| Primary Identifier | IPR030514 | Type | Conserved_site |
| Short Name | Stathmin_CS |
| description | Stathmin [](from the Greek 'stathmos' which means relay), is an ubiquitousintracellular protein, present in a variety of phosphorylated forms and whichis involved in the regulation of the microtubule (MT) filament system bydestabilising microtubules. It prevents assembly and promotes disassembly ofmicrotubules.These proteins possess a stathmin-like domain (SLD) with various N-terminalextensions. SLD is a highly conserved domain of 149 amino acid residues.Structurally, it consists of an N-terminal domain of about 45 residuesfollowed by a 78 residue α-helical domain consisting of a heptad repeatcoiled coil structure and a C-terminal domain of 25 residues[]. The SLD binds two tubulins arranged longitudinally, head-to-tail, in protofilament-like complexes.This entry represents two conserved sites. The first one is a conserved decapeptide which ends with the first three residues of the coiled coil domain. The second conserved site corresponds to part of the central region of the coiled coil. |
