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Q9BW91 (NUDT9_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified January 25, 2012. Version 103. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (4) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Alt products·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended 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 names
Name:NUDT9
Synonyms:NUDT10
ORF Names:PSEC0099, UNQ3012/PRO9771
OrganismHomo sapiens (Human)
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length350 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

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

Catalytic activity

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

Cofactor

Magnesium. Ref.2 Ref.3

Manganese. Ref.2 Ref.3

Subunit structure

Monomer. Interacts with C17orf25. Ref.3 Ref.9

Subcellular location

Isoform 1: Mitochondrion Ref.2 Ref.3.

Tissue specificity

Ubiquitously expressed but isoform 1 is the most predominant isoform. Ref.3

Induction

Isoform 1 is inhibited by fluoride and N-acetyl-p-benzoquinoneimine. Ref.2

Sequence similarities

Belongs to the Nudix hydrolase family. NudF subfamily.

Contains 1 nudix hydrolase domain.

Ontologies

Keywords
   Cellular componentMitochondrion
   Coding sequence diversityAlternative splicing
   DomainTransit peptide
   LigandMagnesium
Manganese
   Molecular functionHydrolase
   PTMPhosphoprotein
   Technical term3D-structure
Complete proteome
Reference proteome
Gene Ontology (GO)
   Cellular componentmitochondrion

Inferred from electronic annotation. Source: UniProtKB-SubCell

   Molecular functionADP-ribose diphosphatase activity

Inferred from electronic annotation. Source: EC

Complete GO annotation...

Alternative products

This entry describes 2 isoforms produced by alternative splicing. [Align] [Select]
Isoform 1 (identifier: Q9BW91-1)

Also known as: NUDT9a;

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.
Isoform 2 (identifier: Q9BW91-2)

Also known as: NUDT9b;

The sequence of this isoform differs from the canonical sequence as follows:
     1-50: Missing.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Transit peptide1 – 4646Mitochondrion Potential
Chain47 – 350304ADP-ribose pyrophosphatase, mitochondrial
PRO_0000019950

Regions

Domain178 – 334157Nudix hydrolase
Motif215 – 23723Nudix box

Amino acid modifications

Modified residue681Phosphoserine Ref.10
Modified residue1211Phosphoserine Ref.11

Natural variations

Alternative sequence1 – 5050Missing in isoform 2.
VSP_010552

Experimental info

Sequence conflict1181S → G in AAM46068. Ref.4
Sequence conflict2931E → V in BAC11601. Ref.7

Secondary structure

........................................ 350
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
Isoform 1 (NUDT9a) [UniParc].

Last modified June 1, 2001. Version 1.
Checksum: 2EA5B24B88FB3420

FASTA35039,125
        10         20         30         40         50         60 
MAGRLLGKAL AAVSLSLALA SVTIRSSRCR GIQAFRNSFS SSWFHLNTNV MSGSNGSKEN 

        70         80         90        100        110        120 
SHNKARTSPY PGSKVERSQV PNEKVGWLVE WQDYKPVEYT AVSVLAGPRW ADPQISESNF 

       130        140        150        160        170        180 
SPKFNEKDGH VERKSKNGLY EIENGRPRNP AGRTGLVGRG LLGRWGPNHA ADPIITRWKR 

       190        200        210        220        230        240 
DSSGNKIMHP VSGKHILQFV AIKRKDCGEW AIPGGMVDPG EKISATLKRE FGEEALNSLQ 

       250        260        270        280        290        300 
KTSAEKREIE EKLHKLFSQD HLVIYKGYVD DPRNTDNAWM ETEAVNYHDE TGEIMDNLML 

       310        320        330        340        350 
EAGDDAGKVK WVDINDKLKL YASHSQFIKL VAEKRDAHWS EDSEADCHAL 

« Hide

Isoform 2 (NUDT9b) [UniParc].

