UniProtKB - P36639 (8ODP_HUMAN)
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- BLAST>sp|P36639|8ODP_HUMAN 7,8-dihydro-8-oxoguanine triphosphatase OS=Homo sapiens OX=9606 GN=NUDT1 PE=1 SV=3 MYWSNQITRRLGERVQGFMSGISPQQMGEPEGSWSGKNPGTMGASRLYTLVLVLQPQRVL LGMKKRGFGAGRWNGFGGKVQEGETIEDGARRELQEESGLTVDALHKVGQIVFEFVGEPE LMDVHVFCTDSIQGTPVESDEMRPCWFQLDQIPFKDMWPDDSYWFPLLLQKKKFHGYFKF QGQDTILDYTLREVDTV
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7,8-dihydro-8-oxoguanine triphosphatase
NUDT1
Annotation score:5 out of 5
<p>The annotation score provides a heuristic measure of the annotation content of a UniProtKB entry or proteome. This score <strong>cannot</strong> be used as a measure of the accuracy of the annotation as we cannot define the ‘correct annotation’ for any given protein.<p><a href='/help/annotation_score' target='_top'>More...</a></p>-Experimental evidence at protein leveli <p>This indicates the type of evidence that supports the existence of the protein. Note that the ‘protein existence’ evidence does not give information on the accuracy or correctness of the sequence(s) displayed.<p><a href='/help/protein_existence' target='_top'>More...</a></p>Select a section on the left to see content.
<p>This section provides any useful information about the protein, mostly biological knowledge.<p><a href='/help/function_section' target='_top'>More...</a></p>Functioni
<p>Manually curated information which has been propagated from a related experimentally characterized protein.</p> <p><a href="/manual/evidences#ECO:0000250">More...</a></p> Manual assertion inferred from sequence similarity toi
14 Publications<p>Manually curated information for which there is published experimental evidence.</p> <p><a href="/manual/evidences#ECO:0000269">More...</a></p> Manual assertion based on experiment ini
- Ref.1"Cloning and expression of cDNA for a human enzyme that hydrolyzes 8-oxo-dGTP, a mutagenic substrate for DNA synthesis."
Sakumi K., Furuichi M., Tsuzuki T., Kakuma T., Kawabata S., Maki H., Sekiguchi M.
J. Biol. Chem. 268:23524-23530(1993) [PubMed] [Europe PMC] [Abstract]Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM P18), PARTIAL PROTEIN SEQUENCE, CATALYTIC ACTIVITY, FUNCTION. - Ref.2"Genomic structure and chromosome location of the human mutT homologue gene MTH1 encoding 8-oxo-dGTPase for prevention of A:T to C:G transversion."
Furuichi M., Yoshida M.C., Oda H., Tajiri T., Nakabeppu Y., Tsuzuki T., Sekiguchi M.
Genomics 24:485-490(1994) [PubMed] [Europe PMC] [Abstract]Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION. - Ref.12"The oxidized forms of dATP are substrates for the human MutT homologue, the hMTH1 protein."
Fujikawa K., Kamiya H., Yakushiji H., Fujii Y., Nakabeppu Y., Kasai H.
J. Biol. Chem. 274:18201-18205(1999) [PubMed] [Europe PMC] [Abstract]Cited for: FUNCTION, CATALYTIC ACTIVITY, ENZYME REGULATION, BIOPHYSICOCHEMICAL PROPERTIES. - Ref.13"Functional significance of the conserved residues for the 23-residue module among MTH1 and MutT family proteins."
Fujii Y., Shimokawa H., Sekiguchi M., Nakabeppu Y.
J. Biol. Chem. 274:38251-38259(1999) [PubMed] [Europe PMC] [Abstract]Cited for: CATALYTIC ACTIVITY, MUTAGENESIS OF GLY-77; GLY-78; VAL-80; GLN-81; GLY-83; ILE-86; ASP-88; GLY-89; ALA-90; LEU-94; GLN-95; GLU-96; GLU-97 AND SER-98, FUNCTION. - Ref.14"Human MTH1 protein hydrolyzes the oxidized ribonucleotide, 2-hydroxy-ATP."
Fujikawa K., Kamiya H., Yakushiji H., Nakabeppu Y., Kasai H.
Nucleic Acids Res. 29:449-454(2001) [PubMed] [Europe PMC] [Abstract]Cited for: FUNCTION, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES. - Ref.15"A molecular basis for the selective recognition of 2-hydroxy-dATP and 8-oxo-dGTP by human MTH1."
Sakai Y., Furuichi M., Takahashi M., Mishima M., Iwai S., Shirakawa M., Nakabeppu Y.
J. Biol. Chem. 277:8579-8587(2002) [PubMed] [Europe PMC] [Abstract]Cited for: FUNCTION, CATALYTIC ACTIVITY, MUTAGENESIS OF PHE-68; TRP-158; ASP-160; LEU-191; ARG-192; GLU-193; VAL-194; ASP-195; THR-196; VAL-197; 192-ARG--VAL-197; 193-GLU--VAL-197; 194-VAL-VAL-197 AND 195-ASP--VAL-197. - Ref.16"An oxidized purine nucleoside triphosphatase, MTH1, suppresses cell death caused by oxidative stress."
Yoshimura D., Sakumi K., Ohno M., Sakai Y., Furuichi M., Iwai S., Nakabeppu Y.
J. Biol. Chem. 278:37965-37973(2003) [PubMed] [Europe PMC] [Abstract]Cited for: FUNCTION, CATALYTIC ACTIVITY, SUBCELLULAR LOCATION (ISOFORM P18). - Ref.17"The GT to GC single nucleotide polymorphism at the beginning of an alternative exon 2C of human MTH1 gene confers an amino terminal extension that functions as a mitochondrial targeting signal."
Sakai Y., Oda H., Yoshimura D., Furuichi M., Kang D., Iwai S., Hara T., Nakabeppu Y.
J. Mol. Med. 84:660-670(2006) [PubMed] [Europe PMC] [Abstract]Cited for: FUNCTION, CATALYTIC ACTIVITY, SUBCELLULAR LOCATION (ISOFORM P26), ALTERNATIVE SPLICING, CHARACTERIZATION OF VARIANT MET-124. - Ref.19"Human MTH3 (NUDT18) protein hydrolyzes oxidized forms of guanosine and deoxyguanosine diphosphates: comparison with MTH1 and MTH2."
Takagi Y., Setoyama D., Ito R., Kamiya H., Yamagata Y., Sekiguchi M.
J. Biol. Chem. 287:21541-21549(2012) [PubMed] [Europe PMC] [Abstract]Cited for: FUNCTION, CATALYTIC ACTIVITY. - Ref.24"MTH1 inhibition eradicates cancer by preventing sanitation of the dNTP pool."
Gad H., Koolmeister T., Jemth A.S., Eshtad S., Jacques S.A., Strom C.E., Svensson L.M., Schultz N., Lundback T., Einarsdottir B.O., Saleh A., Gokturk C., Baranczewski P., Svensson R., Berntsson R.P., Gustafsson R., Stromberg K., Sanjiv K. , Jacques-Cordonnier M.C., Desroses M., Gustavsson A.L., Olofsson R., Johansson F., Homan E.J., Loseva O., Brautigam L., Johansson L., Hoglund A., Hagenkort A., Pham T., Altun M., Gaugaz F.Z., Vikingsson S., Evers B., Henriksson M., Vallin K.S., Wallner O.A., Hammarstrom L.G., Wiita E., Almlof I., Kalderen C., Axelsson H., Djureinovic T., Puigvert J.C., Haggblad M., Jeppsson F., Martens U., Lundin C., Lundgren B., Granelli I., Jensen A.J., Artursson P., Nilsson J.A., Stenmark P., Scobie M., Berglund U.W., Helleday T.
Nature 508:215-221(2014) [PubMed] [Europe PMC] [Abstract]Cited for: X-RAY CRYSTALLOGRAPHY (1.60 ANGSTROMS) OF 42-196 IN COMPLEX WITH SYNTHETIC INHIBITORS, FUNCTION, CATALYTIC ACTIVITY, MUTAGENESIS OF GLU-97. - Ref.25"Stereospecific targeting of MTH1 by (S)-crizotinib as an anticancer strategy."
Huber K.V., Salah E., Radic B., Gridling M., Elkins J.M., Stukalov A., Jemth A.S., Gokturk C., Sanjiv K., Stromberg K., Pham T., Berglund U.W., Colinge J., Bennett K.L., Loizou J.I., Helleday T., Knapp S., Superti-Furga G.
Nature 508:222-227(2014) [PubMed] [Europe PMC] [Abstract]Cited for: X-RAY CRYSTALLOGRAPHY (1.20 ANGSTROMS) OF 42-197 IN COMPLEX WITH SYNTHETIC INHIBITORS, FUNCTION, CATALYTIC ACTIVITY. - Ref.26"MTH1 Substrate Recognition--An Example of Specific Promiscuity."
Nissink J.W., Bista M., Breed J., Carter N., Embrey K., Read J., Winter-Holt J.J.
PLoS ONE 11:e0151154-e0151154(2016) [PubMed] [Europe PMC] [Abstract]Cited for: X-RAY CRYSTALLOGRAPHY (1.24 ANGSTROMS) OF 42-197 IN COMPLEX WITH 8-OXO-GTP; 8-OXO-ATP AND SUBSTRATE ANALOGS, CATALYTIC ACTIVITY, FUNCTION. - Ref.27"Novel Class of Potent and Cellularly Active Inhibitors Devalidates MTH1 as Broad-Spectrum Cancer Target."
Ellermann M., Eheim A., Rahm F., Viklund J., Guenther J., Andersson M., Ericsson U., Forsblom R., Ginman T., Lindstrom J., Silvander C., Tresaugues L., Giese A., Bunse S., Neuhaus R., Weiske J., Quanz M., Glasauer A. , Nowak-Reppel K., Bader B., Irlbacher H., Meyer H., Queisser N., Bauser M., Haegebarth A., Gorjanacz M.
ACS Chem. Biol. 12:1986-1992(2017) [PubMed] [Europe PMC] [Abstract]Cited for: X-RAY CRYSTALLOGRAPHY (1.72 ANGSTROMS) OF 42-197, FUNCTION. - Ref.28"Structural and Kinetic Studies of the Human Nudix Hydrolase MTH1 Reveal the Mechanism for Its Broad Substrate Specificity."
Waz S., Nakamura T., Hirata K., Koga-Ogawa Y., Chirifu M., Arimori T., Tamada T., Ikemizu S., Nakabeppu Y., Yamagata Y.
J. Biol. Chem. 292:2785-2794(2017) [PubMed] [Europe PMC] [Abstract]Cited for: X-RAY CRYSTALLOGRAPHY (1.00 ANGSTROMS) OF 42-197 IN COMPLEXES WITH 8-OXO-GTP AND 2-OXO-ATP, CATALYTIC ACTIVITY, FUNCTION, MUTAGENESIS OF ASP-161.
Caution
<p>Manually curated information for which there is published experimental evidence.</p> <p><a href="/manual/evidences#ECO:0000269">More...</a></p> Manual assertion based on experiment ini
- Ref.24"MTH1 inhibition eradicates cancer by preventing sanitation of the dNTP pool."
Gad H., Koolmeister T., Jemth A.S., Eshtad S., Jacques S.A., Strom C.E., Svensson L.M., Schultz N., Lundback T., Einarsdottir B.O., Saleh A., Gokturk C., Baranczewski P., Svensson R., Berntsson R.P., Gustafsson R., Stromberg K., Sanjiv K. , Jacques-Cordonnier M.C., Desroses M., Gustavsson A.L., Olofsson R., Johansson F., Homan E.J., Loseva O., Brautigam L., Johansson L., Hoglund A., Hagenkort A., Pham T., Altun M., Gaugaz F.Z., Vikingsson S., Evers B., Henriksson M., Vallin K.S., Wallner O.A., Hammarstrom L.G., Wiita E., Almlof I., Kalderen C., Axelsson H., Djureinovic T., Puigvert J.C., Haggblad M., Jeppsson F., Martens U., Lundin C., Lundgren B., Granelli I., Jensen A.J., Artursson P., Nilsson J.A., Stenmark P., Scobie M., Berglund U.W., Helleday T.
Nature 508:215-221(2014) [PubMed] [Europe PMC] [Abstract]Cited for: X-RAY CRYSTALLOGRAPHY (1.60 ANGSTROMS) OF 42-196 IN COMPLEX WITH SYNTHETIC INHIBITORS, FUNCTION, CATALYTIC ACTIVITY, MUTAGENESIS OF GLU-97. - Ref.25"Stereospecific targeting of MTH1 by (S)-crizotinib as an anticancer strategy."
Huber K.V., Salah E., Radic B., Gridling M., Elkins J.M., Stukalov A., Jemth A.S., Gokturk C., Sanjiv K., Stromberg K., Pham T., Berglund U.W., Colinge J., Bennett K.L., Loizou J.I., Helleday T., Knapp S., Superti-Furga G.
Nature 508:222-227(2014) [PubMed] [Europe PMC] [Abstract]Cited for: X-RAY CRYSTALLOGRAPHY (1.20 ANGSTROMS) OF 42-197 IN COMPLEX WITH SYNTHETIC INHIBITORS, FUNCTION, CATALYTIC ACTIVITY. - Ref.27"Novel Class of Potent and Cellularly Active Inhibitors Devalidates MTH1 as Broad-Spectrum Cancer Target."
Ellermann M., Eheim A., Rahm F., Viklund J., Guenther J., Andersson M., Ericsson U., Forsblom R., Ginman T., Lindstrom J., Silvander C., Tresaugues L., Giese A., Bunse S., Neuhaus R., Weiske J., Quanz M., Glasauer A. , Nowak-Reppel K., Bader B., Irlbacher H., Meyer H., Queisser N., Bauser M., Haegebarth A., Gorjanacz M.
ACS Chem. Biol. 12:1986-1992(2017) [PubMed] [Europe PMC] [Abstract]Cited for: X-RAY CRYSTALLOGRAPHY (1.72 ANGSTROMS) OF 42-197, FUNCTION.
<p>This subsection of the <a href="http://www.uniprot.org/help/function_section">Function</a> section describes the catalytic activity of an enzyme, i.e. the chemical reaction it catalyzes. This information usually correlates with the presence of an EC (Enzyme Commission) number in the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section.<p><a href='/help/catalytic_activity' target='_top'>More...</a></p>Catalytic activityi
<p>Manually curated information for which there is published experimental evidence.</p> <p><a href="/manual/evidences#ECO:0000269">More...</a></p> Manual assertion based on experiment ini
- Ref.1"Cloning and expression of cDNA for a human enzyme that hydrolyzes 8-oxo-dGTP, a mutagenic substrate for DNA synthesis."
Sakumi K., Furuichi M., Tsuzuki T., Kakuma T., Kawabata S., Maki H., Sekiguchi M.
J. Biol. Chem. 268:23524-23530(1993) [PubMed] [Europe PMC] [Abstract]Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM P18), PARTIAL PROTEIN SEQUENCE, CATALYTIC ACTIVITY, FUNCTION. - Ref.11"Intracellular localization of 8-oxo-dGTPase in human cells, with special reference to the role of the enzyme in mitochondria."
Kang D., Nishida J., Iyama A., Nakabeppu Y., Furuichi M., Fujiwara T., Sekiguchi M., Takeshige K.
J. Biol. Chem. 270:14659-14665(1995) [PubMed] [Europe PMC] [Abstract]Cited for: SUBCELLULAR LOCATION (ISOFORM P18), CATALYTIC ACTIVITY. - Ref.12"The oxidized forms of dATP are substrates for the human MutT homologue, the hMTH1 protein."
Fujikawa K., Kamiya H., Yakushiji H., Fujii Y., Nakabeppu Y., Kasai H.
J. Biol. Chem. 274:18201-18205(1999) [PubMed] [Europe PMC] [Abstract]Cited for: FUNCTION, CATALYTIC ACTIVITY, ENZYME REGULATION, BIOPHYSICOCHEMICAL PROPERTIES. - Ref.13"Functional significance of the conserved residues for the 23-residue module among MTH1 and MutT family proteins."
Fujii Y., Shimokawa H., Sekiguchi M., Nakabeppu Y.
J. Biol. Chem. 274:38251-38259(1999) [PubMed] [Europe PMC] [Abstract]Cited for: CATALYTIC ACTIVITY, MUTAGENESIS OF GLY-77; GLY-78; VAL-80; GLN-81; GLY-83; ILE-86; ASP-88; GLY-89; ALA-90; LEU-94; GLN-95; GLU-96; GLU-97 AND SER-98, FUNCTION. - Ref.14"Human MTH1 protein hydrolyzes the oxidized ribonucleotide, 2-hydroxy-ATP."
