S100A1

From Wikipedia, the free encyclopedia

S100 calcium binding protein A1

PDB rendering based on 1k2h.

Available structures: 1k2h, 1zfs

Identifiers

Symbol(s)

S100A1; S100; S100-alpha; S100A

External IDs

OMIM: 176940 MGI: 1338917 HomoloGene: 4566

Gene ontology
Molecular Function:	• calcium ion binding • zinc ion binding • protein homodimerization activity • S100 beta binding • S100 alpha binding • ATPase binding
Cellular Component:	• sarcoplasmic reticulum • protein complex
Biological Process:	• intracellular signaling cascade • regulation of heart contraction

RNA expression pattern

More reference expression data

Orthologs

Human

Mouse

Refseq

NM_006271 (mRNA)
NP_006262 (protein)

NM_011309 (mRNA)
NP_035439 (protein)

Location

Chr 1: 151.87 - 151.87 Mb

Chr 3: 90.6 - 90.6 Mb

Pubmed search

[1]

[2]

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]

[edit] References

^ ^a ^b Entrez Gene: S100A1 S100 calcium binding protein A1.

[edit] 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.