P33316 (DUT_HUMAN) Reviewed, UniProtKB/Swiss-Prot
Last modified
May 1, 2013.
Version 140.
History...
Names·Attributes·General annotation·Ontologies·Interactions·Alt products·Sequence annotation·Sequences·References·Web links·Cross-refs·Entry info·DocumentsCustomize order
Names·Attributes·General annotation·Ontologies·Interactions·Alt products·Sequence annotation·Sequences·References·Web links·Cross-refs·Entry info·DocumentsCustomize orderNames and origin
| Protein names | Recommended name: Deoxyuridine 5'-triphosphate nucleotidohydrolase, mitochondrial Short name=dUTPase EC=3.6.1.23 Alternative name(s): dUTP pyrophosphatase | ||
| Gene names |
| ||
| Organism | Homo sapiens (Human) [Reference proteome] | ||
| Taxonomic identifier | 9606 [NCBI] | ||
| Taxonomic lineage | Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Primates › Haplorrhini › Catarrhini › Hominidae › Homo![]() |
Protein attributes
| Sequence length | 252 AA. |
| Sequence status | Complete. |
| Sequence processing | The displayed sequence is further processed into a mature form. |
| Protein existence | Evidence 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 | |
| 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 |
| 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
Binary interactions
With | Entry | #Exp. | IntAct | Notes |
|---|---|---|---|---|
| NUDT18 | Q6ZVK8 | 3 | EBI-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 key | Position(s) | Length | Description | Graphical view | Feature identifier | ||||||||||||||||||||||||||||||||||||
Molecule processing | |||||||||||||||||||||||||||||||||||||||||
|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|
| Transit peptide | 1 – 69 | 69 | Mitochondrion Ref.1 Ref.14 | ||||||||||||||||||||||||||||||||||||||
| Chain | 70 – 252 | 183 | Deoxyuridine 5'-triphosphate nucleotidohydrolase, mitochondrial | PRO_0000007392 | |||||||||||||||||||||||||||||||||||||
Regions | |||||||||||||||||||||||||||||||||||||||||
| Region | 173 – 175 | 3 | Substrate binding | ||||||||||||||||||||||||||||||||||||||
| Region | 187 – 190 | 4 | Substrate binding | ||||||||||||||||||||||||||||||||||||||
| Region | 246 – 247 | 2 | Substrate binding | ||||||||||||||||||||||||||||||||||||||
Sites | |||||||||||||||||||||||||||||||||||||||||
| Binding site | 198 | 1 | Substrate; via amide nitrogen and carbonyl oxygen | ||||||||||||||||||||||||||||||||||||||
| Binding site | 241 | 1 | Substrate By similarity | ||||||||||||||||||||||||||||||||||||||
Amino acid modifications | |||||||||||||||||||||||||||||||||||||||||
| Modified residue | 88 | 1 | Phosphoserine Ref.18 | ||||||||||||||||||||||||||||||||||||||
| Modified residue | 179 | 1 | N6-acetyllysine | ||||||||||||||||||||||||||||||||||||||
Natural variations | |||||||||||||||||||||||||||||||||||||||||
| Alternative sequence | 1 – 93 | 93 | MTPLC…PAPGP → MPCSE in isoform 2. | VSP_001324 | |||||||||||||||||||||||||||||||||||||
| Natural variant | 100 | 1 | P → S. Ref.8 Corresponds to variant rs28381104 [ dbSNP | Ensembl ]. | VAR_022314 | |||||||||||||||||||||||||||||||||||||
Experimental info | |||||||||||||||||||||||||||||||||||||||||
| Mutagenesis | 99 | 1 | S → A: Loss of phosphorylation. Ref.14 | ||||||||||||||||||||||||||||||||||||||
| Sequence conflict | 175 | 1 | G → S in BAF84204. Ref.6 | ||||||||||||||||||||||||||||||||||||||
| Sequence conflict | 182 | 1 | I → T in BAG60677. Ref.6 | ||||||||||||||||||||||||||||||||||||||
Secondary structure | |||||||||||||||||||||||||||||||||||||||||
Helix Strand Turn | |||||||||||||||||||||||||||||||||||||||||
| Beta strand | 113 – 120 | 8 | |||||||||||||||||||||||||||||||||||||||
| Beta strand | 127 – 130 | 4 | |||||||||||||||||||||||||||||||||||||||
| Beta strand | 134 – 139 | 6 | |||||||||||||||||||||||||||||||||||||||
