ID TBB2B_BOVIN Reviewed; 445 AA. AC Q6B856; DT 28-NOV-2006, integrated into UniProtKB/Swiss-Prot. DT 28-NOV-2006, sequence version 2. DT 27-MAR-2024, entry version 163. DE RecName: Full=Tubulin beta-2B chain; GN Name=TUBB2B; OS Bos taurus (Bovine). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia; OC Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae; OC Bovinae; Bos. OX NCBI_TaxID=9913; RN [1] RP NUCLEOTIDE SEQUENCE [MRNA]. RA Hwang K.C., Park S.Y., Cui X.S., Kim N.H.; RT "Differentially expressed genes in bovine 8-cell embryo."; RL Submitted (JUL-2004) to the EMBL/GenBank/DDBJ databases. RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=Hereford; RX PubMed=19390049; DOI=10.1126/science.1169588; RG The bovine genome sequencing and analysis consortium; RT "The genome sequence of taurine cattle: a window to ruminant biology and RT evolution."; RL Science 324:522-528(2009). RN [3] RP FUNCTION, SUBUNIT, AND SUBCELLULAR LOCATION. RX PubMed=6504138; DOI=10.1038/312237a0; RA Mitchison T., Kirschner M.; RT "Dynamic instability of microtubule growth."; RL Nature 312:237-242(1984). RN [4] RP FUNCTION, SUBUNIT, AND SUBCELLULAR LOCATION. RX PubMed=2207090; DOI=10.1021/bi00479a022; RA Stewart R.J., Farrell K.W., Wilson L.; RT "Role of GTP hydrolysis in microtubule polymerization: evidence for a RT coupled hydrolysis mechanism."; RL Biochemistry 29:6489-6498(1990). RN [5] RP FUNCTION, SUBUNIT, AND SUBCELLULAR LOCATION. RX PubMed=7704569; DOI=10.1016/s0960-9822(00)00243-8; RA Drechsel D.N., Kirschner M.W.; RT "The minimum GTP cap required to stabilize microtubules."; RL Curr. Biol. 4:1053-1061(1994). 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:6504138, PubMed:2207090, CC PubMed:7704569). Microtubules grow by the addition of GTP-tubulin CC dimers to the microtubule end, where a stabilizing cap forms. Below the CC cap, tubulin dimers are in GDP-bound state, owing to GTPase activity of CC alpha-tubulin (PubMed:6504138, PubMed:2207090, PubMed:7704569). CC Implicated in neuronal migration (By similarity). CC {ECO:0000250|UniProtKB:Q9BVA1, ECO:0000269|PubMed:2207090, CC ECO:0000269|PubMed:6504138, ECO:0000269|PubMed:7704569}. 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:6504138, CC PubMed:2207090, PubMed:7704569). A typical microtubule is a hollow CC water-filled tube with an outer diameter of 25 nm and an inner diameter CC of 15 nM. Alpha-beta heterodimers associate head-to-tail to form CC protofilaments running lengthwise along the microtubule wall with the CC 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. {ECO:0000269|PubMed:2207090, CC ECO:0000269|PubMed:6504138, ECO:0000269|PubMed:7704569}. CC -!- SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton CC {ECO:0000269|PubMed:2207090, ECO:0000269|PubMed:6504138, CC ECO:0000269|PubMed:7704569}. 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. The precise function of polyglycylation is still unclear. CC {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:Q9BVA1}. 