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Q9UKK3

- PARP4_HUMAN

UniProt

Q9UKK3 - PARP4_HUMAN

Protein

Poly [ADP-ribose] polymerase 4

Gene

PARP4

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 143 (01 Oct 2014)
      Sequence version 3 (05 Oct 2010)
      Previous versions | rss
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    Functioni

    Catalytic activityi

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

    GO - Molecular functioni

    1. DNA binding Source: ProtInc
    2. enzyme binding Source: MGI
    3. NAD+ ADP-ribosyltransferase activity Source: UniProtKB
    4. protein binding Source: IntAct

    GO - Biological processi

    1. cell death Source: UniProtKB
    2. cellular protein modification process Source: UniProtKB
    3. cellular response to DNA damage stimulus Source: UniProtKB
    4. DNA repair Source: UniProtKB
    5. inflammatory response Source: UniProtKB
    6. protein ADP-ribosylation Source: UniProtKB
    7. response to drug Source: UniProtKB
    8. transport Source: UniProtKB

    Keywords - Molecular functioni

    Glycosyltransferase, Ribonucleoprotein, Transferase

    Keywords - Ligandi

    NAD

    Enzyme and pathway databases

    BRENDAi2.4.2.30. 2681.
    SignaLinkiQ9UKK3.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Poly [ADP-ribose] polymerase 4 (EC:2.4.2.30)
    Short name:
    PARP-4
    Alternative name(s):
    193 kDa vault protein
    ADP-ribosyltransferase diphtheria toxin-like 4
    Short name:
    ARTD4
    PARP-related/IalphaI-related H5/proline-rich
    Short name:
    PH5P
    Vault poly(ADP-ribose) polymerase
    Short name:
    VPARP
    Gene namesi
    Name:PARP4
    Synonyms:ADPRTL1, KIAA0177, PARPL
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 13

    Organism-specific databases

    HGNCiHGNC:271. PARP4.

    Subcellular locationi

    Cytoplasm. Nucleus. Cytoplasmcytoskeletonspindle
    Note: Also found in the nucleus, associated with mitotic spindles.

    GO - Cellular componenti

    1. cytoplasm Source: UniProtKB
    2. extracellular vesicular exosome Source: UniProt
    3. membrane Source: UniProtKB
    4. nucleus Source: UniProtKB
    5. ribonucleoprotein complex Source: UniProtKB
    6. spindle microtubule Source: UniProtKB

    Keywords - Cellular componenti

    Cytoplasm, Cytoskeleton, Nucleus

    Pathology & Biotechi

    Organism-specific databases

    PharmGKBiPA24591.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 17241724Poly [ADP-ribose] polymerase 4PRO_0000211330Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei101 – 1011Phosphothreonine1 Publication
    Modified residuei1236 – 12361Phosphoserine1 Publication
    Modified residuei1335 – 13351Phosphoserine2 Publications
    Modified residuei1504 – 15041Phosphoserine1 Publication

    Keywords - PTMi

    Phosphoprotein

    Proteomic databases

    MaxQBiQ9UKK3.
    PaxDbiQ9UKK3.
    PeptideAtlasiQ9UKK3.
    PRIDEiQ9UKK3.

    PTM databases

    PhosphoSiteiQ9UKK3.

    Expressioni

    Tissue specificityi

    Widely expressed; the highest levels are in the kidney; also detected in heart, placenta, lung, liver, skeletal muscle, spleen, leukocytes and pancreas.

    Gene expression databases

    BgeeiQ9UKK3.
    CleanExiHS_PARP4.
    GenevestigatoriQ9UKK3.

    Organism-specific databases

    HPAiHPA011739.

    Interactioni

    Subunit structurei

    Component of the vault ribonucleoprotein particle, at least composed of MVP, PARP4 and one or more vault RNAs (vRNAs). Binds to MVP. Associates with TEP1.

    Binary interactionsi

    WithEntry#Exp.IntActNotes
    ORFQ9Q2G43EBI-2623021,EBI-6248094From a different organism.

    Protein-protein interaction databases

    BioGridi106653. 8 interactions.
    IntActiQ9UKK3. 14 interactions.
    MINTiMINT-6768840.
    STRINGi9606.ENSP00000371419.

