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 02-SEP-2026, entry version 201. DE RecName: Full=Tubulin alpha-1B chain; DE EC=3.6.5.- {ECO:0000269|PubMed:34996871, ECO:0000269|PubMed:38609661}; 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, RC Skin, 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 FUNCTION, SUBUNIT, AND MUTAGENESIS OF GLU-254. RX PubMed=38305685; DOI=10.1126/science.adk6160; RA Brito C., Serna M., Guerra P., Llorca O., Surrey T.; RT "Transition of human gamma-tubulin ring complex into a closed conformation RT during microtubule nucleation."; RL Science 383:870-876(2024). RN [20] {ECO:0007744|PDB:2E4H} 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). RN [21] {ECO:0007744|PDB:7SJ7, ECO:0007744|PDB:7SJ8, ECO:0007744|PDB:7SJ9, ECO:0007744|PDB:7SJA} RP STRUCTURE BY ELECTRON MICROSCOPY (3.60 ANGSTROMS) IN COMPLEX WITH RP BETA-TUBULIN; MAGNESIUM AND GTP, FUNCTION, CATALYTIC ACTIVITY, COFACTOR, RP ACTIVE SITE, SUBCELLULAR LOCATION, SUBUNIT, AND MUTAGENESIS OF GLU-254. RX PubMed=34996871; DOI=10.1073/pnas.2114994119; RA LaFrance B.J., Roostalu J., Henkin G., Greber B.J., Zhang R., Normanno D., RA McCollum C.O., Surrey T., Nogales E.; RT "Structural transitions in the GTP cap visualized by cryo-electron RT microscopy of catalytically inactive microtubules."; RL Proc. Natl. Acad. Sci. U.S.A. 119:0-0(2022). RN [22] {ECO:0007744|PDB:7Z6S} RP STRUCTURE BY ELECTRON MICROSCOPY (2.9 ANGSTROMS) IN COMPLEX WITH RP BETA-TUBULIN; KIAA0895L; MAGNESIUM AND GTP, COFACTOR, SUBCELLULAR LOCATION, RP AND SUBUNIT. RX PubMed=35482892; DOI=10.1126/science.abn6020; RA Landskron L., Bak J., Adamopoulos A., Kaplani K., Moraiti M., RA van den Hengel L.G., Song J.Y., Bleijerveld O.B., Nieuwenhuis J., RA Heidebrecht T., Henneman L., Moutin M.J., Barisic M., Taraviras S., RA Perrakis A., Brummelkamp T.R.; RT "Posttranslational modification of microtubules by the MATCAP RT detyrosinase."; RL Science 376:eabn6020-eabn6020(2022). RN [23] {ECO:0007744|PDB:8VA2, ECO:0007744|PDB:8VRJ, ECO:0007744|PDB:8VRK, ECO:0007744|PDB:8VT7} RP STRUCTURE BY ELECTRON MICROSCOPY (2.66 ANGSTROMS) IN COMPLEXES WITH MZT1; RP ACTB; TUBB3 AND THE GAMMA-TUBULIN RING COMPLEX, FUNCTION, CATALYTIC RP ACTIVITY, COFACTOR, SUBUNIT, AND MUTAGENESIS OF GLU-254. RX PubMed=38609661; DOI=10.1038/s41594-024-01264-z; RA Aher A., Urnavicius L., Xue A., Neselu K., Kapoor T.M.; RT "Structure of the gamma-tubulin ring complex-capped microtubule."; RL Nat. Struct. Mol. Biol. 31:1124-1133(2024). CC -!- FUNCTION: Tubulin is the major constituent of microtubules, protein CC filaments consisting of alpha- and beta-tubulin heterodimers CC (PubMed:38305685, PubMed:34996871, PubMed:38609661). Microtubules grow CC by the addition of GTP-tubulin dimers to the microtubule end, where a CC stabilizing cap forms (PubMed:38305685, PubMed:34996871, CC PubMed:38609661). Below the cap, tubulin dimers are in GDP-bound state, CC owing to GTPase activity of alpha-tubulin (PubMed:34996871, CC PubMed:38609661). {ECO:0000269|PubMed:34996871, CC ECO:0000269|PubMed:38305685, ECO:0000269|PubMed:38609661}. CC -!- CATALYTIC ACTIVITY: CC Reaction=GTP + H2O = GDP + phosphate + H(+); Xref=Rhea:RHEA:19669, CC ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:37565, CC ChEBI:CHEBI:43474, ChEBI:CHEBI:58189; CC Evidence={ECO:0000269|PubMed:34996871, ECO:0000269|PubMed:38609661}; CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:19670; CC Evidence={ECO:0000269|PubMed:34996871}; CC -!