ADP-sugar pyrophosphatase - Homo sapiens (Human)

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Reviewed, UniProtKB/Swiss-Prot Q9UKK9 (NUDT5_HUMAN)

Last modified July 7, 2009. Version 79. History...

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Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents

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Names and origin

Protein names

Recommended name:
    ADP-sugar pyrophosphatase
    EC=3.6.1.13
    EC=3.6.1.-
Alternative name(s):
    Nucleoside diphosphate-linked moiety X motif 5
      Short name=Nudix motif 5
    YSA1H

Gene names

Name:	NUDT5
ORF Names:	HSPC115

Organism

Homo sapiens (Human) [Complete proteome]

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

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

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Protein attributes

Sequence length	219 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is not processed.
Protein existence	Evidence at protein level.

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General annotation (Comments)

Function	Hydrolyzes with similar activities ADP-ribose, ADP-mannose, and ADP-glucose. Can also hydrolyze other nucleotide sugars with low activity.
Catalytic activity	ADP-ribose + H₂O = AMP + D-ribose 5-phosphate. ADP-sugar + H₂O = AMP + alpha-D-aldose 5-phosphate.
Cofactor	Magnesium.
Subunit structure	Homodimer.
Tissue specificity	Widely expressed. Most abundant in liver.
Sequence similarities	Belongs to the Nudix hydrolase family.

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Ontologies

Keywords
Coding sequence diversity	Polymorphism
Ligand	Magnesium
Molecular function	Hydrolase
PTM	Phosphoprotein
Technical term	3D-structure Complete proteome
Gene Ontology (GO)
Biological process	D-ribose catabolic process Ref.1 Non-traceable author statement. Source: UniProtKB ribonucleoside diphosphate catabolic process Ref.2 Traceable author statement. Source: ProtInc
Cellular component	intracellular Ref.1 Non-traceable author statement. Source: UniProtKB
Molecular function	ADP reductase activity Ref.1 Traceable author statement. Source: ProtInc ADP-ribose diphosphatase activity Inferred from electronic annotation. Source: EC magnesium ion binding Inferred from electronic annotation. Source: UniProtKB-KW protein binding Ref.1 Non-traceable author statement. Source: UniProtKB
Complete GO annotation...

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Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 219

219

ADP-sugar pyrophosphatase

PRO_0000057048

Regions

Motif

97 – 118

Nudix box

Amino acid modifications

Modified residue

Phosphoserine By similarity

Modified residue

Phosphoserine By similarity

Modified residue

Phosphotyrosine Ref.6

Natural variations

Natural variant

123

I → T: dbSNP rs34863826.

VAR_034159

Experimental info

Sequence conflict

50 – 52

KRT → NVP in AAF25479. Ref.2

Secondary structure

219

Helix Strand Turn

Details...

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Sequences

Sequence

Length

Mass (Da)

Tools

Q9UKK9-1 [UniParc].

Last modified May 1, 2000. Version 1.
Checksum: 6574E0BF1EA2BB26
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FASTA

219

24,328

        10         20         30         40         50         60 
MESQEPTESS QNGKQYIISE ELISEGKWVK LEKTTYMDPT GKTRTWESVK RTTRKEQTAD 

        70         80         90        100        110        120 
GVAVIPVLQR TLHYECIVLV KQFRPPMGGY CIEFPAGLID DGETPEAAAL RELEEETGYK 

       130        140        150        160        170        180 
GDIAECSPAV CMDPGLSNCT IHIVTVTING DDAENARPKP KPGDGEFVEV ISLPKNDLLQ 

