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| | <StructureSection load='3eu9' size='340' side='right'caption='[[3eu9]], [[Resolution|resolution]] 1.99Å' scene=''> | | <StructureSection load='3eu9' size='340' side='right'caption='[[3eu9]], [[Resolution|resolution]] 1.99Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[3eu9]] is a 3 chain structure with sequence from [https://en.wikipedia.org/wiki/Human Human]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3EU9 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3EU9 FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[3eu9]] is a 3 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=3EU9 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3EU9 FirstGlance]. <br> |
| - | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=GOL:GLYCEROL'>GOL</scene>, <scene name='pdbligand=HIS:HISTIDINE'>HIS</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</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]] 1.99Å</td></tr> |
| - | <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat"><div style='overflow: auto; max-height: 3em;'>[[3b95|3b95]]</div></td></tr> | + | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=GOL:GLYCEROL'>GOL</scene>, <scene name='pdbligand=HIS:HISTIDINE'>HIS</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene></td></tr> |
| - | <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">ZDHHC17, HIP14, HIP3, HYPH, KIAA0946, HSPC294 ([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'>[https://proteopedia.org/fgij/fg.htm?mol=3eu9 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3eu9 OCA], [https://pdbe.org/3eu9 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3eu9 RCSB], [https://www.ebi.ac.uk/pdbsum/3eu9 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3eu9 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=3eu9 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3eu9 OCA], [https://pdbe.org/3eu9 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3eu9 RCSB], [https://www.ebi.ac.uk/pdbsum/3eu9 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3eu9 ProSAT]</span></td></tr> |
| | </table> | | </table> |
| | == Function == | | == Function == |
| - | [[https://www.uniprot.org/uniprot/ZDH17_HUMAN ZDH17_HUMAN]] Palmitoyltransferase specific for a subset of neuronal proteins, including SNAP25, DLG4/PSD95, GAD2, SYT1 and HD. Palmitoylates MPP1 in erythrocytes. May be involved in the sorting or targeting of critical proteins involved in the initiating events of endocytosis at the plasma membrane. Has transforming activity. Mediates Mg(2+) transport.<ref>PMID:12393793</ref> <ref>PMID:15603740</ref> <ref>PMID:15489887</ref> <ref>PMID:18794299</ref> <ref>PMID:22496366</ref>
| + | [https://www.uniprot.org/uniprot/ZDH17_HUMAN ZDH17_HUMAN] Palmitoyltransferase specific for a subset of neuronal proteins, including SNAP25, DLG4/PSD95, GAD2, SYT1 and HD. Palmitoylates MPP1 in erythrocytes. May be involved in the sorting or targeting of critical proteins involved in the initiating events of endocytosis at the plasma membrane. Has transforming activity. Mediates Mg(2+) transport.<ref>PMID:12393793</ref> <ref>PMID:15603740</ref> <ref>PMID:15489887</ref> <ref>PMID:18794299</ref> <ref>PMID:22496366</ref> |
| | == Evolutionary Conservation == | | == Evolutionary Conservation == |
| | [[Image:Consurf_key_small.gif|200px|right]] | | [[Image:Consurf_key_small.gif|200px|right]] |
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| | __TOC__ | | __TOC__ |
| | </StructureSection> | | </StructureSection> |
