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ADP-sugar pyrophosphatase (EC 3.6.1.13) (8-oxo-dGDP phosphatase) (EC 3.6.1.58) (Nuclear ATP-synthesis protein NUDIX5) (EC 2.7.7.96) (Nucleoside diphosphate-linked moiety X motif 5) (Nudix motif 5) (hNUDT5) (YSA1H)

 NUDT5_HUMAN             Reviewed;         219 AA.
Q9UKK9; A8K516; Q6IAG0; Q9UH49;
02-MAY-2002, integrated into UniProtKB/Swiss-Prot.
01-MAY-2000, sequence version 1.
07-NOV-2018, entry version 167.
RecName: Full=ADP-sugar pyrophosphatase;
EC=3.6.1.13 {ECO:0000269|PubMed:17052728, ECO:0000269|PubMed:21389046};
AltName: Full=8-oxo-dGDP phosphatase;
EC=3.6.1.58 {ECO:0000269|PubMed:17052728, ECO:0000269|PubMed:19699693, ECO:0000269|PubMed:21389046};
AltName: Full=Nuclear ATP-synthesis protein NUDIX5 {ECO:0000305|PubMed:27257257};
EC=2.7.7.96 {ECO:0000269|PubMed:27257257};
AltName: Full=Nucleoside diphosphate-linked moiety X motif 5 {ECO:0000305};
Short=Nudix motif 5 {ECO:0000305};
Short=hNUDT5 {ECO:0000303|PubMed:21768126};
AltName: Full=YSA1H {ECO:0000303|PubMed:10567213};
Name=NUDT5; Synonyms=NUDIX5 {ECO:0000303|PubMed:27257257};
ORFNames=HSPC115 {ECO:0000303|PubMed:11042152};
Homo sapiens (Human).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
Catarrhini; Hominidae; Homo.
NCBI_TaxID=9606;
[1]
NUCLEOTIDE SEQUENCE [MRNA], AND FUNCTION.
PubMed=10567213; DOI=10.1042/bj3440331;
Gasmi L., Cartwright J.L., McLennan A.G.;
"Cloning, expression and characterization of YSA1H, a human adenosine
5'-diphosphosugar pyrophosphatase possessing a MutT motif.";
Biochem. J. 344:331-337(1999).
[2]
NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, AND TISSUE SPECIFICITY.
PubMed=10722730; DOI=10.1074/jbc.275.12.8844;
Yang H., Slupska M.M., Wei Y.-F., Tai J.H., Luther W.M., Xia Y.-R.,
Shih D.M., Chiang J.-H., Baikalov C., Fitz-Gibbon S., Phan I.T.,
Conrad A., Miller J.H.;
"Cloning and characterization of a new member of the Nudix hydrolases
from human and mouse.";
J. Biol. Chem. 275:8844-8853(2000).
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
TISSUE=Umbilical cord blood;
PubMed=11042152; DOI=10.1101/gr.140200;
Zhang Q.-H., Ye M., Wu X.-Y., Ren S.-X., Zhao M., Zhao C.-J., Fu G.,
Shen Y., Fan H.-Y., Lu G., Zhong M., Xu X.-R., Han Z.-G., Zhang J.-W.,
Tao J., Huang Q.-H., Zhou J., Hu G.-X., Gu J., Chen S.-J., Chen Z.;
"Cloning and functional analysis of cDNAs with open reading frames for
300 previously undefined genes expressed in CD34+ hematopoietic
stem/progenitor cells.";
Genome Res. 10:1546-1560(2000).
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Ebert L., Schick M., Neubert P., Schatten R., Henze S., Korn B.;
"Cloning of human full open reading frames in Gateway(TM) system entry
vector (pDONR201).";
Submitted (JUN-2004) to the EMBL/GenBank/DDBJ databases.
[5]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
PubMed=14702039; DOI=10.1038/ng1285;
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.;
"Complete sequencing and characterization of 21,243 full-length human
cDNAs.";
Nat. Genet. 36:40-45(2004).