    Structurei

    3D structure databases

    ProteinModelPortaliQ9UKK3.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini1 – 9494BRCTPROSITE-ProRule annotationAdd
    BLAST
    Domaini242 – 370129PARP alpha-helicalPROSITE-ProRule annotationAdd
    BLAST
    Domaini369 – 573205PARP catalyticPROSITE-ProRule annotationAdd
    BLAST
    Domaini607 – 735129VITPROSITE-ProRule annotationAdd
    BLAST
    Domaini876 – 1046171VWFAPROSITE-ProRule annotationAdd
    BLAST

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni1562 – 1724163Interaction with the major vault proteinAdd
    BLAST

    Motif

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Motifi19 – 257Nuclear localization signalSequence Analysis
    Motifi1237 – 124913Nuclear localization signalSequence AnalysisAdd
    BLAST

    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 1 VIT domain.PROSITE-ProRule annotation
    Contains 1 VWFA domain.PROSITE-ProRule annotation

    Phylogenomic databases

    eggNOGiCOG2304.
    HOGENOMiHOG000139369.
    HOVERGENiHBG053515.
    InParanoidiQ9UKK3.
    KOiK10798.
    OMAiQCTHIIL.
    OrthoDBiEOG75F4CF.
    PhylomeDBiQ9UKK3.
    TreeFamiTF329720.

    Family and domain databases

    Gene3Di1.20.142.10. 1 hit.
    3.40.50.10190. 1 hit.
    3.40.50.410. 1 hit.
    3.90.228.10. 1 hit.
    InterProiIPR001357. BRCT_dom.
    IPR012317. Poly(ADP-ribose)pol_cat_dom.
    IPR004102. Poly(ADP-ribose)pol_reg_dom.
    IPR013694. VIT.
    IPR002035. VWF_A.
    [Graphical view]
    PfamiPF00533. BRCT. 1 hit.
    PF00644. PARP. 1 hit.
    PF08487. VIT. 1 hit.
    PF00092. VWA. 1 hit.
    [Graphical view]
    SMARTiSM00292. BRCT. 1 hit.
    SM00609. VIT. 1 hit.
    SM00327. VWA. 1 hit.
    [Graphical view]
    SUPFAMiSSF47587. SSF47587. 1 hit.
    SSF52113. SSF52113. 1 hit.
    SSF53300. SSF53300. 1 hit.
    PROSITEiPS50172. BRCT. 1 hit.
    PS51060. PARP_ALPHA_HD. 1 hit.
    PS51059. PARP_CATALYTIC. 1 hit.
    PS51468. VIT. 1 hit.
    PS50234. VWFA. 1 hit.
    [Graphical view]

    Sequencei

    Sequence statusi: Complete.

