UniProtKB - Q96DE0 (NUD16_HUMAN)
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- BLAST>sp|Q96DE0|NUD16_HUMAN U8 snoRNA-decapping enzyme OS=Homo sapiens OX=9606 GN=NUDT16 PE=1 SV=2 MAGARRLELGEALALGSGWRHACHALLYAPDPGMLFGRIPLRYAILMQMRFDGRLGFPGG FVDTQDRSLEDGLNRELREELGEAAAAFRVERTDYRSSHVGSGPRVVAHFYAKRLTLEEL LAVEAGATRAKDHGLEVLGLVRVPLYTLRDGVGGLPTFLENSFIGSAREQLLEALQDLGL LQSGSISGLKIPAHH
- Align
U8 snoRNA-decapping enzyme
NUDT16
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 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.5"Xenopus U8 snoRNA binding protein is a conserved nuclear decapping enzyme."
Ghosh T., Peterson B., Tomasevic N., Peculis B.A.
Mol. Cell 13:817-828(2004) [PubMed] [Europe PMC] [Abstract]Cited for: FUNCTION AS A DECAPPING ENZYME, CATALYTIC ACTIVITY. - Ref.6"Metal determines efficiency and substrate specificity of the nuclear NUDIX decapping proteins X29 and H29K (Nudt16)."
Peculis B.A., Reynolds K., Cleland M.
J. Biol. Chem. 282:24792-24805(2007) [PubMed] [Europe PMC] [Abstract]Cited for: FUNCTION AS A DECAPPING ENZYME, SUBUNIT, CATALYTIC ACTIVITY, COFACTOR. - Ref.7"Evolutionary conservation supports ancient origin for Nudt16, a nuclear-localized, RNA-binding, RNA-decapping enzyme."
Taylor M.J., Peculis B.A.
Nucleic Acids Res. 36:6021-6034(2008) [PubMed] [Europe PMC] [Abstract]Cited for: FUNCTION AS A DECAPPING ENZYME, CATALYTIC ACTIVITY, SUBUNIT, RNA-BINDING, GENE EVOLUTION, GENE FAMILY ORGANIZATION. - Ref.8"Multiple mRNA decapping enzymes in mammalian cells."
Song M.G., Li Y., Kiledjian M.
Mol. Cell 40:423-432(2010) [PubMed] [Europe PMC] [Abstract]Cited for: FUNCTION AS A DECAPPING ENZYME, CATALYTIC ACTIVITY, SUBCELLULAR LOCATION. - Ref.9"NUDT16 is a (deoxy)inosine diphosphatase, and its deficiency induces accumulation of single-strand breaks in nuclear DNA and growth arrest."
Iyama T., Abolhassani N., Tsuchimoto D., Nonaka M., Nakabeppu Y.
Nucleic Acids Res. 38:4834-4843(2010) [PubMed] [Europe PMC] [Abstract]Cited for: FUNCTION AS AN IDP PHOSPHATASE, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, SUBCELLULAR LOCATION, TISSUE SPECIFICITY, IDENTIFICATION BY MASS SPECTROMETRY. - Ref.11"hNUDT16: a universal decapping enzyme for small nucleolar RNA and cytoplasmic mRNA."
Lu G., Zhang J., Li Y., Li Z., Zhang N., Xu X., Wang T., Guan Z., Gao G.F., Yan J.
Protein Cell 2:64-73(2011) [PubMed] [Europe PMC] [Abstract]Cited for: FUNCTION AS A DECAPPING ENZYME, CATALYTIC ACTIVITY, COFACTOR, SUBCELLULAR LOCATION. - Ref.14"Structural basis for the specificity of human NUDT16 and its regulation by inosine monophosphate."
Tresaugues L., Lundbaeck T., Welin M., Flodin S., Nyman T., Silvander C., Graeslund S., Nordlund P.
PLoS ONE 10:E0131507-E0131507(2015) [PubMed] [Europe PMC] [Abstract]Cited for: X-RAY CRYSTALLOGRAPHY (1.72 ANGSTROMS) IN COMPLEX WITH IMP AND MAGNESIUM IONS, SUBUNIT, CATALYTIC ACTIVITY, ENZYME REGULATION, FUNCTION, COFACTOR.
<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.5"Xenopus U8 snoRNA binding protein is a conserved nuclear decapping enzyme."
Ghosh T., Peterson B., Tomasevic N., Peculis B.A.
Mol. Cell 13:817-828(2004) [PubMed] [Europe PMC] [Abstract]Cited for: FUNCTION AS A DECAPPING ENZYME, CATALYTIC ACTIVITY. - Ref.6"Metal determines efficiency and substrate specificity of the nuclear NUDIX decapping proteins X29 and H29K (Nudt16)."
Peculis B.A., Reynolds K., Cleland M.
J. Biol. Chem. 282:24792-24805(2007) [PubMed] [Europe PMC] [Abstract]Cited for: FUNCTION AS A DECAPPING ENZYME, SUBUNIT, CATALYTIC ACTIVITY, COFACTOR. - Ref.7"Evolutionary conservation supports ancient origin for Nudt16, a nuclear-localized, RNA-binding, RNA-decapping enzyme."
Taylor M.J., Peculis B.A.
Nucleic Acids Res. 36:6021-6034(2008) [PubMed] [Europe PMC] [Abstract]Cited for: FUNCTION AS A DECAPPING ENZYME, CATALYTIC ACTIVITY, SUBUNIT, RNA-BINDING, GENE EVOLUTION, GENE FAMILY ORGANIZATION. - Ref.8"Multiple mRNA decapping enzymes in mammalian cells."
Song M.G., Li Y., Kiledjian M.
Mol. Cell 40:423-432(2010) [PubMed] [Europe PMC] [Abstract]Cited for: FUNCTION AS A DECAPPING ENZYME, CATALYTIC ACTIVITY, SUBCELLULAR LOCATION. - Ref.11"hNUDT16: a universal decapping enzyme for small nucleolar RNA and cytoplasmic mRNA."
Lu G., Zhang J., Li Y., Li Z., Zhang N., Xu X., Wang T., Guan Z., Gao G.F., Yan J.
Protein Cell 2:64-73(2011) [PubMed] [Europe PMC] [Abstract]Cited for: FUNCTION AS A DECAPPING ENZYME, CATALYTIC ACTIVITY, COFACTOR, SUBCELLULAR LOCATION.
<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.9"NUDT16 is a (deoxy)inosine diphosphatase, and its deficiency induces accumulation of single-strand breaks in nuclear DNA and growth arrest."