[6]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L.,
Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R.,
Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V.,
Hannenhalli S., Turner R., Yooseph S., Lu F., Nusskern D.R.,
Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H.,
Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G.,
Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W.,
Venter J.C.;
Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
[7]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
TISSUE=Placenta;
PubMed=15489334; DOI=10.1101/gr.2596504;
The MGC Project Team;
"The status, quality, and expansion of the NIH full-length cDNA
project: the Mammalian Gene Collection (MGC).";
Genome Res. 14:2121-2127(2004).
[8]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-74, AND IDENTIFICATION
BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=15592455; DOI=10.1038/nbt1046;
Rush J., Moritz A., Lee K.A., Guo A., Goss V.L., Spek E.J., Zhang H.,
Zha X.-M., Polakiewicz R.D., Comb M.J.;
"Immunoaffinity profiling of tyrosine phosphorylation in cancer
cells.";
Nat. Biotechnol. 23:94-101(2005).
[9]
ACETYLATION [LARGE SCALE ANALYSIS] AT MET-1, AND IDENTIFICATION BY
MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=19413330; DOI=10.1021/ac9004309;
Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J.,
Mohammed S.;
"Lys-N and trypsin cover complementary parts of the phosphoproteome in
a refined SCX-based approach.";
Anal. Chem. 81:4493-4501(2009).
[10]
FUNCTION, CATALYTIC ACTIVITY, AND BIOPHYSICOCHEMICAL PROPERTIES.
PubMed=19699693; DOI=10.1016/j.dnarep.2009.07.011;
Kamiya H., Hori M., Arimori T., Sekiguchi M., Yamagata Y.,
Harashima H.;
"NUDT5 hydrolyzes oxidized deoxyribonucleoside diphosphates with broad
substrate specificity.";
DNA Repair 8:1250-1254(2009).
[11]
ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-210 AND LYS-218, AND
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=19608861; DOI=10.1126/science.1175371;
Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M.,
Walther T.C., Olsen J.V., Mann M.;
"Lysine acetylation targets protein complexes and co-regulates major
cellular functions.";
Science 325:834-840(2009).
[12]
ACETYLATION [LARGE SCALE ANALYSIS] AT MET-1, PHOSPHORYLATION [LARGE
SCALE ANALYSIS] AT SER-10, AND IDENTIFICATION BY MASS SPECTROMETRY
[LARGE SCALE ANALYSIS].
TISSUE=Cervix carcinoma;
PubMed=20068231; DOI=10.1126/scisignal.2000475;
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.;
"Quantitative phosphoproteomics reveals widespread full
phosphorylation site occupancy during mitosis.";
Sci. Signal. 3:RA3-RA3(2010).
[13]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=21269460; DOI=10.1186/1752-0509-5-17;
Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P.,
Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.;
"Initial characterization of the human central proteome.";
BMC Syst. Biol. 5:17-17(2011).
[14]
FUNCTION, CATALYTIC ACTIVITY, AND BIOPHYSICOCHEMICAL PROPERTIES.
PubMed=21389046; DOI=10.1093/jb/mvr028;
Ito R., Sekiguchi M., Setoyama D., Nakatsu Y., Yamagata Y.,
Hayakawa H.;
"Cleavage of oxidized guanine nucleotide and ADP sugar by human NUDT5
protein.";
J. Biochem. 149:731-738(2011).
[15]
ACETYLATION [LARGE SCALE ANALYSIS] AT MET-1, PHOSPHORYLATION [LARGE
SCALE ANALYSIS] AT SER-3, AND IDENTIFICATION BY MASS SPECTROMETRY
[LARGE SCALE ANALYSIS].
PubMed=21406692; DOI=10.1126/scisignal.2001570;
Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J.,
Johansen P.T., Kratchmarova I., Kassem M., Mann M., Olsen J.V.,
Blagoev B.;
"System-wide temporal characterization of the proteome and
phosphoproteome of human embryonic stem cell differentiation.";
Sci. Signal. 4:RS3-RS3(2011).
