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Q9UKK3 (PARP4_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 139. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (5) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Interactions·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Poly [ADP-ribose] polymerase 4

Short name=PARP-4
EC=2.4.2.30
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 names
Name:PARP4
Synonyms:ADPRTL1, KIAA0177, PARPL
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length1724 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Catalytic activity

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

Subunit structure

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.

Subcellular location

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

Tissue specificity

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

Sequence similarities

Contains 1 BRCT domain.

Contains 1 PARP alpha-helical domain.

Contains 1 PARP catalytic domain.

Contains 1 VIT domain.

Contains 1 VWFA domain.

Sequence caution

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

Ontologies

Keywords
   Cellular componentCytoplasm
Cytoskeleton
Nucleus
   Coding sequence diversityPolymorphism
   LigandNAD
   Molecular functionGlycosyltransferase
Ribonucleoprotein
Transferase
   PTMPhosphoprotein
   Technical termComplete proteome
Direct protein sequencing
Reference proteome
Gene Ontology (GO)
   Biological_processDNA repair

Non-traceable author statement PubMed 12101391. Source: UniProtKB

cell death

Inferred from mutant phenotype PubMed 12140175. Source: UniProtKB

cellular protein modification process

Inferred from direct assay Ref.1. Source: UniProtKB

cellular response to DNA damage stimulus

Non-traceable author statement Ref.1. Source: UniProtKB

inflammatory response

Inferred from mutant phenotype PubMed 12123754. Source: UniProtKB

protein ADP-ribosylation

Non-traceable author statement Ref.2. Source: UniProtKB

response to drug

Non-traceable author statement PubMed 11291045. Source: UniProtKB

transport

Non-traceable author statement PubMed 11855821. Source: UniProtKB

   Cellular_componentcytoplasm

Inferred from direct assay Ref.1. Source: UniProtKB

extracellular vesicular exosome

Inferred from direct assay PubMed 19056867. Source: UniProt

nucleus

Non-traceable author statement Ref.2. Source: UniProtKB

ribonucleoprotein complex

Non-traceable author statement PubMed 11479319. Source: UniProtKB

spindle microtubule

Inferred from direct assay Ref.1. Source: UniProtKB

   Molecular_functionDNA binding

Traceable author statement Ref.6. Source: ProtInc

NAD+ ADP-ribosyltransferase activity

Inferred from direct assay Ref.1. Source: UniProtKB

enzyme binding

Inferred from direct assay PubMed 15169895. Source: MGI

Complete GO annotation...

Binary interactions

With

Entry

#Exp.

IntAct

Notes

ORFQ9Q2G43EBI-2623021,EBI-6248094From a different organism.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 17241724Poly [ADP-ribose] polymerase 4
PRO_0000211330

Regions

Domain1 – 9494BRCT
Domain242 – 370129PARP alpha-helical
Domain369 – 573205PARP catalytic
Domain607 – 735129VIT
Domain876 – 1046171VWFA
Region1562 – 1724163Interaction with the major vault protein
Motif19 – 257Nuclear localization signal Potential
Motif1237 – 124913Nuclear localization signal Potential

Amino acid modifications

Modified residue1011Phosphothreonine Ref.8
Modified residue12361Phosphoserine Ref.8
Modified residue13351Phosphoserine Ref.8 Ref.9
Modified residue15041Phosphoserine Ref.8

Natural variations

Natural variant811I → V.
Corresponds to variant rs35200240 [ dbSNP | Ensembl ].
VAR_056645
Natural variant1221S → N.
Corresponds to variant rs9578751 [ dbSNP | Ensembl ].
VAR_056646
Natural variant2151F → Y.
Corresponds to variant rs9318600 [ dbSNP | Ensembl ].
VAR_056647
Natural variant7921P → L.
Corresponds to variant rs4986818 [ dbSNP | Ensembl ].
VAR_056648
Natural variant8731S → N. Ref.2 Ref.3
Corresponds to variant rs7140044 [ dbSNP | Ensembl ].
VAR_056649
Natural variant8991A → T. Ref.1
Corresponds to variant rs2275660 [ dbSNP | Ensembl ].
VAR_056650
Natural variant9911K → R.
Corresponds to variant rs34689435 [ dbSNP | Ensembl ].
VAR_056651
Natural variant10121V → I.
Corresponds to variant rs9581043 [ dbSNP | Ensembl ].
VAR_056652
Natural variant12531S → T.
Corresponds to variant rs4986822 [ dbSNP | Ensembl ].
VAR_056653
Natural variant12651G → A. Ref.2 Ref.3
Corresponds to variant rs1050110 [ dbSNP | Ensembl ].
VAR_016090
Natural variant12801G → R. Ref.2 Ref.3
Corresponds to variant rs13428 [ dbSNP | Ensembl ].
VAR_016091

