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 27-MAR-2024, entry version 180. 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 FUNCTION, SUBCELLULAR LOCATION, AND SUBUNIT. RX PubMed=7225365; DOI=10.1021/bi00510a030; RA Carlier M.F., Pantaloni D.; RT "Kinetic analysis of guanosine 5'-triphosphate hydrolysis associated with RT tubulin polymerization."; RL Biochemistry 20:1918-1924(1981). RN [6] 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 [7] 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 [8] 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 [9] 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). RN [10] {ECO:0007744|PDB:5HNW, ECO:0007744|PDB:5HNX, ECO:0007744|PDB:5HNY, ECO:0007744|PDB:5HNZ} RP STRUCTURE BY ELECTRON MICROSCOPY (5.80 ANGSTROMS) IN COMPLEX WITH ADP AND RP CHIMERIC CONSTRUCT OF DROSOPHILA NCD AND RAT KIF5C. RX PubMed=27452403; DOI=10.1016/j.str.2016.05.021; RA Yamagishi M., Shigematsu H., Yokoyama T., Kikkawa M., Sugawa M., Aoki M., RA Shirouzu M., Yajima J., Nitta R.; RT "Structural Basis of Backwards Motion in Kinesin-1-Kinesin-14 Chimera: RT Implication for Kinesin-14 Motility."; RL Structure 24:1322-1334(2016). CC -!- FUNCTION: Tubulin is the major constituent of microtubules, a cylinder CC consisting of laterally associated linear protofilaments composed of CC alpha- and beta-tubulin heterodimers (PubMed:7225365). Microtubules CC grow by the addition of GTP-tubulin dimers to the microtubule end, CC where a stabilizing cap forms (PubMed:7225365). Below the cap, tubulin CC dimers are in GDP-bound state, owing to GTPase activity of alpha- CC tubulin (PubMed:7225365). {ECO:0000269|PubMed:7225365}. CC -!- COFACTOR: CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420; CC Evidence={ECO:0000250|UniProtKB:P68363}; CC -!- SUBUNIT: Dimer of alpha and beta chains (PubMed:7225365). A typical CC microtubule is a hollow water-filled tube with an outer diameter of 25 CC nm and an inner diameter of 15 nM. Alpha-beta heterodimers associate CC head-to-tail to form protofilaments running lengthwise along the CC microtubule wall with the beta-tubulin subunit facing the microtubule CC plus end conferring a structural polarity. Microtubules usually have 13 CC protofilaments but different protofilament numbers can be found in some CC organisms and specialized cells. Interacts with NCKAP5L CC (PubMed:26482847). {ECO:0000269|PubMed:26482847, CC ECO:0000269|PubMed:7225365}. CC -!- SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton CC {ECO:0000269|PubMed:7225365}. 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}. 