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UniProtKB/Swiss-Prot entry O95989


[Entry info] [Name and origin] [References] [Comments] [Cross-references] [Keywords] [Features] [Sequence] [Tools]

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Entry information
Entry name NUDT3_HUMAN
Primary accession number O95989
Secondary accession numbers None
Integrated into Swiss-Prot on July 5, 2005
Sequence was last modified on May 1, 1999 (Sequence version 1)
Annotations were last modified on    November 4, 2008 (Entry version 71)
Name and origin of the protein
Protein name Diphosphoinositol polyphosphate phosphohydrolase 1
Synonyms DIPP-1
EC 3.6.1.52
Diadenosine 5',5'''-P1,P6-hexaphosphate hydrolase 1
EC 3.6.1.-
Nucleoside diphosphate-linked moiety X motif 3
Nudix motif 3
Gene name
Name: NUDT3
Synonyms: DIPP, DIPP1
From
Homo sapiens (Human) [TaxID: 9606] 
Taxonomy Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae; Homo.
Protein existence 1: Evidence at protein level;
References
[1]
NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, ENZYME ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, TISSUE SPECIFICITY, AND MUTAGENESIS OF GLU-70.
TISSUE=Uterus;
DOI=10.1093/emboj/17.22.6599; PubMed=9822604 [NCBI, ExPASy, EBI, Israel, Japan]
Safrany S.T., Caffrey J.J., Yang X., Bembenek M.E., Moyer M.B., Burkhart W.A., Shears S.B.;
"A novel context for the 'MutT' module, a guardian of cell integrity, in a diphosphoinositol polyphosphate phosphohydrolase.";
EMBO J. 17:6599-6607(1998).
[2]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Kalnine N., Chen X., Rolfs A., Halleck A., Hines L., Eisenstein S., Koundinya M., Raphael J., Moreira D., Kelley T., LaBaer J., Lin Y., Phelan M., Farmer A.;
"Cloning of human full-length CDSs in BD Creator(TM) system donor vector.";
Submitted (OCT-2004) to the EMBL/GenBank/DDBJ databases.
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
DOI=10.1038/nature02055; PubMed=14574404 [NCBI, ExPASy, EBI, Israel, Japan]
Mungall A.J., Palmer S.A., Sims S.K., Edwards C.A., Ashurst J.L., Wilming L., Jones M.C., Horton R., Hunt S.E., Scott C.E., Gilbert J.G.R., Clamp M.E., Bethel G., Milne S., Ainscough R., Almeida J.P., Ambrose K.D., Andrews T.D., Ashwell R.I.S., Babbage A.K., Bagguley C.L., Bailey J., Banerjee R., Barker D.J., Barlow K.F., Bates K., Beare D.M., Beasley H., Beasley O., Bird C.P., Blakey S.E., Bray-Allen S., Brook J., Brown A.J., Brown J.Y., Burford D.C., Burrill W., Burton J., Carder C., Carter N.P., Chapman J.C., Clark S.Y., Clark G., Clee C.M., Clegg S., Cobley V., Collier R.E., Collins J.E., Colman L.K., Corby N.R., Coville G.J., Culley K.M., Dhami P., Davies J., Dunn M., Earthrowl M.E., Ellington A.E., Evans K.A., Faulkner L., Francis M.D., Frankish A., Frankland J., French L., Garner P., Garnett J., Ghori M.J., Gilby L.M., Gillson C.J., Glithero R.J., Grafham D.V., Grant M., Gribble S., Griffiths C., Griffiths M.N.D., Hall R., Halls K.S., Hammond S., Harley J.L., Hart E.A., Heath P.D., Heathcott R., Holmes S.J., Howden P.J., Howe K.L., Howell G.R., Huckle E., Humphray S.J., Humphries M.D., Hunt A.R., Johnson C.M., Joy A.A., Kay M., Keenan S.J., Kimberley A.M., King A., Laird G.K., Langford C., Lawlor S., Leongamornlert D.A., Leversha M., Lloyd C.R., Lloyd D.M., Loveland J.E., Lovell J., Martin S., Mashreghi-Mohammadi M., Maslen G.L., Matthews L., McCann O.T., McLaren S.J., McLay K., McMurray A., Moore M.J.F., Mullikin J.C., Niblett D., Nickerson T., Novik K.L., Oliver K., Overton-Larty E.K., Parker A., Patel R., Pearce A.V., Peck A.I., Phillimore