[16]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=22905912; DOI=10.1021/pr300539b;
Rosenow A., Noben J.P., Jocken J., Kallendrusch S.,
Fischer-Posovszky P., Mariman E.C., Renes J.;
"Resveratrol-induced changes of the human adipocyte secretion
profile.";
J. Proteome Res. 11:4733-4743(2012).
[17]
ACETYLATION [LARGE SCALE ANALYSIS] AT MET-1, AND IDENTIFICATION BY
MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=22223895; DOI=10.1074/mcp.M111.015131;
Bienvenut W.V., Sumpton D., Martinez A., Lilla S., Espagne C.,
Meinnel T., Giglione C.;
"Comparative large-scale characterisation of plant vs. mammal proteins
reveals similar and idiosyncratic N-alpha acetylation features.";
Mol. Cell. Proteomics 11:M111.015131-M111.015131(2012).
[18]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-3, AND IDENTIFICATION BY
MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Erythroleukemia;
PubMed=23186163; DOI=10.1021/pr300630k;
Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J.,
Mohammed S.;
"Toward a comprehensive characterization of a human cancer cell
phosphoproteome.";
J. Proteome Res. 12:260-271(2013).
[19]
FUNCTION, SUBCELLULAR LOCATION, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL
PROPERTIES, SUBUNIT, INDUCTION, INTERACTION WITH PARG, PHOSPHORYLATION
AT THR-45, AND MUTAGENESIS OF THR-45 AND GLU-112.
PubMed=27257257; DOI=10.1126/science.aad9335;
Wright R.H., Lioutas A., Le Dily F., Soronellas D., Pohl A., Bonet J.,
Nacht A.S., Samino S., Font-Mateu J., Vicent G.P., Wierer M.,
Trabado M.A., Schelhorn C., Carolis C., Macias M.J., Yanes O.,
Oliva B., Beato M.;
"ADP-ribose-derived nuclear ATP synthesis by NUDIX5 is required for
chromatin remodeling.";
Science 352:1221-1225(2016).
[20]
SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-42, AND IDENTIFICATION BY
MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=28112733; DOI=10.1038/nsmb.3366;
Hendriks I.A., Lyon D., Young C., Jensen L.J., Vertegaal A.C.,
Nielsen M.L.;
"Site-specific mapping of the human SUMO proteome reveals co-
modification with phosphorylation.";
Nat. Struct. Mol. Biol. 24:325-336(2017).
[21]
X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS) OF 1-210 IN COMPLEX WITH AMP;
MAGNESIUM IONS AND ADP-RIBOSE, FUNCTION, CATALYTIC ACTIVITY, SUBUNIT,
AND COFACTOR.
PubMed=17052728; DOI=10.1016/j.jmb.2006.09.078;
Zha M., Zhong C., Peng Y., Hu H., Ding J.;
"Crystal structures of human NUDT5 reveal insights into the structural
basis of the substrate specificity.";
J. Mol. Biol. 364:1021-1033(2006).
[22]
X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS) OF 1-210 IN COMPLEX WITH AMPCPR
AND MAGNESIUM IONS, COFACTOR, MUTAGENESIS OF TRP-28; TRP-46; ARG-51;
ARG-84; LEU-98; GLU-112; GLU-116 AND GLU-166, AND SUBUNIT.
PubMed=18462755; DOI=10.1016/j.jmb.2008.04.006;
Zha M., Guo Q., Zhang Y., Yu B., Ou Y., Zhong C., Ding J.;
"Molecular mechanism of ADP-ribose hydrolysis by human NUDT5 from
structural and kinetic studies.";
J. Mol. Biol. 379:568-578(2008).
[23]
X-RAY CRYSTALLOGRAPHY (2.05 ANGSTROMS) OF 13-208 IN COMPLEX WITH
8-OXO-DGDP; 8-OXO-DGMP; 8-OXO-DADP AND MANGANESE IONS, COFACTOR, AND
SUBUNIT.
PubMed=21768126; DOI=10.1093/nar/gkr575;
Arimori T., Tamaoki H., Nakamura T., Kamiya H., Ikemizu S., Takagi Y.,
Ishibashi T., Harashima H., Sekiguchi M., Yamagata Y.;
"Diverse substrate recognition and hydrolysis mechanisms of human
NUDT5.";
Nucleic Acids Res. 39:8972-8983(2011).
