TBB_PIG
ID TBB_PIG Reviewed; 445 AA.
AC P02554;
DT 21-JUL-1986, integrated into UniProtKB/Swiss-Prot.
DT 21-JUL-1986, sequence version 1.
DT 03-AUG-2022, entry version 171.
DE RecName: Full=Tubulin beta chain;
DE AltName: Full=Beta-tubulin;
OS Sus scrofa (Pig).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Suina; Suidae; Sus.
OX NCBI_TaxID=9823;
RN [1]
RP PROTEIN SEQUENCE.
RC TISSUE=Brain;
RX PubMed=6945576; DOI=10.1073/pnas.78.7.4156;
RA Krauhs E., Little M., Kempf T., Hofer-Warbinek R., Ade W., Ponstingl H.;
RT "Complete amino acid sequence of beta-tubulin from porcine brain.";
RL Proc. Natl. Acad. Sci. U.S.A. 78:4156-4160(1981).
RN [2]
RP PROTEIN SEQUENCE OF 63-77.
RX PubMed=3170578; DOI=10.1016/s0021-9258(18)68165-7;
RA Linse K., Mandelkow E.M.;
RT "The GTP-binding peptide of beta-tubulin. Localization by direct
RT photoaffinity labeling and comparison with nucleotide-binding proteins.";
RL J. Biol. Chem. 263:15205-15210(1988).
RN [3]
RP GUANINE NUCLEOTIDE-BINDING SITES.
RX PubMed=6688710; DOI=10.1016/0003-9861(83)90056-5;
RA Zabrecky J.R., Cole R.D.;
RT "Localization of the ATP binding site on alpha-tubulin.";
RL Arch. Biochem. Biophys. 225:475-481(1983).
RN [4]
RP INTERACTION WITH NCKAP5L.
RX PubMed=26482847; DOI=10.1016/j.bbrc.2015.10.069;
RA Mori Y., Taniyama Y., Tanaka S., Fukuchi H., Terada Y.;
RT "Microtubule-bundling activity of the centrosomal protein, Cep169, and its
RT binding to microtubules.";
RL Biochem. Biophys. Res. Commun. 467:754-759(2015).
RN [5]
RP X-RAY CRYSTALLOGRAPHY (3.95 ANGSTROMS).
RX PubMed=11030624; DOI=10.1016/s0092-8674(00)00069-6;
RA Gigant B., Curmi P.A., Martin-Barbey C., Charbaut E., Lachkar S.,
RA Lebeau L., Siavoshian S., Sobel A., Knossow M.;
RT "The 4 A X-ray structure of a tubulin:stathmin-like domain complex.";
RL Cell 102:809-816(2000).
RN [6]
RP STRUCTURE BY ELECTRON MICROSCOPY (3.7 ANGSTROMS) OF 1-427.
RX PubMed=9428769; DOI=10.1038/34465;
RA Nogales E., Wolf S.G., Downing K.H.;
RT "Structure of the alpha beta tubulin dimer by electron crystallography.";
RL Nature 391:199-203(1998).
RN [7]
RP STRUCTURE BY ELECTRON MICROSCOPY (15.0 ANGSTROMS).
RX PubMed=10660047; DOI=10.1016/s0092-8674(00)81562-7;
RA Kikkawa M., Okada Y., Hirokawa N.;
RT "15 A resolution model of the monomeric kinesin motor, KIF1A.";
RL Cell 100:241-252(2000).
RN [8]
RP STRUCTURE BY ELECTRON MICROSCOPY (3.5 ANGSTROMS).
RX PubMed=11700061; DOI=10.1006/jmbi.2001.5077;
RA Loewe J., Li H., Downing K.H., Nogales E.;
RT "Refined structure of alpha beta-tubulin at 3.5 A resolution.";
RL J. Mol. Biol. 313:1045-1057(2001).
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. Interacts with NCKAP5L (PubMed:26482847).
CC {ECO:0000269|PubMed:26482847}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton.
CC -!- DOMAIN: The MREI motif is common among all beta-tubulin isoforms and
CC may be critical for tubulin autoregulation.
CC {ECO:0000250|UniProtKB:P07437}.
