2iy1: Difference between revisions

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 <StructureSection load='2iy1' size='340' side='right'caption='[[2iy1]], [[Resolution|resolution]] 2.46&Aring;' scene=''>
 == Structural highlights ==
-<table><tr><td colspan='2'>[[2iy1]] is a 4 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2IY1 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2IY1 FirstGlance]. <br>
+<table><tr><td colspan='2'>[[2iy1]] is a 4 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=2IY1 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2IY1 FirstGlance]. <br>
-</td></tr><tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[2ckg|2ckg]], [[2ckh|2ckh]], [[1a5r|1a5r]], [[1tgz|1tgz]], [[1wyw|1wyw]], [[1y8r|1y8r]], [[1z5s|1z5s]], [[2asq|2asq]], [[2bf8|2bf8]], [[2iy0|2iy0]], [[2iyc|2iyc]], [[2iyd|2iyd]]</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]] 2.46&#8491;</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=2iy1 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2iy1 OCA], [http://pdbe.org/2iy1 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=2iy1 RCSB], [http://www.ebi.ac.uk/pdbsum/2iy1 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=2iy1 ProSAT]</span></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=2iy1 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2iy1 OCA], [https://pdbe.org/2iy1 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2iy1 RCSB], [https://www.ebi.ac.uk/pdbsum/2iy1 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2iy1 ProSAT]</span></td></tr>
 </table>
-== Disease ==
-[[http://www.uniprot.org/uniprot/SUMO1_HUMAN SUMO1_HUMAN]] Defects in SUMO1 are the cause of non-syndromic orofacial cleft type 10 (OFC10) [MIM:[http://omim.org/entry/613705 613705]]; also called non-syndromic cleft lip with or without cleft palate 10. OFC10 is a birth defect consisting of cleft lips with or without cleft palate. Cleft lips are associated with cleft palate in two-third of cases. A cleft lip can occur on one or both sides and range in severity from a simple notch in the upper lip to a complete opening in the lip extending into the floor of the nostril and involving the upper gum. Note=A chromosomal aberation involving SUMO1 is the cause of OFC10. Translocation t(2;8)(q33.1;q24.3). The breakpoint occurred in the SUMO1 gene and resulted in haploinsufficiency confirmed by protein assays.<ref>PMID:16990542</ref>
 == 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/SUMO1_HUMAN SUMO1_HUMAN]] Ubiquitin-like protein that can be covalently attached to proteins as a monomer or a lysine-linked polymer. Covalent attachment via an isopeptide bond to its substrates requires prior activation by the E1 complex SAE1-SAE2 and linkage to the E2 enzyme UBE2I, and can be promoted by E3 ligases such as PIAS1-4, RANBP2 or CBX4. This post-translational modification on lysine residues of proteins plays a crucial role in a number of cellular processes such as nuclear transport, DNA replication and repair, mitosis and signal transduction. Involved for instance in targeting RANGAP1 to the nuclear pore complex protein RANBP2. Polymeric SUMO1 chains are also susceptible to polyubiquitination which functions as a signal for proteasomal degradation of modified proteins. May also regulate a network of genes involved in palate development.<ref>PMID:9019411</ref> <ref>PMID:9162015</ref> <ref>PMID:18538659</ref> <ref>PMID:18408734</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>
 == Evolutionary Conservation ==
 [[Image:Consurf_key_small.gif|200px|right]]
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 ==See Also==
-*[[SUMO|SUMO]]
+*[[SUMO 3D Structures|SUMO 3D Structures]]
 *[[Sentrin-specific protease|Sentrin-specific protease]]
 == References ==
@@ Line 38: / Line 36: @@
 __TOC__
 </StructureSection>
+[[Category: Homo sapiens]]
 [[Category: Large Structures]]
-[[Category: Dong, C]]
+[[Category: Dong C]]
-[[Category: Naismith, J H]]
+[[Category: Naismith JH]]
-[[Category: Shen, L]]
+[[Category: Shen L]]
-[[Category: Hydrolase]]
-[[Category: Hydrolase-nuclear protein complex]]
-[[Category: Nuclear protein]]
-[[Category: Protease]]
-[[Category: Protein protein complex]]
-[[Category: Thiol protease]]
-[[Category: Ubiquitin]]
-[[Category: Ubl conjugation pathway]]