Fujikawa K., Kamiya H., Yakushiji H., Nakabeppu Y., Kasai H.
Nucleic Acids Res. 29:449-454(2001) [PubMed] [Europe PMC] [Abstract]Cited for: FUNCTION, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES. - Ref.15"A molecular basis for the selective recognition of 2-hydroxy-dATP and 8-oxo-dGTP by human MTH1."
Sakai Y., Furuichi M., Takahashi M., Mishima M., Iwai S., Shirakawa M., Nakabeppu Y.
J. Biol. Chem. 277:8579-8587(2002) [PubMed] [Europe PMC] [Abstract]Cited for: FUNCTION, CATALYTIC ACTIVITY, MUTAGENESIS OF PHE-68; TRP-158; ASP-160; LEU-191; ARG-192; GLU-193; VAL-194; ASP-195; THR-196; VAL-197; 192-ARG--VAL-197; 193-GLU--VAL-197; 194-VAL-VAL-197 AND 195-ASP--VAL-197. - Ref.16"An oxidized purine nucleoside triphosphatase, MTH1, suppresses cell death caused by oxidative stress."
Yoshimura D., Sakumi K., Ohno M., Sakai Y., Furuichi M., Iwai S., Nakabeppu Y.
J. Biol. Chem. 278:37965-37973(2003) [PubMed] [Europe PMC] [Abstract]Cited for: FUNCTION, CATALYTIC ACTIVITY, SUBCELLULAR LOCATION (ISOFORM P18). - Ref.17"The GT to GC single nucleotide polymorphism at the beginning of an alternative exon 2C of human MTH1 gene confers an amino terminal extension that functions as a mitochondrial targeting signal."
Sakai Y., Oda H., Yoshimura D., Furuichi M., Kang D., Iwai S., Hara T., Nakabeppu Y.
J. Mol. Med. 84:660-670(2006) [PubMed] [Europe PMC] [Abstract]Cited for: FUNCTION, CATALYTIC ACTIVITY, SUBCELLULAR LOCATION (ISOFORM P26), ALTERNATIVE SPLICING, CHARACTERIZATION OF VARIANT MET-124. - Ref.19"Human MTH3 (NUDT18) protein hydrolyzes oxidized forms of guanosine and deoxyguanosine diphosphates: comparison with MTH1 and MTH2."
Takagi Y., Setoyama D., Ito R., Kamiya H., Yamagata Y., Sekiguchi M.
J. Biol. Chem. 287:21541-21549(2012) [PubMed] [Europe PMC] [Abstract]Cited for: FUNCTION, CATALYTIC ACTIVITY. - Ref.22"Crystal structure of human MTH1 and the 8-oxo-dGMP product complex."
Svensson L.M., Jemth A.S., Desroses M., Loseva O., Helleday T., Hogbom M., Stenmark P.
FEBS Lett. 585:2617-2621(2011) [PubMed] [Europe PMC] [Abstract]Cited for: X-RAY CRYSTALLOGRAPHY (1.80 ANGSTROMS) OF 42-197 IN COMPLEX WITH 8-OXO-DGMP, BIOPHYSICOCHEMICAL PROPERTIES. - Ref.24"MTH1 inhibition eradicates cancer by preventing sanitation of the dNTP pool."
Gad H., Koolmeister T., Jemth A.S., Eshtad S., Jacques S.A., Strom C.E., Svensson L.M., Schultz N., Lundback T., Einarsdottir B.O., Saleh A., Gokturk C., Baranczewski P., Svensson R., Berntsson R.P., Gustafsson R., Stromberg K., Sanjiv K. , Jacques-Cordonnier M.C., Desroses M., Gustavsson A.L., Olofsson R., Johansson F., Homan E.J., Loseva O., Brautigam L., Johansson L., Hoglund A., Hagenkort A., Pham T., Altun M., Gaugaz F.Z., Vikingsson S., Evers B., Henriksson M., Vallin K.S., Wallner O.A., Hammarstrom L.G., Wiita E., Almlof I., Kalderen C., Axelsson H., Djureinovic T., Puigvert J.C., Haggblad M., Jeppsson F., Martens U., Lundin C., Lundgren B., Granelli I., Jensen A.J., Artursson P., Nilsson J.A., Stenmark P., Scobie M., Berglund U.W., Helleday T.
Nature 508:215-221(2014) [PubMed] [Europe PMC] [Abstract]Cited for: X-RAY CRYSTALLOGRAPHY (1.60 ANGSTROMS) OF 42-196 IN COMPLEX WITH SYNTHETIC INHIBITORS, FUNCTION, CATALYTIC ACTIVITY, MUTAGENESIS OF GLU-97. - Ref.25"Stereospecific targeting of MTH1 by (S)-crizotinib as an anticancer strategy."
Huber K.V., Salah E., Radic B., Gridling M., Elkins J.M., Stukalov A., Jemth A.S., Gokturk C., Sanjiv K., Stromberg K., Pham T., Berglund U.W., Colinge J., Bennett K.L., Loizou J.I., Helleday T., Knapp S., Superti-Furga G.
Nature 508:222-227(2014) [PubMed] [Europe PMC] [Abstract]Cited for: X-RAY CRYSTALLOGRAPHY (1.20 ANGSTROMS) OF 42-197 IN COMPLEX WITH SYNTHETIC INHIBITORS, FUNCTION, CATALYTIC ACTIVITY. - Ref.26"MTH1 Substrate Recognition--An Example of Specific Promiscuity."
Nissink J.W., Bista M., Breed J., Carter N., Embrey K., Read J., Winter-Holt J.J.
PLoS ONE 11:e0151154-e0151154(2016) [PubMed] [Europe PMC] [Abstract]Cited for: X-RAY CRYSTALLOGRAPHY (1.24 ANGSTROMS) OF 42-197 IN COMPLEX WITH 8-OXO-GTP; 8-OXO-ATP AND SUBSTRATE ANALOGS, CATALYTIC ACTIVITY, FUNCTION. - Ref.28"Structural and Kinetic Studies of the Human Nudix Hydrolase MTH1 Reveal the Mechanism for Its Broad Substrate Specificity."
Waz S., Nakamura T., Hirata K., Koga-Ogawa Y., Chirifu M., Arimori T., Tamada T., Ikemizu S., Nakabeppu Y., Yamagata Y.
J. Biol. Chem. 292:2785-2794(2017) [PubMed] [Europe PMC] [Abstract]Cited for: X-RAY CRYSTALLOGRAPHY (1.00 ANGSTROMS) OF 42-197 IN COMPLEXES WITH 8-OXO-GTP AND 2-OXO-ATP, CATALYTIC ACTIVITY, FUNCTION, MUTAGENESIS OF ASP-161.
<p>Manually curated information for which there is published experimental evidence.</p> <p><a href="/manual/evidences#ECO:0000269">More...</a></p> Manual assertion based on experiment ini
- Ref.12"The oxidized forms of dATP are substrates for the human MutT homologue, the hMTH1 protein."
Fujikawa K., Kamiya H., Yakushiji H., Fujii Y., Nakabeppu Y., Kasai H.
J. Biol. Chem. 274:18201-18205(1999) [PubMed] [Europe PMC] [Abstract]Cited for: FUNCTION, CATALYTIC ACTIVITY, ENZYME REGULATION, BIOPHYSICOCHEMICAL PROPERTIES. - Ref.14"Human MTH1 protein hydrolyzes the oxidized ribonucleotide, 2-hydroxy-ATP."
Fujikawa K., Kamiya H., Yakushiji H., Nakabeppu Y., Kasai H.
Nucleic Acids Res. 29:449-454(2001) [PubMed] [Europe PMC] [Abstract]Cited for: FUNCTION, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES. - Ref.15"A molecular basis for the selective recognition of 2-hydroxy-dATP and 8-oxo-dGTP by human MTH1."
Sakai Y., Furuichi M., Takahashi M., Mishima M., Iwai S., Shirakawa M., Nakabeppu Y.
J. Biol. Chem. 277:8579-8587(2002) [PubMed] [Europe PMC] [Abstract]Cited for: FUNCTION, CATALYTIC ACTIVITY, MUTAGENESIS OF PHE-68; TRP-158; ASP-160; LEU-191; ARG-192; GLU-193; VAL-194; ASP-195; THR-196; VAL-197; 192-ARG--VAL-197; 193-GLU--VAL-197; 194-VAL-VAL-197 AND 195-ASP--VAL-197. - Ref.16"An oxidized purine nucleoside triphosphatase, MTH1, suppresses cell death caused by oxidative stress."
Yoshimura D., Sakumi K., Ohno M., Sakai Y., Furuichi M., Iwai S., Nakabeppu Y.
J. Biol. Chem. 278:37965-37973(2003) [PubMed] [Europe PMC] [Abstract]Cited for: FUNCTION, CATALYTIC ACTIVITY, SUBCELLULAR LOCATION (ISOFORM P18). - Ref.17"The GT to GC single nucleotide polymorphism at the beginning of an alternative exon 2C of human MTH1 gene confers an amino terminal extension that functions as a mitochondrial targeting signal."
Sakai Y., Oda H., Yoshimura D., Furuichi M., Kang D., Iwai S., Hara T., Nakabeppu Y.
J. Mol. Med. 84:660-670(2006) [PubMed] [Europe PMC] [Abstract]Cited for: FUNCTION, CATALYTIC ACTIVITY, SUBCELLULAR LOCATION (ISOFORM P26), ALTERNATIVE SPLICING, CHARACTERIZATION OF VARIANT MET-124. - Ref.24"MTH1 inhibition eradicates cancer by preventing sanitation of the dNTP pool."
Gad H., Koolmeister T., Jemth A.S., Eshtad S., Jacques S.A., Strom C.E., Svensson L.M., Schultz N., Lundback T., Einarsdottir B.O., Saleh A., Gokturk C., Baranczewski P., Svensson R., Berntsson R.P., Gustafsson R., Stromberg K., Sanjiv K. , Jacques-Cordonnier M.C., Desroses M., Gustavsson A.L., Olofsson R., Johansson F., Homan E.J., Loseva O., Brautigam L., Johansson L., Hoglund A., Hagenkort A., Pham T., Altun M., Gaugaz F.Z., Vikingsson S., Evers B., Henriksson M., Vallin K.S., Wallner O.A., Hammarstrom L.G., Wiita E., Almlof I., Kalderen C., Axelsson H., Djureinovic T., Puigvert J.C., Haggblad M., Jeppsson F., Martens U., Lundin C., Lundgren B., Granelli I., Jensen A.J., Artursson P., Nilsson J.A., Stenmark P., Scobie M., Berglund U.W., Helleday T.
Nature 508:215-221(2014) [PubMed] [Europe PMC] [Abstract]Cited for: X-RAY CRYSTALLOGRAPHY (1.60 ANGSTROMS) OF 42-196 IN COMPLEX WITH SYNTHETIC INHIBITORS, FUNCTION, CATALYTIC ACTIVITY, MUTAGENESIS OF GLU-97. - Ref.25"Stereospecific targeting of MTH1 by (S)-crizotinib as an anticancer strategy."
Huber K.V., Salah E., Radic B., Gridling M., Elkins J.M., Stukalov A., Jemth A.S., Gokturk C., Sanjiv K., Stromberg K., Pham T., Berglund U.W., Colinge J., Bennett K.L., Loizou J.I., Helleday T., Knapp S., Superti-Furga G.
Nature 508:222-227(2014) [PubMed] [Europe PMC] [Abstract]Cited for: X-RAY CRYSTALLOGRAPHY (1.20 ANGSTROMS) OF 42-197 IN COMPLEX WITH SYNTHETIC INHIBITORS, FUNCTION, CATALYTIC ACTIVITY. - Ref.26"MTH1 Substrate Recognition--An Example of Specific Promiscuity."
Nissink J.W., Bista M., Breed J., Carter N., Embrey K., Read J., Winter-Holt J.J.
PLoS ONE 11:e0151154-e0151154(2016) [PubMed] [Europe PMC] [Abstract]Cited for: X-RAY CRYSTALLOGRAPHY (1.24 ANGSTROMS) OF 42-197 IN COMPLEX WITH 8-OXO-GTP; 8-OXO-ATP AND SUBSTRATE ANALOGS, CATALYTIC ACTIVITY, FUNCTION. - Ref.28"Structural and Kinetic Studies of the Human Nudix Hydrolase MTH1 Reveal the Mechanism for Its Broad Substrate Specificity."
Waz S., Nakamura T., Hirata K., Koga-Ogawa Y., Chirifu M., Arimori T., Tamada T., Ikemizu S., Nakabeppu Y., Yamagata Y.
J. Biol. Chem. 292:2785-2794(2017) [PubMed] [Europe PMC] [Abstract]Cited for: X-RAY CRYSTALLOGRAPHY (1.00 ANGSTROMS) OF 42-197 IN COMPLEXES WITH 8-OXO-GTP AND 2-OXO-ATP, CATALYTIC ACTIVITY, FUNCTION, MUTAGENESIS OF ASP-161.
<p>This subsection of the ‘Function’ section provides information relevant to cofactors. A cofactor is any non-protein substance required for a protein to be catalytically active. Some cofactors are inorganic, such as the metal atoms zinc, iron, and copper in various oxidation states. Others, such as most vitamins, are organic.<p><a href='/help/cofactor' target='_top'>More...</a></p>Cofactori
<p>Manually curated information which has been inferred by a curator based on his/her scientific knowledge or on the scientific content of an article.</p> <p><a href="/manual/evidences#ECO:0000305">More...</a></p> Manual assertion inferred by curator fromi
- Ref.20"Structure of human MTH1, a Nudix family hydrolase that selectively degrades oxidized purine nucleoside triphosphates."
Mishima M., Sakai Y., Itoh N., Kamiya H., Furuichi M., Takahashi M., Yamagata Y., Iwai S., Nakabeppu Y., Shirakawa M.
J. Biol. Chem. 279:33806-33815(2004) [PubMed] [Europe PMC] [Abstract]Cited for: STRUCTURE BY NMR OF 42-197, SUBUNIT, COFACTOR, SUBSTRATE BINDING SITE.
<p>Manually curated information which has been inferred by a curator based on his/her scientific knowledge or on the scientific content of an article.</p> <p><a href="/manual/evidences#ECO:0000305">More...</a></p> Manual assertion inferred by curator fromi
- Ref.20"Structure of human MTH1, a Nudix family hydrolase that selectively degrades oxidized purine nucleoside triphosphates."
Mishima M., Sakai Y., Itoh N., Kamiya H., Furuichi M., Takahashi M., Yamagata Y., Iwai S., Nakabeppu Y., Shirakawa M.
J. Biol. Chem. 279:33806-33815(2004) [PubMed] [Europe PMC] [Abstract]Cited for: STRUCTURE BY NMR OF 42-197, SUBUNIT, COFACTOR, SUBSTRATE BINDING SITE.
<p>This subsection of the ‘Function’ section describes an enzyme regulatory mechanism and reports the components which regulate (by activation or inhibition) the reaction.<p><a href='/help/enzyme_regulation' target='_top'>More...</a></p>Enzyme regulationi
<p>Manually curated information for which there is published experimental evidence.</p> <p><a href="/manual/evidences#ECO:0000269">More...</a></p> Manual assertion based on experiment ini
- Ref.12"The oxidized forms of dATP are substrates for the human MutT homologue, the hMTH1 protein."
Fujikawa K., Kamiya H., Yakushiji H., Fujii Y., Nakabeppu Y., Kasai H.
J. Biol. Chem. 274:18201-18205(1999) [PubMed] [Europe PMC] [Abstract]Cited for: FUNCTION, CATALYTIC ACTIVITY, ENZYME REGULATION, BIOPHYSICOCHEMICAL PROPERTIES.
<p>This subsection of the ‘Function’ section describes biophysical and chemical properties, such as maximal absorption, kinetic parameters, pH dependence, redox potentials and temperature dependence.<p><a href='/help/biophysicochemical_properties' target='_top'>More...</a></p>Kineticsi
- KM=8.3 µM for 2-hydroxy-dATP (at 30 degrees Celsius and pH 8.0)1 Publication
<p>Manually curated information for which there is published experimental evidence.</p> <p><a href="/manual/evidences#ECO:0000269">More...</a></p> Manual assertion based on experiment ini
- Ref.14"Human MTH1 protein hydrolyzes the oxidized ribonucleotide, 2-hydroxy-ATP."
Fujikawa K., Kamiya H., Yakushiji H., Nakabeppu Y., Kasai H.
Nucleic Acids Res. 29:449-454(2001) [PubMed] [Europe PMC] [Abstract]Cited for: FUNCTION, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES.
