Tuba4a
entrez
316531
canonical
uniprot
Q5XIF6
canonical
ensembl
ENSRNOG00000003597
resolver
ensembl
ENSRNOG00055010434
resolver
ensembl
ENSRNOG00060007884
resolver
ensembl
ENSRNOG00065008885
resolver
ensp
ENSRNOP00000004797
resolver
ensp
ENSRNOP00000101677
resolver
ensp
ENSRNOP00055014225
resolver
ensp
ENSRNOP00060009889
resolver
ensp
ENSRNOP00065010631
resolver
enst
ENSRNOT00000004797
resolver
enst
ENSRNOT00000127189
resolver
enst
ENSRNOT00055017667
resolver
enst
ENSRNOT00060013034
resolver
enst
ENSRNOT00065014198
resolver
genesymbol
Tuba4a
resolver
genesymbol_syn
Tuba4
resolver
uniprot_entry
TBA4A_RAT
resolver
amino_acid_sequence
MRECISVHVGQAGVQMGNACWELYCLEHGIQPDGQMPSDKTIGGGDDSFTTFFCETGAGKHVPRAVFVDLEPTVIDEIRNGPYRQLFHPEQLITGKEDAANNYARGHYTIGKEIIDPVLDRIRKLSDQCTGLQGFLVFHSFGGGTGSGFTSLLMERLSVDYGKKSKLEFSIYPAPQVSTAVVEPYNSILTTHTTLEHSDCAFMVDNEAIYDICRRNLDIERPTYTNLNRLISQIVSSITASLRFDGALNVDLTEFQTNLVPYPRIHFPLATYAPVISAEKAYHEQLSVAEITNACFEPANQMVKCDPRHGKYMACCLLYRGDVVPKDVNAAIAAIKTKRSIQFVDWCPTGFKVGINYQPPTVVPGGDLAKVQRAVCMLSNTTAIAEAWARLDHKFDLMYAKRAFVHWYVGEGMEEGEFSEAREDMAALEKDYEEVGIDSYEDEDEGEE
uniprot
proteins
ec_number
3.6.5.-
uniprot
proteins
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.
uniprot
proteins
mass_dalton
49924
uniprot
proteins
post_translational_modification
PTM: Some glutamate residues at the C-terminus are polyglycylated, resulting in polyglycine chains on the gamma-carboxyl group. Glycylation is mainly limited to tubulin incorporated into axonemes (cilia and flagella) whereas glutamylation is prevalent in neuronal cells, centrioles, axonemes, and the mitotic spindle. Both modifications can coexist on the same protein on adjacent residues, and lowering polyglycylation levels increases polyglutamylation, and reciprocally. Cilia and flagella glycylation is required for their stability and maintenance. Flagella glycylation controls sperm motility. {ECO:0000250|UniProtKB:P68368}.; PTM: Some glutamate residues at the C-terminus are polyglutamylated, resulting in polyglutamate chains on the gamma-carboxyl group (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 (By similarity). Glutamylation is also involved in cilia motility (By similarity). {ECO:0000250|UniProtKB:P68368, ECO:0000250|UniProtKB:Q71U36}.; PTM: 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. {ECO:0000250|UniProtKB:Q71U36}.; PTM: Methylation of alpha chains at Lys-40 is found in mitotic microtubules and is required for normal mitosis and cytokinesis contributing to genomic stability. {ECO:0000250|UniProtKB:P68363}.; PTM: Although this tubulin does not encode a C-terminal tyrosine, a C-terminal tyrosine can be added post-translationally by the tubulin tyrosine ligase (TTL). It can then undergo a detyrosination cycle by the tubulin tyrosine carboxypeptidase (MATCAP1/KIAA0895L). {ECO:0000250|UniProtKB:P68366}.
uniprot
proteins
protein_family
Tubulin family
uniprot
proteins
pubmed
15489334
uniprot
proteins
pubmed
22673903
uniprot
proteins
sequence_length
448
uniprot
proteins
subcellular_location
SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton {ECO:0000250}.
uniprot
proteins