TBA1B_HUMAN
ID TBA1B_HUMAN Reviewed; 451 AA.
AC P68363; P04687; P05209; Q27I68; Q8WU19;
DT 13-AUG-1987, integrated into UniProtKB/Swiss-Prot.
DT 13-AUG-1987, sequence version 1.
DT 03-AUG-2022, entry version 182.
DE RecName: Full=Tubulin alpha-1B chain;
DE AltName: Full=Alpha-tubulin ubiquitous;
DE AltName: Full=Tubulin K-alpha-1;
DE AltName: Full=Tubulin alpha-ubiquitous chain;
DE Contains:
DE RecName: Full=Detyrosinated tubulin alpha-1B chain;
GN Name=TUBA1B;
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 [MRNA] (ISOFORM 1).
RC TISSUE=Keratinocyte;
RX PubMed=6646120; DOI=10.1128/mcb.3.10.1738-1745.1983;
RA Cowan N.J., Dobner P., Fuchs E.V., Cleveland D.W.;
RT "Expression of human alpha-tubulin genes: interspecies conservation of 3'
RT untranslated regions.";
RL Mol. Cell. Biol. 3:1738-1745(1983).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
RA de Hostos E.L.;
RL Submitted (JUL-1998) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
RA Li Q., Liu L., Ma S.;
RT "Gene response of gangliocytes stimulated by Herpes simplex virus type 1.";
RL Submitted (FEB-2006) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
RC TISSUE=Brain, Colon, Eye, Kidney, Lung, Muscle, Placenta, Prostate, Skin,
RC and Uterus;
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 [5]
RP PROTEIN SEQUENCE OF 41-60; 65-79; 113-121; 230-280; 312-320; 327-336;
RP 340-370; 374-390; 395-401 AND 403-422, AND IDENTIFICATION BY MASS
RP SPECTROMETRY.
RC TISSUE=Brain, Cajal-Retzius cell, and Fetal brain cortex;
RA Lubec G., Afjehi-Sadat L., Vishwanath V., Chen W.-Q., Sun Y.;
RL Submitted (DEC-2008) to UniProtKB.
RN [6]
RP PROTEIN SEQUENCE OF 41-79; 65-79; 85-121; 125-164; 216-304; 312-370 AND
RP 374-451, PHOSPHORYLATION AT SER-48 AND SER-232, METHYLATION AT ARG-339, AND
RP IDENTIFICATION BY MASS SPECTROMETRY.
RC TISSUE=Embryonic kidney;
RA Bienvenut W.V., Waridel P., Quadroni M.;
RL Submitted (MAR-2009) to UniProtKB.
RN [7]
RP PROTEIN SEQUENCE OF 353-370 AND 395-401.
RC TISSUE=Brain;
RX PubMed=8619814; DOI=10.1006/bbrc.1996.0211;
RA Baumann M.H., Wisniewski T., Levy E., Plant G.T., Ghiso J.;
RT "C-terminal fragments of alpha- and beta-tubulin form amyloid fibrils in
RT vitro and associate with amyloid deposits of familial cerebral amyloid
RT angiopathy, British type.";
RL Biochem. Biophys. Res. Commun. 219:238-242(1996).
RN [8]
RP PROTEIN SEQUENCE OF 439-451, AND NITRATION AT TYR-451.
RX PubMed=10339593; DOI=10.1073/pnas.96.11.6365;
RA Eiserich J.P., Estevez A.G., Bamberg T.V., Ye Y.Z., Chumley P.H.,
RA Beckman J.S., Freeman B.A.;
RT "Microtubule dysfunction by posttranslational nitrotyrosination of alpha-
RT tubulin: a nitric oxide-dependent mechanism of cellular injury.";
RL Proc. Natl. Acad. Sci. U.S.A. 96:6365-6370(1999).
RN [9]
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 [10]
RP ACETYLATION AT LYS-40.