- KM=5.7 µM for 2-hydroxy-dATP (at 30 degrees Celsius and pH 7.2)1 Publication
<p>Manually curated information for which there is published experimental evidence.</p> <p><a href="/manual/evidences#ECO:0000269">More...</a></p> Manual assertion based on experiment ini
- Ref.14"Human MTH1 protein hydrolyzes the oxidized ribonucleotide, 2-hydroxy-ATP."
Fujikawa K., Kamiya H., Yakushiji H., Nakabeppu Y., Kasai H.
Nucleic Acids Res. 29:449-454(2001) [PubMed] [Europe PMC] [Abstract]Cited for: FUNCTION, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES.
- KM=4.3 µM for 2-hydroxy-rATP (at 30 degrees Celsius and pH 8.0)1 Publication
<p>Manually curated information for which there is published experimental evidence.</p> <p><a href="/manual/evidences#ECO:0000269">More...</a></p> Manual assertion based on experiment ini
- Ref.14"Human MTH1 protein hydrolyzes the oxidized ribonucleotide, 2-hydroxy-ATP."
Fujikawa K., Kamiya H., Yakushiji H., Nakabeppu Y., Kasai H.
Nucleic Acids Res. 29:449-454(2001) [PubMed] [Europe PMC] [Abstract]Cited for: FUNCTION, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES.
- KM=13.9 µM for 8-hydroxy-dATP (at 30 degrees Celsius and pH 8.0)1 Publication
<p>Manually curated information for which there is published experimental evidence.</p> <p><a href="/manual/evidences#ECO:0000269">More...</a></p> Manual assertion based on experiment ini
- Ref.14"Human MTH1 protein hydrolyzes the oxidized ribonucleotide, 2-hydroxy-ATP."
Fujikawa K., Kamiya H., Yakushiji H., Nakabeppu Y., Kasai H.
Nucleic Acids Res. 29:449-454(2001) [PubMed] [Europe PMC] [Abstract]Cited for: FUNCTION, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES.
- KM=51.0 µM for 8-hydroxy-rATP (at 30 degrees Celsius and pH 8.0)1 Publication
<p>Manually curated information for which there is published experimental evidence.</p> <p><a href="/manual/evidences#ECO:0000269">More...</a></p> Manual assertion based on experiment ini
- Ref.14"Human MTH1 protein hydrolyzes the oxidized ribonucleotide, 2-hydroxy-ATP."
Fujikawa K., Kamiya H., Yakushiji H., Nakabeppu Y., Kasai H.
Nucleic Acids Res. 29:449-454(2001) [PubMed] [Europe PMC] [Abstract]Cited for: FUNCTION, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES.
- KM=15.2 µM for 8-hydroxy-dGTP (at 30 degrees Celsius and pH 8.0)1 Publication
<p>Manually curated information for which there is published experimental evidence.</p> <p><a href="/manual/evidences#ECO:0000269">More...</a></p> Manual assertion based on experiment ini
- Ref.14"Human MTH1 protein hydrolyzes the oxidized ribonucleotide, 2-hydroxy-ATP."
Fujikawa K., Kamiya H., Yakushiji H., Nakabeppu Y., Kasai H.
Nucleic Acids Res. 29:449-454(2001) [PubMed] [Europe PMC] [Abstract]Cited for: FUNCTION, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES.
- KM=12.8 µM for 8-hydroxy-dGTP (at 30 degrees Celsius and pH 7.2)1 Publication
<p>Manually curated information for which there is published experimental evidence.</p> <p><a href="/manual/evidences#ECO:0000269">More...</a></p> Manual assertion based on experiment ini
- Ref.14"Human MTH1 protein hydrolyzes the oxidized ribonucleotide, 2-hydroxy-ATP."
Fujikawa K., Kamiya H., Yakushiji H., Nakabeppu Y., Kasai H.
Nucleic Acids Res. 29:449-454(2001) [PubMed] [Europe PMC] [Abstract]Cited for: FUNCTION, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES.
- KM=13.2 µM for 8-hydroxy-dGTP (at 22 degrees Celsius and pH 7.5)1 Publication
<p>Manually curated information for which there is published experimental evidence.</p> <p><a href="/manual/evidences#ECO:0000269">More...</a></p> Manual assertion based on experiment ini
- Ref.22"Crystal structure of human MTH1 and the 8-oxo-dGMP product complex."
Svensson L.M., Jemth A.S., Desroses M., Loseva O., Helleday T., Hogbom M., Stenmark P.
FEBS Lett. 585:2617-2621(2011) [PubMed] [Europe PMC] [Abstract]Cited for: X-RAY CRYSTALLOGRAPHY (1.80 ANGSTROMS) OF 42-197 IN COMPLEX WITH 8-OXO-DGMP, BIOPHYSICOCHEMICAL PROPERTIES.
- KM=55.0 µM for 8-hydroxy-rGTP (at 30 degrees Celsius and pH 8.0)1 Publication
<p>Manually curated information for which there is published experimental evidence.</p> <p><a href="/manual/evidences#ECO:0000269">More...</a></p> Manual assertion based on experiment ini
- Ref.14"Human MTH1 protein hydrolyzes the oxidized ribonucleotide, 2-hydroxy-ATP."
Fujikawa K., Kamiya H., Yakushiji H., Nakabeppu Y., Kasai H.
Nucleic Acids Res. 29:449-454(2001) [PubMed] [Europe PMC] [Abstract]Cited for: FUNCTION, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES.
- KM=258 µM for dGTP (at 30 degrees Celsius and pH 8.0)1 Publication
<p>Manually curated information for which there is published experimental evidence.</p> <p><a href="/manual/evidences#ECO:0000269">More...</a></p> Manual assertion based on experiment ini
- Ref.14"Human MTH1 protein hydrolyzes the oxidized ribonucleotide, 2-hydroxy-ATP."
Fujikawa K., Kamiya H., Yakushiji H., Nakabeppu Y., Kasai H.
Nucleic Acids Res. 29:449-454(2001) [PubMed] [Europe PMC] [Abstract]Cited for: FUNCTION, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES.
<p>This subsection of the ‘Function’ section describes biophysical and chemical properties, such as maximal absorption, kinetic parameters, pH dependence, redox potentials and temperature dependence.<p><a href='/help/biophysicochemical_properties' target='_top'>More...</a></p>pH dependencei
<p>Manually curated information for which there is published experimental evidence.</p> <p><a href="/manual/evidences#ECO:0000269">More...</a></p> Manual assertion based on experiment ini
- Ref.12"The oxidized forms of dATP are substrates for the human MutT homologue, the hMTH1 protein."
Fujikawa K., Kamiya H., Yakushiji H., Fujii Y., Nakabeppu Y., Kasai H.
J. Biol. Chem. 274:18201-18205(1999) [PubMed] [Europe PMC] [Abstract]Cited for: FUNCTION, CATALYTIC ACTIVITY, ENZYME REGULATION, BIOPHYSICOCHEMICAL PROPERTIES. - Ref.14"Human MTH1 protein hydrolyzes the oxidized ribonucleotide, 2-hydroxy-ATP."
Fujikawa K., Kamiya H., Yakushiji H., Nakabeppu Y., Kasai H.
Nucleic Acids Res. 29:449-454(2001) [PubMed] [Europe PMC] [Abstract]Cited for: FUNCTION, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES. - Ref.22"Crystal structure of human MTH1 and the 8-oxo-dGMP product complex."
Svensson L.M., Jemth A.S., Desroses M., Loseva O., Helleday T., Hogbom M., Stenmark P.
FEBS Lett. 585:2617-2621(2011) [PubMed] [Europe PMC] [Abstract]Cited for: X-RAY CRYSTALLOGRAPHY (1.80 ANGSTROMS) OF 42-197 IN COMPLEX WITH 8-OXO-DGMP, BIOPHYSICOCHEMICAL PROPERTIES.
Sites
| Feature key | Position(s) | DescriptionActions | Graphical view | Length |
|---|---|---|---|---|
| <p>This subsection of the ‘Function’ section describes the interaction between a single amino acid and another chemical entity. Priority is given to the annotation of physiological ligands.<p><a href='/help/binding' target='_top'>More...</a></p>Binding sitei | 49 | Substrate; via carbonyl oxygenCombined sources <p>Manually validated information inferred from a combination of experimental and computational evidence.</p> <p><a href="/manual/evidences#ECO:0000244">More...</a></p> Manual assertion inferred from combination of experimental and computational evidencei 2 Publications<p>Manually curated information for which there is published experimental evidence.</p> <p><a href="/manual/evidences#ECO:0000269">More...</a></p> Manual assertion based on experiment ini
| 1 | |
| <p>This subsection of the ‘Function’ section describes the interaction between a single amino acid and another chemical entity. Priority is given to the annotation of physiological ligands.<p><a href='/help/binding' target='_top'>More...</a></p>Binding sitei | 64 | SubstrateCombined sources <p>Manually validated information inferred from a combination of experimental and computational evidence.</p> <p><a href="/manual/evidences#ECO:0000244">More...</a></p> Manual assertion inferred from combination of experimental and computational evidencei 2 Publications<p>Manually curated information for which there is published experimental evidence.</p> <p><a href="/manual/evidences#ECO:0000269">More...</a></p> Manual assertion based on experiment ini
| 1 | |
| <p>This subsection describes interesting single amino acid sites on the sequence that are not defined in any other subsection. This subsection can be displayed in different sections (‘Function’, ‘PTM / Processing’, ‘Pathology and Biotech’) according to its content.<p><a href='/help/site' target='_top'>More...</a></p>Sitei | 68 | Important for 2-OH-dATPase and 8-oxo-dGTPase activities1 Publication <p>Manually curated information for which there is published experimental evidence.</p> <p><a href="/manual/evidences#ECO:0000269">More...</a></p> Manual assertion based on experiment ini
| 1 | |
| <p>This subsection of the ‘Function’ section describes the interaction between a single amino acid and another chemical entity. Priority is given to the annotation of physiological ligands.<p><a href='/help/binding' target='_top'>More...</a></p>Binding sitei | 74 | SubstrateCombined sources <p>Manually validated information inferred from a combination of experimental and computational evidence.</p> <p><a href="/manual/evidences#ECO:0000244">More...</a></p> Manual assertion inferred from combination of experimental and computational evidencei 2 Publications<p>Manually curated information for which there is published experimental evidence.</p> <p><a href="/manual/evidences#ECO:0000269">More...</a></p> Manual assertion based on experiment ini
| 1 | |
| <p>This subsection of the ‘Function’ section indicates at which position the protein binds a given metal ion. The nature of the metal is indicated in the ‘Description’ field.<p><a href='/help/metal' target='_top'>More...</a></p>Metal bindingi | 78 | Magnesium; via carbonyl oxygenBy similarity | 1 | |
| <p>This subsection of the ‘Function’ section indicates at which position the protein binds a given metal ion. The nature of the metal is indicated in the ‘Description’ field.<p><a href='/help/metal' target='_top'>More...</a></p>Metal bindingi | 93 | MagnesiumBy similarity | 1 | |
| <p>This subsection of the ‘Function’ section indicates at which position the protein binds a given metal ion. The nature of the metal is indicated in the ‘Description’ field.<p><a href='/help/metal' target='_top'>More...</a></p>Metal bindingi | 96 | MagnesiumBy similarity | 1 | |
| <p>This subsection of the ‘Function’ section indicates at which position the protein binds a given metal ion. The nature of the metal is indicated in the ‘Description’ field.<p><a href='/help/metal' target='_top'>More...</a></p>Metal bindingi | 97 | MagnesiumBy similarity | 1 | |
| <p>This subsection describes interesting single amino acid sites on the sequence that are not defined in any other subsection. This subsection can be displayed in different sections (‘Function’, ‘PTM / Processing’, ‘Pathology and Biotech’) according to its content.<p><a href='/help/site' target='_top'>More...</a></p>Sitei | 158 | Essential for 2-OH-dATPase and 8-oxo-dGTPase activities1 Publication <p>Manually curated information for which there is published experimental evidence.</p> <p><a href="/manual/evidences#ECO:0000269">More...</a></p> Manual assertion based on experiment ini
| 1 | |
| <p>This subsection describes interesting single amino acid sites on the sequence that are not defined in any other subsection. This subsection can be displayed in different sections (‘Function’, ‘PTM / Processing’, ‘Pathology and Biotech’) according to its content.<p><a href='/help/site' target='_top'>More...</a></p>Sitei | 160 | Essential for 2-OH-dATPase activity and important for 8-oxo-dGTPase activity1 Publication <p>Manually curated information for which there is published experimental evidence.</p> <p><a href="/manual/evidences#ECO:0000269">More...</a></p> Manual assertion based on experiment ini
| 1 |
<p>The <a href="http://www.geneontology.org/">Gene Ontology (GO)</a> project provides a set of hierarchical controlled vocabulary split into 3 categories:<p><a href='/help/gene_ontology' target='_top'>More...</a></p>GO - Molecular functioni
- 2-hydroxy-(deoxy)adenosine-triphosphate pyrophosphatase activity Source: ReactomeInferred from experimenti
- 2-hydroxy-adenosine triphosphate pyrophosphatase activity Source: ReactomeInferred from experimenti
- 8-oxo-7,8-dihydrodeoxyguanosine triphosphate pyrophosphatase activity Source: UniProtKB <p>Inferred from Direct Assay</p> <p>Used to indicate a direct assay for the function, process or component indicated by the GO term.</p> <p>More information in the <a href="http://geneontology.org/page/guide-go-evidence-codes#ida">GO evidence code guide</a></p> Inferred from direct assayi
- 8-oxo-7,8-dihydroguanosine triphosphate pyrophosphatase activity Source: UniProtKB <p>Inferred from Direct Assay</p> <p>Used to indicate a direct assay for the function, process or component indicated by the GO term.</p> <p>More information in the <a href="http://geneontology.org/page/guide-go-evidence-codes#ida">GO evidence code guide</a></p> Inferred from direct assayi
- ATP diphosphatase activity Source: UniProtKB <p>Inferred from Direct Assay</p> <p>Used to indicate a direct assay for the function, process or component indicated by the GO term.</p> <p>More information in the <a href="http://geneontology.org/page/guide-go-evidence-codes#ida">GO evidence code guide</a></p> Inferred from direct assayi
- GTPase activity Source: UniProtKB <p>Inferred from Direct Assay</p> <p>Used to indicate a direct assay for the function, process or component indicated by the GO term.</p> <p>More information in the <a href="http://geneontology.org/page/guide-go-evidence-codes#ida">GO evidence code guide</a></p> Inferred from direct assayi
