Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Protein

Diphosphoinositol polyphosphate phosphohydrolase 1

Gene

NUDT3

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

Functioni

Cleaves a beta-phosphate from the diphosphate groups in PP-InsP5 (diphosphoinositol pentakisphosphate) and [PP]2-InsP4 (bisdiphosphoinositol tetrakisphosphate), suggesting that it may play a role in signal transduction. InsP6 (inositol hexakisphophate) is not a substrate. Acts as a negative regulator of the ERK1/2 pathway. Also able to catalyze the hydrolysis of dinucleoside oligophosphates, with Ap6A and Ap5A being the preferred substrates. The major reaction products are ADP and p4a from Ap6A and ADP and ATP from Ap5A. Also able to hydrolyze 5-phosphoribose 1-diphosphate.1 Publication

Catalytic activityi

Diphospho-myo-inositol polyphosphate + H2O = myo-inositol polyphosphate + phosphate.3 Publications

Cofactori

Mg2+1 PublicationNote: Binds 3 Mg2+ ions per subunit.1 Publication

Enzyme regulationi

Inhibited by fluoride and InsP6.1 Publication

Kineticsi

  1. KM=5.9 µM for Ap6A3 Publications
  2. KM=7.7 µM for Ap5A3 Publications
  3. KM=38 mM for 5-phosphoribose 1-diphosphate3 Publications
  4. KM=4.2 nM for PP-InsP53 Publications

    pH dependencei

    Optimum pH is 7-7.5.3 Publications

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Binding sitei10 – 101Substrate
    Binding sitei41 – 411Substrate
    Metal bindingi50 – 501Magnesium 1; via carbonyl oxygen
    Metal bindingi66 – 661Magnesium 2
    Metal bindingi66 – 661Magnesium 3
    Active sitei69 – 691Proton acceptorCurated
    Metal bindingi70 – 701Magnesium 1

    GO - Molecular functioni

    GO - Biological processi

    • cell-cell signaling Source: ProtInc
    • diadenosine polyphosphate catabolic process Source: ProtInc
    • diphosphoinositol polyphosphate catabolic process Source: UniProtKB
    • inositol phosphate metabolic process Source: Reactome
    • small molecule metabolic process Source: Reactome
    Complete GO annotation...

    Keywords - Molecular functioni

    Hydrolase

    Keywords - Ligandi

    Magnesium, Metal-binding

    Enzyme and pathway databases

    BioCyciMetaCyc:HS03602-MONOMER.
    BRENDAi3.6.1.60. 2681.
    ReactomeiREACT_150188. Synthesis of pyrophosphates in the cytosol.
    SABIO-RKO95989.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Diphosphoinositol polyphosphate phosphohydrolase 1 (EC:3.6.1.52)
    Short name:
    DIPP-1
    Alternative name(s):
    Diadenosine 5',5'''-P1,P6-hexaphosphate hydrolase 1 (EC:3.6.1.-)
    Nucleoside diphosphate-linked moiety X motif 3
    Short name:
    Nudix motif 3
    Gene namesi
    Name:NUDT3
    Synonyms:DIPP, DIPP1
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640 Componenti: Chromosome 6

    Organism-specific databases

    HGNCiHGNC:8050. NUDT3.

    Subcellular locationi

    GO - Cellular componenti

    • cytosol Source: Reactome
    • extracellular exosome Source: UniProtKB
    Complete GO annotation...

    Keywords - Cellular componenti

    Cytoplasm

    Pathology & Biotechi

    Mutagenesis

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Mutagenesisi50 – 501G → A or V: Loss of function. 1 Publication
    Mutagenesisi51 – 511G → A: Loss of function. 1 Publication
    Mutagenesisi52 – 521G → A or V: Loss of function. 1 Publication
    Mutagenesisi66 – 661E → Q: Loss of function. 1 Publication
    Mutagenesisi70 – 701E → Q: Loss of function. 1 Publication
    Mutagenesisi72 – 721G → A: Loss of function. 1 Publication
    Mutagenesisi75 – 751G → A: Loss of function. 1 Publication
    Mutagenesisi78 – 781G → A: No effect. 1 Publication
    Mutagenesisi78 – 781G → V: Loss of function. 1 Publication
    Mutagenesisi82 – 821G → A: Loss of function. 1 Publication
    Mutagenesisi84 – 841F → Y: Induces a strong decrease in Ap6A and [PP]-InsP4 hydrolysis, while it only weakly affects PP-InsP5 hydrolysis. 1 Publication
    Mutagenesisi91 – 911H → L: Induces a strong decrease in Ap6A and [PP]-InsP4 hydrolysis, while it only weakly affects PP-InsP5 hydrolysis. 1 Publication

    Organism-specific databases

    PharmGKBiPA31834.

