TUBB3
entrez
10381
canonical
uniprot
Q13509
canonical
ensembl
ENSG00000258947
resolver
ensp
ENSP00000320295
resolver
ensp
ENSP00000451617
resolver
genesymbol
TUBB3
resolver
genesymbol_syn
TUBB4
resolver
hgnc
HGNC:20772
resolver
uniprot
A8K854
resolver
uniprot
Q53G92
resolver
uniprot
Q9BTZ0
resolver
uniprot
Q9BW10
resolver
uniprot_entry
Q53G92_HUMAN
resolver
uniprot_entry
TBB3_HUMAN
resolver
uniprot_sec
A8K854
resolver
uniprot_sec
Q9BTZ0
resolver
uniprot_sec
Q9BW10
resolver
amino_acid_sequence
MREIVHIQAGQCGNQIGAKFWEVISDEHGIDPSGNYVGDSDLQLERISVYYNEASSHKYVPRAILVDLEPGTMDSVRSGAFGHLFRPDNFIFGQSGAGNNWAKGHYTEGAELVDSVLDVVRKECENCDCLQGFQLTHSLGGGTGSGMGTLLISKVREEYPDRIMNTFSVVPSPKVSDTVVEPYNATLSIHQLVENTDETYCIDNEALYDICFRTLKLATPTYGDLNHLVSATMSGVTTSLRFPGQLNADLRKLAVNMVPFPRLHFFMPGFAPLTARGSQQYRALTVPELTQQMFDAKNMMAACDPRHGRYLTVATVFRGRMSMKEVDEQMLAIQSKNSSYFVEWIPNNVKVAVCDIPPRGLKMSSTFIGNSTAIQELFKRISEQFTAMFRRKAFLHWYTGEGMDEMEFTEAESNMNDLVSEYQQYQDATAEEEGEMYEDDEEESEAQGPK
uniprot
proteins
disease_involvement
DISEASE: Fibrosis of extraocular muscles, congenital, 3A (CFEOM3A) [MIM:600638]: A congenital ocular motility disorder marked by restrictive ophthalmoplegia affecting extraocular muscles innervated by the oculomotor and/or trochlear nerves. It is clinically characterized by anchoring of the eyes in downward gaze, ptosis, and backward tilt of the head. Congenital fibrosis of extraocular muscles type 3 presents as a non-progressive, autosomal dominant disorder with variable expression. Patients may be bilaterally or unilaterally affected, and their oculo-motility defects range from complete ophthalmoplegia (with the eyes fixed in a hypo- and exotropic position), to mild asymptomatic restrictions of ocular movement. Ptosis, refractive error, amblyopia, and compensatory head positions are associated with the more severe forms of the disorder. In some cases, the ocular phenotype is accompanied by additional features including developmental delay, corpus callosum agenesis, basal ganglia dysmorphism, facial weakness, polyneuropathy. {ECO:0000269|PubMed:20074521}. Note=The disease is caused by variants affecting the gene represented in this entry.; DISEASE: Cortical dysplasia, complex, with other brain malformations 1 (CDCBM1) [MIM:614039]: A disorder of aberrant neuronal migration and disturbed axonal guidance. Affected individuals have mild to severe intellectual disability, strabismus, axial hypotonia, and spasticity. Brain imaging shows variable malformations of cortical development, including polymicrogyria, gyral disorganization, and fusion of the basal ganglia, as well as thin corpus callosum, hypoplastic brainstem, and dysplastic cerebellar vermis. Extraocular muscles are not involved. {ECO:0000269|PubMed:20829227}. 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, protein filaments consisting of alpha- and beta-tubulin heterodimers (PubMed:34996871, PubMed:38305685, PubMed:38609661). Microtubules grow by the addition of GTP-tubulin dimers to the microtubule end, where a stabilizing cap forms (PubMed:34996871, PubMed:38305685, PubMed:38609661). Below the cap, alpha-beta tubulin heterodimers are in GDP-bound state, owing to GTPase activity of alpha-tubulin (PubMed:34996871, PubMed:38609661). TUBB3 plays a critical role in proper axon guidance and maintenance (PubMed:20074521). Binding of NTN1/Netrin-1 to its receptor UNC5C might cause dissociation of UNC5C from polymerized TUBB3 in microtubules and thereby lead to increased microtubule dynamics and axon repulsion (PubMed:28483977). Plays a role in dorsal root ganglion axon projection towards the spinal cord (PubMed:28483977). {ECO:0000269|PubMed:20074521, ECO:0000269|PubMed:28483977, ECO:0000269|PubMed:34996871, ECO:0000269|PubMed:38305685, ECO:0000269|PubMed:38609661}.
uniprot
proteins
mass_dalton
50433
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
14702039
uniprot
proteins
pubmed
14736079
uniprot
proteins
pubmed
15489334
uniprot
proteins
pubmed
15616553
uniprot
proteins
pubmed
16371510
uniprot
proteins
pubmed
19524510
uniprot
proteins
pubmed
20074521
uniprot
proteins
pubmed
20191564
uniprot
proteins
pubmed
20829227
uniprot
proteins
pubmed
24374158
uniprot
proteins
pubmed
26875866
uniprot
proteins
pubmed
28483977
uniprot
proteins
pubmed
33894126
uniprot
proteins
pubmed
34996871
uniprot
proteins
pubmed
35482892
uniprot
proteins
pubmed
38305685
uniprot
proteins
pubmed
38609661
uniprot
proteins
pubmed
9473684
uniprot
proteins
sequence_length
450
uniprot
proteins
subcellular_location
SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton {ECO:0000269|PubMed:34996871, ECO:0000269|PubMed:35482892}. Cell projection, growth cone {ECO:0000250|UniProtKB:Q9ERD7}. Cell projection, lamellipodium {ECO:0000250|UniProtKB:Q9ERD7}. Cell projection, filopodium {ECO:0000250|UniProtKB:Q9ERD7}.
uniprot
proteins