SSH1

For the SSH-1 protocol, see Secure Shell#Version 1.x

SSH1
Identifiers
Aliases	SSH1, SSH1L, slingshot protein phosphatase 1
External IDs	OMIM: 606778 MGI: 2686240 HomoloGene: 41299 GeneCards: SSH1
Gene location (Human) Chr. Chromosome 12 (human)[1] Band 12q24.11 Start 108,778,191 bp[1] End 108,857,590 bp[1]
Gene location (Mouse) Chr. Chromosome 5 (mouse)[2] Band 5|5 F Start 113,937,094 bp[2] End 113,993,894 bp[2]
RNA expression pattern More reference expression data
Gene ontology Molecular function • phosphoprotein phosphatase activity • phosphatase activity • GO:0001948 protein binding • protein tyrosine phosphatase activity • actin binding • hydrolase activity • protein tyrosine/serine/threonine phosphatase activity Cellular component • cytoplasm • cell projection • cell membrane • midbody • cleavage furrow • cytoskeleton • lamellipodium • cytosol • growth cone • cell leading edge • membrane • integral component of membrane Biological process • regulation of lamellipodium assembly • protein dephosphorylation • regulation of axonogenesis • regulation of actin polymerization or depolymerization • cell morphogenesis • regulation of cellular protein metabolic process • peptidyl-tyrosine dephosphorylation • cellular response to ATP • actin cytoskeleton organization • dephosphorylation • positive regulation of synaptic plasticity • excitatory chemical synaptic transmission • positive regulation of neuron death • positive regulation of AMPA glutamate receptor clustering • positive regulation of vascular associated smooth muscle cell migration • positive regulation of excitatory postsynaptic potential Sources:Amigo / QuickGO
Orthologs
Species	Human	Mouse
Entrez	54434	231637
Ensembl	ENSG00000084112	ENSMUSG00000042121
UniProt	Q8WYL5	Q76I79
RefSeq (mRNA)	NM_001161330 NM_001161331 NM_018984	NM_198109 NM_001363469
RefSeq (protein)	NP_001154802 NP_001154803 NP_061857	NP_932777 NP_001350398
Location (UCSC)	Chr 12: 108.78 – 108.86 Mb	Chr 5: 113.94 – 113.99 Mb
PubMed search	[3]	[4]
Wikidata
View/Edit Human View/Edit Mouse

Protein phosphatase Slingshot homolog 1 is an enzyme that in humans is encoded by the SSH1 gene.[5][6][7]

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: ENSG00000084112 - Ensembl, May 2017
2. GRCm38: Ensembl release 89: ENSMUSG00000042121 - 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. Nagase T, Kikuno R, Ishikawa KI, Hirosawa M, Ohara O (Apr 2000). "Prediction of the coding sequences of unidentified human genes. XVI. The complete sequences of 150 new cDNA clones from brain which code for large proteins in vitro". DNA Res. 7 (1): 65–73. doi:10.1093/dnares/7.1.65. PMID 10718198.
6. 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.
7. "Entrez Gene: SSH1 slingshot homolog 1 (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. Bibcode:2002PNAS...9916899M. doi:10.1073/pnas.242603899. PMC 139241. PMID 12477932.
• Endo M, Ohashi K, Sasaki Y, et al. (2003). "Control of growth cone motility and morphology by LIM kinase and Slingshot via phosphorylation and dephosphorylation of cofilin". J. Neurosci. 23 (7): 2527–37. doi:10.1523/JNEUROSCI.23-07-02527.2003. PMC 6742113. PMID 12684437.
• Kaji N, Ohashi K, Shuin M, et al. (2003). "Cell cycle-associated changes in Slingshot phosphatase activity and roles in cytokinesis in animal cells". J. Biol. Chem. 278 (35): 33450–5. doi:10.1074/jbc.M305802200. PMID 12807904.
• 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.
• Nishita M, Wang Y, Tomizawa C, et al. (2004). "Phosphoinositide 3-kinase-mediated activation of cofilin phosphatase Slingshot and its role for insulin-induced membrane protrusion". J. Biol. Chem. 279 (8): 7193–8. doi:10.1074/jbc.M312591200. PMID 14645219.
• 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.
• Dai S, Sarmiere PD, Wiggan O, et al. (2004). "Efficient Salmonella entry requires activity cycles of host ADF and cofilin". Cell. Microbiol. 6 (5): 459–71. doi:10.1111/j.1462-5822.2004.00375.x. PMID 15056216. S2CID 20238982.
• Nagata-Ohashi K, Ohta Y, Goto K, et al. (2004). "A pathway of neuregulin-induced activation of cofilin-phosphatase Slingshot and cofilin in lamellipodia". J. Cell Biol. 165 (4): 465–71. doi:10.1083/jcb.200401136. PMC 2172350. PMID 15159416.
• Beausoleil SA, Jedrychowski M, Schwartz D, et al. (2004). "Large-scale characterization of HeLa cell nuclear phosphoproteins". Proc. Natl. Acad. Sci. U.S.A. 101 (33): 12130–5. doi:10.1073/pnas.0404720101. PMC 514446. PMID 15302935.
• Zhang Z, Niu Z, Yuan W, et al. (2005). "Fine mapping and identification of a candidate gene SSH1 in disseminated superficial actinic porokeratosis". Hum. Mutat. 24 (5): 438. doi:10.1002/humu.9283. PMID 15459975. S2CID 22946257.
• 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.
• Wang Y, Shibasaki F, Mizuno K (2005). "Calcium signal-induced cofilin dephosphorylation is mediated by Slingshot via calcineurin". J. Biol. Chem. 280 (13): 12683–9. doi:10.1074/jbc.M411494200. PMID 15671020.
• Nishita M, Tomizawa C, Yamamoto M, et al. (2006). "Spatial and temporal regulation of cofilin activity by LIM kinase and Slingshot is critical for directional cell migration". J. Cell Biol. 171 (2): 349–59. doi:10.1083/jcb.200504029. PMC 2171197. PMID 16230460.
• Yamamoto M, Nagata-Ohashi K, Ohta Y, et al. (2006). "Identification of multiple actin-binding sites in cofilin-phosphatase Slingshot-1L". FEBS Lett. 580 (7): 1789–94. doi:10.1016/j.febslet.2006.02.034. PMID 16513117. S2CID 27347823.
• Cai L, Marshall TW, Uetrecht AC, et al. (2007). "Coronin 1B coordinates Arp2/3 complex and cofilin activities at the leading edge". Cell. 128 (5): 915–29. doi:10.1016/j.cell.2007.01.031. PMC 2630706. PMID 17350576.
• 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.