    Polymorphism and mutation databases

    BioMutaiNUDT3.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 172172Diphosphoinositol polyphosphate phosphohydrolase 1PRO_0000057055Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei1 – 11N-acetylmethionine1 Publication

    Keywords - PTMi

    Acetylation

    Proteomic databases

    MaxQBiO95989.
    PaxDbiO95989.
    PeptideAtlasiO95989.
    PRIDEiO95989.

    PTM databases

    PhosphoSiteiO95989.

    Expressioni

    Tissue specificityi

    Widely expressed. Expressed at higher level in brain, heart, pancreas and liver. Also expressed in placenta, lung and kidney.1 Publication

    Gene expression databases

    BgeeiO95989.
    CleanExiHS_NUDT3.
    GenevisibleiO95989. HS.

    Organism-specific databases

    HPAiHPA047027.
    HPA055953.

    Interactioni

    Subunit structurei

    Monomer.By similarity

    Protein-protein interaction databases

    BioGridi116336. 41 interactions.
    IntActiO95989. 38 interactions.
    MINTiMINT-1412881.
    STRINGi9606.ENSP00000351650.

    Structurei

    Secondary structure

    1
    172
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Beta strandi18 – 2811Combined sources
    Beta strandi33 – 386Combined sources
    Beta strandi45 – 473Combined sources
    Beta strandi49 – 524Combined sources
    Helixi59 – 7113Combined sources
    Beta strandi73 – 8614Combined sources
    Turni87 – 904Combined sources
    Beta strandi91 – 10313Combined sources
    Helixi108 – 1136Combined sources
    Beta strandi117 – 1215Combined sources
    Helixi122 – 1298Combined sources
    Turni130 – 1323Combined sources
    Helixi134 – 1396Combined sources

    3D structure databases

    Select the link destinations:
    PDBei
    RCSB PDBi
    PDBji
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    2FVVX-ray1.25A1-172[»]
    2Q9PX-ray1.65A1-172[»]
    ProteinModelPortaliO95989.
    SMRiO95989. Positions 8-142.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiO95989.

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini17 – 142126Nudix hydrolasePROSITE-ProRule annotationAdd
    BLAST

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni18 – 203Substrate binding
    Regioni89 – 913Substrate binding

    Motif

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Motifi51 – 7222Nudix boxAdd
    BLAST

    Sequence similaritiesi

    Belongs to the Nudix hydrolase family. DIPP subfamily.Curated
    Contains 1 nudix hydrolase domain.PROSITE-ProRule annotation

    Phylogenomic databases

    eggNOGiNOG250169.
    GeneTreeiENSGT00390000012928.
    HOGENOMiHOG000237336.
    HOVERGENiHBG053341.
    InParanoidiO95989.
    KOiK07766.
    OMAiLQESCLT.
    OrthoDBiEOG7T7GVQ.
    PhylomeDBiO95989.
    TreeFamiTF106349.

    Family and domain databases

    Gene3Di3.90.79.10. 1 hit.
    InterProiIPR020084. NUDIX_hydrolase_CS.
    IPR000086. NUDIX_hydrolase_dom.
    IPR015797. NUDIX_hydrolase_dom-like.
    [Graphical view]
    PfamiPF00293. NUDIX. 1 hit.
    [Graphical view]
    SUPFAMiSSF55811. SSF55811. 1 hit.
    PROSITEiPS51462. NUDIX. 1 hit.
    PS00893. NUDIX_BOX. 1 hit.
    [Graphical view]

    Sequencei

    Sequence statusi: Complete.