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 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; 5HNW; EM; 6.60 A; B=2-445. DR PDB; 5HNX; EM; 6.60 A; B=1-445. DR PDB; 5HNY; EM; 6.30 A; B=2-427. DR PDB; 5HNZ; EM; 5.80 A; B=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; 6X1C; X-ray; 2.90 A; B/D=1-445. DR PDB; 6X1E; X-ray; 2.90 A; B/D=1-445. DR PDB; 6X1F; X-ray; 2.70 A; B/D=1-445. DR PDB; 6XER; X-ray; 2.50 A; B/D=1-433. DR PDB; 6XES; X-ray; 2.32 A; B/D=1-433. DR PDB; 6XET; X-ray; 2.60 A; B/D=1-433. 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; 7CDA; X-ray; 2.66 A; B/D=1-445. DR PDB; 7CE6; X-ray; 2.69 A; B/D=1-445. DR PDB; 7CE8; X-ray; 2.73 A; B/D=1-445. DR PDB; 7CEK; X-ray; 2.70 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; 7DB9; X-ray; 2.85 A; B/D=1-445. DR PDB; 7DBA; X-ray; 2.46 A; B/D=1-445. DR PDB; 7DBB; X-ray; 2.81 A; B/D=1-445. DR PDB; 7DBC; X-ray; 2.40 A; B/D=1-445. DR PDB; 7DBD; X-ray; 3.09 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; 7EMJ; X-ray; 2.33 A; B/D=1-445. DR PDB; 7EXC; X-ray; 2.39 A; B/D=1-445. DR PDB; 7L05; X-ray; 2.21 A; B/D=1-445. DR PDB; 7LZ7; X-ray; 2.80 A; B/D=1-445. DR PDB; 7LZ8; X-ray; 2.92 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 PDB; 7RS5; EM; 3.90 A; B/D/F/H/J/M/O/Q/S=1-445. DR PDB; 7RS6; EM; 4.10 A; B/D/F/H/J/M/O/Q/S=1-445. DR PDB; 7RX0; EM; 3.89 A; B=1-445. DR PDB; 7SGS; EM; 3.30 A; C=1-445. DR PDB; 7TQX; EM; 2.80 A; B=1-445. DR PDB; 7TQY; EM; 2.60 A; B=1-445. DR PDB; 7TQZ; EM; 2.70 A; B=1-445. DR PDB; 7TR0; EM; 2.70 A; B=1-445. DR PDB; 7TR1; EM; 3.10 A; B=1-445. DR PDB; 7TR2; EM; 3.00 A; B=1-445. DR PDB; 7TR3; EM; 3.90 A; B=1-445. DR PDB; 7U0F; EM; 3.53 A; B/D=1-445. DR PDB; 7X4N; X-ray; 2.88 A; B=1-445. DR PDB; 7YHN; X-ray; 2.60 A; B/D=1-445. DR PDB; 7YSN; EM; 3.50 A; B=1-445. DR PDB; 7YSO; EM; 3.60 A; B=1-445. DR PDB; 7YSP; EM; 3.90 A; B=1-445. DR PDB; 7Z2A; EM; 4.30 A; H=1-426. DR PDB; 7Z2B; EM; 3.30 A; H=1-426. DR PDB; 7Z2C; EM; 4.10 A; H=1-426. DR PDB; 8DIQ; X-ray; 2.40 A; B/D=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; 5HNW; -. DR PDBsum; 5HNX; -. DR PDBsum; 5HNY; -. DR PDBsum; 5HNZ; -. 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; 6X1C; -. DR PDBsum; 6X1E; -. DR PDBsum; 6X1F; -. DR PDBsum; 6XER; -. DR PDBsum; 6XES; -. DR PDBsum; 6XET; -. DR PDBsum; 6Y4M; -. DR PDBsum; 6Y4N; -. DR PDBsum; 6ZPI; -. DR PDBsum; 7CBZ; -. DR PDBsum; 7CDA; -. DR PDBsum; 7CE6; -. DR PDBsum; 7CE8; -. DR PDBsum; 7CEK; -. DR PDBsum; 7CLD; -. DR PDBsum; 7CNM; -. DR PDBsum; 7CNN; -. DR PDBsum; 7CNO; -. DR PDBsum; 7DAD; -. DR PDBsum; 7DAE; -. DR PDBsum; 7DAF; -. DR PDBsum; 7DB9; -. DR PDBsum; 7DBA; -. DR PDBsum; 7DBB; -. DR PDBsum; 7DBC; -. DR PDBsum; 7DBD; -. DR PDBsum; 7DMZ; -. DR PDBsum; 7DN0; -. DR