RX PubMed=24906155; DOI=10.1016/j.cell.2014.03.061;
RA Szyk A., Deaconescu A.M., Spector J., Goodman B., Valenstein M.L.,
RA Ziolkowska N.E., Kormendi V., Grigorieff N., Roll-Mecak A.;
RT "Molecular basis for age-dependent microtubule acetylation by tubulin
RT acetyltransferase.";
RL Cell 157:1405-1415(2014).
RN [11]
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 [12]
RP DETYROSINATION.
RX PubMed=25908662; DOI=10.1126/science.aaa5175;
RA Barisic M., Silva e Sousa R., Tripathy S.K., Magiera M.M., Zaytsev A.V.,
RA Pereira A.L., Janke C., Grishchuk E.L., Maiato H.;
RT "Mitosis. Microtubule detyrosination guides chromosomes during mitosis.";
RL Science 348:799-803(2015).
RN [13]
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 [14]
RP METHYLATION AT LYS-40.
RX PubMed=27518565; DOI=10.1016/j.cell.2016.07.005;
RA Park I.Y., Powell R.T., Tripathi D.N., Dere R., Ho T.H., Blasius T.L.,
RA Chiang Y.C., Davis I.J., Fahey C.C., Hacker K.E., Verhey K.J.,
RA Bedford M.T., Jonasch E., Rathmell W.K., Walker C.L.;
RT "Dual chromatin and cytoskeletal remodeling by SETD2.";
RL Cell 166:950-962(2016).
RN [15]
RP TYROSINATION.
RX PubMed=26972003; DOI=10.1016/j.celrep.2016.02.046;
RA Nirschl J.J., Magiera M.M., Lazarus J.E., Janke C., Holzbaur E.L.;
RT "Alpha-tubulin tyrosination and CLIP-170 phosphorylation regulate the
RT initiation of dynein-driven transport in neurons.";
RL Cell Rep. 14:2637-2652(2016).
RN [16]
RP DETYROSINATION.
RX PubMed=29146869; DOI=10.1126/science.aao5676;
RA Nieuwenhuis J., Adamopoulos A., Bleijerveld O.B., Mazouzi A., Stickel E.,
RA Celie P., Altelaar M., Knipscheer P., Perrakis A., Blomen V.A.,
RA Brummelkamp T.R.;
RT "Vasohibins encode tubulin detyrosinating activity.";
RL Science 358:1453-1456(2017).
RN [17]
RP GLUTAMYLATION AT GLU-443.
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 [18]
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 [19]
RP STRUCTURE BY NMR OF 416-451 IN COMPLEX WITH CLIP1.
RX PubMed=17563362; DOI=10.1073/pnas.0703876104;
RA Mishima M., Maesaki R., Kasa M., Watanabe T., Fukata M., Kaibuchi K.,
RA Hakoshima T.;
RT "Structural basis for tubulin recognition by cytoplasmic linker protein 170
RT and its autoinhibition.";
RL Proc. Natl. Acad. Sci. U.S.A. 104:10346-10351(2007).
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: Dimer of alpha and beta chains. A typical microtubule is a
CC hollow water-filled tube with an outer diameter of 25 nm and an inner
CC diameter of 15 nM. Alpha-beta heterodimers associate head-to-tail to
CC form protofilaments running lengthwise along the microtubule wall with
CC the beta-tubulin subunit facing the microtubule plus end conferring a
CC structural polarity. Microtubules usually have 13 protofilaments but
CC different protofilament numbers can be found in some organisms and
CC specialized cells. Nascent tubulin polypeptide interacts (via beta-
CC tubulin MREC motif) with TTC5/STRAP; this interaction may result in
CC tubulin mRNA-targeted degradation (PubMed:31727855).
CC {ECO:0000269|PubMed:17563362, ECO:0000269|PubMed:31727855}.
