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 location (Human)

Chr.	Chromosome 1 (human)^[1]

Band	No data available	Start	153,561,108 bp^[1]
Band	No data available	End	153,567,890 bp^[1]

RNA expression pattern

More reference expression data

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

Orthologs

Species

Human

Mouse


6273


n/a


ENSG00000196754


n/a


P29034


n/a

RefSeq (mRNA)


NM_005978


n/a

RefSeq (protein)


NP_005969


n/a

Location (UCSC)

Chr 1: 153.56 – 153.57 Mb

n/a

PubMed search

^[2]

n/a

View/Edit Human

S100 calcium-binding protein A2 (S100A2) is a protein that in humans is encoded by the S100A2 gene.^[3]

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.^[4]

References

1 2 3 GRCh38: Ensembl release 89: ENSG00000196754 - Ensembl, May 2017
↑ "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. PMC 46969 . PMID 8341667. doi:10.1073/pnas.90.14.6547.
↑ "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. PMID 8701470. doi:10.1016/S0968-0004(96)80167-8.
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. PMID 1286667. doi:10.1002/elps.11501301199.
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. PMC 48687 . PMID 1372446. doi:10.1073/pnas.89.6.2504.
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. PMID 7759097. doi:10.1016/0888-7543(95)80005-7.
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. PMID 9274623. doi:10.1111/j.1365-2133.1997.tb03698.x.
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. PMID 9468301. doi:10.1016/S0014-5793(97)01535-4.
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. PMID 9481475. doi:10.1016/S0143-4160(97)90063-4.
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. PMID 9668057. doi:10.1074/jbc.273.30.18826.
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. PMID 10429967. doi:10.1007/s004180050381.
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. PMID 10788426. doi:10.1074/jbc.275.18.13219.
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. PMID 10837826. doi:10.1016/S0006-8993(00)02393-3.
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. PMID 10951287. doi:10.1046/j.1523-1747.2000.00078.x.
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. PMID 11956617. doi:10.3892/or.9.3.503.
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. PMID 12445212. doi:10.1046/j.1523-1747.2002.19520.x.
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. PMC 139241 . PMID 12477932. doi:10.1073/pnas.242603899.
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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