S100A10

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S100 calcium binding protein A10
File:PBB Protein S100A10 image.jpg
PDB rendering based on 1a4p.
Available structures
PDB Ortholog search: Template:Homologene2PDBe PDBe, Template:Homologene2uniprot RCSB
Identifiers
Symbols S100A10 ; 42C; ANX2L; ANX2LG; CAL1L; CLP11; Ca[1]; GP11; MGC111133; P11; p10
External IDs Template:OMIM5 Template:MGI HomoloGene: 2228
RNA expression pattern
File:PBB GE S100A10 200872 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 A10, also known as S100A10, 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 exocytosis and endocytosis.[1]

References

  1. ↑ 1.0 1.1 "Entrez Gene: S100A10 S100 calcium binding protein A10".

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.
  • Kwon M, MacLeod TJ, Zhang Y, Waisman DM (2006). "S100A10, annexin A2, and annexin a2 heterotetramer as candidate plasminogen receptors". Front. Biosci. 10: 300–25. PMID 15574370.
  • Dooley TP, Weiland KL, Simon M (1992). "cDNA sequence of human p11 calpactin I light chain". Genomics. 13 (3): 866–8. PMID 1386341.
  • Creutz CE, Moss S, Edwardson JM; et al. (1992). "Differential recognition of secretory vesicles by annexins. European Molecular Biology Organization Course "Advanced Techniques for Studying Secretion"". Biochem. Biophys. Res. Commun. 184 (1): 347–52. PMID 1533123.
  • Harder T, Kube E, Gerke V (1992). "Cloning and characterization of the human gene encoding p11: structural similarity to other members of the S-100 gene family". Gene. 113 (2): 269–74. PMID 1533380.
  • Kube E, Weber K, Gerke V (1991). "Primary structure of human, chicken, and Xenopus laevis p11, a cellular ligand of the Src-kinase substrate, annexin II". Gene. 102 (2): 255–9. PMID 1831433.
  • Becker T, Weber K, Johnsson N (1991). "Protein-protein recognition via short amphiphilic helices; a mutational analysis of the binding site of annexin II for p11". EMBO J. 9 (13): 4207–13. PMID 2148288.
  • 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.
  • Kato S, Sekine S, Oh SW; et al. (1995). "Construction of a human full-length cDNA bank". Gene. 150 (2): 243–50. PMID 7821789.
  • Volz A, Korge BP, Compton JG; et al. (1994). "Physical mapping of a functional cluster of epidermal differentiation genes on chromosome 1q21". Genomics. 18 (1): 92–9. doi:10.1006/geno.1993.1430. PMID 8276421.
  • 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.
  • Jost M, Gerke V (1996). "Mapping of a regulatory important site for protein kinase C phosphorylation in the N-terminal domain of annexin II". Biochim. Biophys. Acta. 1313 (3): 283–9. PMID 8898866.
  • Munz B, Gerke V, Gillitzer R, Werner S (1997). "Differential expression of the calpactin I subunits annexin II and p11 in cultured keratinocytes and during wound repair". J. Invest. Dermatol. 108 (3): 307–12. PMID 9036930.
  • Kang HM, Kassam G, Jarvis SE; et al. (1997). "Characterization of human recombinant annexin II tetramer purified from bacteria: role of N-terminal acetylation". Biochemistry. 36 (8): 2041–50. doi:10.1021/bi962569b. PMID 9047302.
  • Wu T, Angus CW, Yao XL; et al. (1997). "P11, a unique member of the S100 family of calcium-binding proteins, interacts with and inhibits the activity of the 85-kDa cytosolic phospholipase A2". J. Biol. Chem. 272 (27): 17145–53. PMID 9202034.
  • Hsu SY, Kaipia A, Zhu L, Hsueh AJ (1997). "Interference of BAD (Bcl-xL/Bcl-2-associated death promoter)-induced apoptosis in mammalian cells by 14-3-3 isoforms and P11". Mol. Endocrinol. 11 (12): 1858–67. PMID 9369453.
  • Réty S, Sopkova J, Renouard M; et al. (1999). "The crystal structure of a complex of p11 with the annexin II N-terminal peptide". Nat. Struct. Biol. 6 (1): 89–95. doi:10.1038/4965. PMID 9886297.
  • Ramalingam R, Rafii S, Worgall S; et al. (1999). "Induction of endogenous genes following infection of human endothelial cells with an E1(-) E4(+) adenovirus gene transfer vector". J. Virol. 73 (12): 10183–90. PMID 10559334.
  • Mai J, Finley RL, Waisman DM, Sloane BF (2000). "Human procathepsin B interacts with the annexin II tetramer on the surface of tumor cells". J. Biol. Chem. 275 (17): 12806–12. PMID 10777578.

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