SSH2

Protein phosphatase Slingshot homolog 2 is an enzyme that in humans is encoded by the SSH2 gene.[5][6][7]

SSH2
Available structures PDB Ortholog search: PDBe RCSB List of PDB id codes 2NT2
Identifiers
Aliases	SSH2, SSH-2, SSH-2L, slingshot protein phosphatase 2
External IDs	OMIM: 606779 MGI: 2679255 HomoloGene: 14116 GeneCards: SSH2
Gene location (Human) Chr. Chromosome 17 (human)[1] Band 17q11.2 Start 29,625,938 bp[1] End 29,930,276 bp[1]
Gene location (Mouse) Chr. Chromosome 11 (mouse)[2] Band 11|11 B5 Start 77,216,287 bp[2] End 77,460,220 bp[2]
RNA expression pattern More reference expression data
Gene ontology Molecular function • protein tyrosine phosphatase activity • phosphatase activity • actin binding • phosphoprotein phosphatase activity • hydrolase activity • protein tyrosine/serine/threonine phosphatase activity Cellular component • cytoplasm • cytoskeleton • extracellular Biological process • regulation of lamellipodium assembly • regulation of axonogenesis • regulation of actin polymerization or depolymerization • protein dephosphorylation • peptidyl-tyrosine dephosphorylation • actin cytoskeleton organization • dephosphorylation • cell morphogenesis Sources:Amigo / QuickGO
Orthologs
Species	Human	Mouse
Entrez	85464	237860
Ensembl	ENSG00000141298	ENSMUSG00000037926
UniProt	Q76I76	Q5SW75
RefSeq (mRNA)	NM_001282129 NM_001282130 NM_001282131 NM_033389	NM_001291190 NM_177710
RefSeq (protein)	NP_001269058 NP_001269059 NP_001269060 NP_203747	NP_001278119 NP_808378
Location (UCSC)	Chr 17: 29.63 – 29.93 Mb	Chr 11: 77.22 – 77.46 Mb
PubMed search	[3]	[4]
Wikidata
View/Edit Human View/Edit Mouse

For the SSH-2 protocol, see Secure Shell#Version 2.x

The ADF (actin-depolymerizing factor)/cofilin family (see MIM 601442) is composed of stimulus-responsive mediators of actin dynamics. ADF/cofilin proteins are inactivated by kinases such as LIM domain kinase-1 (LIMK1; MIM 601329). The SSH family appears to play a role in actin dynamics by reactivating ADF/cofilin proteins in vivo (Niwa et al., 2002).[supplied by OMIM][7]

References

1. GRCh38: Ensembl release 89: ENSG00000141298 - Ensembl, May 2017
2. GRCm38: Ensembl release 89: ENSMUSG00000037926 - Ensembl, May 2017
3. "Human PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
4. "Mouse PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
5. Niwa R, Nagata-Ohashi K, Takeichi M, Mizuno K, Uemura T (Feb 2002). "Control of actin reorganization by Slingshot, a family of phosphatases that dephosphorylate ADF/cofilin". Cell. 108 (2): 233–46. doi:10.1016/S0092-8674(01)00638-9. PMID 11832213. S2CID 5576208.
6. Nagase T, Kikuno R, Hattori A, Kondo Y, Okumura K, Ohara O (Feb 2001). "Prediction of the coding sequences of unidentified human genes. XIX. The complete sequences of 100 new cDNA clones from brain which code for large proteins in vitro". DNA Res. 7 (6): 347–55. doi:10.1093/dnares/7.6.347. PMID 11214970.
7. "Entrez Gene: SSH2 slingshot homolog 2 (Drosophila)".

Further reading

• Strausberg RL, Feingold EA, Grouse LH, et al. (2003). "Generation and initial analysis of more than 15,000 full-length human and mouse cDNA sequences". Proc. Natl. Acad. Sci. U.S.A. 99 (26): 16899–903. doi:10.1073/pnas.242603899. PMC 139241. PMID 12477932.
• Chan SY, Chan AK, Cheung BP, et al. (2004). "Identification of genes expressed during myocardial development". Chin. Med. J. 116 (9): 1329–32. PMID 14527359.
• Ohta Y, Kousaka K, Nagata-Ohashi K, et al. (2004). "Differential activities, subcellular distribution and tissue expression patterns of three members of Slingshot family phosphatases that dephosphorylate cofilin". Genes Cells. 8 (10): 811–24. doi:10.1046/j.1365-2443.2003.00678.x. PMID 14531860. S2CID 24247372.
• Ota T, Suzuki Y, Nishikawa T, et al. (2004). "Complete sequencing and characterization of 21,243 full-length human cDNAs". Nat. Genet. 36 (1): 40–5. doi:10.1038/ng1285. PMID 14702039.
• Ballif BA, Villén J, Beausoleil SA, et al. (2005). "Phosphoproteomic analysis of the developing mouse brain". Mol. Cell. Proteomics. 3 (11): 1093–101. doi:10.1074/mcp.M400085-MCP200. PMID 15345747.
• Gerhard DS, Wagner L, Feingold EA, et al. (2004). "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)". Genome Res. 14 (10B): 2121–7. doi:10.1101/gr.2596504. PMC 528928. PMID 15489334.
• Soosairajah J, Maiti S, Wiggan O, et al. (2005). "Interplay between components of a novel LIM kinase-slingshot phosphatase complex regulates cofilin". EMBO J. 24 (3): 473–86. doi:10.1038/sj.emboj.7600543. PMC 548651. PMID 15660133.
• Rual JF, Venkatesan K, Hao T, et al. (2005). "Towards a proteome-scale map of the human protein-protein interaction network". Nature. 437 (7062): 1173–8. doi:10.1038/nature04209. PMID 16189514. S2CID 4427026.
• Olsen JV, Blagoev B, Gnad F, et al. (2006). "Global, in vivo, and site-specific phosphorylation dynamics in signaling networks". Cell. 127 (3): 635–48. doi:10.1016/j.cell.2006.09.026. PMID 17081983. S2CID 7827573.
• Kligys K, Claiborne JN, DeBiase PJ, et al. (2007). "The slingshot family of phosphatases mediates Rac1 regulation of cofilin phosphorylation, laminin-332 organization, and motility behavior of keratinocytes". J. Biol. Chem. 282 (44): 32520–8. doi:10.1074/jbc.M707041200. PMC 2754063. PMID 17848544.

External links

• Overview of all the structural information available in the PDB for UniProt: Q76I76 (Protein phosphatase Slingshot homolog 2) at the PDBe-KB.