A0A7J8FYK1 · A0A7J8FYK1_MOLMO
- ProteinTubulin alpha chain
- StatusUniProtKB unreviewed (TrEMBL)
- Amino acids435 (go to sequence)
- Protein existenceInferred from homology
- Annotation score2/5
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.
Catalytic activity
- GTP + H2O = GDP + phosphate + H+This reaction proceeds in the forward direction.
Cofactor
GO annotations
Aspect | Term | |
---|---|---|
Cellular Component | cytoplasm | |
Cellular Component | microtubule | |
Molecular Function | GTP binding | |
Molecular Function | hydrolase activity | |
Molecular Function | structural constituent of cytoskeleton | |
Biological Process | microtubule cytoskeleton organization | |
Biological Process | mitotic cell cycle |
Keywords
- Molecular function
- Ligand
Names & Taxonomy
Protein names
- Recommended nameTubulin alpha chain
Gene names
Organism names
- Strain
- Taxonomic lineageEukaryota > Metazoa > Chordata > Craniata > Vertebrata > Euteleostomi > Mammalia > Eutheria > Laurasiatheria > Chiroptera > Yangochiroptera > Molossidae > Molossus
Accessions
- Primary accessionA0A7J8FYK1
Proteomes
Subcellular Location
PTM/Processing
Keywords
- PTM
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.
Structure
Family & Domains
Features
Showing features for domain, region.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Domain | 49-246 | Tubulin/FtsZ GTPase | ||||
Sequence: FNTFFSETGAGKHVPRAVFVDLEPTVIDEVRTGTYRQLFHPEQLITGKEDAANNYARGHYTIGKEIIDLVLDRIRKLADQCTGLQGFLVFHSFGGGTGSGFTSLLMERLSVDYGKKSKLEFSIYPAPQVSTAVVEPYNSILTTHTTLEHSDCAFMVDNEAIYDICRRNLDIERPTYTNLNRLISQIVSSITASLRFDG | ||||||
Domain | 248-377 | Tubulin/FtsZ 2-layer sandwich | ||||
Sequence: LNVDLTEFQTNLVPYPRIHFPLATYAPVISAEKAYHEQLSVAEITNACFEPANQMVKCDVVPKDVNAAIATIKTKRSIQFVDWCPTGFKVGINYQPPTVVPGGDLAKVQRAVCMLSNTTAIAEAWARLDH | ||||||
Region | 416-435 | Disordered | ||||
Sequence: YEEVGVDSVEGEGEEEGEEY |
Sequence similarities
Belongs to the tubulin family.
Family and domain databases
Sequence
- Sequence statusComplete
- Length435
- Mass (Da)48,286
- Last updated2021-04-07 v1
- Checksum17EDA98608AB1958
Computationally mapped potential isoform sequences
There are 9 potential isoforms mapped to this entry
Entry | Entry name | Gene name | Length | ||
---|---|---|---|---|---|
A0A7J8FZR9 | A0A7J8FZR9_MOLMO | HJG59_008202 | 451 | ||
A0A7J8G0F2 | A0A7J8G0F2_MOLMO | HJG59_008202 | 416 | ||
A0A7J8G0G1 | A0A7J8G0G1_MOLMO | HJG59_008202 | 161 | ||
A0A7J8FZ13 | A0A7J8FZ13_MOLMO | HJG59_008202 | 257 | ||
A0A7J8FZG6 | A0A7J8FZG6_MOLMO | HJG59_008202 | 268 | ||
A0A7J8FYK8 | A0A7J8FYK8_MOLMO | HJG59_008202 | 292 | ||
A0A7J8FYX0 | A0A7J8FYX0_MOLMO | HJG59_008202 | 131 | ||
A0A7J8FZ71 | A0A7J8FZ71_MOLMO | HJG59_008202 | 133 | ||
A0A7J8FYT6 | A0A7J8FYT6_MOLMO | HJG59_008202 | 231 |
Keywords
- Technical term