PDBsum; 7DP8; -. DR PDBsum; 7EMJ; -. DR PDBsum; 7EXC; -. DR PDBsum; 7L05; -. DR PDBsum; 7LZ7; -. DR PDBsum; 7LZ8; -. DR PDBsum; 7NB8; -. DR PDBsum; 7NBA; -. DR PDBsum; 7PQC; -. DR PDBsum; 7PQP; -. DR PDBsum; 7RS5; -. DR PDBsum; 7RS6; -. DR PDBsum; 7RX0; -. DR PDBsum; 7SGS; -. DR PDBsum; 7TQX; -. DR PDBsum; 7TQY; -. DR PDBsum; 7TQZ; -. DR PDBsum; 7TR0; -. DR PDBsum; 7TR1; -. DR PDBsum; 7TR2; -. DR PDBsum; 7TR3; -. DR PDBsum; 7U0F; -. DR PDBsum; 7X4N; -. DR PDBsum; 7YHN; -. DR PDBsum; 7YSN; -. DR PDBsum; 7YSO; -. DR PDBsum; 7YSP; -. DR PDBsum; 7Z2A; -. DR PDBsum; 7Z2B; -. DR PDBsum; 7Z2C; -. DR PDBsum; 8DIQ; -. DR AlphaFoldDB; P02554; -. DR EMDB; EMD-0612; -. DR EMDB; EMD-0613; -. DR EMDB; EMD-0614; -. DR EMDB; EMD-0615; -. DR EMDB; EMD-10060; -. DR EMDB; EMD-10061; -. DR EMDB; EMD-10421; -. DR EMDB; EMD-10422; -. DR EMDB; EMD-11340; -. DR EMDB; EMD-12257; -. DR EMDB; EMD-12258; -. DR EMDB; EMD-14459; -. DR EMDB; EMD-14460; -. DR EMDB; EMD-14461; -. DR EMDB; EMD-2005; -. DR EMDB; EMD-21314; -. DR EMDB; EMD-21315; -. DR EMDB; EMD-24666; -. DR EMDB; EMD-24667; -. DR EMDB; EMD-24721; -. DR EMDB; EMD-25120; -. DR EMDB; EMD-26257; -. DR EMDB; EMD-2697; -. DR EMDB; EMD-2912; -. DR EMDB; EMD-2915; -. DR EMDB; EMD-2916; -. DR EMDB; EMD-2918; -. DR EMDB; EMD-2919; -. DR EMDB; EMD-2920; -. DR EMDB; EMD-30775; -. DR EMDB; EMD-30776; -. DR EMDB; EMD-34077; -. DR EMDB; EMD-34078; -. DR EMDB; EMD-34079; -. DR EMDB; EMD-3529; -. DR EMDB; EMD-3530; -. DR EMDB; EMD-3778; -. DR EMDB; EMD-3780; -. DR EMDB; EMD-3803; -. DR EMDB; EMD-3961; -. DR EMDB; EMD-3962; -. DR EMDB; EMD-3963; -. DR EMDB; EMD-3964; -. DR EMDB; EMD-3965; -. DR EMDB; EMD-41169; -. DR EMDB; EMD-5027; -. DR EMDB; EMD-5895; -. DR EMDB; EMD-5896; -. DR EMDB; EMD-5897; -. DR EMDB; EMD-5916; -. DR EMDB; EMD-6347; -. DR EMDB; EMD-6348; -. DR EMDB; EMD-6349; -. DR EMDB; EMD-6350; -. DR EMDB; EMD-6351; -. DR EMDB; EMD-6352; -. DR EMDB; EMD-6353; -. DR EMDB; EMD-6354; -. DR EMDB; EMD-6355; -. DR EMDB; EMD-6779; -. DR EMDB; EMD-6781; -. DR EMDB; EMD-6782; -. DR EMDB; EMD-6783; -. DR EMDB; EMD-7026; -. DR EMDB; EMD-7027; -. DR EMDB; EMD-7028; -. DR EMDB; EMD-7101; -. DR EMDB; EMD-7769; -. DR EMDB; EMD-7771; -. DR EMDB; EMD-7973; -. DR EMDB; EMD-7974; -. DR EMDB; EMD-7975; -. DR EMDB; EMD-8059; -. DR EMDB; EMD-8060; -. DR EMDB; EMD-8061; -. DR EMDB; EMD-8266; -. DR EMDB; EMD-8320; -. DR EMDB; EMD-8321; -. DR EMDB; EMD-8322; -. DR EMDB; EMD-8323; -. DR EMDB; EMD-9140; -. DR EMDB; EMD-9141; -. DR EMDB; EMD-9996; -. DR EMDB; EMD-9997; -. DR SMR; P02554; -. DR IntAct; P02554; 2. DR STRING; 9823.ENSSSCP00000049151; -. DR BindingDB; P02554; -. DR ChEMBL; CHEMBL2788; -. DR DrugCentral; P02554; -. DR