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Protein

ADP-sugar pyrophosphatase

Gene

Nudt5

Organism
Mus musculus (Mouse)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Hydrolyzes with similar activities ADP-ribose and ADP-mannose. Can also hydrolyzes ADP-glucose (40% of ADP-ribose activity) and other nucleotide sugars with low activity (10%). Does not play a role in U8 snoRNA decapping activity. Binds U8 snoRNA.

Catalytic activityi

ADP-D-ribose + H2O = AMP + D-ribose 5-phosphate.
ADP-sugar + H2O = AMP + alpha-D-aldose 1-phosphate.
8-oxo-dGDP + H2O = 8-oxo-dGMP + phosphate.

Cofactori

Mg2+By similarityNote: Binds 3 Mg2+ ions per subunit.By similarity

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei27 – 271SubstrateBy similarity
Binding sitei83 – 831SubstrateBy similarity
Metal bindingi95 – 951Magnesium 1; via carbonyl oxygenBy similarity
Binding sitei97 – 971Substrate; via amide nitrogenBy similarity
Metal bindingi111 – 1111Magnesium 2By similarity
Metal bindingi111 – 1111Magnesium 3By similarity
Metal bindingi115 – 1151Magnesium 1By similarity
Metal bindingi115 – 1151Magnesium 3By similarity
Binding sitei132 – 1321SubstrateBy similarity
Metal bindingi165 – 1651Magnesium 3By similarity

GO - Molecular functioni

  • ADP-ribose diphosphatase activity Source: MGI
  • ADP-sugar diphosphatase activity Source: UniProtKB
  • magnesium ion binding Source: UniProtKB
  • nucleoside-diphosphatase activity Source: MGI
  • snoRNA binding Source: UniProtKB

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Hydrolase

Keywords - Ligandi

Magnesium, Metal-binding, RNA-binding

Enzyme and pathway databases

ReactomeiR-MMU-2393930. Phosphate bond hydrolysis by NUDT proteins.
SABIO-RKQ9JKX6.

Names & Taxonomyi

Protein namesi
Recommended name:
ADP-sugar pyrophosphatase (EC:3.6.1.13)
Alternative name(s):
8-oxo-dGDP phosphatase (EC:3.6.1.58)
Nucleoside diphosphate-linked moiety X motif 5
Short name:
Nudix motif 5
Gene namesi
Name:Nudt5
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
Proteomesi
  • UP000000589 Componenti: Chromosome 2

Organism-specific databases

MGIiMGI:1858232. Nudt5.

Subcellular locationi

GO - Cellular componenti

Complete GO annotation...

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 218218ADP-sugar pyrophosphatasePRO_0000057049Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei1 – 11N-acetylmethionineBy similarity
Modified residuei10 – 101PhosphoserineCombined sources
Modified residuei209 – 2091N6-acetyllysineBy similarity
Modified residuei217 – 2171N6-acetyllysineBy similarity

Keywords - PTMi

Acetylation, Phosphoprotein

Proteomic databases

EPDiQ9JKX6.
MaxQBiQ9JKX6.
PaxDbiQ9JKX6.
PeptideAtlasiQ9JKX6.
PRIDEiQ9JKX6.

2D gel databases

REPRODUCTION-2DPAGEQ9JKX6.

PTM databases

iPTMnetiQ9JKX6.
PhosphoSiteiQ9JKX6.
SwissPalmiQ9JKX6.

Miscellaneous databases

PMAP-CutDBQ9JKX6.

Expressioni

Tissue specificityi

Widely expressed. Most abundant in liver.

Gene expression databases

BgeeiQ9JKX6.
ExpressionAtlasiQ9JKX6. baseline and differential.
GenevisibleiQ9JKX6. MM.

Interactioni

Protein-protein interaction databases

BioGridi207516. 1 interaction.
IntActiQ9JKX6. 2 interactions.
MINTiMINT-4104265.
STRINGi10090.ENSMUSP00000026927.

