O95848 (NUD14_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Uridine diphosphate glucose pyrophosphatase
Short name=UDPG pyrophosphatase
Short name=UGPPase
EC=3.6.1.45

Alternative name(s):
Nucleoside diphosphate-linked moiety X motif 14
Short name=Nudix motif 14

Gene names

Name:	NUDT14
Synonyms:	UGPP

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	222 AA.
Sequence status	Complete.
Protein existence	Evidence at protein level

General annotation (Comments)

Function	Hydrolyzes UDP-glucose to glucose 1-phosphate and UMP and ADP-ribose to ribose 5-phosphate and AMP. The physiological substrate is probably UDP-glucose. Poor activity on other substrates such as ADP-glucose, CDP-glucose, GDP-glucose and GDP-mannose.
Catalytic activity	UDP-sugar + H2O = UMP + alpha-D-aldose 1-phosphate.
Cofactor	Magnesium.
Subunit structure	Homodimer. Ref.2
Subcellular location	Cytoplasm Ref.2.
Sequence similarities	Belongs to the Nudix hydrolase family. Contains 1 nudix hydrolase domain.
Biophysicochemical properties	pH dependence: Optimum pH is 8.0-9.5.
Sequence caution	The sequence AAD15563.1 differs from that shown. Reason: Erroneous initiation.

Ontologies

Keywords
Cellular component	Cytoplasm
Ligand	Magnesium
Molecular function	Hydrolase
Technical term	3D-structure Complete proteome Reference proteome
Gene Ontology (GO)
Cellular_component	cytoplasm Inferred from electronic annotation. Source: UniProtKB-SubCell
Molecular_function	ADP-ribose diphosphatase activity Inferred from electronic annotation. Source: Compara UDP-sugar diphosphatase activity Inferred from electronic annotation. Source: EC metal ion binding Inferred from electronic annotation. Source: InterPro
Complete GO annotation...

Binary interactions

With	Entry	#Exp.	IntAct	Notes
ARAF	P10398	3	EBI-536866,EBI-365961

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 222

222

Uridine diphosphate glucose pyrophosphatase

PRO_0000057113

Regions

Domain

38 – 206

169

Nudix hydrolase

Motif

111 – 129

19

Nudix box

Secondary structure

1

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222

Helix Strand Turn

Details...

Beta strand

42 – 49

8

Helix

50 – 52

3

Beta strand

54 – 61

8

Helix

63 – 69

7

Beta strand

99 – 102

4

Beta strand

104 – 107

4

Beta strand

110 – 112

3

Helix

115 – 127

13

Helix

133 – 135

3

Beta strand

137 – 144

8

Beta strand

151 – 160

10

Helix

162 – 164

3

Beta strand

179 – 185

7

Helix

186 – 188

3

Helix

189 – 194

6

Helix

202 – 214

13

Helix

216 – 218

3

Sequences

	Sequence		Length	Mass (Da)
	O95848 [UniParc]. Last modified March 1, 2004. Version 2. Checksum: FB1DFA40A67E72B6	FASTA	222	24,118
	10 20 30 40 50 60 MERIEGASVG RCAASPYLRP LTLHYRQNGA QKSWDFMKTH DSVTVLLFNS SRRSLVLVKQ 70 80 90 100 110 120 FRPAVYAGEV ERRFPGSLAA VDQDGPRELQ PALPGSAGVT VELCAGLVDQ PGLSLEEVAC 130 140 150 160 170 180 KEAWEECGYH LAPSDLRRVA TYWSGVGLTG SRQTMFYTEV TDAQRSGPGG GLVEEGELIE 190 200 210 220 VVHLPLEGAQ AFADDPDIPK TLGVIFGVSW FLSQVAPNLD LQ

