TUBB2B
entrez
347733
canonical
uniprot
Q9BVA1
canonical
ensembl
ENSG00000137285
resolver
ensp
ENSP00000259818
resolver
enst
ENST00000259818
resolver
genesymbol
TUBB2B
resolver
hgnc
HGNC:30829
resolver
uniprot
A0A384MEE3
resolver
uniprot
A8K068
resolver
uniprot_entry
A0A384MEE3_HUMAN
resolver
uniprot_entry
TBB2B_HUMAN
resolver
uniprot_sec
A8K068
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:Q9CWF2}.
uniprot
proteins
amino_acid_sequence
MREIVHIQAGQCGNQIGAKFWEVISDEHGIDPTGSYHGDSDLQLERINVYYNEATGNKYVPRAILVDLEPGTMDSVRSGPFGQIFRPDNFVFGQSGAGNNWAKGHYTEGAELVDSVLDVVRKESESCDCLQGFQLTHSLGGGTGSGMGTLLISKIREEYPDRIMNTFSVMPSPKVSDTVVEPYNATLSVHQLVENTDETYCIDNEALYDICFRTLKLTTPTYGDLNHLVSATMSGVTTCLRFPGQLNADLRKLAVNMVPFPRLHFFMPGFAPLTSRGSQQYRALTVPELTQQMFDSKNMMAACDPRHGRYLTVAAIFRGRMSMKEVDEQMLNVQNKNSSYFVEWIPNNVKTAVCDIPPRGLKMSATFIGNSTAIQELFKRISEQFTAMFRRKAFLHWYTGEGMDEMEFTEAESNMNDLVSEYQQYQDATADEQGEFEEEEGEDEA
uniprot
proteins
disease_involvement
DISEASE: Cortical dysplasia, complex, with other brain malformations 7 (CDCBM7) [MIM:610031]: A malformation of the cortex in which the brain surface is irregular and characterized by an excessive number of small gyri with abnormal lamination. Polymicrogyria is a heterogeneous disorder, considered to be the result of postmigratory abnormal cortical organization. {ECO:0000269|PubMed:19465910, ECO:0000269|PubMed:22333901, ECO:0000269|PubMed:23001566, ECO:0000269|PubMed:26732629}. Note=The disease is caused by variants affecting the gene represented in this entry.; DISEASE: Note=Defects in TUBB2B may be involved in cerebellar ataxia, intellectual disability, and dysequilibrium syndrome (CAMRQ). {ECO:0000269|PubMed:28013290}.
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 (PubMed:23001566, PubMed:26732629, PubMed:28013290). 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. Plays a critical role in proper axon guidance in both central and peripheral axon tracts (PubMed:23001566). Implicated in neuronal migration (PubMed:19465910). {ECO:0000269|PubMed:19465910, ECO:0000269|PubMed:23001566, ECO:0000269|PubMed:26732629, ECO:0000269|PubMed:28013290}.
uniprot
proteins
mass_dalton
49953
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
14702039
uniprot
proteins
pubmed
15489334
uniprot
proteins
pubmed
16371510
uniprot
proteins
pubmed
19465910
uniprot
proteins
pubmed
19524510
uniprot
proteins
pubmed
20191564
uniprot
proteins
pubmed
21269460
uniprot
proteins
pubmed
22333901
uniprot
proteins
pubmed
23001566
uniprot
proteins
pubmed
26732629
uniprot
proteins
pubmed
26875866
uniprot
proteins
pubmed
28013290
uniprot
proteins
sequence_length
445
uniprot
proteins
subcellular_location
SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton {ECO:0000269|PubMed:23001566, ECO:0000269|PubMed:28013290}.
uniprot
proteins