CC -!- PTM: Some glutamate residues at the C-terminus are polyglycylated,
CC resulting in polyglycine chains on the gamma-carboxyl group.
CC Glycylation is mainly limited to tubulin incorporated into axonemes
CC (cilia and flagella) whereas glutamylation is prevalent in neuronal
CC cells, centrioles, axonemes, and the mitotic spindle. Both
CC modifications can coexist on the same protein on adjacent residues, and
CC lowering polyglycylation levels increases polyglutamylation, and
CC reciprocally. Cilia and flagella glycylation is required for their
CC stability and maintenance. Flagella glycylation controls sperm
CC motility. {ECO:0000250|UniProtKB:A2AQ07}.
CC -!- PTM: Some glutamate residues at the C-terminus are polyglutamylated,
CC resulting in polyglutamate chains on the gamma-carboxyl group (By
CC similarity). Polyglutamylation plays a key role in microtubule severing
CC by spastin (SPAST). SPAST preferentially recognizes and acts on
CC 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 (By similarity). {ECO:0000250|UniProtKB:A2AQ07,
CC ECO:0000250|UniProtKB:Q71U36}.
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:0000250|UniProtKB:Q3ZCM7}.
CC -!- MISCELLANEOUS: The highly acidic C-terminal region may bind cations
CC such as calcium.
CC -!- MISCELLANEOUS: Pig brain contains at least two forms of this protein.
CC -!- SIMILARITY: Belongs to the tubulin family. {ECO:0000305}.
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DR PIR; A02973; UBPGB.
DR PDB; 1FFX; X-ray; 3.95 A; B/D=1-445.
DR PDB; 1IA0; EM; 15.00 A; B=1-445.
DR PDB; 1JFF; X-ray; 3.50 A; B=1-445.
DR PDB; 1TUB; X-ray; 3.70 A; B=1-427.
DR PDB; 2HXF; EM; 10.00 A; B=1-445.
DR PDB; 2HXH; EM; 11.00 A; B=1-445.
DR PDB; 3EDL; EM; 28.00 A; B/G=1-445.
DR PDB; 3J6E; EM; 4.70 A; B/D/F/H/J/L/N/P/R=1-427.
DR PDB; 3J6F; EM; 4.90 A; B/D/F/H/J/L/N/P/R=1-427.
DR PDB; 3J6G; EM; 5.50 A; B/D/F/H/J/L/N/P/R=1-427.
DR PDB; 3J6H; EM; 8.10 A; B=2-427.
DR PDB; 3J6P; EM; 8.20 A; B=1-445.
DR PDB; 3J7I; EM; 8.90 A; B=1-445.
DR PDB; 3JAK; EM; 3.50 A; B/D/F/G/H/I=1-445.
DR PDB; 3JAL; EM; 3.50 A; B/D/F/G/H/I=1-445.
DR PDB; 3JAR; EM; 3.50 A; B/D/F/G/H/I=1-445.
DR PDB; 3JAS; EM; 3.50 A; B/D/F/G/H/I=1-445.
DR PDB; 3JAT; EM; 3.50 A; B/D/F/G/H/I=1-445.
DR PDB; 3JAW; EM; 3.90 A; B/D=1-445.
DR PDB; 4ABO; EM; 8.60 A; A/C/E/G=1-445.
DR PDB; 4ZHQ; X-ray; 2.55 A; B/D=1-445.
DR PDB; 4ZI7; X-ray; 2.51 A; B/D=1-445.
DR PDB; 4ZOL; X-ray; 2.50 A; B/D=1-445.
DR PDB; 5BMV; X-ray; 2.50 A; B/D=1-445.
DR PDB; 5FNV; X-ray; 2.61 A; B/D=1-445.
DR PDB; 5JCB; X-ray; 2.30 A; B/D=1-445.
DR PDB; 5JQG; X-ray; 2.24 A; B/D=1-445.
DR PDB; 5KMG; EM; 3.50 A; B=1-431.
DR PDB; 5MM4; EM; 4.50 A; B=1-427.
DR PDB; 5MM7; EM; 5.10 A; B=1-427.
