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P33316 (DUT_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 149. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (7) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Interactions·Alt products·Sequence annotation·Sequences·References·Web links·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Deoxyuridine 5'-triphosphate nucleotidohydrolase, mitochondrial

Short name=dUTPase
EC=3.6.1.23
Alternative name(s):
dUTP pyrophosphatase
Gene names
Name:DUT
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length252 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

This enzyme is involved in nucleotide metabolism: it produces dUMP, the immediate precursor of thymidine nucleotides and it decreases the intracellular concentration of dUTP so that uracil cannot be incorporated into DNA. Ref.21

Catalytic activity

dUTP + H2O = dUMP + diphosphate. Ref.21

Cofactor

Magnesium. Ref.21

Enzyme regulation

Phosphorylation is necessary for activity.

Pathway

Pyrimidine metabolism; dUMP biosynthesis; dUMP from dCTP (dUTP route): step 2/2.

Subunit structure

Homotrimer. Ref.21 Ref.22

Subcellular location

Isoform 2: Nucleus Ref.1 Ref.4.

Isoform 3: Mitochondrion Ref.1 Ref.4.

Tissue specificity

Found in a variety of tissues. Isoform 3 expression is constitutive, while isoform 2 expression correlates with the onset of DNA replication (at protein level). Isoform 2 degradation coincides with the cessation of nuclear DNA replication (at protein level). Ref.4

Post-translational modification

Nuclear isoform 2 is phosphorylated in vivo on Ser-11, a reaction that can be catalyzed in vitro by CDC2. Phosphorylation in mature T-cells occurs in a cell cycle-dependent manner. Isoform 3 is not phosphorylated. Ref.13 Ref.14

The initiator methionine is cleaved in isoform 2. Ref.1

Miscellaneous

Each trimer binds three substrate molecules. The ligands are bound between subunits, and for each substrate molecule, residues from adjacent subunits contribute to the binding interactions.

Sequence similarities

Belongs to the dUTPase family.

Biophysicochemical properties

Kinetic parameters:

for both isoform 2 and isoform 3.

KM=2.5 µM for dUTP Ref.1

Sequence caution

The sequence AAB71393.1 differs from that shown. Reason: Frameshift at positions 29 and 47.

The sequence AAB93866.1 differs from that shown. Reason: Frameshift at positions 29 and 47.

The sequence AAB94642.1 differs from that shown. Reason: Frameshift at positions 29 and 47.

Ontologies

Keywords
   Biological processNucleotide metabolism
   Cellular componentMitochondrion
Nucleus
   Coding sequence diversityAlternative splicing
Polymorphism
   DomainTransit peptide
   LigandMagnesium
   Molecular functionHydrolase
   PTMAcetylation
Phosphoprotein
   Technical term3D-structure
Complete proteome
Direct protein sequencing
Reference proteome
Gene Ontology (GO)
   Biological_processDNA replication

Traceable author statement Ref.11. Source: ProtInc

dUMP biosynthetic process

Inferred from electronic annotation. Source: UniProtKB-UniPathway

dUTP metabolic process

Inferred from electronic annotation. Source: InterPro

nucleobase-containing compound metabolic process

Traceable author statement Ref.11. Source: ProtInc

nucleobase-containing small molecule metabolic process

Traceable author statement. Source: Reactome

pyrimidine nucleobase metabolic process

Traceable author statement. Source: Reactome

pyrimidine nucleoside biosynthetic process

Traceable author statement. Source: Reactome

small molecule metabolic process

Traceable author statement. Source: Reactome

   Cellular_componentextracellular vesicular exosome

Inferred from direct assay PubMed 20458337. Source: UniProt

mitochondrion

Traceable author statement Ref.1. Source: ProtInc

nucleoplasm

Traceable author statement. Source: Reactome

nucleus

Inferred from direct assay. Source: HPA

   Molecular_functiondUTP diphosphatase activity

Inferred from experiment. Source: Reactome

poly(A) RNA binding

Inferred from direct assay PubMed 22658674. Source: UniProtKB

Complete GO annotation...

Binary interactions

With

Entry

#Exp.

