Tuba8
entrez
53857
canonical
uniprot
Q9JJZ2
canonical
ensembl
ENSMUSG00000030137
resolver
ensp
ENSMUSP00000032233
resolver
enst
ENSMUST00000032233
resolver
genesymbol
Tuba8
resolver
uniprot
D4P911
resolver
uniprot
Q9CV57
resolver
uniprot_entry
TBA8_MOUSE
resolver
uniprot_sec
D4P911
resolver
uniprot_sec
Q9CV57
resolver
amino_acid_sequence
MRECISVHVGQAGVQIGNACWELFCLEHGIQADGTFGTQASKINDDDSFTTFFSETGNGKHVPRAVMVDLEPTVVDEVRAGTYRQLFHPEQLITGKEDAANNYARGHYTVGKESIDLVLDRIRKLTDACSGLQGFLIFHSFGGGTGSGFTSLLMERLSLDYGKKSKLEFAIYPAPQVSTAVVEPYNSILTTHTTLEHSDCAFMVDNEAIYDICRRNLDIERPTYTNLNRLISQIVSSITASLRFDGALNVDLTEFQTNLVPYPRIHFPLVTYAPIISAEKAYHEQLSVAEITSSCFEPNSQMVKCDPRHGKYMACCMLYRGDVVPKDVNVAIAAIKTKRTIQFVDWCPTGFKVGINYQPPTVVPGGDLAKVQRAVCMLSNTTAIAEAWARLDHKFDLMYAKRAFVHWYVGEGMEEGEFSEAREDLAALEKDYEEVGTDSFEEENEGEEF
uniprot
proteins
ec_number
3.6.5.-
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
50052
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: The C-terminal phenylalanine residue is cleaved by MATCAP1/KIAA0895L. {ECO:0000250|UniProtKB:Q9NY65}.
uniprot
proteins
protein_family
Tubulin family
uniprot
proteins
pubmed
10772959
uniprot
proteins
pubmed
15489334
uniprot
proteins
pubmed
15890843
uniprot
proteins
pubmed
16141072
uniprot
proteins
pubmed
19524510
uniprot
proteins
pubmed
19896110
uniprot
proteins
pubmed
20466094
uniprot
proteins
pubmed
21183079
uniprot
proteins
pubmed
23897886
uniprot
proteins
pubmed
33414192
uniprot
proteins
sequence_length
449
uniprot
proteins
subcellular_location
SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton.
uniprot
proteins