{ "uniprot_canonical_ac": "A2AQ07-1", "ptm_annotation": [ { "annotation": "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.", "evidence": [ { "url": "https://www.uniprot.org/uniprot/A2AQ07", "id": "A2AQ07", "database": "UniProtKB" }, { "url": "https://www.ncbi.nlm.nih.gov/pubmed/P68371", "id": "P68371", "database": "PubMed" }, { "url": "https://www.ncbi.nlm.nih.gov/pubmed/Q13885", "id": "Q13885", "database": "PubMed" }, { "url": "https://www.ncbi.nlm.nih.gov/pubmed/Q9BUF5", "id": "Q9BUF5", "database": "PubMed" }, { "url": "https://www.ncbi.nlm.nih.gov/pubmed/Q9BVA1", "id": "Q9BVA1", "database": "PubMed" }, { "url": "https://www.ncbi.nlm.nih.gov/pubmed/16371510", "id": "16371510", "database": "PubMed" }, { "url": "https://www.ncbi.nlm.nih.gov/pubmed/Q9H4B7", "id": "Q9H4B7", "database": "PubMed" }, { "url": "https://www.ncbi.nlm.nih.gov/pubmed/P04350", "id": "P04350", "database": "PubMed" } ] }, { "annotation": "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).", "evidence": [ { "url": "https://www.uniprot.org/uniprot/A2AQ07", "id": "A2AQ07", "database": "UniProtKB" }, { "url": "https://www.ncbi.nlm.nih.gov/pubmed/Q71U36", "id": "Q71U36", "database": "PubMed" }, { "url": "https://www.ncbi.nlm.nih.gov/pubmed/15890843", "id": "15890843", "database": "PubMed" } ] }, { "annotation": "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. The precise function of polyglycylation is still unclear.", "evidence": [ { "url": "https://www.uniprot.org/uniprot/A2AQ07", "id": "A2AQ07", "database": "UniProtKB" }, { "url": "https://www.ncbi.nlm.nih.gov/pubmed/19524510", "id": "19524510", "database": "PubMed" }, { "url": "https://www.ncbi.nlm.nih.gov/pubmed/P68369", "id": "P68369", "database": "PubMed" } ] } ], "sequence": { "header": "sp|A2AQ07-1|TBB1_MOUSE Isoform 1 of Tubulin beta-1 chain OS=Mus musculus OX=10090 GN=Tubb1 PE=1 SV=1 CANONICAL=A2AQ07-1", "length": 451, "sequence": "MREIVHIQIGQCGNQIGAKFWEVIGEEHGIDCAGSYCGTSALQLERISVYYNEAYGKKYVPRAVLVDLEPGTMDSIRSSRLGVLFQPDSFVHGNSGAGNNWAKGHYTEGAELIENVMDVVRRESESCDCLQGFQIVHSLGGGTGSGMGTLLMNKIREEYPDRILNSFSVMPSPKVSDTVVEPYNAVLSIHQLIENTDACFCIDNEALYDICFRTLRLTTPTYGDLNHLVSLTMSGITTSLRFPGQLNADLRKLAVNMVPFPRLHFFMPGFAPLTAQGSQQYRALSVAELTQQMFDARNIMAACDPRRGRYLTVACIFRGKMSTKEVDQQLLSIQTRNSNCFVEWIPNNVKVAVCDIPPRGLNMAATFLGNNTAIQELFTRVSEHFSAMFRRRAFVHWYTSEGMDISEFGEAESDIHDLVSEYQQFQDVRAGLEDSEEDVEEAEVEAEDKDH" }, "uniprot_id": "TBB1_MOUSE", "enzyme_annotation": [], "glycation": [], "keywords": [], "species": [ { "common_name": "Mouse", "taxid": 10090, "name": "Mus musculus", "evidence": [ { "url": "https://www.uniprot.org/uniprot/A2AQ07", "id": "A2AQ07", "database": "UniProtKB" } ] } ], "crossref_internal": { "gene": [ "Tubb1" ], "site": [ "A2AQ07-1.435.435", "A2AQ07-1.370.372", "A2AQ07-1.172.172" ], "species": [ 10090 ] }, "publication": [ { "reference": [ { "url": "https://www.ncbi.nlm.nih.gov/pubmed/10942379", "type": [ "PubMed" ], "id": "10942379" } ], "title": "Hematopoietic-specific beta 1 tubulin participates in a pathway of platelet biogenesis dependent on the transcription factor NF-E2.", "journal": "Blood", "evidence": [ { "url": "https://www.ncbi.nlm.nih.gov/protein/NP_001074440.1", "id": "NP_001074440.1", "database": "RefSeq" } ], "authors": "Lecine P, Italiano JE Jr, Kim SW, Villeval JL, Shivdasani RA", "date": "2000" }, { "reference": [ { "url": "https://www.ncbi.nlm.nih.gov/pubmed/11369202", "type": [ "PubMed" ], "id": "11369202" } ], "title": "A lineage-restricted and divergent beta-tubulin isoform is essential for the biogenesis, structure and function of blood platelets.", "journal": "Current biology : CB", "evidence": [ { "url": "https://www.ncbi.nlm.nih.gov/protein/NP_001074440.1", "id": "NP_001074440.1", "database": "RefSeq" } ], "authors": "Schwer HD, Lecine P, Tiwari S, Italiano JE Jr, Hartwig JH, Shivdasani RA", "date": "2001" }, { "reference": [ { "url": "https://www.ncbi.nlm.nih.gov/pubmed/12586623", "type": [ "PubMed" ], "id": "12586623" } ], "title": "Mechanisms and implications of platelet discoid shape.", "journal": "Blood", "evidence": [ { "url": "https://www.ncbi.nlm.nih.gov/protein/NP_001074440.1", "id": "NP_001074440.1", "database": "RefSeq" } ], "authors": "Italiano JE Jr, Bergmeier W, Tiwari S, Falet H, Hartwig JH, Hoffmeister KM, Andre P, Wagner DD, Shivdasani RA", "date": "2003" }, { "reference": [ { "url": "https://www.ncbi.nlm.nih.gov/pubmed/15121885", "type": [ "PubMed" ], "id": "15121885" } ], "title": "A ubiquitous beta-tubulin disrupts microtubule assembly and inhibits cell proliferation.", "journal": "Molecular biology of the cell", "evidence": [ { "url": "https://www.ncbi.nlm.nih.gov/protein/NP_001074440.1", "id": "NP_001074440.1", "database": "RefSeq" } ], "authors": "Bhattacharya R, Cabral F", "date": "2004" }, { "reference": [ { "url": "https://www.ncbi.nlm.nih.gov/pubmed/15890843", "type": [ "PubMed" ], "id": "15890843" } ], "title": "Tubulin polyglutamylase enzymes are members of the TTL domain protein family.", "journal": "Science", "evidence": [ { "url": "https://www.uniprot.org/uniprot/A2AQ07", "id": "A2AQ07", "database": "UniProtKB" } ], "authors": "van Dorsselaer A., Strub J.-M., Gaertig J., Wloga D., Boucher D., Janke C., Regnard C., Kajava A.V., Rogowski K., van Dijk J., Edde B., Suryavanshi S., Temurak N.", "date": "2005" }, { "reference": [ { "url": "https://www.ncbi.nlm.nih.gov/pubmed/17242355", "type": [ "PubMed" ], "id": "17242355" } ], "title": "Large-scale phosphorylation analysis of mouse liver.", "journal": "Proc. Natl. Acad. Sci. U.S.A.", "evidence": [ { "url": "https://www.uniprot.org/uniprot/A2AQ07", "id": "A2AQ07", "database": "UniProtKB" } ], "authors": "Beausoleil S.A., Gerber S.A., Gygi S.P., Villen J.", "date": "2007" }, { "reference": [ { "url": "https://www.ncbi.nlm.nih.gov/pubmed/18347012", "type": [ "PubMed" ], "id": "18347012" } ], "title": "RanBP10 is a cytoplasmic guanine nucleotide exchange factor that modulates noncentrosomal microtubules.", "journal": "J. Biol. Chem.", "evidence": [ { "url": "https://www.uniprot.org/uniprot/A2AQ07", "id": "A2AQ07", "database": "UniProtKB" } ], "authors": "Shivdasani R.A., Italiano J.E. Jr., Korpal M., Dose M., Meyer I., Schulze H.", "date": "2008" }, { "reference": [ { "url": "https://www.ncbi.nlm.nih.gov/pubmed/19524510", "type": [ "PubMed" ], "id": "19524510" } ], "title": "Evolutionary divergence of enzymatic mechanisms for posttranslational polyglycylation.", "journal": "Cell", "evidence": [ { "url": "https://www.uniprot.org/uniprot/A2AQ07", "id": "A2AQ07", "database": "UniProtKB" } ], "authors": "Van Dorsselaer A., Strub J.-M., Thomas D., Gaertig J., Wloga D., Janke C., Rogowski K., van Dijk J., Bre M.-H., Juge F., Levilliers N.", "date": "2009" }, { "reference": [ { "url": "https://www.ncbi.nlm.nih.gov/pubmed/24960163", "type": [ "PubMed" ], "id": "24960163" } ], "title": "KLHL40 deficiency destabilizes thin filament proteins and promotes nemaline myopathy.", "journal": "The Journal of clinical investigation", "evidence": [ { "url": "https://www.ncbi.nlm.nih.gov/protein/NP_001074440.1", "id": "NP_001074440.1", "database": "RefSeq" } ], "authors": "Garg A, O'Rourke J, Long C, Doering J, Ravenscroft G, Bezprozvannaya S, Nelson BR, Beetz N, Li L, Chen S, Laing NG, Grange RW, Bassel-Duby R, Olson EN", "date": "2014" }, { "reference": [ { "url": "https://www.ncbi.nlm.nih.gov/pubmed/30110642", "type": [ "PubMed" ], "id": "30110642" } ], "title": "Neuronal-Specific TUBB3 Is Not Required for Normal Neuronal Function but Is Essential for Timely Axon Regeneration.", "journal": "Cell reports", "evidence": [ { "url": "https://www.ncbi.nlm.nih.gov/protein/NP_001074440.1", "id": "NP_001074440.1", "database": "RefSeq" } ], "authors": "Latremoliere A, Cheng L, DeLisle M, Wu C, Chew S, Hutchinson EB, Sheridan A, Alexandre C, Latremoliere F, Sheu SH, Golidy S, Omura T, Huebner EA, Fan Y, Whitman MC, Nguyen E, Hermawan C, Pierpaoli C, Tischfield MA, Woolf CJ, Engle EC", "date": "2018" }, { "reference": [ { "url": "https://www.ncbi.nlm.nih.gov/pubmed/30446499", "type": [ "PubMed" ], "id": "30446499" } ], "title": "TUBB1 mutations cause thyroid dysgenesis associated with abnormal platelet physiology.", "journal": "EMBO molecular medicine", "evidence": [ { "url": "https://www.ncbi.nlm.nih.gov/protein/NP_001074440.1", "id": "NP_001074440.1", "database": "RefSeq" } ], "authors": "Stoupa A, Adam F, Kariyawasam D, Strassel C, Gawade S, Szinnai G, Kauskot A, Lasne D, Janke C, Natarajan K, Schmitt A, Bole-Feysot C, Nitschke P, Leger J, Jabot-Hanin F, Tores F, Michel A, Munnich A, Besmond C, Scharfmann R, Lanza F, Borgel D, Polak M, Carre A", "date": "2018" } ], "uniprot_ac": "A2AQ07", "site_annotation": [ { "end_pos": 372, "annotation": "n_glycosylation_sequon", "start_pos": 370 } ], "isoforms": [ { "url": "https://www.uniprot.org/uniprot/A2AQ07#A2AQ07-1", "isoform_ac": "A2AQ07-1", "sequence": { "header": "sp|A2AQ07-1|TBB1_MOUSE Isoform 1 of Tubulin beta-1 chain OS=Mus musculus OX=10090 GN=Tubb1 PE=1 SV=1 CANONICAL=A2AQ07-1", "length": 451, "sequence": "MREIVHIQIGQCGNQIGAKFWEVIGEEHGIDCAGSYCGTSALQLERISVYYNEAYGKKYVPRAVLVDLEPGTMDSIRSSRLGVLFQPDSFVHGNSGAGNNWAKGHYTEGAELIENVMDVVRRESESCDCLQGFQIVHSLGGGTGSGMGTLLMNKIREEYPDRILNSFSVMPSPKVSDTVVEPYNAVLSIHQLIENTDACFCIDNEALYDICFRTLRLTTPTYGDLNHLVSLTMSGITTSLRFPGQLNADLRKLAVNMVPFPRLHFFMPGFAPLTAQGSQQYRALSVAELTQQMFDARNIMAACDPRRGRYLTVACIFRGKMSTKEVDQQLLSIQTRNSNCFVEWIPNNVKVAVCDIPPRGLNMAATFLGNNTAIQELFTRVSEHFSAMFRRRAFVHWYTSEGMDISEFGEAESDIHDLVSEYQQFQDVRAGLEDSEEDVEEAEVEAEDKDH" }, "locus": { "chromosome": "2", "end_pos": 174450745, "start_pos": 174457879, "strand": "-", "evidence": [ { "url": "https://www.ensembl.org/id/ENSMUST00000016399", "id": "ENSMUST00000016399", "database": "Ensembl Transcript" }, { "url": "https://www.ensembl.org/id/ENSMUSP00000016399", "id": "ENSMUSP00000016399", "database": "Ensembl Peptide" } ] } } ], "pathway": [ { "url": "https://www.genome.jp/dbget-bin/get_linkdb?-t+pathway+mmu:545486", "resource": "KEGG Pathway", "id": "mmu:545486", "name": "" }, { "url": "https://www.reactome.org/PathwayBrowser/#R-MMU-190840", "resource": "Reactome", "id": "R-MMU-190840", "name": "Microtubule-dependent trafficking of connexons from Golgi to the plasma membrane" }, { "url": "https://www.reactome.org/PathwayBrowser/#R-MMU-2132295", "resource": "Reactome", "id": "R-MMU-2132295", "name": "MHC class II antigen presentation" }, { "url": "https://www.reactome.org/PathwayBrowser/#R-MMU-2467813", "resource": "Reactome", "id": "R-MMU-2467813", "name": "Separation of Sister Chromatids" }, { "url": "https://www.reactome.org/PathwayBrowser/#R-MMU-2500257", "resource": "Reactome", "id": "R-MMU-2500257", "name": "Resolution of Sister Chromatid Cohesion" }, { "url": "https://www.reactome.org/PathwayBrowser/#R-MMU-3371497", "resource": "Reactome", "id": "R-MMU-3371497", "name": "HSP90 chaperone cycle for steroid hormone receptors (SHR)" }, { "url": "https://www.reactome.org/PathwayBrowser/#R-MMU-380320", "resource": "Reactome", "id": "R-MMU-380320", "name": "Recruitment of NuMA to mitotic centrosomes" }, { "url": "https://www.reactome.org/PathwayBrowser/#R-MMU-437239", "resource": "Reactome", "id": "R-MMU-437239", "name": "Recycling pathway of L1" }, { "url": "https://www.reactome.org/PathwayBrowser/#R-MMU-5610787", "resource": "Reactome", "id": "R-MMU-5610787", "name": "Hedgehog 'off' state" }, { "url": "https://www.reactome.org/PathwayBrowser/#R-MMU-5617833", "resource": "Reactome", "id": "R-MMU-5617833", "name": "Cilium