    Q9UKK3-1 [UniParc]FASTAAdd to Basket

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    MVMGIFANCI FCLKVKYLPQ QQKKKLQTDI KENGGKFSFS LNPQCTHIIL     50
    DNADVLSQYQ LNSIQKNHVH IANPDFIWKS IREKRLLDVK NYDPYKPLDI 100
    TPPPDQKASS SEVKTEGLCP DSATEEEDTV ELTEFGMQNV EIPHLPQDFE 150
    VAKYNTLEKV GMEGGQEAVV VELQCSRDSR DCPFLISSHF LLDDGMETRR 200
    QFAIKKTSED ASEYFENYIE ELKKQGFLLR EHFTPEATQL ASEQLQALLL 250
    EEVMNSSTLS QEVSDLVEMI WAEALGHLEH MLLKPVNRIS LNDVSKAEGI 300
    LLLVKAALKN GETAEQLQKM MTEFYRLIPH KGTMPKEVNL GLLAKKADLC 350
    QLIRDMVNVC ETNLSKPNPP SLAKYRALRC KIEHVEQNTE EFLRVRKEVL 400
    QNHHSKSPVD VLQIFRVGRV NETTEFLSKL GNVRPLLHGS PVQNIVGILC 450
    RGLLLPKVVE DRGVQRTDVG NLGSGIYFSD SLSTSIKYSH PGETDGTRLL 500
    LICDVALGKC MDLHEKDFSL TEAPPGYDSV HGVSQTASVT TDFEDDEFVV 550
    YKTNQVKMKY IIKFSMPGDQ IKDFHPSDHT ELEEYRPEFS NFSKVEDYQL 600
    PDAKTSSSTK AGLQDASGNL VPLEDVHIKG RIIDTVAQVI VFQTYTNKSH 650
    VPIEAKYIFP LDDKAAVCGF EAFINGKHIV GEIKEKEEAQ QEYLEAVTQG 700
    HGAYLMSQDA PDVFTVSVGN LPPKAKVLIK ITYITELSIL GTVGVFFMPA 750
    TVAPWQQDKA LNENLQDTVE KICIKEIGTK QSFSLTMSIE MPYVIEFIFS 800
    DTHELKQKRT DCKAVISTME GSSLDSSGFS LHIGLSAAYL PRMWVEKHPE 850
    KESEACMLVF QPDLDVDLPD LASESEVIIC LDCSSSMEGV TFLQAKQIAL 900
    HALSLVGEKQ KVNIIQFGTG YKELFSYPKH ITSNTMAAEF IMSATPTMGN 950
    TDFWKTLRYL SLLYPARGSR NILLVSDGHL QDESLTLQLV KRSRPHTRLF 1000
    ACGIGSTANR HVLRILSQCG AGVFEYFNAK SKHSWRKQIE DQMTRLCSPS 1050
    CHSVSVKWQQ LNPDVPEALQ APAQVPSLFL NDRLLVYGFI PHCTQATLCA 1100
    LIQEKEFRTM VSTTELQKTT GTMIHKLAAR ALIRDYEDGI LHENETSHEM 1150
    KKQTLKSLII KLSKENSLIT QFTSFVAVEK RDENESPFPD IPKVSELIAK 1200
    EDVDFLPYMS WQGEPQEAVR NQSLLASSEW PELRLSKRKH RKIPFSKRKM 1250
    ELSQPEVSED FEEDGLGVLP AFTSNLERGG VEKLLDLSWT ESCKPTATEP 1300
    LFKKVSPWET STSSFFPILA PAVGSYLPPT ARAHSPASLS FASYRQVASF 1350
    GSAAPPRQFD ASQFSQGPVP GTCADWIPQS ASCPTGPPQN PPSSPYCGIV 1400
    FSGSSLSSAQ SAPLQHPGGF TTRPSAGTFP ELDSPQLHFS LPTDPDPIRG 1450
    FGSYHPSASS PFHFQPSAAS LTANLRLPMA SALPEALCSQ SRTTPVDLCL 1500
    LEESVGSLEG SRCPVFAFQS SDTESDELSE VLQDSCFLQI KCDTKDDSIL 1550
    CFLEVKEEDE IVCIQHWQDA VPWTELLSLQ TEDGFWKLTP ELGLILNLNT 1600
    NGLHSFLKQK GIQSLGVKGR ECLLDLIATM LVLQFIRTRL EKEGIVFKSL 1650
    MKMDDASISR NIPWAFEAIK QASEWVRRTE GQYPSICPRL ELGNDWDSAT 1700
    KQLLGLQPIS TVSPLHRVLH YSQG 1724
    Length:1,724
    Mass (Da):192,595
    Last modified:October 5, 2010 - v3
    Checksum:iDCA1DD4C001EA22F
    GO

    Sequence cautioni

    The sequence BAA11494.2 differs from that shown. Reason: Erroneous initiation. Translation N-terminally shortened.

