S100A6

S100A6
Available structures
PDB	Ortholog search: PDBe RCSB
List of PDB id codes
	1K8U, 1K96, 1K9K, 1K9P, 2M1K, 4YBH
Identifiers
Aliases	S100A6 , 2A9, 5B10, CABP, CACY, PRA, S100 calcium binding protein A6, S10A6
External IDs	OMIM: 114110 MGI: 1339467 HomoloGene: 7925 GeneCards: S100A6
Gene location (Human)
Chr.	Chromosome 1 (human)
End	153,536,244 bp
Gene location (Mouse)
Chr.	Chromosome 3 (mouse)
End	90,531,488 bp
RNA expression pattern
	Top expressed in
	Achilles tendon; ; ascending aorta; ; upper lobe of left lung; ; right coronary artery; ; left coronary artery; ; right lung; ; tibial nerve; ; popliteal artery; ; rectum; ; gallbladder;
	Top expressed in
	corneal stroma; ; left colon; ; belly cord; ; mucous cell of stomach; ; epithelium of stomach; ; conjunctival fornix; ; superior surface of tongue; ; right lung lobe; ; cervix; ; lip;
	More reference expression data
	n/a
Gene ontology
Molecular function	calcium ion binding ; S100 protein binding ; protein homodimerization activity ; ion transmembrane transporter activity ; zinc ion binding ; metal ion binding ; calcium-dependent protein binding ; protein binding ; tropomyosin binding ;
Cellular component	cytoplasm ; cytosol ; nuclear envelope ; membrane ; ruffle ; extrinsic component of cytoplasmic side of plasma membrane ; plasma membrane ; perinuclear region of cytoplasm ; extracellular exosome ; nucleus ; extracellular region ; collagen-containing extracellular matrix ;
Biological process	axonogenesis ; positive regulation of fibroblast proliferation ; ion transmembrane transport ; signal transduction ;
	Sources:Amigo / QuickGO
Orthologs
	6277
	20200
	ENSG00000197956
	ENSMUSG00000001025
	P06703
	P14069
	NM_014624
	NM_011313
	NP_055439
	NP_035443
	Wikidata
View/Edit Human	View/Edit Mouse

Last updated September 08, 2023

S100 calcium-binding protein A6 (S100A6) is a protein that in humans is encoded by the S100A6 gene.^[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. S100 genes include at least 13 members which are located as a cluster on chromosome 1q21. This protein may function in stimulation of Ca2+-dependent insulin release, stimulation of prolactin secretion, and exocytosis. Chromosomal rearrangements and altered expression of this gene have been implicated in melanoma.^[5]

Interactions

S100A6 has been shown to interact with S100B ^[6]^[7] and SUGT1.^[8]

Pathology

S100A6 to be reported as possible diagnostic marker of papillary thyroid carcinoma.^[9]

Related Research Articles

The S100 proteins are a family of low molecular-weight proteins found in vertebrates characterized by two calcium-binding sites that have helix-loop-helix ("EF-hand-type") conformation. At least 21 different S100 proteins are known. They are encoded by a family of genes whose symbols use the S100 prefix, for example, S100A1, S100A2, S100A3. They are also considered as damage-associated molecular pattern molecules (DAMPs), and knockdown of aryl hydrocarbon receptor downregulates the expression of S100 proteins in THP-1 cells.

Protein S100-A4 (S100A4) is a protein that in humans is encoded by the S100A4 gene.

S100 calcium-binding protein A7 (S100A7), also known as psoriasin, is a protein that in humans is encoded by the S100A7 gene.

S100 calcium-binding protein A2 (S100A2) is a protein that in humans is encoded by the S100A2 gene and it is located on chromosome 1q21 with other S100 proteins.

S100 calcium-binding protein B (S100B) is a protein of the S-100 protein family.

S100 calcium-binding protein A8 (S100A8) is a protein that in humans is encoded by the S100A8 gene. It is also known as calgranulin A.

S100 calcium-binding protein A9 (S100A9) also known as migration inhibitory factor-related protein 14 (MRP14) or calgranulin B is a protein that in humans is encoded by the S100A9 gene.

Protein S100-A1, also known as S100 calcium-binding protein A1 is a protein which in humans is encoded by the S100A1 gene. S100A1 is highly expressed in cardiac and skeletal muscle, and localizes to Z-discs and sarcoplasmic reticulum. S100A1 has shown promise as an effective candidate for gene therapy to treat post-myocardially infarcted cardiac tissue.

S100 calcium-binding protein A10 (S100A10), also known as p11, is a protein that is encoded by the S100A10 gene in humans and the S100a10 gene in other species. S100A10 is a member of the S100 family of proteins containing two EF-hand calcium-binding motifs. S100 proteins are localized in the cytoplasm and/or nucleus of a wide range of cells. They regulate a number of cellular processes such as cell cycle progression and differentiation. The S100 protein is implicated in exocytosis and endocytosis by reorganization of F-actin.

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

S100 calcium-binding protein A12 (S100A12) is a protein that in humans is encoded by the S100A12 gene. Human S100A12, also known as calgranulin C, was first described in 1995.

