The domain within your query sequence starts at position 41 and ends at position 174; the E-value for the Stathmin domain shown below is 3.7e-57.



PFAM accession number:PF00836
Interpro abstract (IPR000956):

Stathmin [ (PUBMED:1957351) ] (from the Greek 'stathmos' which means relay), is a ubiquitous intracellular protein, present in a variety of phosphorylated forms. It is involved in the regulation of the microtubule (MT) filament system by destabilising microtubules. It prevents assembly and promotes disassembly of microtubules [ (PUBMED:14598370) ]. However, when phosphorylated, its destabilisation ability is significantly reduced [ (PUBMED:11160824) ].

The stathmin family also includes:

  • Stathmin 2 (Protein SCG10); a neuron-specific, membrane-associated protein that accumulates in the growth cones of developing neurons. It is highly similar in its sequence to stathmin, but differs in that it contains an additional N-terminal hydrophobic segment of 32 residues which is probably responsible for its interaction with membranes.
  • Stathmin 3 (SCG10-like protein; SCLIP) [ (PUBMED:9603203) ]; a protein specifically expressed in neurons.
  • Stathmin 4 (Stathmin-like protein B3); which contains an additional N- terminal hydrophobic domain [ (PUBMED:9342231) ].

These proteins possess a stathmin-like domain (SLD) with various N-terminal extensions. SLD is a highly conserved domain of 149 amino acid residues. Structurally, it consists of an N-terminal domain of about 45 residues followed by a 78 residue alpha-helical domain consisting of a heptad repeat coiled coil structure and a C-terminal domain of 25 residues [ (PUBMED:15014504) (PUBMED:11278715) ]. The SLD binds two tubulins arranged longitudinally, head-to-tail, in protofilament-like complexes.

GO process:regulation of microtubule polymerization or depolymerization (GO:0031110)

This is a PFAM domain. For full annotation and more information, please see the PFAM entry Stathmin