Tubb3
entrez
22152
canonical
uniprot
Q9ERD7
canonical
ensembl
ENSMUSG00000062380
resolver
ensp
ENSMUSP00000071134
resolver
enst
ENSMUST00000071134
resolver
genesymbol
Tubb3
resolver
uniprot
Q3UF42
resolver
uniprot
Q5I036
resolver
uniprot_entry
TBB3_MOUSE
resolver
uniprot_sec
Q3UF42
resolver
uniprot_sec
Q5I036
resolver
amino_acid_sequence
MREIVHIQAGQCGNQIGAKFWEVISDEHGIDPSGNYVGDSDLQLERISVYYNEASSHKYVPRAILVDLEPGTMDSVRSGAFGHLFRPDNFIFGQSGAGNNWAKGHYTEGAELVDSVLDVVRKECENCDCLQGFQLTHSLGGGTGSGMGTLLISKVREEYPDRIMNTFSVVPSPKVSDTVVEPYNATLSIHQLVENTDETYCIDNEALYDICFRTLKLATPTYGDLNHLVSATMSGVTTSLRFPGQLNADLRKLAVNMVPFPRLHFFMPGFAPLTARGSQQYRALTVPELTQQMFDAKNMMAACDPRHGRYLTVATVFRGRMSMKEVDEQMLAIQSKNSSYFVEWIPNNVKVAVCDIPPRGLKMSSTFIGNSTAIQELFKRISEQFTAMFRRKAFLHWYTGEGMDEMEFTEAESNMNDLVSEYQQYQDATAEEEGEMYEDDDEESEAQGPK
uniprot
proteins
function
FUNCTION: Tubulin is the major constituent of microtubules, protein filaments consisting of alpha- and beta-tubulin heterodimers (By similarity). Microtubules grow by the addition of GTP-tubulin dimers to the microtubule end, where a stabilizing cap forms (By similarity). Below the cap, alpha-beta tubulin heterodimers are in GDP-bound state, owing to GTPase activity of alpha-tubulin (By similarity). 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 (By similarity). {ECO:0000250|UniProtKB:Q13509, ECO:0000269|PubMed:20074521, ECO:0000269|PubMed:28483977}.
uniprot
proteins
mass_dalton
50419
uniprot
proteins
mutagenesis
MUTAGEN 262; /note="R->C: Brain from homozygous mice shows defects in the guidance of commissural axons and nerves, without evidence of cortical cells migration defects."; /evidence="ECO:0000269|PubMed:20074521
uniprot
proteins
post_translational_modification
PTM: Some glutamate residues at the C-terminus are polyglycylated, resulting in polyglycine chains on the gamma-carboxyl group. Glycylation is mainly limited to tubulin incorporated into axonemes (cilia and flagella) whereas glutamylation is prevalent in neuronal cells, centrioles, axonemes, and the mitotic spindle. Both modifications can coexist on the same protein on adjacent residues, and lowering polyglycylation levels increases polyglutamylation, and reciprocally. Cilia and flagella glycylation is required for their stability and maintenance. Flagella glycylation controls sperm motility (PubMed:33414192). {ECO:0000269|PubMed:19524510, ECO:0000269|PubMed:23897886, ECO:0000269|PubMed:33414192}.; PTM: Some glutamate residues at the C-terminus are polyglutamylated, resulting in polyglutamate chains on the gamma-carboxyl group (PubMed:15890843). 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 (By similarity). Glutamylation is also involved in cilia motility (PubMed:23897886). {ECO:0000250|UniProtKB:Q71U36, ECO:0000269|PubMed:15890843, ECO:0000269|PubMed:23897886}.; 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
15489334
uniprot
proteins
pubmed
15890843
uniprot
proteins
pubmed
16141072
uniprot
proteins
pubmed
16371510
uniprot
proteins
pubmed
19524510
uniprot
proteins
pubmed
20074521
uniprot
proteins
pubmed
21183079
uniprot
proteins
pubmed
23897886
uniprot
proteins
pubmed
28483977
uniprot
proteins
pubmed
33414192
uniprot
proteins
pubmed
34792097
uniprot
proteins
sequence_length
450
uniprot
proteins
subcellular_location
SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton {ECO:0000269|PubMed:20074521}. Cell projection, growth cone {ECO:0000269|PubMed:28483977}. Cell projection, lamellipodium {ECO:0000269|PubMed:28483977}. Cell projection, filopodium {ECO:0000269|PubMed:28483977}.
uniprot
proteins