Q6PEY2 · TBA3E_HUMAN
- ProteinTubulin alpha-3E chain
- GeneTUBA3E
- StatusUniProtKB reviewed (Swiss-Prot)
- Organism
- Amino acids450 (go to sequence)
- Protein existenceEvidence at protein 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 | 450 | Involved in polymerization | ||||
Sequence: Y |
GO annotations
Aspect | Term | |
---|---|---|
Cellular Component | cytoplasm | |
Cellular Component | microtubule | |
Cellular Component | microtubule cytoskeleton | |
Cellular Component | nucleus | |
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-3E chain
- EC number
- Alternative names
- Cleaved into 1 chains
Gene names
Organism names
- Organism
- Taxonomic lineageEukaryota > Metazoa > Chordata > Craniata > Vertebrata > Euteleostomi > Mammalia > Eutheria > Euarchontoglires > Primates > Haplorrhini > Catarrhini > Hominidae > Homo
Accessions
- Primary accessionQ6PEY2
Proteomes
Organism-specific databases
Subcellular Location
Disease & Variants
Features
Showing features for natural variant.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Natural variant | VAR_052667 | 101 | in dbSNP:rs3863907 | |||
Sequence: S → N | ||||||
Natural variant | VAR_052668 | 126 | in dbSNP:rs13000721 | |||
Sequence: A → V | ||||||
Natural variant | VAR_054640 | 162 | in dbSNP:rs2261398 | |||
Sequence: S → G | ||||||
Natural variant | VAR_052669 | 402 | in dbSNP:rs1052422 | |||
Sequence: W → R | ||||||
Natural variant | VAR_054641 | 449 | in dbSNP:rs10208844 | |||
Sequence: A → E |
Variants
We now provide the "Disease & Variants" viewer in its own tab.
The viewer provides 592 variants from UniProt as well as other sources including ClinVar and dbSNP.
Organism-specific databases
Miscellaneous
Chemistry
Genetic variation databases
PTM/Processing
Features
Showing features for chain, modified residue, modified residue (large scale data).
Type | ID | Position(s) | Source | Description | |||
---|---|---|---|---|---|---|---|
Chain | PRO_0000437400 | 1-449 | UniProt | Detyrosinated tubulin alpha-3E chain | |||
Sequence: MRECISIHVGQAGVQIGNACWELYCLEHGIQPDGQMPSDKTIGGGDDSFNTFFSETGAGKHVPRAVFVDLEPTVVDEVRTGTYRQLFHPEQLITGKEDAASNYARGHYTIGKEIVDLVLDRIRKLADLCTGLQGFLIFHSFGGGTGSGFASLLMERLSVDYSKKSKLEFAIYPAPQVSTAVVEPYNSILTTHTTLEHSDCAFMVDNEAIYDICRRNLDIERPTYTNLNRLIGQIVSSITASLRFDGALNVDLTEFQTNLVPYPRIHFPLATYAPVISAEKAYHEQLSVAEITNACFEPANQMVKCDPRHGKYMACCMLYRGDVVPKDVNAAIATIKTKRTIQFVDWCPTGFKVGINYQPPTVVPGGDLAKVQRAVCMLSNTTAIAEAWARLVHKFDLMYAKWAFVHWYVGEGMEEGEFSEAREDLAALEKDCEEVGVDSVEAEAEEGEA | |||||||
Chain | PRO_0000293649 | 1-450 | UniProt | Tubulin alpha-3E chain | |||
Sequence: MRECISIHVGQAGVQIGNACWELYCLEHGIQPDGQMPSDKTIGGGDDSFNTFFSETGAGKHVPRAVFVDLEPTVVDEVRTGTYRQLFHPEQLITGKEDAASNYARGHYTIGKEIVDLVLDRIRKLADLCTGLQGFLIFHSFGGGTGSGFASLLMERLSVDYSKKSKLEFAIYPAPQVSTAVVEPYNSILTTHTTLEHSDCAFMVDNEAIYDICRRNLDIERPTYTNLNRLIGQIVSSITASLRFDGALNVDLTEFQTNLVPYPRIHFPLATYAPVISAEKAYHEQLSVAEITNACFEPANQMVKCDPRHGKYMACCMLYRGDVVPKDVNAAIATIKTKRTIQFVDWCPTGFKVGINYQPPTVVPGGDLAKVQRAVCMLSNTTAIAEAWARLVHKFDLMYAKWAFVHWYVGEGMEEGEFSEAREDLAALEKDCEEVGVDSVEAEAEEGEAY | |||||||
Modified residue | 40 | UniProt | N6-acetyllysine | ||||
Sequence: K | |||||||
Modified residue (large scale data) | 41 | PRIDE | Phosphothreonine | ||||
Sequence: T | |||||||
Modified residue (large scale data) | 48 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 51 | PRIDE | Phosphothreonine | ||||