S100 calcium-binding protein P (S100P) is a protein that in humans is encoded by the S100P gene.

S100 calcium-binding protein A13 (S100A13) is a protein that in humans is encoded by the S100A13 gene.

S100 calcium-binding protein A3 (S100A3) is a protein that in humans is encoded by the S100A3 gene.

Serine/threonine-protein kinase 38 is an enzyme that in humans is encoded by the STK38 gene.

Calcium/calmodulin-dependent protein kinase kinase 1 is an enzyme that in humans is encoded by the CAMKK1 gene.

Calcyclin-binding protein is a protein that in humans is encoded by the CACYBP gene.

K_v channel-interacting protein 1 also known as KChIP1 is a protein that in humans is encoded by the KCNIP1 gene.

S100 calcium-binding protein A5 (S100A5) is a protein that in humans is encoded by the S100A5 gene.

S100 calcium binding protein A14 (S100A14) is a protein that in humans is encoded by the S100A14 gene.

References

1 2 3 GRCh38: Ensembl release 89: ENSG00000197956 - Ensembl, May 2017
1 2 3 GRCm38: Ensembl release 89: ENSMUSG00000001025 - Ensembl, May 2017
↑ "Human PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
↑ "Mouse PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
1 2 "Entrez Gene: S100A6 S100 calcium binding protein A6".
↑ 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". J. Biol. Chem. 275 (45): 35302–10. doi: 10.1074/jbc.M003943200 . PMID 10913138.
↑ Yang Q, O'Hanlon D, Heizmann CW, Marks A (February 1999). "Demonstration of heterodimer formation between S100B and S100A6 in the yeast two-hybrid system and human melanoma". Exp. Cell Res. 246 (2): 501–9. doi:10.1006/excr.1998.4314. PMID 9925766.
↑ Nowotny M, Spiechowicz M, Jastrzebska B, Filipek A, Kitagawa K, Kuznicki J (July 2003). "Calcium-regulated interaction of Sgt1 with S100A6 (calcyclin) and other S100 proteins". J. Biol. Chem. 278 (29): 26923–8. doi: 10.1074/jbc.M211518200 . PMID 12746458.
↑ Sofiadis A, Dinets A, Orre LM, Branca RM, Juhlin CC, Foukakis T, Wallin G, Höög A, Hulchiy M, Zedenius J, Larsson C, Lehtiö J (October 2010). "Proteomic study of thyroid tumors reveals frequent up-regulation of the Ca2+ -binding protein S100A6 in papillary thyroid carcinoma". Thyroid. 20 (10): 1067–76. doi:10.1089/thy.2009.0400. PMID 20629554.

