Stratifin

Stratifin (also known as 14-3-3 protein sigma or 14-3-3σ protein) is a protein encoded by the SFN gene in humans.^[5][6] The protein is named for its presence in stratified epithelial cells.^[5]

SFN
Available structures PDB Ortholog search: PDBe RCSB List of PDB id codes 1YWT, 1YZ5, 3IQJ, 3IQU, 3IQV, 3LW1, 3MHR, 3O8I, 3P1N, 3P1O, 3P1P, 3P1Q, 3P1R, 3P1S, 3SMK, 3SML, 3SMM, 3SMN, 3SMO, 3SPR, 3T0L, 3T0M, 3U9X, 3UX0, 4DAT, 4DAU, 4DHM, 4DHN, 4DHO, 4DHP, 4DHQ, 4DHR, 4DHS, 4DHT, 4DHU, 4FL5, 4FR3, 4HQW, 4HRU, 4IEA, 4JC3, 4JDD, 4QLI, 5HF3, 4Y5I, 4Y32, 4Y3B, 3SP5
Identifiers
Aliases	SFN, YWHAS, Stratifin
External IDs	OMIM: 601290 MGI: 1891831 HomoloGene: 4475 GeneCards: SFN
Gene location (Human) Chr. Chromosome 1 (human)^[1] Band 1p36.11 Start 26,863,149 bp^[1] End 26,864,456 bp^[1]
Gene location (Mouse) Chr. Chromosome 4 (mouse)^[2] Band 4 D2.3|4 66.25 cM Start 133,327,867 bp^[2] End 133,329,479 bp^[2]
RNA expression pattern Bgee Human Mouse (ortholog) Top expressed in hair follicle nipple vulva human penis oral cavity body of tongue periodontal fiber pancreatic ductal cell amniotic fluid palpebral conjunctiva Top expressed in lip esophagus morula skin of abdomen skin of back intestinal villus cervix epidermis duodenum stomach More reference expression data BioGPS More reference expression data
Gene ontology Molecular function protein domain specific binding phosphoprotein binding protein binding protein kinase binding protein kinase C inhibitor activity identical protein binding cadherin binding Cellular component extracellular region extracellular exosome cytoplasmic vesicle membrane nucleus mitochondrion extracellular space cytoplasm cytosol Biological process regulation of cyclin-dependent protein serine/threonine kinase activity negative regulation of cysteine-type endopeptidase activity involved in apoptotic process negative regulation of keratinocyte proliferation negative regulation of protein kinase activity establishment of skin barrier keratinization keratinocyte differentiation regulation of cell cycle positive regulation of protein export from nucleus positive regulation of protein insertion into mitochondrial membrane involved in apoptotic signaling pathway keratinocyte development positive regulation of cell growth regulation of epidermal cell division intrinsic apoptotic signaling pathway in response to DNA damage membrane organization positive regulation of epidermal cell differentiation signal transduction release of cytochrome c from mitochondria skin development negative regulation of protein serine/threonine kinase activity DNA damage response, signal transduction by p53 class mediator resulting in cell cycle arrest Sources:Amigo / QuickGO
Orthologs Species Human Mouse Entrez 2810 55948 Ensembl ENSG00000175793 ENSMUSG00000047281 UniProt P31947 O70456 RefSeq (mRNA) NM_006142 NM_018754 RefSeq (protein) NP_006133 NP_061224 Location (UCSC) Chr 1: 26.86 – 26.86 Mb Chr 4: 133.33 – 133.33 Mb PubMed search ^[3] ^[4]
Wikidata
View/Edit Human View/Edit Mouse

Interactions

Stratifin has been shown to interact with PLK4,^[7] ERRFI1,^[8] MARK3,^[7][8] JUB^[8] and YWHAG.^[8]

References

1. GRCh38: Ensembl release 89: ENSG00000175793 - Ensembl, May 2017
2. GRCm38: Ensembl release 89: ENSMUSG00000047281 - 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. Leffers H, Madsen P, Rasmussen HH, Honoré B, Andersen AH, Walbum E, Vandekerckhove J, Celis JE (June 1993). "Molecular cloning and expression of the transformation sensitive epithelial marker stratifin. A member of a protein family that has been involved in the protein kinase C signalling pathway". Journal of Molecular Biology. 231 (4): 982–98. doi:10.1006/jmbi.1993.1346. PMID 8515476.
6. "Entrez Gene: SFN stratifin".
7. Rual JF, Venkatesan K, Hao T, Hirozane-Kishikawa T, Dricot A, Li N, et al. (October 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.
8. Benzinger A, Muster N, Koch HB, Yates JR, Hermeking H (June 2005). "Targeted proteomic analysis of 14-3-3 sigma, a p53 effector commonly silenced in cancer". Molecular & Cellular Proteomics. 4 (6): 785–95. doi:10.1074/mcp.M500021-MCP200. PMID 15778465.