       190        200        210 
RLDALVAEEH LTVDARVYSY ALALKHANAK PFEVPFLKF

« Hide

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References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Cloning, expression and characterization of YSA1H, a human adenosine 5'-diphosphosugar pyrophosphatase possessing a MutT motif." Gasmi L., Cartwright J.L., McLennan A.G. Biochem. J. 344:331-337(1999) [PubMed: 10567213] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA], CHARACTERIZATION.
[2]	"Cloning and characterization of a new member of the Nudix hydrolases from human and mouse." Yang H., Slupska M.M., Wei Y.-F., Tai J.H., Luther W.M., Xia Y.-R., Shih D.M., Chiang J.-H., Baikalov C., Fitz-Gibbon S., Phan I.T., Conrad A., Miller J.H. J. Biol. Chem. 275:8844-8853(2000) [PubMed: 10722730] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA], CHARACTERIZATION.
[3]	"Cloning and functional analysis of cDNAs with open reading frames for 300 previously undefined genes expressed in CD34+ hematopoietic stem/progenitor cells." Zhang Q.-H., Ye M., Wu X.-Y., Ren S.-X., Zhao M., Zhao C.-J., Fu G., Shen Y., Fan H.-Y., Lu G., Zhong M., Xu X.-R., Han Z.-G., Zhang J.-W., Tao J., Huang Q.-H., Zhou J., Hu G.-X. , Gu J., Chen S.-J., Chen Z. Genome Res. 10:1546-1560(2000) [PubMed: 11042152] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. Tissue: Umbilical cord blood.
[4]	"Cloning of human full open reading frames in Gateway(TM) system entry vector (pDONR201)." Ebert L., Schick M., Neubert P., Schatten R., Henze S., Korn B. Submitted (JUN-2004) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
[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: Placenta.
[6]	"Immunoaffinity profiling of tyrosine phosphorylation in cancer cells." Rush J., Moritz A., Lee K.A., Guo A., Goss V.L., Spek E.J., Zhang H., Zha X.-M., Polakiewicz R.D., Comb M.J. Nat. Biotechnol. 23:94-101(2005) [PubMed: 15592455] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-74, MASS SPECTROMETRY.
[7]	Colinge J., Superti-Furga G., Bennett K.L. Submitted (OCT-2008) to UniProtKB Cited for: IDENTIFICATION [LARGE SCALE ANALYSIS], MASS SPECTROMETRY.
+	Additional computationally mapped references.

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Cross-references

Sequence databases

AF155832 mRNA. Translation: AAF06734.1.
AF218818 mRNA. Translation: AAF25479.1.
AF161464 mRNA. Translation: AAF29079.1.
CR457195 mRNA. Translation: CAG33476.1.
BC000025 mRNA. Translation: AAH00025.1.

IPI

IPI00296913.

RefSeq

NP_054861.2.

UniGene

Hs.555956

3D structure databases

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
2DSB	X-ray	2.50	A/B/C/D	1-219	[»]
2DSC	X-ray	2.00	A/B	1-210	[»]
2DSD	X-ray	2.60	A/B	1-210	[»]
3BM4	X-ray	2.00	A/B	1-210	[»]

ModBase

Search...

Protein-protein interaction databases

IntAct

Q9UKK9. 10 interactions.

PTM databases

PhosphoSite

Q9UKK9.

Proteomic databases

PRIDE

Q9UKK9.

Genome annotation databases

Ensembl

ENSG00000165609. Homo sapiens. [Contig view]

GeneID

11164.

KEGG

hsa:11164.

UCSC

uc001ilj.1. human.

Organism-specific databases

GeneCards

GC10M012249.

H-InvDB

HIX0008645.

HGNC

HGNC:8052. NUDT5.

MIM

609230. gene.

PharmGKB

PA31838.

GenAtlas

Search...

Phylogenomic databases

HOVERGEN

Q9UKK9.

Enzyme and pathway databases

BRENDA

3.6.1.13. 247.

Gene expression databases

ArrayExpress

Q9UKK9.

Bgee

Q9UKK9.

CleanEx

HS_NUDT5.

GermOnline

ENSG00000165609. 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

42475.

SOURCE

Search...

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Entry information

Entry name

NUDT5_HUMAN

Accession

Primary (citable) accession number: Q9UKK9
Secondary accession number(s): Q6IAG0, Q9UH49

Entry history

Integrated into UniProtKB/Swiss-Prot:	May 2, 2002
Last sequence update:	May 1, 2000
Last modified:	July 7, 2009
This is version 79 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

HPI (Human Proteome Initiative)

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