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Gene Review

S100A5  -  S100 calcium binding protein A5

Homo sapiens

Synonyms: Protein S-100D, Protein S100-A5, S100 calcium-binding protein A5, S100D
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Disease relevance of S100A5


High impact information on S100A5

  • The product of S100E is cysteine-rich, whereas that of S100D contains a long hydrophobic N-terminal tail [3].
  • 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 [3].
  • While the S100A5 protein was significantly expressed in all the astrocytic tumors (but without any significant modifications in the levels of malignancy), the S100A2 protein was never expressed in these tumors [4].
  • Flow dialysis revealed that the homodimeric S100A5 binds four Ca(2+) ions with strong positive cooperativity and an affinity 20-100-fold higher than the other S100 proteins studied under identical conditions [5].
  • S100A5 also binds two Zn(2+) ions and four Cu(2+) ions per dimer [5].

Biological context of S100A5

  • S100A5 is a novel member of the EF-hand superfamily of calcium-binding proteins that is poorly characterized at the protein level [5].
  • The potential role of S100A5 in copper homeostasis is discussed [5].

Anatomical context of S100A5


Associations of S100A5 with chemical compounds

  • Here we characterized the human recombinant S100A5, especially its interaction with Ca(2+), Zn(2+), and Cu(2+) [5].
  • Thus, it was suggested that S100A5 protein plays an inherent functional role to the post-thick ascending limb of Henle portion in the nephron [2].
  • Then, total RNA was extracted by phenol/chloroform from 1 ml urine of healthy volunteers, and S100A5 was amplified by RT-PCR from all samples (n = 12), indicating that the transcript of S100A5 is detectable even in the cells released into urine [2].

Other interactions of S100A5

  • S100A3 and S100A6 and, to a lesser extent, S100A5 were the most differentially expressed proteins across the different histopathological groups analysed [9].
  • First we identified the cDNA sequences of mouse S100A1, S100A3 and S100A5 [10].
  • In contrast, S100A5 and S100A12 were not significantly expressed in any of the tumor tissues tested [11].
  • Using 63 meningiomas (39 benign and 24 atypical), we performed a semi-quantitative histochemical analysis of both the expression of galectin-3 and its ligand profile and the Ca2+-binding proteins S100A5, S100A6 and S100B [12].
  • In sharp contrast, the levels of expression of the S100A3 and S100A5 proteins differed markedly in the solid tumour tissue in relation to the astrocytic tumour types and grades [13].


  1. S100A5: a marker of recurrence in WHO grade I meningiomas. Hancq, S., Salmon, I., Brotchi, J., De Witte, O., Gabius, H.J., Heizmann, C.W., Kiss, R., Decaestecker, C. Neuropathol. Appl. Neurobiol. (2004) [Pubmed]
  2. Restricted expression of calcium-binding protein S100A5 in human kidney. Teratani, T., Watanabe, T., Yamahara, K., Kumagai, H., Ishikawa, A., Arai, K., Nozawa, R. Biochem. Biophys. Res. Commun. (2002) [Pubmed]
  3. 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. Engelkamp, D., Schäfer, B.W., Mattei, M.G., Erne, P., Heizmann, C.W. Proc. Natl. Acad. Sci. U.S.A. (1993) [Pubmed]
  4. Supratentorial pilocytic astrocytomas, astrocytomas, anaplastic astrocytomas and glioblastomas are characterized by a differential expression of S100 proteins. Camby, I., Nagy, N., Lopes, M.B., Schäfer, B.W., Maurage, C.A., Ruchoux, M.M., Murmann, P., Pochet, R., Heizmann, C.W., Brotchi, J., Salmon, I., Kiss, R., Decaestecker, C. Brain Pathol. (1999) [Pubmed]
  5. Brain S100A5 is a novel calcium-, zinc-, and copper ion-binding protein of the EF-hand superfamily. Schäfer, B.W., Fritschy, J.M., Murmann, P., Troxler, H., Durussel, I., Heizmann, C.W., Cox, J.A. J. Biol. Chem. (2000) [Pubmed]
  6. Differential expression of S100 proteins in the developing human hippocampus and temporal cortex. Chan, W.Y., Xia, C.L., Dong, D.C., Heizmann, C.W., Yew, D.T. Microsc. Res. Tech. (2003) [Pubmed]
  7. Immunolocalization of the calcium binding S100A1, S100A5 and S100A6 proteins in the dog cochlea during postnatal development. Coppens, A.G., Kiss, R., Heizmann, C.W., Schäfer, B.W., Poncelet, L. Brain Res. Dev. Brain Res. (2001) [Pubmed]
  8. S100+ cell response to squamous cell carcinoma of the lip: inverse correlation with metastasis. Wei, N., Tahan, S.R. J. Cutan. Pathol. (1998) [Pubmed]
  9. Differential expression of S100 calcium-binding proteins in epidermoid cysts, branchial cysts, craniopharyngiomas and cholesteatomas. Pelc, P., Vanmuylder, N., Lefranc, F., Heizmann, C.W., Hassid, S., Salmon, I., Kiss, R., Louryan, S., Decaestecker, C. Histopathology (2003) [Pubmed]
  10. Clustered organization of S100 genes in human and mouse. Ridinger, K., Ilg, E.C., Niggli, F.K., Heizmann, C.W., Schäfer, B.W. Biochim. Biophys. Acta (1998) [Pubmed]
  11. Expression analysis of S100 proteins and RAGE in human tumors using tissue microarrays. Hsieh, H.L., Schäfer, B.W., Sasaki, N., Heizmann, C.W. Biochem. Biophys. Res. Commun. (2003) [Pubmed]
  12. Detection of S100B, S100A6 and galectin-3 ligands in meningiomas as markers of aggressiveness. Hancq, S., Salmon, I., Brotchi, J., Gabius, H.J., Heizmann, C.W., Kiss, R., Decaestecker, C. Int. J. Oncol. (2004) [Pubmed]
  13. Differential expression of S100 calcium-binding proteins characterizes distinct clinical entities in both WHO grade II and III astrocytic tumours. Camby, I., Lefranc, F., Titeca, G., Neuci, S., Fastrez, M., Dedecken, L., Schäfer, B.W., Brotchi, J., Heizmann, C.W., Pochet, R., Salmon, I., Kiss, R., Decaestecker, C. Neuropathol. Appl. Neurobiol. (2000) [Pubmed]
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