- GTP diphosphatase activity Source: UniProtKB <p>Inferred from Direct Assay</p> <p>Used to indicate a direct assay for the function, process or component indicated by the GO term.</p> <p>More information in the <a href="http://geneontology.org/page/guide-go-evidence-codes#ida">GO evidence code guide</a></p> Inferred from direct assayi
- metal ion binding Source: UniProtKB-KW
- snoRNA binding Source: UniProtKB
<p>The <a href="http://www.geneontology.org/">Gene Ontology (GO)</a> project provides a set of hierarchical controlled vocabulary split into 3 categories:<p><a href='/help/gene_ontology' target='_top'>More...</a></p>GO - Biological processi
- aging Source: Ensembl
- dATP catabolic process Source: UniProtKB <p>Inferred from Direct Assay</p> <p>Used to indicate a direct assay for the function, process or component indicated by the GO term.</p> <p>More information in the <a href="http://geneontology.org/page/guide-go-evidence-codes#ida">GO evidence code guide</a></p> Inferred from direct assayi
- dGTP catabolic process Source: UniProtKB <p>Inferred from Direct Assay</p> <p>Used to indicate a direct assay for the function, process or component indicated by the GO term.</p> <p>More information in the <a href="http://geneontology.org/page/guide-go-evidence-codes#ida">GO evidence code guide</a></p> Inferred from direct assayi
- DNA protection Source: UniProtKB <p>Inferred from Direct Assay</p> <p>Used to indicate a direct assay for the function, process or component indicated by the GO term.</p> <p>More information in the <a href="http://geneontology.org/page/guide-go-evidence-codes#ida">GO evidence code guide</a></p> Inferred from direct assayi
- DNA repair Source: UniProtKB <p>Inferred by Curator</p> <p>Used for cases where an annotation is not supported by any evidence but can be reasonably inferred by a curator from other GO annotations for which evidence <br />is available.</p> <p>More information in the <a href="http://geneontology.org/page/guide-go-evidence-codes#ic">GO evidence code guide</a></p> Inferred by curatori
- male gonad development Source: Ensembl
- nucleobase-containing small molecule catabolic process Source: Reactome
- purine nucleotide catabolic process Source: UniProtKB <p>Inferred from Direct Assay</p> <p>Used to indicate a direct assay for the function, process or component indicated by the GO term.</p> <p>More information in the <a href="http://geneontology.org/page/guide-go-evidence-codes#ida">GO evidence code guide</a></p> Inferred from direct assayi
- response to cadmium ion Source: Ensembl
- response to oxidative stress Source: ProtInc <p>Traceable Author Statement</p> <p>Used for information from review articles where the original experiments are traceable through that article and also for information from text books or dictionaries.</p> <p>More information in the <a href="http://geneontology.org/page/guide-go-evidence-codes#tas">GO evidence code guide</a></p> Traceable author statementi
<p>UniProtKB Keywords constitute a <a href="http://www.uniprot.org/keywords">controlled vocabulary</a> with a hierarchical structure. Keywords summarise the content of a UniProtKB entry and facilitate the search for proteins of interest.<p><a href='/help/keywords' target='_top'>More...</a></p>Keywordsi
| Molecular function | Hydrolase, RNA-binding |
| Ligand | Magnesium, Metal-binding |
Enzyme and pathway databases
BioCyc Collection of Pathway/Genome Databases More...BioCyci | MetaCyc:HS02879-MONOMER |
BRENDA Comprehensive Enzyme Information System More...BRENDAi | 3.6.1.55 2681 3.6.1.56 2681 |
Reactome - a knowledgebase of biological pathways and processes More...Reactomei | R-HSA-2393930 Phosphate bond hydrolysis by NUDT proteins |
SABIO-RK: Biochemical Reaction Kinetics Database More...SABIO-RKi | P36639 |
<p>This section provides information about the protein and gene name(s) and synonym(s) and about the organism that is the source of the protein sequence.<p><a href='/help/names_and_taxonomy_section' target='_top'>More...</a></p>Names & Taxonomyi
| <p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section provides an exhaustive list of all names of the protein, from commonly used to obsolete, to allow unambiguous identification of a protein.<p><a href='/help/protein_names' target='_top'>More...</a></p>Protein namesi | Recommended name: 7,8-dihydro-8-oxoguanine triphosphatase (EC:3.6.1.557 Publications<p>Manually curated information for which there is published experimental evidence.</p> <p><a href="/manual/evidences#ECO:0000269">More...</a></p> Manual assertion based on experiment ini
Alternative name(s): 2-hydroxy-dATP diphosphatase (EC:3.6.1.565 Publications <p>Manually curated information for which there is published experimental evidence.</p> <p><a href="/manual/evidences#ECO:0000269">More...</a></p> Manual assertion based on experiment ini
8-oxo-dGTPase Nucleoside diphosphate-linked moiety X motif 1 Short name: Nudix motif 1 |
| <p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section indicates the name(s) of the gene(s) that code for the protein sequence(s) described in the entry. Four distinct tokens exist: ‘Name’, ‘Synonyms’, ‘Ordered locus names’ and ‘ORF names’.<p><a href='/help/gene_name' target='_top'>More...</a></p>Gene namesi | Name:NUDT1 Synonyms:MTH11 Publication <p>Manually curated information that is based on statements in scientific articles for which there is no experimental support.</p> <p><a href="/manual/evidences#ECO:0000303">More...</a></p> Manual assertion based on opinion ini
|
| <p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section provides information on the name(s) of the organism that is the source of the protein sequence.<p><a href='/help/organism-name' target='_top'>More...</a></p>Organismi | Homo sapiens (Human) |
| <p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section shows the unique identifier assigned by the NCBI to the source organism of the protein. This is known as the ‘taxonomic identifier’ or ‘taxid’.<p><a href='/help/taxonomic_identifier' target='_top'>More...</a></p>Taxonomic identifieri | 9606 [NCBI] |
| <p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section contains the taxonomic hierarchical classification lineage of the source organism. It lists the nodes as they appear top-down in the taxonomic tree, with the more general grouping listed first.<p><a href='/help/taxonomic_lineage' target='_top'>More...</a></p>Taxonomic lineagei | cellular organisms › Eukaryota › Opisthokonta › Metazoa › Eumetazoa › Bilateria › Deuterostomia › Chordata › Craniata › Vertebrata › Gnathostomata › Teleostomi › Euteleostomi › Sarcopterygii › Dipnotetrapodomorpha › Tetrapoda › Amniota › Mammalia › Theria › Eutheria › Boreoeutheria › Euarchontoglires › Primates › Haplorrhini › Simiiformes › Catarrhini › Hominoidea › Hominidae › Homininae › Homo |
| <p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section is present for entries that are part of a <a href="http://www.uniprot.org/proteomes">proteome</a>, i.e. of a set of proteins thought to be expressed by organisms whose genomes have been completely sequenced.<p><a href='/help/proteomes_manual' target='_top'>More...</a></p>Proteomesi |
|
Organism-specific databases
Eukaryotic Pathogen Database Resources More...EuPathDBi | HostDB:ENSG00000106268.15 |
Human Gene Nomenclature Database More...HGNCi | HGNC:8048 NUDT1 |
Online Mendelian Inheritance in Man (OMIM) More...MIMi | 600312 gene |
neXtProt; the human protein knowledge platform More...neXtProti | NX_P36639 |
<p>This section provides information on the location and the topology of the mature protein in the cell.<p><a href='/help/subcellular_location_section' target='_top'>More...</a></p>Subcellular locationi
Mitochondrion
- Mitochondrion matrix 2 Publications
<p>Manually curated information which has been inferred by a curator based on his/her scientific knowledge or on the scientific content of an article.</p> <p><a href="/manual/evidences#ECO:0000305">More...</a></p> Manual assertion inferred by curator fromi
- Ref.16"An oxidized purine nucleoside triphosphatase, MTH1, suppresses cell death caused by oxidative stress."
Yoshimura D., Sakumi K., Ohno M., Sakai Y., Furuichi M., Iwai S., Nakabeppu Y.
J. Biol. Chem. 278:37965-37973(2003) [PubMed] [Europe PMC] [Abstract]Cited for: FUNCTION, CATALYTIC ACTIVITY, SUBCELLULAR LOCATION (ISOFORM P18). - Ref.17"The GT to GC single nucleotide polymorphism at the beginning of an alternative exon 2C of human MTH1 gene confers an amino terminal extension that functions as a mitochondrial targeting signal."
Sakai Y., Oda H., Yoshimura D., Furuichi M., Kang D., Iwai S., Hara T., Nakabeppu Y.
J. Mol. Med. 84:660-670(2006) [PubMed] [Europe PMC] [Abstract]Cited for: FUNCTION, CATALYTIC ACTIVITY, SUBCELLULAR LOCATION (ISOFORM P26), ALTERNATIVE SPLICING, CHARACTERIZATION OF VARIANT MET-124.
<p>Manually curated information for which there is published experimental evidence.</p> <p><a href="/manual/evidences#ECO:0000269">More...</a></p> Manual assertion based on experiment ini
- Ref.11"Intracellular localization of 8-oxo-dGTPase in human cells, with special reference to the role of the enzyme in mitochondria."
Kang D., Nishida J., Iyama A., Nakabeppu Y., Furuichi M., Fujiwara T., Sekiguchi M., Takeshige K.
J. Biol. Chem. 270:14659-14665(1995) [PubMed] [Europe PMC] [Abstract]Cited for: SUBCELLULAR LOCATION (ISOFORM P18), CATALYTIC ACTIVITY.
- Mitochondrion matrix 2 Publications
Cytosol
- cytosol 3 Publications
<p>Manually curated information for which there is published experimental evidence.</p> <p><a href="/manual/evidences#ECO:0000269">More...</a></p> Manual assertion based on experiment ini
- Ref.11"Intracellular localization of 8-oxo-dGTPase in human cells, with special reference to the role of the enzyme in mitochondria."
Kang D., Nishida J., Iyama A., Nakabeppu Y., Furuichi M., Fujiwara T., Sekiguchi M., Takeshige K.
J. Biol. Chem. 270:14659-14665(1995) [PubMed] [Europe PMC] [Abstract]Cited for: SUBCELLULAR LOCATION (ISOFORM P18), CATALYTIC ACTIVITY. - Ref.16"An oxidized purine nucleoside triphosphatase, MTH1, suppresses cell death caused by oxidative stress."
Yoshimura D., Sakumi K., Ohno M., Sakai Y., Furuichi M., Iwai S., Nakabeppu Y.
J. Biol. Chem. 278:37965-37973(2003) [PubMed] [Europe PMC] [Abstract]Cited for: FUNCTION, CATALYTIC ACTIVITY, SUBCELLULAR LOCATION (ISOFORM P18). - Ref.17"The GT to GC single nucleotide polymorphism at the beginning of an alternative exon 2C of human MTH1 gene confers an amino terminal extension that functions as a mitochondrial targeting signal."
Sakai Y., Oda H., Yoshimura D., Furuichi M., Kang D., Iwai S., Hara T., Nakabeppu Y.
J. Mol. Med. 84:660-670(2006) [PubMed] [Europe PMC] [Abstract]Cited for: FUNCTION, CATALYTIC ACTIVITY, SUBCELLULAR LOCATION (ISOFORM P26), ALTERNATIVE SPLICING, CHARACTERIZATION OF VARIANT MET-124.
- cytosol 3 Publications
Nucleus
- Nucleus 2 Publications
<p>Manually curated information for which there is published experimental evidence.</p> <p><a href="/manual/evidences#ECO:0000269">More...</a></p> Manual assertion based on experiment ini
- Ref.11"Intracellular localization of 8-oxo-dGTPase in human cells, with special reference to the role of the enzyme in mitochondria."
Kang D., Nishida J., Iyama A., Nakabeppu Y., Furuichi M., Fujiwara T., Sekiguchi M., Takeshige K.
J. Biol. Chem. 270:14659-14665(1995) [PubMed] [Europe PMC] [Abstract]Cited for: SUBCELLULAR LOCATION (ISOFORM P18), CATALYTIC ACTIVITY. - Ref.16"An oxidized purine nucleoside triphosphatase, MTH1, suppresses cell death caused by oxidative stress."
Yoshimura D., Sakumi K., Ohno M., Sakai Y., Furuichi M., Iwai S., Nakabeppu Y.
J. Biol. Chem. 278:37965-37973(2003) [PubMed] [Europe PMC] [Abstract]Cited for: FUNCTION, CATALYTIC ACTIVITY, SUBCELLULAR LOCATION (ISOFORM P18).
Note: Mostly present in cytosol (PubMed:7782328). A minor proportion is mitochondrial (PubMed:7782328). A very small amount of the protein is associated with nuclei (PubMed:7782328). Variant Met-124 has decreased efficiency in translocation to mitochondria (PubMed:16607562).2 Publications- Nucleus 2 Publications
- Ref.11"Intracellular localization of 8-oxo-dGTPase in human cells, with special reference to the role of the enzyme in mitochondria."
Kang D., Nishida J., Iyama A., Nakabeppu Y., Furuichi M., Fujiwara T., Sekiguchi M., Takeshige K.
J. Biol. Chem. 270:14659-14665(1995) [PubMed] [Europe PMC] [Abstract]Cited for: SUBCELLULAR LOCATION (ISOFORM P18), CATALYTIC ACTIVITY. - Ref.17"The GT to GC single nucleotide polymorphism at the beginning of an alternative exon 2C of human MTH1 gene confers an amino terminal extension that functions as a mitochondrial targeting signal."
Sakai Y., Oda H., Yoshimura D., Furuichi M., Kang D., Iwai S., Hara T., Nakabeppu Y.
J. Mol. Med. 84:660-670(2006) [PubMed] [Europe PMC] [Abstract]Cited for: FUNCTION, CATALYTIC ACTIVITY, SUBCELLULAR LOCATION (ISOFORM P26), ALTERNATIVE SPLICING, CHARACTERIZATION OF VARIANT MET-124.
<p>Manually curated information for which there is published experimental evidence.</p> <p><a href="/manual/evidences#ECO:0000269">More...</a></p> Manual assertion based on experiment ini
Mitochondrion
- Mitochondrion matrix 1 Publication
<p>Manually curated information for which there is published experimental evidence.</p> <p><a href="/manual/evidences#ECO:0000269">More...</a></p> Manual assertion based on experiment ini
- Ref.17"The GT to GC single nucleotide polymorphism at the beginning of an alternative exon 2C of human MTH1 gene confers an amino terminal extension that functions as a mitochondrial targeting signal."
Sakai Y., Oda H., Yoshimura D., Furuichi M., Kang D., Iwai S., Hara T., Nakabeppu Y.
J. Mol. Med. 84:660-670(2006) [PubMed] [Europe PMC] [Abstract]Cited for: FUNCTION, CATALYTIC ACTIVITY, SUBCELLULAR LOCATION (ISOFORM P26), ALTERNATIVE SPLICING, CHARACTERIZATION OF VARIANT MET-124.
