Reviewed, UniProtKB/Swiss-Prot Q9BW91 (NUDT9_HUMAN)

Names and origin

Protein names

Recommended name:
    ADP-ribose pyrophosphatase, mitochondrial
    EC=3.6.1.13
Alternative name(s):
    ADP-ribose diphosphatase
    Adenosine diphosphoribose pyrophosphatase
      Short name=ADPR-PPase
    ADP-ribose phosphohydrolase
    Nucleoside diphosphate-linked moiety X motif 9
      Short name=Nudix motif 9

Gene names

Name:	NUDT9
Synonyms:	NUDT10
ORF Names:	PSEC0099, UNQ3012/PRO9771

Organism

Homo sapiens (Human) [Complete proteome]

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Primates › Haplorrhini › Catarrhini › Hominidae › Homo

Protein attributes

Sequence length	350 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Evidence 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.

Ontologies

Keywords
Cellular component	Mitochondrion
Coding sequence diversity	Alternative splicing
Domain	Transit peptide
Ligand	Magnesium Manganese
Molecular function	Hydrolase
PTM	Phosphoprotein
Technical term	3D-structure Complete proteome
Gene Ontology (GO)
Biological process	cation transport Ref.1 Non-traceable author statement. Source: UniProtKB
Cellular component	mitochondrion Inferred from electronic annotation. Source: UniProtKB-SubCell
Molecular function	ADP-ribose diphosphatase activity Inferred from electronic annotation. Source: EC calcium activated cation channel activity Ref.1 Non-traceable author statement. Source: UniProtKB magnesium ion binding Inferred from electronic annotation. Source: UniProtKB-KW manganese ion binding Inferred from electronic annotation. Source: UniProtKB-KW
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 key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Transit peptide

1 – 46

46

Mitochondrion Potential

Chain

47 – 350

304

ADP-ribose pyrophosphatase, mitochondrial

PRO_0000019950

Regions

Motif

215 – 237

23

Nudix box

Amino acid modifications

Modified residue

68

1

Phosphoserine Ref.10

Modified residue

121

1

Phosphoserine Ref.11

Natural variations

Alternative sequence

1 – 50

50

Missing in isoform 2.

VSP_010552

Experimental info

Sequence conflict

118

1

S → G in AAM46068. Ref.4

Sequence conflict

293

1

E → V in BAC11601. Ref.7

Secondary structure

1

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350

Helix Strand Turn

Details...

Helix

64 – 66

3

Helix

82 – 84

3

Beta strand

97 – 100

4

Helix

102 – 105

4

Beta strand

126 – 128

3

Beta strand

155 – 160

6

Beta strand

163 – 178

16

Turn

190 – 192

3

Beta strand

197 – 203

7

Turn

205 – 207

3

Beta strand

209 – 211

3

Helix

223 – 235

13

Helix

238 – 240

3

Helix

245 – 256

12

Turn

257 – 259

3

Beta strand

260 – 268

9

Beta strand

276 – 292

17

Turn

293 – 297

5

Beta strand

307 – 313

7

Helix

324 – 335

12

Helix

345 – 347

3

Sequences

	Sequence		Length	Mass (Da)
	Isoform 1 (NUDT9a) [UniParc]. Last modified June 1, 2001. Version 1. Checksum: 2EA5B24B88FB3420	FASTA	350	39,125
	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
	Isoform 2 (NUDT9b). Checksum: 531993C757A82E49	FASTA	300	33,776
	10 20 30 40 50 60 MSGSNGSKEN SHNKARTSPY PGSKVERSQV PNEKVGWLVE WQDYKPVEYT AVSVLAGPRW 70 80 90 100 110 120 ADPQISESNF SPKFNEKDGH VERKSKNGLY EIENGRPRNP AGRTGLVGRG LLGRWGPNHA 130 140 150 160 170 180 ADPIITRWKR DSSGNKIMHP VSGKHILQFV AIKRKDCGEW AIPGGMVDPG EKISATLKRE 190 200 210 220 230 240 FGEEALNSLQ KTSAEKREIE EKLHKLFSQD HLVIYKGYVD DPRNTDNAWM ETEAVNYHDE 250 260 270 280 290 300 TGEIMDNLML EAGDDAGKVK WVDINDKLKL YASHSQFIKL VAEKRDAHWS EDSEADCHAL

References

	« Hide 'large scale' referencesShow '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. , 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. , 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]	"HRI human cDNA sequencing project." Ota T., Nishikawa T., Suzuki Y., Kawai-Hio Y., Hayashi K., Ishii S., Saito K., Yamamoto J., Wakamatsu A., Nagai T., Nakamura Y., Nagahari K., Sugano S., Isogai T. Submitted (SEP-2002) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
[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: Epithelium.
[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.
[12]	Colinge J., Superti-Furga G., Bennett K.L. Submitted (OCT-2008) to UniProtKB Cited for: IDENTIFICATION [LARGE SCALE ANALYSIS], MASS SPECTROMETRY.
[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

EMBLGenBankDDBJ

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.

IPI

IPI00031558.
IPI00415040.

RefSeq

NP_076952.1.
NP_932155.1.

UniGene

Hs.149500

3D structure databases

PDBPDBe

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
1Q33	X-ray	1.81	A	59-350	[»]
1QVJ	X-ray	1.91	A	59-350	[»]

ModBase

Search...

PTM databases

PhosphoSite

Q9BW91.

Proteomic databases

PRIDE

Q9BW91.

Genome annotation databases

Ensembl

ENSG00000170502. Homo sapiens. [Contig view]

GeneID

53343.

KEGG

hsa:53343.

UCSC

uc003hqq.1. human.
uc003hqr.1. human.

Organism-specific databases

GeneCards

GC04P088645.

H-InvDB

HIX0004359.

HGNC

HGNC:8056. NUDT9.

MIM

606022. gene.

PharmGKB

PA31842.

GenAtlas

Search...

Phylogenomic databases

HOGENOM

Q9BW91.

HOVERGEN

Q9BW91.

OMA

Q9BW91. QISESNF.

Enzyme and pathway databases

BRENDA

3.6.1.13. 247.

Gene expression databases

ArrayExpress

Q9BW91.

Bgee

Q9BW91.

CleanEx

HS_NUDT10.
HS_NUDT9.

GermOnline

ENSG00000170502. Homo sapiens.

Family and domain databases

InterPro

IPR000086. NUDIX_hydrolase_core.
[Graphical view]

Gene3D

G3DSA:3.90.79.10. NUDIX_hydrolase. 1 hit.

Pfam

PF00293. NUDIX. 1 hit.
[Graphical view]

PROSITE

PS00893. NUDIX. False negative.
[Graphical view]

ProtoNet

Search...

Other Resources

NextBio

55980.

SOURCE

Search...

Entry information

Entry name

NUDT9_HUMAN

Accession

Primary (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:	July 7, 2009
This is version 78 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

HPI (Human Proteome Initiative)