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Deoxyuridine 5'-triphosphate nucleotidohydrolase, mitochondrial (dUTPase) (EC 3.6.1.23) (dUTP pyrophosphatase)

 DUT_HUMAN               Reviewed;         252 AA.
P33316; A8K650; B4DPR5; O14785; Q16708; Q16860; Q6FHN1; Q6NSA3;
Q96Q81;
01-FEB-1994, integrated into UniProtKB/Swiss-Prot.
21-SEP-2011, sequence version 4.
25-OCT-2017, entry version 187.
RecName: Full=Deoxyuridine 5'-triphosphate nucleotidohydrolase, mitochondrial;
Short=dUTPase;
EC=3.6.1.23;
AltName: Full=dUTP pyrophosphatase;
Flags: Precursor;
Name=DUT;
Homo sapiens (Human).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
Catarrhini; Hominidae; Homo.
NCBI_TaxID=9606;
[1]
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, AND IDENTIFICATION BY MASS
SPECTROMETRY.
TISSUE=T-cell;
PubMed=8631816; DOI=10.1074/jbc.271.13.7745;
Ladner R.D., McNulty D.E., Carr S.A., Roberts G.D., Caradonna S.J.;
"Characterization of distinct nuclear and mitochondrial forms of human
deoxyuridine triphosphate nucleotidohydrolase.";
J. Biol. Chem. 271:7745-7751(1996).
[2]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2).
PubMed=9070952; DOI=10.1006/geno.1996.4540;
Cohen D., Heng H.H.Q., Shi X.-M., McIntosh E.M., Tsui L.-C.,
Pearlman R.E.;
"Assignment of the human dUTPase gene (DUT) to chromosome 15q15-q21. 1
by fluorescence in situ hybridization.";
Genomics 40:213-215(1997).
[3]
NUCLEOTIDE SEQUENCE [GENOMIC DNA] (ISOFORMS 2 AND 3).
Pearlman R.E.;
"Human genomic nuclear and mitochondria dUTPase gene.";
Submitted (OCT-1997) to the EMBL/GenBank/DDBJ databases.
[4]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 3), NUCLEOTIDE SEQUENCE [GENOMIC
DNA] OF 1-139 (ISOFORMS 2 AND 3), SUBCELLULAR LOCATION, AND TISSUE
SPECIFICITY.
TISSUE=Lung fibroblast;
PubMed=9228092; DOI=10.1074/jbc.272.30.19072;
Ladner R.D., Caradonna S.J.;
"The human dUTPase gene encodes both nuclear and mitochondrial
isoforms. Differential expression of the isoforms and characterization
of a cDNA encoding the mitochondrial species.";
J. Biol. Chem. 272:19072-19080(1997).
[5]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2).
Chano T., Okabe H., Baldini N., Lapucci C., Scotlandi K., Serra M.,
Saeki Y.;
"Unknown transcriptional variant of nuclear dUTPase in human
osteosarcoma.";
Submitted (SEP-2000) to the EMBL/GenBank/DDBJ databases.
[6]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 2 AND 3).
PubMed=14702039; DOI=10.1038/ng1285;
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.,
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.;
"Complete sequencing and characterization of 21,243 full-length human
cDNAs.";
Nat. Genet. 36:40-45(2004).
[7]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
Ebert L., Schick M., Neubert P., Schatten R., Henze S., Korn B.;
"Cloning of human full open reading frames in Gateway(TM) system entry
vector (pDONR201).";
Submitted (JUN-2004) to the EMBL/GenBank/DDBJ databases.
[8]
NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND VARIANT SER-100.
NIEHS SNPs program;
Submitted (FEB-2005) to the EMBL/GenBank/DDBJ databases.
[9]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
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., 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.
[10]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 2 AND 3).
TISSUE=Brain, Eye, and Urinary bladder;
PubMed=15489334; DOI=10.1101/gr.2596504;
The MGC Project Team;
"The status, quality, and expansion of the NIH full-length cDNA
project: the Mammalian Gene Collection (MGC).";
Genome Res. 14:2121-2127(2004).