Sequence: T | |||||||
Modified residue (large scale data) | 54 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 56 | PRIDE | Phosphothreonine | ||||
Sequence: T | |||||||
Modified residue (large scale data) | 82 | PRIDE | Phosphothreonine | ||||
Sequence: T | |||||||
Modified residue (large scale data) | 223 | PRIDE | Phosphothreonine | ||||
Sequence: T | |||||||
Modified residue (large scale data) | 224 | PRIDE | Phosphotyrosine | ||||
Sequence: Y | |||||||
Modified residue (large scale data) | 225 | PRIDE | Phosphothreonine | ||||
Sequence: T | |||||||
Modified residue (large scale data) | 262 | PRIDE | Phosphotyrosine | ||||
Sequence: Y | |||||||
Modified residue (large scale data) | 271 | PRIDE | Phosphothreonine | ||||
Sequence: T | |||||||
Modified residue (large scale data) | 272 | PRIDE | Phosphotyrosine | ||||
Sequence: Y | |||||||
Modified residue (large scale data) | 277 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue | 282 | UniProt | 3'-nitrotyrosine | ||||
Sequence: Y | |||||||
Modified residue (large scale data) | 282 | PRIDE | Phosphotyrosine | ||||
Sequence: Y | |||||||
Modified residue (large scale data) | 287 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 334 | PRIDE | Phosphothreonine | ||||
Sequence: T | |||||||
Modified residue (large scale data) | 337 | PRIDE | Phosphothreonine | ||||
Sequence: T | |||||||
Modified residue (large scale data) | 357 | PRIDE | Phosphotyrosine | ||||
Sequence: Y | |||||||
Modified residue (large scale data) | 361 | PRIDE | Phosphothreonine | ||||
Sequence: T | |||||||
Modified residue (large scale data) | 379 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue | 439 | UniProt | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue | 450 | UniProt | 3'-nitrotyrosine | ||||
Sequence: Y |
Post-translational modification
Some glutamate residues at the C-terminus are polyglutamylated, resulting in polyglutamate chains on the gamma-carboxyl group (PubMed:26875866).
Polyglutamylation plays a key role in microtubule severing by spastin (SPAST). SPAST preferentially recognizes and acts on microtubules decorated with short polyglutamate tails: severing activity by SPAST increases as the number of glutamates per tubulin rises from one to eight, but decreases beyond this glutamylation threshold (PubMed:26875866).
Glutamylation is also involved in cilia motility (By similarity).
Polyglutamylation plays a key role in microtubule severing by spastin (SPAST). SPAST preferentially recognizes and acts on microtubules decorated with short polyglutamate tails: severing activity by SPAST increases as the number of glutamates per tubulin rises from one to eight, but decreases beyond this glutamylation threshold (PubMed:26875866).
Glutamylation is also involved in cilia motility (By similarity).
Some glutamate residues at the C-terminus are monoglycylated but not polyglycylated due to the absence of functional TTLL10 in human. Monoglycylation is mainly limited to tubulin incorporated into cilia and flagella axonemes, which is required for their stability and maintenance. Flagella glycylation controls sperm motility. Both polyglutamylation and monoglycylation can coexist on the same protein on adjacent residues, and lowering glycylation levels increases polyglutamylation, and reciprocally.
