SSH3

Slingshot protein phosphatase 3
Identifiers
Symbols	SSH3 ; SSH3L
External IDs	OMIM: 606780 MGI: 2683546 HomoloGene: 32372 GeneCards: SSH3 Gene
EC number	3.1.3.16, 3.1.3.48
Gene ontology Molecular function • DNA binding • actin binding • protein tyrosine phosphatase activity • protein tyrosine/serine/threonine phosphatase activity Cellular component • nucleus • cytoplasm • cytoskeleton Biological process • protein dephosphorylation • regulation of actin polymerization or depolymerization • regulation of lamellipodium assembly • peptidyl-tyrosine dephosphorylation • regulation of axonogenesis Sources: Amigo / QuickGO
RNA expression pattern
More reference expression data
Orthologs
Species	Human	Mouse
Entrez	54961	245857
Ensembl	ENSG00000172830	ENSMUSG00000034616
UniProt	Q8TE77	Q8K330
RefSeq (mRNA)	NM_017857	NM_198113
RefSeq (protein)	NP_060327	NP_932781
Location (UCSC)	Chr 11: 67.3 – 67.31 Mb	Chr 19: 4.26 – 4.27 Mb
PubMed search

Protein phosphatase Slingshot homolog 3 is an enzyme that in humans is encoded by the SSH3 gene.^[1][2]

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]^[2]

References

1. 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.
2. "Entrez Gene: SSH3 slingshot homolog 3 (Drosophila)".

Further reading

• 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.
• Beausoleil SA, Villén J, Gerber SA, et al. (2006). "A probability-based approach for high-throughput protein phosphorylation analysis and site localization.". Nat. Biotechnol. 24 (10): 1285–92. doi:10.1038/nbt1240. PMID 16964243.
• 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.
• 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.
• 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.
• 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.
• 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.
• 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.