[11]
NUCLEOTIDE SEQUENCE [MRNA] OF 112-252.
PubMed=1325640; DOI=10.1073/pnas.89.17.8020;
McIntosh E.M., Ager D.D., Gadsden M.H., Haynes R.H.;
"Human dUTP pyrophosphatase: cDNA sequence and potential biological
importance of the enzyme.";
Proc. Natl. Acad. Sci. U.S.A. 89:8020-8024(1992).
[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]
NUCLEOTIDE SEQUENCE [MRNA] OF 112-252, PARTIAL PROTEIN SEQUENCE, AND
PHOSPHORYLATION.
TISSUE=Lymphocyte;
PubMed=8389461; DOI=10.1073/pnas.90.11.4991;
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.;
"Maturation stage and proliferation-dependent expression of dUTPase in
human T cells.";
Proc. Natl. Acad. Sci. U.S.A. 90:4991-4995(1993).
[14]
PROTEIN SEQUENCE OF N-TERMINUS, PHOSPHORYLATION AT SER-11 (ISOFORM 2),
MUTAGENESIS OF SER-99, AND IDENTIFICATION BY MASS SPECTROMETRY.
PubMed=8631817; DOI=10.1074/jbc.271.13.7752;
Ladner R.D., Carr S.A., Huddleston M.J., McNulty D.E., Caradonna S.J.;
"Identification of a consensus cyclin-dependent kinase phosphorylation
site unique to the nuclear form of human deoxyuridine triphosphate
nucleotidohydrolase.";
J. Biol. Chem. 271:7752-7757(1996).
[15]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Cervix carcinoma;
PubMed=17081983; DOI=10.1016/j.cell.2006.09.026;
Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P.,
Mann M.;
"Global, in vivo, and site-specific phosphorylation dynamics in
signaling networks.";
Cell 127:635-648(2006).
[16]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Cervix carcinoma;
PubMed=16964243; DOI=10.1038/nbt1240;
Beausoleil S.A., Villen J., Gerber S.A., Rush J., Gygi S.P.;
"A probability-based approach for high-throughput protein
phosphorylation analysis and site localization.";
Nat. Biotechnol. 24:1285-1292(2006).
[17]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Cervix carcinoma;
PubMed=18669648; DOI=10.1073/pnas.0805139105;
Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,
Elledge S.J., Gygi S.P.;
"A quantitative atlas of mitotic phosphorylation.";
Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008).
[18]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-88, PHOSPHORYLATION
[LARGE SCALE ANALYSIS] AT SER-11 (ISOFORM 2), AND IDENTIFICATION BY
MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Cervix carcinoma;
PubMed=20068231; DOI=10.1126/scisignal.2000475;
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.;
"Quantitative phosphoproteomics reveals widespread full
phosphorylation site occupancy during mitosis.";
Sci. Signal. 3:RA3-RA3(2010).
[19]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=21269460; DOI=10.1186/1752-0509-5-17;
Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P.,
Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.;
"Initial characterization of the human central proteome.";
BMC Syst. Biol. 5:17-17(2011).
[20]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-11 (ISOFORM 2), AND
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=21406692; DOI=10.1126/scisignal.2001570;
Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J.,
Johansen P.T., Kratchmarova I., Kassem M., Mann M., Olsen J.V.,
Blagoev B.;
"System-wide temporal characterization of the proteome and
phosphoproteome of human embryonic stem cell differentiation.";
Sci. Signal. 4:RS3-RS3(2011).
[21]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-88 AND SER-99, AND
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Cervix carcinoma, and Erythroleukemia;
PubMed=23186163; DOI=10.1021/pr300630k;
Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J.,
Mohammed S.;
"Toward a comprehensive characterization of a human cancer cell
phosphoproteome.";
J. Proteome Res. 12:260-271(2013).
[22]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-88, AND IDENTIFICATION
BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Liver;
PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014;
Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D.,
Wang L., Ye M., Zou H.;
"An enzyme assisted RP-RPLC approach for in-depth analysis of human
liver phosphoproteome.";
J. Proteomics 96:253-262(2014).
[23]
CLEAVAGE OF TRANSIT PEPTIDE [LARGE SCALE ANALYSIS] AFTER GLY-69, AND
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=25944712; DOI=10.1002/pmic.201400617;
Vaca Jacome A.S., Rabilloud T., Schaeffer-Reiss C., Rompais M.,
Ayoub D., Lane L., Bairoch A., Van Dorsselaer A., Carapito C.;
"N-terminome analysis of the human mitochondrial proteome.";
Proteomics 15:2519-2524(2015).
