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.
|
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:
- Nuclear magnetic resonance (NMR) (298 K; pH: 7; TFE)
| References:
- 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:
- Circular dichroism (CD) spectroscopy, near-UV (298 K; )
| References:
- 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:
- Circular dichroism (CD) spectroscopy, near-UV (298 K; TFE)
| References:
- 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:
- Circular dichroism (CD) spectroscopy, near-UV (298 K; TFE)
| References:
- 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:
- Nuclear magnetic resonance (NMR) (298 K; pH: 7; TFE)
- Circular dichroism (CD) spectroscopy, near-UV (298 K; )
| References:
- 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:
|
If you have any comments or wish to provide additional references to this protein or its disordered region(s), please click here to e-mail us. |
Disprot-footer
|