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| | <StructureSection load='6gr8' size='340' side='right'caption='[[6gr8]], [[Resolution|resolution]] 1.75Å' scene=''> | | <StructureSection load='6gr8' size='340' side='right'caption='[[6gr8]], [[Resolution|resolution]] 1.75Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[6gr8]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Human Human]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6GR8 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=6GR8 FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[6gr8]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6GR8 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=6GR8 FirstGlance]. <br> |
| - | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=F8Z:1-[(2~{R},3~{S})-2-[[1,3-benzodioxol-5-ylmethyl(methyl)amino]methyl]-3-methyl-6-oxidanylidene-5-[(2~{S})-1-oxidanylpropan-2-yl]-3,4-dihydro-2~{H}-1,5-benzoxazocin-8-yl]-3-(4-methoxyphenyl)urea'>F8Z</scene></td></tr> | + | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.75Å</td></tr> |
| - | <tr id='NonStdRes'><td class="sblockLbl"><b>[[Non-Standard_Residue|NonStd Res:]]</b></td><td class="sblockDat"><scene name='pdbligand=SEP:PHOSPHOSERINE'>SEP</scene>, <scene name='pdbligand=TPO:PHOSPHOTHREONINE'>TPO</scene></td></tr>
| + | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=F8Z:1-[(2~{R},3~{S})-2-[[1,3-benzodioxol-5-ylmethyl(methyl)amino]methyl]-3-methyl-6-oxidanylidene-5-[(2~{S})-1-oxidanylpropan-2-yl]-3,4-dihydro-2~{H}-1,5-benzoxazocin-8-yl]-3-(4-methoxyphenyl)urea'>F8Z</scene>, <scene name='pdbligand=SEP:PHOSPHOSERINE'>SEP</scene>, <scene name='pdbligand=TPO:PHOSPHOTHREONINE'>TPO</scene></td></tr> |
| - | <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">AURKC, AIE2, AIK3, AIRK3, ARK3, STK13 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 HUMAN]), INCENP ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 HUMAN])</td></tr>
| + | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=6gr8 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6gr8 OCA], [https://pdbe.org/6gr8 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=6gr8 RCSB], [https://www.ebi.ac.uk/pdbsum/6gr8 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=6gr8 ProSAT]</span></td></tr> |
| - | <tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Non-specific_serine/threonine_protein_kinase Non-specific serine/threonine protein kinase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.7.11.1 2.7.11.1] </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=6gr8 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6gr8 OCA], [http://pdbe.org/6gr8 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=6gr8 RCSB], [http://www.ebi.ac.uk/pdbsum/6gr8 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=6gr8 ProSAT]</span></td></tr> | + | |
| | </table> | | </table> |
| | == Disease == | | == Disease == |
| - | [[http://www.uniprot.org/uniprot/AURKC_HUMAN AURKC_HUMAN]] Male infertility due to large-headed multiflagellar polyploid spermatozoa. The disease is caused by mutations affecting the gene represented in this entry. | + | [https://www.uniprot.org/uniprot/AURKC_HUMAN AURKC_HUMAN] Male infertility due to large-headed multiflagellar polyploid spermatozoa. The disease is caused by mutations affecting the gene represented in this entry. |
| | == Function == | | == Function == |
