S100A10

From Wikipedia, the free encyclopedia


S100 calcium binding protein A10
PDB rendering based on 1a4p.
Available structures: 1a4p, 1bt6
Identifiers
Symbol(s) S100A10; 42C; ANX2L; ANX2LG; CAL1L; CLP11; Ca[1]; GP11; MGC111133; P11; p10
External IDs OMIM: 114085 MGI: 1339468 HomoloGene: 2228
RNA expression pattern

More reference expression data
Orthologs
Human Mouse
Entrez 6281 20194
Ensembl ENSG00000197747 ENSMUSG00000041959
Uniprot P60903 Q3TC45
Refseq NM_002966 (mRNA)
NP_002957 (protein)		 NM_009112 (mRNA)
NP_033138 (protein)
Location Chr 1: 150.22 - 150.23 Mb Chr 3: 93.64 - 93.65 Mb
Pubmed search [1] [2]

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]

[edit] References

  1. ^ a b Entrez Gene: S100A10 S100 calcium binding protein A10.

[edit] 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. 
 This article on a gene on chromosome 1 is a stub. You can help Wikipedia by expanding it.