CC -!- INTERACTION:
CC P68363; Q6RW13: AGTRAP; NbExp=3; IntAct=EBI-487083, EBI-741181;
CC P68363; P05067: APP; NbExp=3; IntAct=EBI-487083, EBI-77613;
CC P68363; P37840: SNCA; NbExp=3; IntAct=EBI-487083, EBI-985879;
CC P68363; Q13509: TUBB3; NbExp=3; IntAct=EBI-487083, EBI-350989;
CC P68363; Q8AZK7: EBNA-LP; Xeno; NbExp=3; IntAct=EBI-487083, EBI-1185167;
CC P68363-2; Q8WUW1: BRK1; NbExp=3; IntAct=EBI-25895616, EBI-2837444;
CC P68363-2; P50990: CCT8; NbExp=3; IntAct=EBI-25895616, EBI-356507;
CC -!- SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=P68363-1; Sequence=Displayed;
CC Name=2;
CC IsoId=P68363-2; Sequence=VSP_055764;
CC -!- INDUCTION: Autoregulated by feedback control of mRNA degradation
CC (PubMed:31727855). In excess of soluble tubulin, TTC5/STRAP cofactor
CC triggers co-translation degradation of tubulin mRNA (PubMed:31727855).
CC {ECO:0000269|PubMed:31727855}.
CC -!- DOMAIN: The MREC motif mediates interaction with TTC5/STRAP and may be
CC critical for tubulin autoregulation. {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). Polyglutamylation plays a key role in microtubule
CC severing by spastin (SPAST). SPAST preferentially recognizes and acts
CC on microtubules decorated with short polyglutamate tails: severing
CC activity by SPAST increases as the number of glutamates per tubulin
CC rises from one to eight, but decreases beyond this glutamylation
CC threshold (PubMed:26875866). Glutamylation is also involved in cilia
CC motility (By similarity). {ECO:0000250|UniProtKB:P99024,
CC ECO:0000269|PubMed:26875866}.
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. Both
CC polyglutamylation and monoglycylation can coexist on the same protein
CC on adjacent residues, and lowering glycylation levels increases
CC polyglutamylation, and reciprocally. {ECO:0000250|UniProtKB:P07437,
CC ECO:0000305|PubMed:19524510}.
CC -!- PTM: Acetylation of alpha chains at Lys-40 is located inside the
CC microtubule lumen. This modification has been correlated with increased
CC microtubule stability, intracellular transport and ciliary assembly.
CC {ECO:0000269|PubMed:24906155}.
CC -!- PTM: Methylation of alpha chains at Lys-40 is found in mitotic
CC microtubules and is required for normal mitosis and cytokinesis
CC contributing to genomic stability. {ECO:0000305|PubMed:27518565}.
CC -!- PTM: Nitration of Tyr-451 is irreversible and interferes with normal
CC dynein intracellular distribution. {ECO:0000269|PubMed:10339593}.
CC -!- PTM: Undergoes a tyrosination/detyrosination cycle, the cyclic removal
CC and re-addition of a C-terminal tyrosine residue by the enzymes tubulin
CC tyrosine carboxypeptidase (VASH1 or VASH2) and tubulin tyrosine ligase
CC (TTL), respectively. {ECO:0000269|PubMed:25908662,
CC ECO:0000269|PubMed:26972003, ECO:0000269|PubMed:29146869}.
CC -!- PTM: [Tubulin alpha-1B chain]: Tyrosination promotes microtubule
CC interaction with CAP-Gly domain-containing proteins such as CLIP1,
CC CLIP2 and DCTN1 (By similarity). Tyrosination regulates the initiation
CC of dynein-dynactin motility via interaction with DCTN1, which brings
CC the dynein-dynactin complex into contact with microtubules
CC (PubMed:26972003). In neurons, tyrosinated tubulins mediate the
CC initiation of retrograde vesicle transport (By similarity).
CC {ECO:0000250|UniProtKB:P05213, ECO:0000250|UniProtKB:Q71U36,
CC ECO:0000269|PubMed:26972003}.
CC -!- PTM: [Detyrosinated tubulin alpha-1B chain]: Detyrosination is involved
CC in metaphase plate congression by guiding chromosomes during mitosis:
CC detyrosination promotes interaction with CENPE, promoting pole-proximal
CC transport of chromosomes toward the equator (PubMed:25908662).
CC Detyrosination increases microtubules-dependent mechanotransduction in
CC dystrophic cardiac and skeletal muscle. In cardiomyocytes,
CC detyrosinated microtubules are required to resist to contractile
CC compression during contraction: detyrosination promotes association
CC with desmin (DES) at force-generating sarcomeres, leading to buckled
CC microtubules and mechanical resistance to contraction (By similarity).
