3c9q: Difference between revisions
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== Structural highlights == | == Structural highlights == | ||
<table><tr><td colspan='2'>[[3c9q]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3C9Q OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3C9Q FirstGlance]. <br> | <table><tr><td colspan='2'>[[3c9q]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3C9Q OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3C9Q FirstGlance]. <br> | ||
</td></tr><tr><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=CO3:CARBONATE+ION'>CO3</scene>, <scene name='pdbligand=EDO:1,2-ETHANEDIOL'>EDO</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene>< | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=CO3:CARBONATE+ION'>CO3</scene>, <scene name='pdbligand=EDO:1,2-ETHANEDIOL'>EDO</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene></td></tr> | ||
<tr><td class="sblockLbl"><b>[[Non-Standard_Residue|NonStd Res:]]</b></td><td class="sblockDat"><scene name='pdbligand=MSE:SELENOMETHIONINE'>MSE</scene></td></tr> | <tr id='NonStdRes'><td class="sblockLbl"><b>[[Non-Standard_Residue|NonStd Res:]]</b></td><td class="sblockDat"><scene name='pdbligand=MSE:SELENOMETHIONINE'>MSE</scene></td></tr> | ||
<tr><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">C8orf32 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 Homo sapiens])</td></tr> | <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">C8orf32 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 Homo sapiens])</td></tr> | ||
<tr><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3c9q FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3c9q OCA], [http://www.rcsb.org/pdb/explore.do?structureId=3c9q RCSB], [http://www.ebi.ac.uk/pdbsum/3c9q PDBsum], [http://www.topsan.org/Proteins/CESG/3c9q TOPSAN]</span></td></tr> | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3c9q FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3c9q OCA], [http://www.rcsb.org/pdb/explore.do?structureId=3c9q RCSB], [http://www.ebi.ac.uk/pdbsum/3c9q PDBsum], [http://www.topsan.org/Proteins/CESG/3c9q TOPSAN]</span></td></tr> | ||
<table> | </table> | ||
== Function == | |||
[[http://www.uniprot.org/uniprot/NTAQ1_HUMAN NTAQ1_HUMAN]] Mediates the side-chain deamidation of N-terminal glutamine residues to glutamate, an important step in N-end rule pathway of protein degradation. Conversion of the resulting N-terminal glutamine to glutamate renders the protein susceptible to arginylation, polyubiquitination and degradation as specified by the N-end rule. Does not act on substrates with internal or C-terminal glutamine and does not act on non-glutamine residues in any position. Does not deaminate acetylated N-terminal glutamine. With the exception of proline, all tested second-position residues on substrate peptides do not greatly influence the activity. In contrast, a proline at position 2, virtually abolishes deamidation of N-terminal glutamine (By similarity). | |||
== Evolutionary Conservation == | == Evolutionary Conservation == | ||
[[Image:Consurf_key_small.gif|200px|right]] | [[Image:Consurf_key_small.gif|200px|right]] | ||
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</StructureSection> | </StructureSection> | ||
[[Category: Homo sapiens]] | [[Category: Homo sapiens]] | ||
[[Category: Bingman, C A | [[Category: Bingman, C A]] | ||
[[Category: Bitto, E | [[Category: Bitto, E]] | ||
[[Category: | [[Category: Structural genomic]] | ||
[[Category: McCoy, J G | [[Category: McCoy, J G]] | ||
[[Category: Phillips, G N | [[Category: Phillips, G N]] | ||
[[Category: Wesenberg, G E | [[Category: Wesenberg, G E]] | ||
[[Category: Candidate gene important in the pathogenesis of t-cell prolymphocytic leukemia]] | [[Category: Candidate gene important in the pathogenesis of t-cell prolymphocytic leukemia]] | ||
[[Category: Cesg]] | [[Category: Cesg]] | ||
[[Category: Gene associated with cre-pathway activation]] | [[Category: Gene associated with cre-pathway activation]] | ||
[[Category: Medically relevant]] | [[Category: Medically relevant]] | ||
[[Category: Protein structure initiative | [[Category: PSI, Protein structure initiative]] | ||
[[Category: Putative involvement in human inherited ataxias and disorders of purkinje cell degeneration]] | [[Category: Putative involvement in human inherited ataxias and disorders of purkinje cell degeneration]] | ||
[[Category: Unknown function]] | [[Category: Unknown function]] | ||
Revision as of 01:00, 26 December 2014
Crystal structure of the uncharacterized human protein C8orf32 with bound peptideCrystal structure of the uncharacterized human protein C8orf32 with bound peptide
Structural highlights
Function[NTAQ1_HUMAN] Mediates the side-chain deamidation of N-terminal glutamine residues to glutamate, an important step in N-end rule pathway of protein degradation. Conversion of the resulting N-terminal glutamine to glutamate renders the protein susceptible to arginylation, polyubiquitination and degradation as specified by the N-end rule. Does not act on substrates with internal or C-terminal glutamine and does not act on non-glutamine residues in any position. Does not deaminate acetylated N-terminal glutamine. With the exception of proline, all tested second-position residues on substrate peptides do not greatly influence the activity. In contrast, a proline at position 2, virtually abolishes deamidation of N-terminal glutamine (By similarity). Evolutionary Conservation Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf. |
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Proteopedia Page Contributors and Editors (what is this?)Proteopedia Page Contributors and Editors (what is this?)
OCACategories:
- Homo sapiens
- Bingman, C A
- Bitto, E
- Structural genomic
- McCoy, J G
- Phillips, G N
- Wesenberg, G E
- Candidate gene important in the pathogenesis of t-cell prolymphocytic leukemia
- Cesg
- Gene associated with cre-pathway activation
- Medically relevant
- PSI, Protein structure initiative
- Putative involvement in human inherited ataxias and disorders of purkinje cell degeneration
- Unknown function