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Q9D142

- NUD14_MOUSE

UniProt

Q9D142 - NUD14_MOUSE

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Protein
Uridine diphosphate glucose pyrophosphatase
Gene
Nudt14
Organism
Mus musculus (Mouse)
Status
Reviewed - 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.

Catalytic activityi

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

Cofactori

Magnesium By similarity.

GO - Molecular functioni

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

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
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 222222Uridine diphosphate glucose pyrophosphatase
PRO_0000057114Add
BLAST

Proteomic databases

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.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini38 – 206169Nudix hydrolase
Add
BLAST

Motif

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

Sequence similaritiesi

Belongs to the Nudix hydrolase family.

Phylogenomic databases

eggNOGiCOG0494.
GeneTreeiENSGT00410000025889.
HOGENOMiHOG000102292.
HOVERGENiHBG052689.
InParanoidiQ9D142.
KOiK08077.
OMAiIYARHFH.
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

MERIDGVAVG LCAHSPYLRP FTLHYRQDGV QKSWDFMKTH DSVTILMFNS    50
SRRSLVLVKQ FRPAVYAGEV ERHFPGSLTA VNQDQPQELQ QALPGSAGVM 100
VELCAGIVDQ PGLSLEEAAC KEAWEECGYR LVPTDLRRVA TYMSGVGLTS 150
SRQTMFYAEV TDAQRGGPGG GLAEEGELIE VIHLNLDDAQ AFADNPDIPK 200
TLGVIYAISW FFSQVVPHLS LQ 222
Length:222
Mass (Da):24,444
Last modified:June 1, 2001 - v1
Checksum:iD95555CDABBBC5D9
GO

Sequence conflict

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti192 – 1921F → I in BAB28691. 1 Publication

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
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:
EMBL
GenBank
DDBJ
Links Updated
AK003991 mRNA. Translation: BAB23110.1 .
AK013174 mRNA. Translation: BAB28691.2 .
BC025444 mRNA. Translation: AAH25444.1 .
CCDSi CCDS26201.1.
RefSeqi NP_079675.1. NM_025399.3.
UniGenei Mm.7070.

3D structure databases

ProteinModelPortali Q9D142.
SMRi Q9D142. Positions 39-219.
ModBasei Search...

PTM databases

PhosphoSitei Q9D142.

Proteomic databases

PaxDbi Q9D142.
PRIDEi Q9D142.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENSMUST00000002881 ; ENSMUSP00000002881 ; ENSMUSG00000002804 .
GeneIDi 66174.
KEGGi mmu:66174.
UCSCi uc007pfm.1. mouse.

Organism-specific databases

CTDi 256281.
MGIi MGI:1913424. Nudt14.

Phylogenomic databases

eggNOGi COG0494.
GeneTreei ENSGT00410000025889.
HOGENOMi HOG000102292.
HOVERGENi HBG052689.
InParanoidi Q9D142.
KOi K08077.
OMAi IYARHFH.
OrthoDBi EOG7JHM6K.
PhylomeDBi Q9D142.
TreeFami TF313661.

Miscellaneous databases

NextBioi 320858.
PROi Q9D142.
SOURCEi Search...

Gene expression databases

Bgeei Q9D142.
Genevestigatori Q9D142.

Family and domain databases

Gene3Di 3.90.79.10. 1 hit.
InterProi IPR004385. NDP_pyrophosphatase.
IPR000086. NUDIX_hydrolase_dom.
IPR015797. NUDIX_hydrolase_dom-like.
[Graphical view ]
Pfami PF00293. NUDIX. 1 hit.
[Graphical view ]
SUPFAMi SSF55811. SSF55811. 1 hit.
TIGRFAMsi TIGR00052. TIGR00052. 1 hit.
PROSITEi PS51462. NUDIX. 1 hit.
[Graphical view ]
ProtoNeti Search...

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: July 9, 2014
This is version 86 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

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