CC {ECO:0000250|UniProtKB:P05213, ECO:0000269|PubMed:25908662}.
CC -!- SIMILARITY: Belongs to the tubulin family. {ECO:0000305}.
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DR EMBL; K00558; AAA91576.1; -; mRNA.
DR EMBL; AF081484; AAC31959.1; -; mRNA.
DR EMBL; DQ400107; ABD60581.1; -; mRNA.
DR EMBL; BC000696; AAH00696.1; -; mRNA.
DR EMBL; BC001128; AAH01128.1; -; mRNA.
DR EMBL; BC006379; AAH06379.1; -; mRNA.
DR EMBL; BC006481; AAH06481.1; -; mRNA.
DR EMBL; BC008659; AAH08659.1; -; mRNA.
DR EMBL; BC009314; AAH09314.1; -; mRNA.
DR EMBL; BC009509; AAH09509.1; -; mRNA.
DR EMBL; BC009512; AAH09512.1; -; mRNA.
DR EMBL; BC009513; AAH09513.1; -; mRNA.
DR EMBL; BC010494; AAH10494.1; -; mRNA.
DR EMBL; BC011572; AAH11572.1; -; mRNA.
DR EMBL; BC015883; AAH15883.1; -; mRNA.
DR EMBL; BC017004; AAH17004.1; -; mRNA.
DR EMBL; BC021564; AAH21564.1; -; mRNA.
DR EMBL; BC030820; AAH30820.1; -; mRNA.
DR EMBL; BC071904; AAH71904.1; -; mRNA.
DR CCDS; CCDS31792.1; -. [P68363-1]
DR PIR; I77403; I77403.
DR RefSeq; NP_006073.2; NM_006082.2. [P68363-1]
DR PDB; 2E4H; NMR; -; B=416-451.
DR PDB; 5IJ0; EM; 3.80 A; A=1-437.
DR PDB; 5IJ9; EM; 3.70 A; A=1-437.
DR PDB; 5N5N; EM; 4.00 A; G/H/I/J/K/L=1-437.
DR PDB; 6E7B; EM; 3.50 A; A=1-437.
DR PDB; 6E7C; EM; 3.65 A; A=1-437.
DR PDB; 6I2I; EM; 3.60 A; A=1-451.
DR PDB; 6J4V; X-ray; 2.10 A; C=431-451.
DR PDB; 6J8O; X-ray; 1.85 A; C=444-451.
DR PDB; 6QUS; EM; 3.70 A; O/X=1-451.
DR PDB; 6QUY; EM; 3.80 A; A/C=1-451.
DR PDB; 6QVE; EM; 3.70 A; A/C=1-451.
DR PDB; 6QVJ; EM; 3.80 A; O/X=1-451.
DR PDB; 6S8L; X-ray; 1.80 A; A=1-451.
DR PDB; 7LXB; EM; 3.26 A; A/C/E/G/I/K/M/O=1-451.
DR PDB; 7M18; EM; 3.38 A; A/C/E/G/I/K/M/O=1-451.
DR PDB; 7M20; EM; 3.84 A; A/C/E/G/I/K/M/O/Q=1-451.
DR PDB; 7PJF; X-ray; 1.86 A; A=1-451.
DR PDB; 7SJ7; EM; 3.80 A; A/C/E/J/K/L=1-451.
DR PDB; 7SJ8; EM; 3.60 A; A/C/E/J/K/L=1-451.
DR PDB; 7SJ9; EM; 3.80 A; A/C/E/J/K/L=1-451.
DR PDB; 7SJA; EM; 3.80 A; A/C/E/J/K/L=1-451.
DR PDBsum; 2E4H; -.
DR PDBsum; 5IJ0; -.
DR PDBsum; 5IJ9; -.
DR PDBsum; 5N5N; -.
DR PDBsum; 6E7B; -.
DR PDBsum; 6E7C; -.