B.J.C.T., Phillips S., Plumb R.W., Porter K.M., Ramsey Y., Ranby S.A., Rice C.M., Ross M.T., Searle S.M., Sehra H.K., Sheridan E., Skuce C.D., Smith S., Smith M., Spraggon L., Squares S.L., Steward C.A., Sycamore N., Tamlyn-Hall G., Tester J., Theaker A.J., Thomas D.W., Thorpe A., Tracey A., Tromans A., Tubby B., Wall M., Wallis J.M., West A.P., White S.S., Whitehead S.L., Whittaker H., Wild A., Willey D.J., Wilmer T.E., Wood J.M., Wray P.W., Wyatt J.C., Young L., Younger R.M., Bentley D.R., Coulson A., Durbin R.M., Hubbard T., Sulston J.E., Dunham I., Rogers J., Beck S.;
"The DNA sequence and analysis of human chromosome 6.";
Nature 425:805-811(2003).
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
TISSUE=Uterus;
DOI=10.1101/gr.2596504; PubMed=15489334 [NCBI, ExPASy, EBI, Israel, Japan]
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).
[5]
ENZYME ACTIVITY, AND BIOPHYSICOCHEMICAL PROPERTIES.
DOI=10.1074/jbc.274.31.21735; PubMed=10419486 [NCBI, ExPASy, EBI, Israel, Japan]
Safrany S.T., Ingram S.W., Cartwright J.L., Falck J.R., McLennan A.G., Barnes L.D., Shears S.B.;
"The diadenosine hexaphosphate hydrolases from Schizosaccharomyces pombe and Saccharomyces cerevisiae are homologues of the human diphosphoinositol polyphosphate phosphohydrolase. Overlapping substrate specificities in a MutT-type protein.";
J. Biol. Chem. 274:21735-21740(1999).
[6]
MUTAGENESIS OF GLY-50; GLY-51; GLY-52; GLU-66; GLY-72; GLY-75; GLY-78; GLY-82; PHE-84 AND HIS-91.
DOI=10.1074/jbc.274.50.35434; PubMed=10585413 [NCBI, ExPASy, EBI, Israel, Japan]
Yang X., Safrany S.T., Shears S.B.;
"Site-directed mutagenesis of diphosphoinositol polyphosphate phosphohydrolase, a dual specificity NUDT enzyme that attacks diadenosine polyphosphates and diphosphoinositol polyphosphates.";
J. Biol. Chem. 274:35434-35440(1999).
[7]
ENZYME ACTIVITY, AND BIOPHYSICOCHEMICAL PROPERTIES.
DOI=10.1074/jbc.M209795200; PubMed=12370170 [NCBI, ExPASy, EBI, Israel, Japan]
Fisher D.I., Safrany S.T., Strike P., McLennan A.G., Cartwright J.L.;
"Nudix hydrolases that degrade dinucleoside and diphosphoinositol polyphosphates also have 5-phosphoribosyl 1-pyrophosphate (PRPP) pyrophosphatase activity that generates the glycolytic activator ribose 1,5-bisphosphate.";
J. Biol. Chem. 277:47313-47317(2002).
Comments
Copyright
Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms. Distributed under the Creative Commons Attribution-NoDerivs License.
Cross-references
Sequence databases
EMBL
AF062529; AAC83224.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AF062530; AAC83225.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
BT019984; AAV38787.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
BT019985; AAV38788.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
Z98036; CAI19715.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AL355855; CAI19715.1; JOINED; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AL355855; CAH72222.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
Z98036; CAH72222.1; JOINED; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
BC007727; AAH07727.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
RefSeq NP_006694.1; -.
UniGene Hs.188882
3D structure databases
PDB
2FVV; X-ray; 1.25 A; A=1-172.[ExPASy / RCSB / EBI]
2Q9P; X-ray; 1.65 A; A=1-172.[ExPASy / RCSB / EBI]
Detailed list of linked structures.
PDBsum 2FVV; -.
2Q9P; -.
ModBase O95989.
Protein-protein interaction databases
IntAct O95989; -.
Organism-specific databases
H-InvDB HIX0005790; -.
HGNC HGNC:8050; NUDT3.
GenAtlas NUDT3.
MIM 609228; gene. [NCBI / EBI]
