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Protein

ADP-ribose pyrophosphatase, mitochondrial

Gene

NUDT9

Organism
Homo sapiens (Human)
Status
Reviewed-Annotation score: Annotation score: 5 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

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Hydrolase

Keywords - Ligandi

Magnesium, Manganese

Enzyme and pathway databases

ReactomeiR-HSA-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
Synonyms:NUDT10
ORF Names:PSEC0099, UNQ3012/PRO9771
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
Proteomesi
  • UP000005640 Componenti: Chromosome 4

Organism-specific databases

HGNCiHGNC:8056. NUDT9.

Subcellular locationi

GO - Cellular componenti

  • extracellular exosome Source: UniProtKB
  • intracellular Source: UniProtKB
  • mitochondrial matrix Source: Reactome
Complete GO annotation...

Keywords - Cellular componenti

Mitochondrion

Pathology & Biotechi

Organism-specific databases

PharmGKBiPA31842.

Polymorphism and mutation databases

BioMutaiNUDT9.
DMDMi20455184.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Transit peptidei1 – 4646MitochondrionSequence analysisAdd
BLAST
Chaini47 – 350304ADP-ribose pyrophosphatase, mitochondrialPRO_0000019950Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei121 – 1211PhosphoserineCombined sources

Keywords - PTMi

Phosphoprotein

Proteomic databases

EPDiQ9BW91.
MaxQBiQ9BW91.
PaxDbiQ9BW91.
PRIDEiQ9BW91.

PTM databases

iPTMnetiQ9BW91.
PhosphoSiteiQ9BW91.

Expressioni

Tissue specificityi

Ubiquitously expressed but isoform 1 is the most predominant isoform.1 Publication

Inductioni

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

Gene expression databases

BgeeiQ9BW91.
CleanExiHS_NUDT10.
HS_NUDT9.
ExpressionAtlasiQ9BW91. baseline and differential.
GenevisibleiQ9BW91. HS.

Organism-specific databases

HPAiHPA036917.

Interactioni

Subunit structurei

Monomer. Interacts with GLOD4.2 Publications

Protein-protein interaction databases

BioGridi119744. 14 interactions.
IntActiQ9BW91. 2 interactions.
STRINGi9606.ENSP00000303575.

Structurei

Secondary structure

1
350
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi64 – 663Combined sources
Helixi82 – 843Combined sources
Beta strandi97 – 1004Combined sources
Helixi102 – 1054Combined sources
Beta strandi126 – 1283Combined sources
Beta strandi155 – 1606Combined sources
Beta strandi163 – 17816Combined sources
Turni190 – 1923Combined sources
Beta strandi197 – 2037Combined sources
Turni205 – 2073Combined sources
Beta strandi209 – 2113Combined sources
Helixi223 – 23513Combined sources
Helixi238 – 2403Combined sources
Helixi245 – 25612Combined sources
Turni257 – 2593Combined sources
Beta strandi260 – 2689Combined sources
Beta strandi276 – 29217Combined sources
Turni293 – 2975Combined sources
Beta strandi307 – 3137Combined sources
Helixi324 – 33512Combined sources
Helixi345 – 3473Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1Q33X-ray1.81A59-350[»]
1QVJX-ray1.91A59-350[»]
ProteinModelPortaliQ9BW91.
SMRiQ9BW91. Positions 59-350.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiQ9BW91.

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.
InParanoidiQ9BW91.
KOiK13988.
OMAiQISESNF.
OrthoDBiEOG7QNVMJ.
PhylomeDBiQ9BW91.
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]

Sequences (2)i

Sequence statusi: Complete.

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

This entry describes 2 isoformsi produced by alternative splicing. AlignAdd to basket

Isoform 1 (identifier: Q9BW91-1) [UniParc]FASTAAdd to basket

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.

« Hide

        10         20         30         40         50
MAGRLLGKAL AAVSLSLALA SVTIRSSRCR GIQAFRNSFS SSWFHLNTNV
60 70 80 90 100
MSGSNGSKEN SHNKARTSPY PGSKVERSQV PNEKVGWLVE WQDYKPVEYT
110 120 130 140 150
AVSVLAGPRW ADPQISESNF SPKFNEKDGH VERKSKNGLY EIENGRPRNP
160 170 180 190 200
AGRTGLVGRG LLGRWGPNHA ADPIITRWKR DSSGNKIMHP VSGKHILQFV
210 220 230 240 250
AIKRKDCGEW AIPGGMVDPG EKISATLKRE FGEEALNSLQ KTSAEKREIE
260 270 280 290 300
EKLHKLFSQD HLVIYKGYVD DPRNTDNAWM ETEAVNYHDE TGEIMDNLML
310 320 330 340 350
EAGDDAGKVK WVDINDKLKL YASHSQFIKL VAEKRDAHWS EDSEADCHAL
Length:350
Mass (Da):39,125
Last modified:June 1, 2001 - v1
Checksum:i2EA5B24B88FB3420
GO
Isoform 2 (identifier: Q9BW91-2) [UniParc]FASTAAdd to basket