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Characterization, chromosomal localization, and the complete 30-kb DNA sequence of the human Jagged2 (JAG2) gene." Deng Y., Madan A., Banta A.B., Friedman C., Trask B.J., Hood L., Li L. Genomics 63:133-138(2000) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[2]	"Cloning, expression and characterization of a mammalian Nudix hydrolase-like enzyme that cleaves the pyrophosphate bond of UDP-glucose." Yagi T., Baroja-Fernandez E., Yamamoto R., Munoz F.J., Akazawa T., Hong K.S., Pozueta-Romero J. Biochem. J. 370:409-415(2003) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA], CHARACTERIZATION, SUBCELLULAR LOCATION, SUBUNIT. Tissue: Thyroid.
[3]	"The DNA sequence and analysis of human chromosome 14." Heilig R., Eckenberg R., Petit J.-L., Fonknechten N., Da Silva C., Cattolico L., Levy M., Barbe V., De Berardinis V., Ureta-Vidal A., Pelletier E., Vico V., Anthouard V., Rowen L., Madan A., Qin S., Sun H., Du H. , Pepin K., Artiguenave F., Robert C., Cruaud C., Bruels T., Jaillon O., Friedlander L., Samson G., Brottier P., Cure S., Segurens B., Aniere F., Samain S., Crespeau H., Abbasi N., Aiach N., Boscus D., Dickhoff R., Dors M., Dubois I., Friedman C., Gouyvenoux M., James R., Madan A., Mairey-Estrada B., Mangenot S., Martins N., Menard M., Oztas S., Ratcliffe A., Shaffer T., Trask B., Vacherie B., Bellemere C., Belser C., Besnard-Gonnet M., Bartol-Mavel D., Boutard M., Briez-Silla S., Combette S., Dufosse-Laurent V., Ferron C., Lechaplais C., Louesse C., Muselet D., Magdelenat G., Pateau E., Petit E., Sirvain-Trukniewicz P., Trybou A., Vega-Czarny N., Bataille E., Bluet E., Bordelais I., Dubois M., Dumont C., Guerin T., Haffray S., Hammadi R., Muanga J., Pellouin V., Robert D., Wunderle E., Gauguet G., Roy A., Sainte-Marthe L., Verdier J., Verdier-Discala C., Hillier L.W., Fulton L., McPherson J., Matsuda F., Wilson R., Scarpelli C., Gyapay G., Wincker P., Saurin W., Quetier F., Waterston R., Hood L., Weissenbach J. Nature 421:601-607(2003) [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: Placenta.
[5]	"Crystal structure of human uridine diphosphate glucose pyrophosphatase (NUDT14)." Structural genomics consortium (SGC) Submitted (FEB-2011) to the PDB data bank Cited for: X-RAY CRYSTALLOGRAPHY (2.7 ANGSTROMS) OF 28-222.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ

AF111170 Genomic DNA. Translation: AAD15563.1. Different initiation.
AB087802 mRNA. Translation: BAC65455.1.
AL512355 Genomic DNA. No translation available.
BC041584 mRNA. Translation: AAH41584.1.

IPI

IPI00412878.

RefSeq

NP_803877.2. NM_177533.4.

UniGene

Hs.526432.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
3Q91	X-ray	2.70	A/B/C/D	28-222	[»]

ProteinModelPortal

O95848.

ModBase

Search...

Protein-protein interaction databases

IntAct

O95848. 2 interactions.

STRING

9606.ENSP00000339175.

PTM databases

PhosphoSite

O95848.

Proteomic databases

PaxDb

O95848.

PRIDE

O95848.

Protocols and materials databases

DNASU

256281.

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

Ensembl

ENST00000392568; ENSP00000376349; ENSG00000183828.

GeneID

256281.

KEGG

hsa:256281.

UCSC

uc010tyn.2. human.

Organism-specific databases

CTD

256281.

GeneCards

GC14M105639.

HGNC

HGNC:20141. NUDT14.

HPA

HPA046755.

MIM

609219. gene.

neXtProt

NX_O95848.

PharmGKB

PA134971372.

GenAtlas

Search...

Phylogenomic databases

eggNOG

COG0494.

HOGENOM

HOG000102292.

HOVERGEN

HBG052689.

InParanoid

O95848.

KO

K08077.

OMA

YTYELCA.

OrthoDB

EOG4TMR38.

PhylomeDB

O95848.

Gene expression databases

ArrayExpress

O95848.

Bgee

O95848.

CleanEx

HS_NUDT14.

Genevestigator

O95848.

GermOnline

ENSG00000183828. Homo sapiens.

Family and domain databases

Gene3D

3.90.79.10. 1 hit.

InterPro

IPR004385. NDP_pyrophosphatase.
IPR000086. NUDIX_hydrolase_dom.
IPR015797. NUDIX_hydrolase_dom-like.
[Graphical view]

Pfam

PF00293. NUDIX. 1 hit.
[Graphical view]

SUPFAM

SSF55811. NUDIX_hydrolase. 1 hit.

TIGRFAMs

TIGR00052. TIGR00052. 1 hit.

PROSITE

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

ProtoNet

Search...

Other

EvolutionaryTrace

O95848.

GenomeRNAi

256281.

NextBio

92764.

SOURCE

Search...

Entry information

Entry name

NUD14_HUMAN

Accession

Primary (citable) accession number: O95848
Secondary accession number(s): Q86SJ8

Entry history

Integrated into UniProtKB/Swiss-Prot:	March 1, 2004
Last sequence update:	March 1, 2004
Last modified:	May 1, 2013
This is version 97 of the entry and version 2 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.