PharmGKB PA31834; -.
GeneCards O95989.
Gene expression databases
ArrayExpress O95989; -.
CleanEx HS_NUDT3; -.
GermOnline ENSG00000112664; Homo sapiens.
Ontologies
GO
GO:0008486; Molecular function: diphosphoinositol-polyphosphate diphosphatase activity (traceable author statement from ProtInc).
GO:0007267; Biological process: cell-cell signaling (traceable author statement from ProtInc).
GO:0015961; Biological process: diadenosine polyphosphate catabolic process (traceable author statement from ProtInc).
QuickGo view.
Family and domain databases
InterPro IPR000086; NUDIX_hydrolase_core.
Graphical view of domain structure.
Gene3D G3DSA:3.90.79.10; NUDIX_hydrolase; 1.
Pfam PF00293; NUDIX; 1.
Pfam graphical view of domain structure.
PRINTS PR00502; NUDIXFAMILY.
PROSITE PS00893; NUDIX; 1.
BLOCKS O95989.
ProtoNet O95989.
Proteomic databases
PeptideAtlas O95989; -.
Genome annotation databases
Ensembl ENSG00000112664; Homo sapiens. [Contig view]
GeneID 11165; -.
KEGG hsa:11165; -.
Phylogenomic databases
HOGENOM O95989; -.
HOVERGEN O95989; -.
Other
LinkHub O95989; -.
NextBio 42479; -.
SOURCE NUDT3; Homo sapiens.
UniRef View cluster of proteins with at least 50% / 90% / 100% identity.
Keywords
3D-structure; Cytoplasm; Hydrolase; Magnesium; Metal-binding.
Features
SEVIEWER logo Feature table viewer FT aligner logo Feature aligner
KeyFrom   To Length Description FTId
CHAIN   1   172  172     Diphosphoinositol polyphosphate phosphohydrolase 1. PRO_0000057055
MOTIF   51    72  22     Nudix box. 
METAL   66    66        Magnesium (Probable). 
METAL   70    70        Magnesium (Probable). 
SITE   84    84  1     Important for substrate recognition. 
SITE   91    91  1     Important for substrate recognition. 
MUTAGEN   50    50        G->A,V: Loss of function. 
MUTAGEN   51    51        G->A: Loss of function. 
MUTAGEN   52    52        G->A,V: Loss of function. 
MUTAGEN   66    66        E->Q: Loss of function. 
MUTAGEN   70    70        E->Q: Loss of function. 
MUTAGEN   72    72        G->A: Loss of function. 
MUTAGEN   75    75        G->A: Loss of function. 
MUTAGEN   78    78        G->A: No effect. 
MUTAGEN   78    78        G->V: Loss of function. 
MUTAGEN   82    82        G->A: Loss of function. 
MUTAGEN   84    84        F->Y: Induces a strong decrease in Ap6A and [PP]-InsP4 hydrolysis, while it only weakly affects PP-InsP5 hydrolysis. 
MUTAGEN   91    91        H->L: Induces a strong decrease in Ap6A and [PP]-InsP4 hydrolysis, while it only weakly affects PP-InsP5 hydrolysis. 
STRAND   18    28  11      
STRAND   33    38  6      
STRAND   45    47  3      
STRAND   50    52  3      
HELIX   59    71  13      
STRAND   73    86  14      
TURN   87    90  4      
STRAND   91   103  13      
HELIX   108   113  6      
STRAND   117   121  5      
HELIX   122   129  8      
TURN   130   132  3      
HELIX   134   138  5      
Sequence information
Length: 172 AA [This is the length of the unprocessed precursor] Molecular weight: 19471 Da [This is the MW of the unprocessed precursor] CRC64: DE823FECF5C6438A [This is a checksum on the sequence]
        10         20         30         40         50         60 
MMKLKSNQTR TYDGDGYKKR AACLCFRSES EEEVLLVSSS RHPDRWIVPG GGMEPEEEPS 

        70         80         90        100        110        120 
VAAVREVCEE AGVKGTLGRL VGIFENQERK HRTYVYVLIV TEVLEDWEDS VNIGRKREWF 

       130        140        150        160        170 
KIEDAIKVLQ YHKPVQASYF ETLRQGYSAN NGTPVVATTY SVSAQSSMSG IR 

O95989 in FASTA format

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