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SSH1 - Wikipedia

From Wikipedia, the free encyclopedia

SSH1

Identifiers

Aliases

SSH1, SSH1L, slingshot protein phosphatase 1

External IDs

OMIM: 606778; MGI: 2686240; HomoloGene: 41299; GeneCards: SSH1; OMA:SSH1 - orthologs

Gene location (Human)

Chr.	Chromosome 12 (human)^[1]

Band	12q24.11	Start	108,778,191 bp^[1]
Band	12q24.11	End	108,857,590 bp^[1]

Gene location (Mouse)

Chr.	Chromosome 5 (mouse)^[2]

Band	5\|5 F	Start	114,075,155 bp^[2]
Band	5\|5 F	End	114,131,955 bp^[2]

RNA expression pattern

Bgee

Human

Mouse (ortholog)

Top expressed in

sural nerve

stromal cell of endometrium

saphenous vein

secondary oocyte

trigeminal ganglion

lower lobe of lung

lactiferous duct

tail of epididymis

spinal ganglia

caput epididymis

Top expressed in

internal carotid artery

Rostral migratory stream

external carotid artery

sciatic nerve

substantia nigra

fossa

blood

Gonadal ridge

ciliary body

cumulus cell

More reference expression data

BioGPS


More reference expression data

Gene ontology
Molecular function	phosphoprotein phosphatase activity phosphatase activity protein binding protein tyrosine phosphatase activity actin binding hydrolase activity protein tyrosine/serine/threonine phosphatase activity
Cellular component	cytoplasm cell projection plasma 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: 114.08 – 114.13 Mb

PubMed search

^[3]

^[4]

Wikidata

View/Edit Human

View/Edit Mouse

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

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

^ ^a ^b ^c GRCh38: Ensembl release 89: ENSG00000084112 – Ensembl, May 2017
^ ^a ^b ^c GRCm38: Ensembl release 89: ENSMUSG00000042121 – Ensembl, May 2017
^ "Human PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
^ "Mouse PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
^ 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.
^ 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.
^ ^a ^b "Entrez Gene: SSH1 slingshot homolog 1 (Drosophila)".

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. Bibcode:2004PNAS..10112130B. 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.

Esterase: protein tyrosine phosphatases (EC 3.1.3.48)

Class I

Classical PTPs

Receptor type PTPs	PTPRA PTPRB PTPRC PTPRD PTPRE PTPRF PTPRG PTPRH PTPRJ PTPRK PTPRM PTPRN PTPRN2 PTPRO PTPRQ PTPRR PTPRS PTPRT PTPRU PTPRZ1 PTPRZ2
Non receptor type PTPs	PTPN1 PTPN2 PTPN3 PTPN4 PTPN5 PTPN6 PTPN7 PTPN9 PTPN11 PTPN12 PTPN13 PTPN14 PTPN18 PTPN20 PTPN21 PTPN22 PTPN23

VH1-like or
dual specific
phosphatases
(DSPs)

MAPK phosphatases (MKPs)	DUSP1 DUSP2 DUSP4 DUSP5 DUSP6 DUSP7 DUSP8 DUSP9 DUSP10 DUSP16 MK-STYX
Slingshots	SSH1 SSH2 SSH3
PRLs	PTP4A1 PTP4A2 PTP4A3
CDC14s	CDC14A CDC14B CDKN3 PTP9Q22
Atypical DSPs	DUSP3 DUSP11 DUSP12 DUSP13A DUSP13B DUSP14 DUSP15 DUSP18 DUSP19 DUSP21 DUSP22 DUSP23 DUSP24 DUSP25 DUSP26 DUSP27 EMP2A RNGTT STYX
Phosphatase and tensin homologs (PTENs)	PTEN TPIP TPTE TNS TENC1
Myotubularins	MTM1 MTMR2 MTMR3 MTMR4 MTMR5 MTMR6 MTMR7 MTMR8 MTMR9 MTMR10 MTMR11 MTMR12 MTMR13 MTMR14 MTMR15

Class II

ACP1

Class III

Cdc25
- CDC25A
- CDC25B
- CDC25C

Class IV

This article on a gene on human chromosome 12 is a stub. You can help Wikipedia by expanding it.

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References

Further reading