TBB5_HUMAN
ID TBB5_HUMAN Reviewed; 444 AA.
AC P07437; P05218; Q8WUC1; Q9CY33;
DT 13-AUG-1987, integrated into UniProtKB/Swiss-Prot.
DT 21-DEC-2004, sequence version 2.
DT 03-AUG-2022, entry version 242.
DE RecName: Full=Tubulin beta chain;
DE AltName: Full=Tubulin beta-5 chain;
GN Name=TUBB; Synonyms=TUBB5; ORFNames=OK/SW-cl.56;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=6688039; DOI=10.1016/0092-8674(83)90429-4;
RA Lee M.G.-S., Lewis S.A., Wilde C.D., Cowan N.J.;
RT "Evolutionary history of a multigene family: an expressed human beta-
RT tubulin gene and three processed pseudogenes.";
RL Cell 33:477-487(1983).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=6865944; DOI=10.1128/mcb.3.5.854-862.1983;
RA Hall J.L., Dudley L., Dobner P.R., Lewis S.A., Cowan N.J.;
RT "Identification of two human beta-tubulin isotypes.";
RL Mol. Cell. Biol. 3:854-862(1983).
RN [3]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC TISSUE=Retina;
RX PubMed=11504633; DOI=10.1016/s0968-0896(01)00103-1;
RA Crabtree D.V., Ojima I., Geng X., Adler A.J.;
RT "Tubulins in the primate retina: evidence that xanthophylls may be
RT endogenous ligands for the paclitaxel-binding site.";
RL Bioorg. Med. Chem. 9:1967-1976(2001).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Brain;
RA Yu W., Gibbs R.A.;
RL Submitted (JUN-1998) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Shiina S., Tamiya G., Oka A., Inoko H.;
RT "Homo sapiens 2,229,817bp genomic DNA of 6p21.3 HLA class I region.";
RL Submitted (SEP-1999) to the EMBL/GenBank/DDBJ databases.
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Shiina T., Ota M., Katsuyama Y., Hashimoto N., Inoko H.;
RT "Genome diversity in HLA: a new strategy for detection of genetic
RT polymorphisms in expressed genes within the HLA class III and class I
RT regions.";
RL Submitted (JUL-2002) to the EMBL/GenBank/DDBJ databases.
RN [7]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Colon adenocarcinoma;
RA Shichijo S., Itoh K.;
RT "Identification of immuno-peptidmics that are recognized by tumor-reactive
RT CTL generated from TIL of colon cancer patients.";
RL Submitted (MAY-2001) to the EMBL/GenBank/DDBJ databases.
RN [8]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Brain, Eye, Lung, Muscle, and Placenta;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [9]
RP PROTEIN SEQUENCE OF 1-19; 47-77; 104-174; 242-276; 283-297; 310-359 AND
RP 363-390, METHYLATION AT ARG-318, AND IDENTIFICATION BY MASS SPECTROMETRY.
RC TISSUE=Foreskin fibroblast, and Mammary carcinoma;
RA Bienvenut W.V., Campbell A., Ozanne B.W., Lourenco F., Olson M.F.;
RL Submitted (DEC-2009) to UniProtKB.
RN [10]
RP PROTEIN SEQUENCE OF 3-19; 47-58; 63-77; 104-121; 163-174; 242-251; 253-276;
RP 283-297; 310-318; 325-336 AND 381-390, AND IDENTIFICATION BY MASS
RP SPECTROMETRY.
RC TISSUE=Brain, Cajal-Retzius cell, and Fetal brain cortex;
RA Lubec G., Vishwanath V., Chen W.-Q., Sun Y.;
RL Submitted (DEC-2008) to UniProtKB.
RN [11]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=15592455; DOI=10.1038/nbt1046;
RA Rush J., Moritz A., Lee K.A., Guo A., Goss V.L., Spek E.J., Zhang H.,
RA Zha X.-M., Polakiewicz R.D., Comb M.J.;
RT "Immunoaffinity profiling of tyrosine phosphorylation in cancer cells.";
RL Nat. Biotechnol. 23:94-101(2005).
RN [12]
RP PHOSPHORYLATION AT SER-172.
RX PubMed=16371510; DOI=10.1091/mbc.e05-07-0621;
RA Fourest-Lieuvin A., Peris L., Gache V., Garcia-Saez I., Juillan-Binard C.,
RA Lantez V., Job D.;
RT "Microtubule regulation in mitosis: tubulin phosphorylation by the cyclin-
RT dependent kinase Cdk1.";
RL Mol. Biol. Cell 17:1041-1050(2006).
RN [13]
RP GLYCYLATION.
RX PubMed=19524510; DOI=10.1016/j.cell.2009.05.020;
RA Rogowski K., Juge F., van Dijk J., Wloga D., Strub J.-M., Levilliers N.,
RA Thomas D., Bre M.-H., Van Dorsselaer A., Gaertig J., Janke C.;
RT "Evolutionary divergence of enzymatic mechanisms for posttranslational
RT polyglycylation.";
RL Cell 137:1076-1087(2009).
