S100A1

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S100 calcium binding protein A1
File:PBB Protein S100A1 image.jpg
PDB rendering based on 1k2h.
Available structures
PDB Ortholog search: Template:Homologene2PDBe PDBe, Template:Homologene2uniprot RCSB
Identifiers
Symbols S100A1 ; S100; S100-alpha; S100A
External IDs Template:OMIM5 Template:MGI HomoloGene: 4566
RNA expression pattern
File:PBB GE S100A1 205334 at tn.png
More reference expression data
Orthologs
Template:GNF Ortholog box
Species Human Mouse
Entrez n/a n/a
Ensembl n/a n/a
UniProt n/a n/a
RefSeq (mRNA) n/a n/a
RefSeq (protein) n/a n/a
Location (UCSC) n/a n/a
PubMed search n/a n/a

S100 calcium binding protein A1, also known as S100A1, is a human gene.[1]

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 function in stimulation of Ca2+-induced Ca2+ release, inhibition of microtubule assembly, and inhibition of protein kinase C-mediated phosphorylation. Reduced expression of this protein has been implicated in cardiomyopathies.[1]

References

  1. ↑ 1.0 1.1 "Entrez Gene: S100A1 S100 calcium binding protein A1".

Further reading

  • Zimmer DB, Cornwall EH, Landar A, Song W (1995). "The S100 protein family: history, function, and expression". Brain Res. Bull. 37 (4): 417–29. PMID 7620916.
  • 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.
  • Garbuglia M, Verzini M, Sorci G; et al. (2000). "The calcium-modulated proteins, S100A1 and S100B, as potential regulators of the dynamics of type III intermediate filaments". Braz. J. Med. Biol. Res. 32 (10): 1177–85. PMID 10510252.
  • Engelkamp D, Schäfer BW, Erne P, Heizmann CW (1992). "S100 alpha, CAPL, and CACY: molecular cloning and expression analysis of three calcium-binding proteins from human heart". Biochemistry. 31 (42): 10258–64. PMID 1384693.
  • Morii K, Tanaka R, Takahashi Y; et al. (1991). "Structure and chromosome assignment of human S100 alpha and beta subunit genes". Biochem. Biophys. Res. Commun. 175 (1): 185–91. PMID 1998503.
  • Baudier J, Glasser N, Gerard D (1986). "Ions binding to S100 proteins. I. Calcium- and zinc-binding properties of bovine brain S100 alpha alpha, S100a (alpha beta), and S100b (beta beta) protein: Zn2+ regulates Ca2+ binding on S100b protein". J. Biol. Chem. 261 (18): 8192–203. PMID 3722149.
  • Kato K, Kimura S (1985). "S100ao (alpha alpha) protein is mainly located in the heart and striated muscles". Biochim. Biophys. Acta. 842 (2–3): 146–50. PMID 4052452.
  • 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.
  • Engelkamp D, Schäfer BW, Mattei MG; et al. (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. PMID 8341667.
  • Garbuglia M, Verzini M, Giambanco I; et al. (1996). "Effects of calcium-binding proteins (S-100a(o), S-100a, S-100b) on desmin assembly in vitro". FASEB J. 10 (2): 317–24. PMID 8641565.
  • Landar A, Caddell G, Chessher J, Zimmer DB (1997). "Identification of an S100A1/S100B target protein: phosphoglucomutase". Cell Calcium. 20 (3): 279–85. PMID 8894274.
  • Remppis A, Greten T, Schäfer BW; et al. (1996). "Altered expression of the Ca(2+)-binding protein S100A1 in human cardiomyopathy". Biochim. Biophys. Acta. 1313 (3): 253–7. PMID 8898862.
  • Treves S, Scutari E, Robert M; et al. (1997). "Interaction of S100A1 with the Ca2+ release channel (ryanodine receptor) of skeletal muscle". Biochemistry. 36 (38): 11496–503. doi:10.1021/bi970160w. PMID 9298970.
  • 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.
  • Mandinova A, Atar D, Schäfer BW; et al. (1998). "Distinct subcellular localization of calcium binding S100 proteins in human smooth muscle cells and their relocation in response to rises in intracellular calcium". J. Cell. Sci. 111 ( Pt 14): 2043–54. PMID 9645951.
  • Osterloh D, Ivanenkov VV, Gerke V (1999). "Hydrophobic residues in the C-terminal region of S100A1 are essential for target protein binding but not for dimerization". Cell Calcium. 24 (2): 137–51. PMID 9803314.
  • Garbuglia M, Verzini M, Donato R (1999). "Annexin VI binds S100A1 and S100B and blocks the ability of S100A1 and S100B to inhibit desmin and GFAP assemblies into intermediate filaments". Cell Calcium. 24 (3): 177–91. PMID 9883272.
  • Ridinger K, Ilg EC, Niggli FK; et al. (1999). "Clustered organization of S100 genes in human and mouse". Biochim. Biophys. Acta. 1448 (2): 254–63. PMID 9920416.

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