TUBB
entrez
203068
canonical
uniprot
P07437
canonical
ensembl
ENSG00000183311
resolver
ensembl
ENSG00000196230
resolver
ensembl
ENSG00000224156
resolver
ensembl
ENSG00000227739
resolver
ensembl
ENSG00000229684
resolver
ensembl
ENSG00000232421
resolver
ensembl
ENSG00000232575
resolver
ensembl
ENSG00000235067
resolver
ensp
ENSP00000339001
resolver
ensp
ENSP00000365578
resolver
ensp
ENSP00000373058
resolver
ensp
ENSP00000379668
resolver
ensp
ENSP00000379672
resolver
ensp
ENSP00000383374
resolver
ensp
ENSP00000383375
resolver
ensp
ENSP00000391515
resolver
ensp
ENSP00000392914
resolver
ensp
ENSP00000393340
resolver
ensp
ENSP00000394124
resolver
ensp
ENSP00000394841
resolver
ensp
ENSP00000395838
resolver
ensp
ENSP00000399046
resolver
ensp
ENSP00000399155
resolver
ensp
ENSP00000400663
resolver
ensp
ENSP00000401317
resolver
ensp
ENSP00000403213
resolver
ensp
ENSP00000406811
resolver
ensp
ENSP00000406981
resolver
ensp
ENSP00000407673
resolver
ensp
ENSP00000410071
resolver
ensp
ENSP00000410829
resolver
ensp
ENSP00000414479
resolver
ensp
ENSP00000416480
resolver
ensp
ENSP00000506665
resolver
ensp
ENSP00000746233
resolver
enst
ENST00000327892
resolver
enst
ENST00000330914
resolver
enst
ENST00000383564
resolver
enst
ENST00000396384
resolver
enst
ENST00000400530
resolver
enst
ENST00000400531
resolver
enst
ENST00000413547
resolver
enst
ENST00000419792
resolver
enst
ENST00000420618
resolver
enst
ENST00000421473
resolver
enst
ENST00000422650
resolver
enst
ENST00000422674
resolver
enst
ENST00000425102
resolver
enst
ENST00000427480
resolver
enst
ENST00000432462
resolver
enst
ENST00000435546
resolver
enst
ENST00000436335
resolver
enst
ENST00000436628
resolver
enst
ENST00000437490
resolver
enst
ENST00000444441
resolver
enst
ENST00000446385
resolver
enst
ENST00000453350
resolver
enst
ENST00000454454
resolver
enst
ENST00000454620
resolver
enst
ENST00000681435
resolver
genesymbol
TUBB
resolver
genesymbol_syn
TUBB5
resolver
hgnc
HGNC:20778
resolver
uniprot
B4DMJ5
resolver
uniprot
B4DQN9
resolver
uniprot
B4DY90
resolver
uniprot
P05218
resolver
uniprot
Q5ST81
resolver
uniprot
Q5SU16
resolver
uniprot
Q8WUC1
resolver
uniprot
Q9CY33
resolver
uniprot_entry
B4DMJ5_HUMAN
resolver
uniprot_entry
B4DQN9_HUMAN
resolver
uniprot_entry
B4DY90_HUMAN
resolver
uniprot_entry
Q5ST81_HUMAN
resolver
uniprot_entry
Q5SU16_HUMAN
resolver
uniprot_entry
TBB5_HUMAN
resolver
uniprot_sec
P05218
resolver
uniprot_sec
Q8WUC1
resolver
uniprot_sec
Q9CY33
resolver
amino_acid_sequence
MREIVHIQAGQCGNQIGAKFWEVISDEHGIDPTGTYHGDSDLQLDRISVYYNEATGGKYVPRAILVDLEPGTMDSVRSGPFGQIFRPDNFVFGQSGAGNNWAKGHYTEGAELVDSVLDVVRKEAESCDCLQGFQLTHSLGGGTGSGMGTLLISKIREEYPDRIMNTFSVVPSPKVSDTVVEPYNATLSVHQLVENTDETYCIDNEALYDICFRTLKLTTPTYGDLNHLVSATMSGVTTCLRFPGQLNADLRKLAVNMVPFPRLHFFMPGFAPLTSRGSQQYRALTVPELTQQVFDAKNMMAACDPRHGRYLTVAAVFRGRMSMKEVDEQMLNVQNKNSSYFVEWIPNNVKTAVCDIPPRGLKMAVTFIGNSTAIQELFKRISEQFTAMFRRKAFLHWYTGEGMDEMEFTEAESNMNDLVSEYQQYQDATAEEEEDFGEEAEEEA
uniprot
proteins
disease_involvement
DISEASE: Cortical dysplasia, complex, with other brain malformations 6 (CDCBM6) [MIM:615771]: A disorder of aberrant neuronal migration and disturbed axonal guidance. Affected individuals have microcephaly, ataxia, and severe delayed psychomotor development. Brain imaging shows variable malformations of cortical development, including white matter streaks, dysmorphic basal ganglia, corpus callosum abnormalities, brainstem and cerebellar hypoplasia, cortical dysplasia, polymicrogyria. {ECO:0000269|PubMed:23246003}. Note=The disease is caused by variants affecting the gene represented in this entry.; DISEASE: Skin creases, congenital symmetric circumferential, 1 (CSCSC1) [MIM:156610]: An autosomal dominant disease characterized by multiple, symmetric, circumferential rings of folded skin, affecting primarily the limbs. Affected individuals also exhibit intellectual disability, cleft palate, and dysmorphic features. {ECO:0000269|PubMed:26637975}. 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
49671
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, PubMed:28576883). 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, ECO:0000269|PubMed:28576883}.; 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 (Probable) (PubMed:28576883). Both polyglutamylation and monoglycylation can coexist on the same protein on adjacent residues, and lowering glycylation levels increases polyglutamylation, and reciprocally (Probable) (PubMed:28576883). {ECO:0000269|PubMed:28576883, 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
11504633
uniprot
proteins
pubmed
15489334
uniprot
proteins
pubmed
15592455
uniprot
proteins
pubmed
16371510
uniprot
proteins
pubmed
19524510
uniprot
proteins
pubmed
19608861
uniprot
proteins
pubmed
20191564
uniprot
proteins
pubmed
20643351
uniprot
proteins
pubmed
21269460
uniprot
proteins
pubmed
23186163
uniprot
proteins
pubmed
23246003
uniprot
proteins
pubmed
23325789
uniprot
proteins
pubmed
24275569
uniprot
proteins
pubmed
25944712
uniprot
proteins
pubmed
26637975
uniprot
proteins
pubmed
26875866
uniprot
proteins
pubmed
28576883
uniprot
proteins
pubmed
31727855
uniprot
proteins
pubmed
32747782
uniprot
proteins
pubmed
6688039
uniprot
proteins
pubmed
6865944
uniprot
proteins
sequence_length
444
uniprot
proteins
subcellular_location
SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton {ECO:0000269|PubMed:26637975}.
uniprot
proteins