RN [14]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-58, AND IDENTIFICATION BY MASS
RP SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=19608861; DOI=10.1126/science.1175371;
RA Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T.C.,
RA Olsen J.V., Mann M.;
RT "Lysine acetylation targets protein complexes and co-regulates major
RT cellular functions.";
RL Science 325:834-840(2009).
RN [15]
RP TISSUE SPECIFICITY.
RX PubMed=20191564; DOI=10.1002/cm.20436;
RA Leandro-Garcia L.J., Leskela S., Landa I., Montero-Conde C.,
RA Lopez-Jimenez E., Leton R., Cascon A., Robledo M., Rodriguez-Antona C.;
RT "Tumoral and tissue-specific expression of the major human beta-tubulin
RT isotypes.";
RL Cytoskeleton 67:214-223(2010).
RN [16]
RP INTERACTION WITH PIFO.
RX PubMed=20643351; DOI=10.1016/j.devcel.2010.06.005;
RA Kinzel D., Boldt K., Davis E.E., Burtscher I., Trumbach D., Diplas B.,
RA Attie-Bitach T., Wurst W., Katsanis N., Ueffing M., Lickert H.;
RT "Pitchfork regulates primary cilia disassembly and left-right asymmetry.";
RL Dev. Cell 19:66-77(2010).
RN [17]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=21269460; DOI=10.1186/1752-0509-5-17;
RA Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T.,
RA Bennett K.L., Superti-Furga G., Colinge J.;
RT "Initial characterization of the human central proteome.";
RL BMC Syst. Biol. 5:17-17(2011).
RN [18]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-55; THR-285 AND THR-290, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Erythroleukemia;
RX PubMed=23186163; DOI=10.1021/pr300630k;
RA Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J.,
RA Mohammed S.;
RT "Toward a comprehensive characterization of a human cancer cell
RT phosphoproteome.";
RL J. Proteome Res. 12:260-271(2013).
RN [19]
RP INTERACTION WITH DIAPH1, AND IDENTIFICATION BY MASS SPECTROMETRY.
RX PubMed=23325789; DOI=10.1091/mbc.e12-08-0597;
RA Li D., Dammer E.B., Lucki N.C., Sewer M.B.;
RT "cAMP-stimulated phosphorylation of diaphanous 1 regulates protein
RT stability and interaction with binding partners in adrenocortical cells.";
RL Mol. Biol. Cell 24:848-857(2013).
RN [20]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Liver;
RX PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014;
RA Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., Wang L.,
RA Ye M., Zou H.;
RT "An enzyme assisted RP-RPLC approach for in-depth analysis of human liver
RT phosphoproteome.";
RL J. Proteomics 96:253-262(2014).
RN [21]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=25944712; DOI=10.1002/pmic.201400617;
RA Vaca Jacome A.S., Rabilloud T., Schaeffer-Reiss C., Rompais M., Ayoub D.,
RA Lane L., Bairoch A., Van Dorsselaer A., Carapito C.;
RT "N-terminome analysis of the human mitochondrial proteome.";
RL Proteomics 15:2519-2524(2015).
RN [22]
RP GLUTAMYLATION.
RX PubMed=26875866; DOI=10.1016/j.cell.2016.01.019;
RA Valenstein M.L., Roll-Mecak A.;
RT "Graded control of microtubule severing by tubulin glutamylation.";
RL Cell 164:911-921(2016).
RN [23]
RP GLUTAMYLATION AT GLU-434 AND GLU-441, AND GLYCYLATION AT GLU-438; GLU-439;
RP GLU-441; GLU-442 AND GLU-443.
RX PubMed=28576883; DOI=10.1073/pnas.1617286114;
RA Garnham C.P., Yu I., Li Y., Roll-Mecak A.;
RT "Crystal structure of tubulin tyrosine ligase-like 3 reveals essential
RT architectural elements unique to tubulin monoglycylases.";
RL Proc. Natl. Acad. Sci. U.S.A. 114:6545-6550(2017).
RN [24]
RP GLUTAMYLATION AT GLU-438 AND GLU-439.
RX PubMed=32747782; DOI=10.1038/s41594-020-0462-0;
RA Mahalingan K.K., Keith Keenan E., Strickland M., Li Y., Liu Y., Ball H.L.,
RA Tanner M.E., Tjandra N., Roll-Mecak A.;
RT "Structural basis for polyglutamate chain initiation and elongation by TTLL
RT family enzymes.";
RL Nat. Struct. Mol. Biol. 27:802-813(2020).
RN [25]
RP SUBUNIT, INDUCTION, AND DOMAIN.