Checksum: 531993C757A82E49
Show »

FASTA30033,776

References

« Hide 'large scale' references
[1]"ADP-ribose gating of the calcium-permeable LTRPC2 channel revealed by Nudix motif homology."
Perraud A.-L., Fleig A., Dunn C.A., Bagley L.A., Launay P., Schmitz C., Stokes A.J., Zhu Q., Bessman M.J., Penner R., Kinet J.-P., Scharenberg A.M.
Nature 411:595-599(2001) [PubMed: 11385575] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
Tissue: Spleen.
[2]"Cloning, expression and characterisation of a human Nudix hydrolase specific for adenosine 5'-diphosphoribose (ADP-ribose)."
Lin S., Gasmi L., Xie Y., Ying K., Gu S., Wang Z., Jin H., Chao Y., Wu C., Zhou Z., Tang R., Mao Y., McLennan A.G.
Biochim. Biophys. Acta 1594:127-135(2002) [PubMed: 11825615] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1 AND 2), COFACTOR, SUBCELLULAR LOCATION, INDUCTION.
Tissue: Fetal brain.
[3]"NUDT9, a member of the Nudix hydrolase family, is an evolutionarily conserved mitochondrial ADP-ribose pyrophosphatase."
Perraud A.-L., Shen B., Dunn C.A., Rippe K., Smith M.K., Bessman M.J., Stoddard B.L., Scharenberg A.M.
J. Biol. Chem. 278:1794-1801(2003) [PubMed: 12427752] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1 AND 2), COFACTOR, SUBUNIT, SUBCELLULAR LOCATION, TISSUE SPECIFICITY.
Tissue: Spleen.
[4]"NUDT10, a new member of human nudix hydrolase family."
Lin S., Ying K.
Submitted (JUN-2002) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
Tissue: Brain.
[5]"The secreted protein discovery initiative (SPDI), a large-scale effort to identify novel human secreted and transmembrane proteins: a bioinformatics assessment."
Clark H.F., Gurney A.L., Abaya E., Baker K., Baldwin D.T., Brush J., Chen J., Chow B., Chui C., Crowley C., Currell B., Deuel B., Dowd P., Eaton D., Foster J.S., Grimaldi C., Gu Q., Hass P.E. expand/collapse author list , Heldens S., Huang A., Kim H.S., Klimowski L., Jin Y., Johnson S., Lee J., Lewis L., Liao D., Mark M.R., Robbie E., Sanchez C., Schoenfeld J., Seshagiri S., Simmons L., Singh J., Smith V., Stinson J., Vagts A., Vandlen R.L., Watanabe C., Wieand D., Woods K., Xie M.-H., Yansura D.G., Yi S., Yu G., Yuan J., Zhang M., Zhang Z., Goddard A.D., Wood W.I., Godowski P.J., Gray A.M.
Genome Res. 13:2265-2270(2003) [PubMed: 12975309] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
[6]"Complete sequencing and characterization of 21,243 full-length human cDNAs."
Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S. expand/collapse author list , Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.
Nat. Genet. 36:40-45(2004) [PubMed: 14702039] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
[7]"Signal sequence and keyword trap in silico for selection of full-length human cDNAs encoding secretion or membrane proteins from oligo-capped cDNA libraries."
Otsuki T., Ota T., Nishikawa T., Hayashi K., Suzuki Y., Yamamoto J., Wakamatsu A., Kimura K., Sakamoto K., Hatano N., Kawai Y., Ishii S., Saito K., Kojima S., Sugiyama T., Ono T., Okano K., Yoshikawa Y. expand/collapse author list , Aotsuka S., Sasaki N., Hattori A., Okumura K., Nagai K., Sugano S., Isogai T.
DNA Res. 12:117-126(2005) [PubMed: 16303743] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
Tissue: Teratocarcinoma.
[8]"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: 15489334] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
Tissue: Brain.
[9]"Interaction of C17orf25 with ADP-ribose pyrophosphatase NUDT9 detected via yeast two-hybrid method."
Zhang H.-T., Yan Z.-Q., Hu X.-B., Yang S.-L., Gong Y.
Sheng Wu Hua Xue Yu Sheng Wu Wu Li Xue Bao 35:747-751(2003) [PubMed: 12897971] [Abstract]
Cited for: INTERACTION WITH C17ORF25.
[10]"Improved titanium dioxide enrichment of phosphopeptides from HeLa cells and high confident phosphopeptide identification by cross-validation of MS/MS and MS/MS/MS spectra."
Yu L.-R., Zhu Z., Chan K.C., Issaq H.J., Dimitrov D.S., Veenstra T.D.
J. Proteome Res. 6:4150-4162(2007) [PubMed: 17924679] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-68, MASS SPECTROMETRY.
Tissue: Cervix carcinoma.
[11]"A quantitative atlas of mitotic phosphorylation."
Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E., Elledge S.J., Gygi S.P.
Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008) [PubMed: 18669648] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-121, MASS SPECTROMETRY.
Tissue: Cervix carcinoma.
[12]"Initial characterization of the human central proteome."
Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.
BMC Syst. Biol. 5:17-17(2011) [PubMed: 21269460] [Abstract]
Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[13]"The crystal structure and mutational analysis of human NUDT9."
Shen B.W., Perraud A.-L., Scharenberg A., Stoddard B.L.
J. Mol. Biol. 332:385-398(2003) [PubMed: 12948489] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (1.81 ANGSTROMS) OF 59-350.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AY026252 mRNA. Translation: AAK07671.1.
AY359123 mRNA. Translation: AAQ89480.1.
AF273028 mRNA. Translation: AAM46068.1.
AK074845 mRNA. Translation: BAC11239.1.
AK075408 mRNA. Translation: BAC11601.1.
BC000542 mRNA. Translation: AAH00542.1.
IPIIPI00031558.
IPI00415040.
RefSeqNP_001234940.1. NM_001248011.1.
NP_076952.1. NM_024047.4.
NP_932155.1. NM_198038.2.
UniGeneHs.149500.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
1Q33X-ray1.81A59-350[»]
1QVJX-ray1.91A59-350[»]
ProteinModelPortalQ9BW91.
SMRQ9BW91. Positions 59-350.
ModBaseSearch...