Assembly" }, { "url": "https://www.reactome.org/PathwayBrowser/#R-MMU-5620924", "resource": "Reactome", "id": "R-MMU-5620924", "name": "Intraflagellar transport" }, { "url": "https://www.reactome.org/PathwayBrowser/#R-MMU-5626467", "resource": "Reactome", "id": "R-MMU-5626467", "name": "RHO GTPases activate IQGAPs" }, { "url": "https://www.reactome.org/PathwayBrowser/#R-MMU-5663220", "resource": "Reactome", "id": "R-MMU-5663220", "name": "RHO GTPases Activate Formins" }, { "url": "https://www.reactome.org/PathwayBrowser/#R-MMU-6807878", "resource": "Reactome", "id": "R-MMU-6807878", "name": "COPI-mediated anterograde transport" }, { "url": "https://www.reactome.org/PathwayBrowser/#R-MMU-6811434", "resource": "Reactome", "id": "R-MMU-6811434", "name": "COPI-dependent Golgi-to-ER retrograde traffic" }, { "url": "https://www.reactome.org/PathwayBrowser/#R-MMU-6811436", "resource": "Reactome", "id": "R-MMU-6811436", "name": "COPI-independent Golgi-to-ER retrograde traffic" }, { "url": "https://www.reactome.org/PathwayBrowser/#R-MMU-68877", "resource": "Reactome", "id": "R-MMU-68877", "name": "Mitotic Prometaphase" }, { "url": "https://www.reactome.org/PathwayBrowser/#R-MMU-8852276", "resource": "Reactome", "id": "R-MMU-8852276", "name": "The role of GTSE1 in G2/M progression after G2 checkpoint" }, { "url": "https://www.reactome.org/PathwayBrowser/#R-MMU-8955332", "resource": "Reactome", "id": "R-MMU-8955332", "name": "Carboxyterminal post-translational modifications of tubulin" }, { "url": "https://www.reactome.org/PathwayBrowser/#R-MMU-9646399", "resource": "Reactome", "id": "R-MMU-9646399", "name": "Aggrephagy" }, { "url": "https://www.reactome.org/PathwayBrowser/#R-MMU-9648025", "resource": "Reactome", "id": "R-MMU-9648025", "name": "EML4 and NUDC in mitotic spindle formation" }, { "url": "https://www.reactome.org/PathwayBrowser/#R-MMU-983189", "resource": "Reactome", "id": "R-MMU-983189", "name": "Kinesins" } ], "function": [ { "url": "https://www.ncbi.nlm.nih.gov/protein/NP_001074440.1", "annotation": "Findings highlight the essential requirements of the megakaryocyte/platelet-restricted beta1-tubulin isoform in platelet structure", "evidence": [ { "url": "https://www.ncbi.nlm.nih.gov/protein/NP_001074440.1", "id": "NP_001074440.1", "database": "RefSeq" } ] }, { "url": "https://www.ncbi.nlm.nih.gov/protein/NP_001074440.1", "annotation": "In mice, Tubb1 knock-out disrupted microtubule integrity by preventing beta1-tubulin incorporation and impaired thyroid migration and thyroid hormone secretion.", "evidence": [ { "url": "https://www.ncbi.nlm.nih.gov/protein/NP_001074440.1", "id": "NP_001074440.1", "database": "RefSeq" } ] }, { "url": "https://www.uniprot.org/uniprot/A2AQ07#function", "annotation": "Tubulin is the major constituent of microtubules. It binds two moles of GTP, one at an exchangeable site on the beta chain and one at a non-exchangeable site on the alpha chain (By