DP00169: Tubulin beta-2 chainFASTA viewXML view

General information
DisProt:DP00169
Name:Tubulin beta-2 chain
Synonym(s):TBB2_CHICK
Beta-tubulin class-II
First appeared in release:Release 2.0 (02/14/2005)
UniProt:P32882
UniGene:Gga.1815
SwissProt: TBB2_CHICK
TrEMBL:  
NCBI (GI): 417855
Source organism:Gallus gallus (Chicken)
Sequence length:445
Percent disordered:7%
Homologues: 


Native sequence

        10         20         30         40         50         60
         |          |          |          |          |          |
MREIVHIQAG QCGNQIGAKF WEVISDEHGI DPTGSYHGDS DLQLERINVY YNEATGNKYV - 60
PRAILVDLEP GTMDSVRSGP FGQIFRPDNF VFGQSGAGNN WAKGHYTEGA ELVDSVLDVV - 120
RKESESCDCL QGFQLTHSLG GGTGSGMGTL LISKIREEYP DRIMNTFSVM PSPKVSDTVV - 180
EPYNATLSVH QLVENTDETY CIDNEALYDI CFRTLKLTTP TYGDLNHLVS ATMSGVTTCL - 240
RFPGQLNADL RKLAVNMVPF PRLHFFMPGF APLTSRGSQQ YRALTVPELT QQMFDSKNMM - 300
AACDPRHGRY LTVAAIFRGR MSMKEVDEQM LNVQNKNSSY FVEWIPNNVK TAVCDIPPRG - 360
LKMSATFIGN STAIQELFKR ISEQFTAMFR RKAFLHWYTG EGMDEMEFTE AESNMNDLVS - 420
EYQQYQDATA DEQGEFEEEG EEDEA



Functional narrative    

Beta-tubulin is a major component of microtubules that assist in cell form and movement. Beta-tubulin interacts directly with alpha-tubulin, microtubule-associated protein 2, and microtubule motor proteins. The disordered regions of this protein are located in the C-terminus and are sites of interaction with various partners.

Region 2: 394-404 Region 1: 394-407 Region 3: 412-414 Region 4: 431-431 Region 5: 432-445

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 - Extended
Name: 
Location:394 - 407
Length:14
Region sequence:

FLHWYTGEGMDEME

Modification type: Engineered
Fragment
PDB:  
Structural/functional type: Function arises via a disorder to order transition
Functional classes: Molecular assembly
Functional subclasses: Substrate/ligand binding
Protein-protein binding
Detection methods:
  1. Nuclear magnetic resonance (NMR) (298 K; pH: 7; TFE)

References:
  1. Jimenez MA, Evangelio JA, Aranda C, Lopez-Brauet A, Andreu D, Rico M, Lagos R, Andreu JM, Monasterio O. "Helicity of alpha(404-451) and beta(394-445) tubulin C-terminal recombinant peptides." Protein Sci. 1999; 8(4): 788-799. PubMed: 10211825

Comments:
 



Region 2
Type:Disordered - Extended
Name: 
Location:394 - 404
Length:11
Region sequence:

FLHWYTGEGMD

Modification type: Engineered
Fragment
PDB:  
Structural/functional type: Function arises via a disorder to order transition
Functional classes: Molecular assembly
Functional subclasses: Protein-protein binding
Substrate/ligand binding
Detection methods:
  1. Circular dichroism (CD) spectroscopy, near-UV (298 K; )

References:
  1. Jimenez MA, Evangelio JA, Aranda C, Lopez-Brauet A, Andreu D, Rico M, Lagos R, Andreu JM, Monasterio O. "Helicity of alpha(404-451) and beta(394-445) tubulin C-terminal recombinant peptides." Protein Sci. 1999; 8(4): 788-799. PubMed: 10211825

Comments:
 



Region 3
Type:Disordered - Extended
Name: 
Location:412 - 414
Length:3
Region sequence:

ESN

Modification type: Engineered
Fragment
PDB:  
Structural/functional type: Function arises via a disorder to order transition
Functional classes: Molecular assembly
Functional subclasses: Substrate/ligand binding
Protein-protein binding
Detection methods:
  1. Circular dichroism (CD) spectroscopy, near-UV (298 K; TFE)

References:
  1. Jimenez MA, Evangelio JA, Aranda C, Lopez-Brauet A, Andreu D, Rico M, Lagos R, Andreu JM, Monasterio O. "Helicity of alpha(404-451) and beta(394-445) tubulin C-terminal recombinant peptides." Protein Sci. 1999; 8(4): 788-799. PubMed: 10211825

Comments:
Disorder may be caused by the truncation of this fragment




Region 4
Type:Disordered - Extended
Name: 
Location:431 - 431
Length:1
Region sequence:

D

Modification type: Engineered
Fragment
PDB:  
Structural/functional type: Function arises via a disorder to order transition
Functional classes: Molecular assembly
Functional subclasses: Substrate/ligand binding
Protein-protein binding
Detection methods:
  1. Circular dichroism (CD) spectroscopy, near-UV (298 K; TFE)

References:
  1. Jimenez MA, Evangelio JA, Aranda C, Lopez-Brauet A, Andreu D, Rico M, Lagos R, Andreu JM, Monasterio O. "Helicity of alpha(404-451) and beta(394-445) tubulin C-terminal recombinant peptides." Protein Sci. 1999; 8(4): 788-799. PubMed: 10211825

Comments:
Disorder may be caused by the truncation of this fragment




Region 5
Type:Disordered - Extended
Name: 
Location:432 - 445
Length:14
Region sequence:

EQGEFEEEGEEDEA

Modification type: Engineered
Fragment
PDB:  
Structural/functional type: Function arises via a disorder to order transition
Functional classes: Molecular assembly
Functional subclasses: Substrate/ligand binding
Protein-protein binding
Detection methods:
  1. Nuclear magnetic resonance (NMR) (298 K; pH: 7; TFE)

  2. Circular dichroism (CD) spectroscopy, near-UV (298 K; )

References:
  1. Jimenez MA, Evangelio JA, Aranda C, Lopez-Brauet A, Andreu D, Rico M, Lagos R, Andreu JM, Monasterio O. "Helicity of alpha(404-451) and beta(394-445) tubulin C-terminal recombinant peptides." Protein Sci. 1999; 8(4): 788-799. PubMed: 10211825

Comments:
 


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