- Mitochondrion matrix 1 Publication
Cytosol
- cytosol Source: HPA
Extracellular region or secreted
- extracellular space Source: Ensembl
Mitochondrion
- mitochondrial matrix Source: UniProtKB <p>Inferred from Direct Assay</p> <p>Used to indicate a direct assay for the function, process or component indicated by the GO term.</p> <p>More information in the <a href="http://geneontology.org/page/guide-go-evidence-codes#ida">GO evidence code guide</a></p> Inferred from direct assayi
- mitochondrion Source: UniProtKB <p>Inferred from Direct Assay</p> <p>Used to indicate a direct assay for the function, process or component indicated by the GO term.</p> <p>More information in the <a href="http://geneontology.org/page/guide-go-evidence-codes#ida">GO evidence code guide</a></p> Inferred from direct assayi
Nucleus
- nuclear membrane Source: Ensembl
- nucleus Source: UniProtKB <p>Inferred from Direct Assay</p> <p>Used to indicate a direct assay for the function, process or component indicated by the GO term.</p> <p>More information in the <a href="http://geneontology.org/page/guide-go-evidence-codes#ida">GO evidence code guide</a></p> Inferred from direct assayi
Plasma Membrane
- plasma membrane Source: Ensembl
Other locations
- acrosomal vesicle Source: Ensembl
- cytoplasm Source: UniProtKB <p>Inferred from Direct Assay</p> <p>Used to indicate a direct assay for the function, process or component indicated by the GO term.</p> <p>More information in the <a href="http://geneontology.org/page/guide-go-evidence-codes#ida">GO evidence code guide</a></p> Inferred from direct assayi
<p>UniProtKB Keywords constitute a <a href="http://www.uniprot.org/keywords">controlled vocabulary</a> with a hierarchical structure. Keywords summarise the content of a UniProtKB entry and facilitate the search for proteins of interest.<p><a href='/help/keywords' target='_top'>More...</a></p>Keywords - Cellular componenti
Cytoplasm, Mitochondrion, Nucleus<p>This section provides information on the disease(s) and phenotype(s) associated with a protein.<p><a href='/help/pathology_and_biotech_section' target='_top'>More...</a></p>Pathology & Biotechi
Mutagenesis
| Feature key | Position(s) | DescriptionActions | Graphical view | Length |
|---|---|---|---|---|
| <p>This subsection of the <a href="http://www.uniprot.org/manual/pathology_and_biotech_section">'Pathology and Biotech'</a> section describes the effect of the experimental mutation of one or more amino acid(s) on the biological properties of the protein.<p><a href='/help/mutagen' target='_top'>More...</a></p>Mutagenesisi | 68 | F → A: Reduces 2-OH-dATPase and 8-oxo-dGTPase activities. 1 Publication <p>Manually curated information for which there is published experimental evidence.</p> <p><a href="/manual/evidences#ECO:0000269">More...</a></p> Manual assertion based on experiment ini
| 1 | |
| <p>This subsection of the <a href="http://www.uniprot.org/manual/pathology_and_biotech_section">'Pathology and Biotech'</a> section describes the effect of the experimental mutation of one or more amino acid(s) on the biological properties of the protein.<p><a href='/help/mutagen' target='_top'>More...</a></p>Mutagenesisi | 77 | G → R: Reduces activity by 97%. 1 Publication <p>Manually curated information for which there is published experimental evidence.</p> <p><a href="/manual/evidences#ECO:0000269">More...</a></p> Manual assertion based on experiment ini
| 1 | |
| <p>This subsection of the <a href="http://www.uniprot.org/manual/pathology_and_biotech_section">'Pathology and Biotech'</a> section describes the effect of the experimental mutation of one or more amino acid(s) on the biological properties of the protein.<p><a href='/help/mutagen' target='_top'>More...</a></p>Mutagenesisi | 78 | G → F: Loss of activity. 1 Publication <p>Manually curated information for which there is published experimental evidence.</p> <p><a href="/manual/evidences#ECO:0000269">More...</a></p> Manual assertion based on experiment ini
| 1 | |
| <p>This subsection of the <a href="http://www.uniprot.org/manual/pathology_and_biotech_section">'Pathology and Biotech'</a> section describes the effect of the experimental mutation of one or more amino acid(s) on the biological properties of the protein.<p><a href='/help/mutagen' target='_top'>More...</a></p>Mutagenesisi | 80 | V → E: Loss of activity. 1 Publication <p>Manually curated information for which there is published experimental evidence.</p> <p><a href="/manual/evidences#ECO:0000269">More...</a></p> Manual assertion based on experiment ini
| 1 | |
| <p>This subsection of the <a href="http://www.uniprot.org/manual/pathology_and_biotech_section">'Pathology and Biotech'</a> section describes the effect of the experimental mutation of one or more amino acid(s) on the biological properties of the protein.<p><a href='/help/mutagen' target='_top'>More...</a></p>Mutagenesisi | 81 | Q → P: Reduces activity by 97%. 1 Publication <p>Manually curated information for which there is published experimental evidence.</p> <p><a href="/manual/evidences#ECO:0000269">More...</a></p> Manual assertion based on experiment ini
| 1 | |
| <p>This subsection of the <a href="http://www.uniprot.org/manual/pathology_and_biotech_section">'Pathology and Biotech'</a> section describes the effect of the experimental mutation of one or more amino acid(s) on the biological properties of the protein.<p><a href='/help/mutagen' target='_top'>More...</a></p>Mutagenesisi | 83 | G → I: Reduces activity by 60%. 1 Publication <p>Manually curated information for which there is published experimental evidence.</p> <p><a href="/manual/evidences#ECO:0000269">More...</a></p> Manual assertion based on experiment ini
| 1 | |
| <p>This subsection of the <a href="http://www.uniprot.org/manual/pathology_and_biotech_section">'Pathology and Biotech'</a> section describes the effect of the experimental mutation of one or more amino acid(s) on the biological properties of the protein.<p><a href='/help/mutagen' target='_top'>More...</a></p>Mutagenesisi | 86 | I → K: Loss of activity. 1 Publication <p>Manually curated information for which there is published experimental evidence.</p> <p><a href="/manual/evidences#ECO:0000269">More...</a></p> Manual assertion based on experiment ini
| 1 | |
| <p>This subsection of the <a href="http://www.uniprot.org/manual/pathology_and_biotech_section">'Pathology and Biotech'</a> section describes the effect of the experimental mutation of one or more amino acid(s) on the biological properties of the protein.<p><a href='/help/mutagen' target='_top'>More...</a></p>Mutagenesisi | 88 | D → P: Loss of activity. 1 Publication <p>Manually curated information for which there is published experimental evidence.</p> <p><a href="/manual/evidences#ECO:0000269">More...</a></p> Manual assertion based on experiment ini
| 1 | |
| <p>This subsection of the <a href="http://www.uniprot.org/manual/pathology_and_biotech_section">'Pathology and Biotech'</a> section describes the effect of the experimental mutation of one or more amino acid(s) on the biological properties of the protein.<p><a href='/help/mutagen' target='_top'>More...</a></p>Mutagenesisi | 89 | G → M: Loss of activity. 1 Publication <p>Manually curated information for which there is published experimental evidence.</p> <p><a href="/manual/evidences#ECO:0000269">More...</a></p> Manual assertion based on experiment ini
| 1 | |
| <p>This subsection of the <a href="http://www.uniprot.org/manual/pathology_and_biotech_section">'Pathology and Biotech'</a> section describes the effect of the experimental mutation of one or more amino acid(s) on the biological properties of the protein.<p><a href='/help/mutagen' target='_top'>More...</a></p>Mutagenesisi | 90 | A → P: Loss of activity. 1 Publication <p>Manually curated information for which there is published experimental evidence.</p> <p><a href="/manual/evidences#ECO:0000269">More...</a></p> Manual assertion based on experiment ini
| 1 | |
| <p>This subsection of the <a href="http://www.uniprot.org/manual/pathology_and_biotech_section">'Pathology and Biotech'</a> section describes the effect of the experimental mutation of one or more amino acid(s) on the biological properties of the protein.<p><a href='/help/mutagen' target='_top'>More...</a></p>Mutagenesisi | 94 | L → P: Loss of activity. 1 Publication <p>Manually curated information for which there is published experimental evidence.</p> <p><a href="/manual/evidences#ECO:0000269">More...</a></p> Manual assertion based on experiment ini
| 1 | |
| <p>This subsection of the <a href="http://www.uniprot.org/manual/pathology_and_biotech_section">'Pathology and Biotech'</a> section describes the effect of the experimental mutation of one or more amino acid(s) on the biological properties of the protein.<p><a href='/help/mutagen' target='_top'>More...</a></p>Mutagenesisi | 95 | Q → P: Loss of activity. 1 Publication <p>Manually curated information for which there is published experimental evidence.</p> <p><a href="/manual/evidences#ECO:0000269">More...</a></p> Manual assertion based on experiment ini
| 1 | |
| <p>This subsection of the <a href="http://www.uniprot.org/manual/pathology_and_biotech_section">'Pathology and Biotech'</a> section describes the effect of the experimental mutation of one or more amino acid(s) on the biological properties of the protein.<p><a href='/help/mutagen' target='_top'>More...</a></p>Mutagenesisi | 96 | E → G: Loss of activity. 1 Publication <p>Manually curated information for which there is published experimental evidence.</p> <p><a href="/manual/evidences#ECO:0000269">More...</a></p> Manual assertion based on experiment ini
| 1 | |
| <p>This subsection of the <a href="http://www.uniprot.org/manual/pathology_and_biotech_section">'Pathology and Biotech'</a> section describes the effect of the experimental mutation of one or more amino acid(s) on the biological properties of the protein.<p><a href='/help/mutagen' target='_top'>More...</a></p>Mutagenesisi | 97 | E → A: Loss of ability to prevent DNA damage. Expected to cause loss of enzyme activity. 1 Publication <p>Manually curated information for which there is published experimental evidence.</p> <p><a href="/manual/evidences#ECO:0000269">More...</a></p> Manual assertion based on experiment ini
| 1 | |
| <p>This subsection of the <a href="http://www.uniprot.org/manual/pathology_and_biotech_section">'Pathology and Biotech'</a> section describes the effect of the experimental mutation of one or more amino acid(s) on the biological properties of the protein.<p><a href='/help/mutagen' target='_top'>More...</a></p>Mutagenesisi | 97 | E → Y: Loss of activity. 1 Publication <p>Manually curated information for which there is published experimental evidence.</p> <p><a href="/manual/evidences#ECO:0000269">More...</a></p> Manual assertion based on experiment ini
| 1 | |
| <p>This subsection of the <a href="http://www.uniprot.org/manual/pathology_and_biotech_section">'Pathology and Biotech'</a> section describes the effect of the experimental mutation of one or more amino acid(s) on the biological properties of the protein.<p><a href='/help/mutagen' target='_top'>More...</a></p>Mutagenesisi | 98 | S → R: Loss of activity. 1 Publication <p>Manually curated information for which there is published experimental evidence.</p> <p><a href="/manual/evidences#ECO:0000269">More...</a></p> Manual assertion based on experiment ini
| 1 | |
| <p>This subsection of the <a href="http://www.uniprot.org/manual/pathology_and_biotech_section">'Pathology and Biotech'</a> section describes the effect of the experimental mutation of one or more amino acid(s) on the biological properties of the protein.<p><a href='/help/mutagen' target='_top'>More...</a></p>Mutagenesisi | 158 | W → A: Greatly reduces or abolishes 2-OH-dATPase and 8-oxo-dGTPase activities. 1 Publication <p>Manually curated information for which there is published experimental evidence.</p> <p><a href="/manual/evidences#ECO:0000269">More...</a></p> Manual assertion based on experiment ini
| 1 | |
| <p>This subsection of the <a href="http://www.uniprot.org/manual/pathology_and_biotech_section">'Pathology and Biotech'</a> section describes the effect of the experimental mutation of one or more amino acid(s) on the biological properties of the protein.<p><a href='/help/mutagen' target='_top'>More...</a></p>Mutagenesisi | 158 | W → Y: Enhances 2-OH-dATPase activity and greatly reduces 8-oxo-dGTPase activity. 1 Publication <p>Manually curated information for which there is published experimental evidence.</p> <p><a href="/manual/evidences#ECO:0000269">More...</a></p> Manual assertion based on experiment ini
| 1 | |
| <p>This subsection of the <a href="http://www.uniprot.org/manual/pathology_and_biotech_section">'Pathology and Biotech'</a> section describes the effect of the experimental mutation of one or more amino acid(s) on the biological properties of the protein.<p><a href='/help/mutagen' target='_top'>More...</a></p>Mutagenesisi | 160 | D → A or N: Loss of 2-OH-dATPase activity, reduces 8-oxo-dGTPase activity. 1 Publication <p>Manually curated information for which there is published experimental evidence.</p> <p><a href="/manual/evidences#ECO:0000269">More...</a></p> Manual assertion based on experiment ini
| 1 | |
| <p>This subsection of the <a href="http://www.uniprot.org/manual/pathology_and_biotech_section">'Pathology and Biotech'</a> section describes the effect of the experimental mutation of one or more amino acid(s) on the biological properties of the protein.<p><a href='/help/mutagen' target='_top'>More...</a></p>Mutagenesisi | 161 | D → A or N: Mildly decreased 2-OH-dATPase activity, nearly abolishes 8-oxo-dGTPase activity. 1 Publication <p>Manually curated information for which there is published experimental evidence.</p> <p><a href="/manual/evidences#ECO:0000269">More...</a></p> Manual assertion based on experiment ini
| 1 | |
| <p>This subsection of the <a href="http://www.uniprot.org/manual/pathology_and_biotech_section">'Pathology and Biotech'</a> section describes the effect of the experimental mutation of one or more amino acid(s) on the biological properties of the protein.<p><a href='/help/mutagen' target='_top'>More...</a></p>Mutagenesisi | 191 | L → A: Reduces 2-OH-dATPase and 8-oxo-dGTPase activities and increases thermolability. 1 Publication <p>Manually curated information for which there is published experimental evidence.</p> <p><a href="/manual/evidences#ECO:0000269">More...</a></p> Manual assertion based on experiment ini
| 1 | |
| <p>This subsection of the <a href="http://www.uniprot.org/manual/pathology_and_biotech_section">'Pathology and Biotech'</a> section describes the effect of the experimental mutation of one or more amino acid(s) on the biological properties of the protein.<p><a href='/help/mutagen' target='_top'>More...</a></p>Mutagenesisi | 192 – 197 | Missing : Almost abolishes 2-OH-dATPase and 8-oxo-dGTPase activities and increases thermolability. 1 Publication <p>Manually curated information for which there is published experimental evidence.</p> <p><a href="/manual/evidences#ECO:0000269">More...</a></p> Manual assertion based on experiment ini
| 6 | |
| <p>This subsection of the <a href="http://www.uniprot.org/manual/pathology_and_biotech_section">'Pathology and Biotech'</a> section describes the effect of the experimental mutation of one or more amino acid(s) on the biological properties of the protein.<p><a href='/help/mutagen' target='_top'>More...</a></p>Mutagenesisi | 192 | R → A: Reduces 2-OH-dATPase and 8-oxo-dGTPase activities and increases thermolability. 1 Publication <p>Manually curated information for which there is published experimental evidence.</p> <p><a href="/manual/evidences#ECO:0000269">More...</a></p> Manual assertion based on experiment ini
| 1 | |
| <p>This subsection of the <a href="http://www.uniprot.org/manual/pathology_and_biotech_section">'Pathology and Biotech'</a> section describes the effect of the experimental mutation of one or more amino acid(s) on the biological properties of the protein.<p><a href='/help/mutagen' target='_top'>More...</a></p>Mutagenesisi | 193 – 197 | Missing : Greatly reduces 2-OH-dATPase and 8-oxo-dGTPase activities and increases thermolability. 1 Publication <p>Manually curated information for which there is published experimental evidence.</p> <p><a href="/manual/evidences#ECO:0000269">More...</a></p> Manual assertion based on experiment ini
| 5 | |
| <p>This subsection of the <a href="http://www.uniprot.org/manual/pathology_and_biotech_section">'Pathology and Biotech'</a> section describes the effect of the experimental mutation of one or more amino acid(s) on the biological properties of the protein.<p><a href='/help/mutagen' target='_top'>More...</a></p>Mutagenesisi | 193 | E → A: Reduces 2-OH-dATPase and 8-oxo-dGTPase activities and increases thermolability. 1 Publication <p>Manually curated information for which there is published experimental evidence.</p> <p><a href="/manual/evidences#ECO:0000269">More...</a></p> Manual assertion based on experiment ini
| 1 | |
| <p>This subsection of the <a href="http://www.uniprot.org/manual/pathology_and_biotech_section">'Pathology and Biotech'</a> section describes the effect of the experimental mutation of one or more amino acid(s) on the biological properties of the protein.<p><a href='/help/mutagen' target='_top'>More...</a></p>Mutagenesisi | 194 – 197 | Missing : Reduces 2-OH-dATPase and 8-oxo-dGTPase activities and increases thermolability. 1 Publication <p>Manually curated information for which there is published experimental evidence.</p> <p><a href="/manual/evidences#ECO:0000269">More...</a></p> Manual assertion based on experiment ini
| 4 | |
| <p>This subsection of the <a href="http://www.uniprot.org/manual/pathology_and_biotech_section">'Pathology and Biotech'</a> section describes the effect of the experimental mutation of one or more amino acid(s) on the biological properties of the protein.<p><a href='/help/mutagen' target='_top'>More...</a></p>Mutagenesisi | 194 | V → A: Reduces 2-OH-dATPase and 8-oxo-dGTPase activities and increases thermolability. 1 Publication <p>Manually curated information for which there is published experimental evidence.</p> <p><a href="/manual/evidences#ECO:0000269">More...</a></p> Manual assertion based on experiment ini
| 1 | |
| <p>This subsection of the <a href="http://www.uniprot.org/manual/pathology_and_biotech_section">'Pathology and Biotech'</a> section describes the effect of the experimental mutation of one or more amino acid(s) on the biological properties of the protein.<p><a href='/help/mutagen' target='_top'>More...</a></p>Mutagenesisi | 195 – 197 | Missing : Slightly enhances 2-OH-dATPase and 8-oxo-dGTPase activities and increases thermolability. 1 Publication <p>Manually curated information for which there is published experimental evidence.</p> <p><a href="/manual/evidences#ECO:0000269">More...</a></p> Manual assertion based on experiment ini
| 3 | |
| <p>This subsection of the <a href="http://www.uniprot.org/manual/pathology_and_biotech_section">'Pathology and Biotech'</a> section describes the effect of the experimental mutation of one or more amino acid(s) on the biological properties of the protein.<p><a href='/help/mutagen' target='_top'>More...</a></p>Mutagenesisi | 195 | D → A: Enhances 2-OH-dATPase and 8-oxo-dGTPase activities and increases thermolability. 1 Publication <p>Manually curated information for which there is published experimental evidence.</p> <p><a href="/manual/evidences#ECO:0000269">More...</a></p> Manual assertion based on experiment ini
| 1 | |
| <p>This subsection of the <a href="http://www.uniprot.org/manual/pathology_and_biotech_section">'Pathology and Biotech'</a> section describes the effect of the experimental mutation of one or more amino acid(s) on the biological properties of the protein.<p><a href='/help/mutagen' target='_top'>More...</a></p>Mutagenesisi | 196 | T → A: Reduces 2-OH-dATPase and 8-oxo-dGTPase activities and increases thermolability. 1 Publication <p>Manually curated information for which there is published experimental evidence.</p> <p><a href="/manual/evidences#ECO:0000269">More...</a></p> Manual assertion based on experiment ini
| 1 | |
| <p>This subsection of the <a href="http://www.uniprot.org/manual/pathology_and_biotech_section">'Pathology and Biotech'</a> section describes the effect of the experimental mutation of one or more amino acid(s) on the biological properties of the protein.<p><a href='/help/mutagen' target='_top'>More...</a></p>Mutagenesisi | 197 | V → A: Slightly reduces 2-OH-dATPase and 8-oxo-dGTPase activities and increases thermolability. 1 Publication <p>Manually curated information for which there is published experimental evidence.</p> <p><a href="/manual/evidences#ECO:0000269">More...</a></p> Manual assertion based on experiment ini
| 1 |
Organism-specific databases
DisGeNET More...DisGeNETi | 4521 |
Open Targets More...OpenTargetsi | ENSG00000106268 |
The Pharmacogenetics and Pharmacogenomics Knowledge Base More...PharmGKBi | PA31830 |
Chemistry databases
ChEMBL database of bioactive drug-like small molecules More...ChEMBLi | CHEMBL3708265 |
Polymorphism and mutation databases
Domain mapping of disease mutations (DMDM) More...DMDMi | 254763430 |
<p>This section describes post-translational modifications (PTMs) and/or processing events.<p><a href='/help/ptm_processing_section' target='_top'>More...</a></p>PTM / Processingi
Molecule processing
| Feature key | Position(s) | DescriptionActions | Graphical view | Length |
|---|---|---|---|---|
| <p>This subsection of the ‘PTM / Processing’ section describes the extent of a transit peptide.<p><a href='/help/transit' target='_top'>More...</a></p>Transit peptidei | 1 – 18 | MitochondrionSequence analysisAdd BLAST | 18 | |
| <p>This subsection of the ‘PTM / Processing’ section describes the extent of a polypeptide chain in the mature protein following processing.<p><a href='/help/chain' target='_top'>More...</a></p>ChainiPRO_0000019944 | 19 – 197 | 7,8-dihydro-8-oxoguanine triphosphataseAdd BLAST | 179 |
<p>This subsection of the <a href="http://www.uniprot.org/help/ptm_processing_section">PTM/processing</a> section describes post-translational modifications (PTMs). This subsection <strong>complements</strong> the information provided at the sequence level or describes modifications for which <strong>position-specific data is not yet available</strong>.<p><a href='/help/post-translational_modification' target='_top'>More...</a></p>Post-translational modificationi
Proteomic databases
Encyclopedia of Proteome Dynamics More...EPDi | P36639 |
MaxQB - The MaxQuant DataBase More...MaxQBi | P36639 |
PaxDb, a database of protein abundance averages across all three domains of life More...PaxDbi | P36639 |
PeptideAtlas More...PeptideAtlasi | P36639 |
PRoteomics IDEntifications database More...PRIDEi | P36639 |
ProteomicsDB human proteome resource More...ProteomicsDBi | 55217 55218 [P36639-2] 55219 [P36639-3] 55220 [P36639-4] |
Consortium for Top Down Proteomics More...TopDownProteomicsi | P36639-4 [P36639-4] |
PTM databases
iPTMnet integrated resource for PTMs in systems biology context More...iPTMneti | P36639 |
Comprehensive resource for the study of protein post-translational modifications (PTMs) in human, mouse and rat. More...PhosphoSitePlusi | P36639 |
<p>This section provides information on the expression of a gene at the mRNA or protein level in cells or in tissues of multicellular organisms.<p><a href='/help/expression_section' target='_top'>More...</a></p>Expressioni
<p>This subsection of the ‘Expression’ section provides information on the expression of a gene at the mRNA or protein level in cells or in tissues of multicellular organisms. By default, the information is derived from experiments at the mRNA level, unless specified ‘at protein level’. <br></br>Examples: <a href="http://www.uniprot.org/uniprot/P92958#expression">P92958</a>, <a href="http://www.uniprot.org/uniprot/Q8TDN4#expression">Q8TDN4</a>, <a href="http://www.uniprot.org/uniprot/O14734#expression">O14734</a><p><a href='/help/tissue_specificity' target='_top'>More...</a></p>Tissue specificityi
<p>Manually curated information for which there is published experimental evidence.</p> <p><a href="/manual/evidences#ECO:0000269">More...</a></p> Manual assertion based on experiment ini
- Ref.3"Regulation of expression of the human MTH1 gene encoding 8-oxo-dGTPase. Alternative splicing of transcription products."