RX PubMed=31727855; DOI=10.1126/science.aaz4352;
RA Lin Z., Gasic I., Chandrasekaran V., Peters N., Shao S., Mitchison T.J.,
RA Hegde R.S.;
RT "TTC5 mediates autoregulation of tubulin via mRNA degradation.";
RL Science 367:100-104(2020).
RN [26]
RP VARIANTS CDCBM6 VAL-299; ILE-353 AND LYS-401, AND CHARACTERIZATION OF
RP VARIANTS CDCBM6 VAL-299 AND LYS-401.
RX PubMed=23246003; DOI=10.1016/j.celrep.2012.11.017;
RA Breuss M., Heng J.I., Poirier K., Tian G., Jaglin X.H., Qu Z., Braun A.,
RA Gstrein T., Ngo L., Haas M., Bahi-Buisson N., Moutard M.L., Passemard S.,
RA Verloes A., Gressens P., Xie Y., Robson K.J., Rani D.S., Thangaraj K.,
RA Clausen T., Chelly J., Cowan N.J., Keays D.A.;
RT "Mutations in the beta-tubulin gene TUBB5 cause microcephaly with
RT structural brain abnormalities.";
RL Cell Rep. 2:1554-1562(2012).
RN [27]
RP INVOLVEMENT IN CSCSC1, VARIANTS CSCSC1 LYS-15 AND PHE-222, CHARACTERIZATION
RP OF VARIANTS CSCSC1 LYS-15 AND PHE-222, SUBUNIT, AND SUBCELLULAR LOCATION.
RX PubMed=26637975; DOI=10.1016/j.ajhg.2015.10.014;
RA Isrie M., Breuss M., Tian G., Hansen A.H., Cristofoli F., Morandell J.,
RA Kupchinsky Z.A., Sifrim A., Rodriguez-Rodriguez C.M., Dapena E.P.,
RA Doonanco K., Leonard N., Tinsa F., Moortgat S., Ulucan H., Koparir E.,
RA Karaca E., Katsanis N., Marton V., Vermeesch J.R., Davis E.E., Cowan N.J.,
RA Keays D.A., Van Esch H.;
RT "Mutations in Either TUBB or MAPRE2 Cause Circumferential Skin Creases
RT Kunze Type.";
RL Am. J. Hum. Genet. 97:790-800(2015).
CC -!- FUNCTION: Tubulin is the major constituent of microtubules. It binds
CC two moles of GTP, one at an exchangeable site on the beta chain and one
CC at a non-exchangeable site on the alpha chain.
CC -!- SUBUNIT: Heterodimer of alpha and beta chains (PubMed:26637975). A
CC typical microtubule is a hollow water-filled tube with an outer
CC diameter of 25 nm and an inner diameter of 15 nM. Alpha-beta
CC heterodimers associate head-to-tail to form protofilaments running
CC lengthwise along the microtubule wall with the beta-tubulin subunit
CC facing the microtubule plus end conferring a structural polarity.
CC Microtubules usually have 13 protofilaments but different protofilament
CC numbers can be found in some organisms and specialized cells. Interacts
CC with PIFO (PubMed:20643351). Interacts with DIAPH1 (PubMed:23325789).
CC Interacts with MX1 (By similarity). May interact with RNABP10 (By
CC similarity). Interacts with CFAP157 (By similarity). Nascent tubulin
CC polypeptide interacts (via beta-tubulin MREI motif) with TTC5/STRAP;
CC this interaction results in tubulin mRNA-targeted degradation
CC (PubMed:31727855). {ECO:0000250|UniProtKB:P69893,
CC ECO:0000250|UniProtKB:P99024, ECO:0000269|PubMed:20643351,
CC ECO:0000269|PubMed:23325789, ECO:0000269|PubMed:26637975,
CC ECO:0000269|PubMed:31727855}.
CC -!- INTERACTION:
CC P07437; P05067: APP; NbExp=5; IntAct=EBI-350864, EBI-77613;
CC P07437; P27797: CALR; NbExp=3; IntAct=EBI-350864, EBI-1049597;
CC P07437; P36957: DLST; NbExp=3; IntAct=EBI-350864, EBI-351007;
CC P07437; P51114: FXR1; NbExp=2; IntAct=EBI-350864, EBI-713291;
CC P07437; P42858: HTT; NbExp=9; IntAct=EBI-350864, EBI-466029;
CC P07437; P05412: JUN; NbExp=3; IntAct=EBI-350864, EBI-852823;
CC P07437; Q5S007: LRRK2; NbExp=6; IntAct=EBI-350864, EBI-5323863;
CC P07437; P19404: NDUFV2; NbExp=3; IntAct=EBI-350864, EBI-713665;
CC P07437; Q15843: NEDD8; NbExp=4; IntAct=EBI-350864, EBI-716247;
CC P07437; I6L9F6: NEFL; NbExp=3; IntAct=EBI-350864, EBI-10178578;
CC P07437; Q8TDX7: NEK7; NbExp=3; IntAct=EBI-350864, EBI-1055945;
CC P07437; P37840: SNCA; NbExp=3; IntAct=EBI-350864, EBI-985879;
CC P07437; P00441: SOD1; NbExp=3; IntAct=EBI-350864, EBI-990792;
CC P07437; Q13501: SQSTM1; NbExp=3; IntAct=EBI-350864, EBI-307104;
CC P07437; Q03403: TFF2; NbExp=3; IntAct=EBI-350864, EBI-4314702;
CC P07437; Q9BSI4: TINF2; NbExp=2; IntAct=EBI-350864, EBI-717399;
CC P07437; Q71U36: TUBA1A; NbExp=4; IntAct=EBI-350864, EBI-302552;
CC P07437; Q8AZK7: EBNA-LP; Xeno; NbExp=3; IntAct=EBI-350864, EBI-1185167;
CC -!- SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton
CC {ECO:0000269|PubMed:26637975}.
