P61857 · TBB2_DROME
- ProteinTubulin beta-2 chain
- GenebetaTub85D
- StatusUniProtKB reviewed (Swiss-Prot)
- Amino acids446 (go to sequence)
- Protein existenceEvidence at protein level
- Annotation score4/5
Function
function
Tubulin is the major constituent of microtubules, a cylinder consisting of laterally associated linear protofilaments composed of alpha- and beta-tubulin heterodimers. Microtubules grow by the addition of GTP-tubulin dimers to the microtubule end, where a stabilizing cap forms. Below the cap, tubulin dimers are in GDP-bound state, owing to GTPase activity of alpha-tubulin.
Cofactor
Features
Showing features for binding site.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Binding site | 11 | GTP (UniProtKB | ChEBI) | ||||
Sequence: Q | ||||||
Binding site | 69 | GTP (UniProtKB | ChEBI) | ||||
Sequence: E | ||||||
Binding site | 69 | Mg2+ (UniProtKB | ChEBI) | ||||
Sequence: E | ||||||
Binding site | 138 | GTP (UniProtKB | ChEBI) | ||||
Sequence: S | ||||||
Binding site | 142 | GTP (UniProtKB | ChEBI) | ||||
Sequence: G | ||||||
Binding site | 143 | GTP (UniProtKB | ChEBI) | ||||
Sequence: T | ||||||
Binding site | 144 | GTP (UniProtKB | ChEBI) | ||||
Sequence: G | ||||||
Binding site | 204 | GTP (UniProtKB | ChEBI) | ||||
Sequence: N | ||||||
Binding site | 226 | GTP (UniProtKB | ChEBI) | ||||
Sequence: N |
GO annotations
Aspect | Term | |
---|---|---|
Cellular Component | cytoplasm | |
Cellular Component | microtubule | |
Molecular Function | GTP binding | |
Molecular Function | GTPase activity | |
Molecular Function | metal ion binding | |
Molecular Function | structural constituent of cytoskeleton | |
Biological Process | microtubule cytoskeleton organization | |
Biological Process | mitotic cell cycle | |
Biological Process | salivary gland morphogenesis |
Keywords
- Ligand
Enzyme and pathway databases
Names & Taxonomy
Protein names
- Recommended nameTubulin beta-2 chain
- Alternative names
Gene names
Organism names
- Strains
- Taxonomic lineageEukaryota > Metazoa > Ecdysozoa > Arthropoda > Hexapoda > Insecta > Pterygota > Neoptera > Endopterygota > Diptera > Brachycera > Muscomorpha > Ephydroidea > Drosophilidae > Drosophila > Sophophora
Accessions
- Primary accessionP61857
- Secondary accessions
Proteomes
Organism-specific databases
Subcellular Location
PTM/Processing
Features
Showing features for chain.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Chain | PRO_0000048279 | 1-446 | Tubulin beta-2 chain | |||
Sequence: MREIVHIQAGQCGNQIGGKFWEVISDEHCIDATGTYYGDSDLQLERINVYYNEATGAKYVPRAILVDLEPGTMDSVRSGAFGQIFRPDNFVFGQSGAGNNWAKGHYTEGAELVDSVLDVVRKESEGCDCLQGFQLTHSLGGGTGSGMGTLLISKIREEYPDRIMNTFSVVPSPKVSDTVVEPYNATLSVHQLVENTDETYCIDNEALYDICFRTLKLTTPTYGDLNHLVSATMSGVTTCLRFPGQLNADLRKLAVNMVPFPRLHFFMPGFAPLTSRGSQQYRALTVPELTQQMFDAKNMMAACDPRHGRYLTVAAIFRGRMSMKEVDEQMLNIQNKNSSFFVEWIPNNCKTAVCDIPPRGLKMSATFIGNSTAIQELFKRVSEQFTAMFRRKAFLHWYTGEGMDEMEFTEAESNMNDLVSEYQQYQEATADEEGEFDEDEEGGGDE |
Proteomic databases
Expression
Interaction
Subunit
Dimer of alpha and beta chains. A typical microtubule is a hollow water-filled tube with an outer diameter of 25 nm and an inner diameter of 15 nM. Alpha-beta heterodimers associate head-to-tail to form protofilaments running lengthwise along the microtubule wall with the beta-tubulin subunit facing the microtubule plus end conferring a structural polarity. Microtubules usually have 13 protofilaments but different protofilament numbers can be found in some organisms and specialized cells.
Protein-protein interaction databases
Structure
Family & Domains
Features
Showing features for region, compositional bias.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Region | 424-446 | Disordered | ||||
Sequence: QYQEATADEEGEFDEDEEGGGDE | ||||||
Compositional bias | 428-446 | Acidic residues | ||||
Sequence: ATADEEGEFDEDEEGGGDE |
Sequence similarities
Belongs to the tubulin family.
Phylogenomic databases
Family and domain databases
Sequence
- Sequence statusComplete
- Length446
- Mass (Da)49,870
- Last updated2004-06-07 v1
- ChecksumE11495E67158E358
Features
Showing features for sequence conflict, compositional bias.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Sequence conflict | 135 | in Ref. 1; AAA28991 | ||||
Sequence: L → S | ||||||
Compositional bias | 428-446 | Acidic residues | ||||
Sequence: ATADEEGEFDEDEEGGGDE |
Keywords
- Technical term
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
M20420 EMBL· GenBank· DDBJ | AAA28991.1 EMBL· GenBank· DDBJ | mRNA | ||
AE014297 EMBL· GenBank· DDBJ | AAF54373.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
AY118725 EMBL· GenBank· DDBJ | AAM50585.1 EMBL· GenBank· DDBJ | mRNA |