Iyama T., Abolhassani N., Tsuchimoto D., Nonaka M., Nakabeppu Y.
Nucleic Acids Res. 38:4834-4843(2010) [PubMed] [Europe PMC] [Abstract]Cited for: FUNCTION AS AN IDP PHOSPHATASE, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, SUBCELLULAR LOCATION, TISSUE SPECIFICITY, IDENTIFICATION BY MASS SPECTROMETRY. - Ref.14"Structural basis for the specificity of human NUDT16 and its regulation by inosine monophosphate."
Tresaugues L., Lundbaeck T., Welin M., Flodin S., Nyman T., Silvander C., Graeslund S., Nordlund P.
PLoS ONE 10:E0131507-E0131507(2015) [PubMed] [Europe PMC] [Abstract]Cited for: X-RAY CRYSTALLOGRAPHY (1.72 ANGSTROMS) IN COMPLEX WITH IMP AND MAGNESIUM IONS, SUBUNIT, CATALYTIC ACTIVITY, ENZYME REGULATION, FUNCTION, COFACTOR.
<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.9"NUDT16 is a (deoxy)inosine diphosphatase, and its deficiency induces accumulation of single-strand breaks in nuclear DNA and growth arrest."
Iyama T., Abolhassani N., Tsuchimoto D., Nonaka M., Nakabeppu Y.
Nucleic Acids Res. 38:4834-4843(2010) [PubMed] [Europe PMC] [Abstract]Cited for: FUNCTION AS AN IDP PHOSPHATASE, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, SUBCELLULAR LOCATION, TISSUE SPECIFICITY, IDENTIFICATION BY MASS SPECTROMETRY. - Ref.14"Structural basis for the specificity of human NUDT16 and its regulation by inosine monophosphate."
Tresaugues L., Lundbaeck T., Welin M., Flodin S., Nyman T., Silvander C., Graeslund S., Nordlund P.
PLoS ONE 10:E0131507-E0131507(2015) [PubMed] [Europe PMC] [Abstract]Cited for: X-RAY CRYSTALLOGRAPHY (1.72 ANGSTROMS) IN COMPLEX WITH IMP AND MAGNESIUM IONS, SUBUNIT, CATALYTIC ACTIVITY, ENZYME REGULATION, FUNCTION, COFACTOR.
<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 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.6"Metal determines efficiency and substrate specificity of the nuclear NUDIX decapping proteins X29 and H29K (Nudt16)."
Peculis B.A., Reynolds K., Cleland M.
J. Biol. Chem. 282:24792-24805(2007) [PubMed] [Europe PMC] [Abstract]Cited for: FUNCTION AS A DECAPPING ENZYME, SUBUNIT, CATALYTIC ACTIVITY, COFACTOR. - Ref.11"hNUDT16: a universal decapping enzyme for small nucleolar RNA and cytoplasmic mRNA."
Lu G., Zhang J., Li Y., Li Z., Zhang N., Xu X., Wang T., Guan Z., Gao G.F., Yan J.
Protein Cell 2:64-73(2011) [PubMed] [Europe PMC] [Abstract]Cited for: FUNCTION AS A DECAPPING ENZYME, CATALYTIC ACTIVITY, COFACTOR, SUBCELLULAR LOCATION. - Ref.14"Structural basis for the specificity of human NUDT16 and its regulation by inosine monophosphate."
Tresaugues L., Lundbaeck T., Welin M., Flodin S., Nyman T., Silvander C., Graeslund S., Nordlund P.
PLoS ONE 10:E0131507-E0131507(2015) [PubMed] [Europe PMC] [Abstract]Cited for: X-RAY CRYSTALLOGRAPHY (1.72 ANGSTROMS) IN COMPLEX WITH IMP AND MAGNESIUM IONS, SUBUNIT, CATALYTIC ACTIVITY, ENZYME REGULATION, FUNCTION, COFACTOR.
<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.6"Metal determines efficiency and substrate specificity of the nuclear NUDIX decapping proteins X29 and H29K (Nudt16)."
Peculis B.A., Reynolds K., Cleland M.
J. Biol. Chem. 282:24792-24805(2007) [PubMed] [Europe PMC] [Abstract]Cited for: FUNCTION AS A DECAPPING ENZYME, SUBUNIT, CATALYTIC ACTIVITY, COFACTOR. - Ref.11"hNUDT16: a universal decapping enzyme for small nucleolar RNA and cytoplasmic mRNA."
Lu G., Zhang J., Li Y., Li Z., Zhang N., Xu X., Wang T., Guan Z., Gao G.F., Yan J.
Protein Cell 2:64-73(2011) [PubMed] [Europe PMC] [Abstract]Cited for: FUNCTION AS A DECAPPING ENZYME, CATALYTIC ACTIVITY, COFACTOR, SUBCELLULAR LOCATION.
<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.6"Metal determines efficiency and substrate specificity of the nuclear NUDIX decapping proteins X29 and H29K (Nudt16)."
Peculis B.A., Reynolds K., Cleland M.
J. Biol. Chem. 282:24792-24805(2007) [PubMed] [Europe PMC] [Abstract]Cited for: FUNCTION AS A DECAPPING ENZYME, SUBUNIT, CATALYTIC ACTIVITY, COFACTOR. - Ref.11"hNUDT16: a universal decapping enzyme for small nucleolar RNA and cytoplasmic mRNA."
Lu G., Zhang J., Li Y., Li Z., Zhang N., Xu X., Wang T., Guan Z., Gao G.F., Yan J.
Protein Cell 2:64-73(2011) [PubMed] [Europe PMC] [Abstract]Cited for: FUNCTION AS A DECAPPING ENZYME, CATALYTIC ACTIVITY, COFACTOR, SUBCELLULAR LOCATION.
<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.6"Metal determines efficiency and substrate specificity of the nuclear NUDIX decapping proteins X29 and H29K (Nudt16)."
Peculis B.A., Reynolds K., Cleland M.
J. Biol. Chem. 282:24792-24805(2007) [PubMed] [Europe PMC] [Abstract]Cited for: FUNCTION AS A DECAPPING ENZYME, SUBUNIT, CATALYTIC ACTIVITY, COFACTOR. - Ref.11"hNUDT16: a universal decapping enzyme for small nucleolar RNA and cytoplasmic mRNA."
Lu G., Zhang J., Li Y., Li Z., Zhang N., Xu X., Wang T., Guan Z., Gao G.F., Yan J.
Protein Cell 2:64-73(2011) [PubMed] [Europe PMC] [Abstract]Cited for: FUNCTION AS A DECAPPING ENZYME, CATALYTIC ACTIVITY, COFACTOR, SUBCELLULAR LOCATION.
