General information | DisProt: | DP00174 | Name: | Stathmin | Synonym(s): | STMN1_HUMAN
Phosphoprotein p19
pp19
Leukemia-associated phosphoprotein p18
Proliferation-related phosphoprotein p18
Oncoprotein 18
Op18
pp17
Prosolin
Metablastin
Protein Pr22
| First appeared in release: | Release 2.0 (02/14/2005) | UniProt: | P16949 | UniGene: | Hs.209983 | SwissProt: | STMN1_HUMAN | TrEMBL: | | NCBI (GI): | 134973 | Source organism: | Homo sapiens (Human) | Sequence length: | 149 | Percent disordered: | 100% | Homologues: | |
Native sequence |
10 20 30 40 50 60 | | | | | | MASSDIQVKE LEKRASGQAF ELILSPRSKE SVPEFPLSPP KKKDLSLEEI QKKLEAAEER - 60 RKSHEAEVLK QLAEKREHEK EVLQKAIEEN NNFSKMAEEK LTHKMEANKE NREAQMAAKL - 120 ERLREKDKHI EEVRKNKESK DPADETEAD
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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.
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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.
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Region 1 | Type: | Disordered | Name: | | Location: | 1 - 149 | Length: | 149 | Region sequence: |
MASSDIQVKELEKRASGQAFELILSPRSKESVPEFPLSPPKKKDLSLEEIQKKLEAAEER RKSHEAEVLKQLAEKREHEKEVLQKAIEENNNFSKMAEEKLTHKMEANKENREAQMAAKL ERLREKDKHIEEVRKNKESKDPADETEAD | 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)
| References:
- 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
| Comments: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.
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References |
- 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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