Also known as: NUDT9b

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

Show »
Length:300
Mass (Da):33,776
Checksum:i531993C757A82E49
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti118 – 1181S → G in AAM46068 (Ref. 4) Curated
Sequence conflicti293 – 2931E → V in BAC11601 (PubMed:16303743).Curated

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei1 – 5050Missing in isoform 2. 3 PublicationsVSP_010552Add
BLAST

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
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.
CCDSiCCDS3620.1. [Q9BW91-1]
CCDS3621.1. [Q9BW91-2]
RefSeqiNP_001234940.1. NM_001248011.1.
NP_076952.1. NM_024047.4. [Q9BW91-1]
NP_932155.1. NM_198038.2. [Q9BW91-2]
XP_011530334.1. XM_011532032.1. [Q9BW91-2]
UniGeneiHs.149500.

Genome annotation databases

EnsembliENST00000302174; ENSP00000303575; ENSG00000170502. [Q9BW91-1]
ENST00000473942; ENSP00000421811; ENSG00000170502. [Q9BW91-2]
GeneIDi53343.
KEGGihsa:53343.
UCSCiuc003hqq.4. human. [Q9BW91-1]

Keywords - Coding sequence diversityi

Alternative splicing

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
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.
CCDSiCCDS3620.1. [Q9BW91-1]
CCDS3621.1. [Q9BW91-2]
RefSeqiNP_001234940.1. NM_001248011.1.
NP_076952.1. NM_024047.4. [Q9BW91-1]
NP_932155.1. NM_198038.2. [Q9BW91-2]
XP_011530334.1. XM_011532032.1. [Q9BW91-2]
UniGeneiHs.149500.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1Q33X-ray1.81A59-350[»]
1QVJX-ray1.91A59-350[»]
ProteinModelPortaliQ9BW91.
SMRiQ9BW91. Positions 59-350.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi119744. 14 interactions.
IntActiQ9BW91. 2 interactions.
STRINGi9606.ENSP00000303575.

PTM databases

iPTMnetiQ9BW91.
PhosphoSiteiQ9BW91.

Polymorphism and mutation databases

BioMutaiNUDT9.
DMDMi20455184.

Proteomic databases

EPDiQ9BW91.
MaxQBiQ9BW91.
PaxDbiQ9BW91.
PRIDEiQ9BW91.

Protocols and materials databases

DNASUi53343.
Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000302174; ENSP00000303575; ENSG00000170502. [Q9BW91-1]
ENST00000473942; ENSP00000421811; ENSG00000170502. [Q9BW91-2]
GeneIDi53343.
KEGGihsa:53343.
UCSCiuc003hqq.4. human. [Q9BW91-1]

Organism-specific databases

CTDi53343.
GeneCardsiNUDT9.
HGNCiHGNC:8056. NUDT9.
HPAiHPA036917.
MIMi606022. gene.
neXtProtiNX_Q9BW91.
PharmGKBiPA31842.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiKOG4195. Eukaryota.
ENOG410XPYY. LUCA.
GeneTreeiENSGT00390000017405.
HOGENOMiHOG000130166.
HOVERGENiHBG052693.
InParanoidiQ9BW91.
KOiK13988.
OMAiQISESNF.
OrthoDBiEOG7QNVMJ.
PhylomeDBiQ9BW91.
TreeFamiTF106351.

Enzyme and pathway databases

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

Miscellaneous databases

EvolutionaryTraceiQ9BW91.
GeneWikiiNUDT9.
GenomeRNAii53343.
PROiQ9BW91.
SOURCEiSearch...

Gene expression databases

BgeeiQ9BW91.
CleanExiHS_NUDT10.
HS_NUDT9.
ExpressionAtlasiQ9BW91. baseline and differential.
GenevisibleiQ9BW91. HS.

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

« Hide 'large scale' publications
  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] [Europe PMC] [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] [Europe PMC] [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] [Europe PMC] [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. 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.
    , 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] [Europe PMC] [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.
    , Aotsuka S., Sasaki N., Hattori A., Okumura K., Nagai K., Sugano S., Isogai T.
    DNA Res. 12:117-126(2005) [PubMed] [Europe PMC] [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] [Europe PMC] [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] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH GLOD4.
  10. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-121, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  11. "Quantitative phosphoproteomics reveals widespread full phosphorylation site occupancy during mitosis."
    Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L., Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S., Mann M.
    Sci. Signal. 3:RA3-RA3(2010) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-121, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  12. 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] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (1.81 ANGSTROMS) OF 59-350.

Entry informationi

Entry nameiNUDT9_HUMAN
AccessioniPrimary (citable) accession number: Q9BW91
Secondary accession number(s): Q8NBN1, Q8NCB9, Q8NG25
Entry historyi
Integrated into UniProtKB/Swiss-Prot: May 2, 2002
Last sequence update: June 1, 2001
Last modified: June 8, 2016
This is version 143 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (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.

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

Documents

  1. Human chromosome 4
    Human chromosome 4: entries, gene names and cross-references to MIM
  2. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  3. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  4. 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.