| - | [[http://www.uniprot.org/uniprot/AURKC_HUMAN AURKC_HUMAN]] Serine/threonine-protein kinase component of the chromosomal passenger complex (CPC), a complex that acts as a key regulator of mitosis. The CPC complex has essential functions at the centromere in ensuring correct chromosome alignment and segregation and is required for chromatin-induced microtubule stabilization and spindle assembly. Plays also a role in meiosis and more particularly in spermatogenesis. Has redundant cellular functions with AURKB and can rescue an AURKB knockdown. Like AURKB, AURKC phosphorylates histone H3 at 'Ser-10' and 'Ser-28'. AURKC phosphorylates the CPC complex subunits BIRC5/survivin and INCENP leading to increased AURKC activity. Phosphorylates TACC1, another protein involved in cell division, at 'Ser-228'.<ref>PMID:15316025</ref> <ref>PMID:15499654</ref> <ref>PMID:15670791</ref> <ref>PMID:15938719</ref> <ref>PMID:21493633</ref> <ref>PMID:21531210</ref> <ref>PMID:27332895</ref> [[http://www.uniprot.org/uniprot/INCE_HUMAN INCE_HUMAN]] Component of the chromosomal passenger complex (CPC), a complex that acts as a key regulator of mitosis. The CPC complex has essential functions at the centromere in ensuring correct chromosome alignment and segregation and is required for chromatin-induced microtubule stabilization and spindle assembly. Probably acts through association with AURKB or AURKC. Seems to bind directly to microtubules. Controls the kinetochore localization of BUB1.<ref>PMID:15316025</ref> <ref>PMID:12925766</ref> <ref>PMID:16760428</ref> | + | [https://www.uniprot.org/uniprot/AURKC_HUMAN AURKC_HUMAN] Serine/threonine-protein kinase component of the chromosomal passenger complex (CPC), a complex that acts as a key regulator of mitosis. The CPC complex has essential functions at the centromere in ensuring correct chromosome alignment and segregation and is required for chromatin-induced microtubule stabilization and spindle assembly. Plays also a role in meiosis and more particularly in spermatogenesis. Has redundant cellular functions with AURKB and can rescue an AURKB knockdown. Like AURKB, AURKC phosphorylates histone H3 at 'Ser-10' and 'Ser-28'. AURKC phosphorylates the CPC complex subunits BIRC5/survivin and INCENP leading to increased AURKC activity. Phosphorylates TACC1, another protein involved in cell division, at 'Ser-228'.<ref>PMID:15316025</ref> <ref>PMID:15499654</ref> <ref>PMID:15670791</ref> <ref>PMID:15938719</ref> <ref>PMID:21493633</ref> <ref>PMID:21531210</ref> <ref>PMID:27332895</ref> |
| | + | |
| | + | ==See Also== |
| | + | *[[Centromere protein 3D structure|Centromere protein 3D structure]] |
| | == References == | | == References == |
| | <references/> | | <references/> |
| | __TOC__ | | __TOC__ |
| | </StructureSection> | | </StructureSection> |
| - | [[Category: Human]] | + | [[Category: Homo sapiens]] |
| | [[Category: Large Structures]] | | [[Category: Large Structures]] |
| - | [[Category: Non-specific serine/threonine protein kinase]] | + | [[Category: Abdul Azeez KR]] |
| - | [[Category: Arrowsmith, C]] | + | [[Category: Arrowsmith C]] |
| - | [[Category: Azeez, K R.Abdul]]
| + | [[Category: Bountra C]] |
| - | [[Category: Bountra, C]] | + | [[Category: Edwards AM]] |
| - | [[Category: Delft, F von]]
| + | [[Category: Elkins JM]] |
| - | [[Category: Edwards, A M]] | + | [[Category: Knapp S]] |
| - | [[Category: Elkins, J M]] | + | [[Category: Sorrell FJ]] |
| - | [[Category: Knapp, S]] | + | [[Category: Von Delft F]] |
| - | [[Category: Sorrell, F J]] | + | |
| - | [[Category: Kinase]] | + | |
| - | [[Category: Sgc]]
| + | |
| - | [[Category: Structural genomic]]
| + | |
| - | [[Category: Transferase]]
| + | |
| Structural highlights
Disease
AURKC_HUMAN Male infertility due to large-headed multiflagellar polyploid spermatozoa. The disease is caused by mutations affecting the gene represented in this entry.