-!- FUNCTION: Enzyme that can either act as an ADP-sugar
pyrophosphatase in absence of diphosphate or catalyze the
synthesis of ATP in presence of diphosphate (PubMed:27257257). In
absence of diphosphate, hydrolyzes with similar activities various
modified nucleoside diphosphates such as ADP-ribose, ADP-mannose,
ADP-glucose, 8-oxo-GDP and 8-oxo-dGDP (PubMed:10567213,
PubMed:10722730, PubMed:19699693, PubMed:21389046,
PubMed:17052728). Can also hydrolyze other nucleotide sugars with
low activity (PubMed:19699693, PubMed:21389046). In presence of
diphosphate, mediates the synthesis of ATP in the nucleus by
catalyzing the conversion of ADP-ribose to ATP and ribose 5-
phosphate. Nuclear ATP synthesis takes place when dephosphorylated
at Thr-45 (PubMed:27257257). Nuclear ATP generation is required
for extensive chromatin remodeling events that are energy-
consuming (PubMed:27257257). Does not play a role in U8 snoRNA
decapping activity (By similarity). Binds U8 snoRNA (By
similarity). {ECO:0000250|UniProtKB:Q9JKX6,
ECO:0000269|PubMed:10567213, ECO:0000269|PubMed:10722730,
ECO:0000269|PubMed:17052728, ECO:0000269|PubMed:19699693,
ECO:0000269|PubMed:21389046, ECO:0000269|PubMed:27257257}.
-!- CATALYTIC ACTIVITY: ATP + D-ribose 5-phosphate = diphosphate +
ADP-D-ribose. {ECO:0000269|PubMed:27257257}.
-!- CATALYTIC ACTIVITY: ADP-D-ribose + H(2)O = AMP + D-ribose 5-
phosphate. {ECO:0000269|PubMed:17052728,
ECO:0000269|PubMed:21389046}.
-!- CATALYTIC ACTIVITY: 8-oxo-dGDP + H(2)O = 8-oxo-dGMP + phosphate.
{ECO:0000269|PubMed:17052728, ECO:0000269|PubMed:19699693,
ECO:0000269|PubMed:21389046}.
-!- COFACTOR:
Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
Evidence={ECO:0000269|PubMed:17052728,
ECO:0000269|PubMed:18462755, ECO:0000269|PubMed:21768126};
Note=Binds 3 Mg(2+) ions per subunit.
{ECO:0000269|PubMed:17052728, ECO:0000269|PubMed:18462755,
ECO:0000269|PubMed:21768126};
-!- BIOPHYSICOCHEMICAL PROPERTIES:
Kinetic parameters:
KM=2.1 uM for 8-oxo-dGDP {ECO:0000269|PubMed:19699693};
KM=2.9 uM for 8-oxo-dADP {ECO:0000269|PubMed:19699693};
KM=8.8 uM for 2-oxo-dADP {ECO:0000269|PubMed:19699693};
KM=4.0 uM for 5-CHO-dUDP {ECO:0000269|PubMed:19699693};
KM=7.6 uM for dGDP {ECO:0000269|PubMed:19699693};
KM=12.6 uM for dADP {ECO:0000269|PubMed:19699693};
KM=3.8 uM for 8-oxo-dGDP (at pH 8.0)
{ECO:0000269|PubMed:21389046};
KM=3.5 uM for 8-oxo-dGDP (at pH 10.0)
{ECO:0000269|PubMed:21389046};
KM=1.9 uM for ADP-D-ribose (at pH 8.0)
{ECO:0000269|PubMed:21389046};
KM=36 uM for 8-oxo-dGTP (at pH 10.0)
{ECO:0000269|PubMed:21389046};
KM=42.6 uM for ADP-D-ribose (in the presence of diphosphate)
{ECO:0000269|PubMed:27257257};
Vmax=11 pmol/min/ug enzyme with 8-oxo-dGDP as substrate (at pH
8.0) {ECO:0000269|PubMed:21389046};
Vmax=2400 pmol/min/ug enzyme with ADP-D-ribose as substrate (at
pH 8.0) {ECO:0000269|PubMed:21389046};
Vmax=46 pmol/min/ug enzyme with 8-oxo-dGDP as substrate (at pH
10.0) {ECO:0000269|PubMed:21389046};
Vmax=1.7 pmol/min/ug enzyme with 8-oxo-dGTP as substrate (at pH
10.0) {ECO:0000269|PubMed:21389046};
Note=kcat is 0.369 min(-1) for 8-OH-dGDP. kcat is 0.538 min(-1)
for 8-OH-dADP. kcat is 0.226 min(-1) for 2-OH-dADP. kcat is
0.209 min(-1) for 5-CHO-dUDP. kcat is 0.929 min(-1) for dGDP.