similarity).", "evidence": [ { "url": "https://www.uniprot.org/uniprot/A2AQ07#function", "id": "A2AQ07", "database": "UniProtKB" } ] } ], "orthologs": [ { "uniprot_canonical_ac": "M0R8B6-1", "protein_name": "Tubulin beta chain", "sequence": { "length": 452, "sequence": "MREIVHIQIGQCGNQIGAKFWEVIGEEHGIDCAGSYCGTSALQLERISVYYNEAYGKKYVPRAVLVDLEPGTMDSIRSSRLGILFQPDSFVHGNSGAGNNWAKGHYTEGAELIETVMDVVRRESESCDCLQGFQIVHSLGGGTGSGMGTLLMNKIREEYPDRILNSFSVMPSPKVSDTVVEPYNAVLSIHQLIENTDACFCIDNEALYDICFRTLRLTTPTYGDLNHLVSLTMSGITTSLRFPGQLNADLRKLAVNMVPFPRLHFFMPGFAPLTAQGSQQYRALSVAELTQQMFDARNIMAACDPRRGRYLTVACIFRGKMSTKEVDQQLLSIQTRNSNCFVEWIPNNVKVAVCDIPPRGLNMAATFLGNNTAIQELFTRVSEHFSAMFRRRAFVHWYTSEGMDISEFGEAEADILDLVSEYQQFQDVRAGLEDIEEGGEEEAEMGAEDKNH" }, "evidence": [ { "url": "http://www.informatics.jax.org/homology/69474", "id": "69474", "database": "MGI" }, { "url": "https://omabrowser.org/oma/group/A2AQ07/", "id": "A2AQ07", "database": "OMA" } ], "common_name": "Rat", "organism": "Rattus norvegicus", "tax_id": 10116 }, { "uniprot_canonical_ac": "Q9H4B7-1", "protein_name": "Tubulin beta-1 chain", "sequence": { "length": 451, "sequence": "MREIVHIQIGQCGNQIGAKFWEMIGEEHGIDLAGSDRGASALQLERISVYYNEAYGRKYVPRAVLVDLEPGTMDSIRSSKLGALFQPDSFVHGNSGAGNNWAKGHYTEGAELIENVLEVVRHESESCDCLQGFQIVHSLGGGTGSGMGTLLMNKIREEYPDRIMNSFSVMPSPKVSDTVVEPYNAVLSIHQLIENADACFCIDNEALYDICFRTLKLTTPTYGDLNHLVSLTMSGITTSLRFPGQLNADLRKLAVNMVPFPRLHFFMPGFAPLTAQGSQQYRALSVAELTQQMFDARNTMAACDLRRGRYLTVACIFRGKMSTKEVDQQLLSVQTRNSSCFVEWIPNNVKVAVCDIPPRGLSMAATFIGNNTAIQEIFNRVSEHFSAMFKRKAFVHWYTSEGMDINEFGEAENNIHDLVSEYQQFQDAKAVLEEDEEVTEEAEMEPEDKGH" }, "evidence": [ { "url": "http://www.informatics.jax.org/homology/69474", "id": "69474", "database": "MGI" }, { "url": "https://omabrowser.org/oma/group/A2AQ07/", "id": "A2AQ07", "database": "OMA" } ], "common_name": "Human", "organism": "Homo sapiens", "tax_id": 9606 } ], "interactions": [], "synthesized_glycans": [], "snv": [], "cluster_types": [ { "name": "homologset.mgi", "label": "MGI Homologs" }, { "name": "homologset.oma", "label": "OMA Homologs" } ], "refseq": { "url": "https://www.ncbi.nlm.nih.gov/protein/NP_001074440.1", "ac": "NP_001074440.1", "name": "tubulin beta-1 chain", "summary": "" }, "go_annotation": { "categories": [ { "go_terms": [ { "url": "https://www.ebi.ac.uk/QuickGO/term/GO:0005200", "pmid": "15121885", "id": "GO:0005200", "name": "structural constituent of cytoskeleton", "evidence": [ { "url": "https://www.uniprot.org/uniprot/A2AQ07", "id": "A2AQ07", "database": "UniProtKB" } ] }, { "url": "https://www.ebi.ac.uk/QuickGO/term/GO:0005525", "pmid": "21873635", "id": "GO:0005525", "name": "GTP binding", "evidence": [ { "url": "https://www.uniprot.org/uniprot/A2AQ07", "id": "A2AQ07", "database": "UniProtKB" } ] }, { "url": "https://www.ebi.ac.uk/QuickGO/term/GO:0003924", "pmid": "", "id": "GO:0003924", "name": "GTPase 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