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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"}],"commentType":"FUNCTION"},{"commentType":"COFACTOR","cofactors":[{"name":"Mg(2+)","evidences":[{"evidenceCode":"ECO:0000250","source":"UniProtKB","id":"P68363"}],"cofactorCrossReference":{"database":"ChEBI","id":"CHEBI:18420"}}]},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000250","source":"UniProtKB","id":"P69893"},{"evidenceCode":"ECO:0000250","source":"UniProtKB","id":"P99024"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"20643351"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"23325789"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"26637975"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"31727855"}],"value":"Heterodimer of alpha and beta chains (PubMed:26637975). 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Nascent tubulin polypeptide interacts (via beta-tubulin MREI motif) with TTC5/STRAP; this interaction results in tubulin mRNA-targeted degradation (PubMed:31727855)"}],"commentType":"SUBUNIT"},{"commentType":"INTERACTION","interactions":[{"interactantOne":{"uniProtKBAccession":"P07437","intActId":"EBI-350864"},"interactantTwo":{"uniProtKBAccession":"P05067","geneName":"APP","intActId":"EBI-77613"},"numberOfExperiments":5,"organismDiffer":false},{"interactantOne":{"uniProtKBAccession":"P07437","intActId":"EBI-350864"},"interactantTwo":{"uniProtKBAccession":"P27797","geneName":"CALR","intActId":"EBI-1049597"},"numberOfExperiments":3,"organismDiffer":false},{"interactantOne":{"uniProtKBAccession":"P07437","intActId":"EBI-350864"},"interactantTwo":{"uniProtKBAccession":"P36957","geneName":"DLST","intActId":"EBI-351007"},"numberOfExperiments":3,"organismDiffer":false},{"interactantOne":{"uniProtKBAccession":"P07437","intActId":"EBI-350864"},"interactantTwo":{"uniProtKBAccession":"P51114","geneName":"FXR1","intActId":"EBI-713291"},"numberOfExperiments":2,"organismDiffer":false},{"interactantOne":{"uniProtKBAccession":"P07437","intActId":"EBI-350864"},"interactantTwo":{"uniProtKBAccession":"P42858","geneName":"HTT","intActId":"EBI-466029"},"numberOfExperiments":9,"organismDiffer":false},{"interactantOne":{"uniProtKBAccession":"P07437","intActId":"EBI-350864"},"interactantTwo":{"uniProtKBAccession":"P05412","geneName":"JUN","intActId":"EBI-852823"},"numberOfExperiments":3,"organismDiffer":false},{"interactantOne":{"uniProtKBAccession":"P07437","intActId":"EBI-350864"},"interactantTwo":{"uniProtKBAccession":"Q5S007","geneName":"LRRK2","intActId":"EBI-5323863"},"numberOfExperiments":6,"organismDiffer":false},{"interactantOne":{"uniProtKBAccession":"P07437","intActId":"EBI-350864"},"interactantTwo":{"uniProtKBAccession":"P10636-8","geneName":"MAPT","intActId":"EBI-366233"},"numberOfExperiments":4,"organismDiffer":false},{"interactantOne":{"uniProtKBAccession":"P07437","intActId":"EBI-350864"},"interactantTwo":{"uniProtKBAccession":"P19404","geneName":"NDUFV2","intActId":"EBI-713665"},"numberOfExperiments":3,"organismDiffer":false},{"interactantOne":{"uniProtKBAccession":"P07437","intActId":"EBI-350864"},"interactantTwo":{"uniProtKBAccession":"Q15843","geneName":"NEDD8","intActId":"EBI-716247"},"numberOfExperiments":4,"organismDiffer":false},{"interactantOne":{"uniProtKBAccession":"P07437","intActId":"EBI-350864"},"interactantTwo":{"uniProtKBAccession":"I6L9F6","geneName":"NEFL","intActId":"EBI-10178578"},"numberOfExperiments":3,"organismDiffer":false},{"interactantOne":{"uniProtKBAccession":"P07437","intActId":"EBI-350864"},"interactantTwo":{"uniProtKBAccession":"Q8TDX7","geneName":"NEK7","intActId":"EBI-1055945"},"numberOfExperiments":3,"organismDiffer":false},{"interactantOne":{"uniProtKBAccession":"P07437","intActId":"EBI-350864"},"interactantTwo":{"uniProtKBAccession":"P37840","geneName":"SNCA","intActId":"EBI-985879"},"numberOfExperiments":3,"organismDiffer":false},{"interactantOne":{"uniProtKBAccession":"P07437","intActId":"EBI-350864"},"interactantTwo":{"uniProtKBAccession":"P00441","geneName":"SOD1","intActId":"EBI-990792"},"numberOfExperiments":3,"organismDiffer":false},{"interactantOne":{"uniProtKBAccession":"P07437","intActId":"EBI-350864"},"interactantTwo":{"uniProtKBAccession":"Q13501","geneName":"SQSTM1","intActId":"EBI-307104"},"numberOfExperiments":4,"organismDiffer":false},{"interactantOne":{"uniProtKBAccession":"P07437","intActId":"EBI-350864"},"interactantTwo":{"uniProtKBAccession":"Q03403","geneName":"TFF2","intActId":"EBI-4314702"},"numberOfExperiments":3,"organismDiffer":false},{"interactantOne":{"uniProtKBAccession":"P07437","intActId":"EBI-350864"},"interactantTwo":{"uniProtKBAccession":"Q9BSI4","geneName":"TINF2","intActId":"EBI-717399"},"numberOfExperiments":2,"organismDiffer":false},{"interactantOne":{"uniProtKBAccession":"P07437","intActId":"EBI-350864"},"interactantTwo":{"uniProtKBAccession":"Q71U36","geneName":"TUBA1A","intActId":"EBI-302552"},"numberOfExperiments":5,"organismDiffer":false},{"interactantOne":{"uniProtKBAccession":"P07437","intActId":"EBI-350864"},"interactantTwo":{"uniProtKBAccession":"Q8AZK7","geneName":"EBNA-LP","intActId":"EBI-1185167"},"numberOfExperiments":3,"organismDiffer":true}]},{"commentType":"SUBCELLULAR LOCATION","subcellularLocations":[{"location":{"evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"26637975"}],"value":"Cytoplasm, cytoskeleton","id":"SL-0090"}}]},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"20191564"}],"value":"Ubiquitously expressed with highest levels in spleen, thymus and immature brain"}],"commentType":"TISSUE SPECIFICITY"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"31727855"}],"value":"Autoregulated by feedback control of mRNA degradation (PubMed:31727855). 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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)"}],"commentType":"PTM"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"28576883"},{"evidenceCode":"ECO:0000305","source":"PubMed","id":"19524510"}],"value":"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). 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