kcat is 0.365 min(-1) for dADP. {ECO:0000269|PubMed:19699693};
-!- SUBUNIT: Homodimer (PubMed:27257257, PubMed:17052728,
PubMed:18462755, PubMed:21768126). Interacts with PARG
(PubMed:27257257). {ECO:0000269|PubMed:17052728,
ECO:0000269|PubMed:18462755, ECO:0000269|PubMed:21768126,
ECO:0000269|PubMed:27257257}.
-!- SUBCELLULAR LOCATION: Nucleus {ECO:0000305|PubMed:27257257}.
-!- TISSUE SPECIFICITY: Widely expressed. Most abundant in liver.
{ECO:0000269|PubMed:10722730}.
-!- INDUCTION: Overexpressed in cancer patients with a poor outcome.
{ECO:0000269|PubMed:27257257}.
-!- PTM: Phosphorylation at Thr-45 is required for homodimer
stability; dephosphorylation results in destabilization of the
homodimer. Dephosphorylation at Thr-45 promotes the ATP-synthesis
activity. {ECO:0000269|PubMed:27257257}.
-!- SIMILARITY: Belongs to the Nudix hydrolase family. {ECO:0000305}.
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EMBL; AF155832; AAF06734.1; -; mRNA.
EMBL; AF218818; AAF25479.1; -; mRNA.
EMBL; AF161464; AAF29079.1; -; mRNA.
EMBL; CR457195; CAG33476.1; -; mRNA.
EMBL; AK291131; BAF83820.1; -; mRNA.
EMBL; CH471072; EAW86322.1; -; Genomic_DNA.
EMBL; BC000025; AAH00025.1; -; mRNA.
CCDS; CCDS7089.1; -.
RefSeq; NP_054861.2; NM_014142.3.
UniGene; Hs.555956; -.
UniGene; Hs.656304; -.
PDB; 2DSB; X-ray; 2.50 A; A/B/C/D=1-219.
PDB; 2DSC; X-ray; 2.00 A; A/B=1-210.
PDB; 2DSD; X-ray; 2.60 A; A/B=1-210.
PDB; 3AC9; X-ray; 2.10 A; A/B=14-208.
PDB; 3ACA; X-ray; 2.05 A; A/B=13-208.
PDB; 3BM4; X-ray; 2.00 A; A/B=1-210.
PDB; 3L85; X-ray; 2.30 A; A/B=14-208.
PDB; 5NQR; X-ray; 2.20 A; A/B=1-219.
PDB; 5NWH; X-ray; 2.60 A; A/B=1-219.
PDB; 6GRU; X-ray; 1.93 A; A/B/C/D=1-208.
PDBsum; 2DSB; -.
PDBsum; 2DSC; -.
PDBsum; 2DSD; -.
PDBsum; 3AC9; -.
PDBsum; 3ACA; -.
PDBsum; 3BM4; -.
PDBsum; 3L85; -.
PDBsum; 5NQR; -.
PDBsum; 5NWH; -.
PDBsum; 6GRU; -.
ProteinModelPortal; Q9UKK9; -.
SMR; Q9UKK9; -.
BioGrid; 116335; 27.
IntAct; Q9UKK9; 13.
MINT; Q9UKK9; -.
STRING; 9606.ENSP00000419628; -.
iPTMnet; Q9UKK9; -.
PhosphoSitePlus; Q9UKK9; -.
