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P33316

- DUT_HUMAN

UniProt

P33316 - DUT_HUMAN

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Protein

Deoxyuridine 5'-triphosphate nucleotidohydrolase, mitochondrial

Gene

DUT

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli

Functioni

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.1 Publication

Catalytic activityi

dUTP + H2O = dUMP + diphosphate.1 Publication

Cofactori

Magnesium.1 Publication

Enzyme regulationi

Phosphorylation is necessary for activity.

Kineticsi

for both isoform 2 and isoform 3.

  1. KM=2.5 µM for dUTP1 Publication

Pathwayi

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei198 – 1981Substrate; via amide nitrogen and carbonyl oxygen1 Publication
Binding sitei241 – 2411SubstrateBy similarity

GO - Molecular functioni

  1. dUTP diphosphatase activity Source: Reactome
  2. poly(A) RNA binding Source: UniProtKB
  3. pyrimidine deoxyribonucleotide binding Source: Ensembl
  4. receptor inhibitor activity Source: Ensembl

GO - Biological processi

  1. DNA replication Source: ProtInc
  2. dUMP biosynthetic process Source: UniProtKB-UniPathway
  3. dUTP catabolic process Source: Ensembl
  4. liver development Source: Ensembl
  5. nucleobase-containing compound metabolic process Source: ProtInc
  6. nucleobase-containing small molecule metabolic process Source: Reactome
  7. protein homotrimerization Source: Ensembl
  8. pyrimidine nucleobase metabolic process Source: Reactome
  9. pyrimidine nucleoside biosynthetic process Source: Reactome
  10. regulation of protein heterodimerization activity Source: Ensembl
  11. response to organic cyclic compound Source: Ensembl
  12. small molecule metabolic process Source: Reactome
Complete GO annotation...

Keywords - Molecular functioni

Hydrolase

Keywords - Biological processi

Nucleotide metabolism

Keywords - Ligandi

Magnesium

Enzyme and pathway databases

BioCyciMetaCyc:HS05235-MONOMER.
BRENDAi3.6.1.23. 2681.
ReactomeiREACT_21376. Pyrimidine biosynthesis.
SABIO-RKP33316.
UniPathwayiUPA00610; UER00666.

Names & Taxonomyi

Protein namesi
Recommended name:
Deoxyuridine 5'-triphosphate nucleotidohydrolase, mitochondrial (EC:3.6.1.23)
Short name:
dUTPase
Alternative name(s):
dUTP pyrophosphatase
Gene namesi
Name:DUT
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640: Chromosome 15

Organism-specific databases

HGNCiHGNC:3078. DUT.

Subcellular locationi

GO - Cellular componenti

  1. cytosol Source: Ensembl
  2. extracellular vesicular exosome Source: UniProt
  3. mitochondrion Source: ProtInc
  4. nucleoplasm Source: Reactome
  5. nucleus Source: HPA
Complete GO annotation...

Keywords - Cellular componenti

Mitochondrion, Nucleus

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi99 – 991S → A: Loss of phosphorylation. 1 Publication

Organism-specific databases

PharmGKBiPA151.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Transit peptidei1 – 6969Mitochondrion2 PublicationsAdd
BLAST
Chaini70 – 252183Deoxyuridine 5'-triphosphate nucleotidohydrolase, mitochondrialPRO_0000007392Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei88 – 881Phosphoserine1 Publication

Post-translational modificationi

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.2 Publications
The initiator methionine is cleaved in isoform 2.

Keywords - PTMi

Phosphoprotein

Proteomic databases

MaxQBiP33316.
PaxDbiP33316.
PeptideAtlasiP33316.
PRIDEiP33316.

PTM databases

PhosphoSiteiP33316.

Expressioni

Tissue specificityi

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).1 Publication

Gene expression databases

BgeeiP33316.
CleanExiHS_DUT.
ExpressionAtlasiP33316. baseline and differential.
GenevestigatoriP33316.

Organism-specific databases

HPAiHPA054422.

Interactioni

Subunit structurei

Homotrimer.2 Publications

Binary interactionsi

WithEntry#Exp.IntActNotes
NUDT18Q6ZVK83EBI-353224,EBI-740486

Protein-protein interaction databases

BioGridi108187. 14 interactions.
IntActiP33316. 21 interactions.
MINTiMINT-1436411.

