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Protein

Uridine diphosphate glucose pyrophosphatase

Gene

Nudt14

Organism
Mus musculus (Mouse)
Status
Reviewed-Annotation score: Annotation score: 3 out of 5-Experimental evidence at transcript 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 (By similarity).By similarity

Catalytic activityi

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

Cofactori

Mg2+By similarity

GO - Molecular functioni

  1. ADP-ribose diphosphatase activity Source: MGI
  2. metal ion binding Source: InterPro
  3. UDP-sugar diphosphatase activity Source: MGI

GO - Biological processi

  1. metabolic process Source: GOC
Complete GO annotation...

Keywords - Molecular functioni

Hydrolase

Keywords - Ligandi

Magnesium

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
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
ProteomesiUP000000589: Chromosome 12

Organism-specific databases

MGIiMGI:1913424. Nudt14.

Subcellular locationi

Cytoplasm By similarity

GO - Cellular componenti

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

Keywords - Cellular componenti

Cytoplasm

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 222222Uridine diphosphate glucose pyrophosphatasePRO_0000057114Add
BLAST

Proteomic databases

MaxQBiQ9D142.
PaxDbiQ9D142.
PRIDEiQ9D142.

PTM databases

PhosphoSiteiQ9D142.

Expressioni

Gene expression databases

BgeeiQ9D142.
GenevestigatoriQ9D142.

Interactioni

Subunit structurei

Homodimer.By similarity

Structurei

3D structure databases

ProteinModelPortaliQ9D142.
SMRiQ9D142. Positions 39-219.
ModBaseiSearch...
MobiDBiSearch...

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.
InParanoidiQ9D142.
KOiK08077.
OMAiYTYELCA.
OrthoDBiEOG7JHM6K.
PhylomeDBiQ9D142.
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.

Q9D142-1 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
MERIDGVAVG LCAHSPYLRP FTLHYRQDGV QKSWDFMKTH DSVTILMFNS
60 70 80 90 100
SRRSLVLVKQ FRPAVYAGEV ERHFPGSLTA VNQDQPQELQ QALPGSAGVM
110 120 130 140 150
VELCAGIVDQ PGLSLEEAAC KEAWEECGYR LVPTDLRRVA TYMSGVGLTS
160 170 180 190 200
SRQTMFYAEV TDAQRGGPGG GLAEEGELIE VIHLNLDDAQ AFADNPDIPK
210 220
TLGVIYAISW FFSQVVPHLS LQ
Length:222
Mass (Da):24,444
Last modified:June 1, 2001 - v1
Checksum:iD95555CDABBBC5D9
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti192 – 1921F → I in BAB28691. (PubMed:16141072)Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AK003991 mRNA. Translation: BAB23110.1.
AK013174 mRNA. Translation: BAB28691.2.
BC025444 mRNA. Translation: AAH25444.1.
CCDSiCCDS26201.1.
RefSeqiNP_079675.1. NM_025399.3.
UniGeneiMm.7070.

Genome annotation databases

EnsembliENSMUST00000002881; ENSMUSP00000002881; ENSMUSG00000002804.
GeneIDi66174.
KEGGimmu:66174.
UCSCiuc007pfm.1. mouse.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AK003991 mRNA. Translation: BAB23110.1.
AK013174 mRNA. Translation: BAB28691.2.
BC025444 mRNA. Translation: AAH25444.1.
CCDSiCCDS26201.1.
RefSeqiNP_079675.1. NM_025399.3.
UniGeneiMm.7070.

3D structure databases

ProteinModelPortaliQ9D142.
SMRiQ9D142. Positions 39-219.
ModBaseiSearch...
MobiDBiSearch...

PTM databases

PhosphoSiteiQ9D142.

Proteomic databases

MaxQBiQ9D142.
PaxDbiQ9D142.
PRIDEiQ9D142.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSMUST00000002881; ENSMUSP00000002881; ENSMUSG00000002804.
GeneIDi66174.
KEGGimmu:66174.
UCSCiuc007pfm.1. mouse.

Organism-specific databases

CTDi256281.
MGIiMGI:1913424. Nudt14.

Phylogenomic databases

eggNOGiCOG0494.
GeneTreeiENSGT00410000025889.
HOGENOMiHOG000102292.
HOVERGENiHBG052689.
InParanoidiQ9D142.
KOiK08077.
OMAiYTYELCA.
OrthoDBiEOG7JHM6K.
PhylomeDBiQ9D142.
TreeFamiTF313661.

Miscellaneous databases

NextBioi320858.
PROiQ9D142.
SOURCEiSearch...

Gene expression databases

BgeeiQ9D142.
GenevestigatoriQ9D142.

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

  1. "The transcriptional landscape of the mammalian genome."
    Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.
    , Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.
    Science 309:1559-1563(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Strain: C57BL/6J.
    Tissue: Embryo.
  2. "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].

Entry informationi

Entry nameiNUD14_MOUSE
AccessioniPrimary (citable) accession number: Q9D142
Secondary accession number(s): Q9CSD2
Entry historyi
Integrated into UniProtKB/Swiss-Prot: March 1, 2004
Last sequence update: June 1, 2001
Last modified: February 4, 2015
This is version 91 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. MGD cross-references
    Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
  2. 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.