BioMuta; NUDT5; -.
EPD; Q9UKK9; -.
MaxQB; Q9UKK9; -.
PaxDb; Q9UKK9; -.
PeptideAtlas; Q9UKK9; -.
PRIDE; Q9UKK9; -.
ProteomicsDB; 84813; -.
DNASU; 11164; -.
Ensembl; ENST00000491614; ENSP00000419628; ENSG00000165609.
Ensembl; ENST00000537776; ENSP00000445116; ENSG00000165609.
GeneID; 11164; -.
KEGG; hsa:11164; -.
UCSC; uc001ilj.4; human.
CTD; 11164; -.
EuPathDB; HostDB:ENSG00000165609.12; -.
GeneCards; NUDT5; -.
HGNC; HGNC:8052; NUDT5.
HPA; HPA019827; -.
MIM; 609230; gene.
neXtProt; NX_Q9UKK9; -.
OpenTargets; ENSG00000165609; -.
PharmGKB; PA31838; -.
eggNOG; KOG3041; Eukaryota.
eggNOG; COG0494; LUCA.
GeneTree; ENSGT00390000006280; -.
HOGENOM; HOG000174302; -.
HOVERGEN; HBG052691; -.
InParanoid; Q9UKK9; -.
KO; K13987; -.
PhylomeDB; Q9UKK9; -.
TreeFam; TF106347; -.
BioCyc; MetaCyc:HS09255-MONOMER; -.
BRENDA; 3.6.1.13; 2681.
BRENDA; 3.6.1.58; 2681.
Reactome; R-HSA-2393930; Phosphate bond hydrolysis by NUDT proteins.
SABIO-RK; Q9UKK9; -.
ChiTaRS; NUDT5; human.
EvolutionaryTrace; Q9UKK9; -.
GeneWiki; NUDT5; -.
GenomeRNAi; 11164; -.
PRO; PR:Q9UKK9; -.
Proteomes; UP000005640; Chromosome 10.
Bgee; ENSG00000165609; Expressed in 195 organ(s), highest expression level in liver.
CleanEx; HS_NUDT5; -.
ExpressionAtlas; Q9UKK9; baseline and differential.
Genevisible; Q9UKK9; HS.
GO; GO:0005829; C:cytosol; TAS:Reactome.
GO; GO:0070062; C:extracellular exosome; HDA:UniProtKB.
GO; GO:0005622; C:intracellular; NAS:UniProtKB.
GO; GO:0005634; C:nucleus; IDA:UniProtKB.
GO; GO:0044715; F:8-oxo-dGDP phosphatase activity; IDA:UniProtKB.
GO; GO:0047631; F:ADP-ribose diphosphatase activity; IDA:UniProtKB.
GO; GO:0019144; F:ADP-sugar diphosphatase activity; IDA:UniProtKB.
GO; GO:0000287; F:magnesium ion binding; IDA:UniProtKB.
GO; GO:0016779; F:nucleotidyltransferase activity; IDA:UniProtKB.
GO; GO:0042803; F:protein homodimerization activity; IDA:UniProtKB.
GO; GO:0030515; F:snoRNA binding; ISS:UniProtKB.
GO; GO:1990966; P:ATP generation from poly-ADP-D-ribose; IDA:UniProtKB.
GO; GO:0006338; P:chromatin remodeling; IDA:UniProtKB.
GO; GO:0019303; P:D-ribose catabolic process; IDA:UniProtKB.
GO; GO:0034656; P:nucleobase-containing small molecule catabolic process; TAS:Reactome.
GO; GO:0009117; P:nucleotide metabolic process; NAS:ProtInc.
GO; GO:0009191; P:ribonucleoside diphosphate catabolic process; IDA:UniProtKB.
InterPro; IPR020476; Nudix_hydrolase.
InterPro; IPR015797; NUDIX_hydrolase-like_dom_sf.
InterPro; IPR020084; NUDIX_hydrolase_CS.
InterPro; IPR000086; NUDIX_hydrolase_dom.
Pfam; PF00293; NUDIX; 1.
PRINTS; PR00502; NUDIXFAMILY.