DR PDB; 5OAM; EM; 5.50 A; B=1-445.
DR PDB; 5OCU; EM; 5.20 A; B=1-445.
DR PDB; 5OGC; EM; 4.80 A; B=1-445.
DR PDB; 5SYC; EM; 3.50 A; B=1-426.
DR PDB; 5SYE; EM; 3.50 A; B=1-426.
DR PDB; 5SYF; EM; 3.50 A; B=1-426.
DR PDB; 5SYG; EM; 3.50 A; B=1-426.
DR PDB; 5XIW; X-ray; 2.90 A; B/D=1-445.
DR PDB; 5XKE; X-ray; 2.60 A; B/D=1-445.
DR PDB; 5XKF; X-ray; 2.80 A; B/D=1-445.
DR PDB; 5XKG; X-ray; 2.20 A; B/D=1-445.
DR PDB; 5XKH; X-ray; 2.25 A; B/D=1-445.
DR PDB; 5XP3; X-ray; 2.30 A; B/D=1-445.
DR PDB; 5XXT; EM; 5.35 A; B/D/F/H/J/L/N/P/R=2-427.
DR PDB; 5XXV; EM; 6.46 A; B/D/F/H/J/L/N/P/R=2-427.
DR PDB; 5XXW; EM; 6.00 A; B/D/F/H/J/L/N/P/R=2-427.
DR PDB; 5XXX; EM; 6.43 A; B/D/F/H/J/L/N/P/R=2-427.
DR PDB; 5YL2; X-ray; 2.09 A; B/D=1-445.
DR PDB; 5YLJ; X-ray; 2.70 A; B/D=1-445.
DR PDB; 5YLS; X-ray; 3.00 A; B/D=1-445.
DR PDB; 6B0C; EM; 3.51 A; B/D=1-445.
DR PDB; 6B0I; EM; 3.78 A; B=1-445.
DR PDB; 6B0L; EM; 3.98 A; B=1-445.
DR PDB; 6BJC; EM; 3.30 A; B/D/F/G/H/I=1-445.
DR PDB; 6BR1; X-ray; 2.30 A; B/D=1-445.
DR PDB; 6BRF; X-ray; 2.50 A; B/D=1-445.
DR PDB; 6BRY; X-ray; 2.70 A; B/D=1-445.
DR PDB; 6BS2; X-ray; 2.65 A; B/D=1-445.
DR PDB; 6CVJ; EM; 3.20 A; B/C=1-445.
DR PDB; 6CVN; EM; 3.90 A; A/C=1-445.
DR PDB; 6D88; X-ray; 2.85 A; B/D=1-445.
DR PDB; 6DPU; EM; 3.10 A; B/D/F/G/H/I=1-445.
DR PDB; 6DPV; EM; 3.30 A; B/D/F/G/H/I=1-445.
DR PDB; 6DPW; EM; 3.50 A; B/D/F/G/H/I=1-445.
DR PDB; 6EVW; EM; 4.40 A; B/D/F/G/H/I=1-429.
DR PDB; 6EVX; EM; 4.20 A; B/D/F/G/H/I=1-445.
DR PDB; 6EVY; EM; 4.40 A; B/D/F/G/H/I=1-445.
DR PDB; 6EVZ; EM; 3.80 A; B/D/F/G/H/I=1-445.
DR PDB; 6EW0; EM; 3.80 A; B/D/F/G/H/I=1-445.
DR PDB; 6KIO; EM; 3.94 A; b=2-427.
DR PDB; 6KIQ; EM; 3.62 A; b=2-427.
DR PDB; 6KPP; X-ray; 2.75 A; B/D=1-445.
DR PDB; 6LS4; X-ray; 2.40 A; B/D=1-445.
DR PDB; 6LSM; X-ray; 2.75 A; B/D=1-445.
DR PDB; 6LSN; X-ray; 2.44 A; B/D=1-445.
DR PDB; 6MLQ; EM; 4.20 A; B=1-445.
DR PDB; 6MLR; EM; 4.20 A; B=1-445.
DR PDB; 6MZE; X-ray; 3.60 A; B/D/I/K/P/R/W/Y=1-445.