Structurei

Secondary structure

1
252
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi113 – 1208
Beta strandi127 – 1304
Beta strandi134 – 1396
Beta strandi144 – 1463
Beta strandi150 – 1556
Beta strandi158 – 1614
Beta strandi166 – 1716
Helixi174 – 1807
Beta strandi182 – 1854
Beta strandi198 – 2036
Beta strandi205 – 2073
Beta strandi209 – 2113
Beta strandi216 – 22611
Beta strandi229 – 2324
Beta strandi240 – 2423
Turni246 – 2494

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
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-ray2.10A/C97-109[»]
4MZ6X-ray1.88A/C97-109[»]
ProteinModelPortaliP33316.
SMRiP33316. Positions 112-236.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP33316.

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni173 – 1753Substrate binding
Regioni187 – 1904Substrate binding
Regioni246 – 2472Substrate binding

Sequence similaritiesi

Belongs to the dUTPase family.Curated

Keywords - Domaini

Transit peptide

Phylogenomic databases

eggNOGiCOG0756.
GeneTreeiENSGT00390000018390.
KOiK01520.
OMAiMIEDENE.
PhylomeDBiP33316.
TreeFamiTF105416.

Family and domain databases

Gene3Di2.70.40.10. 1 hit.
InterProiIPR029054. dUTPase-like.
IPR008180. dUTPase/dCTP_deaminase.
IPR008181. dUTPase_1.
[Graphical view]
PfamiPF00692. dUTPase. 1 hit.
[Graphical view]
SUPFAMiSSF51283. SSF51283. 1 hit.
TIGRFAMsiTIGR00576. dut. 1 hit.

Sequences (2)i

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

This entry describes 2 isoformsi produced by alternative splicing. Align

Isoform 3 (identifier: P33316-3) [UniParc]FASTAAdd to Basket

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.

« Hide

        10         20         30         40         50
MTPLCPRPAL CYHFLTSLLR SAMQNARGAR QRAEAAVLSG PGPPLGRAAQ
60 70 80 90 100
HGIPRPLSSA GRLSQGCRGA STVGAAGWKG ELPKAGGSPA PGPETPAISP
110 120 130 140 150
SKRARPAEVG GMQLRFARLS EHATAPTRGS ARAAGYDLYS AYDYTIPPME
160 170 180 190 200
KAVVKTDIQI ALPSGCYGRV APRSGLAAKH FIDVGAGVID EDYRGNVGVV
210 220 230 240 250
LFNFGKEKFE VKKGDRIAQL ICERIFYPEI EEVQALDDTE RGSGGFGSTG

KN
Length:252
Mass (Da):26,563
Last modified:September 21, 2011 - v4
Checksum:i8E2EBC9ED5B0FAD2
GO
Isoform 2 (identifier: P33316-2) [UniParc]FASTAAdd to Basket

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.

Show »
Length:164
Mass (Da):17,748
Checksum:iE75BC583BF8C7245
GO

Sequence cautioni

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.

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti175 – 1751G → S in BAF84204. (PubMed:14702039)Curated
Sequence conflicti182 – 1821I → T in BAG60677. (PubMed:14702039)Curated

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti100 – 1001P → S.1 Publication
Corresponds to variant rs28381104 [ dbSNP | Ensembl ].
VAR_022314

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei1 – 9393MTPLC…PAPGP → MPCSE in isoform 2. 6 PublicationsVSP_001324Add
BLAST

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
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.
CCDSiCCDS32231.1. [P33316-3]
CCDS45255.1. [P33316-2]
PIRiA46256.
G02777.
RefSeqiNP_001020419.1. NM_001025248.1. [P33316-3]
NP_001020420.1. NM_001025249.1.
NP_001939.1. NM_001948.3. [P33316-2]
UniGeneiHs.527980.

Genome annotation databases

EnsembliENST00000331200; ENSP00000370376; ENSG00000128951. [P33316-3]
ENST00000455976; ENSP00000405160; ENSG00000128951. [P33316-2]
ENST00000558813; ENSP00000453717; ENSG00000128951.
GeneIDi1854.
KEGGihsa:1854.
UCSCiuc001zws.3. human. [P33316-3]
uc001zww.3. human. [P33316-2]

Polymorphism databases

DMDMi347595814.