| - | [[Category: Human]] | + | [[Category: Homo sapiens]] |
| | [[Category: Large Structures]] | | [[Category: Large Structures]] |
| - | [[Category: Cheng, X]] | + | [[Category: Cheng X]] |
| - | [[Category: Collins, R E]] | + | [[Category: Collins RE]] |
| - | [[Category: Gao, T]] | + | [[Category: Gao T]] |
| - | [[Category: Horton, J R]] | + | [[Category: Horton JR]] |
| - | [[Category: Zhang, R]] | + | [[Category: Zhang R]] |
| - | [[Category: Zhang, X]] | + | [[Category: Zhang X]] |
| - | [[Category: Acyltransferase]]
| + | |
| - | [[Category: Ank repeat]]
| + | |
| - | [[Category: Ankyrin repeat]]
| + | |
| - | [[Category: Cytoplasmic vesicle]]
| + | |
| - | [[Category: Epigenetic]]
| + | |
| - | [[Category: Golgi apparatus]]
| + | |
| - | [[Category: Huntingtin interacting protein 14]]
| + | |
| - | [[Category: Membrane]]
| + | |
| - | [[Category: Metal-binding]]
| + | |
| - | [[Category: Methyl-lysine-binding protein]]
| + | |
| - | [[Category: Methyllyine binding]]
| + | |
| - | [[Category: Oncogene]]
| + | |
| - | [[Category: Phosphoprotein]]
| + | |
| - | [[Category: Protein binding]]
| + | |
| - | [[Category: Transferase]]
| + | |
| - | [[Category: Transmembrane]]
| + | |
| - | [[Category: Zinc-finger]]
| + | |
| Structural highlights
Function
ZDH17_HUMAN Palmitoyltransferase specific for a subset of neuronal proteins, including SNAP25, DLG4/PSD95, GAD2, SYT1 and HD. Palmitoylates MPP1 in erythrocytes. May be involved in the sorting or targeting of critical proteins involved in the initiating events of endocytosis at the plasma membrane. Has transforming activity. Mediates Mg(2+) transport.[1] [2] [3] [4] [5]
Evolutionary Conservation
Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.
References
- ↑ Singaraja RR, Hadano S, Metzler M, Givan S, Wellington CL, Warby S, Yanai A, Gutekunst CA, Leavitt BR, Yi H, Fichter K, Gan L, McCutcheon K, Chopra V, Michel J, Hersch SM, Ikeda JE, Hayden MR. HIP14, a novel ankyrin domain-containing protein, links huntingtin to intracellular trafficking and endocytosis. Hum Mol Genet. 2002 Nov 1;11(23):2815-28. PMID:12393793
- ↑ Huang K, Yanai A, Kang R, Arstikaitis P, Singaraja RR, Metzler M, Mullard A, Haigh B, Gauthier-Campbell C, Gutekunst CA, Hayden MR, El-Husseini A. Huntingtin-interacting protein HIP14 is a palmitoyl transferase involved in palmitoylation and trafficking of multiple neuronal proteins. Neuron. 2004 Dec 16;44(6):977-86. PMID:15603740 doi:http://dx.doi.org/S0896627304007500
- ↑ Ducker CE, Stettler EM, French KJ, Upson JJ, Smith CD. Huntingtin interacting protein 14 is an oncogenic human protein: palmitoyl acyltransferase. Oncogene. 2004 Dec 9;23(57):9230-7. PMID:15489887 doi:http://dx.doi.org/10.1038/sj.onc.1208171
- ↑ Goytain A, Hines RM, Quamme GA. Huntingtin-interacting proteins, HIP14 and HIP14L, mediate dual functions, palmitoyl acyltransferase and Mg2+ transport. J Biol Chem. 2008 Nov 28;283(48):33365-74. doi: 10.1074/jbc.M801469200. Epub 2008, Sep 15. PMID:18794299 doi:http://dx.doi.org/10.1074/jbc.M801469200
- ↑ Lach A, Grzybek M, Heger E, Korycka J, Wolny M, Kubiak J, Kolondra A, Boguslawska DM, Augoff K, Majkowski M, Podkalicka J, Kaczor J, Stefanko A, Kuliczkowski K, Sikorski AF. Palmitoylation of MPP1 (membrane-palmitoylated protein 1)/p55 is crucial for lateral membrane organization in erythroid cells. J Biol Chem. 2012 Jun 1;287(23):18974-84. doi: 10.1074/jbc.M111.332981. Epub 2012, Apr 10. PMID:22496366 doi:http://dx.doi.org/10.1074/jbc.M111.332981
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