DR PDB; 6MZF; X-ray; 4.40 A; B/D/I/K/P/R/W/Y=1-445.
DR PDB; 6MZG; X-ray; 3.21 A; B/D/H/J=1-445.
DR PDB; 6NNG; X-ray; 2.40 A; B/D=1-445.
DR PDB; 6O2Q; EM; 3.70 A; B/D/F/G/H/I=1-445.
DR PDB; 6O2R; EM; 3.30 A; B/D/F/G/H/I=1-445.
DR PDB; 6O2S; EM; 4.00 A; 1H/1O/1P/1Q/1R/1S/1T/1U/1V/1W/1X/1Y/1Z/2H/2O/2P/2Q/2R/2S/2T/2U/2V/2W/2X/2Y/2Z/3H/3O/3P/3Q=1-445.
DR PDB; 6O2T; EM; 4.10 A; 1H/1O/1P/1Q/1R/1S/1T/1U/1V/1W/1X/1Y/1Z/2H/2O/2P/2Q/2R/2S/2T/2U/2V/2W/2X/2Y/2Z/3H/3O/3P/3Q=1-445.
DR PDB; 6O5M; X-ray; 2.30 A; B/D=1-445.
DR PDB; 6O5N; X-ray; 3.00 A; B/D=1-445.
DR PDB; 6O61; X-ray; 2.60 A; B/D=1-445.
DR PDB; 6PC4; X-ray; 2.60 A; B/D=1-445.
DR PDB; 6RZA; EM; 5.40 A; B/D=1-426.
DR PDB; 6RZB; EM; 5.00 A; B=1-426.
DR PDB; 6TA3; EM; 3.80 A; B=1-429.
DR PDB; 6TA4; EM; 6.10 A; B=1-429.
DR PDB; 6TIW; EM; 1.09 A; B=1-429.
DR PDB; 6VPO; EM; 4.40 A; B=1-445.
DR PDB; 6VPP; EM; 4.40 A; B=1-445.
DR PDB; 6Y4M; X-ray; 3.34 A; B/D=1-445.
DR PDB; 6Y4N; X-ray; 2.85 A; B/D=1-445.
DR PDB; 6ZPI; EM; 4.50 A; B=1-431.
DR PDB; 7CBZ; X-ray; 2.61 A; B/D=1-445.
DR PDB; 7CE6; X-ray; 2.69 A; B/D=1-445.
DR PDB; 7CLD; X-ray; 2.61 A; B/D=1-445.
DR PDB; 7CNM; X-ray; 2.44 A; B/D=1-445.
DR PDB; 7CNN; X-ray; 2.50 A; B/D=1-445.
DR PDB; 7CNO; X-ray; 2.50 A; B/D=1-445.
DR PDB; 7DAD; X-ray; 2.85 A; B/D=1-445.
DR PDB; 7DAE; X-ray; 2.39 A; B/D=1-445.
DR PDB; 7DAF; X-ray; 2.40 A; B/D=1-445.
DR PDB; 7DMZ; EM; 4.30 A; C/E/F=1-445.
DR PDB; 7DN0; EM; 3.50 A; E/F=1-445.
DR PDB; 7DP8; X-ray; 2.45 A; B/D=1-445.
DR PDB; 7L05; X-ray; 2.21 A; B/D=1-445.
DR PDB; 7NB8; EM; 4.40 A; B=1-445.
DR PDB; 7NBA; EM; 4.00 A; B=1-445.
DR PDB; 7PQC; EM; 4.10 A; A/C/E/G/I/K/M=1-445.
DR PDB; 7PQP; EM; 4.10 A; A/C/E/G/I/K/M=1-445.
DR PDBsum; 1FFX; -.
DR PDBsum; 1IA0; -.
DR PDBsum; 1JFF; -.
DR PDBsum; 1TUB; -.
DR PDBsum; 2HXF; -.
DR PDBsum; 2HXH; -.
DR PDBsum; 3EDL; -.
DR PDBsum; 3J6E; -.
DR PDBsum; 3J6F; -.
DR PDBsum; 3J6G; -.
DR PDBsum; 3J6H; -.
DR PDBsum; 3J6P; -.