DR PDBsum; 6I2I; -.
DR PDBsum; 6J4V; -.
DR PDBsum; 6J8O; -.
DR PDBsum; 6QUS; -.
DR PDBsum; 6QUY; -.
DR PDBsum; 6QVE; -.
DR PDBsum; 6QVJ; -.
DR PDBsum; 6S8L; -.
DR PDBsum; 7LXB; -.
DR PDBsum; 7M18; -.
DR PDBsum; 7M20; -.
DR PDBsum; 7PJF; -.
DR PDBsum; 7SJ7; -.
DR PDBsum; 7SJ8; -.
DR PDBsum; 7SJ9; -.
DR PDBsum; 7SJA; -.
DR AlphaFoldDB; P68363; -.
DR SMR; P68363; -.
DR BioGRID; 115651; 347.
DR CORUM; P68363; -.
DR IntAct; P68363; 122.
DR MINT; P68363; -.
DR STRING; 9606.ENSP00000336799; -.
DR ChEMBL; CHEMBL3797010; -.
DR DrugBank; DB07574; 2-MERCAPTO-N-[1,2,3,10-TETRAMETHOXY-9-OXO-5,6,7,9-TETRAHYDRO-BENZO[A]HEPTALEN-7-YL]ACETAMIDE.
DR DrugBank; DB05147; CYT997.
DR DrugBank; DB01873; Epothilone D.
DR DrugBank; DB03010; Patupilone.
DR DrugCentral; P68363; -.
DR CarbonylDB; P68363; -.
DR GlyGen; P68363; 18 sites, 1 O-linked glycan (18 sites).
DR iPTMnet; P68363; -.
DR MetOSite; P68363; -.
DR PhosphoSitePlus; P68363; -.
DR SwissPalm; P68363; -.
DR BioMuta; TUBA1B; -.
DR DMDM; 55977474; -.
DR OGP; P68363; -.
DR SWISS-2DPAGE; P68363; -.
DR EPD; P68363; -.
DR jPOST; P68363; -.
DR MassIVE; P68363; -.
DR MaxQB; P68363; -.
DR PaxDb; P68363; -.
DR PeptideAtlas; P68363; -.
DR PRIDE; P68363; -.
DR ProteomicsDB; 57533; -. [P68363-1]
DR TopDownProteomics; P68363-1; -. [P68363-1]
DR ABCD; P68363; 2 sequenced antibodies.
DR Antibodypedia; 3156; 667 antibodies from 41 providers.
DR DNASU; 10376; -.
DR Ensembl; ENST00000336023.9; ENSP00000336799.5; ENSG00000123416.15. [P68363-1]
DR GeneID; 10376; -.
DR KEGG; hsa:10376; -.
DR MANE-Select; ENST00000336023.9; ENSP00000336799.5; NM_006082.3; NP_006073.2.
DR UCSC; uc001rtm.4; human. [P68363-1]
DR CTD; 10376; -.
DR DisGeNET; 10376; -.
DR GeneCards; TUBA1B; -.
DR HGNC; HGNC:18809; TUBA1B.
DR HPA; ENSG00000123416; Low tissue specificity.
DR MIM; 602530; gene.
DR neXtProt; NX_P68363; -.
DR OpenTargets; ENSG00000123416; -.
DR PharmGKB; PA162407332; -.
DR VEuPathDB; HostDB:ENSG00000123416; -.
DR eggNOG; KOG1376; Eukaryota.
DR GeneTree; ENSGT00950000182825; -.
DR HOGENOM; CLU_015718_0_0_1; -.
DR InParanoid; P68363; -.
DR OMA; ILTCHTT; -.
DR OrthoDB; 514396at2759; -.
DR PhylomeDB; P68363; -.
DR TreeFam; TF300314; -.
DR PathwayCommons; P68363; -.
DR Reactome; R-HSA-1445148; Translocation of SLC2A4 (GLUT4) to the plasma membrane.
DR Reactome; R-HSA-190840; Microtubule-dependent trafficking of connexons from Golgi to the plasma membrane.
DR Reactome; R-HSA-190861; Gap junction assembly.