- COFACTOR: CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420; CC Evidence={ECO:0000269|PubMed:34996871, ECO:0000269|PubMed:35482892, CC ECO:0000269|PubMed:38609661}; CC -!- SUBUNIT: Heterodimer of alpha- and beta-tubulin (PubMed:17563362, CC PubMed:34996871, PubMed:35482892, PubMed:38305685, PubMed:38609661). 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 (PubMed:34996871, CC PubMed:35482892). 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 (PubMed:34996871, PubMed:35482892, PubMed:38305685, CC PubMed:38609661). Microtubules usually have 13 protofilaments but CC different protofilament numbers can be found in some organisms and CC specialized cells (PubMed:34996871, PubMed:35482892, PubMed:38305685, CC PubMed:38609661). Interacts with gamma-tubulin; the interaction allows CC microtubules to nucleate from the gamma-tubulin ring complex (gTuRC) CC (PubMed:38305685, PubMed:38609661). Nascent microtubule interacts (via CC alpha-tubulin MREC motif) with TTC5/STRAP; this interaction may result CC in tubulin mRNA-targeted degradation (PubMed:31727855). Component of CC sperm flagellar doublet microtubules (By similarity). CC {ECO:0000250|UniProtKB:P68369, ECO:0000269|PubMed:17563362, CC ECO:0000269|PubMed:31727855, ECO:0000269|PubMed:34996871, CC ECO:0000269|PubMed:35482892, ECO:0000269|PubMed:38609661}. 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=4; 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 {ECO:0000269|PubMed:34996871, ECO:0000269|PubMed:35482892}. 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 cotranslation 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 (MATCAP1/KIAA0895L, VASH1 or VASH2) and CC tubulin tyrosine ligase (TTL), respectively. CC {ECO:0000269|PubMed:25908662, ECO:0000269|PubMed:26972003, CC 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}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- 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_006082.3. [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 PDB; 7Z6S; EM; 2.90 A; A/K=1-451. DR PDB; 7ZCW; EM; 3.60 A; A/E=1-451. DR PDB; 8T42; EM; 3.60 A; A/F=1-451. DR PDB; 8U3Z; EM; 3.60 A; A/F=1-451. DR PDB; 8V2J; EM; 2.90 A; A/D=1-451. DR PDB; 8VA2; EM; 4.50 A; a/b=1-451. DR PDB; 8VRJ; EM; 7.70 A; 1/O/P/Q/R/S/T/U/V/W/X/Y/Z=1-451. DR PDB; 8VRK; EM; 8.50 A; 1/O/P/Q/R/S/T/U/V/W/X/Y/Z=1-451. DR PDB; 8VT7; EM; 2.66 A; B/J=1-451. DR PDB; 9BP6; EM; 3.10 A; A/I=1-451. DR PDB; 9CMM; EM; 3.10 A; A/C/E/I=1-451. DR PDB; 9COC; EM; 2.90 A; A/C/D/I=1-451. DR PDB; 9F3B; EM; 3.60 A; A/C/E/G/I/K=1-42, A/C/E/G/I/K=47-441. DR PDB; 9F3H; EM; 4.30 A; A/C/E/G/I/K=1-42, A/C/E/G/I/K=47-441. DR PDB; 9F3R; EM; 4.30 A; A/C/E/G/I/K=1-42, A/C/E/G/I/K=47-441. DR PDB; 9F3S; EM; 4.20 A; A/C/E/G/I/K=1-42, A/C/E/G/I/K=47-441. DR PDB; 9HQ4; EM; 3.28 A; A/C=1-451. DR AlphaFoldDB; P68363; -. DR EMDB; EMD-0331; -. DR EMDB; EMD-14529; -. DR EMDB; EMD-14634; -. DR EMDB; EMD-23569; -. DR EMDB; EMD-23615; -. DR EMDB; EMD-23627; -. DR EMDB; EMD-25156; -. DR EMDB; EMD-25157; -. DR EMDB; EMD-25159; -. DR EMDB; EMD-25160; -. DR EMDB; EMD-32033; -. DR EMDB; EMD-3589; -. DR EMDB; EMD-41018; -. DR EMDB; EMD-42884; -. DR