S100 proteins were first discovered in 1965 by Moore as a major protein fraction (0.6% of total soluble protein) isolated from bovine brain (Moore 1965). The protein was given the name S100 due to its high solubility in saturated ammonium sulfate. Later experiments showed the S100 protein fraction constituted two different dimeric species comprised of two b protomers (S100B) or an a, b heterodi...

S100P protein consists of 95 amino acids with a molecular weight of 10.4 kDa. S100P is a Ca binding protein that belongs to S100 family ("Soluble in 100% saturated solution with ammonium sulfate") which was first isolated from human placenta and is therefore designated as "P". S100 family includes at least 26 members, which are thought to be expressed only in vertebrates and are present in a ti...

Other names: 42C, ANX2L, ANX2LG, Annexin II ligand, CAL1L, CLP11, Ca[1], Calpactin, GP11, MGC111133, p10, p11 HGNC (Hugo): S100A10 Location: 1q21.3 Local order: According to NCBI Map Viewer, genes flanking S100A10 in centromere to telomere direction on 1q21 are: THEM4 (1q21) thioesterase superfamily member 4, KRT8P28 (1q21.3) keratin 8 pseudogene 28, S100A10 (1q21) S100 calcium binding protein ...

Description The gene contains five exons and four introns; it is composed of a variable 5' untranslated region, a 296 bp coding sequence, a 3' untranslated region and a polyA tail. Transcription The gene has 5 alternatively spliced variants encoding the same protein; the variant 1 represents the longest transcript (951 bp), all the other variants have distinct and shorter 5'UTR as compared to v...