CC -!- TISSUE SPECIFICITY: Ubiquitously expressed with highest levels in
CC spleen, thymus and immature brain. {ECO:0000269|PubMed:20191564}.
CC -!- INDUCTION: Autoregulated by feedback control of mRNA degradation
CC (PubMed:31727855). In excess of soluble tubulin, nascent beta-tubulin
CC chain binds TTC5/STRAP cofactor through the MREI motif which triggers
CC cotranslation degradation of tubulin mRNA (PubMed:31727855).
CC {ECO:0000269|PubMed:31727855}.
CC -!- DOMAIN: The highly acidic C-terminal region may bind cations such as
CC calcium.
CC -!- DOMAIN: The MREI motif is common among all beta-tubulin isoforms and
CC may be critical for tubulin autoregulation.
CC {ECO:0000269|PubMed:31727855}.
CC -!- PTM: Some glutamate residues at the C-terminus are polyglutamylated,
CC resulting in polyglutamate chains on the gamma-carboxyl group
CC (PubMed:26875866, PubMed:28576883). Polyglutamylation plays a key role
CC in microtubule severing by spastin (SPAST). SPAST preferentially
CC recognizes and acts on microtubules decorated with short polyglutamate
CC tails: severing activity by SPAST increases as the number of glutamates
CC per tubulin rises from one to eight, but decreases beyond this
CC glutamylation threshold (PubMed:26875866). Glutamylation is also
CC involved in cilia motility (By similarity).
CC {ECO:0000250|UniProtKB:P99024, ECO:0000269|PubMed:26875866,
CC ECO:0000269|PubMed:28576883}.
CC -!- PTM: Some glutamate residues at the C-terminus are monoglycylated but
CC not polyglycylated due to the absence of functional TTLL10 in human.
CC Monoglycylation is mainly limited to tubulin incorporated into cilia
CC and flagella axonemes, which is required for their stability and
CC maintenance. Flagella glycylation controls sperm motility (Probable)
CC (PubMed:28576883). Both polyglutamylation and monoglycylation can
CC coexist on the same protein on adjacent residues, and lowering
CC glycylation levels increases polyglutamylation, and reciprocally
CC (Probable) (PubMed:28576883). {ECO:0000269|PubMed:28576883,
CC ECO:0000305|PubMed:19524510}.
CC -!- PTM: Phosphorylated on Ser-172 by CDK1 during the cell cycle, from
CC metaphase to telophase, but not in interphase. This phosphorylation
CC inhibits tubulin incorporation into microtubules.
CC {ECO:0000269|PubMed:16371510}.
CC -!- DISEASE: Cortical dysplasia, complex, with other brain malformations 6
CC (CDCBM6) [MIM:615771]: A disorder of aberrant neuronal migration and
CC disturbed axonal guidance. Affected individuals have microcephaly,
CC ataxia, and severe delayed psychomotor development. Brain imaging shows
CC variable malformations of cortical development, including white matter
CC streaks, dysmorphic basal ganglia, corpus callosum abnormalities,
CC brainstem and cerebellar hypoplasia, cortical dysplasia,
CC polymicrogyria. {ECO:0000269|PubMed:23246003}. Note=The disease is
CC caused by variants affecting the gene represented in this entry.
CC -!- DISEASE: Skin creases, congenital symmetric circumferential, 1 (CSCSC1)
CC [MIM:156610]: An autosomal dominant disease characterized by multiple,
CC symmetric, circumferential rings of folded skin, affecting primarily
CC the limbs. Affected individuals also exhibit intellectual disability,
CC cleft palate, and dysmorphic features. {ECO:0000269|PubMed:26637975}.
CC Note=The disease is caused by variants affecting the gene represented
CC in this entry.
CC -!- SIMILARITY: Belongs to the tubulin family. {ECO:0000305}.