Experimental info

Sequence conflict5191S → P in AAD47250. Ref.1
Sequence conflict8971Q → E in AAC62491. Ref.2
Sequence conflict8971Q → E in BAA11494. Ref.3
Sequence conflict9361M → A in AAC62491. Ref.2
Sequence conflict9361M → A in BAA11494. Ref.3
Sequence conflict9361M → T in AAD47250. Ref.1
Sequence conflict10651V → A in AAD47250. Ref.1
Sequence conflict10651V → A in AAC62491. Ref.2
Sequence conflict10801L → R in AAD47250. Ref.1
Sequence conflict10801L → R in AAC62491. Ref.2
Sequence conflict10801L → R in BAA11494. Ref.3
Sequence conflict11081R → C in AAD47250. Ref.1
Sequence conflict11081R → C in AAC62491. Ref.2
Sequence conflict11081R → C in BAA11494. Ref.3
Sequence conflict13281P → T in AAD47250. Ref.1
Sequence conflict13281P → T in AAC62491. Ref.2
Sequence conflict13281P → T in BAA11494. Ref.3
Sequence conflict13311A → T in AAD47250. Ref.1
Sequence conflict13311A → T in AAC62491. Ref.2
Sequence conflict13311A → T in BAA11494. Ref.3
Sequence conflict13941S → A in AAD47250. Ref.1
Sequence conflict13941S → A in AAC62491. Ref.2
Sequence conflict13941S → A in BAA11494. Ref.3
Sequence conflict14591S → Y in AAD47250. Ref.1
Sequence conflict14591S → Y in AAC62491. Ref.2
Sequence conflict14591S → Y in BAA11494. Ref.3
Sequence conflict15501L → P in AAD47250. Ref.1
Sequence conflict15501L → P in AAC62491. Ref.2
Sequence conflict15501L → P in BAA11494. Ref.3
Sequence conflict15551V → L in AAD47250. Ref.1
Sequence conflict15641I → T in AAD47250. Ref.1
Sequence conflict15641I → T in AAC62491. Ref.2
Sequence conflict15641I → T in BAA11494. Ref.3
Sequence conflict16561A → P in AAD47250. Ref.1
Sequence conflict16561A → P in AAC62491. Ref.2
Sequence conflict16561A → P in BAA11494. Ref.3

Sequences

Sequence LengthMass (Da)Tools
Q9UKK3 [UniParc].

Last modified October 5, 2010. Version 3.
Checksum: DCA1DD4C001EA22F

FASTA1,724192,595
        10         20         30         40         50         60 
MVMGIFANCI FCLKVKYLPQ QQKKKLQTDI KENGGKFSFS LNPQCTHIIL DNADVLSQYQ 

        70         80         90        100        110        120 
LNSIQKNHVH IANPDFIWKS IREKRLLDVK NYDPYKPLDI TPPPDQKASS SEVKTEGLCP 

       130        140        150        160        170        180 
DSATEEEDTV ELTEFGMQNV EIPHLPQDFE VAKYNTLEKV GMEGGQEAVV VELQCSRDSR 

       190        200        210        220        230        240 
DCPFLISSHF LLDDGMETRR QFAIKKTSED ASEYFENYIE ELKKQGFLLR EHFTPEATQL 

       250        260        270        280        290        300 
ASEQLQALLL EEVMNSSTLS QEVSDLVEMI WAEALGHLEH MLLKPVNRIS LNDVSKAEGI 

       310        320        330        340        350        360 
LLLVKAALKN GETAEQLQKM MTEFYRLIPH KGTMPKEVNL GLLAKKADLC QLIRDMVNVC 

       370        380        390        400        410        420 
ETNLSKPNPP SLAKYRALRC KIEHVEQNTE EFLRVRKEVL QNHHSKSPVD VLQIFRVGRV 

       430        440        450        460        470        480 
NETTEFLSKL GNVRPLLHGS PVQNIVGILC RGLLLPKVVE DRGVQRTDVG NLGSGIYFSD 

