Q96G61 (NUD11_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended 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

Organism

Homo sapiens (Human) [Reference proteome]

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Opisthokonta › Metazoa › Eumetazoa › Bilateria › Deuterostomia › Chordata › Craniata › Vertebrata › Gnathostomata › Teleostomi › Euteleostomi › Sarcopterygii › Tetrapoda › Amniota › Mammalia › Theria › Eutheria › Euarchontoglires › Primates › Haplorrhini › Simiiformes › Catarrhini › Hominoidea › Hominidae › Homininae › 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.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 component	Cytoplasm
Coding sequence diversity	Polymorphism
Ligand	Magnesium Manganese Metal-binding
Molecular function	Hydrolase
PTM	Phosphoprotein
Technical term	Complete proteome Reference proteome
Gene Ontology (GO)
Cellular_component	cytoplasm Inferred from electronic annotation. Source: UniProtKB-SubCell intracellular Inferred from direct assay. Source: LIFEdb
Molecular_function	diphosphoinositol-polyphosphate diphosphatase activity Inferred from sequence or structural similarity. Source: UniProtKB inositol diphosphate tetrakisphosphate diphosphatase activity Inferred from electronic annotation. Source: EC inositol-1,5-bisdiphosphate-2,3,4,6-tetrakisphosphate 1-diphosphatase activity Inferred from electronic annotation. Source: EC inositol-1,5-bisdiphosphate-2,3,4,6-tetrakisphosphate 5-diphosphatase activity Inferred from electronic annotation. Source: EC inositol-1-diphosphate-2,3,4,5,6-pentakisphosphate diphosphatase activity Inferred from electronic annotation. Source: EC inositol-3,5-bisdiphosphate-2,3,4,6-tetrakisphosphate 5-diphosphatase activity Inferred from electronic annotation. Source: EC inositol-3-diphosphate-1,2,4,5,6-pentakisphosphate diphosphatase activity Inferred from electronic annotation. Source: EC inositol-5-diphosphate-1,2,3,4,6-pentakisphosphate diphosphatase activity Inferred from electronic annotation. Source: EC 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-beta		PRO_0000057065
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 By similarity
	Modified residue	150	1	Phosphothreonine By similarity
Natural variations
	Natural variant	39	1	S → N. Ref.2 Ref.5		VAR_022738

Sequences

	Sequence		Length	Mass (Da)
	Q96G61 [UniParc]. Last modified December 1, 2001. Version 1. Checksum: 8E7F342C8A38872F	FASTA	164	18,559
	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

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] [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]	"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.
IPI	IPI00305384.
RefSeq	NP_060629.2. NM_018159.3.
UniGene	Hs.200016.
3D structure databases
ProteinModelPortal	Q96G61.
ModBase	Search...
Protein-protein interaction databases
STRING	9606.ENSP00000365160.
PTM databases
PhosphoSite	Q96G61.
Polymorphism databases
DMDM	68565927.
Proteomic databases
PaxDb	Q96G61.
PRIDE	Q96G61.
Protocols and materials databases
DNASU	55190.
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
Ensembl	ENST00000375992; ENSP00000365160; ENSG00000196368. ENST00000597464; ENSP00000469526; ENSG00000269203.
GeneID	55190.
KEGG	hsa:55190.
UCSC	uc010njt.3. human.
Organism-specific databases
CTD	55190.
GeneCards	GC0XM051232.
HGNC	HGNC:18011. NUDT11.
MIM	300528. gene.
neXtProt	NX_Q96G61.
PharmGKB	PA31832.
GenAtlas	Search...
Phylogenomic databases
eggNOG	NOG250169.
HOGENOM	HOG000237336.
HOVERGEN	HBG053341.
InParanoid	Q96G61.
KO	K07766.
OMA	CICVRSE.
OrthoDB	EOG479F89.
PhylomeDB	Q96G61.
Enzyme and pathway databases
BioCyc	MetaCyc:HS05381-MONOMER.
BRENDA	3.6.1.52. 2681.
Reactome	REACT_111217. Metabolism.
Gene expression databases
Bgee	Q96G61.
CleanEx	HS_NUDT11.
Genevestigator	Q96G61.
GermOnline	ENSG00000196368. Homo sapiens.
Family and domain databases
Gene3D	3.90.79.10. 1 hit.
InterPro	IPR020084. NUDIX_hydrolase_CS. IPR000086. NUDIX_hydrolase_dom. IPR015797. NUDIX_hydrolase_dom-like. [Graphical view]
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
GenomeRNAi	55190.
NextBio	59039.
SOURCE	Search...

Entry information

Entry name

NUD11_HUMAN

Accession

Primary (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:	May 1, 2013
This is version 108 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.