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| | <StructureSection load='1v38' size='340' side='right'caption='[[1v38]], [[NMR_Ensembles_of_Models | 20 NMR models]]' scene=''> | | <StructureSection load='1v38' size='340' side='right'caption='[[1v38]], [[NMR_Ensembles_of_Models | 20 NMR models]]' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[1v38]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Lk3_transgenic_mice Lk3 transgenic mice]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1V38 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1V38 FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[1v38]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Lk3_transgenic_mice Lk3 transgenic mice]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1V38 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1V38 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=1v38 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1v38 OCA], [http://pdbe.org/1v38 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1v38 RCSB], [http://www.ebi.ac.uk/pdbsum/1v38 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=1v38 ProSAT], [http://www.topsan.org/Proteins/RSGI/1v38 TOPSAN]</span></td></tr> | + | </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=1v38 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1v38 OCA], [https://pdbe.org/1v38 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1v38 RCSB], [https://www.ebi.ac.uk/pdbsum/1v38 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1v38 ProSAT], [https://www.topsan.org/Proteins/RSGI/1v38 TOPSAN]</span></td></tr> |
| | </table> | | </table> |
| | == Function == | | == Function == |
| - | [[http://www.uniprot.org/uniprot/SAMN1_MOUSE SAMN1_MOUSE]] Negative regulator of B-cell activation. Down-regulates cell proliferation (in vitro). Promotes RAC1-dependent membrane ruffle formation and reorganization of the actin cytoskeleton. Regulates cell spreading and cell polarization. Stimulates HDAC1 activity. Regulates LYN activity by modulating its tyrosine phosphorylation.<ref>PMID:15381729</ref> <ref>PMID:19923443</ref> <ref>PMID:20478393</ref> <ref>PMID:21296879</ref> | + | [[https://www.uniprot.org/uniprot/SAMN1_MOUSE SAMN1_MOUSE]] Negative regulator of B-cell activation. Down-regulates cell proliferation (in vitro). Promotes RAC1-dependent membrane ruffle formation and reorganization of the actin cytoskeleton. Regulates cell spreading and cell polarization. Stimulates HDAC1 activity. Regulates LYN activity by modulating its tyrosine phosphorylation.<ref>PMID:15381729</ref> <ref>PMID:19923443</ref> <ref>PMID:20478393</ref> <ref>PMID:21296879</ref> |
| | == Evolutionary Conservation == | | == Evolutionary Conservation == |
| | [[Image:Consurf_key_small.gif|200px|right]] | | [[Image:Consurf_key_small.gif|200px|right]] |
| Structural highlights
Function
[SAMN1_MOUSE] Negative regulator of B-cell activation. Down-regulates cell proliferation (in vitro). Promotes RAC1-dependent membrane ruffle formation and reorganization of the actin cytoskeleton. Regulates cell spreading and cell polarization. Stimulates HDAC1 activity. Regulates LYN activity by modulating its tyrosine phosphorylation.[1] [2] [3] [4]
Evolutionary Conservation
Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.
References
- ↑ Zhu YX, Benn S, Li ZH, Wei E, Masih-Khan E, Trieu Y, Bali M, McGlade CJ, Claudio JO, Stewart AK. The SH3-SAM adaptor HACS1 is up-regulated in B cell activation signaling cascades. J Exp Med. 2004 Sep 20;200(6):737-47. PMID:15381729 doi:http://dx.doi.org/10.1084/jem.20031816
- ↑ Wang D, Stewart AK, Zhuang L, Zhu Y, Wang Y, Shi C, Keating A, Slutsky A, Zhang H, Wen XY. Enhanced adaptive immunity in mice lacking the immunoinhibitory adaptor Hacs1. FASEB J. 2010 Mar;24(3):947-56. doi: 10.1096/fj.09-140806. Epub 2009 Nov 18. PMID:19923443 doi:http://dx.doi.org/10.1096/fj.09-140806
- ↑ Brandt S, Ellwanger K, Beuter-Gunia C, Schuster M, Hausser A, Schmitz I, Beer-Hammer S. SLy2 targets the nuclear SAP30/HDAC1 complex. Int J Biochem Cell Biol. 2010 Sep;42(9):1472-81. doi:, 10.1016/j.biocel.2010.05.004. Epub 2010 May 15. PMID:20478393 doi:http://dx.doi.org/10.1016/j.biocel.2010.05.004
- ↑ von Holleben M, Gohla A, Janssen KP, Iritani BM, Beer-Hammer S. Immunoinhibitory adapter protein Src homology domain 3 lymphocyte protein 2 (SLy2) regulates actin dynamics and B cell spreading. J Biol Chem. 2011 Apr 15;286(15):13489-501. doi: 10.1074/jbc.M110.155184. Epub, 2011 Feb 4. PMID:21296879 doi:http://dx.doi.org/10.1074/jbc.M110.155184
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