PaxDb; 9823-ENSSSCP00000001076; -. DR PeptideAtlas; P02554; -. DR ABCD; P02554; 1 sequenced antibody. DR eggNOG; KOG1375; Eukaryota. DR InParanoid; P02554; -. DR EvolutionaryTrace; P02554; -. DR Proteomes; UP000008227; Unplaced. DR Proteomes; UP000314985; Unplaced. DR Proteomes; UP000694570; Unplaced. DR Proteomes; UP000694571; Unplaced. DR Proteomes; UP000694720; Unplaced. DR Proteomes; UP000694722; Unplaced. DR Proteomes; UP000694723; Unplaced. DR Proteomes; UP000694724; Unplaced. DR Proteomes; UP000694725; Unplaced. DR Proteomes; UP000694726; Unplaced. DR Proteomes; UP000694727; Unplaced. DR Proteomes; UP000694728; 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:0003924; F:GTPase activity; IEA:InterPro. DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW. 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:0000278; P:mitotic cell cycle; IBA:GO_Central. DR CDD; cd02187; beta_tubulin; 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; 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; TUBULIN; 1. DR PANTHER; PTHR11588:SF247; TUBULIN BETA-4B CHAIN; 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; SSF55307; Tubulin C-terminal domain-like; 1. DR SUPFAM; SSF52490; Tubulin nucleotide-binding domain-like; 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; Magnesium; KW Metal-binding; Methylation; Microtubule; Nucleotide-binding; KW Phosphoprotein; Reference proteome; 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 11 FT /ligand="GTP" FT /ligand_id="ChEBI:CHEBI:37565" FT /evidence="ECO:0000250|UniProtKB:Q13509" FT BINDING 69 FT /ligand="GTP" FT /ligand_id="ChEBI:CHEBI:37565" FT /evidence="ECO:0000250|UniProtKB:P68363" FT BINDING 69 FT /ligand="Mg(2+)" FT /ligand_id="ChEBI:CHEBI:18420" FT /evidence="ECO:0000250|UniProtKB:P68363" FT BINDING 138 FT /ligand="GTP" FT /ligand_id="ChEBI:CHEBI:37565" FT /evidence="ECO:0000250|UniProtKB:Q13509" FT BINDING 142 FT /ligand="GTP" FT /ligand_id="ChEBI:CHEBI:37565" FT /evidence="ECO:0000250|UniProtKB:Q13509" FT BINDING 143 FT /ligand="GTP" FT /ligand_id="ChEBI:CHEBI:37565" FT /evidence="ECO:0000250|UniProtKB:Q13509" FT BINDING 144 FT /ligand="GTP" FT /ligand_id="ChEBI:CHEBI:37565" FT /evidence="ECO:0000250|UniProtKB:Q13509" FT BINDING 204 FT /ligand="GTP" FT /ligand_id="ChEBI:CHEBI:37565" FT /evidence="ECO:0000250|UniProtKB:Q13509" FT BINDING 226 FT /ligand="GTP" FT /ligand_id="ChEBI:CHEBI:37565" FT /evidence="ECO:0000250|UniProtKB:Q13509" 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 HELIX 279..281 FT /evidence="ECO:0007829|PDB:7SGS" 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:7CEK" 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 //