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Protein

Uridine diphosphate glucose pyrophosphatase

Gene

NUDT14

Organism
Homo sapiens (Human)
Status
Reviewed-Annotation score: Annotation score: 4 out of 5-Experimental evidence at protein leveli

Functioni

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 activityi

UDP-sugar + H2O = UMP + alpha-D-aldose 1-phosphate.

Cofactori

pH dependencei

Optimum pH is 8.0-9.5.

GO - Molecular functioni

  1. ADP-ribose diphosphatase activity Source: Ensembl
  2. metal ion binding Source: InterPro
  3. UDP-sugar diphosphatase activity Source: UniProtKB-EC
Complete GO annotation...

Keywords - Molecular functioni

Hydrolase

Keywords - Ligandi

Magnesium

Enzyme and pathway databases

BRENDAi3.6.1.45. 2681.

Names & Taxonomyi

Protein namesi
Recommended name:
Uridine diphosphate glucose pyrophosphatase (EC:3.6.1.45)
Short name:
UDPG pyrophosphatase
Short name:
UGPPase
Alternative name(s):
Nucleoside diphosphate-linked moiety X motif 14
Short name:
Nudix motif 14
Gene namesi
Name:NUDT14
Synonyms:UGPP
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640 Componenti: Chromosome 14

Organism-specific databases

HGNCiHGNC:20141. NUDT14.

Subcellular locationi

Cytoplasm 1 Publication

GO - Cellular componenti

  1. cytoplasm Source: UniProtKB-SubCell
  2. extracellular vesicular exosome Source: UniProtKB
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm

Pathology & Biotechi

Organism-specific databases

PharmGKBiPA134971372.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 222222Uridine diphosphate glucose pyrophosphatasePRO_0000057113Add
BLAST

Proteomic databases

MaxQBiO95848.
PaxDbiO95848.
PRIDEiO95848.

PTM databases

PhosphoSiteiO95848.

Expressioni

Gene expression databases

BgeeiO95848.
CleanExiHS_NUDT14.
ExpressionAtlasiO95848. baseline and differential.
GenevestigatoriO95848.

Organism-specific databases

HPAiHPA046755.

Interactioni

Subunit structurei

Homodimer.1 Publication

Binary interactionsi

WithEntry#Exp.IntActNotes
ARAFP103983EBI-536866,EBI-365961

Protein-protein interaction databases

BioGridi129152. 8 interactions.
IntActiO95848. 2 interactions.
STRINGi9606.ENSP00000339175.

Structurei

Secondary structure

1
222
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi42 – 498Combined sources
Helixi50 – 523Combined sources
Beta strandi54 – 618Combined sources
Helixi63 – 697Combined sources
Beta strandi99 – 1024Combined sources
Beta strandi104 – 1074Combined sources
Beta strandi110 – 1123Combined sources
Helixi115 – 12713Combined sources
Helixi133 – 1353Combined sources
Beta strandi137 – 1448Combined sources
Beta strandi151 – 16010Combined sources
Helixi162 – 1643Combined sources
Beta strandi179 – 1857Combined sources
Helixi186 – 1883Combined sources
Helixi189 – 1946Combined sources
Helixi202 – 21413Combined sources
Helixi216 – 2183Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
3Q91X-ray2.70A/B/C/D28-222[»]
ProteinModelPortaliO95848.
SMRiO95848. Positions 39-220.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiO95848.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini38 – 206169Nudix hydrolasePROSITE-ProRule annotationAdd
BLAST

Motif

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Motifi111 – 12919Nudix boxAdd
BLAST

Sequence similaritiesi

Belongs to the Nudix hydrolase family.Curated
Contains 1 nudix hydrolase domain.PROSITE-ProRule annotation

Phylogenomic databases

eggNOGiCOG0494.
GeneTreeiENSGT00410000025889.
HOGENOMiHOG000102292.
HOVERGENiHBG052689.
InParanoidiO95848.
KOiK08077.
OMAiYTYELCA.
OrthoDBiEOG7JHM6K.
PhylomeDBiO95848.
TreeFamiTF313661.

