Leukemia-associated phosphoprotein p18
Proliferation-related phosphoprotein p18
| First appeared in release:||Release 2.0 (02/14/2005)|
|SwissProt: ||STMN1_HUMAN |
|TrEMBL: || |
|NCBI (GI): ||134973 |
|Source organism:||Homo sapiens (Human)|
10 20 30 40 50 60
| | | | | |
MASSDIQVKE LEKRASGQAF ELILSPRSKE SVPEFPLSPP KKKDLSLEEI QKKLEAAEER - 60
RKSHEAEVLK QLAEKREHEK EVLQKAIEEN NNFSKMAEEK LTHKMEANKE NREAQMAAKL - 120
ERLREKDKHI EEVRKNKESK DPADETEAD
|Functional narrative |
Stathmin, a protein found in the cytoplasm of a cell, destabilizes alpha/beta-tubulin complexes, preventing assembly and promoting disassembly of microtubules. A member of the op18/stathmin family. Abnormalities in this protein have been found in association with multiple forms of leukemia.
Stathmin undergoes a disorder to order transition upon interaction with the alpha/beta tubulin heterodimer. An additional transition upon phosphorylation, from order to disorder, has been hypothesized by Steinmetz (2001). This transition would allow for the release of the alpha/beta-tubulin heterodimers thereby inducing assembly of microtubules.
|Map of ordered and disordered regions|
Note: 'Mouse' over a region to see the start and stop residues. Click on a region to see detailed information.
|Location:||1 - 149|
|Modification type: ||Native |
|PDB: || |
|Structural/functional type: ||Function arises via a disorder to order transition |
|Functional classes: ||Molecular assembly |
|Functional subclasses: ||Protein-protein binding |
|Detection methods: |
- Nuclear magnetic resonance (NMR) (296 K; pH: 6.8; )
- Circular dichroism (CD) spectroscopy, far-UV (pH: 6.8; EGTA 1 mM; GTP 1 mM; MgCl2 1 mM; PIPES-KOH 8 mM)
- Nuclear magnetic resonance (NMR) (296 K; pH: 7.5; )
- Circular dichroism (CD) spectroscopy, far-UV (pH: 7.5; EGTA 1 mM; GTP 1 mM; MgCl2 1 mM; PIPES-KOH 8 mM)
- Honnappa S, Cutting B, Jahnke W, Seelig J, Steinmetz MO. "Thermodynamics of the Op18/stathmin-tubulin interaction." J Biol Chem. 2003; 278(40): 38926-38934. PubMed: 12860982
- Steinmetz MO, Kammerer RA, Jahnke W, Goldie KN, Lustig A, van Oostrum J. "Op18/stathmin caps a kinked protofilament-like tubulin tetramer." Embo J. 2000; 19(4): 572-80. PubMed: 10675326
pH had little to no effect upon the disordered regions of this protein. Temperature however, did play a factor in measurement of the disordered regions. At lower temperatures, such as 5◦C, this protein was found to be extensively helical.
- Steinmetz MO, Jahnke W, Towbin H, Garcia-Echeverria C, Voshol H, Muller D, van Oostrum J. "Phosphorylation disrupts the central helix in Op18/stathmin and suppresses binding to tubulin." EMBO Rep. 2001; 2(6): 505-510. PubMed: 11415983
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