TUBB8
entrez
347688
canonical
uniprot
Q3ZCM7
canonical
ensembl
ENSG00000261456
resolver
ensp
ENSP00000456206
resolver
enst
ENST00000568584
resolver
genesymbol
TUBB8
resolver
hgnc
HGNC:20773
resolver
uniprot
Q5SQX9
resolver
uniprot
Q8WZ78
resolver
uniprot_entry
TBB8_HUMAN
resolver
uniprot_sec
Q5SQX9
resolver
uniprot_sec
Q8WZ78
resolver
amino_acid_sequence
MREIVLTQIGQCGNQIGAKFWEVISDEHAIDSAGTYHGDSHLQLERINVYYNEASGGRYVPRAVLVDLEPGTMDSVRSGPFGQVFRPDNFIFGQCGAGNNWAKGHYTEGAELMESVMDVVRKEAESCDCLQGFQLTHSLGGGTGSGMGTLLLSKIREEYPDRIINTFSILPSPKVSDTVVEPYNATLSVHQLIENADETFCIDNEALYDICSKTLKLPTPTYGDLNHLVSATMSGVTTCLRFPGQLNADLRKLAVNMVPFPRLHFFMPGFAPLTSRGSQQYRALTVAELTQQMFDAKNMMAACDPRHGRYLTAAAIFRGRMPMREVDEQMFNIQDKNSSYFADWLPNNVKTAVCDIPPRGLKMSATFIGNNTAIQELFKRVSEQFTAMFRRKAFLHWYTGEGMDEMEFTEAESNMNDLVSEYQQYQDATAEEEEDEEYAEEEVA
uniprot
proteins
disease_involvement
DISEASE: Oocyte/zygote/embryo maturation arrest 2 (OZEMA2) [MIM:616780]: A primary infertility disorder caused by defective oocyte maturation. Oocytes are arrested at metaphase I, and have an abnormal or no detectable spindle on polarization microscopy. OOMD2 inheritance can be autosomal dominant or autosomal recessive. {ECO:0000269|PubMed:26789871, ECO:0000269|PubMed:27273344, ECO:0000269|PubMed:32316999, ECO:0000269|PubMed:34509376}. 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. TUBB8 has a key role in meiotic spindle assembly and oocyte maturation (PubMed:26789871, PubMed:34509376). {ECO:0000269|PubMed:26789871, ECO:0000269|PubMed:34509376}.
uniprot
proteins
mass_dalton
49776
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
11731935
uniprot
proteins
pubmed
15164054
uniprot
proteins
pubmed
15489334
uniprot
proteins
pubmed
16371510
uniprot
proteins
pubmed
19524510
uniprot
proteins
pubmed
21269460
uniprot
proteins
pubmed
26789871
uniprot
proteins
pubmed
26875866
uniprot
proteins
pubmed
27273344
uniprot
proteins
pubmed
32316999
uniprot
proteins
pubmed
34509376
uniprot
proteins
sequence_length
444
uniprot
proteins
subcellular_location
SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton {ECO:0000269|PubMed:26789871}. Cytoplasm, cytoskeleton, spindle {ECO:0000269|PubMed:26789871}.
uniprot
proteins