    O95989-1 [UniParc]FASTAAdd to basket

    « Hide

            10         20         30         40         50
    MMKLKSNQTR TYDGDGYKKR AACLCFRSES EEEVLLVSSS RHPDRWIVPG
    60 70 80 90 100
    GGMEPEEEPS VAAVREVCEE AGVKGTLGRL VGIFENQERK HRTYVYVLIV
    110 120 130 140 150
    TEVLEDWEDS VNIGRKREWF KIEDAIKVLQ YHKPVQASYF ETLRQGYSAN
    160 170
    NGTPVVATTY SVSAQSSMSG IR
    Length:172
    Mass (Da):19,471
    Last modified:May 1, 1999 - v1
    Checksum:iDE823FECF5C6438A
    GO

    Sequence databases

    Select the link destinations:
    EMBLi
    GenBanki
    DDBJi
    Links Updated
    AF062529 mRNA. Translation: AAC83224.1.
    AF062530 mRNA. Translation: AAC83225.1.
    BT019984 mRNA. Translation: AAV38787.1.
    BT019985 mRNA. Translation: AAV38788.1.
    AK313440 mRNA. Translation: BAG36231.1.
    Z98036, AL355855 Genomic DNA. Translation: CAI19715.1.
    AL355855, Z98036 Genomic DNA. Translation: CAH72222.1.
    CH471081 Genomic DNA. Translation: EAX03781.1.
    BC007727 mRNA. Translation: AAH07727.1.
    CCDSiCCDS4791.1.
    RefSeqiNP_006694.1. NM_006703.3.
    UniGeneiHs.188882.

    Genome annotation databases

    EnsembliENST00000607016; ENSP00000476119; ENSG00000272325.
    GeneIDi11165.
    KEGGihsa:11165.
    UCSCiuc003ojl.3. human.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBLi
    GenBanki
    DDBJi
    Links Updated
    AF062529 mRNA. Translation: AAC83224.1.
    AF062530 mRNA. Translation: AAC83225.1.
    BT019984 mRNA. Translation: AAV38787.1.
    BT019985 mRNA. Translation: AAV38788.1.
    AK313440 mRNA. Translation: BAG36231.1.
    Z98036, AL355855 Genomic DNA. Translation: CAI19715.1.
    AL355855, Z98036 Genomic DNA. Translation: CAH72222.1.
    CH471081 Genomic DNA. Translation: EAX03781.1.
    BC007727 mRNA. Translation: AAH07727.1.
    CCDSiCCDS4791.1.
    RefSeqiNP_006694.1. NM_006703.3.
    UniGeneiHs.188882.

    3D structure databases

    Select the link destinations:
    PDBei
    RCSB PDBi
    PDBji
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    2FVVX-ray1.25A1-172[»]
    2Q9PX-ray1.65A1-172[»]
    ProteinModelPortaliO95989.
    SMRiO95989. Positions 8-142.
    ModBaseiSearch...
    MobiDBiSearch...

    Protein-protein interaction databases

    BioGridi116336. 41 interactions.
    IntActiO95989. 38 interactions.
    MINTiMINT-1412881.
    STRINGi9606.ENSP00000351650.

    PTM databases

    PhosphoSiteiO95989.

    Polymorphism and mutation databases

    BioMutaiNUDT3.

    Proteomic databases

    MaxQBiO95989.
    PaxDbiO95989.
    PeptideAtlasiO95989.
    PRIDEiO95989.

    Protocols and materials databases

    DNASUi11165.
    Structural Biology KnowledgebaseSearch...

    Genome annotation databases

    EnsembliENST00000607016; ENSP00000476119; ENSG00000272325.
    GeneIDi11165.
    KEGGihsa:11165.
    UCSCiuc003ojl.3. human.

    Organism-specific databases

    CTDi11165.
    GeneCardsiGC06M035727.
    HGNCiHGNC:8050. NUDT3.
    HPAiHPA047027.
    HPA055953.
    MIMi609228. gene.
    neXtProtiNX_O95989.
    PharmGKBiPA31834.
    GenAtlasiSearch...

    Phylogenomic databases

    eggNOGiNOG250169.
    GeneTreeiENSGT00390000012928.
    HOGENOMiHOG000237336.
    HOVERGENiHBG053341.
    InParanoidiO95989.
    KOiK07766.
    OMAiLQESCLT.
    OrthoDBiEOG7T7GVQ.
    PhylomeDBiO95989.
    TreeFamiTF106349.

    Enzyme and pathway databases

    BioCyciMetaCyc:HS03602-MONOMER.
    BRENDAi3.6.1.60. 2681.
    ReactomeiREACT_150188. Synthesis of pyrophosphates in the cytosol.
    SABIO-RKO95989.