[24]
X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS) OF 112-252 IN COMPLEX WITH
SUBSTRATE AND MAGNESIUM IONS, COFACTOR, FUNCTION, CATALYTIC ACTIVITY,
AND SUBUNIT.
PubMed=8805593; DOI=10.1016/S0969-2126(96)00114-1;
Mol C.D., Harris J.M., McIntosh E.M., Tainer J.A.;
"Human dUTP pyrophosphatase: uracil recognition by a beta hairpin and
active sites formed by three separate subunits.";
Structure 4:1077-1092(1996).
[25]
X-RAY CRYSTALLOGRAPHY (1.8 ANGSTROMS) OF 89-252 (ISOFORM 2) IN COMPLEX
WITH SUBSTRATE ANALOG AND MAGNESIUM IONS, IDENTIFICATION BY MASS
SPECTROMETRY, AND SUBUNIT.
PubMed=17880943; DOI=10.1016/j.febslet.2007.09.005;
Varga B., Barabas O., Kovari J., Toth J., Hunyadi-Gulyas E.,
Klement E., Medzihradszky K.F., Toelgyesi F., Fidy J., Vertessy B.G.;
"Active site closure facilitates juxtaposition of reactant atoms for
initiation of catalysis by human dUTPase.";
FEBS Lett. 581:4783-4788(2007).
-!- 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.
{ECO:0000269|PubMed:8805593}.
-!- CATALYTIC ACTIVITY: dUTP + H(2)O = dUMP + diphosphate.
{ECO:0000269|PubMed:8805593}.
-!- COFACTOR:
Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
Evidence={ECO:0000269|PubMed:8805593};
-!- ENZYME REGULATION: Phosphorylation is necessary for activity.
-!- BIOPHYSICOCHEMICAL PROPERTIES:
Kinetic parameters:
KM=2.5 uM for dUTP {ECO:0000269|PubMed:8631816};
Note=for both isoform 2 and isoform 3.;
-!- PATHWAY: Pyrimidine metabolism; dUMP biosynthesis; dUMP from dCTP
(dUTP route): step 2/2.
-!- SUBUNIT: Homotrimer. {ECO:0000269|PubMed:17880943,
ECO:0000269|PubMed:8805593}.
-!- INTERACTION:
Q6ZVK8:NUDT18; NbExp=3; IntAct=EBI-353224, EBI-740486;
-!- SUBCELLULAR LOCATION: Isoform 2: Nucleus
{ECO:0000269|PubMed:8631816, ECO:0000269|PubMed:9070952}.
-!- SUBCELLULAR LOCATION: Isoform 3: Mitochondrion
{ECO:0000269|PubMed:8631816, ECO:0000269|PubMed:9070952}.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=2;
Name=3; Synonyms=DUT-M;
IsoId=P33316-3; Sequence=Displayed;
Name=2; Synonyms=DUT-N;
IsoId=P33316-2; Sequence=VSP_001324;
Note=Major isoform. Initiator Met-1 is removed. Contains a
phosphoserine at position 11. {ECO:0000244|PubMed:20068231,
ECO:0000244|PubMed:21406692, ECO:0000269|PubMed:8631816,
ECO:0000269|PubMed:8631817};
-!- 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). {ECO:0000269|PubMed:9228092}.
-!- PTM: 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. {ECO:0000269|PubMed:8389461}.
-!- 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.
-!- SIMILARITY: Belongs to the dUTPase family. {ECO:0000305}.
