S100A2

S100A2

Available structures

Human UniProt search: PDBe RCSB

List of PDB id codes
2RGI, 4DUQ

Identifiers

S100A2, CAN19, S100L, S100 calcium binding protein A2

External IDs

HomoloGene: 48389 GeneCards: S100A2

Gene ontology
Molecular function	• metal ion binding • calcium ion binding • identical protein binding • protein binding
Cellular component	• cellular component
Biological process	• endothelial cell migration
Sources:Amigo / QuickGO

RNA expression pattern

More reference expression data

Orthologs

Species

Human

Mouse


6273


n/a


ENSG00000196754


n/a


P29034


n/a

RefSeq (mRNA)


NM_005978


n/a

RefSeq (protein)


NP_005969.1


n/a

Location (UCSC)

Chr 1: 153.56 – 153.57 Mb

n/a

PubMed search

^[1]

n/a

View/Edit Human

S100 calcium-binding protein A2 (S100A2) is a protein that in humans is encoded by the S100A2 gene.^[2]

The protein encoded by this gene is a member of the S100 family of proteins containing 2 EF-hand calcium-binding motifs. S100 proteins are localized in the cytoplasm and/or nucleus of a wide range of cells, and involved in the regulation of a number of cellular processes such as cell cycle progression and differentiation. S100 genes include at least 13 members which are located as a cluster on chromosome 1q21. This protein may have a tumor suppressor function. Chromosomal rearrangements and altered expression of this gene have been implicated in breast cancer.^[3]

References

↑ "Human PubMed Reference:".
↑ Engelkamp D, Schafer BW, Mattei MG, Erne P, Heizmann CW (Aug 1993). "Six S100 genes are clustered on human chromosome 1q21: identification of two genes coding for the two previously unreported calcium-binding proteins S100D and S100E". Proc Natl Acad Sci U S A. 90 (14): 6547–51. doi:10.1073/pnas.90.14.6547. PMC 46969. PMID 8341667.
↑ "Entrez Gene: S100A2 S100 calcium binding protein A2".

Further reading

Schäfer BW, Heizmann CW (1996). "The S100 family of EF-hand calcium-binding proteins: functions and pathology". Trends Biochem. Sci. 21 (4): 134–40. doi:10.1016/S0968-0004(96)80167-8. PMID 8701470.
Rasmussen HH, van Damme J, Puype M, et al. (1993). "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.
Lee SW, Tomasetto C, Swisshelm K, et al. (1992). "Down-regulation of a member of the S100 gene family in mammary carcinoma cells and reexpression by azadeoxycytidine treatment". Proc. Natl. Acad. Sci. U.S.A. 89 (6): 2504–8. doi:10.1073/pnas.89.6.2504. PMC 48687. PMID 1372446.
Schäfer BW, Wicki R, Engelkamp D, et al. (1995). "Isolation of a YAC clone covering a cluster of nine S100 genes on human chromosome 1q21: rationale for a new nomenclature of the S100 calcium-binding protein family". Genomics. 25 (3): 638–43. doi:10.1016/0888-7543(95)80005-7. PMID 7759097.
Gimona M, Lando Z, Dolginov Y, et al. (1997). "Ca2+-dependent interaction of S100A2 with muscle and nonmuscle tropomyosins". J. Cell. Sci. 110 (5): 611–21. PMID 9092943.
Böni R, Burg G, Doguoglu A, et al. (1997). "Immunohistochemical localization of the Ca2+ binding S100 proteins in normal human skin and melanocytic lesions". Br. J. Dermatol. 137 (1): 39–43. doi:10.1111/j.1365-2133.1997.tb03698.x. PMID 9274623.
Groves P, Finn BE, Kuźnicki J, Forsén S (1998). "A model for target protein binding to calcium-activated S100 dimers". FEBS Lett. 421 (3): 175–9. doi:10.1016/S0014-5793(97)01535-4. PMID 9468301.
Wicki R, Franz C, Scholl FA, et al. (1998). "Repression of the candidate tumor suppressor gene S100A2 in breast cancer is mediated by site-specific hypermethylation". Cell Calcium. 22 (4): 243–54. doi:10.1016/S0143-4160(97)90063-4. PMID 9481475.
Franz C, Durussel I, Cox JA, et al. (1998). "Binding of Ca2+ and Zn2+ to human nuclear S100A2 and mutant proteins". J. Biol. Chem. 273 (30): 18826–34. doi:10.1074/jbc.273.30.18826. PMID 9668057.
Mueller A, Bächi T, Höchli M, et al. (1999). "Subcellular distribution of S100 proteins in tumor cells and their relocation in response to calcium activation". Histochem. Cell Biol. 111 (6): 453–9. doi:10.1007/s004180050381. PMID 10429967.
Stradal TB, Troxler H, Heizmann CW, Gimona M (2000). "Mapping the zinc ligands of S100A2 by site-directed mutagenesis". J. Biol. Chem. 275 (18): 13219–27. doi:10.1074/jbc.275.18.13219. PMID 10788426.
Hoyaux D, Decaestecker C, Heizmann CW, et al. (2000). "S100 proteins in Corpora amylacea from normal human brain". Brain Res. 867 (1–2): 280–8. doi:10.1016/S0006-8993(00)02393-3. PMID 10837826.
Deshpande R, Woods TL, Fu J, et al. (2000). "Biochemical characterization of S100A2 in human keratinocytes: subcellular localization, dimerization, and oxidative cross-linking". J. Invest. Dermatol. 115 (3): 477–85. doi:10.1046/j.1523-1747.2000.00078.x. PMID 10951287.
Nagy N, Hoyaux D, Gielen I, et al. (2002). "The Ca2+-binding S100A2 protein is differentially expressed in epithelial tissue of glandular or squamous origin". Histol. Histopathol. 17 (1): 123–30. PMID 11813862.
Kyriazanos ID, Tachibana M, Dhar DK, et al. (2002). "Expression and prognostic significance of S100A2 protein in squamous cell carcinoma of the esophagus". Oncol. Rep. 9 (3): 503–10. doi:10.3892/or.9.3.503. PMID 11956617.
Zhang T, Woods TL, Elder JT (2003). "Differential responses of S100A2 to oxidative stress and increased intracellular calcium in normal, immortalized, and malignant human keratinocytes". J. Invest. Dermatol. 119 (5): 1196–201. doi:10.1046/j.1523-1747.2002.19520.x. PMID 12445212.
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. doi:10.1073/pnas.242603899. PMC 139241. PMID 12477932.
Hibi K, Fujitake S, Takase T, et al. (2004). "Identification of S100A2 as a target of the DeltaNp63 oncogenic pathway". Clin. Cancer Res. 9 (11): 4282–5. PMID 14519656.

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