       490        500        510        520        530        540 
SLSTSIKYSH PGETDGTRLL LICDVALGKC MDLHEKDFSL TEAPPGYDSV HGVSQTASVT 

       550        560        570        580        590        600 
TDFEDDEFVV YKTNQVKMKY IIKFSMPGDQ IKDFHPSDHT ELEEYRPEFS NFSKVEDYQL 

       610        620        630        640        650        660 
PDAKTSSSTK AGLQDASGNL VPLEDVHIKG RIIDTVAQVI VFQTYTNKSH VPIEAKYIFP 

       670        680        690        700        710        720 
LDDKAAVCGF EAFINGKHIV GEIKEKEEAQ QEYLEAVTQG HGAYLMSQDA PDVFTVSVGN 

       730        740        750        760        770        780 
LPPKAKVLIK ITYITELSIL GTVGVFFMPA TVAPWQQDKA LNENLQDTVE KICIKEIGTK 

       790        800        810        820        830        840 
QSFSLTMSIE MPYVIEFIFS DTHELKQKRT DCKAVISTME GSSLDSSGFS LHIGLSAAYL 

       850        860        870        880        890        900 
PRMWVEKHPE KESEACMLVF QPDLDVDLPD LASESEVIIC LDCSSSMEGV TFLQAKQIAL 

       910        920        930        940        950        960 
HALSLVGEKQ KVNIIQFGTG YKELFSYPKH ITSNTMAAEF IMSATPTMGN TDFWKTLRYL 

       970        980        990       1000       1010       1020 
SLLYPARGSR NILLVSDGHL QDESLTLQLV KRSRPHTRLF ACGIGSTANR HVLRILSQCG 

      1030       1040       1050       1060       1070       1080 
AGVFEYFNAK SKHSWRKQIE DQMTRLCSPS CHSVSVKWQQ LNPDVPEALQ APAQVPSLFL 

      1090       1100       1110       1120       1130       1140 
NDRLLVYGFI PHCTQATLCA LIQEKEFRTM VSTTELQKTT GTMIHKLAAR ALIRDYEDGI 

      1150       1160       1170       1180       1190       1200 
LHENETSHEM KKQTLKSLII KLSKENSLIT QFTSFVAVEK RDENESPFPD IPKVSELIAK 

      1210       1220       1230       1240       1250       1260 
EDVDFLPYMS WQGEPQEAVR NQSLLASSEW PELRLSKRKH RKIPFSKRKM ELSQPEVSED 

      1270       1280       1290       1300       1310       1320 
FEEDGLGVLP AFTSNLERGG VEKLLDLSWT ESCKPTATEP LFKKVSPWET STSSFFPILA 

      1330       1340       1350       1360       1370       1380 
PAVGSYLPPT ARAHSPASLS FASYRQVASF GSAAPPRQFD ASQFSQGPVP GTCADWIPQS 

      1390       1400       1410       1420       1430       1440 
ASCPTGPPQN PPSSPYCGIV FSGSSLSSAQ SAPLQHPGGF TTRPSAGTFP ELDSPQLHFS 

      1450       1460       1470       1480       1490       1500 
LPTDPDPIRG FGSYHPSASS PFHFQPSAAS LTANLRLPMA SALPEALCSQ SRTTPVDLCL 

      1510       1520       1530       1540       1550       1560 
LEESVGSLEG SRCPVFAFQS SDTESDELSE VLQDSCFLQI KCDTKDDSIL CFLEVKEEDE 

      1570       1580       1590       1600       1610       1620 
IVCIQHWQDA VPWTELLSLQ TEDGFWKLTP ELGLILNLNT NGLHSFLKQK GIQSLGVKGR 

      1630       1640       1650       1660       1670       1680 
ECLLDLIATM LVLQFIRTRL EKEGIVFKSL MKMDDASISR NIPWAFEAIK QASEWVRRTE 

      1690       1700       1710       1720 
GQYPSICPRL ELGNDWDSAT KQLLGLQPIS TVSPLHRVLH YSQG 

« Hide

References

« Hide 'large scale' references
[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. expand/collapse author list , 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]"Vaults and telomerase share a common subunit, TEP1."
Kickhoefer V.A., Stephen A.G., Harrington L., Robinson M.O., Rome L.H.
J. Biol. Chem. 274:32712-32717(1999) [PubMed] [Europe PMC] [Abstract]
Cited for: ASSOCIATION WITH TEP1.
[8]"A quantitative atlas of mitotic phosphorylation."
Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E., Elledge S.J., Gygi S.P.
Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008) [PubMed] [Europe PMC] [Abstract]
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]"Initial characterization of the human central proteome."
Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.
BMC Syst. Biol. 5:17-17(2011) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AF158255 mRNA. Translation: AAD47250.1.
AF057160 mRNA. Translation: AAC62491.1.
D79999 mRNA. Translation: BAA11494.2. Different initiation.
AL359763 Genomic DNA. Translation: CAI12394.1.
RefSeqNP_006428.2. NM_006437.3.
UniGeneHs.744855.

