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| | <StructureSection load='6nnq' size='340' side='right'caption='[[6nnq]], [[Resolution|resolution]] 2.62Å' scene=''> | | <StructureSection load='6nnq' size='340' side='right'caption='[[6nnq]], [[Resolution|resolution]] 2.62Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[6nnq]] is a 2 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6NNQ OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=6NNQ FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[6nnq]] 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=6NNQ OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=6NNQ FirstGlance]. <br> |
| - | </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=6nnq FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6nnq OCA], [http://pdbe.org/6nnq PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=6nnq RCSB], [http://www.ebi.ac.uk/pdbsum/6nnq PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=6nnq ProSAT]</span></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]] 2.621Å</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=6nnq FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6nnq OCA], [https://pdbe.org/6nnq PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=6nnq RCSB], [https://www.ebi.ac.uk/pdbsum/6nnq PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=6nnq ProSAT]</span></td></tr> |
| | </table> | | </table> |
| | == Function == | | == Function == |
| - | [[http://www.uniprot.org/uniprot/SENP1_HUMAN SENP1_HUMAN]] Protease that catalyzes two essential functions in the SUMO pathway: processing of full-length SUMO1, SUMO2 and SUMO3 to their mature forms and deconjugation of SUMO1, SUMO2 and SUMO3 from targeted proteins. Deconjugates SUMO1 from HIPK2. Deconjugates SUMO1 from HDAC1, which decreases its transcriptional repression activity.<ref>PMID:10652325</ref> <ref>PMID:15199155</ref> <ref>PMID:16253240</ref> <ref>PMID:16553580</ref> [[http://www.uniprot.org/uniprot/SUMO3_HUMAN SUMO3_HUMAN]] Ubiquitin-like protein which can be covalently attached to target lysines either as a monomer or as a lysine-linked polymer. Does not seem to be involved in protein degradation and may function as an antagonist of ubiquitin in the degradation process. Plays a role in a number of cellular processes such as nuclear transport, DNA replication and repair, mitosis and signal transduction. Covalent attachment to its substrates requires prior activation by the E1 complex SAE1-SAE2 and linkage to the E2 enzyme UBE2I, and can be promoted by an E3 ligase such as PIAS1-4, RANBP2 or CBX4.<ref>PMID:11451954</ref> <ref>PMID:18538659</ref> | + | [https://www.uniprot.org/uniprot/SENP1_HUMAN SENP1_HUMAN] Protease that catalyzes two essential functions in the SUMO pathway: processing of full-length SUMO1, SUMO2 and SUMO3 to their mature forms and deconjugation of SUMO1, SUMO2 and SUMO3 from targeted proteins. Deconjugates SUMO1 from HIPK2. Deconjugates SUMO1 from HDAC1, which decreases its transcriptional repression activity.<ref>PMID:10652325</ref> <ref>PMID:15199155</ref> <ref>PMID:16253240</ref> <ref>PMID:16553580</ref> |
| | + | |
| | + | ==See Also== |
| | + | *[[SUMO 3D Structures|SUMO 3D Structures]] |
| | + | *[[Sentrin-specific protease|Sentrin-specific protease]] |
| | == References == | | == References == |
| | <references/> | | <references/> |
| | __TOC__ | | __TOC__ |
| | </StructureSection> | | </StructureSection> |
| | + | [[Category: Homo sapiens]] |
| | [[Category: Large Structures]] | | [[Category: Large Structures]] |
| - | [[Category: Ambaye, N D]] | + | [[Category: Ambaye ND]] |
| - | [[Category: Hydrolase-protein binding complex]]
| + | |
| - | [[Category: Senp1]]
| + | |
| - | [[Category: Sumo2]]
| + | |
| - | [[Category: Sumoylation]]
| + | |
| Structural highlights
Function
SENP1_HUMAN Protease that catalyzes two essential functions in the SUMO pathway: processing of full-length SUMO1, SUMO2 and SUMO3 to their mature forms and deconjugation of SUMO1, SUMO2 and SUMO3 from targeted proteins. Deconjugates SUMO1 from HIPK2. Deconjugates SUMO1 from HDAC1, which decreases its transcriptional repression activity.[1] [2] [3] [4]
See Also
References
- ↑ Gong L, Millas S, Maul GG, Yeh ET. Differential regulation of sentrinized proteins by a novel sentrin-specific protease. J Biol Chem. 2000 Feb 4;275(5):3355-9. PMID:10652325
- ↑ Cheng J, Wang D, Wang Z, Yeh ET. SENP1 enhances androgen receptor-dependent transcription through desumoylation of histone deacetylase 1. Mol Cell Biol. 2004 Jul;24(13):6021-8. PMID:15199155 doi:10.1128/MCB.24.13.6021-6028.2004
- ↑ Kim YH, Sung KS, Lee SJ, Kim YO, Choi CY, Kim Y. Desumoylation of homeodomain-interacting protein kinase 2 (HIPK2) through the cytoplasmic-nuclear shuttling of the SUMO-specific protease SENP1. FEBS Lett. 2005 Nov 7;579(27):6272-8. Epub 2005 Oct 19. PMID:16253240 doi:S0014-5793(05)01251-2
- ↑ Shen LN, Dong C, Liu H, Naismith JH, Hay RT. The structure of SENP1-SUMO-2 complex suggests a structural basis for discrimination between SUMO paralogues during processing. Biochem J. 2006 Jul 15;397(2):279-88. PMID:16553580 doi:10.1042/BJ20052030
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