S100A2 | |||||||||||||||||||||||||||||||||||||||||||||||||||
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Aliases | S100A2 , CAN19, S100L, S100 calcium binding protein A2 | ||||||||||||||||||||||||||||||||||||||||||||||||||
External IDs | OMIM: 176993; HomoloGene: 48389; GeneCards: S100A2; OMA:S100A2 - orthologs | ||||||||||||||||||||||||||||||||||||||||||||||||||
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S100 calcium-binding protein A2 (S100A2) is a protein that in humans is encoded by the S100A2 gene [2] and it is located on chromosome 1q21 with other S100 proteins.
S100A2, also known as CaN19 or S100L was first isolated from bovine lung tissue. [3] However, in human tissue it was discovered several years later, in the mammary epithelial cells. [4] Under normal circumstances it is highly expressed in human lungs, prostate, kidneys, hair follicles and salivary and mammary glands. [5] S100A2 is predominantly found in the nucleus, which is not very common in other S100 proteins. Moreover, it can also be found in the cytoplasm, and its distribution is rather diffuse. Its occurrence in cytoplasm is most likely dependent on calcium levels in the cell. [6] [7] [8] In the extracellular environment, it can be found as a homodimer in vivo and in vitro , but it also exists in monomeric, polymeric and multimeric forms. In multimeric form, it functions as a RAGE receptor ligand. [9]
S100A2 is important in cytoskeleton organization. [10] Also, S100A2 is induced by p53, which it interacts and participates in the transcription of p21. [8] [11] It also plays a role in differentiation, regeneration of tissues and healing [12] [13] and it was shown it attract eosinophils by chemotaxis. [14]
Its expression is reduced in many types of cancer, thereby distinguishing the cancerous expression profile of the other proteins of the S100 group. [15] [16] [17] It has been reported that S100A2 is downregulated in lung, kidney, prostate cancer and melanoma. [15] Chromosomal rearrangements and altered expression of this gene have also been implicated in breast cancer. [18] [17] [7] In addition, its decline is associated with poor prognosis, disease progression, increased occurrence of metastasis and increased patient mortality. [19] Although in most cancers it has been found in reduced levels, there are studies that show that in some cases it is overproduced. [20] [21]
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 B (S100B) is a protein of the S100 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 A6 (S100A6) is a protein that in humans is encoded by the S100A6 gene.
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.
S100 calcium-binding protein A5 (S100A5) is a protein that is encoded by the S100A5 gene in humans.
Protein S100-A7A (S100A7A), also known as koebnerisin, is a protein that in humans is encoded by the S100A7A gene.
S100 calcium binding protein A14 (S100A14) is a protein that in humans is encoded by the S100A14 gene.
The S100 calcium-binding protein mS100a7a15 is the murine ortholog of human S100A7 (Psoriasin) and human S100A15 (Koebnerisin). mS100a7a15 is also known as S100a15, mS100a7 and mS100a7a and is encoded by the mS100a7a gene
The epidermal differentiation complex (EDC) is a gene complex comprising over fifty genes encoding proteins involved in the terminal differentiation and cornification of keratinocytes, the primary cell type of the epidermis. In humans, the complex is located on a 1.9 Mbp stretch within chromosome 1q21. The proteins encoded by EDC genes are closely related in terms of function, and evolutionarily they belong to three distinct gene families: the cornified envelope precursor family, the S100 protein family and the S100 fused type protein (SFTP) family.