DR Reactome; R-HSA-2132295; MHC class II antigen presentation.
DR Reactome; R-HSA-2467813; Separation of Sister Chromatids.
DR Reactome; R-HSA-2500257; Resolution of Sister Chromatid Cohesion.
DR Reactome; R-HSA-3371497; HSP90 chaperone cycle for steroid hormone receptors (SHR) in the presence of ligand.
DR Reactome; R-HSA-380320; Recruitment of NuMA to mitotic centrosomes.
DR Reactome; R-HSA-389960; Formation of tubulin folding intermediates by CCT/TriC.
DR Reactome; R-HSA-389977; Post-chaperonin tubulin folding pathway.
DR Reactome; R-HSA-437239; Recycling pathway of L1.
DR Reactome; R-HSA-5610787; Hedgehog 'off' state.
DR Reactome; R-HSA-5617833; Cilium Assembly.
DR Reactome; R-HSA-5620924; Intraflagellar transport.
DR Reactome; R-HSA-5626467; RHO GTPases activate IQGAPs.
DR Reactome; R-HSA-5663220; RHO GTPases Activate Formins.
DR Reactome; R-HSA-6807878; COPI-mediated anterograde transport.
DR Reactome; R-HSA-6811434; COPI-dependent Golgi-to-ER retrograde traffic.
DR Reactome; R-HSA-6811436; COPI-independent Golgi-to-ER retrograde traffic.
DR Reactome; R-HSA-68877; Mitotic Prometaphase.
DR Reactome; R-HSA-8852276; The role of GTSE1 in G2/M progression after G2 checkpoint.
DR Reactome; R-HSA-8955332; Carboxyterminal post-translational modifications of tubulin.
DR Reactome; R-HSA-9013407; RHOH GTPase cycle.
DR Reactome; R-HSA-9609690; HCMV Early Events.
DR Reactome; R-HSA-9609736; Assembly and cell surface presentation of NMDA receptors.
DR Reactome; R-HSA-9619483; Activation of AMPK downstream of NMDARs.
DR Reactome; R-HSA-9646399; Aggrephagy.
DR Reactome; R-HSA-9648025; EML4 and NUDC in mitotic spindle formation.
DR Reactome; R-HSA-9668328; Sealing of the nuclear envelope (NE) by ESCRT-III.
DR Reactome; R-HSA-983189; Kinesins.
DR SignaLink; P68363; -.
DR SIGNOR; P68363; -.
DR BioGRID-ORCS; 10376; 621 hits in 1052 CRISPR screens.
DR ChiTaRS; TUBA1B; human.
DR EvolutionaryTrace; P68363; -.
DR GeneWiki; TUBA1B; -.
DR GenomeRNAi; 10376; -.
DR Pharos; P68363; Tchem.
DR PRO; PR:P68363; -.
DR Proteomes; UP000005640; Chromosome 12.
DR RNAct; P68363; protein.
DR Bgee; ENSG00000123416; Expressed in ventricular zone and 114 other tissues.
DR ExpressionAtlas; P68363; baseline and differential.
DR Genevisible; P68363; HS.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0005881; C:cytoplasmic microtubule; IEA:Ensembl.
DR GO; GO:0005874; C:microtubule; IDA:UniProtKB.
DR GO; GO:0015630; C:microtubule cytoskeleton; IDA:HPA.
DR GO; GO:0003725; F:double-stranded RNA binding; IDA:MGI.
DR GO; GO:0005525; F:GTP binding; IBA:GO_Central.
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:0071353; P:cellular response to interleukin-4; IEA:Ensembl.
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 DisProt; DP02251; -.
DR Gene3D; 1.10.287.600; -; 1.
DR Gene3D; 3.30.1330.20; -; 1.
DR Gene3D; 3.40.50.1440; -; 1.
DR InterPro; IPR002452; Alpha_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; PR01162; ALPHATUBULIN.
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.
PE 1: Evidence at protein level;
KW 3D-structure; Acetylation; Alternative splicing; Cytoplasm; Cytoskeleton;
KW Direct protein sequencing; GTP-binding; Isopeptide bond; Methylation;
KW Microtubule; Nitration; Nucleotide-binding; Phosphoprotein;
KW Reference proteome; Ubl conjugation.
