The domain within your query sequence starts at position 4 and ends at position 102; the E-value for the Stathmin domain shown below is 2.9e-58.
SDIQVKELEKRASGQAFELILSPRSKESVPDFPLSPPKKKDLSLEEIQKKLEAAEERRKS HEAEVLKQLAEKREHEKEVLQKAIEENNNFSKMAEEKLT
Stathmin |
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PFAM accession number: | PF00836 |
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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:
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