Q8NFP7 (NUD10_HUMAN) Reviewed, UniProtKB/Swiss-Prot

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
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.
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 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.6 Ref.7
Cofactor	Binds 3 magnesium or manganese ions per subunit By similarity. Manganese may be the true cofactor in vivo. Ref.6
Subcellular location	Cytoplasm Probable Ref.6.
Tissue specificity	Mainly expressed in testis and, at lower level in brain. According to Ref.6, it is widely expressed. Ref.1 Ref.6
Sequence similarities	Belongs to the Nudix hydrolase family. DIPP subfamily. Contains 1 nudix hydrolase domain.
Biophysicochemical properties	Kinetic parameters: KM=0.088 µM for PP-InsP5 Ref.1 Ref.6 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
PTM	Phosphoprotein
Technical term	3D-structure Complete proteome Reference proteome
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 metal 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

Domain

17 – 144

128

Nudix hydrolase

Region

17 – 19

3

Substrate binding By similarity

Region

89 – 91

3

Substrate binding By similarity

Motif

50 – 71

22

Nudix box

Sites

Active site

68

1

Proton acceptor By similarity

Metal binding

49

1

Magnesium 1; via carbonyl oxygen By similarity

Metal binding

65

1

Magnesium 2 By similarity

Metal binding

65

1

Magnesium 3 By similarity

Metal binding

69

1

Magnesium 1 By similarity

Binding site

9

1

Substrate By similarity

Binding site

40

1

Substrate By similarity

Amino acid modifications

Modified residue

148

1

Phosphoserine Ref.8

Modified residue

150

1

Phosphothreonine Ref.8

Modified residue

154

1

Phosphoserine Ref.8

Modified residue

158

1

Phosphoserine Ref.8

Modified residue

159

1

Phosphoserine Ref.8

Modified residue

162

1

Phosphoserine Ref.8

Experimental info

Sequence conflict

90

1

K → E in AAH50700. Ref.5

Sequence conflict

135

1

V → M in AAH49383. Ref.5

Secondary structure

1

.

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.

.

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164

Helix Strand Turn

Details...

Beta strand

18 – 27

10

Beta strand

32 – 37

6

Beta strand

39 – 41

3

Beta strand

44 – 46

3

Helix

62 – 69

8

Beta strand

92 – 99

8

Helix

108 – 112

5

Beta strand

117 – 121

5

Helix

122 – 130

9

Helix

134 – 144

11

Sequences

	Sequence		Length	Mass (Da)
	Q8NFP7 [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]	"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: 14702039] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
[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: 15772651] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[4]	Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S., Turner R. , Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W., Venter J.C. Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[5]	"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.
[6]	"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.
[7]	"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.
[8]	"Lys-N and trypsin cover complementary parts of the phosphoproteome in a refined SCX-based approach." Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J., Mohammed S. Anal. Chem. 81:4493-4501(2009) [PubMed: 19413330] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-148; THR-150; SER-154; SER-158; SER-159 AND SER-162, MASS SPECTROMETRY. Tissue: Embryonic kidney.
[9]	"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: 21269460] [Abstract] Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[10]	"Crystal structure of human diphosphoinositol polyphosphate phosphohydrolase 3-alpha." Structural genomics consortium (SGC) Submitted (APR-2010) to the PDB data bank Cited for: X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS) OF 17-144 IN COMPLEX WITH CITRATE.
+	Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ

AF469196 mRNA. Translation: AAM64113.1.
AK291952 mRNA. Translation: BAF84641.1.
AL158055 Genomic DNA. Translation: CAI40295.1.
CH471180 Genomic DNA. Translation: EAW89910.1.
CH471180 Genomic DNA. Translation: EAW89911.1.
BC049383 mRNA. Translation: AAH49383.1.
BC050700 mRNA. Translation: AAH50700.1.

IPI

IPI00549204.

RefSeq

NP_694853.1. NM_153183.2.

UniGene

Hs.375178.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
3MCF	X-ray	2.00	A/B	17-144	[»]

ProteinModelPortal

Q8NFP7.

SMR

Q8NFP7. Positions 17-144.

ModBase

Search...

Protein-protein interaction databases

IntAct

Q8NFP7. 2 interactions.

MINT

MINT-1383448.

STRING

Q8NFP7.

PTM databases

PhosphoSite

Q8NFP7.

Polymorphism databases

DMDM

68565913.

Proteomic databases

PRIDE

Q8NFP7.

Protocols and materials databases

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

Ensembl

ENST00000356450; ENSP00000348831; ENSG00000122824.
ENST00000376006; ENSP00000365174; ENSG00000122824.

GeneID

170685.

KEGG

hsa:170685.

UCSC

uc004dph.1. human.

Organism-specific databases

CTD

170685.

GeneCards

GC0XP051091.

H-InvDB

HIX0028345.

HGNC

HGNC:17621. NUDT10.

MIM

300527. gene.

neXtProt

NX_Q8NFP7.

PharmGKB

PA31831.

GenAtlas

Search...

Phylogenomic databases

eggNOG

prNOG09035.

GeneTree

ENSGT00390000012928.

HOGENOM

HBG713158.

HOVERGEN

HBG053341.

InParanoid

Q8NFP7.

OMA

SSMSENC.

OrthoDB

EOG479F89.

PhylomeDB

Q8NFP7.

Enzyme and pathway databases

BioCyc

MetaCyc:ENSG00000122824-MONOMER.

Gene expression databases

ArrayExpress

Q8NFP7.

Bgee

Q8NFP7.

CleanEx

HS_NUDT10.

Genevestigator

Q8NFP7.

GermOnline

ENSG00000122824. Homo sapiens.

Family and domain databases

InterPro

IPR020084. NUDIX_hydrolase_CS.
IPR000086. NUDIX_hydrolase_dom.
IPR015797. NUDIX_hydrolase_dom-like.
[Graphical view]

Gene3D

G3DSA:3.90.79.10. NUDIX_hydrolase. 1 hit.

Pfam

PF00293. NUDIX. 1 hit.
[Graphical view]

SUPFAM

SSF55811. NUDIX_hydrolase. 1 hit.

PROSITE

PS51462. NUDIX. 1 hit.
PS00893. NUDIX_BOX. 1 hit.
[Graphical view]

ProtoNet

Search...

Other

NextBio

89092.

SOURCE

Search...

Entry information

Entry name

NUD10_HUMAN

Accession

Primary (citable) accession number: Q8NFP7
Secondary accession number(s): A8K7D7 , D3DX69, Q86VK1, Q86VR0

Entry history

Integrated into UniProtKB/Swiss-Prot:	July 5, 2005
Last sequence update:	October 1, 2002
Last modified:	January 25, 2012
This is version 82 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program

Disclaimer

Any 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.