FT CHAIN 1..451
FT /note="Tubulin alpha-1B chain"
FT /id="PRO_0000048108"
FT CHAIN 1..450
FT /note="Detyrosinated tubulin alpha-1B chain"
FT /evidence="ECO:0000305|PubMed:25908662,
FT ECO:0000305|PubMed:29146869"
FT /id="PRO_0000437384"
FT REGION 432..451
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 1..4
FT /note="MREC motif"
FT /evidence="ECO:0000269|PubMed:31727855"
FT BINDING 142..148
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000255"
FT SITE 451
FT /note="Involved in polymerization"
FT MOD_RES 40
FT /note="N6,N6,N6-trimethyllysine; alternate"
FT /evidence="ECO:0000269|PubMed:27518565"
FT MOD_RES 40
FT /note="N6-acetyllysine; alternate"
FT /evidence="ECO:0000269|PubMed:24906155"
FT MOD_RES 48
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|Ref.6"
FT MOD_RES 232
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|Ref.6"
FT MOD_RES 282
FT /note="3'-nitrotyrosine"
FT /evidence="ECO:0000250|UniProtKB:P68373"
FT MOD_RES 339
FT /note="Omega-N-methylarginine"
FT /evidence="ECO:0000269|Ref.6"
FT MOD_RES 439
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P68373"
FT MOD_RES 443
FT /note="5-glutamyl polyglutamate"
FT /evidence="ECO:0000269|PubMed:32747782"
FT MOD_RES 445
FT /note="5-glutamyl polyglutamate"
FT /evidence="ECO:0000250|UniProtKB:P68369"
FT MOD_RES 451
FT /note="3'-nitrotyrosine"
FT /evidence="ECO:0000269|PubMed:10339593"
FT CROSSLNK 326
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in ubiquitin)"
FT CROSSLNK 370
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in ubiquitin)"
FT VAR_SEQ 108..223
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_055764"
FT CONFLICT 131
FT /note="G -> R (in Ref. 1; AAA91576)"
FT /evidence="ECO:0000305"
FT CONFLICT 290
FT /note="E -> D (in Ref. 1; AAA91576)"
FT /evidence="ECO:0000305"
FT CONFLICT 308
FT /note="R -> G (in Ref. 1; AAA91576)"
FT /evidence="ECO:0000305"
FT CONFLICT 340
FT /note="S -> T (in Ref. 1; AAA91576)"
FT /evidence="ECO:0000305"
FT STRAND 4..9
FT /evidence="ECO:0007829|PDB:6S8L"
FT HELIX 10..28
FT /evidence="ECO:0007829|PDB:6S8L"
FT STRAND 37..39
FT /evidence="ECO:0007829|PDB:7LXB"
FT STRAND 41..43
FT /evidence="ECO:0007829|PDB:7LXB"
FT HELIX 48..51
FT /evidence="ECO:0007829|PDB:6S8L"
FT STRAND 53..55
FT /evidence="ECO:0007829|PDB:6S8L"
FT STRAND 57..59
FT /evidence="ECO:0007829|PDB:7PJF"
FT STRAND 61..63
FT /evidence="ECO:0007829|PDB:6S8L"
FT STRAND 65..72
FT /evidence="ECO:0007829|PDB:6S8L"
FT HELIX 73..80
FT /evidence="ECO:0007829|PDB:6S8L"
FT TURN 82..86
FT /evidence="ECO:0007829|PDB:6S8L"