<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.14"Structural basis for the specificity of human NUDT16 and its regulation by inosine monophosphate."
Tresaugues L., Lundbaeck T., Welin M., Flodin S., Nyman T., Silvander C., Graeslund S., Nordlund P.
PLoS ONE 10:E0131507-E0131507(2015) [PubMed] [Europe PMC] [Abstract]Cited for: X-RAY CRYSTALLOGRAPHY (1.72 ANGSTROMS) IN COMPLEX WITH IMP AND MAGNESIUM IONS, SUBUNIT, CATALYTIC ACTIVITY, ENZYME REGULATION, FUNCTION, COFACTOR.
<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
<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.9"NUDT16 is a (deoxy)inosine diphosphatase, and its deficiency induces accumulation of single-strand breaks in nuclear DNA and growth arrest."
Iyama T., Abolhassani N., Tsuchimoto D., Nonaka M., Nakabeppu Y.
Nucleic Acids Res. 38:4834-4843(2010) [PubMed] [Europe PMC] [Abstract]Cited for: FUNCTION AS AN IDP PHOSPHATASE, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, SUBCELLULAR LOCATION, TISSUE SPECIFICITY, IDENTIFICATION BY MASS SPECTROMETRY.
- KM=0.062 µM for IDP (at 37 degrees Celsius)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.9"NUDT16 is a (deoxy)inosine diphosphatase, and its deficiency induces accumulation of single-strand breaks in nuclear DNA and growth arrest."
Iyama T., Abolhassani N., Tsuchimoto D., Nonaka M., Nakabeppu Y.
Nucleic Acids Res. 38:4834-4843(2010) [PubMed] [Europe PMC] [Abstract]Cited for: FUNCTION AS AN IDP PHOSPHATASE, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, SUBCELLULAR LOCATION, TISSUE SPECIFICITY, IDENTIFICATION BY MASS SPECTROMETRY.
- KM=0.088 µM for dIDP (at 37 degrees Celsius)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.9"NUDT16 is a (deoxy)inosine diphosphatase, and its deficiency induces accumulation of single-strand breaks in nuclear DNA and growth arrest."
Iyama T., Abolhassani N., Tsuchimoto D., Nonaka M., Nakabeppu Y.
Nucleic Acids Res. 38:4834-4843(2010) [PubMed] [Europe PMC] [Abstract]Cited for: FUNCTION AS AN IDP PHOSPHATASE, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, SUBCELLULAR LOCATION, TISSUE SPECIFICITY, IDENTIFICATION BY MASS SPECTROMETRY.
- KM=0.330 µM for GDP (at 37 degrees Celsius)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.9"NUDT16 is a (deoxy)inosine diphosphatase, and its deficiency induces accumulation of single-strand breaks in nuclear DNA and growth arrest."
Iyama T., Abolhassani N., Tsuchimoto D., Nonaka M., Nakabeppu Y.
Nucleic Acids Res. 38:4834-4843(2010) [PubMed] [Europe PMC] [Abstract]Cited for: FUNCTION AS AN IDP PHOSPHATASE, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, SUBCELLULAR LOCATION, TISSUE SPECIFICITY, IDENTIFICATION BY MASS SPECTROMETRY.
- KM=0.319 mM for dGDP (at 37 degrees Celsius)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.9"NUDT16 is a (deoxy)inosine diphosphatase, and its deficiency induces accumulation of single-strand breaks in nuclear DNA and growth arrest."
Iyama T., Abolhassani N., Tsuchimoto D., Nonaka M., Nakabeppu Y.
Nucleic Acids Res. 38:4834-4843(2010) [PubMed] [Europe PMC] [Abstract]Cited for: FUNCTION AS AN IDP PHOSPHATASE, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, SUBCELLULAR LOCATION, TISSUE SPECIFICITY, IDENTIFICATION BY MASS SPECTROMETRY.
- KM=15.7 mM for XDP (at 37 degrees Celsius)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.9"NUDT16 is a (deoxy)inosine diphosphatase, and its deficiency induces accumulation of single-strand breaks in nuclear DNA and growth arrest."
Iyama T., Abolhassani N., Tsuchimoto D., Nonaka M., Nakabeppu Y.
Nucleic Acids Res. 38:4834-4843(2010) [PubMed] [Europe PMC] [Abstract]Cited for: FUNCTION AS AN IDP PHOSPHATASE, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, SUBCELLULAR LOCATION, TISSUE SPECIFICITY, IDENTIFICATION BY MASS SPECTROMETRY.
- KM=22.1 mM for ITP (at 37 degrees Celsius)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.9"NUDT16 is a (deoxy)inosine diphosphatase, and its deficiency induces accumulation of single-strand breaks in nuclear DNA and growth arrest."
Iyama T., Abolhassani N., Tsuchimoto D., Nonaka M., Nakabeppu Y.
Nucleic Acids Res. 38:4834-4843(2010) [PubMed] [Europe PMC] [Abstract]Cited for: FUNCTION AS AN IDP PHOSPHATASE, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, SUBCELLULAR LOCATION, TISSUE SPECIFICITY, IDENTIFICATION BY MASS SPECTROMETRY.
- KM=24.1 mM for dITP (at 37 degrees Celsius)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.9"NUDT16 is a (deoxy)inosine diphosphatase, and its deficiency induces accumulation of single-strand breaks in nuclear DNA and growth arrest."
Iyama T., Abolhassani N., Tsuchimoto D., Nonaka M., Nakabeppu Y.
Nucleic Acids Res. 38:4834-4843(2010) [PubMed] [Europe PMC] [Abstract]Cited for: FUNCTION AS AN IDP PHOSPHATASE, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, SUBCELLULAR LOCATION, TISSUE SPECIFICITY, IDENTIFICATION BY MASS SPECTROMETRY.
<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.9"NUDT16 is a (deoxy)inosine diphosphatase, and its deficiency induces accumulation of single-strand breaks in nuclear DNA and growth arrest."
Iyama T., Abolhassani N., Tsuchimoto D., Nonaka M., Nakabeppu Y.
Nucleic Acids Res. 38:4834-4843(2010) [PubMed] [Europe PMC] [Abstract]Cited for: FUNCTION AS AN IDP PHOSPHATASE, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, SUBCELLULAR LOCATION, TISSUE SPECIFICITY, IDENTIFICATION BY MASS SPECTROMETRY.
<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>Temperature 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.9"NUDT16 is a (deoxy)inosine diphosphatase, and its deficiency induces accumulation of single-strand breaks in nuclear DNA and growth arrest."