| Beta strand | 144 – 146 | 3 | |||||||||||||||||||||||||||||||||||||||
| Beta strand | 150 – 155 | 6 | |||||||||||||||||||||||||||||||||||||||
| Beta strand | 158 – 161 | 4 | |||||||||||||||||||||||||||||||||||||||
| Beta strand | 166 – 171 | 6 | |||||||||||||||||||||||||||||||||||||||
| Helix | 174 – 180 | 7 | |||||||||||||||||||||||||||||||||||||||
| Beta strand | 182 – 185 | 4 | |||||||||||||||||||||||||||||||||||||||
| Beta strand | 198 – 203 | 6 | |||||||||||||||||||||||||||||||||||||||
| Beta strand | 205 – 207 | 3 | |||||||||||||||||||||||||||||||||||||||
| Beta strand | 209 – 211 | 3 | |||||||||||||||||||||||||||||||||||||||
| Beta strand | 216 – 226 | 11 | |||||||||||||||||||||||||||||||||||||||
| Beta strand | 229 – 232 | 4 | |||||||||||||||||||||||||||||||||||||||
| Beta strand | 240 – 242 | 3 | |||||||||||||||||||||||||||||||||||||||
| Turn | 246 – 249 | 4 | |||||||||||||||||||||||||||||||||||||||
Sequences
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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, 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. 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. 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-99 (ISOFORM 2), MUTAGENESIS OF SER-99, 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), MASS SPECTROMETRY. 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), MASS SPECTROMETRY. |
| [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, 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 AF018431 Genomic DNA. Translation: AAB71393.1. Frameshift.AF018432 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. | ||||||||||||||||||||||||||||||||||||||||||
| IPI | IPI00375015. IPI00749113. | ||||||||||||||||||||||||||||||||||||||||||
| PIR | A46256. G02777. | ||||||||||||||||||||||||||||||||||||||||||
| RefSeq | NP_001020419.1. NM_001025248.1. NP_001020420.1. NM_001025249.1. NP_001939.1. NM_001948.3. | ||||||||||||||||||||||||||||||||||||||||||
| UniGene | Hs.527980. | ||||||||||||||||||||||||||||||||||||||||||
3D structure databases | |||||||||||||||||||||||||||||||||||||||||||
| PDBe RCSB PDB PDBj |
| ||||||||||||||||||||||||||||||||||||||||||
| ProteinModelPortal | P33316. | ||||||||||||||||||||||||||||||||||||||||||
| SMR | P33316. Positions 112-236. | ||||||||||||||||||||||||||||||||||||||||||
| ModBase | Search... | ||||||||||||||||||||||||||||||||||||||||||
Protein-protein interaction databases | |||||||||||||||||||||||||||||||||||||||||||
| IntAct | P33316. 20 interactions. | ||||||||||||||||||||||||||||||||||||||||||
| MINT | MINT-1436411. | ||||||||||||||||||||||||||||||||||||||||||
PTM databases | |||||||||||||||||||||||||||||||||||||||||||
| PhosphoSite | P33316. | ||||||||||||||||||||||||||||||||||||||||||
Polymorphism databases | |||||||||||||||||||||||||||||||||||||||||||
| DMDM | 3041664. | ||||||||||||||||||||||||||||||||||||||||||
Proteomic databases | |||||||||||||||||||||||||||||||||||||||||||
| PaxDb | P33316. | ||||||||||||||||||||||||||||||||||||||||||
| PeptideAtlas | P33316. | ||||||||||||||||||||||||||||||||||||||||||
| PRIDE | P33316. | ||||||||||||||||||||||||||||||||||||||||||
Protocols and materials databases | |||||||||||||||||||||||||||||||||||||||||||
| DNASU | 1854. | ||||||||||||||||||||||||||||||||||||||||||
| StructuralBiologyKnowledgebase | Search... | ||||||||||||||||||||||||||||||||||||||||||
Genome annotation databases | |||||||||||||||||||||||||||||||||||||||||||
| Ensembl | ENST00000331200; ENSP00000370376; ENSG00000128951. ENST00000455976; ENSP00000405160; ENSG00000128951. ENST00000558813; ENSP00000453717; ENSG00000128951. | ||||||||||||||||||||||||||||||||||||||||||
| GeneID | 1854. | ||||||||||||||||||||||||||||||||||||||||||
