P41383 · TBA2_PATVU
- ProteinTubulin alpha-2/alpha-4 chain
- GeneTUB2; TUB4
- StatusUniProtKB reviewed (Swiss-Prot)
- Organism
- Amino acids452 (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.
Catalytic activity
- GTP + H2O = GDP + H+ + phosphateThis reaction proceeds in the forward direction.
Cofactor
Features
Showing features for binding site, active site, site.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Binding site | 11 | GTP (UniProtKB | ChEBI) | ||||
Sequence: Q | ||||||
Binding site | 71 | GTP (UniProtKB | ChEBI) | ||||
Sequence: E | ||||||
Binding site | 71 | Mg2+ (UniProtKB | ChEBI) | ||||
Sequence: E | ||||||
Binding site | 140 | GTP (UniProtKB | ChEBI) | ||||
Sequence: S | ||||||
Binding site | 144 | GTP (UniProtKB | ChEBI) | ||||
Sequence: G | ||||||
Binding site | 145 | GTP (UniProtKB | ChEBI) | ||||
Sequence: T | ||||||
Binding site | 179 | GTP (UniProtKB | ChEBI) | ||||
Sequence: T | ||||||
Binding site | 206 | GTP (UniProtKB | ChEBI) | ||||
Sequence: N | ||||||
Binding site | 228 | GTP (UniProtKB | ChEBI) | ||||
Sequence: N | ||||||
Active site | 254 | |||||
Sequence: E | ||||||
Site | 452 | Involved in polymerization | ||||
Sequence: Y |
GO annotations
all annotations | all molecular function | virus receptor activity | dna binding | rna binding | cytoskeletal motor activity | catalytic activity | gtpase activity | structural molecule activity | transporter activity | cytoskeletal protein binding | lipid binding | cyclase activity | antioxidant activity | oxidoreductase activity | transferase activity | hydrolase activity | lyase activity | isomerase activity | ligase activity | protein tag activity | cargo receptor activity | histone binding | protein folding chaperone | translation regulator activity | nutrient reservoir activity | receptor ligand activity | molecular transducer activity | molecular adaptor activity | toxin activity | cell adhesion mediator activity | molecular function regulator activity | virus coreceptor activity | catalytic activity, acting on a protein | catalytic activity, acting on dna | catalytic activity, acting on rna | molecular carrier activity | transcription regulator activity | general transcription initiation factor activity | molecular sensor activity | molecular sequestering activity | atp-dependent activity | other molecular function | all biological process | mitotic cell cycle | cytokinesis | cytoplasmic translation | immune system process | muscle system process | circulatory system process | renal system process | respiratory system process | carbohydrate metabolic process | generation of precursor metabolites and energy | dna replication | dna repair | dna recombination | chromatin organization | dna-templated transcription | regulation of dna-templated transcription | trna metabolic process | protein folding | protein glycosylation | amino acid metabolic process | modified amino acid metabolic process | lipid metabolic process | vitamin metabolic process | sulfur compound metabolic process | intracellular protein transport | nucleocytoplasmic transport | autophagy | inflammatory response | mitochondrion organization | cytoskeleton organization | microtubule-based movement | peroxisome organization | lysosome organization | chromosome segregation | cell adhesion | establishment or maintenance of cell polarity | programmed cell death | photosynthesis | mrna metabolic process | snrna metabolic process | vesicle-mediated transport | reproductive process | digestive system process | signaling | cell differentiation | protein catabolic process | extracellular matrix organization | regulatory ncrna-mediated gene silencing | telomere organization | cell junction organization | wound healing | ribosome biogenesis | cilium organization | anatomical structure development | cell motility | nervous system process | endocrine process | protein