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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

  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: 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.

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. 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.

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.
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.
GenevestigatoriO95989.

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: March 4, 2015
This is version 136 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.