S100A4

S100 calcium binding protein A4

PDB rendering based on 1m31.

Available structures
PDB	1M31, 2Q91, 3C1V, 3CGA, 3KO0, 3M0W

Identifiers

Symbols

S100A4; 18A2; 42A; CAPL; FSP1; MTS1; P9KA; PEL98

External IDs

OMIM: 114210 MGI: 1330282 HomoloGene: 7924 GeneCards: S100A4 Gene

Gene Ontology
Molecular function	• calcium ion binding • protein binding • identical protein binding • calcium-dependent protein binding • RAGE receptor binding
Cellular component	• nucleus • neuron projection • perinuclear region of cytoplasm
Biological process	• epithelial to mesenchymal transition • positive regulation of I-kappaB kinase/NF-kappaB cascade
Sources: Amigo / QuickGO

RNA expression pattern

More reference expression data

Orthologs

Species

Human

Mouse

RefSeq (mRNA)

RefSeq (protein)

Location (UCSC)

Chr 1:
153.52 – 153.52 Mb

Chr 3:
90.41 – 90.41 Mb

PubMed search

[1]

[2]

Protein S100-A4 is a protein that in humans is encoded by the S100A4 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 motility, invasion, and tubulin polymerization. Chromosomal rearrangements and altered expression of this gene have been implicated in tumor metastasis. Multiple alternatively spliced variants, encoding the same protein, have been identified.^[2]

Interactions

S100A4 has been shown to interact with S100 calcium binding protein A1.^[3]^[4]

References

^ Stoler A, Bouck N (Mar 1985). "Identification of a single chromosome in the normal human genome essential for suppression of hamster cell transformation". Proc Natl Acad Sci U S A 82 (2): 570–4. doi:10.1073/pnas.82.2.570. PMC 397082. PMID 3155863. http://www.pubmedcentral.nih.gov/articlerender.fcgi?tool=pmcentrez&artid=397082.
^ "Entrez Gene: S100A4 S100 calcium binding protein A4". http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=6275.
^ Rual, Jean-François; Venkatesan Kavitha, Hao Tong, Hirozane-Kishikawa Tomoko, Dricot Amélie, Li Ning, Berriz Gabriel F, Gibbons Francis D, Dreze Matija, Ayivi-Guedehoussou Nono, Klitgord Niels, Simon Christophe, Boxem Mike, Milstein Stuart, Rosenberg Jennifer, Goldberg Debra S, Zhang Lan V, Wong Sharyl L, Franklin Giovanni, Li Siming, Albala Joanna S, Lim Janghoo, Fraughton Carlene, Llamosas Estelle, Cevik Sebiha, Bex Camille, Lamesch Philippe, Sikorski Robert S, Vandenhaute Jean, Zoghbi Huda Y, Smolyar Alex, Bosak Stephanie, Sequerra Reynaldo, Doucette-Stamm Lynn, Cusick Michael E, Hill David E, Roth Frederick P, Vidal Marc (Oct. 2005). "Towards a proteome-scale map of the human protein-protein interaction network". Nature (England) 437 (7062): 1173–8. doi:10.1038/nature04209. PMID 16189514.
^ Wang, G; Rudland P S, White M R, Barraclough R (Apr. 2000). "Interaction in vivo and in vitro of the metastasis-inducing S100 protein, S100A4 (p9Ka) with S100A1". J. Biol. Chem. (UNITED STATES) 275 (15): 11141–6. doi:10.1074/jbc.275.15.11141. ISSN 0021-9258. PMID 10753920.