Structurei

3D structure databases

ProteinModelPortaliQ9JKX6.
SMRiQ9JKX6. Positions 12-207.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini56 – 196141Nudix hydrolasePROSITE-ProRule annotationAdd
BLAST

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni45 – 462Substrate binding; shared with dimeric partner

Motif

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Motifi96 – 11722Nudix boxAdd
BLAST

Sequence similaritiesi

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

Phylogenomic databases

eggNOGiKOG3041. Eukaryota.
COG0494. LUCA.
GeneTreeiENSGT00390000006280.
HOGENOMiHOG000174302.
HOVERGENiHBG052691.
InParanoidiQ9JKX6.
KOiK13987.
OMAiECFTVPL.
OrthoDBiEOG7CVPZW.
PhylomeDBiQ9JKX6.
TreeFamiTF106347.

Family and domain databases

Gene3Di3.90.79.10. 1 hit.
InterProiIPR020476. Nudix_hydrolase.
IPR020084. NUDIX_hydrolase_CS.
IPR000086. NUDIX_hydrolase_dom.
IPR015797. NUDIX_hydrolase_dom-like.
[Graphical view]
PfamiPF00293. NUDIX. 1 hit.
[Graphical view]
PRINTSiPR00502. NUDIXFAMILY.
SUPFAMiSSF55811. SSF55811. 1 hit.
PROSITEiPS51462. NUDIX. 1 hit.
PS00893. NUDIX_BOX. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Q9JKX6-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
METRESTESS PGKHLVTSEE LISEGKWVKF EKTTYMDPTG KTRTWETVKL
60 70 80 90 100
TTRKGKSADA VSVIPVLQRT LHHECVILVK QFRPPMGSYC LEFPAGFIED
110 120 130 140 150
GESPEAAALR ELEEETGYKG EVAECSPAVC MDPGLSNCTT HVVTVTINGD
160 170 180 190 200
DAGNVRPKPK PGDGEFMEVI SLPKNDLLTR LDALGAEQHL TVDAKVYAYG
210
LALKHANSKP FEVPFLKF
Length:218
Mass (Da):23,984
Last modified:October 1, 2000 - v1
Checksum:iE831852919F85DFE
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti103 – 1031S → N in AAH04571 (PubMed:15489334).Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF222786 mRNA. Translation: AAF44630.1.
AK088222 mRNA. Translation: BAC40220.1.
AL928924 Genomic DNA. Translation: CAM20348.1.
BC004571 mRNA. Translation: AAH04571.1.
BC049595 mRNA. Translation: AAH49595.1.
CCDSiCCDS15667.1.
RefSeqiNP_058614.1. NM_016918.3.
XP_006497575.1. XM_006497512.2.
XP_006497576.1. XM_006497513.2.
UniGeneiMm.251904.

Genome annotation databases

EnsembliENSMUST00000026927; ENSMUSP00000026927; ENSMUSG00000025817.
ENSMUST00000179748; ENSMUSP00000136233; ENSMUSG00000025817.
GeneIDi53893.
KEGGimmu:53893.
UCSCiuc033hlj.1. mouse.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF222786 mRNA. Translation: AAF44630.1.
AK088222 mRNA. Translation: BAC40220.1.
AL928924 Genomic DNA. Translation: CAM20348.1.
BC004571 mRNA. Translation: AAH04571.1.
BC049595 mRNA. Translation: AAH49595.1.
CCDSiCCDS15667.1.
RefSeqiNP_058614.1. NM_016918.3.
XP_006497575.1. XM_006497512.2.
XP_006497576.1. XM_006497513.2.
UniGeneiMm.251904.

3D structure databases

ProteinModelPortaliQ9JKX6.
SMRiQ9JKX6. Positions 12-207.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi207516. 1 interaction.
IntActiQ9JKX6. 2 interactions.
MINTiMINT-4104265.
STRINGi10090.ENSMUSP00000026927.

PTM databases

iPTMnetiQ9JKX6.
PhosphoSiteiQ9JKX6.
SwissPalmiQ9JKX6.

