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Q96G61

- NUD11_HUMAN

UniProt

Q96G61 - NUD11_HUMAN

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Protein

Diphosphoinositol polyphosphate phosphohydrolase 3-beta

Gene

NUDT11

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), suggesting that it may play a role in signal transduction. 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.

Catalytic activityi

Diphospho-myo-inositol polyphosphate + H2O = myo-inositol polyphosphate + phosphate.
P1,P(6)-bis(5'-adenosyl)hexaphosphate + H2O = adenosine 5'-pentaphosphate + AMP.
P1,P(5)-bis(5'-adenosyl)pentaphosphate + H2O = adenosine 5'-tetraphosphate + AMP.

Cofactori

Mg2+By similarity1 Publication, Mn2+By similarity1 PublicationNote: Binds 3 Mg(2+) or Mn(2+) ions per subunit. Mn(2+) may be the true cofactor in vivo.By similarity1 Publication

Kineticsi

  1. KM=0.053 µM for PP-InsP52 Publications
  2. KM=13 µM for Ap6A2 Publications
  3. KM=37 µM for Ap5A2 Publications

pH dependencei

Optimum pH is 8.5.2 Publications

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei9 – 91SubstrateBy similarity
Binding sitei40 – 401SubstrateBy similarity
Metal bindingi49 – 491Magnesium 1; via carbonyl oxygenBy similarity
Metal bindingi65 – 651Magnesium 2By similarity
Metal bindingi65 – 651Magnesium 3By similarity
Active sitei68 – 681Proton acceptorBy similarity
Metal bindingi69 – 691Magnesium 1By similarity

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. metal ion binding Source: UniProtKB-KW

GO - Biological processi

  1. inositol phosphate metabolic process Source: Reactome
  2. small molecule metabolic process Source: Reactome
Complete GO annotation...

Keywords - Molecular functioni

Hydrolase

Keywords - Ligandi

Magnesium, Manganese, Metal-binding

Enzyme and pathway databases

BioCyciMetaCyc:HS05381-MONOMER.
BRENDAi3.6.1.52. 2681.
ReactomeiREACT_150188. Synthesis of pyrophosphates in the cytosol.

Names & Taxonomyi

Protein namesi
Recommended name:
Diphosphoinositol polyphosphate phosphohydrolase 3-beta (EC:3.6.1.52)
Short name:
DIPP-3-beta
Short name:
DIPP3-beta
Short name:
hDIPP3beta
Alternative name(s):
Diadenosine 5',5'''-P1,P6-hexaphosphate hydrolase 3-beta
Diadenosine hexaphosphate hydrolase (AMP-forming) (EC:3.6.1.60)
Nucleoside diphosphate-linked moiety X motif 11
Short name:
Nudix motif 11
hAps1
Gene namesi
Name:NUDT11
Synonyms:APS1, DIPP3B
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640: Chromosome X

Organism-specific databases

HGNCiHGNC:18011. NUDT11.

Subcellular locationi

Cytoplasm 1 Publication

GO - Cellular componenti

  1. cytosol Source: Reactome
  2. intracellular Source: LIFEdb
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm

Pathology & Biotechi

Organism-specific databases

PharmGKBiPA31832.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 164164Diphosphoinositol polyphosphate phosphohydrolase 3-betaPRO_0000057065Add
BLAST

Proteomic databases

MaxQBiQ96G61.
PaxDbiQ96G61.
PRIDEiQ96G61.

PTM databases

PhosphoSiteiQ96G61.

Expressioni

Tissue specificityi

Mainly expressed in testis and, at lower level in brain. According to PubMed:12121577, it is also expressed in pancreas and weakly expressed in thymus, prostate, ovary, lung, small intestine and heart.2 Publications

Gene expression databases

BgeeiQ96G61.
CleanExiHS_NUDT11.
GenevestigatoriQ96G61.

Interactioni

Protein-protein interaction databases

BioGridi120487. 1 interaction.
MINTiMINT-3053121.
STRINGi9606.ENSP00000365160.

Structurei

3D structure databases

ProteinModelPortaliQ96G61.
SMRiQ96G61. Positions 17-144.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini17 – 144128Nudix hydrolasePROSITE-ProRule annotationAdd
BLAST

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni17 – 193Substrate bindingBy similarity
Regioni89 – 913Substrate bindingBy similarity

Motif

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Motifi50 – 7122Nudix 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.
InParanoidiQ96G61.
KOiK07766.
OMAiCICVRSE.
OrthoDBiEOG7T7GVQ.
PhylomeDBiQ96G61.
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.