Iyama T., Abolhassani N., Tsuchimoto D., Nonaka M., Nakabeppu Y.
Nucleic Acids Res. 38:4834-4843(2010) [PubMed] [Europe PMC] [Abstract]Cited for: FUNCTION AS AN IDP PHOSPHATASE, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, SUBCELLULAR LOCATION, TISSUE SPECIFICITY, IDENTIFICATION BY MASS SPECTROMETRY.
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 | 24 | Substrate1 Publication <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
| 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 | 50 | Substrate1 Publication <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
| 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 | 57 | Substrate; via amide nitrogen1 Publication <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
| 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 | 59 | Magnesium or manganese 1; via carbonyl oxygen1 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 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 | 76 | Magnesium or manganese 21 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 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 | 76 | Magnesium or manganese 3By similarity <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 | 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 | 80 | Magnesium or manganese 11 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 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 | 80 | Magnesium or manganese 3By similarity <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 | 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 | 136 | Magnesium or manganese 3By similarity <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 | 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 | 136 | Magnesium or manganese 4By similarity <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 | 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 | 170 | Substrate1 Publication <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
| 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
- cobalt ion binding 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
- dIDP diphosphatase activity Source: ReactomeInferred from experimenti
- dITP diphosphatase activity Source: UniProtKB
- GTP binding 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
- identical protein binding Source: IntAct <p>Inferred from Physical Interaction</p> <p>Covers physical interactions between the gene product of interest and another molecule (or ion, or complex).</p> <p>More information in the <a href="http://geneontology.org/page/guide-go-evidence-codes#ipi">GO evidence code guide</a></p> Inferred from physical interactioni
- IDP phosphatase activity Source: ReactomeInferred from experimenti
- ITP binding 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
- m7G(5')pppN 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
- magnesium ion binding 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
- manganese ion binding 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
- metalloexopeptidase 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
- mRNA binding 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
- nucleotide phosphatase activity, acting on free nucleotides 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
- protein homodimerization 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
- snoRNA binding 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
- XTP binding 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>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
- adenosine to inosine editing Source: UniProtKB <p>Inferred from Mutant Phenotype</p> <p>Describes annotations that are concluded from looking at variations or changes in a gene product such as mutations or abnormal levels and includes techniques such as knockouts, overexpression, anti-sense experiments and use of specific protein inhibitors.</p> <p>More information in the <a href="http://geneontology.org/page/guide-go-evidence-codes#imp">GO evidence code guide</a></p> Inferred from mutant phenotypei
- dITP catabolic process Source: UniProtKB
- IDP 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
- mRNA 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
- negative regulation of rRNA processing Source: UniProtKB
- nucleobase-containing small molecule catabolic process Source: Reactome
- positive regulation of cell cycle process Source: UniProtKB <p>Inferred from Mutant Phenotype</p> <p>Describes annotations that are concluded from looking at variations or changes in a gene product such as mutations or abnormal levels and includes techniques such as knockouts, overexpression, anti-sense experiments and use of specific protein inhibitors.</p> <p>More information in the <a href="http://geneontology.org/page/guide-go-evidence-codes#imp">GO evidence code guide</a></p> Inferred from mutant phenotypei
- positive regulation of cell proliferation Source: UniProtKB <p>Inferred from Mutant Phenotype</p> <p>Describes annotations that are concluded from looking at variations or changes in a gene product such as mutations or abnormal levels and includes techniques such as knockouts, overexpression, anti-sense experiments and use of specific protein inhibitors.</p> <p>More information in the <a href="http://geneontology.org/page/guide-go-evidence-codes#imp">GO evidence code guide</a></p> Inferred from mutant phenotypei
- positive regulation of double-strand break repair Source: UniProtKB <p>Inferred from Mutant Phenotype</p> <p>Describes annotations that are concluded from looking at variations or changes in a gene product such as mutations or abnormal levels and includes techniques such as knockouts, overexpression, anti-sense experiments and use of specific protein inhibitors.</p> <p>More information in the <a href="http://geneontology.org/page/guide-go-evidence-codes#imp">GO evidence code guide</a></p> Inferred from mutant phenotypei
- snoRNA 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
- XDP 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
<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 |
| Biological process | Nucleotide metabolism |
| Ligand | Magnesium, Manganese, Metal-binding, Nucleotide-binding |
Enzyme and pathway databases
BioCyc Collection of Pathway/Genome Databases More...BioCyci | MetaCyc:MONOMER-17869 |
BRENDA Comprehensive Enzyme Information System More...BRENDAi | 3.6.1.62 2681 3.6.1.64 2681 |
Reactome - a knowledgebase of biological pathways and processes More...Reactomei | R-HSA-2393930 Phosphate bond hydrolysis by NUDT proteins |
<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: U8 snoRNA-decapping enzyme (EC:3.6.1.625 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): IDP phosphatase (EC:3.6.1.642 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
Short name: IDPase Inosine diphosphate phosphatase Nucleoside diphosphate-linked moiety X motif 16 Short name: Nudix motif 16 Nudix hydrolase 16 U8 snoRNA-binding protein H29K1 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
m7GpppN-mRNA hydrolase |
| <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:NUDT16 |
| <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:ENSG00000198585.11 |
Human Gene Nomenclature Database More...HGNCi | HGNC:26442 NUDT16 |
Online Mendelian Inheritance in Man (OMIM) More...MIMi | 617381 gene |
neXtProt; the human protein knowledge platform More...neXtProti | NX_Q96DE0 |
<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
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.9"NUDT16 is a (deoxy)inosine diphosphatase, and its deficiency induces accumulation of single-strand breaks in nuclear DNA and growth arrest."
Iyama T., Abolhassani N., Tsuchimoto D., Nonaka M., Nakabeppu Y.
Nucleic Acids Res. 38:4834-4843(2010) [PubMed] [Europe PMC] [Abstract]Cited for: FUNCTION AS AN IDP PHOSPHATASE, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, SUBCELLULAR LOCATION, TISSUE SPECIFICITY, IDENTIFICATION BY MASS SPECTROMETRY. - Ref.11"hNUDT16: a universal decapping enzyme for small nucleolar RNA and cytoplasmic mRNA."
Lu G., Zhang J., Li Y., Li Z., Zhang N., Xu X., Wang T., Guan Z., Gao G.F., Yan J.
Protein Cell 2:64-73(2011) [PubMed] [Europe PMC] [Abstract]Cited for: FUNCTION AS A DECAPPING ENZYME, CATALYTIC ACTIVITY, COFACTOR, SUBCELLULAR LOCATION.
