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S100A11

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S100A11
Available structures
PDBHuman UniProt search: PDBe RCSB
Identifiers
AliasesS100A11, HEL-S-43, MLN70, S100C, S100 calcium binding protein A11
External IDsOMIM: 603114; MGI: 3645720; HomoloGene: 55916; GeneCards: S100A11; OMA:S100A11 - orthologs
Orthologs
SpeciesHumanMouse
Entrez
Ensembl
UniProt
RefSeq (mRNA)

NM_005620

n/a

RefSeq (protein)

NP_005611

n/a

Location (UCSC)Chr 1: 152.03 – 152.05 Mbn/a
PubMed search[2][3]
Wikidata
View/Edit HumanView/Edit Mouse

S100 calcium-binding protein A11 (S100A11) is a protein that in humans is encoded by the S100A11 gene.[4][5]

Function

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.[6] S100A11 is localized in the cytoplasm of resting human keratinocytes in vitro.[7]

S100A11, along with all 13 members of the S100 family, are located as a cluster on chromosome 1q21. The protein may function in motility, invasion, and tubulin polymerization. Chromosomal rearrangements and altered expression of this gene have been implicated in tumor metastasis.[5]

Suppression of S100A11 by small interfering RNA caused cells to apoptosis, and overexpression of S100A11 has been found to inhibit apoptosis in tumor cells.[8] Furthermore, the knock-down of S100A11 via siRNA reduces the sister-chromatid exchange and the viability of cells.

IL-8 and TNF-alpha induce S100A11 expression and release in chondrocytes in culture and exogenous S100A11 causes chondrocyte hypertrophy.[9]

It has been shown that S100A11 enhances the recombination activity of human RAD51 in vitro. A knock-down leads to diffuse distribution of RAD54B.[10] These finding suggest a potential role of S100A11 in the process of homologous recombination repair of double-strand breaks.[11]

Interactions

S100A11 has been shown to interact with Nucleolin,[12] S100B[13] and RAD54B.[10]

References

  1. ^ a b c GRCh38: Ensembl release 89: ENSG00000163191Ensembl, May 2017
  2. ^ "Human PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
  3. ^ "Mouse PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
  4. ^ Wicki R, Marenholz I, Mischke D, Schäfer BW, Heizmann CW (December 1996). "Characterization of the human S100A12 (calgranulin C, p6, CAAF1, CGRP) gene, a new member of the S100 gene cluster on chromosome 1q21". Cell Calcium. 20 (6): 459–64. doi:10.1016/S0143-4160(96)90087-1. PMID 8985590.
  5. ^ a b "Entrez Gene: S100A11 S100 calcium binding protein A11".
  6. ^ He H, Li J, Weng S, Li M, Yu Y (2009). "S100A11: diverse function and pathology corresponding to different target proteins". Cell Biochemistry and Biophysics. 55 (3): 117–26. doi:10.1007/s12013-009-9061-8. PMID 19649745.
  7. ^ Sakaguchi M, Huh NH (October 2011). "S100A11, a dual growth regulator of epidermal keratinocytes". Amino Acids. 41 (4): 797–807. doi:10.1007/s00726-010-0747-4. PMID 20872027.
  8. ^ Kanamori T, Takakura K, Mandai M, Kariya M, Fukuhara K, Sakaguchi M, Huh NH, Saito K, Sakurai T, Fujita J, Fujii S (October 2004). "Increased expression of calcium-binding protein S100 in human uterine smooth muscle tumours". Molecular Human Reproduction. 10 (10): 735–42. doi:10.1093/molehr/gah100. PMID 15322223.
  9. ^ Cecil DL, Johnson K, Rediske J, Lotz M, Schmidt AM, Terkeltaub R (December 2005). "Inflammation-induced chondrocyte hypertrophy is driven by receptor for advanced glycation end products". Journal of Immunology. 175 (12): 8296–302. doi:10.4049/jimmunol.175.12.8296. PMID 16339570.
  10. ^ a b Murzik U, Hemmerich P, Weidtkamp-Peters S, Ulbricht T, Bussen W, Hentschel J, von Eggeling F, Melle C (July 2008). "Rad54B targeting to DNA double-strand break repair sites requires complex formation with S100A11". Molecular Biology of the Cell. 19 (7): 2926–35. doi:10.1091/mbc.e07-11-1167. PMC 2441681. PMID 18463164.
  11. ^ Foertsch F, Szambowska A, Weise A, Zielinski A, Schlott B, Kraft F, Mrasek K, Borgmann K, Pospiech H, Grosse F, Melle C (October 2016). "S100A11 plays a role in homologous recombination and genome maintenance by influencing the persistence of RAD51 in DNA repair foci". Cell Cycle. 15 (20): 2766–79. doi:10.1080/15384101.2016.1220457. PMC 5053559. PMID 27590262.
  12. ^ Sakaguchi M, Miyazaki M, Takaishi M, Sakaguchi Y, Makino E, Kataoka N, Yamada H, Namba M, Huh NH (November 2003). "S100C/A11 is a key mediator of Ca(2+)-induced growth inhibition of human epidermal keratinocytes". The Journal of Cell Biology. 163 (4): 825–35. doi:10.1083/jcb.200304017. PMC 2173690. PMID 14623863.
  13. ^ Deloulme JC, Assard N, Mbele GO, Mangin C, Kuwano R, Baudier J (November 2000). "S100A6 and S100A11 are specific targets of the calcium- and zinc-binding S100B protein in vivo". The Journal of Biological Chemistry. 275 (45): 35302–10. doi:10.1074/jbc.M003943200. PMID 10913138.{{cite journal}}: CS1 maint: unflagged free DOI (link)

Further reading