DR PDBsum; 3J7I; -.
DR PDBsum; 3JAK; -.
DR PDBsum; 3JAL; -.
DR PDBsum; 3JAR; -.
DR PDBsum; 3JAS; -.
DR PDBsum; 3JAT; -.
DR PDBsum; 3JAW; -.
DR PDBsum; 4ABO; -.
DR PDBsum; 4ZHQ; -.
DR PDBsum; 4ZI7; -.
DR PDBsum; 4ZOL; -.
DR PDBsum; 5BMV; -.
DR PDBsum; 5FNV; -.
DR PDBsum; 5JCB; -.
DR PDBsum; 5JQG; -.
DR PDBsum; 5KMG; -.
DR PDBsum; 5MM4; -.
DR PDBsum; 5MM7; -.
DR PDBsum; 5OAM; -.
DR PDBsum; 5OCU; -.
DR PDBsum; 5OGC; -.
DR PDBsum; 5SYC; -.
DR PDBsum; 5SYE; -.
DR PDBsum; 5SYF; -.
DR PDBsum; 5SYG; -.
DR PDBsum; 5XIW; -.
DR PDBsum; 5XKE; -.
DR PDBsum; 5XKF; -.
DR PDBsum; 5XKG; -.
DR PDBsum; 5XKH; -.
DR PDBsum; 5XP3; -.
DR PDBsum; 5XXT; -.
DR PDBsum; 5XXV; -.
DR PDBsum; 5XXW; -.
DR PDBsum; 5XXX; -.
DR PDBsum; 5YL2; -.
DR PDBsum; 5YLJ; -.
DR PDBsum; 5YLS; -.
DR PDBsum; 6B0C; -.
DR PDBsum; 6B0I; -.
DR PDBsum; 6B0L; -.
DR PDBsum; 6BJC; -.
DR PDBsum; 6BR1; -.
DR PDBsum; 6BRF; -.
DR PDBsum; 6BRY; -.
DR PDBsum; 6BS2; -.
DR PDBsum; 6CVJ; -.
DR PDBsum; 6CVN; -.
DR PDBsum; 6D88; -.
DR PDBsum; 6DPU; -.
DR PDBsum; 6DPV; -.
DR PDBsum; 6DPW; -.
DR PDBsum; 6EVW; -.
DR PDBsum; 6EVX; -.
DR PDBsum; 6EVY; -.
DR PDBsum; 6EVZ; -.
DR PDBsum; 6EW0; -.
DR PDBsum; 6KIO; -.
DR PDBsum; 6KIQ; -.
DR PDBsum; 6KPP; -.
DR PDBsum; 6LS4; -.
DR PDBsum; 6LSM; -.
DR PDBsum; 6LSN; -.
DR PDBsum; 6MLQ; -.
DR PDBsum; 6MLR; -.
DR PDBsum; 6MZE; -.
DR PDBsum; 6MZF; -.
DR PDBsum; 6MZG; -.
DR PDBsum; 6NNG; -.
DR PDBsum; 6O2Q; -.
DR PDBsum; 6O2R; -.
DR PDBsum; 6O2S; -.
DR PDBsum; 6O2T; -.
DR PDBsum; 6O5M; -.
DR PDBsum; 6O5N; -.
DR PDBsum; 6O61; -.
DR PDBsum; 6PC4; -.
DR PDBsum; 6RZA; -.
DR PDBsum; 6RZB; -.
DR PDBsum; 6TA3; -.
DR PDBsum; 6TA4; -.
DR PDBsum; 6TIW; -.
DR PDBsum; 6VPO; -.
DR PDBsum; 6VPP; -.
DR PDBsum; 6Y4M; -.
DR PDBsum; 6Y4N; -.
DR PDBsum; 6ZPI; -.
DR PDBsum; 7CBZ; -.
DR PDBsum; 7CE6; -.
DR PDBsum; 7CLD; -.
DR PDBsum; 7CNM; -.
DR PDBsum; 7CNN; -.
DR PDBsum; 7CNO; -.
DR PDBsum; 7DAD; -.
DR PDBsum; 7DAE; -.
DR PDBsum; 7DAF; -.
