Tuba1a
entrez
22142
canonical
uniprot
P68369
canonical
ensembl
ENSMUSG00000072235
resolver
ensp
ENSMUSP00000094778
resolver
enst
ENSMUST00000097014
resolver
genesymbol
Tuba1a
resolver
genesymbol_syn
Tuba1
resolver
uniprot
P02551
resolver
uniprot
P05210
resolver
uniprot
P05212
resolver
uniprot
Q3TGF0
resolver
uniprot
Q3TIW2
resolver
uniprot
Q3TPJ1
resolver
uniprot
Q3ULN1
resolver
uniprot
Q5XJF8
resolver
uniprot_entry
TBA1A_MOUSE
resolver
uniprot_sec
P02551
resolver
uniprot_sec
P05210
resolver
uniprot_sec
P05212
resolver
uniprot_sec
Q3TGF0
resolver
uniprot_sec
Q3TIW2
resolver
uniprot_sec
Q3TPJ1
resolver
uniprot_sec
Q3ULN1
resolver
uniprot_sec
Q5XJF8
resolver
activity_regulation
ACTIVITY REGULATION: In oocytes and preimplantation embryos, GTP-bound tubulins are maintained inactive by cytoplasmic lattices in a poised but restrained state, regulating their availability for early embryonic development. {ECO:0000269|PubMed:41917274, ECO:0000269|PubMed:41986725}.
uniprot
proteins
amino_acid_sequence
MRECISIHVGQAGVQIGNACWELYCLEHGIQPDGQMPSDKTIGGGDDSFNTFFSETGAGKHVPRAVFVDLEPTVIDEVRTGTYRQLFHPEQLITGKEDAANNYARGHYTIGKEIIDLVLDRIRKLADQCTGLQGFLVFHSFGGGTGSGFTSLLMERLSVDYGKKSKLEFSIYPAPQVSTAVVEPYNSILTTHTTLEHSDCAFMVDNEAIYDICRRNLDIERPTYTNLNRLIGQIVSSITASLRFDGALNVDLTEFQTNLVPYPRIHFPLATYAPVISAEKAYHEQLSVAEITNACFEPANQMVKCDPRHGKYMACCLLYRGDVVPKDVNAAIATIKTKRTIQFVDWCPTGFKVGINYQPPTVVPGGDLAKVQRAVCMLSNTTAIAEAWARLDHKFDLMYAKRAFVHWYVGEGMEEGEFSEAREDMAALEKDYEEVGVDSVEGEGEEEGEEY
uniprot
proteins
ec_number
3.6.5.-
uniprot
proteins
function
FUNCTION: Tubulin is the major constituent of microtubules, protein filaments consisting of alpha- and beta-tubulin heterodimers (By similarity). Microtubules grow by the addition of GTP-tubulin dimers to the microtubule end, where a stabilizing cap forms (By similarity). Below the cap, tubulin dimers are in GDP-bound state, owing to GTPase activity of alpha-tubulin (By similarity). {ECO:0000250|UniProtKB:P68363}.
uniprot
proteins
mass_dalton
50136
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 (PubMed:33414192). {ECO:0000269|PubMed:19524510, ECO:0000269|PubMed:23897886, ECO:0000269|PubMed:33414192}.; PTM: Some glutamate residues at the C-terminus are polyglutamylated, resulting in polyglutamate chains on the gamma-carboxyl group (PubMed:15890843, PubMed:1967194). 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 (PubMed:23897886). {ECO:0000250|UniProtKB:Q71U36, ECO:0000269|PubMed:15890843, ECO:0000269|PubMed:1967194, ECO:0000269|PubMed:23897886}.; 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: Nitration of Tyr-451 is irreversible and interferes with normal dynein intracellular distribution. {ECO:0000250|UniProtKB:Q71U36}.; PTM: Undergoes a tyrosination/detyrosination cycle, the cyclic removal and re-addition of a C-terminal tyrosine residue by the enzymes tubulin tyrosine carboxypeptidase (MATCAP1, VASH1 or VASH2) and tubulin tyrosine ligase (TTL), respectively. {ECO:0000269|PubMed:16954346, ECO:0000269|PubMed:19564401, ECO:0000269|PubMed:26446751, ECO:0000269|PubMed:27102488, ECO:0000269|PubMed:29146868}.; PTM: [Tubulin alpha-1A chain]: Tyrosination promotes microtubule interaction with CAP-Gly domain-containing proteins such as CLIP1, CLIP2 and DCTN1 (PubMed:16954346, PubMed:19564401). Tyrosination regulates the initiation of dynein-dynactin motility via interaction with DCTN1, which brings the dynein-dynactin complex into contact with microtubules. In neurons, tyrosinated tubulins mediate the initiation of retrograde vesicle transport (By similarity). {ECO:0000250|UniProtKB:Q71U36, ECO:0000269|PubMed:16954346, ECO:0000269|PubMed:19564401}.; PTM: [Detyrosinated tubulin alpha-1A 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 (By similarity). Detyrosination increases microtubules-dependent mechanotransduction in dystrophic cardiac and skeletal muscle (PubMed:26446751). 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 (PubMed:27102488). {ECO:0000250|UniProtKB:Q71U36, ECO:0000269|PubMed:26446751, ECO:0000269|PubMed:27102488}.
uniprot
proteins
protein_family
Tubulin family
uniprot
proteins
pubmed
15489334
uniprot
proteins
pubmed
15890843
uniprot
proteins
pubmed
16141072
uniprot
proteins
pubmed
16954346
uniprot
proteins
pubmed
19524510
uniprot
proteins
pubmed
19564401
uniprot
proteins
pubmed
1967194
uniprot
proteins
pubmed
23897886
uniprot
proteins
pubmed
26446751
uniprot
proteins
pubmed
27102488
uniprot
proteins
pubmed
29146868
uniprot
proteins
pubmed
33414192
uniprot
proteins
pubmed
3785200
uniprot
proteins
pubmed
37865089
uniprot
proteins
pubmed
3839797
uniprot
proteins
pubmed
41917274
uniprot
proteins
pubmed
41986725
uniprot
proteins
sequence_length
451
uniprot
proteins
subcellular_location
SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton. Cytoplasm, cytoskeleton, flagellum axoneme {ECO:0000269|PubMed:37865089}.
uniprot
proteins