2D gel databases

REPRODUCTION-2DPAGEQ9JKX6.

Proteomic databases

EPDiQ9JKX6.
MaxQBiQ9JKX6.
PaxDbiQ9JKX6.
PeptideAtlasiQ9JKX6.
PRIDEiQ9JKX6.

Protocols and materials databases

DNASUi53893.
Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSMUST00000026927; ENSMUSP00000026927; ENSMUSG00000025817.
ENSMUST00000179748; ENSMUSP00000136233; ENSMUSG00000025817.
GeneIDi53893.
KEGGimmu:53893.
UCSCiuc033hlj.1. mouse.

Organism-specific databases

CTDi11164.
MGIiMGI:1858232. Nudt5.

Phylogenomic databases

eggNOGiKOG3041. Eukaryota.
COG0494. LUCA.
GeneTreeiENSGT00390000006280.
HOGENOMiHOG000174302.
HOVERGENiHBG052691.
InParanoidiQ9JKX6.
KOiK13987.
OMAiECFTVPL.
OrthoDBiEOG7CVPZW.
PhylomeDBiQ9JKX6.
TreeFamiTF106347.

Enzyme and pathway databases

ReactomeiR-MMU-2393930. Phosphate bond hydrolysis by NUDT proteins.
SABIO-RKQ9JKX6.

Miscellaneous databases

PMAP-CutDBQ9JKX6.
PROiQ9JKX6.
SOURCEiSearch...

Gene expression databases

BgeeiQ9JKX6.
ExpressionAtlasiQ9JKX6. baseline and differential.
GenevisibleiQ9JKX6. MM.

Family and domain databases

Gene3Di3.90.79.10. 1 hit.
InterProiIPR020476. Nudix_hydrolase.
IPR020084. NUDIX_hydrolase_CS.
IPR000086. NUDIX_hydrolase_dom.
IPR015797. NUDIX_hydrolase_dom-like.
[Graphical view]
PfamiPF00293. NUDIX. 1 hit.
[Graphical view]
PRINTSiPR00502. NUDIXFAMILY.
SUPFAMiSSF55811. SSF55811. 1 hit.
PROSITEiPS51462. NUDIX. 1 hit.
PS00893. NUDIX_BOX. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. Cited for: NUCLEOTIDE SEQUENCE [MRNA], CHARACTERIZATION.
  2. "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: NOD.
    Tissue: Thymus.
  3. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: C57BL/6J.
  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: Testis.
  5. Lubec G., Sunyer B., Chen W.-Q.
    Submitted (JAN-2009) to UniProtKB
    Cited for: PROTEIN SEQUENCE OF 175-180, IDENTIFICATION BY MASS SPECTROMETRY.
    Strain: OF1.
    Tissue: Hippocampus.
  6. "Large scale localization of protein phosphorylation by use of electron capture dissociation mass spectrometry."
    Sweet S.M., Bailey C.M., Cunningham D.L., Heath J.K., Cooper H.J.
    Mol. Cell. Proteomics 8:904-912(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-10, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Embryonic fibroblast.
  7. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Brain, Brown adipose tissue, Heart, Kidney, Liver, Lung, Pancreas, Spleen and Testis.
  8. "Multiple mRNA decapping enzymes in mammalian cells."
    Song M.G., Li Y., Kiledjian M.
    Mol. Cell 40:423-432(2010) [PubMed] [Europe PMC] [Abstract]
    Cited for: ABSENCE OF FUNCTION AS A DECAPPING ENZYME, RNA-BINDING.

Entry informationi

Entry nameiNUDT5_MOUSE
AccessioniPrimary (citable) accession number: Q9JKX6
Secondary accession number(s): A2ATT6, Q99KM4
Entry historyi
Integrated into UniProtKB/Swiss-Prot: March 1, 2004
Last sequence update: October 1, 2000
Last modified: July 6, 2016
This is version 118 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, Direct protein sequencing, 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

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.