Q96G61-1 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
MKCKPNQTRT YDPEGFKKRA ACLCFRSERE DEVLLVSSSR YPDRWIVPGG
60 70 80 90 100
GMEPEEEPGG AAVREVYEEA GVKGKLGRLL GVFEQNQDRK HRTYVYVLTV
110 120 130 140 150
TELLEDWEDS VSIGRKREWF KVEDAIKVLQ CHKPVHAEYL EKLKLGGSPT
160
NGNSMAPSSP DSDP
Length:164
Mass (Da):18,559
Last modified:December 1, 2001 - v1
Checksum:i8E7F342C8A38872F
GO

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti39 – 391S → N.2 Publications
VAR_022738

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AK001490 mRNA. Translation: BAA91720.1.
AL158055 Genomic DNA. Translation: CAI40294.1.
BC009942 mRNA. Translation: AAH09942.1.
CCDSiCCDS43952.1.
RefSeqiNP_060629.2. NM_018159.3.
UniGeneiHs.200016.

Genome annotation databases

EnsembliENST00000375992; ENSP00000365160; ENSG00000196368.
GeneIDi55190.
KEGGihsa:55190.
UCSCiuc010njt.3. human.

Polymorphism databases

DMDMi68565927.

Keywords - Coding sequence diversityi

Polymorphism

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AK001490 mRNA. Translation: BAA91720.1 .
AL158055 Genomic DNA. Translation: CAI40294.1 .
BC009942 mRNA. Translation: AAH09942.1 .
CCDSi CCDS43952.1.
RefSeqi NP_060629.2. NM_018159.3.
UniGenei Hs.200016.

3D structure databases

ProteinModelPortali Q96G61.
SMRi Q96G61. Positions 17-144.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 120487. 1 interaction.
MINTi MINT-3053121.
STRINGi 9606.ENSP00000365160.

PTM databases

PhosphoSitei Q96G61.

Polymorphism databases

DMDMi 68565927.

Proteomic databases

MaxQBi Q96G61.
PaxDbi Q96G61.
PRIDEi Q96G61.

Protocols and materials databases

DNASUi 55190.
Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENST00000375992 ; ENSP00000365160 ; ENSG00000196368 .
GeneIDi 55190.
KEGGi hsa:55190.
UCSCi uc010njt.3. human.

Organism-specific databases

CTDi 55190.
GeneCardsi GC0XM051232.
HGNCi HGNC:18011. NUDT11.
MIMi 300528. gene.
neXtProti NX_Q96G61.
PharmGKBi PA31832.
GenAtlasi Search...

Phylogenomic databases

eggNOGi NOG250169.
GeneTreei ENSGT00390000012928.
HOGENOMi HOG000237336.
HOVERGENi HBG053341.
InParanoidi Q96G61.
KOi K07766.
OMAi CICVRSE.
OrthoDBi EOG7T7GVQ.
PhylomeDBi Q96G61.
TreeFami TF106349.

Enzyme and pathway databases

BioCyci MetaCyc:HS05381-MONOMER.
BRENDAi 3.6.1.52. 2681.
Reactomei REACT_150188. Synthesis of pyrophosphates in the cytosol.

Miscellaneous databases

GeneWikii NUDT11.
GenomeRNAii 55190.
NextBioi 59039.
PROi Q96G61.
SOURCEi Search...

Gene expression databases

Bgeei Q96G61.
CleanExi HS_NUDT11.
Genevestigatori Q96G61.