- nucleoplasm By similarity
<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
- nucleolus By similarity
<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
- Nucleus 2 Publications
Other locations
- Cytoplasm 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.8"Multiple mRNA decapping enzymes in mammalian cells."
Song M.G., Li Y., Kiledjian M.
Mol. Cell 40:423-432(2010) [PubMed] [Europe PMC] [Abstract]Cited for: FUNCTION AS A DECAPPING ENZYME, CATALYTIC ACTIVITY, SUBCELLULAR LOCATION. - Ref.11"hNUDT16: a universal decapping enzyme for small nucleolar RNA and cytoplasmic mRNA."
Lu G., Zhang J., Li Y., Li Z., Zhang N., Xu X., Wang T., Guan Z., Gao G.F., Yan J.
Protein Cell 2:64-73(2011) [PubMed] [Europe PMC] [Abstract]Cited for: FUNCTION AS A DECAPPING ENZYME, CATALYTIC ACTIVITY, COFACTOR, SUBCELLULAR LOCATION.
Note: Localized predominantly in the cytoplasm (PubMed:21070968). Localized in nucleolus, and in a minor proportion in distinct foci in the nucleoplasm (By similarity).By similarity- Cytoplasm 2 Publications
- Ref.8"Multiple mRNA decapping enzymes in mammalian cells."
Song M.G., Li Y., Kiledjian M.
Mol. Cell 40:423-432(2010) [PubMed] [Europe PMC] [Abstract]Cited for: FUNCTION AS A DECAPPING ENZYME, CATALYTIC ACTIVITY, SUBCELLULAR LOCATION.
<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
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
Nucleus
- nucleolus 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
- nucleoplasm Source: Reactome
- 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
Other locations
- 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, 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
Organism-specific databases
DisGeNET More...DisGeNETi | 131870 |
Open Targets More...OpenTargetsi | ENSG00000198585 |
The Pharmacogenetics and Pharmacogenomics Knowledge Base More...PharmGKBi | PA134955224 |
Polymorphism and mutation databases
BioMuta curated single-nucleotide variation and disease association database More...BioMutai | NUDT16 |
Domain mapping of disease mutations (DMDM) More...DMDMi | 68565926 |
<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 polypeptide chain in the mature protein following processing.<p><a href='/help/chain' target='_top'>More...</a></p>ChainiPRO_0000057117 | 1 – 195 | U8 snoRNA-decapping enzymeAdd BLAST | 195 |
Proteomic databases
Encyclopedia of Proteome Dynamics More...EPDi | Q96DE0 |
MaxQB - The MaxQuant DataBase More...MaxQBi | Q96DE0 |
PaxDb, a database of protein abundance averages across all three domains of life More...PaxDbi | Q96DE0 |
PeptideAtlas More...PeptideAtlasi | Q96DE0 |
PRoteomics IDEntifications database More...PRIDEi | Q96DE0 |
ProteomicsDB human proteome resource More...ProteomicsDBi | 76283 |
Consortium for Top Down Proteomics More...TopDownProteomicsi | Q96DE0-1 [Q96DE0-1] |
PTM databases
iPTMnet integrated resource for PTMs in systems biology context More...iPTMneti | Q96DE0 |
Comprehensive resource for the study of protein post-translational modifications (PTMs) in human, mouse and rat. More...PhosphoSitePlusi | Q96DE0 |
<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.9"NUDT16 is a (deoxy)inosine diphosphatase, and its deficiency induces accumulation of single-strand breaks in nuclear DNA and growth arrest."
Iyama T., Abolhassani N., Tsuchimoto D., Nonaka M., Nakabeppu Y.
Nucleic Acids Res. 38:4834-4843(2010) [PubMed] [Europe PMC] [Abstract]Cited for: FUNCTION AS AN IDP PHOSPHATASE, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, SUBCELLULAR LOCATION, TISSUE SPECIFICITY, IDENTIFICATION BY MASS SPECTROMETRY.
Gene expression databases
Bgee dataBase for Gene Expression Evolution More...Bgeei | ENSG00000198585 |
CleanEx database of gene expression profiles More...CleanExi | HS_NUDT16 |
Genevisible search portal to normalized and curated expression data from Genevestigator More...Genevisiblei | Q96DE0 HS |
Organism-specific databases
Human Protein Atlas More...HPAi | HPA060452 HPA062492 |
<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.6"Metal determines efficiency and substrate specificity of the nuclear NUDIX decapping proteins X29 and H29K (Nudt16)."
Peculis B.A., Reynolds K., Cleland M.
J. Biol. Chem. 282:24792-24805(2007) [PubMed] [Europe PMC] [Abstract]Cited for: FUNCTION AS A DECAPPING ENZYME, SUBUNIT, CATALYTIC ACTIVITY, COFACTOR. - Ref.7"Evolutionary conservation supports ancient origin for Nudt16, a nuclear-localized, RNA-binding, RNA-decapping enzyme."
Taylor M.J., Peculis B.A.
Nucleic Acids Res. 36:6021-6034(2008) [PubMed] [Europe PMC] [Abstract]Cited for: FUNCTION AS A DECAPPING ENZYME, CATALYTIC ACTIVITY, SUBUNIT, RNA-BINDING, GENE EVOLUTION, GENE FAMILY ORGANIZATION. - Ref.14"Structural basis for the specificity of human NUDT16 and its regulation by inosine monophosphate."
Tresaugues L., Lundbaeck T., Welin M., Flodin S., Nyman T., Silvander C., Graeslund S., Nordlund P.
PLoS ONE 10:E0131507-E0131507(2015) [PubMed] [Europe PMC] [Abstract]Cited for: X-RAY CRYSTALLOGRAPHY (1.72 ANGSTROMS) IN COMPLEX WITH IMP AND MAGNESIUM IONS, SUBUNIT, CATALYTIC ACTIVITY, ENZYME REGULATION, FUNCTION, COFACTOR.
