| Structural highlights
3eu9 is a 3 chain structure with sequence from Homo sapiens. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
| | Ligands: | , , |
| Related: | 3b95 |
| Gene: | ZDHHC17, HIP14, HIP3, HYPH, KIAA0946, HSPC294 (Homo sapiens) |
| Resources: | FirstGlance, OCA, RCSB, PDBsum |
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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