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti519 – 5191S → P in AAD47250. (PubMed:10477748)Curated
    Sequence conflicti897 – 8971Q → E in AAC62491. (PubMed:10644454)Curated
    Sequence conflicti897 – 8971Q → E in BAA11494. (PubMed:8724849)Curated
    Sequence conflicti936 – 9361M → A in AAC62491. (PubMed:10644454)Curated
    Sequence conflicti936 – 9361M → A in BAA11494. (PubMed:8724849)Curated
    Sequence conflicti936 – 9361M → T in AAD47250. (PubMed:10477748)Curated
    Sequence conflicti1065 – 10651V → A in AAD47250. (PubMed:10477748)Curated
    Sequence conflicti1065 – 10651V → A in AAC62491. (PubMed:10644454)Curated
    Sequence conflicti1080 – 10801L → R in AAD47250. (PubMed:10477748)Curated
    Sequence conflicti1080 – 10801L → R in AAC62491. (PubMed:10644454)Curated
    Sequence conflicti1080 – 10801L → R in BAA11494. (PubMed:8724849)Curated
    Sequence conflicti1108 – 11081R → C in AAD47250. (PubMed:10477748)Curated
    Sequence conflicti1108 – 11081R → C in AAC62491. (PubMed:10644454)Curated
    Sequence conflicti1108 – 11081R → C in BAA11494. (PubMed:8724849)Curated
    Sequence conflicti1328 – 13281P → T in AAD47250. (PubMed:10477748)Curated
    Sequence conflicti1328 – 13281P → T in AAC62491. (PubMed:10644454)Curated
    Sequence conflicti1328 – 13281P → T in BAA11494. (PubMed:8724849)Curated
    Sequence conflicti1331 – 13311A → T in AAD47250. (PubMed:10477748)Curated
    Sequence conflicti1331 – 13311A → T in AAC62491. (PubMed:10644454)Curated
    Sequence conflicti1331 – 13311A → T in BAA11494. (PubMed:8724849)Curated
    Sequence conflicti1394 – 13941S → A in AAD47250. (PubMed:10477748)Curated
    Sequence conflicti1394 – 13941S → A in AAC62491. (PubMed:10644454)Curated
    Sequence conflicti1394 – 13941S → A in BAA11494. (PubMed:8724849)Curated
    Sequence conflicti1459 – 14591S → Y in AAD47250. (PubMed:10477748)Curated
    Sequence conflicti1459 – 14591S → Y in AAC62491. (PubMed:10644454)Curated
    Sequence conflicti1459 – 14591S → Y in BAA11494. (PubMed:8724849)Curated
    Sequence conflicti1550 – 15501L → P in AAD47250. (PubMed:10477748)Curated
    Sequence conflicti1550 – 15501L → P in AAC62491. (PubMed:10644454)Curated
    Sequence conflicti1550 – 15501L → P in BAA11494. (PubMed:8724849)Curated
    Sequence conflicti1555 – 15551V → L in AAD47250. (PubMed:10477748)Curated
    Sequence conflicti1564 – 15641I → T in AAD47250. (PubMed:10477748)Curated
    Sequence conflicti1564 – 15641I → T in AAC62491. (PubMed:10644454)Curated
    Sequence conflicti1564 – 15641I → T in BAA11494. (PubMed:8724849)Curated
    Sequence conflicti1656 – 16561A → P in AAD47250. (PubMed:10477748)Curated
    Sequence conflicti1656 – 16561A → P in AAC62491. (PubMed:10644454)Curated
    Sequence conflicti1656 – 16561A → P in BAA11494. (PubMed:8724849)Curated

    Natural variant

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti81 – 811I → V.
    Corresponds to variant rs35200240 [ dbSNP | Ensembl ].
    VAR_056645
    Natural varianti122 – 1221S → N.
    Corresponds to variant rs9578751 [ dbSNP | Ensembl ].
    VAR_056646
    Natural varianti215 – 2151F → Y.
    Corresponds to variant rs9318600 [ dbSNP | Ensembl ].
    VAR_056647
    Natural varianti792 – 7921P → L.
    Corresponds to variant rs4986818 [ dbSNP | Ensembl ].
    VAR_056648
    Natural varianti873 – 8731S → N.2 Publications
    Corresponds to variant rs7140044 [ dbSNP | Ensembl ].
    VAR_056649
    Natural varianti899 – 8991A → T.1 Publication
    Corresponds to variant rs2275660 [ dbSNP | Ensembl ].
    VAR_056650
    Natural varianti991 – 9911K → R.
    Corresponds to variant rs34689435 [ dbSNP | Ensembl ].
    VAR_056651
    Natural varianti1012 – 10121V → I.
    Corresponds to variant rs9581043 [ dbSNP | Ensembl ].
    VAR_056652
    Natural varianti1253 – 12531S → T.
    Corresponds to variant rs4986822 [ dbSNP | Ensembl ].
    VAR_056653
    Natural varianti1265 – 12651G → A.2 Publications
    Corresponds to variant rs1050110 [ dbSNP | Ensembl ].
    VAR_016090
    Natural varianti1280 – 12801G → R.2 Publications
    Corresponds to variant rs13428 [ dbSNP | Ensembl ].
    VAR_016091

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AF158255 mRNA. Translation: AAD47250.1.
    AF057160 mRNA. Translation: AAC62491.1.
    D79999 mRNA. Translation: BAA11494.2. Different initiation.
    AL359763 Genomic DNA. Translation: CAI12394.1.
    CCDSiCCDS9307.1.
    RefSeqiNP_006428.2. NM_006437.3.
    UniGeneiHs.744855.

