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Q9UKK3

- PARP4_HUMAN

UniProt

Q9UKK3 - PARP4_HUMAN

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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

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

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
Complete GO annotation...

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
Complete GO annotation...

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. 9 interactions.
IntActiQ9UKK3. 15 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.
GeneTreeiENSGT00530000063006.
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

« Hide

        10         20         30         40         50
MVMGIFANCI FCLKVKYLPQ QQKKKLQTDI KENGGKFSFS LNPQCTHIIL
60 70 80 90 100
DNADVLSQYQ LNSIQKNHVH IANPDFIWKS IREKRLLDVK NYDPYKPLDI
110 120 130 140 150
TPPPDQKASS SEVKTEGLCP DSATEEEDTV ELTEFGMQNV EIPHLPQDFE
160 170 180 190 200
VAKYNTLEKV GMEGGQEAVV VELQCSRDSR DCPFLISSHF LLDDGMETRR
210 220 230 240 250
QFAIKKTSED ASEYFENYIE ELKKQGFLLR EHFTPEATQL ASEQLQALLL
260 270 280 290 300
EEVMNSSTLS QEVSDLVEMI WAEALGHLEH MLLKPVNRIS LNDVSKAEGI
310 320 330 340 350
LLLVKAALKN GETAEQLQKM MTEFYRLIPH KGTMPKEVNL GLLAKKADLC
360 370 380 390 400
QLIRDMVNVC ETNLSKPNPP SLAKYRALRC KIEHVEQNTE EFLRVRKEVL
410 420 430 440 450
QNHHSKSPVD VLQIFRVGRV NETTEFLSKL GNVRPLLHGS PVQNIVGILC
460 470 480 490 500
RGLLLPKVVE DRGVQRTDVG NLGSGIYFSD SLSTSIKYSH PGETDGTRLL
510 520 530 540 550
LICDVALGKC MDLHEKDFSL TEAPPGYDSV HGVSQTASVT TDFEDDEFVV
560 570 580 590 600
YKTNQVKMKY IIKFSMPGDQ IKDFHPSDHT ELEEYRPEFS NFSKVEDYQL
610 620 630 640 650
PDAKTSSSTK AGLQDASGNL VPLEDVHIKG RIIDTVAQVI VFQTYTNKSH
660 670 680 690 700
VPIEAKYIFP LDDKAAVCGF EAFINGKHIV GEIKEKEEAQ QEYLEAVTQG
710 720 730 740 750
HGAYLMSQDA PDVFTVSVGN LPPKAKVLIK ITYITELSIL GTVGVFFMPA
760 770 780 790 800
TVAPWQQDKA LNENLQDTVE KICIKEIGTK QSFSLTMSIE MPYVIEFIFS
810 820 830 840 850
DTHELKQKRT DCKAVISTME GSSLDSSGFS LHIGLSAAYL PRMWVEKHPE
860 870 880 890 900
KESEACMLVF QPDLDVDLPD LASESEVIIC LDCSSSMEGV TFLQAKQIAL
910 920 930 940 950
HALSLVGEKQ KVNIIQFGTG YKELFSYPKH ITSNTMAAEF IMSATPTMGN
960 970 980 990 1000
TDFWKTLRYL SLLYPARGSR NILLVSDGHL QDESLTLQLV KRSRPHTRLF
1010 1020 1030 1040 1050
ACGIGSTANR HVLRILSQCG AGVFEYFNAK SKHSWRKQIE DQMTRLCSPS
1060 1070 1080 1090 1100
CHSVSVKWQQ LNPDVPEALQ APAQVPSLFL NDRLLVYGFI PHCTQATLCA
1110 1120 1130 1140 1150
LIQEKEFRTM VSTTELQKTT GTMIHKLAAR ALIRDYEDGI LHENETSHEM
1160 1170 1180 1190 1200
KKQTLKSLII KLSKENSLIT QFTSFVAVEK RDENESPFPD IPKVSELIAK
1210 1220 1230 1240 1250
EDVDFLPYMS WQGEPQEAVR NQSLLASSEW PELRLSKRKH RKIPFSKRKM
1260 1270 1280 1290 1300
ELSQPEVSED FEEDGLGVLP AFTSNLERGG VEKLLDLSWT ESCKPTATEP
1310 1320 1330 1340 1350
LFKKVSPWET STSSFFPILA PAVGSYLPPT ARAHSPASLS FASYRQVASF
1360 1370 1380 1390 1400
GSAAPPRQFD ASQFSQGPVP GTCADWIPQS ASCPTGPPQN PPSSPYCGIV
1410 1420 1430 1440 1450
FSGSSLSSAQ SAPLQHPGGF TTRPSAGTFP ELDSPQLHFS LPTDPDPIRG
1460 1470 1480 1490 1500
FGSYHPSASS PFHFQPSAAS LTANLRLPMA SALPEALCSQ SRTTPVDLCL
1510 1520 1530 1540 1550
LEESVGSLEG SRCPVFAFQS SDTESDELSE VLQDSCFLQI KCDTKDDSIL
1560 1570 1580 1590 1600
CFLEVKEEDE IVCIQHWQDA VPWTELLSLQ TEDGFWKLTP ELGLILNLNT
1610 1620 1630 1640 1650
NGLHSFLKQK GIQSLGVKGR ECLLDLIATM LVLQFIRTRL EKEGIVFKSL
1660 1670 1680 1690 1700
MKMDDASISR NIPWAFEAIK QASEWVRRTE GQYPSICPRL ELGNDWDSAT
1710 1720
KQLLGLQPIS TVSPLHRVLH YSQG
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. 9 interactions.
IntActi Q9UKK3. 15 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.
GeneTreei ENSGT00530000063006.
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

« Hide 'large scale' publications
  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 29, 2014
This is version 144 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