EMDB; EMD-42916; -. DR EMDB; EMD-43085; -. DR EMDB; EMD-43482; -. DR EMDB; EMD-43483; -. DR EMDB; EMD-43519; -. DR EMDB; EMD-44762; -. DR EMDB; EMD-45750; -. DR EMDB; EMD-45775; -. DR EMDB; EMD-4643; -. DR EMDB; EMD-4644; -. DR EMDB; EMD-4650; -. DR EMDB; EMD-4654; -. DR EMDB; EMD-50172; -. DR EMDB; EMD-50174; -. DR EMDB; EMD-50177; -. DR EMDB; EMD-50178; -. DR EMDB; EMD-52338; -. DR EMDB; EMD-8094; -. DR EMDB; EMD-8095; -. DR EMDB; EMD-8997; -. DR EMDB; EMD-8998; -. DR SMR; P68363; -. DR BioGRID; 115651; 539. DR CORUM; P68363; -. DR FunCoup; P68363; 1876. DR IntAct; P68363; 206. DR MINT; P68363; -. DR NDEx; IQUERY-CP-TUBA1B; 8 NDEx IQuery Curated Pathways. DR STRING; 9606.ENSP00000336799; -. DR BindingDB; P68363; -. 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; DB01873; Epothilone D. DR DrugBank; DB08974; Flubendazole. DR DrugBank; DB05147; Lexibulin. DR DrugBank; DB03010; Patupilone. DR DrugCentral; P68363; -. DR CarbonylDB; P68363; -. DR GlyCosmos; P68363; 18 sites, 1 glycan. DR GlyGen; P68363; 24 sites, 1 N-linked glycan (1 site), 1 O-linked glycan (23 sites). DR iPTMnet; P68363; -. DR MetOSite; P68363; -. DR PhosphoSitePlus; P68363; -. DR SwissPalm; P68363; -. DR BioMuta; TUBA1B; -. DR DMDM; 55977474; -. DR OGP; P68363; -. DR jPOST; P68363; -. DR MassIVE; P68363; -. DR PaxDb; 9606-ENSP00000336799; -. DR PeptideAtlas; P68363; -. DR PRIDE; P68363; -. DR ProteomicsDB; 57533; -. [P68363-1] DR Pumba; P68363; -. DR TopDownProteomics; P68363-1; -. [P68363-1] DR ABCD; P68363; 2 sequenced antibodies. DR Antibodypedia; 3156; 666 antibodies from 45 providers. DR DNASU; 10376; -. DR Ensembl; ENST00000336023.9; ENSP00000336799.5; ENSG00000123416.16. [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 AGR; HGNC:18809; -. DR ClinPGx; PA162407332; -. 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 OpenTargets; ENSG00000123416; -. DR VEuPathDB; HostDB:ENSG00000123416; -. DR eggNOG; KOG1376; Eukaryota. DR GeneTree; ENSGT00950000182825; -. DR HOGENOM; CLU_015718_0_0_1; -. DR InParanoid; P68363; -. DR OMA; WARTRNT; -. DR OrthoDB; 9540336at2759; -. DR PAN-GO; P68363; 7 GO annotations based on evolutionary models. DR PhylomeDB; P68363; -. 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-5620920; Cargo trafficking to the periciliary membrane. 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 Reactome; R-HSA-9833482; PKR-mediated signaling. DR SignaLink; P68363; -. DR SIGNOR; P68363; -. DR Agora; ENSG00000123416; -. DR BioGRID-ORCS; 10376; 636 hits in 1112 CRISPR screens. DR CD-CODE; 232F8A39; P-body. DR CD-CODE; 91857CE7; Nucleolus. DR CD-CODE; FB4E32DD; Presynaptic clusters and postsynaptic densities. 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 116 other cell types or tissues. DR ExpressionAtlas; P68363; baseline and differential. DR GO; GO:0005929; C:cilium; IDA:HPA. 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:UniProtKB. DR GO; GO:0003725; F:double-stranded RNA binding; IDA:MGI. DR GO; GO:0005525; F:GTP binding; IDA:UniProtKB. DR GO; GO:0003924; F:GTPase activity; IDA:UniProtKB. DR GO; GO:0005200; F:structural constituent of cytoskeleton; IDA:UniProtKB. 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; IDA:UniProtKB. 