DR PDBsum; 7DMZ; -.
DR PDBsum; 7DN0; -.
DR PDBsum; 7DP8; -.
DR PDBsum; 7L05; -.
DR PDBsum; 7NB8; -.
DR PDBsum; 7NBA; -.
DR PDBsum; 7PQC; -.
DR PDBsum; 7PQP; -.
DR AlphaFoldDB; P02554; -.
DR SMR; P02554; -.
DR IntAct; P02554; 2.
DR BindingDB; P02554; -.
DR ChEMBL; CHEMBL2788; -.
DR DrugCentral; P02554; -.
DR PaxDb; P02554; -.
DR PeptideAtlas; P02554; -.
DR PRIDE; P02554; -.
DR ABCD; P02554; 1 sequenced antibody.
DR eggNOG; KOG1375; Eukaryota.
DR EvolutionaryTrace; P02554; -.
DR Proteomes; UP000008227; Unplaced.
DR Proteomes; UP000314985; Unplaced.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0005874; C:microtubule; IBA:GO_Central.
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:0000226; P:microtubule cytoskeleton organization; IBA:GO_Central.
DR GO; GO:0007017; P:microtubule-based process; IEA:InterPro.
DR GO; GO:0000278; P:mitotic cell cycle; IBA:GO_Central.
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; GTP-binding; Isopeptide bond; Methylation;
KW Microtubule; Nucleotide-binding; Phosphoprotein; Reference proteome;
KW Ubl conjugation.
FT CHAIN 1..445
FT /note="Tubulin beta chain"
FT /id="PRO_0000048261"
FT REGION 424..445
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 1..4
FT /note="MREI motif"
FT /evidence="ECO:0000250|UniProtKB:P07437"
FT COMPBIAS 431..445
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 58
FT /note="N6-acetyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:P07437"
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:0000250|UniProtKB:Q13885"
FT MOD_RES 285
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:P07437"
FT MOD_RES 290
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:P07437"
FT MOD_RES 318
FT /note="Omega-N-methylarginine"
FT /evidence="ECO:0000250|UniProtKB:P07437"
FT MOD_RES 438
FT /note="5-glutamyl polyglutamate"
FT /evidence="ECO:0000250|UniProtKB:Q2T9S0"
FT CROSSLNK 58
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in ubiquitin); alternate"
FT /evidence="ECO:0000250|UniProtKB:P07437"
FT CROSSLNK 324
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in ubiquitin)"
FT /evidence="ECO:0000250|UniProtKB:P07437"
FT VARIANT 37
FT /note="H -> V (in 2nd form)"
FT VARIANT 48
FT /note="N -> S (in 2nd form)"
FT VARIANT 55..57
FT /note="AGN -> SSH (in 2nd form)"
FT VARIANT 275
FT /note="S -> A (in 2nd form)"
FT STRAND 3..9
FT /evidence="ECO:0007829|PDB:5YL2"
FT HELIX 10..27
FT /evidence="ECO:0007829|PDB:5YL2"
FT STRAND 34..36
FT /evidence="ECO:0007829|PDB:5YL2"
FT HELIX 41..43
FT /evidence="ECO:0007829|PDB:5YL2"
FT TURN 44..46
FT /evidence="ECO:0007829|PDB:5YL2"
FT HELIX 47..49
FT /evidence="ECO:0007829|PDB:5YL2"
FT STRAND 51..53
FT /evidence="ECO:0007829|PDB:5YL2"