-!- SEQUENCE CAUTION:
Sequence=AAB71393.1; Type=Frameshift; Positions=29, 47; Evidence={ECO:0000305};
Sequence=AAB93866.1; Type=Frameshift; Positions=29, 47; Evidence={ECO:0000305};
Sequence=AAB94642.1; Type=Frameshift; Positions=29, 47; Evidence={ECO:0000305};
-!- WEB RESOURCE: Name=NIEHS-SNPs;
URL="http://egp.gs.washington.edu/data/dut/";
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EMBL; U31930; AAC50418.1; -; mRNA.
EMBL; U62891; AAC51123.1; -; mRNA.
EMBL; AF018432; AAB71393.1; ALT_FRAME; Genomic_DNA.
EMBL; AF018429; AAB71393.1; JOINED; Genomic_DNA.
EMBL; AF018430; AAB71393.1; JOINED; Genomic_DNA.
EMBL; AF018431; AAB71393.1; JOINED; Genomic_DNA.
EMBL; AF018432; AAB71394.1; -; Genomic_DNA.
EMBL; AF018429; AAB71394.1; JOINED; Genomic_DNA.
EMBL; AF018430; AAB71394.1; JOINED; Genomic_DNA.
EMBL; AF018431; AAB71394.1; JOINED; Genomic_DNA.
EMBL; U90223; AAB94642.1; ALT_FRAME; mRNA.
EMBL; U90224; AAB93866.1; ALT_FRAME; Genomic_DNA.
EMBL; U90224; AAB93867.1; -; Genomic_DNA.
EMBL; AB049113; BAB13724.1; -; mRNA.
EMBL; AY935242; AAX14045.1; -; Genomic_DNA.
EMBL; AK291515; BAF84204.1; -; mRNA.
EMBL; AK312122; BAG35058.1; -; mRNA.
EMBL; CR541720; CAG46521.1; -; mRNA.
EMBL; CR541781; CAG46580.1; -; mRNA.
EMBL; CH471082; EAW77350.1; -; Genomic_DNA.
EMBL; AK298464; BAG60677.1; -; mRNA.
EMBL; BC033645; AAH33645.1; -; mRNA.
EMBL; BC070339; AAH70339.1; -; mRNA.
EMBL; BC110377; AAI10378.1; -; mRNA.
EMBL; M89913; AAA58444.1; -; mRNA.
EMBL; L11877; AAA36801.1; -; mRNA.
CCDS; CCDS32231.1; -. [P33316-3]
CCDS; CCDS45255.1; -. [P33316-2]
PIR; A46256; A46256.
PIR; G02777; G02777.
RefSeq; NP_001020419.1; NM_001025248.1. [P33316-3]
RefSeq; NP_001020420.1; NM_001025249.1.
RefSeq; NP_001317215.1; NM_001330286.1.
RefSeq; NP_001939.1; NM_001948.3. [P33316-2]
UniGene; Hs.527980; -.
PDB; 1Q5H; X-ray; 2.00 A; A/B/C=112-252.
PDB; 1Q5U; X-ray; 2.00 A; X/Y/Z=112-252.
PDB; 2HQU; X-ray; 2.20 A; A/B/C=94-252.
PDB; 3ARA; X-ray; 1.70 A; A/B/C=94-252.
PDB; 3ARN; X-ray; 1.80 A; A/B/C=94-252.
PDB; 3EHW; X-ray; 1.80 A; A/B/C/X/Y/Z=94-252.
PDB; 4MZ5; X-ray; 2.10 A; A/C=97-109.
PDB; 4MZ6; X-ray; 1.88 A; A/C=97-109.
PDBsum; 1Q5H; -.
PDBsum; 1Q5U; -.
PDBsum; 2HQU; -.
PDBsum; 3ARA; -.
PDBsum; 3ARN; -.
PDBsum; 3EHW; -.
PDBsum; 4MZ5; -.
PDBsum; 4MZ6; -.
ProteinModelPortal; P33316; -.
SMR; P33316; -.
BioGrid; 108187; 72.
IntAct; P33316; 22.
MINT; MINT-1436411; -.