CC -!- WEB RESOURCE: Name=Wikipedia; Note=Tubulin entry;
CC URL="https://en.wikipedia.org/wiki/Tubulin";
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DR EMBL; J00314; AAB59507.1; -; Genomic_DNA.
DR EMBL; AF141349; AAD33873.1; -; mRNA.
DR EMBL; AF070561; AAC28642.1; -; mRNA.
DR EMBL; AF070593; AAC28650.1; -; mRNA.
DR EMBL; AF070600; AAC28654.1; -; mRNA.
DR EMBL; BA000025; BAB63321.1; -; Genomic_DNA.
DR EMBL; AB088100; BAC54932.1; -; Genomic_DNA.
DR EMBL; AB062393; BAB93480.1; -; mRNA.
DR EMBL; BC001938; AAH01938.1; -; mRNA.
DR EMBL; BC002347; AAH02347.1; -; mRNA.
DR EMBL; BC005838; AAH05838.1; -; mRNA.
DR EMBL; BC007605; AAH07605.1; -; mRNA.
DR EMBL; BC013374; AAH13374.1; -; mRNA.
DR EMBL; BC019924; AAH19924.1; -; mRNA.
DR EMBL; BC020946; AAH20946.1; -; mRNA.
DR EMBL; BC021909; AAH21909.1; -; mRNA.
DR EMBL; BC070326; AAH70326.1; -; mRNA.
DR CCDS; CCDS4687.1; -.
DR PIR; A26561; A26561.
DR RefSeq; NP_001280141.1; NM_001293212.1.
DR RefSeq; NP_001280142.1; NM_001293213.1.
DR RefSeq; NP_001280143.1; NM_001293214.1.
DR RefSeq; NP_001280144.1; NM_001293215.1.
DR RefSeq; NP_001280145.1; NM_001293216.1.
DR RefSeq; NP_821133.1; NM_178014.3.
DR PDB; 3QNZ; X-ray; 2.20 A; C=429-438.
DR PDB; 3QO0; X-ray; 2.30 A; C=422-441.
DR PDB; 5N5N; EM; 4.00 A; A/B/C/D/E/F=1-426.
DR PDB; 6I2I; EM; 3.60 A; B=1-444.
DR PDB; 6QUS; EM; 3.70 A; S/U=1-444.
DR PDB; 6QUY; EM; 3.80 A; G/H=1-444.
DR PDB; 6QVE; EM; 3.70 A; G/H=1-444.
DR PDB; 6QVJ; EM; 3.80 A; S/U=1-444.
DR PDBsum; 3QNZ; -.
DR PDBsum; 3QO0; -.
DR PDBsum; 5N5N; -.
DR PDBsum; 6I2I; -.
DR PDBsum; 6QUS; -.
DR PDBsum; 6QUY; -.
DR PDBsum; 6QVE; -.
DR PDBsum; 6QVJ; -.
DR AlphaFoldDB; P07437; -.
DR SMR; P07437; -.
DR BioGRID; 128444; 736.
DR CORUM; P07437; -.
DR DIP; DIP-32772N; -.
DR IntAct; P07437; 210.
DR MINT; P07437; -.
DR STRING; 9606.ENSP00000339001; -.
DR BindingDB; P07437; -.
DR ChEMBL; CHEMBL5444; -.
DR DrugBank; DB11638; Artenimol.
DR DrugBank; DB05284; CA4P.
DR DrugBank; DB15534; Colchiceine.
DR DrugBank; DB01394; Colchicine.
DR DrugBank; DB09130; Copper.
DR DrugBank; DB05147; CYT997.
DR DrugBank; DB11731; Depatuxizumab mafodotin.
DR DrugBank; DB01873; Epothilone D.
DR DrugBank; DB12334; Milataxel.
DR DrugBank; DB03010; Patupilone.
DR DrugBank; DB01179; Podofilox.
DR DrugBank; DB06137; Tirbanibulin.
DR DrugBank; DB00570; Vinblastine.
DR DrugBank; DB00541; Vincristine.
DR DrugBank; DB11641; Vinflunine.
DR DrugBank; DB00361; Vinorelbine.
DR DrugBank; DB06042; ZEN-012.
DR DrugCentral; P07437; -.
DR GuidetoPHARMACOLOGY; 2640; -.
DR GlyGen; P07437; 1 site, 1 O-linked glycan (1 site).
DR iPTMnet; P07437; -.
DR MetOSite; P07437; -.
DR PhosphoSitePlus; P07437; -.
DR SwissPalm; P07437; -.
DR BioMuta; TUBB; -.
DR DMDM; 56757569; -.
DR OGP; P07437; -.
DR REPRODUCTION-2DPAGE; P07437; -.
DR SWISS-2DPAGE; P07437; -.
DR UCD-2DPAGE; P07437; -.
DR EPD; P07437; -.