    Genome annotation databases

    EnsembliENST00000381989; ENSP00000371419; ENSG00000102699.
    GeneIDi143.
    KEGGihsa:143.
    UCSCiuc001upl.3. human.

    Polymorphism databases

    DMDMi308153574.

    Keywords - Coding sequence diversityi

    Polymorphism

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AF158255 mRNA. Translation: AAD47250.1 .
    AF057160 mRNA. Translation: AAC62491.1 .
    D79999 mRNA. Translation: BAA11494.2 . Different initiation.
    AL359763 Genomic DNA. Translation: CAI12394.1 .
    CCDSi CCDS9307.1.
    RefSeqi NP_006428.2. NM_006437.3.
    UniGenei Hs.744855.

    3D structure databases

    ProteinModelPortali Q9UKK3.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 106653. 8 interactions.
    IntActi Q9UKK3. 14 interactions.
    MINTi MINT-6768840.
    STRINGi 9606.ENSP00000371419.

    Chemistry

    ChEMBLi CHEMBL6142.

    PTM databases

    PhosphoSitei Q9UKK3.

    Polymorphism databases

    DMDMi 308153574.

    Proteomic databases

    MaxQBi Q9UKK3.
    PaxDbi Q9UKK3.
    PeptideAtlasi Q9UKK3.
    PRIDEi Q9UKK3.

    Protocols and materials databases

    DNASUi 143.
    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000381989 ; ENSP00000371419 ; ENSG00000102699 .
    GeneIDi 143.
    KEGGi hsa:143.
    UCSCi uc001upl.3. human.

    Organism-specific databases

    CTDi 143.
    GeneCardsi GC13M024995.
    H-InvDB HIX0019099.
    HGNCi HGNC:271. PARP4.
    HPAi HPA011739.
    MIMi 607519. gene.
    neXtProti NX_Q9UKK3.
    PharmGKBi PA24591.
    HUGEi Search...
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi COG2304.
    HOGENOMi HOG000139369.
    HOVERGENi HBG053515.
    InParanoidi Q9UKK3.
    KOi K10798.
    OMAi QCTHIIL.
    OrthoDBi EOG75F4CF.
    PhylomeDBi Q9UKK3.
    TreeFami TF329720.

    Enzyme and pathway databases

    BRENDAi 2.4.2.30. 2681.
    SignaLinki Q9UKK3.

    Miscellaneous databases

    ChiTaRSi PARP4. human.
    GeneWikii PARP4.
    GenomeRNAii 143.
    NextBioi 569.
    PROi Q9UKK3.
    SOURCEi Search...

    Gene expression databases

    Bgeei Q9UKK3.
    CleanExi HS_PARP4.
    Genevestigatori Q9UKK3.

