TUBB4A
entrez
10382
canonical
uniprot
P04350
canonical
ensembl
ENSG00000104833
resolver
ensp
ENSP00000264071
resolver
ensp
ENSP00000470627
resolver
ensp
ENSP00000471880
resolver
ensp
ENSP00000472375
resolver
enst
ENST00000264071
resolver
enst
ENST00000596291
resolver
enst
ENST00000597686
resolver
enst
ENST00000598635
resolver
genesymbol
TUBB4A
resolver
genesymbol_syn
TUBB4
resolver
genesymbol_syn
TUBB5
resolver
hgnc
HGNC:20774
resolver
uniprot
B3KQP4
resolver
uniprot
M0QZL7
resolver
uniprot
M0R1I1
resolver
uniprot
M0R278
resolver
uniprot
Q969E5
resolver
uniprot_entry
M0QZL7_HUMAN
resolver
uniprot_entry
M0R1I1_HUMAN
resolver
uniprot_entry
M0R278_HUMAN
resolver
uniprot_entry
TBB4A_HUMAN
resolver
uniprot_sec
B3KQP4
resolver
uniprot_sec
Q969E5
resolver
amino_acid_sequence
MREIVHLQAGQCGNQIGAKFWEVISDEHGIDPTGTYHGDSDLQLERINVYYNEATGGNYVPRAVLVDLEPGTMDSVRSGPFGQIFRPDNFVFGQSGAGNNWAKGHYTEGAELVDAVLDVVRKEAESCDCLQGFQLTHSLGGGTGSGMGTLLISKIREEFPDRIMNTFSVVPSPKVSDTVVEPYNATLSVHQLVENTDETYCIDNEALYDICFRTLKLTTPTYGDLNHLVSATMSGVTTCLRFPGQLNADLRKLAVNMVPFPRLHFFMPGFAPLTSRGSQQYRALTVPELTQQMFDAKNMMAACDPRHGRYLTVAAVFRGRMSMKEVDEQMLSVQSKNSSYFVEWIPNNVKTAVCDIPPRGLKMAATFIGNSTAIQELFKRISEQFTAMFRRKAFLHWYTGEGMDEMEFTEAESNMNDLVSEYQQYQDATAEEGEFEEEAEEEVA
uniprot
proteins
disease_involvement
DISEASE: Dystonia 4, torsion, autosomal dominant (DYT4) [MIM:128101]: A form of torsion dystonia, a disease defined by the presence of sustained involuntary muscle contractions, often leading to abnormal postures. 'Torsion' refers to the twisting nature of body movements, often affecting the trunk. DYT4 is characterized by onset in the second to third decade of progressive laryngeal dysphonia followed by the involvement of other muscles, such as the neck or limbs. Some patients develop an ataxic gait. {ECO:0000269|PubMed:23424103}. Note=The disease is caused by variants affecting the gene represented in this entry.; DISEASE: Leukodystrophy, hypomyelinating, 6 (HLD6) [MIM:612438]: A neurologic disorder characterized by onset in infancy or early childhood of delayed motor development and gait instability, followed by extrapyramidal movement disorders, such as dystonia, choreoathetosis, rigidity, opisthotonus, and oculogyric crises, progressive spastic tetraplegia, ataxia, and, more rarely, seizures. Most patients have cognitive decline and speech delay, but some can function normally. Brain MRI shows a combination of hypomyelination, cerebellar atrophy, and atrophy or disappearance of the putamen. {ECO:0000269|PubMed:23582646}. Note=The disease is caused by variants affecting the gene represented in this entry.
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
49586
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: Phosphorylated on Ser-172 by CDK1 during the cell cycle, from metaphase to telophase, but not in interphase. This phosphorylation inhibits tubulin incorporation into microtubules. {ECO:0000269|PubMed:16371510}.
uniprot
proteins
protein_family
Tubulin family
uniprot
proteins
pubmed
14654843
uniprot
proteins
pubmed
15489334
uniprot
proteins
pubmed
16303743
uniprot
proteins
pubmed
16371510
uniprot
proteins
pubmed
19524510
uniprot
proteins
pubmed
20191564
uniprot
proteins
pubmed
21269460
uniprot
proteins
pubmed
23424103
uniprot
proteins
pubmed
23582646
uniprot
proteins
pubmed
26875866
uniprot
proteins
pubmed
6462917
uniprot
proteins
pubmed
8619814
uniprot
proteins
sequence_length
444
uniprot
proteins
subcellular_location
SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton.
uniprot
proteins