Reviewed, UniProtKB/Swiss-Prot Q8NFP7 (NUD10_HUMAN)

Names and origin

Protein names

Recommended name:
    Diphosphoinositol polyphosphate phosphohydrolase 3-alpha
      Short name=DIPP-3-alpha
      Short name=DIPP3-alpha
      Short name=hDIPP3alpha
    EC=3.6.1.52
Alternative name(s):
    Diadenosine 5',5'''-P1,P6-hexaphosphate hydrolase 3-alpha
    EC=3.6.1.-
    Nucleoside diphosphate-linked moiety X motif 10
      Short name=Nudix motif 10
      Short name=hAps2

Gene names

Name:	NUDT10
Synonyms:	APS2, DIPP3A

Organism

Homo sapiens (Human)

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Primates › Haplorrhini › Catarrhini › Hominidae › Homo

Protein attributes

Sequence length	164 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is not processed.
Protein existence	Evidence 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 catalyzes 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.4 Ref.5
Cofactor	Magnesium or manganese. Manganese may be the true cofactor in vivo. Ref.4
Subcellular location	Cytoplasm Probable.
Tissue specificity	Mainly expressed in testis and, at lower level in brain. According to Ref.4, it is widely expressed. Ref.1 Ref.4
Sequence similarities	Belongs to the Nudix hydrolase family. DIPP subfamily.
biophysicochemical properties	Kinetic parameters: KM=0.088 µM for PP-InsP5 KM=19 µM for Ap6A KM=50 µM for Ap5A pH dependence: Optimum pH is 8.5.

Ontologies

Keywords
Cellular component	Cytoplasm
Ligand	Magnesium Manganese Metal-binding
Molecular function	Hydrolase
Gene Ontology (GO)
Cellular component	cytoplasm Inferred from electronic annotation. Source: UniProtKB-SubCell
Molecular function	diphosphoinositol-polyphosphate diphosphatase activity Inferred from sequence or structural similarity. Source: UniProtKB magnesium ion binding Inferred from electronic annotation. Source: UniProtKB-KW manganese ion binding Inferred from electronic annotation. Source: UniProtKB-KW
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 164	164	Diphosphoinositol polyphosphate phosphohydrolase 3-alpha		PRO_0000057062
Regions
	Motif	50 – 71	22	Nudix box
Sites
	Metal binding	65	1	Magnesium or manganese By similarity
	Metal binding	69	1	Magnesium or manganese By similarity
Experimental info
	Sequence conflict	90	1	K → E in AAH50700. Ref.3
	Sequence conflict	135	1	V → M in AAH49383. Ref.3

Sequences

	Sequence		Length	Mass (Da)
	Q8NFP7-1 [UniParc]. Last modified October 1, 2002. Version 1. Checksum: 589F342E02B285A7	FASTA	164	18,500
	10 20 30 40 50 60 MKCKPNQTRT YDPEGFKKRA ACLCFRSERE DEVLLVSSSR YPDRWIVPGG GMEPEEEPGG 70 80 90 100 110 120 AAVREVYEEA GVKGKLGRLL GVFEQNQDPK HRTYVYVLTV TELLEDWEDS VSIGRKREWF 130 140 150 160 KVEDAIKVLQ CHKPVHAEYL EKLKLGGSPT NGNSMAPSSP DSDP

References

	« Hide 'large scale' referencesShow '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: 12105228] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA], ENZYME ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, TISSUE SPECIFICITY.
[2]	"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: 15772651] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[3]	"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: 15489334] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. Tissue: Ovary.
[4]	"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: 12121577] [Abstract] Cited for: ENZYME ACTIVITY, SUBCELLULAR LOCATION, COFACTOR, BIOPHYSICOCHEMICAL PROPERTIES, TISSUE SPECIFICITY.
[5]	"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: 12370170] [Abstract] Cited for: ENZYME ACTIVITY.
[6]	Colinge J., Superti-Furga G., Bennett K.L. Submitted (OCT-2008) to UniProtKB Cited for: IDENTIFICATION [LARGE SCALE ANALYSIS], MASS SPECTROMETRY.

Cross-references

Sequence databases
EMBLGenBankDDBJ	AF469196 mRNA. Translation: AAM64113.1. AL158055 Genomic DNA. Translation: CAI40295.1. BC049383 mRNA. Translation: AAH49383.1. BC050700 mRNA. Translation: AAH50700.1.
IPI	IPI00549204.
RefSeq	NP_694853.1.
UniGene	Hs.375178
3D structure databases
SMR	Q8NFP7. Positions 8-146.
ModBase	Search...
Protein-protein interaction databases
IntAct	Q8NFP7. 1 interaction.
Proteomic databases
PRIDE	Q8NFP7.
Genome annotation databases
Ensembl	ENSG00000122824. Homo sapiens. [Contig view]
GeneID	170685.
KEGG	hsa:170685.
Organism-specific databases
GeneCards	GC0XP051091.
H-InvDB	HIX0028345.
HGNC	HGNC:17621. NUDT10.
MIM	300527. gene.
PharmGKB	PA31831.
GenAtlas	Search...
Phylogenomic databases
HOGENOM	Q8NFP7.
HOVERGEN	Q8NFP7.
OMA	Q8NFP7. DEWEDSK.
Enzyme and pathway databases
BRENDA	3.6.1.52. 247.
Gene expression databases
ArrayExpress	Q8NFP7.
Bgee	Q8NFP7.
CleanEx	HS_NUDT10.
GermOnline	ENSG00000122824. Homo sapiens.
Family and domain databases
InterPro	IPR000086. NUDIX_hydrolase_core. [Graphical view]
Gene3D	G3DSA:3.90.79.10. NUDIX_hydrolase. 1 hit.
Pfam	PF00293. NUDIX. 1 hit. [Graphical view]
PROSITE	PS00893. NUDIX. 1 hit. [Graphical view]
ProtoNet	Search...
Other Resources
NextBio	89092.
SOURCE	Search...

Entry information

Entry name

NUD10_HUMAN

Accession

Primary (citable) accession number: Q8NFP7
Secondary accession number(s): Q86VK1, Q86VR0

Entry history

Integrated into UniProtKB/Swiss-Prot:	July 5, 2005
Last sequence update:	October 1, 2002
Last modified:	June 16, 2009
This is version 55 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

HPI (Human Proteome Initiative)