    Family and domain databases

    Gene3Di 1.20.142.10. 1 hit.
    3.40.50.10190. 1 hit.
    3.40.50.410. 1 hit.
    3.90.228.10. 1 hit.
    InterProi IPR001357. BRCT_dom.
    IPR012317. Poly(ADP-ribose)pol_cat_dom.
    IPR004102. Poly(ADP-ribose)pol_reg_dom.
    IPR013694. VIT.
    IPR002035. VWF_A.
    [Graphical view ]
    Pfami PF00533. BRCT. 1 hit.
    PF00644. PARP. 1 hit.
    PF08487. VIT. 1 hit.
    PF00092. VWA. 1 hit.
    [Graphical view ]
    SMARTi SM00292. BRCT. 1 hit.
    SM00609. VIT. 1 hit.
    SM00327. VWA. 1 hit.
    [Graphical view ]
    SUPFAMi SSF47587. SSF47587. 1 hit.
    SSF52113. SSF52113. 1 hit.
    SSF53300. SSF53300. 1 hit.
    PROSITEi PS50172. BRCT. 1 hit.
    PS51060. PARP_ALPHA_HD. 1 hit.
    PS51059. PARP_CATALYTIC. 1 hit.
    PS51468. VIT. 1 hit.
    PS50234. VWFA. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "The 193 kDa vault protein, VPARP, is a novel poly(ADP-ribose) polymerase."
      Kickhoefer V.A., Siva A.C., Kedersha N.L., Inman E.M., Ruland C., Streuli M., Rome L.H.
      J. Cell Biol. 146:917-928(1999) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA], PROTEIN SEQUENCE OF 306-319, VARIANT THR-899.
    2. "Identification of a novel gene (ADPRTL1) encoding a potential poly(ADP-ribosyl)transferase protein."
      Still I.H., Vince P., Cowell J.K.
      Genomics 62:533-536(1999) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA], VARIANTS ASN-873; ALA-1265 AND ARG-1280.
      Tissue: Thymus.
    3. "Prediction of the coding sequences of unidentified human genes. V. The coding sequences of 40 new genes (KIAA0161-KIAA0200) deduced by analysis of cDNA clones from human cell line KG-1."
      Nagase T., Seki N., Ishikawa K., Tanaka A., Nomura N.
      DNA Res. 3:17-24(1996) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA], VARIANTS ASN-873; ALA-1265 AND ARG-1280.
      Tissue: Bone marrow.
    4. Ohara O., Nagase T., Kikuno R., Nomura N.
      Submitted (JAN-2003) to the EMBL/GenBank/DDBJ databases
      Cited for: SEQUENCE REVISION.
    5. "The DNA sequence and analysis of human chromosome 13."
      Dunham A., Matthews L.H., Burton J., Ashurst J.L., Howe K.L., Ashcroft K.J., Beare D.M., Burford D.C., Hunt S.E., Griffiths-Jones S., Jones M.C., Keenan S.J., Oliver K., Scott C.E., Ainscough R., Almeida J.P., Ambrose K.D., Andrews D.T.
      , Ashwell R.I.S., Babbage A.K., Bagguley C.L., Bailey J., Bannerjee R., Barlow K.F., Bates K., Beasley H., Bird C.P., Bray-Allen S., Brown A.J., Brown J.Y., Burrill W., Carder C., Carter N.P., Chapman J.C., Clamp M.E., Clark S.Y., Clarke G., Clee C.M., Clegg S.C., Cobley V., Collins J.E., Corby N., Coville G.J., Deloukas P., Dhami P., Dunham I., Dunn M., Earthrowl M.E., Ellington A.G., Faulkner L., Frankish A.G., Frankland J., French L., Garner P., Garnett J., Gilbert J.G.R., Gilson C.J., Ghori J., Grafham D.V., Gribble S.M., Griffiths C., Hall R.E., Hammond S., Harley J.L., Hart E.A., Heath P.D., Howden P.J., Huckle E.J., Hunt P.J., Hunt A.R., Johnson C., Johnson D., Kay M., Kimberley A.M., King A., Laird G.K., Langford C.J., Lawlor S., Leongamornlert D.A., Lloyd D.M., Lloyd C., Loveland J.E., Lovell J., Martin S., Mashreghi-Mohammadi M., McLaren S.J., McMurray A., Milne S., Moore M.J.F., Nickerson T., Palmer S.A., Pearce A.V., Peck A.I., Pelan S., Phillimore B., Porter K.M., Rice C.M., Searle S., Sehra H.K., Shownkeen R., Skuce C.D., Smith M., Steward C.A., Sycamore N., Tester J., Thomas D.W., Tracey A., Tromans A., Tubby B., Wall M., Wallis J.M., West A.P., Whitehead S.L., Willey D.L., Wilming L., Wray P.W., Wright M.W., Young L., Coulson A., Durbin R.M., Hubbard T., Sulston J.E., Beck S., Bentley D.R., Rogers J., Ross M.T.
      Nature 428:522-528(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    6. "The nuclear protein PH5P of the inter-alpha-inhibitor superfamily: a missing link between poly(ADP-ribose)polymerase and the inter-alpha-inhibitor family and a novel actor of DNA repair?"
      Jean L., Risler J.-L., Nagase T., Coulouarn C., Nomura N., Salier J.-P.
      FEBS Lett. 446:6-8(1999) [PubMed] [Europe PMC] [Abstract]
      Cited for: DISCUSSION OF SEQUENCE.
    7. Cited for: ASSOCIATION WITH TEP1.
    8. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-101; SER-1236; SER-1335 AND SER-1504, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    9. "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-1335, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    10. "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.
    11. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].

    Entry informationi

    Entry nameiPARP4_HUMAN
    AccessioniPrimary (citable) accession number: Q9UKK3
    Secondary accession number(s): O75903
    , Q14682, Q5QNZ9, Q9H1M6
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: September 26, 2001
    Last sequence update: October 5, 2010
    Last modified: October 1, 2014
    This is version 143 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

    Complete proteome, Direct protein sequencing, Reference proteome

    Documents

    1. Human chromosome 13
      Human chromosome 13: 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. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3