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Protein

Uridine diphosphate glucose pyrophosphatase

Gene

NUDT14

Organism
Homo sapiens (Human)
Status
Reviewed-Annotation score: Annotation score: 5 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

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Hydrolase

Keywords - Ligandi

Magnesium

Enzyme and pathway databases

BioCyciZFISH:HS11943-MONOMER.
BRENDAi3.6.1.45. 2681.
ReactomeiR-HSA-480985. Synthesis of dolichyl-phosphate-glucose.

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
Proteomesi
  • UP000005640 Componenti: Chromosome 14

Organism-specific databases

HGNCiHGNC:20141. NUDT14.

Subcellular locationi

GO - Cellular componenti

  • cytosol Source: Reactome
  • extracellular exosome Source: UniProtKB
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm

Pathology & Biotechi

Organism-specific databases

OpenTargetsiENSG00000183828.
PharmGKBiPA134971372.

Polymorphism and mutation databases

BioMutaiNUDT14.

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00000571131 – 222Uridine diphosphate glucose pyrophosphataseAdd BLAST222

Proteomic databases

EPDiO95848.
MaxQBiO95848.
PaxDbiO95848.
PeptideAtlasiO95848.
PRIDEiO95848.

PTM databases

iPTMnetiO95848.
PhosphoSitePlusiO95848.

Expressioni

Gene expression databases

BgeeiENSG00000183828.
CleanExiHS_NUDT14.
ExpressionAtlasiO95848. baseline and differential.
GenevisibleiO95848. HS.

Organism-specific databases

HPAiHPA046755.

Interactioni

Subunit structurei

Homodimer.1 Publication

Binary interactionsi

WithEntry#Exp.IntActNotes
itself3EBI-536866,EBI-536866
ARAFP103983EBI-536866,EBI-365961
LNX1Q8TBB17EBI-536866,EBI-739832
NIF3L1Q9GZT85EBI-536866,EBI-740897
RELQ048643EBI-536866,EBI-307352
TERF2IPQ9NYB02EBI-536866,EBI-750109
WDYHV1Q96HA83EBI-536866,EBI-741158
ZCCHC10Q8TBK63EBI-536866,EBI-597063

Protein-protein interaction databases

BioGridi129152. 8 interactors.
IntActiO95848. 10 interactors.
STRINGi9606.ENSP00000376349.

Structurei

Secondary structure

1222
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Beta strandi42 – 49Combined sources8
Helixi50 – 52Combined sources3
Beta strandi54 – 61Combined sources8
Helixi63 – 69Combined sources7
Beta strandi99 – 102Combined sources4
Beta strandi104 – 107Combined sources4
Beta strandi110 – 112Combined sources3
Helixi115 – 127Combined sources13
Helixi133 – 135Combined sources3
Beta strandi137 – 144Combined sources8
Beta strandi151 – 160Combined sources10
Helixi162 – 164Combined sources3
Beta strandi179 – 185Combined sources7
Helixi186 – 188Combined sources3
Helixi189 – 194Combined sources6
Helixi202 – 214Combined sources13
Helixi216 – 218Combined sources3

3D structure databases

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

Miscellaneous databases

EvolutionaryTraceiO95848.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Domaini38 – 206Nudix hydrolasePROSITE-ProRule annotationAdd BLAST169

Motif

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Motifi111 – 129Nudix boxAdd BLAST19

Sequence similaritiesi

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

Phylogenomic databases

eggNOGiKOG4432. Eukaryota.
COG0494. LUCA.
GeneTreeiENSGT00410000025889.
HOGENOMiHOG000102292.
HOVERGENiHBG052689.
InParanoidiO95848.
KOiK08077.
OMAiYTYELCA.
OrthoDBiEOG091G0Q7M.
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]
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:March 1, 2004 - v2
Checksum:iFB1DFA40A67E72B6
GO

Sequence cautioni

The sequence AAD15563 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.4. 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
PDB entryMethodResolution (Å)ChainPositionsPDBsum
3Q91X-ray2.70A/B/C/D28-222[»]
ProteinModelPortaliO95848.
SMRiO95848.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi129152. 8 interactors.
IntActiO95848. 10 interactors.
STRINGi9606.ENSP00000376349.

PTM databases

iPTMnetiO95848.
PhosphoSitePlusiO95848.

Polymorphism and mutation databases

BioMutaiNUDT14.

Proteomic databases

EPDiO95848.
MaxQBiO95848.
PaxDbiO95848.
PeptideAtlasiO95848.
PRIDEiO95848.

Protocols and materials databases

DNASUi256281.
Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000392568; ENSP00000376349; ENSG00000183828.
GeneIDi256281.
KEGGihsa:256281.
UCSCiuc010tyn.4. human.

Organism-specific databases

CTDi256281.
GeneCardsiNUDT14.
HGNCiHGNC:20141. NUDT14.
HPAiHPA046755.
MIMi609219. gene.
neXtProtiNX_O95848.
OpenTargetsiENSG00000183828.
PharmGKBiPA134971372.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiKOG4432. Eukaryota.
COG0494. LUCA.
GeneTreeiENSGT00410000025889.
HOGENOMiHOG000102292.
HOVERGENiHBG052689.
InParanoidiO95848.
KOiK08077.
OMAiYTYELCA.
OrthoDBiEOG091G0Q7M.
PhylomeDBiO95848.
TreeFamiTF313661.

Enzyme and pathway databases

BioCyciZFISH:HS11943-MONOMER.
BRENDAi3.6.1.45. 2681.
ReactomeiR-HSA-480985. Synthesis of dolichyl-phosphate-glucose.

Miscellaneous databases

EvolutionaryTraceiO95848.
GenomeRNAii256281.
PROiO95848.
SOURCEiSearch...

Gene expression databases

BgeeiENSG00000183828.
CleanExiHS_NUDT14.
ExpressionAtlasiO95848. baseline and differential.
GenevisibleiO95848. HS.

Family and domain databases

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

Entry informationi

Entry nameiNUD14_HUMAN
AccessioniPrimary (citable) accession number: O95848
Secondary accession number(s): Q86SJ8
Entry historyi
Integrated into UniProtKB/Swiss-Prot: March 1, 2004
Last sequence update: March 1, 2004
Last modified: November 30, 2016
This is version 128 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

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 one 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.