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O95989

- NUDT3_HUMAN

UniProt

O95989 - NUDT3_HUMAN

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Protein

Diphosphoinositol polyphosphate phosphohydrolase 1

Gene

NUDT3

Organism
Homo sapiens (Human)
Status
Reviewed - 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

Binds 3 magnesium 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

  1. diphosphoinositol-polyphosphate diphosphatase activity Source: UniProtKB
  2. inositol-1,5-bisdiphosphate-2,3,4,6-tetrakisphosphate 1-diphosphatase activity Source: UniProtKB-EC
  3. inositol-1,5-bisdiphosphate-2,3,4,6-tetrakisphosphate 5-diphosphatase activity Source: UniProtKB-EC
  4. inositol-1-diphosphate-2,3,4,5,6-pentakisphosphate diphosphatase activity Source: UniProtKB-EC
  5. inositol-3,5-bisdiphosphate-2,3,4,6-tetrakisphosphate 5-diphosphatase activity Source: UniProtKB-EC
  6. inositol-3-diphosphate-1,2,4,5,6-pentakisphosphate diphosphatase activity Source: UniProtKB-EC
  7. inositol-5-diphosphate-1,2,3,4,6-pentakisphosphate diphosphatase activity Source: UniProtKB-EC
  8. inositol diphosphate tetrakisphosphate diphosphatase activity Source: UniProtKB-EC
  9. magnesium ion binding Source: UniProtKB

GO - Biological processi

  1. cell-cell signaling Source: ProtInc
  2. diadenosine polyphosphate catabolic process Source: ProtInc
  3. diphosphoinositol polyphosphate catabolic process Source: UniProtKB
  4. inositol phosphate metabolic process Source: Reactome
  5. 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.
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: Chromosome 6

Organism-specific databases

HGNCiHGNC:8050. NUDT3.

Subcellular locationi

Cytoplasm Curated

GO - Cellular componenti

  1. cytosol Source: Reactome
  2. extracellular vesicular exosome Source: UniProt
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.

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.
GenevestigatoriO95989.

Organism-specific databases

HPAiHPA047027.
HPA055953.

Interactioni

Subunit structurei

Monomer.By similarity

Protein-protein interaction databases

BioGridi116336. 39 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 – 2811
Beta strandi33 – 386
Beta strandi45 – 473
Beta strandi49 – 524
Helixi59 – 7113
Beta strandi73 – 8614
Turni87 – 904
Beta strandi91 – 10313
Helixi108 – 1136
Beta strandi117 – 1215
Helixi122 – 1298
Turni130 – 1323
Helixi134 – 1396

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
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.
OMAiFLHIRIT.
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:
EMBL
GenBank
DDBJ
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:
EMBL
GenBank
DDBJ
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 .
CCDSi CCDS4791.1.
RefSeqi NP_006694.1. NM_006703.3.
UniGenei Hs.188882.

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
2FVV X-ray 1.25 A 1-172 [» ]
2Q9P X-ray 1.65 A 1-172 [» ]
ProteinModelPortali O95989.
SMRi O95989. Positions 8-142.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 116336. 39 interactions.
IntActi O95989. 38 interactions.
MINTi MINT-1412881.
STRINGi 9606.ENSP00000351650.

PTM databases

PhosphoSitei O95989.

Proteomic databases

MaxQBi O95989.
PaxDbi O95989.
PeptideAtlasi O95989.
PRIDEi O95989.

Protocols and materials databases

DNASUi 11165.
Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENST00000607016 ; ENSP00000476119 ; ENSG00000272325 .
GeneIDi 11165.
KEGGi hsa:11165.
UCSCi uc003ojl.3. human.

Organism-specific databases

CTDi 11165.
GeneCardsi GC06M035727.
HGNCi HGNC:8050. NUDT3.
HPAi HPA047027.
HPA055953.
MIMi 609228. gene.
neXtProti NX_O95989.
PharmGKBi PA31834.
GenAtlasi Search...

Phylogenomic databases

eggNOGi NOG250169.
GeneTreei ENSGT00390000012928.
HOGENOMi HOG000237336.
HOVERGENi HBG053341.
InParanoidi O95989.
KOi K07766.
OMAi FLHIRIT.
OrthoDBi EOG7T7GVQ.
PhylomeDBi O95989.
TreeFami TF106349.

Enzyme and pathway databases

BioCyci MetaCyc:HS03602-MONOMER.
Reactomei REACT_150188. Synthesis of pyrophosphates in the cytosol.
SABIO-RK O95989.

Miscellaneous databases

ChiTaRSi NUDT3. human.
EvolutionaryTracei O95989.
GeneWikii NUDT3.
GenomeRNAii 11165.
NextBioi 42479.
PROi O95989.
SOURCEi Search...

Gene expression databases

Bgeei O95989.
CleanExi HS_NUDT3.
Genevestigatori O95989.

Family and domain databases

Gene3Di 3.90.79.10. 1 hit.
InterProi IPR020084. NUDIX_hydrolase_CS.
IPR000086. NUDIX_hydrolase_dom.
IPR015797. NUDIX_hydrolase_dom-like.
[Graphical view ]
Pfami PF00293. NUDIX. 1 hit.
[Graphical view ]
SUPFAMi SSF55811. SSF55811. 1 hit.
PROSITEi PS51462. NUDIX. 1 hit.
PS00893. NUDIX_BOX. 1 hit.
[Graphical view ]
ProtoNeti Search...

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: October 29, 2014
This is version 133 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