SSH2

From Wikipedia, the free encyclopedia

Slingshot homolog 2 (Drosophila)

PDB rendering based on 2nt2.

Available structures: 2nt2

Identifiers

Symbol(s)

SSH2; KIAA1725; MGC78588; SSH-2

External IDs

OMIM: 606779 MGI: 2679255 HomoloGene: 14116

Gene ontology
Molecular Function:	• actin binding • protein tyrosine phosphatase activity • protein tyrosine/serine/threonine phosphatase activity • hydrolase activity
Cellular Component:	• cytoskeleton
Biological Process:	• protein amino acid dephosphorylation • actin cytoskeleton organization and biogenesis

RNA expression pattern

More reference expression data

Orthologs

Human

Mouse

Refseq

NM_033389 (mRNA)
NP_203747 (protein)

NM_177710 (mRNA)
NP_808378 (protein)

Location

Chr 17: 24.98 - 25.28 Mb

Chr 11: 77.03 - 77.27 Mb

Pubmed search

[1]

[2]

For the SSH-2 protocol, see Secure Shell

Slingshot homolog 2 (Drosophila), also known as SSH2, is a human gene.^[1]

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]^[1]

[edit] References

^ ^a ^b Entrez Gene: SSH2 slingshot homolog 2 (Drosophila).

[edit] Further reading

Nagase T, Kikuno R, Hattori A, et al. (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. PMID 11214970.
Niwa R, Nagata-Ohashi K, Takeichi M, et al. (2002). "Control of actin reorganization by Slingshot, a family of phosphatases that dephosphorylate ADF/cofilin.". Cell 108 (2): 233-46. PMID 11832213.
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. 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. PMID 14531860.
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. 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. 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.
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.
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. PMID 17848544.