TUBB2A
entrez
7280
canonical
uniprot
Q13885
canonical
ensembl
ENSG00000137267
resolver
ensp
ENSP00000369703
resolver
enst
ENST00000333628
resolver
genesymbol
TUBB2A
resolver
genesymbol_syn
TUBB2
resolver
hgnc
HGNC:12412
resolver
uniprot
Q6FGZ8
resolver
uniprot
Q8IWR2
resolver
uniprot_entry
TBB2A_HUMAN
resolver
uniprot_sec
Q6FGZ8
resolver
uniprot_sec
Q8IWR2
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:0000250|UniProtKB:Q7TMM9}.
uniprot
proteins
amino_acid_sequence
MREIVHIQAGQCGNQIGAKFWEVISDEHGIDPTGSYHGDSDLQLERINVYYNEAAGNKYVPRAILVDLEPGTMDSVRSGPFGQIFRPDNFVFGQSGAGNNWAKGHYTEGAELVDSVLDVVRKESESCDCLQGFQLTHSLGGGTGSGMGTLLISKIREEYPDRIMNTFSVMPSPKVSDTVVEPYNATLSVHQLVENTDETYSIDNEALYDICFRTLKLTTPTYGDLNHLVSATMSGVTTCLRFPGQLNADLRKLAVNMVPFPRLHFFMPGFAPLTSRGSQQYRALTVPELTQQMFDSKNMMAACDPRHGRYLTVAAIFRGRMSMKEVDEQMLNVQNKNSSYFVEWIPNNVKTAVCDIPPRGLKMSATFIGNSTAIQELFKRISEQFTAMFRRKAFLHWYTGEGMDEMEFTEAESNMNDLVSEYQQYQDATADEQGEFEEEEGEDEA
uniprot
proteins
disease_involvement
DISEASE: Cortical dysplasia, complex, with other brain malformations 5 (CDCBM5) [MIM:615763]: A disorder of aberrant neuronal migration and disturbed axonal guidance. Clinical features include seizures, global developmental delay, and various brain malformations such as a diffuse simplified gyral pattern with reduced volume of white matter, globular basal ganglia, thin and dysmorphic corpus callosum, mild brainstem hypoplasia with a flat pons, mild cerebellar vermis hypoplasia, and mildly enlarged posterior fossa. {ECO:0000269|PubMed:24702957}. 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
49907
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
14574404
uniprot
proteins
pubmed
15489334
uniprot
proteins
pubmed
16371510
uniprot
proteins
pubmed
16959974
uniprot
proteins
pubmed
19131338
uniprot
proteins
pubmed
19524510
uniprot
proteins
pubmed
20191564
uniprot
proteins
pubmed
21269460
uniprot
proteins
pubmed
24702957
uniprot
proteins
pubmed
26875866
uniprot
proteins
sequence_length
445
uniprot
proteins
subcellular_location
SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton {ECO:0000250}.
uniprot
proteins