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:0030182; P:neuron differentiation; IBA:GO_Central. DR CDD; cd02186; alpha_tubulin; 1. DR DisProt; DP02251; -. DR FunFam; 1.10.287.600:FF:000005; Tubulin alpha chain; 1. DR FunFam; 3.30.1330.20:FF:000001; Tubulin alpha chain; 1. DR FunFam; 3.40.50.1440:FF:000002; Tubulin alpha chain; 1. DR Gene3D; 1.10.287.600; Helix hairpin bin; 1. DR Gene3D; 3.30.1330.20; Tubulin/FtsZ, C-terminal domain; 1. DR Gene3D; 3.40.50.1440; Tubulin/FtsZ, GTPase domain; 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; TUBULIN; 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; SSF55307; Tubulin C-terminal domain-like; 1. DR SUPFAM; SSF52490; Tubulin nucleotide-binding domain-like; 1. DR PROSITE; PS00227; TUBULIN; 1. 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 PDBsum; 7Z6S; -. DR PDBsum; 7ZCW; -. DR PDBsum; 8T42; -. DR PDBsum; 8U3Z; -. DR PDBsum; 8V2J; -. DR PDBsum; 8VA2; -. DR PDBsum; 8VRJ; -. DR PDBsum; 8VRK; -. DR PDBsum; 8VT7; -. DR PDBsum; 9BP6; -. DR PDBsum; 9CMM; -. DR PDBsum; 9COC; -. DR PDBsum; 9F3B; -. DR PDBsum; 9F3H; -. DR PDBsum; 9F3R; -. DR PDBsum; 9F3S; -. DR PDBsum; 9HQ4; -. PE 1: Evidence at protein level; KW 3D-structure; Acetylation; Alternative splicing; Cytoplasm; Cytoskeleton; KW Direct protein sequencing; GTP-binding; Hydrolase; Isopeptide bond; KW Methylation; Microtubule; Nitration; Nucleotide-binding; Phosphoprotein; KW Proteomics identification; 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 ACT_SITE 254 FT /evidence="ECO:0000269|PubMed:34996871" FT BINDING 10 FT /ligand="GTP" FT /ligand_id="ChEBI:CHEBI:37565" FT /evidence="ECO:0000269|PubMed:38609661, FT ECO:0007744|PDB:8VT7" FT BINDING 11 FT /ligand="GTP" FT /ligand_id="ChEBI:CHEBI:37565" FT /evidence="ECO:0000269|PubMed:34996871, FT ECO:0000269|PubMed:35482892, ECO:0000269|PubMed:38609661, FT ECO:0007744|PDB:7SJ7, ECO:0007744|PDB:7Z6S, FT ECO:0007744|PDB:8VT7" FT BINDING 12 FT /ligand="GTP" FT /ligand_id="ChEBI:CHEBI:37565" FT /evidence="ECO:0000269|PubMed:38609661, FT ECO:0007744|PDB:8VT7" FT BINDING 15 FT /ligand="GTP" FT /ligand_id="ChEBI:CHEBI:37565" FT /evidence="ECO:0000269|PubMed:38609661, FT ECO:0007744|PDB:8VT7" FT BINDING 71 FT /ligand="GTP" FT /ligand_id="ChEBI:CHEBI:37565" FT /evidence="ECO:0000269|PubMed:34996871, FT ECO:0000269|PubMed:35482892, ECO:0007744|PDB:7SJ7, FT ECO:0007744|PDB:7Z6S" FT BINDING 71 FT /ligand="Mg(2+)" FT /ligand_id="ChEBI:CHEBI:18420" FT /evidence="ECO:0000269|PubMed:34996871, FT ECO:0000269|PubMed:35482892, ECO:0000269|PubMed:38609661, FT ECO:0007744|PDB:7SJ7, ECO:0007744|PDB:7Z6S, FT ECO:0007744|PDB:8VT7" FT BINDING 99 FT /ligand="GTP" FT /ligand_id="ChEBI:CHEBI:37565" FT /evidence="ECO:0000269|PubMed:38609661, FT ECO:0007744|PDB:8VT7" FT BINDING 140 FT /ligand="GTP" FT /ligand_id="ChEBI:CHEBI:37565" FT /evidence="ECO:0000269|PubMed:34996871, FT ECO:0000269|PubMed:35482892, ECO:0000269|PubMed:38609661, FT ECO:0007744|PDB:7SJ7, ECO:0007744|PDB:7Z6S, FT ECO:0007744|PDB:8VT7" FT BINDING 143 FT /ligand="GTP" FT /ligand_id="ChEBI:CHEBI:37565" FT /evidence="ECO:0000269|PubMed:38609661, FT ECO:0007744|PDB:8VT7" FT BINDING 144 FT /ligand="GTP" FT /ligand_id="ChEBI:CHEBI:37565" FT /evidence="ECO:0000269|PubMed:34996871, FT ECO:0000269|PubMed:35482892, ECO:0000269|PubMed:38609661, FT ECO:0007744|PDB:7SJ7, ECO:0007744|PDB:7Z6S, FT ECO:0007744|PDB:8VT7" FT BINDING 145 FT /ligand="GTP" FT /ligand_id="ChEBI:CHEBI:37565" FT /evidence="ECO:0000269|PubMed:34996871, FT ECO:0000269|PubMed:35482892, ECO:0000269|PubMed:38609661, FT ECO:0007744|PDB:7SJ7, ECO:0007744|PDB:7Z6S, FT ECO:0007744|PDB:8VT7" FT BINDING 146 FT /ligand="GTP" FT /ligand_id="ChEBI:CHEBI:37565" FT /evidence="ECO:0000269|PubMed:38609661, FT ECO:0007744|PDB:8VT7" FT BINDING 179 FT /ligand="GTP" FT /ligand_id="ChEBI:CHEBI:37565" FT /evidence="ECO:0000269|PubMed:34996871, FT ECO:0000269|PubMed:35482892, ECO:0000269|PubMed:38609661, FT ECO:0007744|PDB:7SJ7, ECO:0007744|PDB:7Z6S, FT ECO:0007744|PDB:8VT7" FT BINDING 183 FT /ligand="GTP" FT /ligand_id="ChEBI:CHEBI:37565" FT /evidence="ECO:0000269|PubMed:38609661, FT ECO:0007744|PDB:8VT7" FT BINDING 206 FT /ligand="GTP" FT /ligand_id="ChEBI:CHEBI:37565" FT /evidence="ECO:0000269|PubMed:34996871, FT ECO:0000269|PubMed:35482892, ECO:0000269|PubMed:38609661, FT ECO:0007744|PDB:7SJ7, ECO:0007744|PDB:7Z6S, FT ECO:0007744|PDB:8VT7" FT BINDING 224 FT /ligand="GTP" FT /ligand_id="ChEBI:CHEBI:37565" FT /evidence="ECO:0000269|PubMed:38609661, FT ECO:0007744|PDB:8VT7" FT BINDING 228 FT /ligand="GTP" FT /ligand_id="ChEBI:CHEBI:37565" FT /evidence="ECO:0000269|PubMed:34996871, FT ECO:0000269|PubMed:35482892, ECO:0000269|PubMed:38609661, FT ECO:0007744|PDB:7SJ7, ECO:0007744|PDB:7Z6S, FT ECO:0007744|PDB:8VT7" FT BINDING 252 FT /ligand="GTP" FT /ligand_id="ChEBI:CHEBI:37565" FT /evidence="ECO:0000269|PubMed:38609661, FT ECO:0007744|PDB:8VT7" 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 MUTAGEN 254 FT /note="E->A: Abolished GTPase activity; microtubules have FT an expanded lattice with a negative twist and display high FT binding to microtubule-end binding proteins such as FT MAPRE3." FT /evidence="ECO:0000269|PubMed:34996871" FT MUTAGEN 254 FT /note="E->D: Promotes microtubule nucleation efficiency and FT slows GTP hydrolysis." FT /evidence="ECO:0000269|PubMed:38305685, FT ECO:0000269|PubMed:38609661" FT MUTAGEN 254 FT /note="E->N: Abolished GTPase activity; microtubules have FT an expanded lattice with a positive twist and display low FT binding to microtubule-end binding proteins such as FT MAPRE3." FT /evidence="ECO:0000269|PubMed:34996871" 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 44..46 FT /evidence="ECO:0007829|PDB:9BP6" 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 HELIX 111..113 FT /evidence="ECO:0007829|PDB:6S8L" FT HELIX 115..127 FT /evidence="ECO:0007829|PDB:6S8L" FT STRAND 129..131 FT /evidence="ECO:0007829|PDB:6E7B" FT STRAND 134..143 FT /evidence="ECO:0007829|PDB:6S8L" FT HELIX 145..149 FT /evidence="ECO:0007829|PDB:6S8L" FT HELIX 150..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 STRAND 179..182 FT /evidence="ECO:0007829|PDB:6E7B" FT HELIX 183..195 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 278..281 FT /evidence="ECO:0007829|PDB:8VT7" FT HELIX 283..287 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 339..341 FT /evidence="ECO:0007829|PDB:8VT7" FT STRAND 345..347 FT /evidence="ECO:0007829|PDB:7LXB" FT STRAND 352..356 FT /evidence="ECO:0007829|PDB:6S8L" FT HELIX 359..361 FT /evidence="ECO:0007829|PDB:6S8L" FT HELIX 368..370 FT /evidence="ECO:0007829|PDB:7M18" 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 HELIX 438..440 FT /evidence="ECO:0007829|PDB:7Z6S" 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 //