IntAct

Notes

NUDT18Q6ZVK83EBI-353224,EBI-740486

Alternative products

This entry describes 2 isoforms produced by alternative splicing. [Align] [Select]
Isoform 3 (identifier: P33316-3)

Also known as: DUT-M;

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.
Isoform 2 (identifier: P33316-2)

Also known as: DUT-N;

The sequence of this isoform differs from the canonical sequence as follows:
     1-93: MTPLCPRPAL...KAGGSPAPGP → MPCSE
Note: Major isoform. Phosphorylated in Ser-11. Contains a phosphoserine at position 11.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Transit peptide1 – 6969Mitochondrion Ref.1 Ref.14
Chain70 – 252183Deoxyuridine 5'-triphosphate nucleotidohydrolase, mitochondrial
PRO_0000007392

Regions

Region173 – 1753Substrate binding
Region187 – 1904Substrate binding
Region246 – 2472Substrate binding

Sites

Binding site1981Substrate; via amide nitrogen and carbonyl oxygen
Binding site2411Substrate By similarity

Amino acid modifications

Modified residue881Phosphoserine Ref.18
Modified residue1791N6-acetyllysine

Natural variations

Alternative sequence1 – 9393MTPLC…PAPGP → MPCSE in isoform 2.
VSP_001324
Natural variant1001P → S. Ref.8
Corresponds to variant rs28381104 [ dbSNP | Ensembl ].
VAR_022314

Experimental info

Mutagenesis991S → A: Loss of phosphorylation. Ref.14
Sequence conflict1751G → S in BAF84204. Ref.6
Sequence conflict1821I → T in BAG60677. Ref.6

Secondary structure

................................. 252
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
Isoform 3 (DUT-M) [UniParc].

Last modified September 21, 2011. Version 4.
Checksum: 8E2EBC9ED5B0FAD2

FASTA25226,563
        10         20         30         40         50         60 
MTPLCPRPAL CYHFLTSLLR SAMQNARGAR QRAEAAVLSG PGPPLGRAAQ HGIPRPLSSA 

        70         80         90        100        110        120 
GRLSQGCRGA STVGAAGWKG ELPKAGGSPA PGPETPAISP SKRARPAEVG GMQLRFARLS 

       130        140        150        160        170        180 
EHATAPTRGS ARAAGYDLYS AYDYTIPPME KAVVKTDIQI ALPSGCYGRV APRSGLAAKH 

       190        200        210        220        230        240 
FIDVGAGVID EDYRGNVGVV LFNFGKEKFE VKKGDRIAQL ICERIFYPEI EEVQALDDTE 

       250 
RGSGGFGSTG KN 

« Hide

Isoform 2 (DUT-N) [UniParc].

Checksum: E75BC583BF8C7245
Show »