SUPFAM; SSF55811; SSF55811; 1.
PROSITE; PS51462; NUDIX; 1.
PROSITE; PS00893; NUDIX_BOX; 1.
1: Evidence at protein level;
3D-structure; Acetylation; Complete proteome; Hydrolase;
Isopeptide bond; Magnesium; Metal-binding; Nucleus; Phosphoprotein;
Polymorphism; Reference proteome; RNA-binding; Transferase;
Ubl conjugation.
CHAIN 1 219 ADP-sugar pyrophosphatase.
/FTId=PRO_0000057048.
DOMAIN 57 197 Nudix hydrolase. {ECO:0000255|PROSITE-
ProRule:PRU00794}.
REGION 46 47 Substrate binding; shared with dimeric
partner. {ECO:0000269|PubMed:17052728,
ECO:0000269|PubMed:18462755,
ECO:0000269|PubMed:21768126}.
MOTIF 97 118 Nudix box.
METAL 96 96 Magnesium 1; via carbonyl oxygen.
{ECO:0000269|PubMed:17052728,
ECO:0000269|PubMed:18462755,
ECO:0000269|PubMed:21768126}.
METAL 112 112 Magnesium 2.
{ECO:0000269|PubMed:17052728,
ECO:0000269|PubMed:18462755,
ECO:0000269|PubMed:21768126}.
METAL 112 112 Magnesium 3.
{ECO:0000269|PubMed:17052728,
ECO:0000269|PubMed:18462755,
ECO:0000269|PubMed:21768126}.
METAL 116 116 Magnesium 1.
{ECO:0000269|PubMed:17052728,
ECO:0000269|PubMed:18462755,
ECO:0000269|PubMed:21768126}.
METAL 116 116 Magnesium 3.
{ECO:0000269|PubMed:17052728,
ECO:0000269|PubMed:18462755,
ECO:0000269|PubMed:21768126}.
METAL 166 166 Magnesium 3.
{ECO:0000269|PubMed:17052728,
ECO:0000269|PubMed:18462755,
ECO:0000269|PubMed:21768126}.
BINDING 28 28 Substrate. {ECO:0000269|PubMed:17052728,
ECO:0000269|PubMed:18462755,
ECO:0000269|PubMed:21768126}.
BINDING 51 51 Substrate; shared with dimeric partner.
{ECO:0000269|PubMed:17052728,
ECO:0000269|PubMed:18462755,
ECO:0000269|PubMed:21768126}.
BINDING 84 84 Substrate. {ECO:0000269|PubMed:17052728,
ECO:0000269|PubMed:18462755,
ECO:0000269|PubMed:21768126}.
BINDING 98 98 Substrate; via amide nitrogen.
{ECO:0000269|PubMed:17052728}.
BINDING 133 133 Substrate. {ECO:0000269|PubMed:17052728}.
MOD_RES 1 1 N-acetylmethionine.
{ECO:0000244|PubMed:19413330,
ECO:0000244|PubMed:20068231,
ECO:0000244|PubMed:21406692,
ECO:0000244|PubMed:22223895}.
MOD_RES 3 3 Phosphoserine.
{ECO:0000244|PubMed:21406692,
ECO:0000244|PubMed:23186163}.
MOD_RES 10 10 Phosphoserine.
{ECO:0000244|PubMed:20068231}.
MOD_RES 45 45 Phosphothreonine.
{ECO:0000269|PubMed:27257257}.
MOD_RES 74 74 Phosphotyrosine.
{ECO:0000244|PubMed:15592455}.
MOD_RES 210 210 N6-acetyllysine.
{ECO:0000244|PubMed:19608861}.
MOD_RES 218 218 N6-acetyllysine.
{ECO:0000244|PubMed:19608861}.
CROSSLNK 42 42 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in SUMO2).
{ECO:0000244|PubMed:28112733}.
VARIANT 123 123 I -> T (in dbSNP:rs34863826).
/FTId=VAR_034159.
MUTAGEN 28 28 W->A: Reduces affinity for substrate
about 8-fold. Strongly reduced catalytic
activity and strongly reduced affinity
for substrate; when associated with A-46.