DR jPOST; P07437; -.
DR MassIVE; P07437; -.
DR PaxDb; P07437; -.
DR PeptideAtlas; P07437; -.
DR PRIDE; P07437; -.
DR ProteomicsDB; 52002; -.
DR TopDownProteomics; P07437; -.
DR ABCD; P07437; 2 sequenced antibodies.
DR Antibodypedia; 48344; 1040 antibodies from 44 providers.
DR CPTC; P07437; 1 antibody.
DR DNASU; 203068; -.
DR Ensembl; ENST00000327892.13; ENSP00000339001.7; ENSG00000196230.14.
DR Ensembl; ENST00000383564.8; ENSP00000373058.4; ENSG00000183311.16.
DR Ensembl; ENST00000419792.6; ENSP00000401317.2; ENSG00000235067.10.
DR Ensembl; ENST00000421473.6; ENSP00000399155.2; ENSG00000224156.10.
DR Ensembl; ENST00000422650.6; ENSP00000400663.2; ENSG00000229684.10.
DR Ensembl; ENST00000422674.6; ENSP00000406811.2; ENSG00000227739.10.
DR Ensembl; ENST00000432462.6; ENSP00000410829.2; ENSG00000232421.10.
DR Ensembl; ENST00000436628.6; ENSP00000410071.2; ENSG00000232575.10.
DR GeneID; 203068; -.
DR KEGG; hsa:203068; -.
DR MANE-Select; ENST00000327892.13; ENSP00000339001.7; NM_178014.4; NP_821133.1.
DR CTD; 203068; -.
DR DisGeNET; 203068; -.
DR GeneCards; TUBB; -.
DR GeneReviews; TUBB; -.
DR HGNC; HGNC:20778; TUBB.
DR HPA; ENSG00000196230; Low tissue specificity.
DR MalaCards; TUBB; -.
DR MIM; 156610; phenotype.
DR MIM; 191130; gene.
DR MIM; 615771; phenotype.
DR neXtProt; NX_P07437; -.
DR OpenTargets; ENSG00000196230; -.
DR Orphanet; 2505; Multiple benign circumferential skin creases on limbs.
DR PharmGKB; PA358; -.
DR VEuPathDB; HostDB:ENSG00000196230; -.
DR eggNOG; KOG1375; Eukaryota.
DR GeneTree; ENSGT00940000154370; -.
DR HOGENOM; CLU_015718_1_1_1; -.
DR InParanoid; P07437; -.
DR OMA; RYQGEND; -.
DR OrthoDB; 962471at2759; -.
DR PhylomeDB; P07437; -.
DR TreeFam; TF300298; -.
DR PathwayCommons; P07437; -.
DR Reactome; R-HSA-2565942; Regulation of PLK1 Activity at G2/M Transition.
DR Reactome; R-HSA-380259; Loss of Nlp from mitotic centrosomes.
DR Reactome; R-HSA-380270; Recruitment of mitotic centrosome proteins and complexes.
DR Reactome; R-HSA-380284; Loss of proteins required for interphase microtubule organization from the centrosome.
DR Reactome; R-HSA-380320; Recruitment of NuMA to mitotic centrosomes.
DR Reactome; R-HSA-5620912; Anchoring of the basal body to the plasma membrane.
DR Reactome; R-HSA-6798695; Neutrophil degranulation.
DR Reactome; R-HSA-8854518; AURKA Activation by TPX2.
DR Reactome; R-HSA-9679191; Potential therapeutics for SARS.
DR SignaLink; P07437; -.
DR SIGNOR; P07437; -.
DR BioGRID-ORCS; 203068; 766 hits in 1065 CRISPR screens.
DR ChiTaRS; TUBB; human.
DR GeneWiki; TUBB; -.
DR GenomeRNAi; 203068; -.
DR Pharos; P07437; Tclin.
DR PRO; PR:P07437; -.
DR Proteomes; UP000005640; Chromosome 6.
DR RNAct; P07437; protein.
DR Bgee; ENSG00000196230; Expressed in cortical plate and 99 other tissues.
DR ExpressionAtlas; P07437; baseline and differential.
DR Genevisible; P07437; HS.
DR GO; GO:0035578; C:azurophil granule lumen; TAS:Reactome.
DR GO; GO:0044297; C:cell body; IDA:DFLAT.
DR GO; GO:0005737; C:cytoplasm; IDA:CAFA.
DR GO; GO:0036464; C:cytoplasmic ribonucleoprotein granule; IDA:ParkinsonsUK-UCL.
DR GO; GO:0005856; C:cytoskeleton; TAS:UniProtKB.
DR GO; GO:0005829; C:cytosol; TAS:Reactome.
DR GO; GO:0070062; C:extracellular exosome; HDA:UniProtKB.
DR GO; GO:0005576; C:extracellular region; TAS:Reactome.
