Annotations for this protein have been verified by the authors of the corresponding papers



DP00174: StathminFASTA viewXML view

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



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.

Region 1: 1-149

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.


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:
  1. Nuclear magnetic resonance (NMR) (296 K; pH: 6.8; )

  2. Circular dichroism (CD) spectroscopy, far-UV (pH: 6.8; EGTA 1 mM; GTP 1 mM; MgCl2 1 mM; PIPES-KOH 8 mM)

  3. Nuclear magnetic resonance (NMR) (296 K; pH: 7.5; )

  4. Circular dichroism (CD) spectroscopy, far-UV (pH: 7.5; EGTA 1 mM; GTP 1 mM; MgCl2 1 mM; PIPES-KOH 8 mM)

References:
  1. 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

  2. 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.




References

  1. 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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