<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 |
|---|---|---|---|---|
| itself | 2 | EBI-5464685,EBI-5464685 |
<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
- identical protein binding Source: IntAct <p>Inferred from Physical Interaction</p> <p>Covers physical interactions between the gene product of interest and another molecule (or ion, or complex).</p> <p>More information in the <a href="http://geneontology.org/page/guide-go-evidence-codes#ipi">GO evidence code guide</a></p> Inferred from physical interactioni
- protein homodimerization 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
Protein-protein interaction databases
The Biological General Repository for Interaction Datasets (BioGrid) More...BioGridi | 126295, 13 interactors |
Protein interaction database and analysis system More...IntActi | Q96DE0, 1 interactor |
Molecular INTeraction database More...MINTi | Q96DE0 |
STRING: functional protein association networks More...STRINGi | 9606.ENSP00000422375 |
<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 | 5 – 7 | 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 | 9 – 13 | 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 | 5 | |
| <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 | 20 – 35 | 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 | 16 | |
| <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 | 36 – 38 | 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 | 39 – 50 | 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 | 58 – 61 | 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 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 | 64 – 66 | 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 | 69 – 81 | 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 helical regions within the protein sequence.<p><a href='/help/helix' target='_top'>More...</a></p>Helixi | 83 – 87 | 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 | 5 | |
| <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 | 92 – 94 | 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 | 95 – 100 | 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 | 6 | |
| <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 | 102 – 114 | 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 helical regions within the protein sequence.<p><a href='/help/helix' target='_top'>More...</a></p>Helixi | 117 – 126 | 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 helical regions within the protein sequence.<p><a href='/help/helix' target='_top'>More...</a></p>Helixi | 127 – 129 | 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 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 | 134 – 136 | 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 | 137 – 142 | 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 | 6 | |
| <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 | 155 – 158 | 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 | 167 – 177 | 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 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 | 178 – 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 | 4 |
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 |
| 2XSQ | X-ray | 1.72 | A | 1-195 | [»] | |
| 3COU | X-ray | 1.80 | A | 1-195 | [»] | |
| 3MGM | X-ray | 1.80 | A/B | 1-195 | [»] | |
Protein Model Portal of the PSI-Nature Structural Biology Knowledgebase More...ProteinModelPortali | Q96DE0 | |||||
SWISS-MODEL Repository - a database of annotated 3D protein structure models More...SMRi | Q96DE0 | |||||
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 | Q96DE0 |
<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 | 18 – 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 | 156 |
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 | 61 – 82 | Nudix boxAdd 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
Phylogenomic databases
evolutionary genealogy of genes: Non-supervised Orthologous Groups More...eggNOGi | ENOG410IYGP Eukaryota ENOG4111QA1 LUCA |
Ensembl GeneTree More...GeneTreei | ENSGT00390000016224 |
The HOGENOM Database of Homologous Genes from Fully Sequenced Organisms More...HOGENOMi | HOG000007083 |
The HOVERGEN Database of Homologous Vertebrate Genes More...HOVERGENi | HBG067297 |
InParanoid: Eukaryotic Ortholog Groups More...InParanoidi | Q96DE0 |
KEGG Orthology (KO) More...KOi | K16855 |
Identification of Orthologs from Complete Genome Data More...OMAi | FYAKCLT |
Database of Orthologous Groups More...OrthoDBi | EOG091G0XY4 |
Database for complete collections of gene phylogenies More...PhylomeDBi | Q96DE0 |
Family and domain databases
Integrated resource of protein families, domains and functional sites More...InterProi | View protein in InterPro IPR015797 NUDIX_hydrolase-like_dom_sf IPR000086 NUDIX_hydrolase_dom |
Pfam protein domain database More...Pfami | View protein in Pfam PF00293 NUDIX, 1 hit |
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 |
<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.
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 splicing. 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
MAGARRLELG EALALGSGWR HACHALLYAP DPGMLFGRIP LRYAILMQMR
60 70 80 90 100
FDGRLGFPGG FVDTQDRSLE DGLNRELREE LGEAAAAFRV ERTDYRSSHV
110 120 130 140 150
GSGPRVVAHF YAKRLTLEEL LAVEAGATRA KDHGLEVLGL VRVPLYTLRD
160 170 180 190
GVGGLPTFLE NSFIGSAREQ LLEALQDLGL LQSGSISGLK IPAHH
The sequence of this isoform differs from the canonical sequence as follows:
1-33: Missing.
138-195: LGLVRVPLYT...ISGLKIPAHH → GPAWDSVPFP...MSLCCSLLTV
10 20 30 40 50
MLFGRIPLRY AILMQMRFDG RLGFPGGFVD TQDRSLEDGL NRELREELGE
60 70 80 90 100
AAAAFRVERT DYRSSHVGSG PRVVAHFYAK RLTLEELLAV EAGATRAKDH
110 120 130 140 150
GLEVGPAWDS VPFPISSSPK AFSPPRKHPW RKVFAPLTLP SPQLSWWSWD
160 170 180 190
RDHLYSELVL PTWAFCKGLS HPLPGEILSR THSSMSLCCS LLTV
The sequence of this isoform differs from the canonical sequence as follows:
1-46: Missing.
174-195: ALQDLGLLQSGSISGLKIPAHH → AALHGPMKTEMRTLVLGREGRTWECFLIGSER
10 20 30 40 50
MQMRFDGRLG FPGGFVDTQD RSLEDGLNRE LREELGEAAA AFRVERTDYR
60 70 80 90 100
SSHVGSGPRV VAHFYAKRLT LEELLAVEAG ATRAKDHGLE VLGLVRVPLY
110 120 130 140 150
TLRDGVGGLP TFLENSFIGS AREQLLEAAL HGPMKTEMRT LVLGREGRTW
ECFLIGSER
The sequence of this isoform differs from the canonical sequence as follows:
138-195: LGLVRVPLYT...ISGLKIPAHH → GPAWDSVPFP...MSLCCSLLTV
10 20 30 40 50
MAGARRLELG EALALGSGWR HACHALLYAP DPGMLFGRIP LRYAILMQMR
60 70 80 90 100
FDGRLGFPGG FVDTQDRSLE DGLNRELREE LGEAAAAFRV ERTDYRSSHV
110 120 130 140 150
GSGPRVVAHF YAKRLTLEEL LAVEAGATRA KDHGLEVGPA WDSVPFPISS
160 170 180 190 200
SPKAFSPPRK HPWRKVFAPL TLPSPQLSWW SWDRDHLYSE LVLPTWAFCK
210 220
GLSHPLPGEI LSRTHSSMSL CCSLLTV
<p>This subsection of the ‘Sequence’ section reports difference(s) between the protein sequence shown in the UniProtKB entry and other available protein sequences derived from the same gene.<p><a href='/help/sequence_caution' target='_top'>More...</a></p>Sequence cautioni
Experimental Info
| Feature key | Position(s) | DescriptionActions | Graphical view | Length | |
|---|---|---|---|---|---|
| <p>This subsection of the ‘Sequence’ section reports difference(s) between the canonical sequence (displayed by default in the entry) and the different sequence submissions merged in the entry. These various submissions may originate from different sequencing projects, different types of experiments, or different biological samples. Sequence conflicts are usually of unknown origin.<p><a href='/help/conflict' target='_top'>More...</a></p>Sequence conflicti | 22 | A → V in AAH31215 (PubMed:15489334).Curated | 1 | ||
| Isoform 3 (identifier: Q96DE0-3) | |||||
| <p>This subsection of the ‘Sequence’ section reports difference(s) between the canonical sequence (displayed by default in the entry) and the different sequence submissions merged in the entry. These various submissions may originate from different sequencing projects, different types of experiments, or different biological samples. Sequence conflicts are usually of unknown origin.<p><a href='/help/conflict' target='_top'>More...</a></p>Sequence conflicti | 128 | Missing in BP199028 (PubMed:16344560).Curated | 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_045449 | 1 – 46 | Missing in isoform 3. 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
| 46 | |
| <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_045450 | 1 – 33 | Missing in isoform 2. 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
| 33 | |
| <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_045451 | 138 – 195 | LGLVR…IPAHH → GPAWDSVPFPISSSPKAFSP PRKHPWRKVFAPLTLPSPQL SWWSWDRDHLYSELVLPTWA FCKGLSHPLPGEILSRTHSS MSLCCSLLTV in isoform 2 and isoform 4. 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
| 58 | |
| <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_045452 | 174 – 195 | ALQDL…IPAHH → AALHGPMKTEMRTLVLGREG RTWECFLIGSER in isoform 3. 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
| 22 |
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 | AK055827 mRNA Translation: BAB71024.1 Different initiation. AK304650 mRNA Translation: BAG65426.1 BP199028 mRNA No translation available. AC010210 Genomic DNA No translation available. BC009546 mRNA Translation: AAH09546.1 BC031215 mRNA Translation: AAH31215.2 |
The Consensus CDS (CCDS) project More...CCDSi | CCDS3070.2 [Q96DE0-1] CCDS54640.1 [Q96DE0-4] CCDS54641.1 [Q96DE0-3] |
NCBI Reference Sequences More...RefSeqi | NP_001165376.1, NM_001171905.1 [Q96DE0-3] NP_001165377.1, NM_001171906.1 [Q96DE0-4] NP_689608.2, NM_152395.2 [Q96DE0-1] |
UniGene gene-oriented nucleotide sequence clusters More...UniGenei | Hs.282050 |
Genome annotation databases
Ensembl eukaryotic genome annotation project More...Ensembli | ENST00000502852; ENSP00000422375; ENSG00000198585 [Q96DE0-4] ENST00000521288; ENSP00000429274; ENSG00000198585 [Q96DE0-1] ENST00000537561; ENSP00000440230; ENSG00000198585 [Q96DE0-3] |
Database of genes from NCBI RefSeq genomes More...GeneIDi | 131870 |
KEGG: Kyoto Encyclopedia of Genes and Genomes More...KEGGi | hsa:131870 |
UCSC genome browser More...UCSCi | uc003eog.3 human [Q96DE0-1] |
<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 splicing<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 | |
|---|---|---|---|---|---|
| Q96DE0 | Nudix hydrolase 16 | 195 | |||
| Uncharacterized protein | 195 | ||||
| UPI0002074EED | 200 | ||||
| U8 snoRNA-decapping enzyme isoform 2 | 195 | ||||
| Nudix hydrolase 16 | 195 | ||||
| +21 | |||||
| Q96DE0-2 | UPI00020AC47D | 231 | |||
| NUDT16 isoform 3 | 227 | ||||
| Nudix hydrolase 16 | 227 | ||||
| NUDT16 isoform 3 | 227 | ||||
| Nudix hydrolase 16 | 226 | ||||
| +6 | |||||
| Q96DE0-3 | NUDT16 isoform 1 | 159 | |||
| U8 snoRNA-decapping enzyme | 159 | ||||
| Nudix hydrolase 16 | 159 | ||||
| Uncharacterized protein | 159 | ||||
| Nudix hydrolase 16 | 159 | ||||
| +12 | |||||
| Q96DE0-4 | UPI00020AC47D | 231 | |||
| NUDT16 isoform 3 | 227 | ||||
| Nudix hydrolase 16 | 227 | ||||
| NUDT16 isoform 3 | 227 | ||||
| Nudix hydrolase 16 | 226 | ||||
| +6 | |||||
| Protein | Similar proteins | Species | Score | Length | |
|---|---|---|---|---|---|
| Q96DE0 | Nudix hydrolase 16 | 195 | |||
| Uncharacterized protein | 195 | ||||
| UPI0002074EED | 200 | ||||
| NUDT16 isoform 2 | 195 | ||||
| Nudix hydrolase 16 | 195 | ||||
| +31 | |||||
| Q96DE0-2 | UPI00020AC47D | 231 | |||
| NUDT16 isoform 3 | 227 | ||||
| Nudix hydrolase 16 | 227 | ||||
| NUDT16 isoform 3 | 227 | ||||
| Nudix hydrolase 16 | 226 | ||||
| +28 | |||||
| Q96DE0-3 | NUDT16 isoform 1 | 159 | |||
| U8 snoRNA-decapping enzyme | 159 | ||||
| Nudix hydrolase 16 | 159 | ||||
| Nudix hydrolase 16 | 159 | ||||
| Uncharacterized protein | 159 | ||||
| +13 | |||||
| Q96DE0-4 | UPI00020AC47D | 231 | |||
| NUDT16 isoform 3 | 227 | ||||
| Nudix hydrolase 16 | 227 | ||||
| NUDT16 isoform 3 | 227 | ||||
| Nudix hydrolase 16 | 226 | ||||
| +28 | |||||
<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
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 | AK055827 mRNA Translation: BAB71024.1 Different initiation. AK304650 mRNA Translation: BAG65426.1 BP199028 mRNA No translation available. AC010210 Genomic DNA No translation available. BC009546 mRNA Translation: AAH09546.1 BC031215 mRNA Translation: AAH31215.2 |
The Consensus CDS (CCDS) project More...CCDSi | CCDS3070.2 [Q96DE0-1] CCDS54640.1 [Q96DE0-4] CCDS54641.1 [Q96DE0-3] |
NCBI Reference Sequences More...RefSeqi | NP_001165376.1, NM_001171905.1 [Q96DE0-3] NP_001165377.1, NM_001171906.1 [Q96DE0-4] NP_689608.2, NM_152395.2 [Q96DE0-1] |