DR GO; GO:0045171; C:intercellular bridge; IDA:HPA.
DR GO; GO:0045121; C:membrane raft; IEA:Ensembl.
DR GO; GO:0005874; C:microtubule; IDA:UniProtKB.
DR GO; GO:0015630; C:microtubule cytoskeleton; IDA:HPA.
DR GO; GO:0072686; C:mitotic spindle; IDA:HPA.
DR GO; GO:0005641; C:nuclear envelope lumen; IDA:DFLAT.
DR GO; GO:0005634; C:nucleus; HDA:UniProtKB.
DR GO; GO:0032991; C:protein-containing complex; IEA:Ensembl.
DR GO; GO:0005525; F:GTP binding; IBA:GO_Central.
DR GO; GO:0032794; F:GTPase activating protein binding; IEA:Ensembl.
DR GO; GO:0042288; F:MHC class I protein binding; IDA:UniProtKB.
DR GO; GO:0019904; F:protein domain specific binding; IEA:Ensembl.
DR GO; GO:0044877; F:protein-containing complex binding; IEA:Ensembl.
DR GO; GO:0005200; F:structural constituent of cytoskeleton; IBA:GO_Central.
DR GO; GO:0005198; F:structural molecule activity; TAS:BHF-UCL.
DR GO; GO:0031625; F:ubiquitin protein ligase binding; IPI:ParkinsonsUK-UCL.
DR GO; GO:0051301; P:cell division; TAS:BHF-UCL.
DR GO; GO:0030705; P:cytoskeleton-dependent intracellular transport; TAS:BHF-UCL.
DR GO; GO:0000226; P:microtubule cytoskeleton organization; IBA:GO_Central.
DR GO; GO:0007017; P:microtubule-based process; TAS:BHF-UCL.
DR GO; GO:0000278; P:mitotic cell cycle; IBA:GO_Central.
DR GO; GO:0042267; P:natural killer cell mediated cytotoxicity; NAS:UniProtKB.
DR GO; GO:0071895; P:odontoblast differentiation; IDA:GO_Central.
DR GO; GO:0050807; P:regulation of synapse organization; IEA:Ensembl.
DR GO; GO:0051225; P:spindle assembly; IEA:Ensembl.
DR Gene3D; 1.10.287.600; -; 1.
DR Gene3D; 3.30.1330.20; -; 1.
DR Gene3D; 3.40.50.1440; -; 1.
DR InterPro; IPR013838; Beta-tubulin_BS.
DR InterPro; IPR002453; Beta_tubulin.
DR InterPro; IPR008280; Tub_FtsZ_C.
DR InterPro; IPR000217; Tubulin.
DR InterPro; IPR037103; Tubulin/FtsZ-like_C.
DR InterPro; IPR018316; Tubulin/FtsZ_2-layer-sand-dom.
DR InterPro; IPR036525; Tubulin/FtsZ_GTPase_sf.
DR InterPro; IPR023123; Tubulin_C.
DR InterPro; IPR017975; Tubulin_CS.
DR InterPro; IPR003008; Tubulin_FtsZ_GTPase.
DR PANTHER; PTHR11588; PTHR11588; 1.
DR Pfam; PF00091; Tubulin; 1.
DR Pfam; PF03953; Tubulin_C; 1.
DR PRINTS; PR01163; BETATUBULIN.
DR PRINTS; PR01161; TUBULIN.
DR SMART; SM00864; Tubulin; 1.
DR SMART; SM00865; Tubulin_C; 1.
DR SUPFAM; SSF52490; SSF52490; 1.
DR SUPFAM; SSF55307; SSF55307; 1.
DR PROSITE; PS00227; TUBULIN; 1.
DR PROSITE; PS00228; TUBULIN_B_AUTOREG; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Acetylation; Cytoplasm; Cytoskeleton;
KW Direct protein sequencing; Disease variant; GTP-binding; Isopeptide bond;
KW Methylation; Microtubule; Nucleotide-binding; Phosphoprotein;
KW Reference proteome; Ubl conjugation.