FT STRAND 57..61
FT /evidence="ECO:0007829|PDB:5YL2"
FT STRAND 63..70
FT /evidence="ECO:0007829|PDB:5YL2"
FT HELIX 71..77
FT /evidence="ECO:0007829|PDB:5YL2"
FT STRAND 79..81
FT /evidence="ECO:0007829|PDB:4ZOL"
FT HELIX 82..84
FT /evidence="ECO:0007829|PDB:5YL2"
FT HELIX 87..89
FT /evidence="ECO:0007829|PDB:5YL2"
FT STRAND 90..92
FT /evidence="ECO:0007829|PDB:5YL2"
FT HELIX 101..105
FT /evidence="ECO:0007829|PDB:5YL2"
FT HELIX 108..125
FT /evidence="ECO:0007829|PDB:5YL2"
FT STRAND 128..142
FT /evidence="ECO:0007829|PDB:5YL2"
FT HELIX 143..158
FT /evidence="ECO:0007829|PDB:5YL2"
FT STRAND 162..170
FT /evidence="ECO:0007829|PDB:5YL2"
FT HELIX 173..175
FT /evidence="ECO:0007829|PDB:5YL2"
FT STRAND 177..180
FT /evidence="ECO:0007829|PDB:3JAS"
FT HELIX 181..195
FT /evidence="ECO:0007829|PDB:5YL2"
FT STRAND 197..203
FT /evidence="ECO:0007829|PDB:5YL2"
FT HELIX 204..213
FT /evidence="ECO:0007829|PDB:5YL2"
FT HELIX 222..241
FT /evidence="ECO:0007829|PDB:5YL2"
FT STRAND 244..246
FT /evidence="ECO:0007829|PDB:5XKG"
FT HELIX 250..257
FT /evidence="ECO:0007829|PDB:5YL2"
FT STRAND 259..262
FT /evidence="ECO:0007829|PDB:7CBZ"
FT STRAND 265..272
FT /evidence="ECO:0007829|PDB:5YL2"
FT STRAND 276..278
FT /evidence="ECO:0007829|PDB:5XKH"
FT STRAND 280..282
FT /evidence="ECO:0007829|PDB:3JAS"
FT HELIX 286..294
FT /evidence="ECO:0007829|PDB:5YL2"
FT HELIX 296..298
FT /evidence="ECO:0007829|PDB:5YL2"
FT STRAND 299..302
FT /evidence="ECO:0007829|PDB:5YL2"
FT HELIX 305..307
FT /evidence="ECO:0007829|PDB:5YL2"
FT STRAND 310..320
FT /evidence="ECO:0007829|PDB:5YL2"
FT HELIX 323..336
FT /evidence="ECO:0007829|PDB:5YL2"
FT HELIX 338..340
FT /evidence="ECO:0007829|PDB:5YL2"
FT STRAND 343..345
FT /evidence="ECO:0007829|PDB:6D88"
FT STRAND 349..356
FT /evidence="ECO:0007829|PDB:5YL2"
FT STRAND 362..371
FT /evidence="ECO:0007829|PDB:5YL2"
FT HELIX 372..374
FT /evidence="ECO:0007829|PDB:5YL2"
FT HELIX 375..389
FT /evidence="ECO:0007829|PDB:5YL2"
FT TURN 390..395
FT /evidence="ECO:0007829|PDB:5YL2"
FT HELIX 396..399
FT /evidence="ECO:0007829|PDB:5YL2"
FT TURN 400..402
FT /evidence="ECO:0007829|PDB:5YL2"
FT HELIX 405..427
FT /evidence="ECO:0007829|PDB:5YL2"
SQ SEQUENCE 445 AA; 49861 MW; EF71423B12C5E1B2 CRC64;
MREIVHIQAG QCGNQIGAKF WEVISDEHGI DPTGSYHGDS DLQLERINVY YNEAAGNKYV
PRAILVDLEP GTMDSVRSGP FGQIFRPDNF VFGQSGAGNN WAKGHYTEGA ELVDSVLDVV
RKESESCDCL QGFQLTHSLG GGTGSGMGTL LISKIREEYP DRIMNTFSVV PSPKVSDTVV
EPYNATLSVH QLVENTDETY CIDNEALYDI CFRTLKLTTP TYGDLNHLVS ATMSGVTTCL
RFPGQLNADL RKLAVNMVPF PRLHFFMPGF APLTSRGSQQ YRALTVPELT QQMFDAKNMM
AACDPRHGRY LTVAAVFRGR MSMKEVDEQM LNVQNKNSSY FVEWIPNNVK TAVCDIPPRG
LKMSATFIGN STAIQELFKR ISEQFTAMFR RKAFLHWYTG EGMDEMEFTE AESNMNDLVS
EYQQYQDATA DEQGEFEEEG EEDEA
