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Protein

ADP-ribose pyrophosphatase, mitochondrial

Gene

Nudt9

Organism
Mus musculus (Mouse)
Status
Reviewed-Annotation score: Annotation score: 4 out of 5-Experimental evidence at protein leveli

Functioni

Hydrolyzes ADP-ribose (ADPR) to AMP and ribose 5'-phosphate.

Catalytic activityi

ADP-D-ribose + H2O = AMP + D-ribose 5-phosphate.

Cofactori

Protein has several cofactor binding sites:

GO - Molecular functioni

  • adenosine-diphosphatase activity Source: MGI
  • ADP-ribose diphosphatase activity Source: MGI

GO - Biological processi

  • ADP catabolic process Source: MGI
  • IDP catabolic process Source: MGI
Complete GO annotation...

Keywords - Molecular functioni

Hydrolase

Keywords - Ligandi

Magnesium, Manganese

Enzyme and pathway databases

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

Names & Taxonomyi

Protein namesi
Recommended name:
ADP-ribose pyrophosphatase, mitochondrial (EC:3.6.1.13)
Alternative name(s):
ADP-ribose diphosphatase
ADP-ribose phosphohydrolase
Adenosine diphosphoribose pyrophosphatase
Short name:
ADPR-PPase
Nucleoside diphosphate-linked moiety X motif 9
Short name:
Nudix motif 9
Gene namesi
Name:Nudt9
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
Proteomesi
  • UP000000589 Componenti: Chromosome 5

Organism-specific databases

MGIiMGI:1921417. Nudt9.

Subcellular locationi

GO - Cellular componenti

  • extracellular exosome Source: MGI
  • mitochondrion Source: MGI
Complete GO annotation...

Keywords - Cellular componenti

Mitochondrion

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Transit peptidei1 – 4646MitochondrionSequence analysisAdd
BLAST
Chaini47 – 350304ADP-ribose pyrophosphatase, mitochondrialPRO_0000019951Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei121 – 1211PhosphoserineBy similarity

Keywords - PTMi

Phosphoprotein

Proteomic databases

EPDiQ8BVU5.
MaxQBiQ8BVU5.
PaxDbiQ8BVU5.
PRIDEiQ8BVU5.

PTM databases

iPTMnetiQ8BVU5.
PhosphoSiteiQ8BVU5.

Expressioni

Gene expression databases

BgeeiQ8BVU5.
ExpressionAtlasiQ8BVU5. baseline and differential.
GenevisibleiQ8BVU5. MM.

Interactioni

Subunit structurei

Monomer. Interacts with GLOD4.By similarity

Protein-protein interaction databases

STRINGi10090.ENSMUSP00000031250.

Structurei

3D structure databases

ProteinModelPortaliQ8BVU5.
SMRiQ8BVU5. Positions 59-350.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini178 – 334157Nudix hydrolasePROSITE-ProRule annotationAdd
BLAST

Motif

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Motifi215 – 23723Nudix boxAdd
BLAST

Sequence similaritiesi

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

Keywords - Domaini

Transit peptide

Phylogenomic databases

eggNOGiKOG4195. Eukaryota.
ENOG410XPYY. LUCA.
GeneTreeiENSGT00390000017405.
HOGENOMiHOG000130166.
HOVERGENiHBG052693.
InParanoidiQ8BVU5.
KOiK13988.
OMAiQISESNF.
PhylomeDBiQ8BVU5.
TreeFamiTF106351.

Family and domain databases

Gene3Di3.90.79.10. 1 hit.
InterProiIPR000086. NUDIX_hydrolase_dom.
IPR015797. NUDIX_hydrolase_dom-like.
[Graphical view]
PfamiPF00293. NUDIX. 1 hit.
[Graphical view]
SUPFAMiSSF55811. SSF55811. 1 hit.
PROSITEiPS51462. NUDIX. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