Family and domain databases

Gene3Di3.90.79.10. 1 hit.
InterProiIPR004385. NDP_pyrophosphatase.
IPR000086. NUDIX_hydrolase_dom.
IPR015797. NUDIX_hydrolase_dom-like.
[Graphical view]
PfamiPF00293. NUDIX. 1 hit.
[Graphical view]
SUPFAMiSSF55811. SSF55811. 1 hit.
TIGRFAMsiTIGR00052. TIGR00052. 1 hit.
PROSITEiPS51462. NUDIX. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

O95848-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MERIEGASVG RCAASPYLRP LTLHYRQNGA QKSWDFMKTH DSVTVLLFNS
60 70 80 90 100
SRRSLVLVKQ FRPAVYAGEV ERRFPGSLAA VDQDGPRELQ PALPGSAGVT
110 120 130 140 150
VELCAGLVDQ PGLSLEEVAC KEAWEECGYH LAPSDLRRVA TYWSGVGLTG
160 170 180 190 200
SRQTMFYTEV TDAQRSGPGG GLVEEGELIE VVHLPLEGAQ AFADDPDIPK
210 220
TLGVIFGVSW FLSQVAPNLD LQ
Length:222
Mass (Da):24,118
Last modified:February 29, 2004 - v2
Checksum:iFB1DFA40A67E72B6
GO

Sequence cautioni

The sequence AAD15563.1 differs from that shown. Reason: Erroneous initiation. Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF111170 Genomic DNA. Translation: AAD15563.1. Different initiation.
AB087802 mRNA. Translation: BAC65455.1.
AL512355 Genomic DNA. No translation available.
BC041584 mRNA. Translation: AAH41584.1.
CCDSiCCDS10000.1.
RefSeqiNP_803877.2. NM_177533.4.
UniGeneiHs.526432.

Genome annotation databases

EnsembliENST00000392568; ENSP00000376349; ENSG00000183828.
GeneIDi256281.
KEGGihsa:256281.
UCSCiuc010tyn.3. human.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF111170 Genomic DNA. Translation: AAD15563.1. Different initiation.
AB087802 mRNA. Translation: BAC65455.1.
AL512355 Genomic DNA. No translation available.
BC041584 mRNA. Translation: AAH41584.1.
CCDSiCCDS10000.1.
RefSeqiNP_803877.2. NM_177533.4.
UniGeneiHs.526432.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
3Q91X-ray2.70A/B/C/D28-222[»]
ProteinModelPortaliO95848.
SMRiO95848. Positions 39-220.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi129152. 8 interactions.
IntActiO95848. 2 interactions.
STRINGi9606.ENSP00000339175.

PTM databases

PhosphoSiteiO95848.

Proteomic databases

MaxQBiO95848.
PaxDbiO95848.
PRIDEiO95848.

Protocols and materials databases

DNASUi256281.
Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000392568; ENSP00000376349; ENSG00000183828.
GeneIDi256281.
KEGGihsa:256281.
UCSCiuc010tyn.3. human.

Organism-specific databases

CTDi256281.
GeneCardsiGC14M105639.
HGNCiHGNC:20141. NUDT14.
HPAiHPA046755.
MIMi609219. gene.
neXtProtiNX_O95848.
PharmGKBiPA134971372.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiCOG0494.
GeneTreeiENSGT00410000025889.
HOGENOMiHOG000102292.
HOVERGENiHBG052689.
InParanoidiO95848.
KOiK08077.
OMAiYTYELCA.
OrthoDBiEOG7JHM6K.
PhylomeDBiO95848.
TreeFamiTF313661.

Enzyme and pathway databases

BRENDAi3.6.1.45. 2681.

Miscellaneous databases

EvolutionaryTraceiO95848.
GenomeRNAii256281.
NextBioi92764.
PROiO95848.
SOURCEiSearch...

Gene expression databases

BgeeiO95848.
CleanExiHS_NUDT14.
ExpressionAtlasiO95848. baseline and differential.
GenevestigatoriO95848.

Family and domain databases

Gene3Di3.90.79.10. 1 hit.
InterProiIPR004385. NDP_pyrophosphatase.
IPR000086. NUDIX_hydrolase_dom.
IPR015797. NUDIX_hydrolase_dom-like.
[Graphical view]
PfamiPF00293. NUDIX. 1 hit.
[Graphical view]
SUPFAMiSSF55811. SSF55811. 1 hit.
TIGRFAMsiTIGR00052. TIGR00052. 1 hit.
PROSITEiPS51462. NUDIX. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  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(1999) [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(2002) [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(2002) [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(2003) [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 (JAN-2011) to the PDB data bank
    Cited for: X-RAY CRYSTALLOGRAPHY (2.7 ANGSTROMS) OF 28-222.

Entry informationi

Entry nameiNUD14_HUMAN
AccessioniPrimary (citable) accession number: O95848
Secondary accession number(s): Q86SJ8
Entry historyi
Integrated into UniProtKB/Swiss-Prot: February 29, 2004
Last sequence update: February 29, 2004
Last modified: March 31, 2015
This is version 114 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
DisclaimerAny 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.

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

Documents

  1. Human chromosome 14
    Human chromosome 14: entries, gene names and cross-references to MIM
  2. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  3. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  4. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into Uniref entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.