Protein-protein interaction databases

IntActQ9BW91. 2 interactions.
STRINGQ9BW91.

PTM databases

PhosphoSiteQ9BW91.

Polymorphism databases

DMDM20455184.

Proteomic databases

PRIDEQ9BW91.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000302174; ENSP00000303575; ENSG00000170502.
GeneID53343.
KEGGhsa:53343.
UCSCuc003hqq.1. human.
uc003hqr.1. human.

Organism-specific databases

CTD53343.
GeneCardsGC04P088343.
HGNCHGNC:8056. NUDT9.
HPAHPA036917.
MIM606022. gene.
neXtProtNX_Q9BW91.
GenAtlasSearch...

Phylogenomic databases

eggNOGprNOG05572.
GeneTreeENSGT00390000017405.
HOGENOMHBG379993.
HOVERGENHBG052693.
InParanoidQ9BW91.
OMAQISESNF.
OrthoDBEOG4VHK76.
PhylomeDBQ9BW91.

Enzyme and pathway databases

BRENDA3.6.1.13. 2681.

Gene expression databases

ArrayExpressQ9BW91.
BgeeQ9BW91.
CleanExHS_NUDT10.
HS_NUDT9.
GenevestigatorQ9BW91.
GermOnlineENSG00000170502. Homo sapiens.

Family and domain databases

InterProIPR000086. NUDIX_hydrolase_dom.
IPR015797. NUDIX_hydrolase_dom-like.
[Graphical view]
Gene3DG3DSA:3.90.79.10. NUDIX_hydrolase. 1 hit.
KOK13988.
PfamPF00293. NUDIX. 1 hit.
[Graphical view]
SUPFAMSSF55811. NUDIX_hydrolase. 1 hit.
PROSITEPS51462. NUDIX. 1 hit.
PS00893. NUDIX_BOX. False negative.
[Graphical view]
ProtoNetSearch...

Other

NextBio55980.
SOURCESearch...

Entry information

Entry nameNUDT9_HUMAN
AccessionPrimary (citable) accession number: Q9BW91
Secondary accession number(s): Q8NBN1, Q8NCB9, Q8NG25
Entry history
Integrated into UniProtKB/Swiss-Prot: May 2, 2002
Last sequence update: June 1, 2001
Last modified: January 25, 2012
This is version 103 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (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.

Relevant documents

Human chromosome 4

Human chromosome 4: entries, gene names and cross-references to MIM

MIM cross-references

Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

SIMILARITY comments

Index of protein domains and families