2ysx
From Proteopedia
(Difference between revisions)
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==Solution structure of the human SHIP SH2 domain== | ==Solution structure of the human SHIP SH2 domain== | ||
- | <StructureSection load='2ysx' size='340' side='right' caption='[[2ysx]], [[NMR_Ensembles_of_Models | 20 NMR models]]' scene=''> | + | <StructureSection load='2ysx' size='340' side='right'caption='[[2ysx]], [[NMR_Ensembles_of_Models | 20 NMR models]]' scene=''> |
== Structural highlights == | == Structural highlights == | ||
- | <table><tr><td colspan='2'>[[2ysx]] is a 1 chain structure with sequence from [ | + | <table><tr><td colspan='2'>[[2ysx]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Human Human]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2YSX OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2YSX FirstGlance]. <br> |
- | </td></tr><tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">SHIP ([ | + | </td></tr><tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">SHIP ([https://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'>[ | + | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=2ysx FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2ysx OCA], [https://pdbe.org/2ysx PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2ysx RCSB], [https://www.ebi.ac.uk/pdbsum/2ysx PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2ysx ProSAT], [https://www.topsan.org/Proteins/RSGI/2ysx TOPSAN]</span></td></tr> |
</table> | </table> | ||
== Function == | == Function == | ||
- | [[ | + | [[https://www.uniprot.org/uniprot/SHIP1_HUMAN SHIP1_HUMAN]] Phosphatidylinositol (PtdIns) phosphatase that specifically hydrolyzes the 5-phosphate of phosphatidylinositol-3,4,5-trisphosphate (PtdIns(3,4,5)P3) to produce PtdIns(3,4)P2, thereby negatively regulating the PI3K (phosphoinositide 3-kinase) pathways. Acts as a negative regulator of B-cell antigen receptor signaling. Mediates signaling from the FC-gamma-RIIB receptor (FCGR2B), playing a central role in terminating signal transduction from activating immune/hematopoietic cell receptor systems. Acts as a negative regulator of myeloid cell proliferation/survival and chemotaxis, mast cell degranulation, immune cells homeostasis, integrin alpha-IIb/beta-3 signaling in platelets and JNK signaling in B-cells. Regulates proliferation of osteoclast precursors, macrophage programming, phagocytosis and activation and is required for endotoxin tolerance. Involved in the control of cell-cell junctions, CD32a signaling in neutrophils and modulation of EGF-induced phospholipase C activity. Key regulator of neutrophil migration, by governing the formation of the leading edge and polarization required for chemotaxis. Modulates FCGR3/CD16-mediated cytotoxicity in NK cells. Mediates the activin/TGF-beta-induced apoptosis through its Smad-dependent expression. May also hydrolyze PtdIns(1,3,4,5)P4, and could thus affect the levels of the higher inositol polyphosphates like InsP6.<ref>PMID:12421919</ref> <ref>PMID:16682172</ref> |
== 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: Human]] | [[Category: Human]] | ||
+ | [[Category: Large Structures]] | ||
[[Category: Harada, T]] | [[Category: Harada, T]] | ||
[[Category: Kasai, T]] | [[Category: Kasai, T]] |
Revision as of 13:37, 24 November 2021
Solution structure of the human SHIP SH2 domain
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Categories: Human | Large Structures | Harada, T | Kasai, T | Kigawa, T | Koshiba, S | Structural genomic | Watanabe, S | Yokoyama, S | National project on protein structural and functional analyse | Nppsfa | Phosphotyrosine binding domain | Protein tyrosine kinase | Rsgi | Sh2 domain | Signal transduction | Signaling protein