Oda H., Nakabeppu Y., Furuichi M., Sekiguchi M.
J. Biol. Chem. 272:17843-17850(1997) [PubMed] [Europe PMC] [Abstract]Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM P18), TISSUE SPECIFICITY, DEVELOPMENTAL STAGE, VARIANT MET-124.
<p>This subsection of the ‘Expression’ section provides information on the expression of the gene product at various stages of a cell, tissue or organism development. By default, the information is derived from experiments at the mRNA level, unless specified ‘at the protein level’.<p><a href='/help/developmental_stage' target='_top'>More...</a></p>Developmental stagei
<p>Manually curated information for which there is published experimental evidence.</p> <p><a href="/manual/evidences#ECO:0000269">More...</a></p> Manual assertion based on experiment ini
- Ref.3"Regulation of expression of the human MTH1 gene encoding 8-oxo-dGTPase. Alternative splicing of transcription products."
Oda H., Nakabeppu Y., Furuichi M., Sekiguchi M.
J. Biol. Chem. 272:17843-17850(1997) [PubMed] [Europe PMC] [Abstract]Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM P18), TISSUE SPECIFICITY, DEVELOPMENTAL STAGE, VARIANT MET-124.
Gene expression databases
Bgee dataBase for Gene Expression Evolution More...Bgeei | ENSG00000106268 |
CleanEx database of gene expression profiles More...CleanExi | HS_NUDT1 |
ExpressionAtlas, Differential and Baseline Expression More...ExpressionAtlasi | P36639 baseline and differential |
Genevisible search portal to normalized and curated expression data from Genevestigator More...Genevisiblei | P36639 HS |
Organism-specific databases
Human Protein Atlas More...HPAi | HPA012636 |
<p>This section provides information on the quaternary structure of a protein and on interaction(s) with other proteins or protein complexes.<p><a href='/help/interaction_section' target='_top'>More...</a></p>Interactioni
<p>This subsection of the <a href="http://www.uniprot.org/help/interaction_section">'Interaction'</a> section provides information about the protein quaternary structure and interaction(s) with other proteins or protein complexes (with the exception of physiological receptor-ligand interactions which are annotated in the <a href="http://www.uniprot.org/help/function_section">'Function'</a> section).<p><a href='/help/subunit_structure' target='_top'>More...</a></p>Subunit structurei
<p>Manually curated information for which there is published experimental evidence.</p> <p><a href="/manual/evidences#ECO:0000269">More...</a></p> Manual assertion based on experiment ini
- Ref.20"Structure of human MTH1, a Nudix family hydrolase that selectively degrades oxidized purine nucleoside triphosphates."
Mishima M., Sakai Y., Itoh N., Kamiya H., Furuichi M., Takahashi M., Yamagata Y., Iwai S., Nakabeppu Y., Shirakawa M.
J. Biol. Chem. 279:33806-33815(2004) [PubMed] [Europe PMC] [Abstract]Cited for: STRUCTURE BY NMR OF 42-197, SUBUNIT, COFACTOR, SUBSTRATE BINDING SITE. - Ref.22"Crystal structure of human MTH1 and the 8-oxo-dGMP product complex."
Svensson L.M., Jemth A.S., Desroses M., Loseva O., Helleday T., Hogbom M., Stenmark P.
FEBS Lett. 585:2617-2621(2011) [PubMed] [Europe PMC] [Abstract]Cited for: X-RAY CRYSTALLOGRAPHY (1.80 ANGSTROMS) OF 42-197 IN COMPLEX WITH 8-OXO-DGMP, BIOPHYSICOCHEMICAL PROPERTIES.
<p>This subsection of the '<a href="http://www.uniprot.org/help/interaction_section%27">Interaction</a> section provides information about binary protein-protein interactions. The data presented in this section are a quality-filtered subset of binary interactions automatically derived from the <a href="http://www.ebi.ac.uk/intact/">IntAct database</a>. It is updated on a monthly basis. Each binary interaction is displayed on a separate line.<p><a href='/help/binary_interactions' target='_top'>More...</a></p>Binary interactionsi
| With | Entry | #Exp. | IntAct | Notes |
|---|---|---|---|---|
| HEL-S-5 | V9HWA0 | 3 | EBI-1048967,EBI-10207332 |
Protein-protein interaction databases
The Biological General Repository for Interaction Datasets (BioGrid) More...BioGridi | 110621, 14 interactors |
Protein interaction database and analysis system More...IntActi | P36639, 11 interactors |
STRING: functional protein association networks More...STRINGi | 9606.ENSP00000339503 |
Chemistry databases
BindingDB database of measured binding affinities More...BindingDBi | P36639 |
<p>This section provides information on the tertiary and secondary structure of a protein.<p><a href='/help/structure_section' target='_top'>More...</a></p>Structurei
Secondary structure
| Feature key | Position(s) | DescriptionActions | Graphical view | Length |
|---|---|---|---|---|
| <p>This subsection of the ‘Structure’ section is used to indicate the positions of experimentally determined beta strands within the protein sequence.<p><a href='/help/strand' target='_top'>More...</a></p>Beta strandi | 45 – 54 | Combined sources <p>Manually validated information inferred from a combination of experimental and computational evidence.</p> <p><a href="/manual/evidences#ECO:0000244">More...</a></p> Manual assertion inferred from combination of experimental and computational evidencei | 10 | |
| <p>This subsection of the ‘Structure’ section is used to indicate the positions of experimentally determined beta strands within the protein sequence.<p><a href='/help/strand' target='_top'>More...</a></p>Beta strandi | 56 – 64 | Combined sources <p>Manually validated information inferred from a combination of experimental and computational evidence.</p> <p><a href="/manual/evidences#ECO:0000244">More...</a></p> Manual assertion inferred from combination of experimental and computational evidencei | 9 | |
| <p>This subsection of the ‘Structure’ section is used to indicate the positions of experimentally determined hydrogen-bonded turns within the protein sequence. These elements correspond to the DSSP secondary structure code ‘T’.<p><a href='/help/turn' target='_top'>More...</a></p>Turni | 68 – 71 | Combined sources <p>Manually validated information inferred from a combination of experimental and computational evidence.</p> <p><a href="/manual/evidences#ECO:0000244">More...</a></p> Manual assertion inferred from combination of experimental and computational evidencei | 4 | |
| <p>This subsection of the ‘Structure’ section is used to indicate the positions of experimentally determined beta strands within the protein sequence.<p><a href='/help/strand' target='_top'>More...</a></p>Beta strandi | 72 – 74 | Combined sources <p>Manually validated information inferred from a combination of experimental and computational evidence.</p> <p><a href="/manual/evidences#ECO:0000244">More...</a></p> Manual assertion inferred from combination of experimental and computational evidencei | 3 | |
| <p>This subsection of the ‘Structure’ section is used to indicate the positions of experimentally determined beta strands within the protein sequence.<p><a href='/help/strand' target='_top'>More...</a></p>Beta strandi | 76 – 79 | Combined sources <p>Manually validated information inferred from a combination of experimental and computational evidence.</p> <p><a href="/manual/evidences#ECO:0000244">More...</a></p> Manual assertion inferred from combination of experimental and computational evidencei | 4 | |
| <p>This subsection of the ‘Structure’ section is used to indicate the positions of experimentally determined helical regions within the protein sequence.<p><a href='/help/helix' target='_top'>More...</a></p>Helixi | 86 – 98 | Combined sources <p>Manually validated information inferred from a combination of experimental and computational evidence.</p> <p><a href="/manual/evidences#ECO:0000244">More...</a></p> Manual assertion inferred from combination of experimental and computational evidencei | 13 | |
| <p>This subsection of the ‘Structure’ section is used to indicate the positions of experimentally determined beta strands within the protein sequence.<p><a href='/help/strand' target='_top'>More...</a></p>Beta strandi | 101 – 103 | Combined sources <p>Manually validated information inferred from a combination of experimental and computational evidence.</p> <p><a href="/manual/evidences#ECO:0000244">More...</a></p> Manual assertion inferred from combination of experimental and computational evidencei | 3 | |
| <p>This subsection of the ‘Structure’ section is used to indicate the positions of experimentally determined beta strands within the protein sequence.<p><a href='/help/strand' target='_top'>More...</a></p>Beta strandi | 105 – 115 | Combined sources <p>Manually validated information inferred from a combination of experimental and computational evidence.</p> <p><a href="/manual/evidences#ECO:0000244">More...</a></p> Manual assertion inferred from combination of experimental and computational evidencei | 11 | |
| <p>This subsection of the ‘Structure’ section is used to indicate the positions of experimentally determined beta strands within the protein sequence.<p><a href='/help/strand' target='_top'>More...</a></p>Beta strandi | 120 – 131 | Combined sources <p>Manually validated information inferred from a combination of experimental and computational evidence.</p> <p><a href="/manual/evidences#ECO:0000244">More...</a></p> Manual assertion inferred from combination of experimental and computational evidencei | 12 | |
| <p>This subsection of the ‘Structure’ section is used to indicate the positions of experimentally determined beta strands within the protein sequence.<p><a href='/help/strand' target='_top'>More...</a></p>Beta strandi | 132 – 134 | Combined sources <p>Manually validated information inferred from a combination of experimental and computational evidence.</p> <p><a href="/manual/evidences#ECO:0000244">More...</a></p> Manual assertion inferred from combination of experimental and computational evidencei | 3 | |
| <p>This subsection of the ‘Structure’ section is used to indicate the positions of experimentally determined beta strands within the protein sequence.<p><a href='/help/strand' target='_top'>More...</a></p>Beta strandi | 140 – 148 | Combined sources <p>Manually validated information inferred from a combination of experimental and computational evidence.</p> <p><a href="/manual/evidences#ECO:0000244">More...</a></p> Manual assertion inferred from combination of experimental and computational evidencei | 9 | |
| <p>This subsection of the ‘Structure’ section is used to indicate the positions of experimentally determined helical regions within the protein sequence.<p><a href='/help/helix' target='_top'>More...</a></p>Helixi | 149 – 151 | Combined sources <p>Manually validated information inferred from a combination of experimental and computational evidence.</p> <p><a href="/manual/evidences#ECO:0000244">More...</a></p> Manual assertion inferred from combination of experimental and computational evidencei | 3 | |
| <p>This subsection of the ‘Structure’ section is used to indicate the positions of experimentally determined helical regions within the protein sequence.<p><a href='/help/helix' target='_top'>More...</a></p>Helixi | 154 – 156 | Combined sources <p>Manually validated information inferred from a combination of experimental and computational evidence.</p> <p><a href="/manual/evidences#ECO:0000244">More...</a></p> Manual assertion inferred from combination of experimental and computational evidencei | 3 | |
| <p>This subsection of the ‘Structure’ section is used to indicate the positions of experimentally determined helical regions within the protein sequence.<p><a href='/help/helix' target='_top'>More...</a></p>Helixi | 161 – 169 | Combined sources <p>Manually validated information inferred from a combination of experimental and computational evidence.</p> <p><a href="/manual/evidences#ECO:0000244">More...</a></p> Manual assertion inferred from combination of experimental and computational evidencei | 9 | |
| <p>This subsection of the ‘Structure’ section is used to indicate the positions of experimentally determined beta strands within the protein sequence.<p><a href='/help/strand' target='_top'>More...</a></p>Beta strandi | 173 – 181 | Combined sources <p>Manually validated information inferred from a combination of experimental and computational evidence.</p> <p><a href="/manual/evidences#ECO:0000244">More...</a></p> Manual assertion inferred from combination of experimental and computational evidencei | 9 | |
| <p>This subsection of the ‘Structure’ section is used to indicate the positions of experimentally determined hydrogen-bonded turns within the protein sequence. These elements correspond to the DSSP secondary structure code ‘T’.<p><a href='/help/turn' target='_top'>More...</a></p>Turni | 182 – 184 | Combined sources <p>Manually validated information inferred from a combination of experimental and computational evidence.</p> <p><a href="/manual/evidences#ECO:0000244">More...</a></p> Manual assertion inferred from combination of experimental and computational evidencei | 3 | |
| <p>This subsection of the ‘Structure’ section is used to indicate the positions of experimentally determined beta strands within the protein sequence.<p><a href='/help/strand' target='_top'>More...</a></p>Beta strandi | 185 – 195 | Combined sources <p>Manually validated information inferred from a combination of experimental and computational evidence.</p> <p><a href="/manual/evidences#ECO:0000244">More...</a></p> Manual assertion inferred from combination of experimental and computational evidencei | 11 |
3D structure databases
Protein Model Portal of the PSI-Nature Structural Biology Knowledgebase More...ProteinModelPortali | P36639 |
SWISS-MODEL Repository - a database of annotated 3D protein structure models More...SMRi | P36639 |
Database of comparative protein structure models More...ModBasei | Search... |
MobiDB: a database of protein disorder and mobility annotations More...MobiDBi | Search... |
Miscellaneous databases
Relative evolutionary importance of amino acids within a protein sequence More...EvolutionaryTracei | P36639 |
<p>This section provides information on sequence similarities with other proteins and the domain(s) present in a protein.<p><a href='/help/family_and_domains_section' target='_top'>More...</a></p>Family & Domainsi
Domains and Repeats
| Feature key | Position(s) | DescriptionActions | Graphical view | Length |
|---|---|---|---|---|
| <p>This subsection of the <a href="http://www.uniprot.org/help/family_and_domains_section">Family and Domains</a> section describes the position and type of a domain, which is defined as a specific combination of secondary structures organized into a characteristic three-dimensional structure or fold.<p><a href='/help/domain' target='_top'>More...</a></p>Domaini | 44 – 173 | Nudix hydrolasePROSITE-ProRule annotation <p>Manual validated information which has been generated by the UniProtKB automatic annotation system.</p> <p><a href="/manual/evidences#ECO:0000255">More...</a></p> Manual assertion according to rulesi Add BLAST | 130 |