Acetylation of alpha chains at Lys-40 is located inside the microtubule lumen. This modification has been correlated with increased microtubule stability, intracellular transport and ciliary assembly.
Methylation of alpha chains at Lys-40 is found in mitotic microtubules and is required for normal mitosis and cytokinesis contributing to genomic stability.
Nitration of Tyr-450 is irreversible and interferes with normal dynein intracellular distribution.
Undergoes a tyrosination/detyrosination cycle, the cyclic removal and re-addition of a C-terminal tyrosine residue by the enzymes tubulin tyrosine carboxypeptidase (MATCAP1/KIAA0895L, VASH1 or VASH2) and tubulin tyrosine ligase (TTL), respectively.
Tubulin alpha-3E chain
Tyrosination promotes microtubule interaction with CAP-Gly domain-containing proteins such as CLIP1, CLIP2 and DCTN1 (By similarity).
Tyrosination regulates the initiation of dynein-dynactin motility via interaction with DCTN1, which brings the dynein-dynactin complex into contact with microtubules (PubMed:26972003).
In neurons, tyrosinated tubulins mediate the initiation of retrograde vesicle transport (By similarity).
Tyrosination regulates the initiation of dynein-dynactin motility via interaction with DCTN1, which brings the dynein-dynactin complex into contact with microtubules (PubMed:26972003).
In neurons, tyrosinated tubulins mediate the initiation of retrograde vesicle transport (By similarity).
Detyrosinated tubulin alpha-3E chain
Detyrosination is involved in metaphase plate congression by guiding chromosomes during mitosis: detyrosination promotes interaction with CENPE, promoting pole-proximal transport of chromosomes toward the equator (PubMed:25908662).
Detyrosination increases microtubules-dependent mechanotransduction in dystrophic cardiac and skeletal muscle. In cardiomyocytes, detyrosinated microtubules are required to resist to contractile compression during contraction: detyrosination promotes association with desmin (DES) at force-generating sarcomeres, leading to buckled microtubules and mechanical resistance to contraction (By similarity).
Detyrosination increases microtubules-dependent mechanotransduction in dystrophic cardiac and skeletal muscle. In cardiomyocytes, detyrosinated microtubules are required to resist to contractile compression during contraction: detyrosination promotes association with desmin (DES) at force-generating sarcomeres, leading to buckled microtubules and mechanical resistance to contraction (By similarity).
Keywords
- PTM
Proteomic databases
PTM 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.
Binary interactions
Type | Entry 1 | Entry 2 | Number of experiments | Intact | |
---|---|---|---|---|---|
BINARY | Q6PEY2 | FHL3 Q13643 | 3 | EBI-2551023, EBI-741101 | |
BINARY | Q6PEY2 | NMI Q13287 | 9 | EBI-2551023, EBI-372942 | |
BINARY | Q6PEY2 | TCP11L2 Q8N4U5 | 2 | EBI-2551023, EBI-11897462 |
Protein-protein interaction databases
Chemistry
Miscellaneous
Structure
Family & Domains
Features
Showing features for motif.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Motif | 1-4 | MREC motif | ||||
Sequence: MREC |
Domain
The MREC motif may be critical for tubulin autoregulation.
Sequence similarities
Belongs to the tubulin family.
Phylogenomic databases
Family and domain databases
Sequence
- Sequence statusComplete
- Length450
- Mass (Da)49,859
- Last updated2009-03-03 v2
- Checksum3326FDF17B37A540
Computationally mapped potential isoform sequences
There is 1 potential isoform mapped to this entry
Entry | Entry name | Gene name | Length | ||
---|---|---|---|---|---|
A0AAG2UW83 | A0AAG2UW83_HUMAN | TUBA3E | 450 |
Keywords
- Technical term
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
AC018804 EMBL· GenBank· DDBJ | - | Genomic DNA | No translation available. | |
BC057811 EMBL· GenBank· DDBJ | AAH57811.1 EMBL· GenBank· DDBJ | mRNA |