Schäfer BW, Heizmann CW (1996). "The S100 family of EF-hand calcium-binding proteins: functions and pathology". Trends Biochem. Sci. 21 (4): 134–40. doi:10.1016/S0968-0004(96)80167-8. PMID 8701470.
Minami H, Tokumitsu H, Mizutani A, Watanabe Y, Watanabe M, Hidaka H (1992). "Specific binding of CAP-50 to calcyclin". FEBS Lett. 305 (3): 217–9. doi: 10.1016/0014-5793(92)80671-3 . PMID 1299619.
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. doi:10.1021/bi00157a012. PMID 1384693.
Tomida Y, Terasawa M, Kobayashi R, Hidaka H (1992). "Calcyclin and calvasculin exist in human platelets". Biochem. Biophys. Res. Commun. 189 (3): 1310–6. doi:10.1016/0006-291X(92)90216-8. PMID 1482346.
Filipek A, Gerke V, Weber K, Kuźnicki J (1991). "Characterization of the cell-cycle-regulated protein calcyclin from Ehrlich ascites tumor cells. Identification of two binding proteins obtained by Ca2(+)-dependent affinity chromatography". Eur. J. Biochem. 195 (3): 795–800. doi: 10.1111/j.1432-1033.1991.tb15768.x . PMID 1999197.
Murphy LC, Murphy LJ, Tsuyuki D, Duckworth ML, Shiu RP (1988). "Cloning and characterization of a cDNA encoding a highly conserved, putative calcium binding protein, identified by an anti-prolactin receptor antiserum". J. Biol. Chem. 263 (5): 2397–401. doi: 10.1016/S0021-9258(18)69220-8 . PMID 2448309.
Gabius HJ, Bardosi A, Gabius S, Hellmann KP, Karas M, Kratzin H (1989). "Identification of a cell cycle-dependent gene product as a sialic acid-binding protein". Biochem. Biophys. Res. Commun. 163 (1): 506–12. doi:10.1016/0006-291X(89)92166-9. PMID 2775283.
Ferrari S, Calabretta B, deRiel JK, Battini R, Ghezzo F, Lauret E, Griffin C, Emanuel BS, Gurrieri F, Baserga R (1987). "Structural and functional analysis of a growth-regulated gene, the human calcyclin". J. Biol. Chem. 262 (17): 8325–32. doi: 10.1016/S0021-9258(18)47567-9 . PMID 3036810.
Calabretta B, Battini R, Kaczmarek L, de Riel JK, Baserga R (1986). "Molecular cloning of the cDNA for a growth factor-inducible gene with strong homology to S-100, a calcium-binding protein". J. Biol. Chem. 261 (27): 12628–32. doi: 10.1016/S0021-9258(18)67137-6 . PMID 3755724.
Schäfer BW, Wicki R, Engelkamp D, Mattei MG, Heizmann CW (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. doi:10.1016/0888-7543(95)80005-7. PMID 7759097.
Engelkamp D, Schäfer BW, Mattei MG, Erne P, Heizmann CW (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. Bibcode:1993PNAS...90.6547E. doi: 10.1073/pnas.90.14.6547 . PMC 46969 . PMID 8341667.
Filipek A, Wojda U (1996). "p30, a novel protein target of mouse calcyclin (S100A6)". Biochem. J. 320 ( Pt 2) (Pt 2): 585–7. doi:10.1042/bj3200585. PMC 1217969 . PMID 8973570.
Kordowska J, Stafford WF, Wang CL (1998). "Ca2+ and Zn2+ bind to different sites and induce different conformational changes in human calcyclin". Eur. J. Biochem. 253 (1): 57–66. doi:10.1046/j.1432-1327.1998.2530057.x. PMID 9578461.
Yang Q, O'Hanlon D, Heizmann CW, Marks A (1999). "Demonstration of heterodimer formation between S100B and S100A6 in the yeast two-hybrid system and human melanoma". Exp. Cell Res. 246 (2): 501–9. doi:10.1006/excr.1998.4314. PMID 9925766.
Sudo T, Hidaka H (1999). "Characterization of the calcyclin (S100A6) binding site of annexin XI-A by site-directed mutagenesis". FEBS Lett. 444 (1): 11–4. doi: 10.1016/S0014-5793(99)00014-9 . PMID 10037139.
Deloulme JC, Assard N, Mbele GO, Mangin C, Kuwano R, Baudier J (2000). "S100A6 and S100A11 are specific targets of the calcium- and zinc-binding S100B protein in vivo". J. Biol. Chem. 275 (45): 35302–10. doi: 10.1074/jbc.M003943200 . PMID 10913138.
Li Y, Yang L, Cui JT, Li WM, Guo RF, Lu YY (2002). "Construction of cDNA representational difference analysis based on two cDNA libraries and identification of garlic inducible expression genes in human gastric cancer cells". World J. Gastroenterol. 8 (2): 208–12. doi: 10.3748/wjg.v8.i2.208 . PMC 4658352 . PMID 11925593.
Otterbein LR, Kordowska J, Witte-Hoffmann C, Wang CL, Dominguez R (2002). "Crystal structures of S100A6 in the Ca(2+)-free and Ca(2+)-bound states: the calcium sensor mechanism of S100 proteins revealed at atomic resolution". Structure. 10 (4): 557–67. doi: 10.1016/S0969-2126(02)00740-2 . PMID 11937060.
Filipek A, Jastrzebska B, Nowotny M, Kuznicki J (2002). "CacyBP/SIP, a calcyclin and Siah-1-interacting protein, binds EF-hand proteins of the S100 family". J. Biol. Chem. 277 (32): 28848–52. doi: 10.1074/jbc.M203602200 . PMID 12042313.

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[refGRCh38Ensembl-1] 1 2 3 GRCh38: Ensembl release 89: ENSG00000197956 - Ensembl, May 2017

[refGRCm38Ensembl-2] 1 2 3 GRCm38: Ensembl release 89: ENSMUSG00000001025 - Ensembl, May 2017

[3] "Human PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.

[4] "Mouse PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.

[entrez-5] 1 2 "Entrez Gene: S100A6 S100 calcium binding protein A6".

[pmid10913138-6] 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". J. Biol. Chem. 275 (45): 35302–10. doi: 10.1074/jbc.M003943200 . PMID 10913138.

[pmid9925766-7] Yang Q, O'Hanlon D, Heizmann CW, Marks A (February 1999). "Demonstration of heterodimer formation between S100B and S100A6 in the yeast two-hybrid system and human melanoma". Exp. Cell Res. 246 (2): 501–9. doi:10.1006/excr.1998.4314. PMID 9925766.

[pmid12746458-8] Nowotny M, Spiechowicz M, Jastrzebska B, Filipek A, Kitagawa K, Kuznicki J (July 2003). "Calcium-regulated interaction of Sgt1 with S100A6 (calcyclin) and other S100 proteins". J. Biol. Chem. 278 (29): 26923–8. doi: 10.1074/jbc.M211518200 . PMID 12746458.

[9] Sofiadis A, Dinets A, Orre LM, Branca RM, Juhlin CC, Foukakis T, Wallin G, Höög A, Hulchiy M, Zedenius J, Larsson C, Lehtiö J (October 2010). "Proteomic study of thyroid tumors reveals frequent up-regulation of the Ca2+ -binding protein S100A6 in papillary thyroid carcinoma". Thyroid. 20 (10): 1067–76. doi:10.1089/thy.2009.0400. PMID 20629554.

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