Q8BVU5-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MAGRSLGQAV ATVSLSVALA SVTVRSSACR AVPAPRNTFP TCGFHLNANI
60 70 80 90 100
MSGSNGAKEN SHNKARTSPY PGSKVERSQV PNEKVGWLVE WQDYNPVEYT
110 120 130 140 150
AVSVLAGPQW ADPQISESNF SPKFNEKDGH VERKSQNGLY EIENGRPRNP
160 170 180 190 200
AGRTGLVGRG LLGRWGPNHA ADPIITRWKR DESGNKITHP VSGKCILQFV
210 220 230 240 250
AIKRKDCGEW AIPGGMVDPG EKISATLKRE FGEEALNSLQ KSSAEKREIE
260 270 280 290 300
EKLHALFSQE HLVIYKGYVD DPRNTDNAWM ETEAVNYHDE TGETMDNLTL
310 320 330 340 350
EAGDDAGKVK WVDISDQLKL YASHSQFIKL VAEKRDAHWS EDHAADSRGL
Length:350
Mass (Da):38,604
Last modified:March 1, 2003 - v1
Checksum:iEDD9371307AB3373
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti343 – 3431H → R in AAH33921 (PubMed:15489334).Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AK076500 mRNA. Translation: BAC36366.1.
AK158058 mRNA. Translation: BAE34342.1.
AL714024 Genomic DNA. Translation: CAM13353.1.
BC033921 mRNA. Translation: AAH33921.1.
CCDSiCCDS19482.1.
RefSeqiNP_083070.2. NM_028794.4.
UniGeneiMm.241484.

Genome annotation databases

EnsembliENSMUST00000031250; ENSMUSP00000031250; ENSMUSG00000029310.
GeneIDi74167.
KEGGimmu:74167.
UCSCiuc008yka.1. mouse.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AK076500 mRNA. Translation: BAC36366.1.
AK158058 mRNA. Translation: BAE34342.1.
AL714024 Genomic DNA. Translation: CAM13353.1.
BC033921 mRNA. Translation: AAH33921.1.
CCDSiCCDS19482.1.
RefSeqiNP_083070.2. NM_028794.4.
UniGeneiMm.241484.

3D structure databases

ProteinModelPortaliQ8BVU5.
SMRiQ8BVU5. Positions 59-350.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi10090.ENSMUSP00000031250.

PTM databases

iPTMnetiQ8BVU5.
PhosphoSiteiQ8BVU5.

Proteomic databases

EPDiQ8BVU5.
MaxQBiQ8BVU5.
PaxDbiQ8BVU5.
PRIDEiQ8BVU5.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSMUST00000031250; ENSMUSP00000031250; ENSMUSG00000029310.
GeneIDi74167.
KEGGimmu:74167.
UCSCiuc008yka.1. mouse.

Organism-specific databases

CTDi53343.
MGIiMGI:1921417. Nudt9.

Phylogenomic databases

eggNOGiKOG4195. Eukaryota.
ENOG410XPYY. LUCA.
GeneTreeiENSGT00390000017405.
HOGENOMiHOG000130166.
HOVERGENiHBG052693.
InParanoidiQ8BVU5.
KOiK13988.
OMAiQISESNF.
PhylomeDBiQ8BVU5.
TreeFamiTF106351.

Enzyme and pathway databases

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

Miscellaneous databases

PROiQ8BVU5.
SOURCEiSearch...

Gene expression databases

BgeeiQ8BVU5.
ExpressionAtlasiQ8BVU5. baseline and differential.
GenevisibleiQ8BVU5. MM.

Family and domain databases

Gene3Di3.90.79.10. 1 hit.
InterProiIPR000086. NUDIX_hydrolase_dom.
IPR015797. NUDIX_hydrolase_dom-like.
[Graphical view]
PfamiPF00293. NUDIX. 1 hit.
[Graphical view]
SUPFAMiSSF55811. SSF55811. 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: Head and Inner ear.
  2. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: C57BL/6J.
  3. "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].
    Strain: Czech II.
    Tissue: Mammary tumor.
  4. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Brain, Lung, Spleen and Testis.

Entry informationi

Entry nameiNUDT9_MOUSE
AccessioniPrimary (citable) accession number: Q8BVU5
Secondary accession number(s): A2AH31, Q3TZ68, Q8K1J4
Entry historyi
Integrated into UniProtKB/Swiss-Prot: June 7, 2005
Last sequence update: March 1, 2003
Last modified: June 8, 2016
This is version 101 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

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.