{ECO:0000269|PubMed:18462755}.
MUTAGEN 45 45 T->A: Impaired phosphorylation; generates
ATP in the presence of diphosphate.
{ECO:0000269|PubMed:27257257}.
MUTAGEN 45 45 T->D: Phosphomimetic mutant; unable to
generate ATP in the presence of
diphosphate.
{ECO:0000269|PubMed:27257257}.
MUTAGEN 46 46 W->A: Reduces affinity for substrate
about 6-fold. Strongly reduced catalytic
activity and strongly reduced affinity
for substrate; when associated with A-28.
{ECO:0000269|PubMed:18462755}.
MUTAGEN 51 51 R->Q: Reduces affinity for substrate
about 15-fold and reduces catalytic rate
about 17-fold.
{ECO:0000269|PubMed:18462755}.
MUTAGEN 84 84 R->Q: Reduces affinity for substrate
about 5-fold and reduces catalytic rate
67-fold. {ECO:0000269|PubMed:18462755}.
MUTAGEN 98 98 L->A: Reduces affinity for substrate
about 6-fold.
{ECO:0000269|PubMed:18462755}.
MUTAGEN 112 112 E->Q: Catalytic inactive mutant for both
ADP-sugar pyrophosphatase and nuclear
ATP-synthesis activities. Reduces
catalytic rate 6300-fold.
{ECO:0000269|PubMed:18462755,
ECO:0000269|PubMed:27257257}.
MUTAGEN 116 116 E->Q: Reduces catalytic rate 2000-fold.
{ECO:0000269|PubMed:18462755}.
MUTAGEN 166 166 E->Q: Reduces catalytic rate 120-fold.
{ECO:0000269|PubMed:18462755}.
CONFLICT 50 52 KRT -> NVP (in Ref. 2; AAF25479).
{ECO:0000305}.
STRAND 16 25 {ECO:0000244|PDB:6GRU}.
STRAND 27 37 {ECO:0000244|PDB:6GRU}.
STRAND 43 52 {ECO:0000244|PDB:6GRU}.
STRAND 58 69 {ECO:0000244|PDB:6GRU}.
STRAND 76 84 {ECO:0000244|PDB:6GRU}.
TURN 85 88 {ECO:0000244|PDB:6GRU}.
STRAND 89 93 {ECO:0000244|PDB:6GRU}.
STRAND 95 98 {ECO:0000244|PDB:6GRU}.
HELIX 105 117 {ECO:0000244|PDB:6GRU}.
STRAND 122 126 {ECO:0000244|PDB:6GRU}.
STRAND 130 132 {ECO:0000244|PDB:6GRU}.
TURN 134 136 {ECO:0000244|PDB:6GRU}.
STRAND 140 149 {ECO:0000244|PDB:6GRU}.
HELIX 153 155 {ECO:0000244|PDB:6GRU}.
STRAND 164 166 {ECO:0000244|PDB:3AC9}.
STRAND 169 174 {ECO:0000244|PDB:6GRU}.
HELIX 175 177 {ECO:0000244|PDB:6GRU}.
HELIX 178 189 {ECO:0000244|PDB:6GRU}.
STRAND 192 194 {ECO:0000244|PDB:6GRU}.
HELIX 195 206 {ECO:0000244|PDB:6GRU}.
TURN 211 213 {ECO:0000244|PDB:2DSB}.
HELIX 214 216 {ECO:0000244|PDB:2DSB}.
SEQUENCE 219 AA; 24328 MW; 6574E0BF1EA2BB26 CRC64;
MESQEPTESS QNGKQYIISE ELISEGKWVK LEKTTYMDPT GKTRTWESVK RTTRKEQTAD
GVAVIPVLQR TLHYECIVLV KQFRPPMGGY CIEFPAGLID DGETPEAAAL RELEEETGYK
GDIAECSPAV CMDPGLSNCT IHIVTVTING DDAENARPKP KPGDGEFVEV ISLPKNDLLQ
RLDALVAEEH LTVDARVYSY ALALKHANAK PFEVPFLKF


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