Region
| Feature key | Position(s) | DescriptionActions | Graphical view | Length |
|---|---|---|---|---|
| <p>This subsection of the ‘Family and Domains’ section describes a region of interest that cannot be described in other subsections.<p><a href='/help/region' target='_top'>More...</a></p>Regioni | 76 – 79 | Substrate bindingCombined sources <p>Manually validated information inferred from a combination of experimental and computational evidence.</p> <p><a href="/manual/evidences#ECO:0000244">More...</a></p> Manual assertion inferred from combination of experimental and computational evidencei 1 Publication<p>Manually curated information for which there is published experimental evidence.</p> <p><a href="/manual/evidences#ECO:0000269">More...</a></p> Manual assertion based on experiment ini
| 4 | |
| <p>This subsection of the ‘Family and Domains’ section describes a region of interest that cannot be described in other subsections.<p><a href='/help/region' target='_top'>More...</a></p>Regioni | 158 – 161 | Substrate bindingCombined sources <p>Manually validated information inferred from a combination of experimental and computational evidence.</p> <p><a href="/manual/evidences#ECO:0000244">More...</a></p> Manual assertion inferred from combination of experimental and computational evidencei 2 Publications<p>Manually curated information for which there is published experimental evidence.</p> <p><a href="/manual/evidences#ECO:0000269">More...</a></p> Manual assertion based on experiment ini
| 4 |
Motif
| Feature key | Position(s) | DescriptionActions | Graphical view | Length |
|---|---|---|---|---|
| <p>This subsection of the ‘Family and Domains’ section describes a short (usually not more than 20 amino acids) conserved sequence motif of biological significance.<p><a href='/help/motif' target='_top'>More...</a></p>Motifi | 78 – 99 | Nudix boxPROSITE-ProRule annotation <p>Manual validated information which has been generated by the UniProtKB automatic annotation system.</p> <p><a href="/manual/evidences#ECO:0000255">More...</a></p> Manual assertion according to rulesi Add BLAST | 22 |
<p>This subsection of the ‘Family and domains’ section provides information about the sequence similarity with other proteins.<p><a href='/help/sequence_similarities' target='_top'>More...</a></p>Sequence similaritiesi
<p>UniProtKB Keywords constitute a <a href="http://www.uniprot.org/keywords">controlled vocabulary</a> with a hierarchical structure. Keywords summarise the content of a UniProtKB entry and facilitate the search for proteins of interest.<p><a href='/help/keywords' target='_top'>More...</a></p>Keywords - Domaini
Transit peptidePhylogenomic databases
evolutionary genealogy of genes: Non-supervised Orthologous Groups More...eggNOGi | ENOG410IXIA Eukaryota COG0494 LUCA |
Ensembl GeneTree More...GeneTreei | ENSGT00390000000341 |
The HOGENOM Database of Homologous Genes from Fully Sequenced Organisms More...HOGENOMi | HOG000261970 |
The HOVERGEN Database of Homologous Vertebrate Genes More...HOVERGENi | HBG000032 |
InParanoid: Eukaryotic Ortholog Groups More...InParanoidi | P36639 |
KEGG Orthology (KO) More...KOi | K17816 |
Identification of Orthologs from Complete Genome Data More...OMAi | GAGKWNG |
Database of Orthologous Groups More...OrthoDBi | EOG091G0O4Y |
Database for complete collections of gene phylogenies More...PhylomeDBi | P36639 |
TreeFam database of animal gene trees More...TreeFami | TF106348 |
Family and domain databases
Integrated resource of protein families, domains and functional sites More...InterProi | View protein in InterPro IPR020476 Nudix_hydrolase IPR015797 NUDIX_hydrolase-like_dom_sf IPR020084 NUDIX_hydrolase_CS IPR000086 NUDIX_hydrolase_dom IPR003563 OxG-triPHTase |
Pfam protein domain database More...Pfami | View protein in Pfam PF00293 NUDIX, 1 hit |
Protein Motif fingerprint database; a protein domain database More...PRINTSi | PR01403 8OXTPHPHTASE PR00502 NUDIXFAMILY |
Superfamily database of structural and functional annotation More...SUPFAMi | SSF55811 SSF55811, 1 hit |
PROSITE; a protein domain and family database More...PROSITEi | View protein in PROSITE PS51462 NUDIX, 1 hit PS00893 NUDIX_BOX, 1 hit |
<p>This section displays by default the canonical protein sequence and upon request all isoforms described in the entry. It also includes information pertinent to the sequence(s), including <a href="http://www.uniprot.org/help/sequence_length">length</a> and <a href="http://www.uniprot.org/help/sequences">molecular weight</a>.<p><a href='/help/sequences_section' target='_top'>More...</a></p>Sequences (4)i
<p>This subsection of the <a href="http://www.uniprot.org/help/sequences_section">Sequence</a> section indicates if the <a href="http://www.uniprot.org/help/canonical_and_isoforms">canonical sequence</a> displayed by default in the entry is complete or not.<p><a href='/help/sequence_status' target='_top'>More...</a></p>Sequence statusi: Complete.
<p>This subsection of the <a href="http://www.uniprot.org/help/sequences_section">Sequence</a> section indicates if the <a href="http://www.uniprot.org/help/canonical_and_isoforms">canonical sequence</a> displayed by default in the entry is in its mature form or if it represents the precursor.<p><a href='/help/sequence_processing' target='_top'>More...</a></p>Sequence processingi: The displayed sequence is further processed into a mature form.
This entry describes 4 <p>This subsection of the ‘Sequence’ section lists the alternative protein sequences (isoforms) that can be generated from the same gene by a single or by the combination of up to four biological events (alternative promoter usage, alternative splicing, alternative initiation and ribosomal frameshifting). Additionally, this section gives relevant information on each alternative protein isoform.<p><a href='/help/alternative_products' target='_top'>More...</a></p> isoformsi produced by alternative initiation. AlignAdd to basketAdded to basket
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.
10 20 30 40 50
MYWSNQITRR LGERVQGFMS GISPQQMGEP EGSWSGKNPG TMGASRLYTL
60 70 80 90 100
VLVLQPQRVL LGMKKRGFGA GRWNGFGGKV QEGETIEDGA RRELQEESGL
110 120 130 140 150
TVDALHKVGQ IVFEFVGEPE LMDVHVFCTD SIQGTPVESD EMRPCWFQLD
160 170 180 190
QIPFKDMWPD DSYWFPLLLQ KKKFHGYFKF QGQDTILDYT LREVDTV
The sequence of this isoform differs from the canonical sequence as follows:
1-18: Missing.
10 20 30 40 50
MSGISPQQMG EPEGSWSGKN PGTMGASRLY TLVLVLQPQR VLLGMKKRGF
60 70 80 90 100
GAGRWNGFGG KVQEGETIED GARRELQEES GLTVDALHKV GQIVFEFVGE
110 120 130 140 150
PELMDVHVFC TDSIQGTPVE SDEMRPCWFQ LDQIPFKDMW PDDSYWFPLL
160 170
LQKKKFHGYF KFQGQDTILD YTLREVDTV
The sequence of this isoform differs from the canonical sequence as follows:
1-26: Missing.
10 20 30 40 50
MGEPEGSWSG KNPGTMGASR LYTLVLVLQP QRVLLGMKKR GFGAGRWNGF
60 70 80 90 100
GGKVQEGETI EDGARRELQE ESGLTVDALH KVGQIVFEFV GEPELMDVHV
110 120 130 140 150
FCTDSIQGTP VESDEMRPCW FQLDQIPFKD MWPDDSYWFP LLLQKKKFHG
160 170
YFKFQGQDTI LDYTLREVDT V
The sequence of this isoform differs from the canonical sequence as follows:
1-41: Missing.
10 20 30 40 50
MGASRLYTLV LVLQPQRVLL GMKKRGFGAG RWNGFGGKVQ EGETIEDGAR
60 70 80 90 100
RELQEESGLT VDALHKVGQI VFEFVGEPEL MDVHVFCTDS IQGTPVESDE
110 120 130 140 150
MRPCWFQLDQ IPFKDMWPDD SYWFPLLLQK KKFHGYFKFQ GQDTILDYTL
REVDTV
<p>This subsection of the ‘Sequence’ section provides information on polymorphic variants. If the variant is associated with a disease state, the description of the latter can be found in the <a href="http://www.uniprot.org/manual/involvement_in_disease">'Involvement in disease'</a> subsection.<p><a href='/help/polymorphism' target='_top'>More...</a></p>Polymorphismi
<p>Manually curated information for which there is published experimental evidence.</p> <p><a href="/manual/evidences#ECO:0000269">More...</a></p> Manual assertion based on experiment ini
- Ref.4"Multi-forms of human MTH1 polypeptides produced by alternative translation initiation and single nucleotide polymorphism."
Oda H., Taketomi A., Maruyama R., Itoh R., Nishioka K., Yakushiji H., Suzuki T., Sekiguchi M., Nakabeppu Y.
Nucleic Acids Res. 27:4335-4343(1999) [PubMed] [Europe PMC] [Abstract]Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS P18/P21/P22/P26), ALTERNATIVE INITIATION, POLYMORPHISM.
Natural variant
| Feature key | Position(s) | DescriptionActions | Graphical view | Length |
|---|---|---|---|---|
| <p>This subsection of the ‘Sequence’ section describes natural variant(s) of the protein sequence.<p><a href='/help/variant' target='_top'>More...</a></p>Natural variantiVAR_068715 | 77 | G → W. Corresponds to variant dbSNP:rs11547459Ensembl. | 1 | |
| <p>This subsection of the ‘Sequence’ section describes natural variant(s) of the protein sequence.<p><a href='/help/variant' target='_top'>More...</a></p>Natural variantiVAR_013757 | 124 | V → M Associated with type I diabetes in Japanese female population; may be associated with an increased risk for small cell lung carcinoma (SCLC); decreased efficiency of translocation to mitochondria. 5 Publications <p>Manually curated information for which there is published experimental evidence.</p> <p><a href="/manual/evidences#ECO:0000269">More...</a></p> Manual assertion based on experiment ini
| 1 |
Alternative sequence
| Feature key | Position(s) | DescriptionActions | Graphical view | Length |
|---|---|---|---|---|
| <p>This subsection of the ‘Sequence’ section describes the sequence of naturally occurring alternative protein isoform(s). The changes in the amino acid sequence may be due to alternative splicing, alternative promoter usage, alternative initiation, or ribosomal frameshifting. The information stored in this subsection is used to automatically construct alternative protein sequence(s) for display.<p><a href='/help/var_seq' target='_top'>More...</a></p>Alternative sequenceiVSP_018814 | 1 – 41 | Missing in isoform p18. 4 Publications <p>Manually curated information that is based on statements in scientific articles for which there is no experimental support.</p> <p><a href="/manual/evidences#ECO:0000303">More...</a></p> Manual assertion based on opinion ini
| 41 | |
| <p>This subsection of the ‘Sequence’ section describes the sequence of naturally occurring alternative protein isoform(s). The changes in the amino acid sequence may be due to alternative splicing, alternative promoter usage, alternative initiation, or ribosomal frameshifting. The information stored in this subsection is used to automatically construct alternative protein sequence(s) for display.<p><a href='/help/var_seq' target='_top'>More...</a></p>Alternative sequenceiVSP_018813 | 1 – 26 | Missing in isoform p21. CuratedAdd BLAST | 26 | |
| <p>This subsection of the ‘Sequence’ section describes the sequence of naturally occurring alternative protein isoform(s). The changes in the amino acid sequence may be due to alternative splicing, alternative promoter usage, alternative initiation, or ribosomal frameshifting. The information stored in this subsection is used to automatically construct alternative protein sequence(s) for display.<p><a href='/help/var_seq' target='_top'>More...</a></p>Alternative sequenceiVSP_018812 | 1 – 18 | Missing in isoform p22. 1 Publication <p>Manually curated information that is based on statements in scientific articles for which there is no experimental support.</p> <p><a href="/manual/evidences#ECO:0000303">More...</a></p> Manual assertion based on opinion ini
| 18 |
Sequence databases
| Select the link destinations: EMBL nucleotide sequence database More...EMBLiGenBank nucleotide sequence database More...GenBankiDNA Data Bank of Japan; a nucleotide sequence database More...DDBJiLinks Updated | D16581 mRNA Translation: BAA04013.1 D38594 Genomic DNA Translation: BAA07601.1 AB025233 mRNA Translation: BAA83791.1 AB025234 mRNA Translation: BAA83792.1 AB025235 mRNA Translation: BAA83793.1 AB025236 mRNA Translation: BAA83794.1 AB025237 mRNA Translation: BAA83795.1 AB025238 mRNA Translation: BAA83796.1 AB025239 mRNA Translation: BAA83797.1 AB025240 mRNA Translation: BAA83798.1 AB025241 mRNA Translation: BAA83799.1 AB025242 mRNA Translation: BAA83800.1 DQ230907 Genomic DNA Translation: ABB02181.1 CH236953 Genomic DNA Translation: EAL23948.1 CH236953 Genomic DNA Translation: EAL23949.1 CR407655 mRNA Translation: CAG28583.1 CH471144 Genomic DNA Translation: EAW87225.1 CH471144 Genomic DNA Translation: EAW87227.1 AC004971 Genomic DNA No translation available. BC014618 mRNA Translation: AAH14618.1 BC040144 mRNA Translation: AAH40144.2 BC051375 mRNA Translation: AAH51375.2 BC065367 mRNA Translation: AAH65367.1 |
The Consensus CDS (CCDS) project More...CCDSi | CCDS5329.1 [P36639-2] CCDS5330.1 [P36639-4] |
NCBI Reference Sequences More...RefSeqi | NP_002443.3, NM_002452.3 [P36639-4] NP_945186.1, NM_198948.1 [P36639-4] NP_945187.1, NM_198949.1 [P36639-2] NP_945188.1, NM_198950.1 [P36639-4] NP_945190.1, NM_198952.1 [P36639-2] NP_945191.1, NM_198953.1 [P36639-4] NP_945192.1, NM_198954.1 [P36639-2] |
UniGene gene-oriented nucleotide sequence clusters More...UniGenei | Hs.534331 |
Genome annotation databases
Ensembl eukaryotic genome annotation project More...Ensembli | ENST00000339737; ENSP00000343439; ENSG00000106268 [P36639-4] ENST00000343985; ENSP00000339503; ENSG00000106268 [P36639-2] ENST00000356714; ENSP00000349148; ENSG00000106268 [P36639-4] ENST00000397046; ENSP00000380239; ENSG00000106268 [P36639-4] ENST00000397048; ENSP00000380241; ENSG00000106268 [P36639-2] ENST00000397049; ENSP00000380242; ENSG00000106268 [P36639-4] |
Database of genes from NCBI RefSeq genomes More...GeneIDi | 4521 |
KEGG: Kyoto Encyclopedia of Genes and Genomes More...KEGGi | hsa:4521 |
UCSC genome browser More...UCSCi | uc003slr.1 human [P36639-1] |
<p>UniProtKB Keywords constitute a <a href="http://www.uniprot.org/keywords">controlled vocabulary</a> with a hierarchical structure. Keywords summarise the content of a UniProtKB entry and facilitate the search for proteins of interest.<p><a href='/help/keywords' target='_top'>More...</a></p>Keywords - Coding sequence diversityi
Alternative initiation, Polymorphism<p>This section provides links to proteins that are similar to the protein sequence(s) described in this entry at different levels of sequence identity thresholds (100%, 90% and 50%) based on their membership in UniProt Reference Clusters (<a href="http://www.uniprot.org/help/uniref">UniRef</a>).<p><a href='/help/similar_proteins_section' target='_top'>More...</a></p>Similar proteinsi