| KEGG | hsa:1854. | ||||||||||||||||||||||||||||||||||||||||||
| UCSC | uc001zws.3. human. uc001zww.3. human. | ||||||||||||||||||||||||||||||||||||||||||
Organism-specific databases | |||||||||||||||||||||||||||||||||||||||||||
| CTD | 1854. | ||||||||||||||||||||||||||||||||||||||||||
| GeneCards | GC15P048623. | ||||||||||||||||||||||||||||||||||||||||||
| HGNC | HGNC:3078. DUT. | ||||||||||||||||||||||||||||||||||||||||||
| MIM | 601266. gene. | ||||||||||||||||||||||||||||||||||||||||||
| neXtProt | NX_P33316. | ||||||||||||||||||||||||||||||||||||||||||
| PharmGKB | PA151. | ||||||||||||||||||||||||||||||||||||||||||
| GenAtlas | Search... | ||||||||||||||||||||||||||||||||||||||||||
Phylogenomic databases | |||||||||||||||||||||||||||||||||||||||||||
| eggNOG | COG0756. | ||||||||||||||||||||||||||||||||||||||||||
| KO | K01520. | ||||||||||||||||||||||||||||||||||||||||||
| OMA | MTPLCPR. | ||||||||||||||||||||||||||||||||||||||||||
Enzyme and pathway databases | |||||||||||||||||||||||||||||||||||||||||||
| BRENDA | 3.6.1.23. 2681. | ||||||||||||||||||||||||||||||||||||||||||
| Reactome | REACT_111217. Metabolism. | ||||||||||||||||||||||||||||||||||||||||||
| SABIO-RK | P33316. | ||||||||||||||||||||||||||||||||||||||||||
| UniPathway | UPA00610; UER00666. | ||||||||||||||||||||||||||||||||||||||||||
Gene expression databases | |||||||||||||||||||||||||||||||||||||||||||
| ArrayExpress | P33316. | ||||||||||||||||||||||||||||||||||||||||||
| Bgee | P33316. | ||||||||||||||||||||||||||||||||||||||||||
| CleanEx | HS_DUT. | ||||||||||||||||||||||||||||||||||||||||||
| Genevestigator | P33316. | ||||||||||||||||||||||||||||||||||||||||||
| GermOnline | ENSG00000128951. Homo sapiens. | ||||||||||||||||||||||||||||||||||||||||||
Family and domain databases | |||||||||||||||||||||||||||||||||||||||||||
| InterPro | IPR008180. dUTP_pyroPase. IPR008181. dUTP_pyroPase_sf. [Graphical view] | ||||||||||||||||||||||||||||||||||||||||||
| PANTHER | PTHR11241. PTHR11241. 1 hit. | ||||||||||||||||||||||||||||||||||||||||||
| Pfam | PF00692. dUTPase. 1 hit. [Graphical view] | ||||||||||||||||||||||||||||||||||||||||||
| TIGRFAMs | TIGR00576. dut. 1 hit. | ||||||||||||||||||||||||||||||||||||||||||
| ProtoNet | Search... | ||||||||||||||||||||||||||||||||||||||||||
Other | |||||||||||||||||||||||||||||||||||||||||||
| BindingDB | P33316. | ||||||||||||||||||||||||||||||||||||||||||
| ChEMBL | CHEMBL5203. | ||||||||||||||||||||||||||||||||||||||||||
| EvolutionaryTrace | P33316. | ||||||||||||||||||||||||||||||||||||||||||
| GenomeRNAi | 1854. | ||||||||||||||||||||||||||||||||||||||||||
| NextBio | 7591. | ||||||||||||||||||||||||||||||||||||||||||
| SOURCE | Search... | ||||||||||||||||||||||||||||||||||||||||||
Entry information
| Entry name | DUT_HUMAN | ||||||||
| Accession | Primary (citable) accession number: P33316 Secondary accession number(s): A8K650 Q96Q81 | ||||||||
| Entry history |
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| Entry status | Reviewed (UniProtKB/Swiss-Prot) | ||||||||
| Annotation program | Chordata Protein Annotation Program | ||||||||
| Disclaimer | Any 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
| Human chromosome 15 Human chromosome 15: entries, gene names and cross-references to MIM |
| Human entries with polymorphisms or disease mutations List of human entries with polymorphisms or disease mutations |
| Human polymorphisms and disease mutations Index of human polymorphisms and disease mutations |
| MIM cross-references Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot |
| PATHWAY comments Index of metabolic and biosynthesis pathways |
| PDB cross-references Index of Protein Data Bank (PDB) cross-references |
| SIMILARITY comments Index of protein domains and families |

Clusters with