UniGene gene-oriented nucleotide sequence clusters More...UniGenei | Hs.282050 |
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 |
| 2XSQ | X-ray | 1.72 | A | 1-195 | [»] | |
| 3COU | X-ray | 1.80 | A | 1-195 | [»] | |
| 3MGM | X-ray | 1.80 | A/B | 1-195 | [»] | |
Protein Model Portal of the PSI-Nature Structural Biology Knowledgebase More...ProteinModelPortali | Q96DE0 | |||||
SWISS-MODEL Repository - a database of annotated 3D protein structure models More...SMRi | Q96DE0 | |||||
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 | 126295, 13 interactors |
Protein interaction database and analysis system More...IntActi | Q96DE0, 1 interactor |
Molecular INTeraction database More...MINTi | Q96DE0 |
STRING: functional protein association networks More...STRINGi | 9606.ENSP00000422375 |
PTM databases
iPTMnet integrated resource for PTMs in systems biology context More...iPTMneti | Q96DE0 |
Comprehensive resource for the study of protein post-translational modifications (PTMs) in human, mouse and rat. More...PhosphoSitePlusi | Q96DE0 |
Polymorphism and mutation databases
BioMuta curated single-nucleotide variation and disease association database More...BioMutai | NUDT16 |
Domain mapping of disease mutations (DMDM) More...DMDMi | 68565926 |
Proteomic databases
Encyclopedia of Proteome Dynamics More...EPDi | Q96DE0 |
MaxQB - The MaxQuant DataBase More...MaxQBi | Q96DE0 |
PaxDb, a database of protein abundance averages across all three domains of life More...PaxDbi | Q96DE0 |
PeptideAtlas More...PeptideAtlasi | Q96DE0 |
PRoteomics IDEntifications database More...PRIDEi | Q96DE0 |
ProteomicsDB human proteome resource More...ProteomicsDBi | 76283 |
Consortium for Top Down Proteomics More...TopDownProteomicsi | Q96DE0-1 [Q96DE0-1] |
Protocols and materials databases
| Structural Biology Knowledgebase | Search... |
Genome annotation databases
Ensembl eukaryotic genome annotation project More...Ensembli | ENST00000502852; ENSP00000422375; ENSG00000198585 [Q96DE0-4] ENST00000521288; ENSP00000429274; ENSG00000198585 [Q96DE0-1] ENST00000537561; ENSP00000440230; ENSG00000198585 [Q96DE0-3] |
Database of genes from NCBI RefSeq genomes More...GeneIDi | 131870 |
KEGG: Kyoto Encyclopedia of Genes and Genomes More...KEGGi | hsa:131870 |
UCSC genome browser More...UCSCi | uc003eog.3 human [Q96DE0-1] |
Organism-specific databases
Comparative Toxicogenomics Database More...CTDi | 131870 |
DisGeNET More...DisGeNETi | 131870 |
Eukaryotic Pathogen Database Resources More...EuPathDBi | HostDB:ENSG00000198585.11 |
GeneCards: human genes, protein and diseases More...GeneCardsi | NUDT16 |
H-Invitational Database, human transcriptome db More...H-InvDBi | HIX0003684 |
Human Gene Nomenclature Database More...HGNCi | HGNC:26442 NUDT16 |
Human Protein Atlas More...HPAi | HPA060452 HPA062492 |
Online Mendelian Inheritance in Man (OMIM) More...MIMi | 617381 gene |
neXtProt; the human protein knowledge platform More...neXtProti | NX_Q96DE0 |
Open Targets More...OpenTargetsi | ENSG00000198585 |
The Pharmacogenetics and Pharmacogenomics Knowledge Base More...PharmGKBi | PA134955224 |
GenAtlas: human gene database More...GenAtlasi | Search... |
Phylogenomic databases
evolutionary genealogy of genes: Non-supervised Orthologous Groups More...eggNOGi | ENOG410IYGP Eukaryota ENOG4111QA1 LUCA |
Ensembl GeneTree More...GeneTreei | ENSGT00390000016224 |
The HOGENOM Database of Homologous Genes from Fully Sequenced Organisms More...HOGENOMi | HOG000007083 |
The HOVERGEN Database of Homologous Vertebrate Genes More...HOVERGENi | HBG067297 |
InParanoid: Eukaryotic Ortholog Groups More...InParanoidi | Q96DE0 |
KEGG Orthology (KO) More...KOi | K16855 |
Identification of Orthologs from Complete Genome Data More...OMAi | FYAKCLT |
Database of Orthologous Groups More...OrthoDBi | EOG091G0XY4 |
Database for complete collections of gene phylogenies More...PhylomeDBi | Q96DE0 |
Enzyme and pathway databases
BioCyc Collection of Pathway/Genome Databases More...BioCyci | MetaCyc:MONOMER-17869 |
BRENDA Comprehensive Enzyme Information System More...BRENDAi | 3.6.1.62 2681 3.6.1.64 2681 |
Reactome - a knowledgebase of biological pathways and processes More...Reactomei | R-HSA-2393930 Phosphate bond hydrolysis by NUDT proteins |
Miscellaneous databases
ChiTaRS: a database of human, mouse and fruit fly chimeric transcripts and RNA-sequencing data More...ChiTaRSi | NUDT16 human |
Relative evolutionary importance of amino acids within a protein sequence More...EvolutionaryTracei | Q96DE0 |
Database of phenotypes from RNA interference screens in Drosophila and Homo sapiens More...GenomeRNAii | 131870 |
Protein Ontology More...PROi | PR:Q96DE0 |
The Stanford Online Universal Resource for Clones and ESTs More...SOURCEi | Search... |
Gene expression databases
Bgee dataBase for Gene Expression Evolution More...Bgeei | ENSG00000198585 |
CleanEx database of gene expression profiles More...CleanExi | HS_NUDT16 |
Genevisible search portal to normalized and curated expression data from Genevestigator More...Genevisiblei | Q96DE0 HS |
Family and domain databases
Integrated resource of protein families, domains and functional sites More...InterProi | View protein in InterPro IPR015797 NUDIX_hydrolase-like_dom_sf IPR000086 NUDIX_hydrolase_dom |
Pfam protein domain database More...Pfami | View protein in Pfam PF00293 NUDIX, 1 hit |
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 |
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 | NUD16_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 | Q96DE0Primary (citable) accession number: Q96DE0 Secondary accession number(s): B4E3B4 , E9PED4, F5GYJ1, Q96N82 | |
| <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: | July 5, 2005 |
| Last sequence update: | July 5, 2005 | |
| Last modified: | June 20, 2018 | |
| This is version 136 of the entry and version 2 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, Reference proteomeDocuments
- Human chromosome 3
Human chromosome 3: entries, gene names and cross-references to MIM - MIM cross-references
Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot - PDB cross-references
Index of Protein Data Bank (PDB) cross-references - SIMILARITY comments
Index of protein domains and families
