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Q96G61 (NUD11_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 117. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (5) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Diphosphoinositol polyphosphate phosphohydrolase 3-beta

Short name=DIPP-3-beta
Short name=DIPP3-beta
Short name=hDIPP3beta
EC=3.6.1.52
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 names
Name:NUDT11
Synonyms:APS1, DIPP3B
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length164 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

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 activity

Diphospho-myo-inositol polyphosphate + H2O = myo-inositol polyphosphate + phosphate. Ref.1 Ref.5 Ref.6

P1,P(6)-bis(5'-adenosyl)hexaphosphate + H2O = adenosine 5'-pentaphosphate + AMP. Ref.1 Ref.5 Ref.6

P1,P(5)-bis(5'-adenosyl)pentaphosphate + H2O = adenosine 5'-tetraphosphate + AMP. Ref.1 Ref.5 Ref.6

Cofactor

Binds 3 magnesium or manganese ions per subunit By similarity. Manganese may be the true cofactor in vivo. Ref.5

Subcellular location

Cytoplasm Ref.5.

Tissue specificity

Mainly expressed in testis and, at lower level in brain. According to Ref.5, it is also expressed in pancreas and weakly expressed in thymus, prostate, ovary, lung, small intestine and heart. Ref.1 Ref.5

Sequence similarities

Belongs to the Nudix hydrolase family. DIPP subfamily.

Contains 1 nudix hydrolase domain.

Biophysicochemical properties

Kinetic parameters:

KM=0.053 µM for PP-InsP5 Ref.1 Ref.5

KM=13 µM for Ap6A

KM=37 µM for Ap5A

pH dependence:

Optimum pH is 8.5.

Ontologies

Keywords
   Cellular componentCytoplasm
   Coding sequence diversityPolymorphism
   LigandMagnesium
Manganese
Metal-binding
   Molecular functionHydrolase
   Technical termComplete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processinositol phosphate metabolic process

Traceable author statement. Source: Reactome

small molecule metabolic process

Traceable author statement. Source: Reactome

   Cellular_componentcytosol

Traceable author statement. Source: Reactome

intracellular

Inferred from direct assay. Source: LIFEdb

   Molecular_functiondiphosphoinositol-polyphosphate diphosphatase activity

Inferred from sequence or structural similarity. Source: UniProtKB

inositol diphosphate tetrakisphosphate diphosphatase activity

Inferred from electronic annotation. Source: UniProtKB-EC

inositol-1,5-bisdiphosphate-2,3,4,6-tetrakisphosphate 1-diphosphatase activity

Inferred from electronic annotation. Source: UniProtKB-EC

inositol-1,5-bisdiphosphate-2,3,4,6-tetrakisphosphate 5-diphosphatase activity

Inferred from electronic annotation. Source: UniProtKB-EC

inositol-1-diphosphate-2,3,4,5,6-pentakisphosphate diphosphatase activity

Inferred from electronic annotation. Source: UniProtKB-EC

inositol-3,5-bisdiphosphate-2,3,4,6-tetrakisphosphate 5-diphosphatase activity

Inferred from electronic annotation. Source: UniProtKB-EC

inositol-3-diphosphate-1,2,4,5,6-pentakisphosphate diphosphatase activity

Inferred from electronic annotation. Source: UniProtKB-EC

inositol-5-diphosphate-1,2,3,4,6-pentakisphosphate diphosphatase activity

Inferred from electronic annotation. Source: UniProtKB-EC

metal ion binding

Inferred from electronic annotation. Source: UniProtKB-KW

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 164164Diphosphoinositol polyphosphate phosphohydrolase 3-beta
PRO_0000057065

Regions

Domain17 – 144128Nudix hydrolase
Region17 – 193Substrate binding By similarity
Region89 – 913Substrate binding By similarity
Motif50 – 7122Nudix box

Sites

Active site681Proton acceptor By similarity
Metal binding491Magnesium 1; via carbonyl oxygen By similarity
Metal binding651Magnesium 2 By similarity
Metal binding651Magnesium 3 By similarity
Metal binding691Magnesium 1 By similarity
Binding site91Substrate By similarity
Binding site401Substrate By similarity

Natural variations

Natural variant391S → N. Ref.2 Ref.5
VAR_022738

Sequences

Sequence LengthMass (Da)Tools
Q96G61 [UniParc].

