SSH2

Protein-coding gene in the species Homo sapiens
SSH2
Available structures
PDBOrtholog search: PDBe RCSB
List of PDB id codes

2NT2

Identifiers
AliasesSSH2, SSH-2, SSH-2L, slingshot protein phosphatase 2
External IDsOMIM: 606779; MGI: 2679255; HomoloGene: 14116; GeneCards: SSH2; OMA:SSH2 - orthologs
Gene location (Human)
Chromosome 17 (human)
Chr.Chromosome 17 (human)[1]
Chromosome 17 (human)
Genomic location for SSH2
Genomic location for SSH2
Band17q11.2Start29,625,938 bp[1]
End29,930,276 bp[1]
Gene location (Mouse)
Chromosome 11 (mouse)
Chr.Chromosome 11 (mouse)[2]
Chromosome 11 (mouse)
Genomic location for SSH2
Genomic location for SSH2
Band11|11 B5Start77,107,113 bp[2]
End77,351,046 bp[2]
RNA expression pattern
Bgee
HumanMouse (ortholog)
Top expressed in
  • tibialis anterior muscle

  • deltoid muscle

  • cardiac muscle tissue of right atrium

  • blood

  • Skeletal muscle tissue of rectus abdominis

  • gastrocnemius muscle

  • quadriceps femoris muscle

  • Skeletal muscle tissue of biceps brachii

  • vastus lateralis muscle

  • white blood cell
Top expressed in
  • spermatocyte

  • extraocular muscle

  • digastric muscle

  • temporal muscle

  • sternocleidomastoid muscle

  • interventricular septum

  • soleus muscle

  • vastus lateralis muscle

  • triceps brachii muscle

  • lymph node
More reference expression data
BioGPS
More reference expression data
Gene ontology
Molecular 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
Orthologs
SpeciesHumanMouse
Entrez

85464

237860

Ensembl

ENSG00000141298

ENSMUSG00000037926

UniProt

Q76I76

Q5SW75

RefSeq (mRNA)

NM_001282129
NM_001282130
NM_001282131
NM_033389

NM_001291190
NM_177710

RefSeq (protein)

NP_001269058
NP_001269059
NP_001269060
NP_203747

NP_001278119
NP_808378

Location (UCSC)Chr 17: 29.63 – 29.93 MbChr 11: 77.11 – 77.35 Mb
PubMed 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]

References

  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)".

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.
  • 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.

External links

  • Overview of all the structural information available in the PDB for UniProt: Q76I76 (Protein phosphatase Slingshot homolog 2) at the PDBe-KB.
  • v
  • t
  • e
  • 2nt2: Crystal Structure of Slingshot phosphatase 2
    2nt2: Crystal Structure of Slingshot phosphatase 2
  • v
  • t
  • e
Class I
Classical PTPs
Receptor type PTPs
Non receptor type PTPs
VH1-like or
dual specific
phosphatases
(DSPs)
MAPK phosphatases (MKPs)
Slingshots
PRLs
CDC14s
Atypical DSPs
Phosphatase and tensin
homologs (PTENs)
Myotubularins
Class II
Class III
Class IV


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