FT HELIX 89..91
FT /evidence="ECO:0007829|PDB:6S8L"
FT STRAND 92..94
FT /evidence="ECO:0007829|PDB:6S8L"
FT HELIX 103..107
FT /evidence="ECO:0007829|PDB:6S8L"
FT TURN 108..110
FT /evidence="ECO:0007829|PDB:7PJF"
FT HELIX 111..113
FT /evidence="ECO:0007829|PDB:6S8L"
FT HELIX 115..127
FT /evidence="ECO:0007829|PDB:6S8L"
FT STRAND 134..143
FT /evidence="ECO:0007829|PDB:6S8L"
FT HELIX 144..160
FT /evidence="ECO:0007829|PDB:6S8L"
FT TURN 161..163
FT /evidence="ECO:0007829|PDB:7PJF"
FT STRAND 165..172
FT /evidence="ECO:0007829|PDB:6S8L"
FT HELIX 175..177
FT /evidence="ECO:0007829|PDB:6S8L"
FT HELIX 183..194
FT /evidence="ECO:0007829|PDB:6S8L"
FT TURN 195..197
FT /evidence="ECO:0007829|PDB:6S8L"
FT STRAND 199..205
FT /evidence="ECO:0007829|PDB:6S8L"
FT HELIX 206..215
FT /evidence="ECO:0007829|PDB:6S8L"
FT HELIX 224..243
FT /evidence="ECO:0007829|PDB:6S8L"
FT STRAND 247..249
FT /evidence="ECO:0007829|PDB:7PJF"
FT HELIX 252..259
FT /evidence="ECO:0007829|PDB:6S8L"
FT STRAND 261..264
FT /evidence="ECO:0007829|PDB:6S8L"
FT STRAND 269..273
FT /evidence="ECO:0007829|PDB:6S8L"
FT HELIX 288..293
FT /evidence="ECO:0007829|PDB:6S8L"
FT HELIX 294..296
FT /evidence="ECO:0007829|PDB:6S8L"
FT HELIX 298..300
FT /evidence="ECO:0007829|PDB:6S8L"
FT STRAND 301..303
FT /evidence="ECO:0007829|PDB:6S8L"
FT HELIX 307..309
FT /evidence="ECO:0007829|PDB:6S8L"
FT STRAND 312..322
FT /evidence="ECO:0007829|PDB:6S8L"
FT HELIX 325..336
FT /evidence="ECO:0007829|PDB:6S8L"
FT STRAND 345..347
FT /evidence="ECO:0007829|PDB:7LXB"
FT STRAND 352..356
FT /evidence="ECO:0007829|PDB:6S8L"
FT STRAND 372..381
FT /evidence="ECO:0007829|PDB:6S8L"
FT HELIX 382..384
FT /evidence="ECO:0007829|PDB:6S8L"
FT HELIX 385..399
FT /evidence="ECO:0007829|PDB:6S8L"
FT TURN 400..404
FT /evidence="ECO:0007829|PDB:6S8L"
FT HELIX 405..409
FT /evidence="ECO:0007829|PDB:6S8L"
FT TURN 410..412
FT /evidence="ECO:0007829|PDB:6S8L"
FT HELIX 416..435
FT /evidence="ECO:0007829|PDB:6S8L"
FT STRAND 448..450
FT /evidence="ECO:0007829|PDB:6J8O"
SQ SEQUENCE 451 AA; 50152 MW; 94355B4EC2086429 CRC64;
MRECISIHVG QAGVQIGNAC WELYCLEHGI QPDGQMPSDK TIGGGDDSFN TFFSETGAGK
HVPRAVFVDL EPTVIDEVRT GTYRQLFHPE QLITGKEDAA NNYARGHYTI GKEIIDLVLD
RIRKLADQCT GLQGFLVFHS FGGGTGSGFT SLLMERLSVD YGKKSKLEFS IYPAPQVSTA
VVEPYNSILT THTTLEHSDC AFMVDNEAIY DICRRNLDIE RPTYTNLNRL ISQIVSSITA
SLRFDGALNV DLTEFQTNLV PYPRIHFPLA TYAPVISAEK AYHEQLSVAE ITNACFEPAN
QMVKCDPRHG KYMACCLLYR GDVVPKDVNA AIATIKTKRS IQFVDWCPTG FKVGINYQPP
TVVPGGDLAK VQRAVCMLSN TTAIAEAWAR LDHKFDLMYA KRAFVHWYVG EGMEEGEFSE
AREDMAALEK DYEEVGVDSV EGEGEEEGEE Y