STRING; 9606.ENSP00000370376; -.
BindingDB; P33316; -.
ChEMBL; CHEMBL5203; -.
DrugBank; DB03413; Deoxyuridine-5'-Diphosphate.
iPTMnet; P33316; -.
PhosphoSitePlus; P33316; -.
SwissPalm; P33316; -.
BioMuta; DUT; -.
DMDM; 347595814; -.
EPD; P33316; -.
PaxDb; P33316; -.
PeptideAtlas; P33316; -.
PRIDE; P33316; -.
TopDownProteomics; P33316-2; -. [P33316-2]
TopDownProteomics; P33316-3; -. [P33316-3]
DNASU; 1854; -.
Ensembl; ENST00000331200; ENSP00000370376; ENSG00000128951. [P33316-3]
Ensembl; ENST00000455976; ENSP00000405160; ENSG00000128951. [P33316-2]
GeneID; 1854; -.
KEGG; hsa:1854; -.
UCSC; uc001zws.4; human. [P33316-3]
CTD; 1854; -.
DisGeNET; 1854; -.
EuPathDB; HostDB:ENSG00000128951.13; -.
GeneCards; DUT; -.
HGNC; HGNC:3078; DUT.
HPA; HPA054422; -.
HPA; HPA060360; -.
MIM; 601266; gene.
neXtProt; NX_P33316; -.
OpenTargets; ENSG00000128951; -.
PharmGKB; PA151; -.
eggNOG; KOG3370; Eukaryota.
eggNOG; COG0756; LUCA.
GeneTree; ENSGT00390000018390; -.
KO; K01520; -.
OrthoDB; EOG091G14FN; -.
PhylomeDB; P33316; -.
TreeFam; TF105416; -.
BioCyc; MetaCyc:HS05235-MONOMER; -.
BRENDA; 3.6.1.23; 2681.
Reactome; R-HSA-499943; Interconversion of nucleotide di- and triphosphates.
SABIO-RK; P33316; -.
UniPathway; UPA00610; UER00666.
ChiTaRS; DUT; human.
EvolutionaryTrace; P33316; -.
GeneWiki; DUT_(gene); -.
GenomeRNAi; 1854; -.
PRO; PR:P33316; -.
Proteomes; UP000005640; Chromosome 15.
Bgee; ENSG00000128951; -.
CleanEx; HS_DUT; -.
ExpressionAtlas; P33316; baseline and differential.
Genevisible; P33316; HS.
GO; GO:0070062; C:extracellular exosome; IDA:UniProtKB.
GO; GO:0005739; C:mitochondrion; TAS:ProtInc.
GO; GO:0005654; C:nucleoplasm; IDA:HPA.
GO; GO:0005634; C:nucleus; TAS:ProtInc.
GO; GO:0004170; F:dUTP diphosphatase activity; EXP:Reactome.
GO; GO:0000287; F:magnesium ion binding; IBA:GO_Central.
GO; GO:0003723; F:RNA binding; IDA:UniProtKB.
GO; GO:0006260; P:DNA replication; TAS:ProtInc.
GO; GO:0006226; P:dUMP biosynthetic process; IBA:GO_Central.
GO; GO:0046081; P:dUTP catabolic process; IBA:GO_Central.
GO; GO:0006139; P:nucleobase-containing compound metabolic process; TAS:ProtInc.
GO; GO:0015949; P:nucleobase-containing small molecule interconversion; TAS:Reactome.
CDD; cd07557; trimeric_dUTPase; 1.
InterPro; IPR029054; dUTPase-like.
InterPro; IPR036157; dUTPase-like_sf.
InterPro; IPR008181; dUTPase_1.
InterPro; IPR033704; dUTPase_trimeric.
Pfam; PF00692; dUTPase; 1.
SUPFAM; SSF51283; SSF51283; 1.
TIGRFAMs; TIGR00576; dut; 1.
1: Evidence at protein level;
3D-structure; Alternative splicing; Complete proteome;
Direct protein sequencing; Hydrolase; Magnesium; Mitochondrion;
Nucleotide metabolism; Nucleus; Phosphoprotein; Polymorphism;
Reference proteome; Transit peptide.