Kalluri R, Neilson EG (2004). "Epithelial-mesenchymal transition and its implications for fibrosis". J. Clin. Invest. 112 (12): 1776–84. doi:10.1172/JCI20530. PMC 297008. PMID 14679171. http://www.pubmedcentral.nih.gov/articlerender.fcgi?tool=pmcentrez&artid=297008.
Garrett SC, Varney KM, Weber DJ, Bresnick AR (2006). "S100A4, a mediator of metastasis". J. Biol. Chem. 281 (2): 677–80. doi:10.1074/jbc.R500017200. PMID 16243835.
Tarabykina S, Griffiths TR, Tulchinsky E, et al. (2007). "Metastasis-associated protein S100A4: spotlight on its role in cell migration". Current cancer drug targets 7 (3): 217–28. doi:10.2174/156800907780618329. PMID 17504119.
Tulchinsky E, Ford HL, Kramerov D, et al. (1992). "Transcriptional analysis of the mts1 gene with specific reference to 5' flanking sequences". Proc. Natl. Acad. Sci. U.S.A. 89 (19): 9146–50. doi:10.1073/pnas.89.19.9146. PMC 50082. PMID 1329089. http://www.pubmedcentral.nih.gov/articlerender.fcgi?tool=pmcentrez&artid=50082.
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 (1993). "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.
Ambartsumian N, Tarabykina S, Grigorian M, et al. (1995). "Characterization of two splice variants of metastasis-associated human mts1 gene". Gene 159 (1): 125–30. doi:10.1016/0378-1119(94)00778-Q. PMID 7607566.
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. doi:10.1016/0888-7543(95)80005-7. PMID 7759097.
Takenaga K, Nakamura Y, Sakiyama S, et al. (1994). "Binding of pEL98 protein, an S100-related calcium-binding protein, to nonmuscle tropomyosin". J. Cell Biol. 124 (5): 757–68. doi:10.1083/jcb.124.5.757. PMC 2119958. PMID 8120097. http://www.pubmedcentral.nih.gov/articlerender.fcgi?tool=pmcentrez&artid=2119958.
Pedrocchi M, Schäfer BW, Durussel I, et al. (1994). "Purification and characterization of the recombinant human calcium-binding S100 proteins CAPL and CACY". Biochemistry 33 (21): 6732–8. doi:10.1021/bi00187a045. PMID 8204608.
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. doi:10.1073/pnas.90.14.6547. PMC 46969. PMID 8341667. http://www.pubmedcentral.nih.gov/articlerender.fcgi?tool=pmcentrez&artid=46969.
Ford HL, Silver DL, Kachar B, et al. (1998). "Effect of Mts1 on the structure and activity of nonmuscle myosin II". Biochemistry 36 (51): 16321–7. doi:10.1021/bi971182l. PMID 9405067.
Liu JH, Wei S, Burnette PK, et al. (1999). "Functional association of TGF-beta receptor II with cyclin B". Oncogene 18 (1): 269–75. doi:10.1038/sj.onc.1202263. PMID 9926943.
Wang G, Rudland PS, White MR, Barraclough R (2000). "Interaction in vivo and in vitro of the metastasis-inducing S100 protein, S100A4 (p9Ka) with S100A1". J. Biol. Chem. 275 (15): 11141–6. doi:10.1074/jbc.275.15.11141. PMID 10753920.
Tarabykina S, Kriajevska M, Scott DJ, et al. (2000). "Heterocomplex formation between metastasis-related protein S100A4 (Mts1) and S100A1 as revealed by the yeast two-hybrid system". FEBS Lett. 475 (3): 187–91. doi:10.1016/S0014-5793(00)01652-5. PMID 10869553.
Tarabykina S, Scott DJ, Herzyk P, et al. (2001). "The dimerization interface of the metastasis-associated protein S100A4 (Mts1): in vivo and in vitro studies". J. Biol. Chem. 276 (26): 24212–22. doi:10.1074/jbc.M009477200. PMID 11278510.
Grigorian M, Andresen S, Tulchinsky E, et al. (2001). "Tumor suppressor p53 protein is a new target for the metastasis-associated Mts1/S100A4 protein: functional consequences of their interaction". J. Biol. Chem. 276 (25): 22699–708. doi:10.1074/jbc.M010231200. PMID 11278647.
Chen H, Fernig DG, Rudland PS, et al. (2001). "Binding to intracellular targets of the metastasis-inducing protein, S100A4 (p9Ka)". Biochem. Biophys. Res. Commun. 286 (5): 1212–7. doi:10.1006/bbrc.2001.5517. PMID 11527429.
Zhang H, Wang Z, Ding Y, et al. (2002). "Crystallization and preliminary crystallographic analysis of a metastasis-inducing protein, human S100A4". Acta Crystallogr. D Biol. Crystallogr. 58 (Pt 1): 127–9. doi:10.1107/S090744490101650X. PMID 11752788.

PDB gallery

1m31: Three-Dimensional Solution Structure of Apo-Mts1

S100A4

Interactions

References

Further reading