Last modified December 1, 2001. Version 1.
Checksum: 8E7F342C8A38872F

FASTA16418,559
        10         20         30         40         50         60 
MKCKPNQTRT YDPEGFKKRA ACLCFRSERE DEVLLVSSSR YPDRWIVPGG GMEPEEEPGG 

        70         80         90        100        110        120 
AAVREVYEEA GVKGKLGRLL GVFEQNQDRK HRTYVYVLTV TELLEDWEDS VSIGRKREWF 

       130        140        150        160 
KVEDAIKVLQ CHKPVHAEYL EKLKLGGSPT NGNSMAPSSP DSDP 

« Hide

References

« Hide 'large scale' references
[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. expand/collapse author list , 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. expand/collapse author list , 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]"Initial characterization of the human central proteome."
Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.
BMC Syst. Biol. 5:17-17(2011) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AK001490 mRNA. Translation: BAA91720.1.
AL158055 Genomic DNA. Translation: CAI40294.1.
BC009942 mRNA. Translation: AAH09942.1.
CCDSCCDS43952.1.
RefSeqNP_060629.2. NM_018159.3.
UniGeneHs.200016.

3D structure databases

ProteinModelPortalQ96G61.
SMRQ96G61. Positions 17-144.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid120487. 1 interaction.
MINTMINT-3053121.
STRING9606.ENSP00000365160.

PTM databases

PhosphoSiteQ96G61.

Polymorphism databases

DMDM68565927.

Proteomic databases

MaxQBQ96G61.
PaxDbQ96G61.
PRIDEQ96G61.

Protocols and materials databases

DNASU55190.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000375992; ENSP00000365160; ENSG00000196368.
ENST00000597464; ENSP00000469526; ENSG00000269203.
GeneID55190.
KEGGhsa:55190.
UCSCuc010njt.3. human.

Organism-specific databases

CTD55190.
GeneCardsGC0XM051232.
HGNCHGNC:18011. NUDT11.
MIM300528. gene.
neXtProtNX_Q96G61.
PharmGKBPA31832.
GenAtlasSearch...

Phylogenomic databases

eggNOGNOG250169.
HOGENOMHOG000237336.
HOVERGENHBG053341.
InParanoidQ96G61.
KOK07766.
OMACICVRSE.
OrthoDBEOG7T7GVQ.
PhylomeDBQ96G61.
TreeFamTF106349.

Enzyme and pathway databases

BioCycMetaCyc:HS05381-MONOMER.
BRENDA3.6.1.52. 2681.
ReactomeREACT_111217. Metabolism.

Gene expression databases

BgeeQ96G61.
CleanExHS_NUDT11.
GenevestigatorQ96G61.

Family and domain databases

Gene3D3.90.79.10. 1 hit.
InterProIPR020084. NUDIX_hydrolase_CS.
IPR000086. NUDIX_hydrolase_dom.
IPR015797. NUDIX_hydrolase_dom-like.
[Graphical view]
PfamPF00293. NUDIX. 1 hit.
[Graphical view]
SUPFAMSSF55811. SSF55811. 1 hit.
PROSITEPS51462. NUDIX. 1 hit.
PS00893. NUDIX_BOX. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

GeneWikiNUDT11.
GenomeRNAi55190.
NextBio59039.
PROQ96G61.
SOURCESearch...

Entry information

Entry nameNUD11_HUMAN
AccessionPrimary (citable) accession number: Q96G61
Secondary accession number(s): Q9NVN0
Entry history
Integrated into UniProtKB/Swiss-Prot: July 5, 2005
Last sequence update: December 1, 2001
Last modified: July 9, 2014
This is version 117 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (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.

Relevant documents

SIMILARITY comments

Index of protein domains and families

MIM cross-references

Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot

Human polymorphisms and disease mutations

Index of human polymorphisms and disease mutations

Human entries with polymorphisms or disease mutations

List of human entries with polymorphisms or disease mutations

Human chromosome X

Human chromosome X: entries, gene names and cross-references to MIM