| Protein | Similar proteins | Species | Score | Length | |
|---|---|---|---|---|---|
| P36639 | Nudix (Nucleoside diphosphate linked moiety X)-type motif 1, isoform CRA_b | 179 | |||
| P36639-2 | 179 | ||||
| P36639-3 | 171 | ||||
| P36639-4 | Nudix (Nucleoside diphosphate linked moiety X)-type motif 1, isoform CRA_a | 156 | |||
| NUDT1 isoform 1 | 156 | ||||
| NUDT1 isoform 4 (Fragment) | 37 | ||||
| UPI000CEFFE93 | 216 | ||||
| 7,8-dihydro-8-oxoguanine triphosphatase (Fragment) | 37 | ||||
| +1 | |||||
| Protein | Similar proteins | Species | Score | Length | |
|---|---|---|---|---|---|
| P36639 | Nudix (Nucleoside diphosphate linked moiety X)-type motif 1, isoform CRA_b | 179 | |||
| NUDT1 isoform 3 | 179 | ||||
| NUDT1 isoform 3 | 179 | ||||
| UPI00020AEBE9 | 179 | ||||
| Nudix hydrolase 1 | 178 | ||||
| +13 | |||||
| Protein | Similar proteins | Species | Score | Length | |
|---|---|---|---|---|---|
| P36639 | Nudix (Nucleoside diphosphate linked moiety X)-type motif 1, isoform CRA_b | 179 | |||
| UPI00020AEBE9 | 179 | ||||
| NUDT1 isoform 3 | 179 | ||||
| NUDT1 isoform 3 | 179 | ||||
| Nudix hydrolase 1 | 178 | ||||
| +58 | |||||
<p>This section is used to point to information related to entries and found in data collections other than UniProtKB.<p><a href='/help/cross_references_section' target='_top'>More...</a></p>Cross-referencesi
<p>This subsection of the <a href="http://www.uniprot.org/manual/cross_references_section">Cross-references</a> section provides links to various web resources that are relevant for a specific protein.<p><a href='/help/web_resource' target='_top'>More...</a></p>Web resourcesi
| NIEHS-SNPs |
Sequence databases
| Select the link destinations: EMBL nucleotide sequence database More...EMBLiGenBank nucleotide sequence database More...GenBankiDNA Data Bank of Japan; a nucleotide sequence database More...DDBJiLinks Updated | D16581 mRNA Translation: BAA04013.1 D38594 Genomic DNA Translation: BAA07601.1 AB025233 mRNA Translation: BAA83791.1 AB025234 mRNA Translation: BAA83792.1 AB025235 mRNA Translation: BAA83793.1 AB025236 mRNA Translation: BAA83794.1 AB025237 mRNA Translation: BAA83795.1 AB025238 mRNA Translation: BAA83796.1 AB025239 mRNA Translation: BAA83797.1 AB025240 mRNA Translation: BAA83798.1 AB025241 mRNA Translation: BAA83799.1 AB025242 mRNA Translation: BAA83800.1 DQ230907 Genomic DNA Translation: ABB02181.1 CH236953 Genomic DNA Translation: EAL23948.1 CH236953 Genomic DNA Translation: EAL23949.1 CR407655 mRNA Translation: CAG28583.1 CH471144 Genomic DNA Translation: EAW87225.1 CH471144 Genomic DNA Translation: EAW87227.1 AC004971 Genomic DNA No translation available. BC014618 mRNA Translation: AAH14618.1 BC040144 mRNA Translation: AAH40144.2 BC051375 mRNA Translation: AAH51375.2 BC065367 mRNA Translation: AAH65367.1 |
The Consensus CDS (CCDS) project More...CCDSi | CCDS5329.1 [P36639-2] CCDS5330.1 [P36639-4] |
NCBI Reference Sequences More...RefSeqi | NP_002443.3, NM_002452.3 [P36639-4] NP_945186.1, NM_198948.1 [P36639-4] NP_945187.1, NM_198949.1 [P36639-2] NP_945188.1, NM_198950.1 [P36639-4] NP_945190.1, NM_198952.1 [P36639-2] NP_945191.1, NM_198953.1 [P36639-4] NP_945192.1, NM_198954.1 [P36639-2] |
UniGene gene-oriented nucleotide sequence clusters More...UniGenei | Hs.534331 |
3D structure databases
| Select the link destinations: Protein Data Bank Europe More...PDBeiProtein Data Bank RCSB More...RCSB PDBiProtein Data Bank Japan More...PDBjiLinks Updated | PDB entry | Method | Resolution (Å) | Chain | Positions | PDBsum |
| 1IRY | NMR | - | A | 42-197 | [»] | |
| 3Q93 | X-ray | 1.80 | A/B | 42-197 | [»] | |
| 3WHW | X-ray | 2.70 | A/B | 42-197 | [»] | |
| 3ZR0 | X-ray | 1.80 | A/B | 42-197 | [»] | |
| 3ZR1 | X-ray | 1.90 | A/B | 42-197 | [»] | |
| 4C9W | X-ray | 1.65 | A | 42-197 | [»] | |
| 4C9X | X-ray | 1.20 | A | 42-197 | [»] | |
| 4N1T | X-ray | 1.60 | A | 42-197 | [»] | |
| 4N1U | X-ray | 1.60 | A/B | 42-196 | [»] | |
| 5ANS | X-ray | 1.60 | A | 42-197 | [»] | |
| 5ANT | X-ray | 2.00 | A/B/C | 42-197 | [»] | |
| 5ANU | X-ray | 1.80 | A | 42-197 | [»] | |
| 5ANV | X-ray | 1.16 | A | 42-197 | [»] | |
| 5ANW | X-ray | 1.37 | A | 42-197 | [»] | |
| 5FSI | X-ray | 1.63 | A | 42-197 | [»] | |
| 5FSK | X-ray | 1.56 | A | 42-197 | [»] | |
| 5FSL | X-ray | 1.24 | A | 42-197 | [»] | |
| 5FSM | X-ray | 1.67 | A | 42-197 | [»] | |
| 5FSN | X-ray | 1.69 | A | 42-197 | [»] | |
| 5FSO | X-ray | 1.67 | A | 42-197 | [»] | |
| 5GHI | X-ray | 1.21 | A/B | 42-197 | [»] | |
| 5GHJ | X-ray | 1.20 | A/B | 42-197 | [»] | |
| 5GHM | X-ray | 1.50 | A/B | 42-197 | [»] | |
| 5GHN | X-ray | 1.39 | A/B | 42-197 | [»] | |
| 5GHO | X-ray | 1.19 | A/B | 42-197 | [»] | |
| 5GHP | X-ray | 1.19 | A/B | 42-197 | [»] | |
| 5GHQ | X-ray | 1.18 | A/B | 42-197 | [»] | |
| 5NGR | X-ray | 2.20 | A/B | 42-197 | [»] | |
| 5NGS | X-ray | 1.85 | A/B | 42-197 | [»] | |
| 5NGT | X-ray | 1.54 | A | 42-197 | [»] | |
| 5NHY | X-ray | 1.72 | A/B | 42-197 | [»] | |
| 5WS7 | X-ray | 1.00 | A/B | 42-197 | [»] | |
| 6F1X | X-ray | 1.90 | A/B | 42-197 | [»] | |
| 6F20 | X-ray | 2.00 | A/B | 42-197 | [»] | |
| 6F22 | X-ray | 1.55 | A/B | 42-197 | [»] | |
| 6F23 | X-ray | 1.84 | A/B | 42-197 | [»] | |
Protein Model Portal of the PSI-Nature Structural Biology Knowledgebase More...ProteinModelPortali | P36639 | |||||
SWISS-MODEL Repository - a database of annotated 3D protein structure models More...SMRi | P36639 | |||||
Database of comparative protein structure models More...ModBasei | Search... | |||||
MobiDB: a database of protein disorder and mobility annotations More...MobiDBi | Search... | |||||
Protein-protein interaction databases
The Biological General Repository for Interaction Datasets (BioGrid) More...BioGridi | 110621, 14 interactors |
Protein interaction database and analysis system More...IntActi | P36639, 11 interactors |
STRING: functional protein association networks More...STRINGi | 9606.ENSP00000339503 |
Chemistry databases
BindingDB database of measured binding affinities More...BindingDBi | P36639 |
ChEMBL database of bioactive drug-like small molecules More...ChEMBLi | CHEMBL3708265 |
PTM databases
iPTMnet integrated resource for PTMs in systems biology context More...iPTMneti | P36639 |
Comprehensive resource for the study of protein post-translational modifications (PTMs) in human, mouse and rat. More...PhosphoSitePlusi | P36639 |
Polymorphism and mutation databases
Domain mapping of disease mutations (DMDM) More...DMDMi | 254763430 |
Proteomic databases
Encyclopedia of Proteome Dynamics More...EPDi | P36639 |
MaxQB - The MaxQuant DataBase More...MaxQBi | P36639 |
PaxDb, a database of protein abundance averages across all three domains of life More...PaxDbi | P36639 |
PeptideAtlas More...PeptideAtlasi | P36639 |
PRoteomics IDEntifications database More...PRIDEi | P36639 |
ProteomicsDB human proteome resource More...ProteomicsDBi | 55217 55218 [P36639-2] 55219 [P36639-3] 55220 [P36639-4] |
Consortium for Top Down Proteomics More...TopDownProteomicsi | P36639-4 [P36639-4] |
Protocols and materials databases
The DNASU plasmid repository More...DNASUi | 4521 |
| Structural Biology Knowledgebase | Search... |
Genome annotation databases
Ensembl eukaryotic genome annotation project More...Ensembli | ENST00000339737; ENSP00000343439; ENSG00000106268 [P36639-4] ENST00000343985; ENSP00000339503; ENSG00000106268 [P36639-2] ENST00000356714; ENSP00000349148; ENSG00000106268 [P36639-4] ENST00000397046; ENSP00000380239; ENSG00000106268 [P36639-4] ENST00000397048; ENSP00000380241; ENSG00000106268 [P36639-2] ENST00000397049; ENSP00000380242; ENSG00000106268 [P36639-4] |
Database of genes from NCBI RefSeq genomes More...GeneIDi | 4521 |
KEGG: Kyoto Encyclopedia of Genes and Genomes More...KEGGi | hsa:4521 |
UCSC genome browser More...UCSCi | uc003slr.1 human [P36639-1] |
Organism-specific databases
Comparative Toxicogenomics Database More...CTDi | 4521 |
DisGeNET More...DisGeNETi | 4521 |
Eukaryotic Pathogen Database Resources More...EuPathDBi | HostDB:ENSG00000106268.15 |
GeneCards: human genes, protein and diseases More...GeneCardsi | NUDT1 |
Human Gene Nomenclature Database More...HGNCi | HGNC:8048 NUDT1 |
Human Protein Atlas More...HPAi | HPA012636 |
Online Mendelian Inheritance in Man (OMIM) More...MIMi | 600312 gene |
neXtProt; the human protein knowledge platform More...neXtProti | NX_P36639 |
Open Targets More...OpenTargetsi | ENSG00000106268 |
The Pharmacogenetics and Pharmacogenomics Knowledge Base More...PharmGKBi | PA31830 |
GenAtlas: human gene database More...GenAtlasi | Search... |
Phylogenomic databases
evolutionary genealogy of genes: Non-supervised Orthologous Groups More...eggNOGi | ENOG410IXIA Eukaryota COG0494 LUCA |
Ensembl GeneTree More...GeneTreei | ENSGT00390000000341 |
The HOGENOM Database of Homologous Genes from Fully Sequenced Organisms More...HOGENOMi | HOG000261970 |
The HOVERGEN Database of Homologous Vertebrate Genes More...HOVERGENi | HBG000032 |
InParanoid: Eukaryotic Ortholog Groups More...InParanoidi | P36639 |
KEGG Orthology (KO) More...KOi | K17816 |
Identification of Orthologs from Complete Genome Data More...OMAi | GAGKWNG |
Database of Orthologous Groups More...OrthoDBi | EOG091G0O4Y |
Database for complete collections of gene phylogenies More...PhylomeDBi | P36639 |
TreeFam database of animal gene trees More...TreeFami | TF106348 |
Enzyme and pathway databases
BioCyc Collection of Pathway/Genome Databases More...BioCyci | MetaCyc:HS02879-MONOMER |
BRENDA Comprehensive Enzyme Information System More...BRENDAi | 3.6.1.55 2681 3.6.1.56 2681 |
Reactome - a knowledgebase of biological pathways and processes More...Reactomei | R-HSA-2393930 Phosphate bond hydrolysis by NUDT proteins |
SABIO-RK: Biochemical Reaction Kinetics Database More...SABIO-RKi | P36639 |
Miscellaneous databases
Relative evolutionary importance of amino acids within a protein sequence More...EvolutionaryTracei | P36639 |
The Gene Wiki collection of pages on human genes and proteins More...GeneWikii | NUDT1 |
Database of phenotypes from RNA interference screens in Drosophila and Homo sapiens More...GenomeRNAii | 4521 |
Protein Ontology More...PROi | PR:P36639 |
The Stanford Online Universal Resource for Clones and ESTs More...SOURCEi | Search... |
Gene expression databases
Bgee dataBase for Gene Expression Evolution More...Bgeei | ENSG00000106268 |
CleanEx database of gene expression profiles More...CleanExi | HS_NUDT1 |
ExpressionAtlas, Differential and Baseline Expression More...ExpressionAtlasi | P36639 baseline and differential |
Genevisible search portal to normalized and curated expression data from Genevestigator More...Genevisiblei | P36639 HS |
Family and domain databases
Integrated resource of protein families, domains and functional sites More...InterProi | View protein in InterPro IPR020476 Nudix_hydrolase IPR015797 NUDIX_hydrolase-like_dom_sf IPR020084 NUDIX_hydrolase_CS IPR000086 NUDIX_hydrolase_dom IPR003563 OxG-triPHTase |
Pfam protein domain database More...Pfami | View protein in Pfam PF00293 NUDIX, 1 hit |
Protein Motif fingerprint database; a protein domain database More...PRINTSi | PR01403 8OXTPHPHTASE PR00502 NUDIXFAMILY |
Superfamily database of structural and functional annotation More...SUPFAMi | SSF55811 SSF55811, 1 hit |
PROSITE; a protein domain and family database More...PROSITEi | View protein in PROSITE PS51462 NUDIX, 1 hit PS00893 NUDIX_BOX, 1 hit |
ProtoNet; Automatic hierarchical classification of proteins More...ProtoNeti | Search... |
<p>This section provides general information on the entry.<p><a href='/help/entry_information_section' target='_top'>More...</a></p>Entry informationi
| <p>This subsection of the ‘Entry information’ section provides a mnemonic identifier for a UniProtKB entry, but it is not a stable identifier. Each reviewed entry is assigned a unique entry name upon integration into UniProtKB/Swiss-Prot.<p><a href='/help/entry_name' target='_top'>More...</a></p>Entry namei | 8ODP_HUMAN | |
| <p>This subsection of the ‘Entry information’ section provides one or more accession number(s). These are stable identifiers and should be used to cite UniProtKB entries. Upon integration into UniProtKB, each entry is assigned a unique accession number, which is called ‘Primary (citable) accession number’.<p><a href='/help/accession_numbers' target='_top'>More...</a></p>Accessioni | P36639Primary (citable) accession number: P36639 Secondary accession number(s): A4D205 , Q6LES7, Q6P0Y6, Q7Z7N6, Q8IV95, Q9UBM0, Q9UBM9 | |
| <p>This subsection of the ‘Entry information’ section shows the date of integration of the entry into UniProtKB, the date of the last sequence update and the date of the last annotation modification (‘Last modified’). The version number for both the entry and the <a href="http://www.uniprot.org/help/canonical_and_isoforms">canonical sequence</a> are also displayed.<p><a href='/help/entry_history' target='_top'>More...</a></p>Entry historyi | Integrated into UniProtKB/Swiss-Prot: | June 1, 1994 |
| Last sequence update: | July 28, 2009 | |
| Last modified: | July 18, 2018 | |
| This is version 178 of the entry and version 3 of the sequence. See complete history. | ||
| <p>This subsection of the ‘Entry information’ section indicates whether the entry has been manually annotated and reviewed by UniProtKB curators or not, in other words, if the entry belongs to the Swiss-Prot section of UniProtKB (<strong>reviewed</strong>) or to the computer-annotated TrEMBL section (<strong>unreviewed</strong>).<p><a href='/help/entry_status' target='_top'>More...</a></p>Entry statusi | Reviewed (UniProtKB/Swiss-Prot) | |
| Annotation program | Chordata Protein Annotation Program | |
| Disclaimer | Any 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. | |
<p>This section contains any relevant information that doesn’t fit in any other defined sections<p><a href='/help/miscellaneous_section' target='_top'>More...</a></p>Miscellaneousi
<p>UniProtKB Keywords constitute a <a href="http://www.uniprot.org/keywords">controlled vocabulary</a> with a hierarchical structure. Keywords summarise the content of a UniProtKB entry and facilitate the search for proteins of interest.<p><a href='/help/keywords' target='_top'>More...</a></p>Keywords - Technical termi
3D-structure, Complete proteome, Direct protein sequencing, Reference proteomeDocuments
- Human chromosome 7
Human chromosome 7: entries, gene names and cross-references to MIM - Human entries with polymorphisms or disease mutations
List of human entries with polymorphisms or disease mutations - Human polymorphisms and disease mutations
Index of human polymorphisms and disease mutations - 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