3D structure databases

ProteinModelPortalQ9UKK3.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid106653. 8 interactions.
IntActQ9UKK3. 14 interactions.
MINTMINT-6768840.
STRING9606.ENSP00000371419.

Chemistry

ChEMBLCHEMBL6142.

PTM databases

PhosphoSiteQ9UKK3.

Polymorphism databases

DMDM308153574.

Proteomic databases

PaxDbQ9UKK3.
PeptideAtlasQ9UKK3.
PRIDEQ9UKK3.

Protocols and materials databases

DNASU143.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000381989; ENSP00000371419; ENSG00000102699.
GeneID143.
KEGGhsa:143.
UCSCuc001upl.3. human.

Organism-specific databases

CTD143.
GeneCardsGC13M024995.
H-InvDBHIX0019099.
HGNCHGNC:271. PARP4.
HPAHPA011739.
MIM607519. gene.
neXtProtNX_Q9UKK3.
PharmGKBPA24591.
HUGESearch...
GenAtlasSearch...

Phylogenomic databases

eggNOGCOG2304.
HOGENOMHOG000139369.
HOVERGENHBG053515.
InParanoidQ9UKK3.
KOK10798.
OMAQCTHIIL.
OrthoDBEOG75F4CF.
PhylomeDBQ9UKK3.
TreeFamTF329720.

Enzyme and pathway databases

BRENDA2.4.2.30. 2681.
SignaLinkQ9UKK3.

Gene expression databases

BgeeQ9UKK3.
CleanExHS_PARP4.
GenevestigatorQ9UKK3.

Family and domain databases

Gene3D1.20.142.10. 1 hit.
3.40.50.10190. 1 hit.
3.40.50.410. 1 hit.
3.90.228.10. 1 hit.
InterProIPR001357. BRCT_dom.
IPR012317. Poly(ADP-ribose)pol_cat_dom.
IPR004102. Poly(ADP-ribose)pol_reg_dom.
IPR013694. VIT.
IPR002035. VWF_A.
[Graphical view]
PfamPF00533. BRCT. 1 hit.
PF00644. PARP. 1 hit.
PF08487. VIT. 1 hit.
PF00092. VWA. 1 hit.
[Graphical view]
SMARTSM00292. BRCT. 1 hit.
SM00609. VIT. 1 hit.
SM00327. VWA. 1 hit.
[Graphical view]
SUPFAMSSF47587. SSF47587. 1 hit.
SSF52113. SSF52113. 1 hit.
SSF53300. SSF53300. 1 hit.
PROSITEPS50172. BRCT. 1 hit.
PS51060. PARP_ALPHA_HD. 1 hit.
PS51059. PARP_CATALYTIC. 1 hit.
PS51468. VIT. 1 hit.
PS50234. VWFA. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

ChiTaRSPARP4. human.
GeneWikiPARP4.
GenomeRNAi143.
NextBio569.
PROQ9UKK3.
SOURCESearch...

Entry information

Entry namePARP4_HUMAN
AccessionPrimary (citable) accession number: Q9UKK3
Secondary accession number(s): O75903 expand/collapse secondary AC list , Q14682, Q5QNZ9, Q9H1M6
Entry history
Integrated into UniProtKB/Swiss-Prot: September 26, 2001
Last sequence update: October 5, 2010
Last modified: April 16, 2014
This is version 139 of the entry and version 3 of the sequence. [Complete history]
Entry statusReviewed (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.

Relevant documents

SIMILARITY comments

Index of protein domains and families

MIM cross-references

Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot

Human polymorphisms and disease mutations

Index of human polymorphisms and disease mutations

Human entries with polymorphisms or disease mutations

List of human entries with polymorphisms or disease mutations

Human chromosome 13

Human chromosome 13: entries, gene names and cross-references to MIM