P29515 · TBB7_ARATH
- ProteinTubulin beta-7 chain
- GeneTUBB7
- StatusUniProtKB reviewed (Swiss-Prot)
- Amino acids449 (go to sequence)
- Protein existenceEvidence at transcript level
- Annotation score5/5
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.
Miscellaneous
There are nine genes coding for beta-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 | cytosol | |
Cellular Component | Golgi apparatus | |
Cellular Component | microtubule | |
Cellular Component | peroxisome | |
Cellular Component | plant-type cell wall | |
Cellular Component | plasma membrane | |
Cellular Component | plasmodesma | |
Cellular Component | tubulin complex | |
Cellular Component | vacuole | |
Molecular Function | GTP binding | |
Molecular Function | GTPase activity | |
Molecular Function | metal ion binding | |
Molecular Function | mRNA binding | |
Molecular Function | structural constituent of cytoskeleton | |
Biological Process | microtubule-based process |
Keywords
- Ligand
Names & Taxonomy
Protein names
- Recommended nameTubulin beta-7 chain
- Alternative names
Gene names
Organism names
- Strain
- Taxonomic lineageEukaryota > Viridiplantae > Streptophyta > Embryophyta > Tracheophyta > Spermatophyta > Magnoliopsida > eudicotyledons > Gunneridae > Pentapetalae > rosids > malvids > Brassicales > Brassicaceae > Camelineae > Arabidopsis
Accessions
- Primary accessionP29515
Proteomes
Organism-specific databases
Genome annotation databases
Subcellular Location
PTM/Processing
Features
Showing features for chain.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Chain | PRO_0000048326 | 1-449 | Tubulin beta-7 chain | |||
Sequence: MREILHIQGGQCGNQIGSKFWEVVNLEHGIDQTGRYVGDSELQLERVNVYYNEASCGRYVPRAVLMDLEPGTMDSVRSGPYGQIFRPDNFVFGQSGAGNNWAKGHYTEGAELIDSVLDVVRKEAENCDCLQGFQVCHSLGGGTGSGMGTLLISKIREEYPDRMMMTFSVFPSPKVSDTVVEPYNATLSVHQLVENADECMVLDNEALYDICFRTLKLSTPSFGDLNHLISATMSGVTCCLRFPGQLNSDLRKLAVNLIPFPRLHFFMVGFAPLTSRGSQQYRNLTVPELTQQMWDAKNMMCAADPRHGRYLTASAMFRGKMSTKEVDEQMLNVQNKNSSYFVEWIPNNVKSTVCDIPPTGLKMASTFIGNSTSIQEMFRRVSEQFTAMFRRKAFLHWYTGEGMDEMEFTEAESNMNDLVSEYQQYQDATADEEGEYEEEEAEYEQEETY |
Proteomic databases
PTM databases
Expression
Gene expression databases
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 | 422-449 | Disordered | ||||
Sequence: YQQYQDATADEEGEYEEEEAEYEQEETY | ||||||
Compositional bias | 428-449 | Acidic residues | ||||
Sequence: ATADEEGEYEEEEAEYEQEETY |
Sequence similarities
Belongs to the tubulin family.
Phylogenomic databases
Family and domain databases
Sequence
- Sequence statusComplete
- Length449
- Mass (Da)50,747
- Last updated1993-04-01 v1
- ChecksumCB61368BF21A77B0
Features
Showing features for compositional bias.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Compositional bias | 428-449 | Acidic residues | ||||
Sequence: ATADEEGEYEEEEAEYEQEETY |
Keywords
- Technical term
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
M84704 EMBL· GenBank· DDBJ | AAA32885.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
AC004561 EMBL· GenBank· DDBJ | AAC95184.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
CP002685 EMBL· GenBank· DDBJ | AEC08272.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
AF370568 EMBL· GenBank· DDBJ | AAK49574.1 EMBL· GenBank· DDBJ | mRNA | ||
AY090345 EMBL· GenBank· DDBJ | AAL91251.1 EMBL· GenBank· DDBJ | mRNA | ||
BT001121 EMBL· GenBank· DDBJ | AAN64512.1 EMBL· GenBank· DDBJ | mRNA | ||
AY085710 EMBL· GenBank· DDBJ | AAM62928.1 EMBL· GenBank· DDBJ | mRNA |