Name

SERPINB10 Gene

serpin peptidase inhibitor, clade B (ovalbumin), member 10

The superfamily of high molecular weight serine proteinase inhibitors (serpins) regulate a diverse set of intracellular and extracellular processes such as complement activation, fibrinolysis, coagulation, cellular differentiation, tumor suppression, apoptosis, and cell migration. Serpins are characterized by a well-conserved tertiary structure that consists of 3 beta sheets and 8 or 9 alpha helices (Huber and Carrell, 1989 [PubMed 2690952]). A critical portion of the molecule, the reactive center loop connects beta sheets A and C. Protease inhibitor-10 (PI10; SERPINB10) is a member of the ov-serpin subfamily, which, relative to the archetypal serpin PI1 (MIM 107400), is characterized by a high degree of homology to chicken ovalbumin, lack of N- and C-terminal extensions, absence of a signal peptide, and a serine rather than an asparagine residue at the penultimate position (summary by Bartuski et al., 1997 [PubMed 9268635]).[supplied by OMIM, Jan 2010]

serpinb10 Gene Set

From GeneRIF Biological Term Annotations

genes co-occuring with the biological term serpinb10 in literature-supported statements describing functions of genes from the GeneRIF Biological Term Annotations dataset.

SERPINB10 Gene Set

From Pathway Commons Protein-Protein Interactions

interacting proteins for SERPINB10 from the Pathway Commons Protein-Protein Interactions dataset.