Keywords - Coding sequence diversityi

Alternative splicing, Polymorphism

Cross-referencesi

Web resourcesi

NIEHS-SNPs

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
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 .
CCDSi CCDS32231.1. [P33316-3 ]
CCDS45255.1. [P33316-2 ]
PIRi A46256.
G02777.
RefSeqi NP_001020419.1. NM_001025248.1. [P33316-3 ]
NP_001020420.1. NM_001025249.1.
NP_001939.1. NM_001948.3. [P33316-2 ]
UniGenei Hs.527980.

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
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 [» ]
4MZ5 X-ray 2.10 A/C 97-109 [» ]
4MZ6 X-ray 1.88 A/C 97-109 [» ]
ProteinModelPortali P33316.
SMRi P33316. Positions 112-236.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 108187. 14 interactions.
IntActi P33316. 21 interactions.
MINTi MINT-1436411.

Chemistry

BindingDBi P33316.
ChEMBLi CHEMBL5203.

PTM databases

PhosphoSitei P33316.

Polymorphism databases

DMDMi 347595814.

Proteomic databases

MaxQBi P33316.
PaxDbi P33316.
PeptideAtlasi P33316.
PRIDEi P33316.

Protocols and materials databases

DNASUi 1854.
Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENST00000331200 ; ENSP00000370376 ; ENSG00000128951 . [P33316-3 ]
ENST00000455976 ; ENSP00000405160 ; ENSG00000128951 . [P33316-2 ]
ENST00000558813 ; ENSP00000453717 ; ENSG00000128951 .
GeneIDi 1854.
KEGGi hsa:1854.
UCSCi uc001zws.3. human. [P33316-3 ]
uc001zww.3. human. [P33316-2 ]

Organism-specific databases

CTDi 1854.
GeneCardsi GC15P048623.
HGNCi HGNC:3078. DUT.
HPAi HPA054422.
MIMi 601266. gene.
neXtProti NX_P33316.
PharmGKBi PA151.
GenAtlasi Search...

Phylogenomic databases

eggNOGi COG0756.
GeneTreei ENSGT00390000018390.
KOi K01520.
OMAi MIEDENE.
PhylomeDBi P33316.
TreeFami TF105416.

Enzyme and pathway databases

UniPathwayi UPA00610 ; UER00666 .
BioCyci MetaCyc:HS05235-MONOMER.
BRENDAi 3.6.1.23. 2681.
Reactomei REACT_21376. Pyrimidine biosynthesis.
SABIO-RK P33316.

Miscellaneous databases

EvolutionaryTracei P33316.
GeneWikii DUT_(gene).
GenomeRNAii 1854.
NextBioi 7591.
PROi P33316.
SOURCEi Search...

Gene expression databases

Bgeei P33316.
CleanExi HS_DUT.
ExpressionAtlasi P33316. baseline and differential.
Genevestigatori P33316.

Family and domain databases

Gene3Di 2.70.40.10. 1 hit.
InterProi IPR029054. dUTPase-like.
IPR008180. dUTPase/dCTP_deaminase.
IPR008181. dUTPase_1.
[Graphical view ]
Pfami PF00692. dUTPase. 1 hit.
[Graphical view ]
SUPFAMi SSF51283. SSF51283. 1 hit.
TIGRFAMsi TIGR00576. dut. 1 hit.
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  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.
    , 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. 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. 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. 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.

Entry informationi

Entry nameiDUT_HUMAN
AccessioniPrimary (citable) accession number: P33316
Secondary accession number(s): A8K650
, B4DPR5, O14785, Q16708, Q16860, Q6FHN1, Q6NSA3, Q96Q81
Entry historyi
Integrated into UniProtKB/Swiss-Prot: February 1, 1994
Last sequence update: September 21, 2011
Last modified: October 29, 2014
This is version 155 of the entry and version 4 of the sequence. [Complete history]
Entry statusiReviewed (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.

Miscellaneousi

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.

Keywords - Technical termi

3D-structure, Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. Human chromosome 15
    Human chromosome 15: entries, gene names and cross-references to MIM
  2. Human entries with polymorphisms or disease mutations
    List of human entries with polymorphisms or disease mutations
  3. Human polymorphisms and disease mutations
    Index of human polymorphisms and disease mutations
  4. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  5. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  6. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  7. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3