maturation | transmembrane transport | nucleobase-containing small molecule metabolic process | hepaticobiliary system process | membrane organization | protein-containing complex assembly | cell wall organization or biogenesis | nitrogen cycle metabolic process | protein localization to plasma membrane | defense response to other organism | detoxification | meiotic nuclear division | mitotic nuclear division | mitochondrial gene expression | carbohydrate derivative metabolic process | other biological process | all cellular component | nuclear chromosome | extracellular region | extracellular space | cell wall | nucleus | nuclear envelope | nucleoplasm | chromosome | nucleolus | mitochondrion | lysosome | endosome | vacuole | peroxisome | endoplasmic reticulum | golgi apparatus | lipid droplet | microtubule organizing center | cytosol | ribosome | cytoskeleton | plasma membrane | cilium | plastid | thylakoid | external encapsulating structure | extracellular matrix | cytoplasmic vesicle | organelle | other cellular component | |||
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Aspect | Term | |
---|---|---|
Cellular Component | cytoplasm | |
Cellular Component | microtubule | |
Molecular Function | GTP binding | |
Molecular Function | hydrolase activity | |
Molecular Function | metal ion binding | |
Molecular Function | structural constituent of cytoskeleton | |
Biological Process | microtubule cytoskeleton organization | |
Biological Process | mitotic cell cycle |
Keywords
- Molecular function
- Ligand
Enzyme and pathway databases
Names & Taxonomy
Protein names
- Recommended nameTubulin alpha-2/alpha-4 chain
- EC number
Gene names
Organism names
- Organism
- Taxonomic lineageEukaryota > Metazoa > Spiralia > Lophotrochozoa > Mollusca > Gastropoda > Patellogastropoda > Patelloidea > Patellidae > Patella
Accessions
- Primary accessionP41383
Subcellular Location
PTM/Processing
Features
Showing features for chain, modified residue.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Chain | PRO_0000048209 | 1-452 | Tubulin alpha-2/alpha-4 chain | |||
Sequence: MRECISVHIGQAGVQMGNACWELYCLEHGIQPDGQMPSDKTIGGGDDSFNTFFSETGAGKHVPRAVFVDLEPTVVDEVRTGTYRQLFHPEQLITGKEDAANNYARGHYTVGKEIIDLVLDRIRKLADQCTGLQGFLIFHSFGGGTGSGFSSLLMERLSVDYGKKSKLEFAIYPAPQISTAVVEPYNSILTTHTTLEHSDCAFMVDNEAIYDICRRNLDIERPTYTNLNRLIGQIVSSITASLRFDGALNVDLTEFQTNLVPYPRIHFPLATYAPVISAEKAYHEQLTVAEITNACFEPANQMVKCDPRHGKYMSCCMLYRGDVVPKDVNAAIATIKTKRTIQFVDWCPTGFKVGINYQPPTVVPGGDLAKVQRAVCMLSNTTAIAEAWARLDHKFDLMYAKRAFVHWYVGEGMEEGEFSEAREDLAALEKDYEEVGVDSVEGEGEEEGGEEY | ||||||
Modified residue | 40 | N6-acetyllysine | ||||
Sequence: K |
Post-translational modification
Undergoes a tyrosination/detyrosination cycle, the cyclic removal and re-addition of a C-terminal tyrosine residue by the enzymes tubulin tyrosine carboxypeptidase (TTCP) and tubulin tyrosine ligase (TTL), respectively.
Acetylation of alpha chains at Lys-40 stabilizes microtubules and affects affinity and processivity of microtubule motors. This modification has a role in multiple cellular functions, ranging from cell motility, cell cycle progression or cell differentiation to intracellular trafficking and signaling (By similarity).
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 region, compositional bias.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Region | 432-452 | Disordered | ||||
Sequence: YEEVGVDSVEGEGEEEGGEEY | ||||||
Compositional bias | 438-452 | Acidic residues | ||||
Sequence: DSVEGEGEEEGGEEY |
Sequence similarities
Belongs to the tubulin family.
Family and domain databases
Sequence
- Sequence statusComplete
- Length452
- Mass (Da)50,211
- Last updated1995-11-01 v1
- Checksum9730E9AD9A1CF21A
Features
Showing features for compositional bias.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Compositional bias | 438-452 | Acidic residues | ||||
Sequence: DSVEGEGEEEGGEEY |