TUBA4A
entrez
7277
canonical
uniprot
P68366
canonical
ensembl
ENSG00000127824
resolver
ensp
ENSP00000248437
resolver
ensp
ENSP00000375938
resolver
genesymbol
TUBA4A
resolver
genesymbol_syn
TUBA1
resolver
hgnc
HGNC:12407
resolver
uniprot
A8MUB1
resolver
uniprot
B3KNQ6
resolver
uniprot
P05215
resolver
uniprot_entry
TBA4A_HUMAN
resolver
uniprot_sec
A8MUB1
resolver
uniprot_sec
B3KNQ6
resolver
uniprot_sec
P05215
resolver
amino_acid_sequence
MRECISVHVGQAGVQMGNACWELYCLEHGIQPDGQMPSDKTIGGGDDSFTTFFCETGAGKHVPRAVFVDLEPTVIDEIRNGPYRQLFHPEQLITGKEDAANNYARGHYTIGKEIIDPVLDRIRKLSDQCTGLQGFLVFHSFGGGTGSGFTSLLMERLSVDYGKKSKLEFSIYPAPQVSTAVVEPYNSILTTHTTLEHSDCAFMVDNEAIYDICRRNLDIERPTYTNLNRLISQIVSSITASLRFDGALNVDLTEFQTNLVPYPRIHFPLATYAPVISAEKAYHEQLSVAEITNACFEPANQMVKCDPRHGKYMACCLLYRGDVVPKDVNAAIAAIKTKRSIQFVDWCPTGFKVGINYQPPTVVPGGDLAKVQRAVCMLSNTTAIAEAWARLDHKFDLMYAKRAFVHWYVGEGMEEGEFSEAREDMAALEKDYEEVGIDSYEDEDEGEE
uniprot
proteins
disease_involvement
DISEASE: Frontotemporal dementia and/or amyotrophic lateral sclerosis 9 (FTDALS9) [MIM:616208]: An autosomal dominant neurodegenerative disorder characterized by adult onset of frontotemporal dementia or amyotrophic lateral sclerosis with upper and lower neuron involvement. Some patients manifest both frontotemporal dementia and amyotrophic lateral sclerosis. {ECO:0000269|PubMed:25374358, ECO:0000269|PubMed:34169147, ECO:0000269|PubMed:38884572}. Note=The disease is caused by variants affecting the gene represented in this entry.; DISEASE: Congenital myopathy 26 (CMYO26) [MIM:621225]: A form of congenital myopathy, a clinically and genetically heterogeneous group of muscle disorders characterized by hypotonia and muscle weakness typically noticed at birth or during the neonatal period, and, in some cases, delayed motor development later in childhood. Specific pathological features are observed on muscle biopsy. CMYO26 is an autosomal dominant form characterized by limb muscle weakness and mild motor delay apparent from infancy, hyporeflexia, myopathic face with high-arched palate, and ophthalmoplegia in some patients. Skeletal muscle biopsy shows myopathic features with myofibrillar disorganization and rimmed vacuoles. {ECO:0000269|PubMed:38413182}. Note=The disease is caused by variants affecting the gene represented in this entry.; DISEASE: Spastic ataxia 11, autosomal dominant (SPAX11) [MIM:621226]: A form of spastic ataxia, a heterogeneous group of progressive neurodegenerative disorders characterized by lower-limb spasticity and generalized ataxia with dysarthria, impaired ocular movements, and gait disturbance. SPAX11 is an autosomal dominant, progressive form with age at onset usually in the first 2 decades. Brain imaging often shows cerebellar atrophy. {ECO:0000269|PubMed:37418012, ECO:0000269|PubMed:38884572}. Note=The disease is caused by variants affecting the gene represented in this entry.; DISEASE: Oocyte/zygote/embryo maturation arrest 23 (OZEMA23) [MIM:621231]: A female infertility disorder characterized by oocyte maturation arrest at the oocyte, zygote, or embryo stage. Inheritance can be autosomal dominant or autosomal recessive. {ECO:0000269|PubMed:37024973, ECO:0000269|PubMed:39209701, ECO:0000269|PubMed:39872894}. Note=The disease is caused by variants affecting the gene represented in this entry.
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 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). {ECO:0000250|UniProtKB:P99024, ECO:0000269|PubMed:26875866}.; PTM: 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. {ECO:0000250|UniProtKB:P07437, ECO:0000305|PubMed:19524510}.; 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:0000269|PubMed:24906155}.; 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) (PubMed:35482892). It can then undergo a detyrosination cycle by the tubulin tyrosine carboxypeptidase (MATCAP1/KIAA0895L) (PubMed:35482892). {ECO:0000269|PubMed:35482892}.
uniprot
proteins
protein_family
Tubulin family
uniprot
proteins
pubmed
14654843
uniprot
proteins
pubmed
14702039
uniprot
proteins
pubmed
15489334
uniprot
proteins
pubmed
15815621
uniprot
proteins
pubmed
18088087
uniprot
proteins
pubmed
18669648
uniprot
proteins
pubmed
18691976
uniprot
proteins
pubmed
19524510
uniprot
proteins
pubmed
21269460
uniprot
proteins
pubmed
23186163
uniprot
proteins
pubmed
24275569
uniprot
proteins
pubmed
24906155
uniprot
proteins
pubmed
25374358
uniprot
proteins
pubmed
25944712
uniprot
proteins
pubmed
26875866
uniprot
proteins
pubmed
3029670
uniprot
proteins
pubmed
34169147
uniprot
proteins
pubmed
35482892
uniprot
proteins
pubmed
37024973
uniprot
proteins
pubmed
37418012
uniprot
proteins
pubmed
38413182
uniprot
proteins
pubmed
38884572
uniprot
proteins
pubmed
39209701
uniprot
proteins
pubmed
39872894
uniprot
proteins
sequence_length
448
uniprot
proteins
subcellular_location
SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton.
uniprot
proteins