
    NextBioi 37913.
    PROi Q9Y6F1.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi Q9Y6F1.
    Bgeei Q9Y6F1.
    CleanExi HS_PARP3.
    Genevestigatori Q9Y6F1.

    Family and domain databases

    Gene3Di 1.20.142.10. 1 hit.
    2.20.140.10. 1 hit.
    3.90.228.10. 1 hit.
    InterProi IPR012317. Poly(ADP-ribose)pol_cat_dom.
    IPR004102. Poly(ADP-ribose)pol_reg_dom.
    IPR008893. WGR_domain.
    [Graphical view ]
    Pfami PF00644. PARP. 1 hit.
    PF02877. PARP_reg. 1 hit.
    PF05406. WGR. 1 hit.
    [Graphical view ]
    SMARTi SM00773. WGR. 1 hit.
    [Graphical view ]
    SUPFAMi SSF142921. SSF142921. 1 hit.
    SSF47587. SSF47587. 1 hit.
    PROSITEi PS51060. PARP_ALPHA_HD. 1 hit.
    PS51059. PARP_CATALYTIC. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. Koch-Nolte F.
      Submitted (MAR-1998) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2), VARIANT ARG-100.
    2. "A human poly(ADP-ribose) polymerase gene family (ADPRTL): cDNA cloning of two novel poly(ADP-ribose) polymerase homologues."
      Johansson M.
      Genomics 57:442-445(1999) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), VARIANT ARG-100.
      Tissue: Fetal brain.
    3. "PARP-3 localizes preferentially to the daughter centriole and interferes with the G1/S cell cycle progression."
      Augustin A., Spenlehauer C., Dumond H., Menissier-de Murcia J., Piel M., Schmit A.-C., Apiou F., Vonesch J.-L., Kock M., Bornens M., de Murcia G.M.
      J. Cell Sci. 116:1551-1562(2003) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2), VARIANT ARG-100, SUBCELLULAR LOCATION.
      Tissue: Frontal cortex.
    4. "The DNA sequence, annotation and analysis of human chromosome 3."
      Muzny D.M., Scherer S.E., Kaul R., Wang J., Yu J., Sudbrak R., Buhay C.J., Chen R., Cree A., Ding Y., Dugan-Rocha S., Gill R., Gunaratne P., Harris R.A., Hawes A.C., Hernandez J., Hodgson A.V., Hume J.
      , Jackson A., Khan Z.M., Kovar-Smith C., Lewis L.R., Lozado R.J., Metzker M.L., Milosavljevic A., Miner G.R., Morgan M.B., Nazareth L.V., Scott G., Sodergren E., Song X.-Z., Steffen D., Wei S., Wheeler D.A., Wright M.W., Worley K.C., Yuan Y., Zhang Z., Adams C.Q., Ansari-Lari M.A., Ayele M., Brown M.J., Chen G., Chen Z., Clendenning J., Clerc-Blankenburg K.P., Chen R., Chen Z., Davis C., Delgado O., Dinh H.H., Dong W., Draper H., Ernst S., Fu G., Gonzalez-Garay M.L., Garcia D.K., Gillett W., Gu J., Hao B., Haugen E., Havlak P., He X., Hennig S., Hu S., Huang W., Jackson L.R., Jacob L.S., Kelly S.H., Kube M., Levy R., Li Z., Liu B., Liu J., Liu W., Lu J., Maheshwari M., Nguyen B.-V., Okwuonu G.O., Palmeiri A., Pasternak S., Perez L.M., Phelps K.A., Plopper F.J., Qiang B., Raymond C., Rodriguez R., Saenphimmachak C., Santibanez J., Shen H., Shen Y., Subramanian S., Tabor P.E., Verduzco D., Waldron L., Wang J., Wang J., Wang Q., Williams G.A., Wong G.K.-S., Yao Z., Zhang J., Zhang X., Zhao G., Zhou J., Zhou Y., Nelson D., Lehrach H., Reinhardt R., Naylor S.L., Yang H., Olson M., Weinstock G., Gibbs R.A.
      Nature 440:1194-1198(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    5. "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] (ISOFORM 1), VARIANT ARG-100.
      Tissue: B-cell.
    6. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 75-533 (ISOFORM 1), VARIANT ARG-100.
      Tissue: Kidney.
    7. "PARP-3 associates with polycomb group bodies and with components of the DNA damage repair machinery."
      Rouleau M., McDonald D., Gagne P., Ouellet M.E., Droit A., Hunter J.M., Dutertre S., Prigent C., Hendzel M.J., Poirier G.G.
      J. Cell. Biochem. 100:385-401(2007) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, SUBCELLULAR LOCATION, INTERACTION WITH PRKDC; PARP1; EZH2; HDAC1; HDAC2; SUZ12; YY1; LRIG3 AND LIG4.
    8. "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.
    9. "Human poly(ADP-ribose) polymerase 3, catalytic fragment in complex with an inhibitor 3-aminobenzoic acid."
      Structural genomics consortium (SGC)
      Submitted (APR-2007) to the PDB data bank
      Cited for: X-RAY CRYSTALLOGRAPHY (2.3 ANGSTROMS) OF 178-532 IN COMPLEX WITH THE INHIBITOR 3-AMINOBENZOIC ACID.
    10. "Solution structure of the WGR domain from human poly [ADP-ribose] polymerase-3."
      RIKEN structural genomics initiative (RSGI)
      Submitted (APR-2008) to the PDB data bank
      Cited for: STRUCTURE BY NMR OF 41-157.

    Entry informationi

    Entry nameiPARP3_HUMAN
    AccessioniPrimary (citable) accession number: Q9Y6F1
    Secondary accession number(s): Q8NER9, Q96CG2, Q9UG81
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: September 26, 2001
    Last sequence update: March 3, 2009
    Last modified: October 1, 2014
    This is version 141 of the entry and version 3 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

    Keywords - Technical termi

    3D-structure, Complete proteome, Reference proteome

    Documents

    1. Human chromosome 3
      Human chromosome 3: 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