P33316 (DUT_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Names 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

Name:

DUT

Organism

Homo sapiens (Human) [Reference proteome]

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Opisthokonta › Metazoa › Eumetazoa › Bilateria › Deuterostomia › Chordata › Craniata › Vertebrata › Gnathostomata › Teleostomi › Euteleostomi › Sarcopterygii › Tetrapoda › Amniota › Mammalia › Theria › Eutheria › Euarchontoglires › Primates › Haplorrhini › Simiiformes › Catarrhini › Hominoidea › Hominidae › Homininae › 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	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 process	Nucleotide metabolism
Cellular component	Mitochondrion Nucleus
Coding sequence diversity	Alternative splicing Polymorphism
Domain	Transit peptide
Ligand	Magnesium
Molecular function	Hydrolase
PTM	Acetylation Phosphoprotein
Technical term	3D-structure Complete proteome Direct protein sequencing Reference proteome
Gene Ontology (GO)
Biological_process	DNA 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 pyrimidine nucleobase metabolic process Traceable author statement. Source: Reactome pyrimidine nucleoside biosynthetic process Traceable author statement. Source: Reactome
Cellular_component	mitochondrion Traceable author statement Ref.1. Source: ProtInc nucleoplasm Traceable author statement. Source: Reactome
Molecular_function	dUTP diphosphatase activity Inferred from experiment. Source: Reactome
Complete GO annotation...

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

1

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252

Helix Strand Turn

Details...

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

	Sequence		Length	Mass (Da)
	Isoform 3 (DUT-M) [UniParc]. Last modified September 21, 2011. Version 4. Checksum: 8E2EBC9ED5B0FAD2	FASTA	252	26,563
	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
	Isoform 2 (DUT-N) [UniParc]. Checksum: E75BC583BF8C7245	FASTA	164	17,748
	10 20 30 40 50 60 MPCSEETPAI SPSKRARPAE VGGMQLRFAR LSEHATAPTR GSARAAGYDL YSAYDYTIPP 70 80 90 100 110 120 MEKAVVKTDI QIALPSGCYG RVAPRSGLAA KHFIDVGAGV IDEDYRGNVG VVLFNFGKEK 130 140 150 160 FEVKKGDRIA QLICERIFYP EIEEVQALDD TERGSGGFGS TGKN

References

	« Hide 'large scale' referencesShow '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. , 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. , 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-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

NIEHS-SNPs

Cross-references

Sequence databases

EMBL
GenBank
DDBJ

U31930 mRNA. Translation: AAC50418.1.
U62891 mRNA. Translation: AAC51123.1.
AF018432 , AF018429, AF018430, AF018431 Genomic DNA. Translation: AAB71393.1. Frameshift.
AF018432 , 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.

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

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
1Q5H	X-ray	2.00	A/B/C	112-252	[»]
1Q5U	X-ray	2.00	X/Y/Z	112-252	[»]
2HQU	X-ray	2.20	A/B/C	94-252	[»]
3ARA	X-ray	1.70	A/B/C	94-252	[»]
3ARN	X-ray	1.80	A/B/C	94-252	[»]
3EHW	X-ray	1.80	A/B/C/X/Y/Z	94-252	[»]

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 , 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:	May 1, 2013
This is version 140 of the entry and version 4 of the sequence. [Complete history]

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.