TRANSIT 1 69 Mitochondrion.
{ECO:0000244|PubMed:25944712,
ECO:0000269|PubMed:8631816,
ECO:0000269|PubMed:8631817}.
CHAIN 70 252 Deoxyuridine 5'-triphosphate
nucleotidohydrolase, mitochondrial.
/FTId=PRO_0000007392.
REGION 173 175 Substrate binding.
REGION 187 190 Substrate binding.
REGION 246 247 Substrate binding.
BINDING 198 198 Substrate; via amide nitrogen and
carbonyl oxygen.
{ECO:0000269|PubMed:8805593}.
BINDING 241 241 Substrate. {ECO:0000250}.
MOD_RES 88 88 Phosphoserine.
{ECO:0000244|PubMed:20068231,
ECO:0000244|PubMed:23186163,
ECO:0000244|PubMed:24275569}.
MOD_RES 99 99 Phosphoserine.
{ECO:0000244|PubMed:23186163}.
VAR_SEQ 1 93 MTPLCPRPALCYHFLTSLLRSAMQNARGARQRAEAAVLSGP
GPPLGRAAQHGIPRPLSSAGRLSQGCRGASTVGAAGWKGEL
PKAGGSPAPGP -> MPCSE (in isoform 2).
{ECO:0000303|PubMed:14702039,
ECO:0000303|PubMed:15489334,
ECO:0000303|PubMed:8631816,
ECO:0000303|PubMed:9070952,
ECO:0000303|Ref.5, ECO:0000303|Ref.7}.
/FTId=VSP_001324.
VARIANT 100 100 P -> S (in dbSNP:rs28381104).
{ECO:0000269|Ref.8}.
/FTId=VAR_022314.
MUTAGEN 99 99 S->A: Loss of phosphorylation.
{ECO:0000269|PubMed:8631817}.
CONFLICT 175 175 G -> S (in Ref. 6; BAF84204).
{ECO:0000305}.
CONFLICT 182 182 I -> T (in Ref. 6; BAG60677).
{ECO:0000305}.
STRAND 113 120 {ECO:0000244|PDB:3ARA}.
STRAND 127 130 {ECO:0000244|PDB:3EHW}.
STRAND 134 139 {ECO:0000244|PDB:3ARA}.
STRAND 144 146 {ECO:0000244|PDB:3ARA}.
STRAND 150 155 {ECO:0000244|PDB:3ARA}.
STRAND 158 161 {ECO:0000244|PDB:3ARA}.
STRAND 166 171 {ECO:0000244|PDB:3ARA}.
HELIX 174 180 {ECO:0000244|PDB:3ARA}.
STRAND 182 185 {ECO:0000244|PDB:3ARA}.
STRAND 198 203 {ECO:0000244|PDB:3ARA}.
STRAND 205 207 {ECO:0000244|PDB:3ARA}.
STRAND 209 211 {ECO:0000244|PDB:3ARA}.
STRAND 216 226 {ECO:0000244|PDB:3ARA}.
STRAND 229 232 {ECO:0000244|PDB:3ARA}.
STRAND 240 242 {ECO:0000244|PDB:3EHW}.
TURN 246 249 {ECO:0000244|PDB:3EHW}.
SEQUENCE 252 AA; 26563 MW; 8E2EBC9ED5B0FAD2 CRC64;
MTPLCPRPAL CYHFLTSLLR SAMQNARGAR QRAEAAVLSG PGPPLGRAAQ HGIPRPLSSA
GRLSQGCRGA STVGAAGWKG ELPKAGGSPA PGPETPAISP SKRARPAEVG GMQLRFARLS
EHATAPTRGS ARAAGYDLYS AYDYTIPPME KAVVKTDIQI ALPSGCYGRV APRSGLAAKH
FIDVGAGVID EDYRGNVGVV LFNFGKEKFE VKKGDRIAQL ICERIFYPEI EEVQALDDTE
RGSGGFGSTG KN


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