SSH2 (original) (raw)

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Protein-coding gene in the species Homo sapiens

SSH2
Available structuresPDBOrtholog search: PDBe RCSB List of PDB id codes2NT2
Identifiers
Aliases	SSH2, SSH-2, SSH-2L, slingshot protein phosphatase 2
External IDs	OMIM: 606779; MGI: 2679255; HomoloGene: 14116; GeneCards: SSH2; OMA:SSH2 - orthologs
Gene location (Human)Chr.Chromosome 17 (human)[1]Band17q11.2Start29,625,938 bp[1]End29,930,276 bp[1]
Gene location (Mouse)Chr.Chromosome 11 (mouse)[2]Band11|11 B5Start77,107,113 bp[2]End77,351,046 bp[2]
RNA expression patternBgeeHuman Mouse (ortholog)Top expressed intibialis anterior muscledeltoid musclecardiac muscle tissue of right atriumbloodSkeletal muscle tissue of rectus abdominisgastrocnemius musclequadriceps femoris muscleSkeletal muscle tissue of biceps brachiivastus lateralis musclewhite blood cellTop expressed inspermatocyteextraocular muscledigastric muscletemporal musclesternocleidomastoid muscleinterventricular septumsoleus musclevastus lateralis muscletriceps brachii musclelymph nodeMore reference expression dataBioGPSMore reference expression data
Gene ontologyMolecular 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 space 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
OrthologsSpeciesHuman MouseEntrez85464237860EnsemblENSG00000141298ENSMUSG00000037926UniProtQ76I76Q5SW75RefSeq (mRNA)NM_001282129NM_001282130NM_001282131NM_033389NM_001291190NM_177710RefSeq (protein)NP_001269058NP_001269059NP_001269060NP_203747NP_001278119NP_808378Location (UCSC)Chr 17: 29.63 – 29.93 MbChr 11: 77.11 – 77.35 MbPubMed search[3][4]
Wikidata
View/Edit HumanView/Edit Mouse

Protein phosphatase Slingshot homolog 2 is an enzyme that in humans is encoded by the SSH2 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]

1. ^ a b c GRCh38: Ensembl release 89: ENSG00000141298 – Ensembl, May 2017
2. ^ a b c 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. ^ a b "Entrez Gene: SSH2 slingshot homolog 2 (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.

• 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. Bibcode:2005Natur.437.1173R. 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.

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