FASTA16417,748

References

« Hide 'large scale' references
[1]"Characterization of distinct nuclear and mitochondrial forms of human deoxyuridine triphosphate nucleotidohydrolase."
Ladner R.D., McNulty D.E., Carr S.A., Roberts G.D., Caradonna S.J.
J. Biol. Chem. 271:7745-7751(1996) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2), PROTEIN SEQUENCE OF 70-93 (ISOFORM 3), PROTEIN SEQUENCE OF N-TERMINUS, PROTEIN SEQUENCE OF 94-115; 119-128; 133-151; 156-169; 180-206 AND 217-241 (ISOFORMS 2/3), CLEAVAGE OF INITIATOR METHIONINE (ISOFORM 2), SUBCELLULAR LOCATION, BIOPHYSICOCHEMICAL PROPERTIES, IDENTIFICATION BY MASS SPECTROMETRY.
Tissue: T-cell.
[2]"Assignment of the human dUTPase gene (DUT) to chromosome 15q15-q21. 1 by fluorescence in situ hybridization."
Cohen D., Heng H.H.Q., Shi X.-M., McIntosh E.M., Tsui L.-C., Pearlman R.E.
Genomics 40:213-215(1997) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2).
[3]"Human genomic nuclear and mitochondria dUTPase gene."
Pearlman R.E.
Submitted (OCT-1997) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] (ISOFORMS 2 AND 3).
[4]"The human dUTPase gene encodes both nuclear and mitochondrial isoforms. Differential expression of the isoforms and characterization of a cDNA encoding the mitochondrial species."
Ladner R.D., Caradonna S.J.
J. Biol. Chem. 272:19072-19080(1997) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 3), NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-139 (ISOFORMS 2 AND 3), SUBCELLULAR LOCATION, TISSUE SPECIFICITY.
Tissue: Lung fibroblast.
[5]"Unknown transcriptional variant of nuclear dUTPase in human osteosarcoma."
Chano T., Okabe H., Baldini N., Lapucci C., Scotlandi K., Serra M., Saeki Y.
Submitted (SEP-2000) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2).
[6]"Complete sequencing and characterization of 21,243 full-length human cDNAs."
Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S. expand/collapse author list , Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.
Nat. Genet. 36:40-45(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 2 AND 3).
[7]"Cloning of human full open reading frames in Gateway(TM) system entry vector (pDONR201)."
Ebert L., Schick M., Neubert P., Schatten R., Henze S., Korn B.
Submitted (JUN-2004) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
[8]NIEHS SNPs program
Submitted (FEB-2005) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], VARIANT SER-100.
[9]Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S., Turner R. expand/collapse author list , Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W., Venter J.C.
Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[10]"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] (ISOFORMS 2 AND 3).
Tissue: Brain, Eye and Urinary bladder.
[11]"Human dUTP pyrophosphatase: cDNA sequence and potential biological importance of the enzyme."
McIntosh E.M., Ager D.D., Gadsden M.H., Haynes R.H.
Proc. Natl. Acad. Sci. U.S.A. 89:8020-8024(1992) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 112-252.
[12]Erratum
McIntosh E.M., Ager D.D., Gadsden M.H., Haynes R.H.
Proc. Natl. Acad. Sci. U.S.A. 90:4328-4328(1993)
[13]"Maturation stage and proliferation-dependent expression of dUTPase in human T cells."
Strahler J.R., Zhu X.-X., Wang Y.K., Hora N., Andrews P.C., Roseman N.A., Neel J.V., Turka L., Hanash S.M.
Proc. Natl. Acad. Sci. U.S.A. 90:4991-4995(1993) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 112-252, PARTIAL PROTEIN SEQUENCE, PHOSPHORYLATION.
Tissue: Lymphocyte.
[14]"Identification of a consensus cyclin-dependent kinase phosphorylation site unique to the nuclear form of human deoxyuridine triphosphate nucleotidohydrolase."
Ladner R.D., Carr S.A., Huddleston M.J., McNulty D.E., Caradonna S.J.
J. Biol. Chem. 271:7752-7757(1996) [PubMed] [Europe PMC] [Abstract]
Cited for: PROTEIN SEQUENCE OF N-TERMINUS, PHOSPHORYLATION AT SER-11 (ISOFORM 2), MUTAGENESIS OF SER-99, IDENTIFICATION BY MASS SPECTROMETRY.
[15]"Global, in vivo, and site-specific phosphorylation dynamics in signaling networks."
Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P., Mann M.
Cell 127:635-648(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Cervix carcinoma.
[16]"A probability-based approach for high-throughput protein phosphorylation analysis and site localization."
Beausoleil S.A., Villen J., Gerber S.A., Rush J., Gygi S.P.
Nat. Biotechnol. 24:1285-1292(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Cervix carcinoma.
[17]"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: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Cervix carcinoma.
[18]"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-88, PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-11 (ISOFORM 2), IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Cervix carcinoma.
[19]"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].
[20]"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-11 (ISOFORM 2), IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[21]"Human dUTP pyrophosphatase: uracil recognition by a beta hairpin and active sites formed by three separate subunits."
Mol C.D., Harris J.M., McIntosh E.M., Tainer J.A.
Structure 4:1077-1092(1996) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS) OF 112-252 IN COMPLEX WITH SUBSTRATE AND MAGNESIUM IONS, COFACTOR, FUNCTION, CATALYTIC ACTIVITY, SUBUNIT.
[22]"Active site closure facilitates juxtaposition of reactant atoms for initiation of catalysis by human dUTPase."
Varga B., Barabas O., Kovari J., Toth J., Hunyadi-Gulyas E., Klement E., Medzihradszky K.F., Toelgyesi F., Fidy J., Vertessy B.G.
FEBS Lett. 581:4783-4788(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (1.8 ANGSTROMS) OF 89-252 (ISOFORM 2) IN COMPLEX WITH SUBSTRATE ANALOG AND MAGNESIUM IONS, IDENTIFICATION BY MASS SPECTROMETRY, SUBUNIT.
+Additional computationally mapped references.