FT CHAIN 1..444
FT /note="Tubulin beta chain"
FT /id="PRO_0000048243"
FT REGION 423..444
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 1..4
FT /note="MREI motif"
FT /evidence="ECO:0000269|PubMed:31727855"
FT COMPBIAS 427..444
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 140..146
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000255"
FT MOD_RES 40
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P99024"
FT MOD_RES 55
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 58
FT /note="N6-acetyllysine; alternate"
FT /evidence="ECO:0007744|PubMed:19608861"
FT MOD_RES 58
FT /note="N6-succinyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:P99024"
FT MOD_RES 172
FT /note="Phosphoserine; by CDK1"
FT /evidence="ECO:0000269|PubMed:16371510"
FT MOD_RES 285
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 290
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 318
FT /note="Omega-N-methylarginine"
FT /evidence="ECO:0000269|Ref.9"
FT MOD_RES 434
FT /note="5-glutamyl polyglutamate"
FT /evidence="ECO:0000269|PubMed:28576883"
FT MOD_RES 438
FT /note="5-glutamyl glycine"
FT /evidence="ECO:0000269|PubMed:28576883"
FT MOD_RES 438
FT /note="5-glutamyl polyglutamate"
FT /evidence="ECO:0000269|PubMed:32747782"
FT MOD_RES 439
FT /note="5-glutamyl glycine"
FT /evidence="ECO:0000269|PubMed:28576883"
FT MOD_RES 439
FT /note="5-glutamyl polyglutamate"
FT /evidence="ECO:0000269|PubMed:32747782"
FT MOD_RES 441
FT /note="5-glutamyl glycine"
FT /evidence="ECO:0000269|PubMed:28576883"
FT MOD_RES 441
FT /note="5-glutamyl polyglutamate"
FT /evidence="ECO:0000269|PubMed:28576883"
FT MOD_RES 442
FT /note="5-glutamyl glycine"
FT /evidence="ECO:0000269|PubMed:28576883"
FT MOD_RES 443
FT /note="5-glutamyl glycine"
FT /evidence="ECO:0000269|PubMed:28576883"
FT CROSSLNK 58
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in ubiquitin); alternate"
FT CROSSLNK 324
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in ubiquitin)"
FT VARIANT 15
FT /note="Q -> K (in CSCSC1; disrupts heterodimer assembly and
FT microtubule dynamics; dbSNP:rs864321676)"
FT /evidence="ECO:0000269|PubMed:26637975"
FT /id="VAR_076543"
FT VARIANT 222
FT /note="Y -> F (in CSCSC1; disrupts heterodimer assembly and
FT microtubule dynamics; dbSNP:rs864321677)"
FT /evidence="ECO:0000269|PubMed:26637975"
FT /id="VAR_076544"
FT VARIANT 299
FT /note="M -> V (in CDCBM6; decreases the ability of the
FT protein to assemble into tubulin heterodimers;
FT dbSNP:rs587777355)"
FT /evidence="ECO:0000269|PubMed:23246003"
FT /id="VAR_071763"
FT VARIANT 353
FT /note="V -> I (in CDCBM6; does not affect the ability of
FT the mutant polypeptides to assemble into heterodimers and
FT incorporate into microtubules; dbSNP:rs587777356)"
FT /evidence="ECO:0000269|PubMed:23246003"
FT /id="VAR_071764"
FT VARIANT 401
FT /note="E -> K (in CDCBM6; arrests the assembly pathway of
FT alpha/beta-tubulin; the mutant protein is unable to
FT coassemble into a tubulin heterodimer but is instead
FT distributed throughout the cytoplasm; dbSNP:rs587777357)"
FT /evidence="ECO:0000269|PubMed:23246003"
FT /id="VAR_071765"
FT CONFLICT 216
FT /note="K -> R (in Ref. 1; no nucleotide entry and 2;
FT AAB59507)"
FT /evidence="ECO:0000305"
FT CONFLICT 231
FT /note="A -> G (in Ref. 1; no nucleotide entry and 2;
FT AAB59507)"
FT /evidence="ECO:0000305"
FT CONFLICT 234..235
FT /note="SG -> EC (in Ref. 1; no nucleotide entry and 2;
FT AAB59507)"
FT /evidence="ECO:0000305"
FT CONFLICT 288
FT /note="E -> D (in Ref. 1; no nucleotide entry and 2;
FT AAB59507)"
FT /evidence="ECO:0000305"
FT CONFLICT 298
FT /note="N -> D (in Ref. 8; AAH20946)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 444 AA; 49671 MW; 1E6CD0A36773A103 CRC64;
MREIVHIQAG QCGNQIGAKF WEVISDEHGI DPTGTYHGDS DLQLDRISVY YNEATGGKYV
PRAILVDLEP GTMDSVRSGP FGQIFRPDNF VFGQSGAGNN WAKGHYTEGA ELVDSVLDVV
RKEAESCDCL QGFQLTHSLG GGTGSGMGTL LISKIREEYP DRIMNTFSVV PSPKVSDTVV
EPYNATLSVH QLVENTDETY CIDNEALYDI CFRTLKLTTP TYGDLNHLVS ATMSGVTTCL
RFPGQLNADL RKLAVNMVPF PRLHFFMPGF APLTSRGSQQ YRALTVPELT QQVFDAKNMM
AACDPRHGRY LTVAAVFRGR MSMKEVDEQM LNVQNKNSSY FVEWIPNNVK TAVCDIPPRG
LKMAVTFIGN STAIQELFKR ISEQFTAMFR RKAFLHWYTG EGMDEMEFTE AESNMNDLVS
EYQQYQDATA EEEEDFGEEA EEEA