    Miscellaneous databases

    ChiTaRSiNUDT3. human.
    EvolutionaryTraceiO95989.
    GeneWikiiNUDT3.
    GenomeRNAii11165.
    NextBioi42479.
    PROiO95989.
    SOURCEiSearch...

    Gene expression databases

    BgeeiO95989.
    CleanExiHS_NUDT3.
    GenevisibleiO95989. HS.

    Family and domain databases

    Gene3Di3.90.79.10. 1 hit.
    InterProiIPR020084. NUDIX_hydrolase_CS.
    IPR000086. NUDIX_hydrolase_dom.
    IPR015797. NUDIX_hydrolase_dom-like.
    [Graphical view]
    PfamiPF00293. NUDIX. 1 hit.
    [Graphical view]
    SUPFAMiSSF55811. SSF55811. 1 hit.
    PROSITEiPS51462. NUDIX. 1 hit.
    PS00893. NUDIX_BOX. 1 hit.
    [Graphical view]
    ProtoNetiSearch...

    Publicationsi

    « Hide 'large scale' publications
    1. "A novel context for the 'MutT' module, a guardian of cell integrity, in a diphosphoinositol polyphosphate phosphohydrolase."
      Safrany S.T., Caffrey J.J., Yang X., Bembenek M.E., Moyer M.B., Burkhart W.A., Shears S.B.
      EMBO J. 17:6599-6607(1998) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, ENZYME ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, TISSUE SPECIFICITY, MUTAGENESIS OF GLU-70.
      Tissue: Uterus.
    2. "Cloning of human full-length CDSs in BD Creator(TM) system donor vector."
      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.
      Submitted (OCT-2004) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    3. "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].
      Tissue: Amygdala.
    4. "The DNA sequence and analysis of human chromosome 6."
      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.
      Nature 425:805-811(2003) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    5. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    6. "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].
      Tissue: Uterus.
    7. "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."
      Safrany S.T., Ingram S.W., Cartwright J.L., Falck J.R., McLennan A.G., Barnes L.D., Shears S.B.
      J. Biol. Chem. 274:21735-21740(1999) [PubMed] [Europe PMC] [Abstract]
      Cited for: ENZYME ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES.
    8. "Site-directed mutagenesis of diphosphoinositol polyphosphate phosphohydrolase, a dual specificity NUDT enzyme that attacks diadenosine polyphosphates and diphosphoinositol polyphosphates."
      Yang X., Safrany S.T., Shears S.B.
      J. Biol. Chem. 274:35434-35440(1999) [PubMed] [Europe PMC] [Abstract]
      Cited for: MUTAGENESIS OF GLY-50; GLY-51; GLY-52; GLU-66; GLY-72; GLY-75; GLY-78; GLY-82; PHE-84 AND HIS-91.
    9. "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."
      Fisher D.I., Safrany S.T., Strike P., McLennan A.G., Cartwright J.L.
      J. Biol. Chem. 277:47313-47317(2002) [PubMed] [Europe PMC] [Abstract]
      Cited for: ENZYME ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES.
    10. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    11. Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT MET-1, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    12. "Crystal structure of human diphosphoinositol phosphatase 1."
      Thorsell A.G., Persson C., Graslund S., Hammarstrom M., Busam R.D., Hallberg B.M.
      Proteins 77:242-246(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (1.25 ANGSTROMS) IN COMPLEX WITH MAGNESIUM IONS; FLUORIDE AND INOSITOL HEXAKISPHOSPHATE, COFACTOR, ENZYME REGULATION.

    Entry informationi

    Entry nameiNUDT3_HUMAN
    AccessioniPrimary (citable) accession number: O95989
    Secondary accession number(s): B2R8N4
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: July 5, 2005
    Last sequence update: May 1, 1999
    Last modified: June 24, 2015
    This is version 140 of the entry and version 1 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

    Keywords - Technical termi

    3D-structure, Complete proteome, Reference proteome

    Documents

    1. Human chromosome 6
      Human chromosome 6: entries, gene names and cross-references to MIM
    2. MIM cross-references
      Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
    3. PDB cross-references
      Index of Protein Data Bank (PDB) cross-references
    4. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3

    Similar proteinsi

    Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
    100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into Uniref entry.
    90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
    50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.