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. "An adjacent pair of human NUDT genes on chromosome X are preferentially expressed in testis and encode two new isoforms of diphosphoinositol polyphosphate phosphohydrolase."
    Hidaka K., Caffrey J.J., Hua L., Zhang T., Falck J.R., Nickel G.C., Carrel L., Barnes L.D., Shears S.B.
    J. Biol. Chem. 277:32730-32738(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA], CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, TISSUE SPECIFICITY.
  2. "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], VARIANT ASN-39.
  3. "The DNA sequence of the human X chromosome."
    Ross M.T., Grafham D.V., Coffey A.J., Scherer S., McLay K., Muzny D., Platzer M., Howell G.R., Burrows C., Bird C.P., Frankish A., Lovell F.L., Howe K.L., Ashurst J.L., Fulton R.S., Sudbrak R., Wen G., Jones M.C.
    , Hurles M.E., Andrews T.D., Scott C.E., Searle S., Ramser J., Whittaker A., Deadman R., Carter N.P., Hunt S.E., Chen R., Cree A., Gunaratne P., Havlak P., Hodgson A., Metzker M.L., Richards S., Scott G., Steffen D., Sodergren E., Wheeler D.A., Worley K.C., Ainscough R., Ambrose K.D., Ansari-Lari M.A., Aradhya S., Ashwell R.I., Babbage A.K., Bagguley C.L., Ballabio A., Banerjee R., Barker G.E., Barlow K.F., Barrett I.P., Bates K.N., Beare D.M., Beasley H., Beasley O., Beck A., Bethel G., Blechschmidt K., Brady N., Bray-Allen S., Bridgeman A.M., Brown A.J., Brown M.J., Bonnin D., Bruford E.A., Buhay C., Burch P., Burford D., Burgess J., Burrill W., Burton J., Bye J.M., Carder C., Carrel L., Chako J., Chapman J.C., Chavez D., Chen E., Chen G., Chen Y., Chen Z., Chinault C., Ciccodicola A., Clark S.Y., Clarke G., Clee C.M., Clegg S., Clerc-Blankenburg K., Clifford K., Cobley V., Cole C.G., Conquer J.S., Corby N., Connor R.E., David R., Davies J., Davis C., Davis J., Delgado O., Deshazo D., Dhami P., Ding Y., Dinh H., Dodsworth S., Draper H., Dugan-Rocha S., Dunham A., Dunn M., Durbin K.J., Dutta I., Eades T., Ellwood M., Emery-Cohen A., Errington H., Evans K.L., Faulkner L., Francis F., Frankland J., Fraser A.E., Galgoczy P., Gilbert J., Gill R., Gloeckner G., Gregory S.G., Gribble S., Griffiths C., Grocock R., Gu Y., Gwilliam R., Hamilton C., Hart E.A., Hawes A., Heath P.D., Heitmann K., Hennig S., Hernandez J., Hinzmann B., Ho S., Hoffs M., Howden P.J., Huckle E.J., Hume J., Hunt P.J., Hunt A.R., Isherwood J., Jacob L., Johnson D., Jones S., de Jong P.J., Joseph S.S., Keenan S., Kelly S., Kershaw J.K., Khan Z., Kioschis P., Klages S., Knights A.J., Kosiura A., Kovar-Smith C., Laird G.K., Langford C., Lawlor S., Leversha M., Lewis L., Liu W., Lloyd C., Lloyd D.M., Loulseged H., Loveland J.E., Lovell J.D., Lozado R., Lu J., Lyne R., Ma J., Maheshwari M., Matthews L.H., McDowall J., McLaren S., McMurray A., Meidl P., Meitinger T., Milne S., Miner G., Mistry S.L., Morgan M., Morris S., Mueller I., Mullikin J.C., Nguyen N., Nordsiek G., Nyakatura G., O'dell C.N., Okwuonu G., Palmer S., Pandian R., Parker D., Parrish J., Pasternak S., Patel D., Pearce A.V., Pearson D.M., Pelan S.E., Perez L., Porter K.M., Ramsey Y., Reichwald K., Rhodes S., Ridler K.A., Schlessinger D., Schueler M.G., Sehra H.K., Shaw-Smith C., Shen H., Sheridan E.M., Shownkeen R., Skuce C.D., Smith M.L., Sotheran E.C., Steingruber H.E., Steward C.A., Storey R., Swann R.M., Swarbreck D., Tabor P.E., Taudien S., Taylor T., Teague B., Thomas K., Thorpe A., Timms K., Tracey A., Trevanion S., Tromans A.C., d'Urso M., Verduzco D., Villasana D., Waldron L., Wall M., Wang Q., Warren J., Warry G.L., Wei X., West A., Whitehead S.L., Whiteley M.N., Wilkinson J.E., Willey D.L., Williams G., Williams L., Williamson A., Williamson H., Wilming L., Woodmansey R.L., Wray P.W., Yen J., Zhang J., Zhou J., Zoghbi H., Zorilla S., Buck D., Reinhardt R., Poustka A., Rosenthal A., Lehrach H., Meindl A., Minx P.J., Hillier L.W., Willard H.F., Wilson R.K., Waterston R.H., Rice C.M., Vaudin M., Coulson A., Nelson D.L., Weinstock G., Sulston J.E., Durbin R.M., Hubbard T., Gibbs R.A., Beck S., Rogers J., Bentley D.R.
    Nature 434:325-337(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  4. "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.
  5. "Cloning and characterisation of hAps1 and hAps2, human diadenosine polyphosphate-metabolising Nudix hydrolases."
    Leslie N.R., McLennan A.G., Safrany S.T.
    BMC Biochem. 3:20-20(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: CATALYTIC ACTIVITY, SUBCELLULAR LOCATION, COFACTOR, BIOPHYSICOCHEMICAL PROPERTIES, TISSUE SPECIFICITY, VARIANT ASN-39.
  6. "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: CATALYTIC ACTIVITY.
  7. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].

Entry informationi

Entry nameiNUD11_HUMAN
AccessioniPrimary (citable) accession number: Q96G61
Secondary accession number(s): Q9NVN0
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 5, 2005
Last sequence update: December 1, 2001
Last modified: November 26, 2014
This is version 121 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

Complete proteome, Reference proteome

Documents

  1. Human chromosome X
    Human chromosome X: 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. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3