Function
AURKC_HUMAN Serine/threonine-protein kinase component of the chromosomal passenger complex (CPC), a complex that acts as a key regulator of mitosis. The CPC complex has essential functions at the centromere in ensuring correct chromosome alignment and segregation and is required for chromatin-induced microtubule stabilization and spindle assembly. Plays also a role in meiosis and more particularly in spermatogenesis. Has redundant cellular functions with AURKB and can rescue an AURKB knockdown. Like AURKB, AURKC phosphorylates histone H3 at 'Ser-10' and 'Ser-28'. AURKC phosphorylates the CPC complex subunits BIRC5/survivin and INCENP leading to increased AURKC activity. Phosphorylates TACC1, another protein involved in cell division, at 'Ser-228'.[1] [2] [3] [4] [5] [6] [7]
See Also
References
- ↑ Li X, Sakashita G, Matsuzaki H, Sugimoto K, Kimura K, Hanaoka F, Taniguchi H, Furukawa K, Urano T. Direct association with inner centromere protein (INCENP) activates the novel chromosomal passenger protein, Aurora-C. J Biol Chem. 2004 Nov 5;279(45):47201-11. Epub 2004 Aug 16. PMID:15316025 doi:http://dx.doi.org/10.1074/jbc.M403029200
- ↑ Sasai K, Katayama H, Stenoien DL, Fujii S, Honda R, Kimura M, Okano Y, Tatsuka M, Suzuki F, Nigg EA, Earnshaw WC, Brinkley WR, Sen S. Aurora-C kinase is a novel chromosomal passenger protein that can complement Aurora-B kinase function in mitotic cells. Cell Motil Cytoskeleton. 2004 Dec;59(4):249-63. doi: 10.1002/cm.20039. PMID:15499654 doi:http://dx.doi.org/10.1002/cm.20039
- ↑ Yan X, Wu Y, Li Q, Cao L, Liu X, Saiyin H, Yu L. Cloning and characterization of a novel human Aurora C splicing variant. Biochem Biophys Res Commun. 2005 Mar 4;328(1):353-61. doi:, 10.1016/j.bbrc.2004.12.168. PMID:15670791 doi:http://dx.doi.org/10.1016/j.bbrc.2004.12.168
- ↑ Yan X, Cao L, Li Q, Wu Y, Zhang H, Saiyin H, Liu X, Zhang X, Shi Q, Yu L. Aurora C is directly associated with Survivin and required for cytokinesis. Genes Cells. 2005 Jun;10(6):617-26. doi: 10.1111/j.1365-2443.2005.00863.x. PMID:15938719 doi:http://dx.doi.org/10.1111/j.1365-2443.2005.00863.x
- ↑ Avo Santos M, van de Werken C, de Vries M, Jahr H, Vromans MJ, Laven JS, Fauser BC, Kops GJ, Lens SM, Baart EB. A role for Aurora C in the chromosomal passenger complex during human preimplantation embryo development. Hum Reprod. 2011 Jul;26(7):1868-81. doi: 10.1093/humrep/der111. Epub 2011 Apr 14. PMID:21493633 doi:http://dx.doi.org/10.1093/humrep/der111
- ↑ Gabillard JC, Ulisse S, Baldini E, Sorrenti S, Cremet JY, Coccaro C, Prigent C, D'Armiento M, Arlot-Bonnemains Y. Aurora-C interacts with and phosphorylates the transforming acidic coiled-coil 1 protein. Biochem Biophys Res Commun. 2011 May 20;408(4):647-53. doi:, 10.1016/j.bbrc.2011.04.078. Epub 2011 Apr 21. PMID:21531210 doi:http://dx.doi.org/10.1016/j.bbrc.2011.04.078
- ↑ Sasai K, Katayama H, Hawke DH, Sen S. Aurora-C Interactions with Survivin and INCENP Reveal Shared and Distinct Features Compared with Aurora-B Chromosome Passenger Protein Complex. PLoS One. 2016 Jun 22;11(6):e0157305. doi: 10.1371/journal.pone.0157305., eCollection 2016. PMID:27332895 doi:http://dx.doi.org/10.1371/journal.pone.0157305
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