Web resources

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
U31930 mRNA. Translation: AAC50418.1.
U62891 mRNA. Translation: AAC51123.1.
AF018432 expand/collapse EMBL AC list , AF018429, AF018430, AF018431 Genomic DNA. Translation: AAB71393.1. Frameshift.
AF018432 expand/collapse EMBL AC list , AF018429, AF018430, AF018431 Genomic DNA. Translation: AAB71394.1.
U90223 mRNA. Translation: AAB94642.1. Frameshift.
U90224 Genomic DNA. Translation: AAB93866.1. Frameshift.
U90224 Genomic DNA. Translation: AAB93867.1.
AB049113 mRNA. Translation: BAB13724.1.
AY935242 Genomic DNA. Translation: AAX14045.1.
AK291515 mRNA. Translation: BAF84204.1.
AK312122 mRNA. Translation: BAG35058.1.
CR541720 mRNA. Translation: CAG46521.1.
CR541781 mRNA. Translation: CAG46580.1.
CH471082 Genomic DNA. Translation: EAW77350.1.
AK298464 mRNA. Translation: BAG60677.1.
BC033645 mRNA. Translation: AAH33645.1.
BC070339 mRNA. Translation: AAH70339.1.
BC110377 mRNA. Translation: AAI10378.1.
M89913 mRNA. Translation: AAA58444.1.
L11877 mRNA. Translation: AAA36801.1.
PIRA46256.
G02777.
RefSeqNP_001020419.1. NM_001025248.1.
NP_001020420.1. NM_001025249.1.
NP_001939.1. NM_001948.3.
UniGeneHs.527980.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
1Q5HX-ray2.00A/B/C112-252[»]
1Q5UX-ray2.00X/Y/Z112-252[»]
2HQUX-ray2.20A/B/C94-252[»]
3ARAX-ray1.70A/B/C94-252[»]
3ARNX-ray1.80A/B/C94-252[»]
3EHWX-ray1.80A/B/C/X/Y/Z94-252[»]
4MZ5X-ray2.10C/D97-109[»]
4MZ6X-ray1.88C/D97-109[»]
ProteinModelPortalP33316.
SMRP33316. Positions 112-236.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid108187. 14 interactions.
IntActP33316. 21 interactions.
MINTMINT-1436411.

Chemistry

BindingDBP33316.
ChEMBLCHEMBL5203.

PTM databases

PhosphoSiteP33316.

Polymorphism databases

DMDM347595814.

Proteomic databases

PaxDbP33316.
PeptideAtlasP33316.
PRIDEP33316.

Protocols and materials databases

DNASU1854.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000331200; ENSP00000370376; ENSG00000128951. [P33316-3]
ENST00000455976; ENSP00000405160; ENSG00000128951. [P33316-2]
ENST00000558813; ENSP00000453717; ENSG00000128951.
GeneID1854.
KEGGhsa:1854.
UCSCuc001zws.3. human. [P33316-3]
uc001zww.3. human. [P33316-2]

Organism-specific databases

CTD1854.
GeneCardsGC15P048623.
HGNCHGNC:3078. DUT.
HPAHPA054422.
MIM601266. gene.
neXtProtNX_P33316.
PharmGKBPA151.
GenAtlasSearch...

Phylogenomic databases

eggNOGCOG0756.
KOK01520.
TreeFamTF105416.

Enzyme and pathway databases

BioCycMetaCyc:HS05235-MONOMER.
BRENDA3.6.1.23. 2681.
ReactomeREACT_111217. Metabolism.
SABIO-RKP33316.
UniPathwayUPA00610; UER00666.

Gene expression databases

ArrayExpressP33316.
BgeeP33316.
CleanExHS_DUT.
GenevestigatorP33316.

Family and domain databases

InterProIPR008180. dUTP_pyroPase.
IPR008181. dUTP_pyroPase_sf.
[Graphical view]
PfamPF00692. dUTPase. 1 hit.
[Graphical view]
TIGRFAMsTIGR00576. dut. 1 hit.
ProtoNetSearch...

Other

EvolutionaryTraceP33316.
GeneWikiDUT_(gene).
GenomeRNAi1854.
NextBio7591.
PROP33316.
SOURCESearch...

Entry information

Entry nameDUT_HUMAN
AccessionPrimary (citable) accession number: P33316
Secondary accession number(s): A8K650 expand/collapse secondary AC list , B4DPR5, O14785, Q16708, Q16860, Q6FHN1, Q6NSA3, Q96Q81
Entry history
Integrated into UniProtKB/Swiss-Prot: February 1, 1994
Last sequence update: September 21, 2011
Last modified: April 16, 2014
This is version 149 of the entry and version 4 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

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

PATHWAY comments

Index of metabolic and biosynthesis pathways

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 15

Human chromosome 15: entries, gene names and cross-references to MIM