Further reading

• Hermeking H (January 2005). "Extracellular 14-3-3sigma protein: a potential mediator of epithelial-mesenchymal interactions". The Journal of Investigative Dermatology. 124 (1): ix–x. doi:10.1111/j.0022-202X.2004.23534.x. PMID 15654940.
• Mhawech P (April 2005). "14-3-3 proteins--an update". Cell Research. 15 (4): 228–36. doi:10.1038/sj.cr.7290291. PMID 15857577.
• Lodygin D, Hermeking H (April 2005). "The role of epigenetic inactivation of 14-3-3sigma in human cancer". Cell Research. 15 (4): 237–46. doi:10.1038/sj.cr.7290292. PMID 15857578.
• Rasmussen HH, van Damme J, Puype M, Gesser B, Celis JE, Vandekerckhove J (December 1992). "Microsequences of 145 proteins recorded in the two-dimensional gel protein database of normal human epidermal keratinocytes". Electrophoresis. 13 (12): 960–9. doi:10.1002/elps.11501301199. PMID 1286667. S2CID 41855774.
• Prasad GL, Valverius EM, McDuffie E, Cooper HL (August 1992). "Complementary DNA cloning of a novel epithelial cell marker protein, HME1, that may be down-regulated in neoplastic mammary cells". Cell Growth & Differentiation. 3 (8): 507–13. PMID 1390337.
• Hermeking H, Lengauer C, Polyak K, He TC, Zhang L, Thiagalingam S, Kinzler KW, Vogelstein B (December 1997). "14-3-3sigma is a p53-regulated inhibitor of G2/M progression". Molecular Cell. 1 (1): 3–11. doi:10.1016/S1097-2765(00)80002-7. PMID 9659898.
• Chan TA, Hermeking H, Lengauer C, Kinzler KW, Vogelstein B (October 1999). "14-3-3Sigma is required to prevent mitotic catastrophe after DNA damage". Nature. 401 (6753): 616–20. Bibcode:1999Natur.401..616C. doi:10.1038/44188. PMID 10524633. S2CID 4413753.
• Laronga C, Yang HY, Neal C, Lee MH (July 2000). "Association of the cyclin-dependent kinases and 14-3-3 sigma negatively regulates cell cycle progression". The Journal of Biological Chemistry. 275 (30): 23106–12. doi:10.1074/jbc.M905616199. PMID 10767298.
• Samuel T, Weber HO, Rauch P, Verdoodt B, Eppel JT, McShea A, Hermeking H, Funk JO (November 2001). "The G2/M regulator 14-3-3sigma prevents apoptosis through sequestration of Bax". The Journal of Biological Chemistry. 276 (48): 45201–6. doi:10.1074/jbc.M106427200. PMID 11574543.
• Johnson BA, Stehn JR, Yaffe MB, Blackwell TK (May 2002). "Cytoplasmic localization of tristetraprolin involves 14-3-3-dependent and -independent mechanisms". The Journal of Biological Chemistry. 277 (20): 18029–36. doi:10.1074/jbc.M110465200. PMID 11886850.
• Tian H, Faje AT, Lee SL, Jorgensen TJ (2002). "Radiation-induced phosphorylation of Chk1 at S345 is associated with p53-dependent cell cycle arrest pathways". Neoplasia. 4 (2): 171–80. doi:10.1038/sj.neo.7900219. PMC 1550321. PMID 11896572.
• Ku NO, Michie S, Resurreccion EZ, Broome RL, Omary MB (April 2002). "Keratin binding to 14-3-3 proteins modulates keratin filaments and hepatocyte mitotic progression". Proceedings of the National Academy of Sciences of the United States of America. 99 (7): 4373–8. Bibcode:2002PNAS...99.4373K. doi:10.1073/pnas.072624299. PMC 123655. PMID 11917136.
• Urano T, Saito T, Tsukui T, Fujita M, Hosoi T, Muramatsu M, Ouchi Y, Inoue S (June 2002). "Efp targets 14-3-3 sigma for proteolysis and promotes breast tumour growth". Nature. 417 (6891): 871–5. Bibcode:2002Natur.417..871U. doi:10.1038/nature00826. PMID 12075357. S2CID 4348545.
• Liu MY, Cai S, Espejo A, Bedford MT, Walker CL (November 2002). "14-3-3 interacts with the tumor suppressor tuberin at Akt phosphorylation site(s)". Cancer Research. 62 (22): 6475–80. PMID 12438239.
• Bhatia K, Siraj AK, Hussain A, Bu R, Gutiérrez MI (February 2003). "The tumor suppressor gene 14-3-3 sigma is commonly methylated in normal and malignant lymphoid cells". Cancer Epidemiology, Biomarkers & Prevention. 12 (2): 165–9. PMID 12582028.
• Kino T, Souvatzoglou E, De Martino MU, Tsopanomihalu M, Wan Y, Chrousos GP (July 2003). "Protein 14-3-3sigma interacts with and favors cytoplasmic subcellular localization of the glucocorticoid receptor, acting as a negative regulator of the glucocorticoid signaling pathway". The Journal of Biological Chemistry. 278 (28): 25651–6. doi:10.1074/jbc.M302818200. PMID 12730237.
• Nakajima T, Shimooka H, Weixa P, Segawa A, Motegi A, Jian Z, Masuda N, Ide M, Sano T, Oyama T, Tsukagoshi H, Hamanaka K, Maeda M (June 2003). "Immunohistochemical demonstration of 14-3-3 sigma protein in normal human tissues and lung cancers, and the preponderance of its strong expression in epithelial cells of squamous cell lineage". Pathology International. 53 (6): 353–60. doi:10.1046/j.1440-1827.2003.01481.x. PMID 12787309. S2CID 24822056.
• Rishi AK, Zhang L, Boyanapalli M, Wali A, Mohammad RM, Yu Y, Fontana JA, Hatfield JS, Dawson MI, Majumdar AP, Reichert U (August 2003). "Identification and characterization of a cell cycle and apoptosis regulatory protein-1 as a novel mediator of apoptosis signaling by retinoid CD437". The Journal of Biological Chemistry. 278 (35): 33422–35. doi:10.1074/jbc.M303173200. PMID 12816952.