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; AY675081; AAT84374.1; -; mRNA. DR RefSeq; NP_001003900.1; NM_001003900.1. DR PDB; 1SA0; X-ray; 3.58 A; B/D=1-439. DR PDB; 1SA1; X-ray; 4.20 A; B/D=1-439. DR PDB; 1TVK; X-ray; 2.89 A; B=1-427. DR PDB; 1Z2B; X-ray; 4.10 A; B/D=1-445. DR PDB; 2P4N; EM; 9.00 A; B=1-445. DR PDB; 2WBE; EM; 9.40 A; B=1-445. DR PDB; 2XRP; EM; 8.20 A; A/C/E/G=1-445. DR PDB; 3DCO; EM; 1.90 A; B=1-445. DR PDB; 3DU7; X-ray; 4.10 A; B/D=1-445. DR PDB; 3E22; X-ray; 3.80 A; B/D=1-445. DR PDB; 3IZ0; EM; 8.60 A; B=1-445. DR PDB; 3J1T; EM; 9.70 A; C=1-427. DR PDB; 3J1U; EM; 9.70 A; C=1-427. DR PDB; 3J2U; EM; 10.80 A; B/D=1-445. DR PDB; 4AQV; EM; 9.70 A; B=1-445. DR PDB; 4AQW; EM; 9.50 A; B=1-445. DR PDB; 4ATU; EM; 8.30 A; A/C/E/G=1-445. DR PDB; 4ATX; EM; 8.20 A; A=1-445. DR PDB; 4CK5; EM; 10.00 A; B=1-445. DR PDB; 4CK6; EM; 9.20 A; B=1-445. DR PDB; 4CK7; EM; 9.20 A; B=1-445. DR PDB; 4I4T; X-ray; 1.80 A; B/D=1-445. DR PDB; 4I50; X-ray; 2.30 A; B/D=1-445. DR PDB; 4I55; X-ray; 2.20 A; B/D=1-445. DR PDB; 4IHJ; X-ray; 2.00 A; B/D=1-445. DR PDB; 4IIJ; X-ray; 2.60 A; B/D=1-445. DR PDB; 4O2A; X-ray; 2.50 A; B/D=1-445. DR PDB; 4O2B; X-ray; 2.30 A; B/D=1-445. DR PDB; 4O4H; X-ray; 2.10 A; B/D=1-445. DR PDB; 4O4I; X-ray; 2.40 A; B/D=1-445. DR PDB; 4O4J; X-ray; 2.20 A; B/D=1-445. DR PDB; 4O4L; X-ray; 2.20 A; B/D=1-445. DR PDB; 4TUY; X-ray; 2.10 A; B/D=1-445. DR PDB; 4TV8; X-ray; 2.10 A; B/D=1-445. DR PDB; 4TV9; X-ray; 2.00 A; B/D=1-445. DR PDB; 4UXO; EM; 6.30 A; B=1-445. DR PDB; 4UXP; EM; 6.30 A; B=1-445. DR PDB; 4UXR; EM; 7.00 A; B=1-445. DR PDB; 4UXS; EM; 7.00 A; B=1-445. DR PDB; 4UXT; EM; 7.40 A; B=1-445. DR PDB; 4UXY; EM; 6.50 A; B=1-445. DR PDB; 4UY0; EM; 7.70 A; B=2-427. DR PDB; 4YJ2; X-ray; 2.60 A; B/D=1-445. DR PDB; 4YJ3; X-ray; 3.75 A; B/D=1-445. DR PDB; 5EIB; X-ray; 2.10 A; D=1-445. DR PDB; 5EZY; X-ray; 2.05 A; B/D=1-445. DR PDB; 5GON; X-ray; 2.48 A; B/D=1-431. DR PDB; 5H74; X-ray; 2.60 A; B/D=1-445. DR PDB; 5H7O; X-ray; 2.80 A; B/D=1-445. DR PDB; 5ITZ; X-ray; 2.20 A; B=1-445. DR PDB; 5IYZ; X-ray; 1.80 A; B/D=1-445. DR PDB; 5J2T; X-ray; 2.20 A; B/D=1-445. DR PDB; 5J2U; X-ray; 2.50 A; B/D=1-445. DR PDB; 5JH7; X-ray; 2.25 A; B/D=1-445. DR PDB; 5JVD; X-ray; 2.39 A; B/D=1-445. DR PDB; 5LA6; X-ray; 2.10 A; B/D=1-445. DR PDB; 5LOV; X-ray; 2.40 A; B/D=1-445. DR PDB; 5LP6; X-ray; 2.90 A; B/D=1-445. DR PDB; 5LXS; X-ray; 2.20 A; B/D=1-445. DR PDB; 5LXT; X-ray; 1.90 A; B/D=1-445. DR PDB; 5LYJ; X-ray; 2.40 A; B/D=1-445. DR PDB; 5M50; EM; 5.30 A; B/E=1-427. DR PDB; 5M54; EM; 8.00 A; B/E=2-427. DR PDB; 5M5C; EM; 4.80 A; B/E=2-427. DR PDB; 5M5I; EM; 9.30 A; B=1-445. DR PDB; 5M5L; EM; 9.30 A; B=1-445. DR PDB; 5M5M; EM; 9.30 A; B=1-445. DR PDB; 5M5N; EM; 9.30 A; B=1-445. DR PDB; 5M5O; EM; 9.30 A; B=1-445. DR PDB; 5M7E; X-ray; 2.05 A; B/D=1-445. DR PDB; 5M7G; X-ray; 2.25 A; B/D=1-445. DR PDB; 5M8D; X-ray; 2.25 A; B/D=1-445. DR PDB; 5M8G; X-ray; 2.15 A; B/D=1-445. DR PDB; 5MF4; X-ray; 2.30 A; B/D=1-445. DR PDB; 5ND2; EM; 5.80 A; B=1-445. DR PDB; 5ND3; EM; 6.10 A; B=1-445. DR PDB; 5ND4; EM; 4.40 A; B=2-427. DR PDB; 5ND7; EM; 7.90 A; B=1-445. DR PDB; 5NFZ; X-ray; 2.10 A; B/D=1-445. DR PDB; 5NG1; X-ray; 2.20 A; B/D=1-445. DR PDB; 5NJH; X-ray; 2.39 A; B/D=1-445. DR PDB; 5NM5; X-ray; 2.05 A; B=1-445. DR PDB; 5NQT; X-ray; 2.15 A; B=1-445. DR PDB; 5NQU; X-ray; 1.80 A; B=1-445. DR PDB; 5O7A; X-ray; 2.50 A; B/D=1-445. DR PDB; 5OSK; X-ray; 2.11 A; B/D=1-445. DR PDB; 5OV7; X-ray; 2.40 A; B/D=1-445. DR PDB; 5S4L; X-ray; 2.30 A; B/D=1-445. DR PDB; 5S4M; X-ray; 2.15 A; B/D=1-445. DR PDB; 5S4N; X-ray; 2.53 A; B/D=1-445. DR PDB; 5S4O; X-ray; 2.30 A; B/D=1-445. DR PDB; 5S4P; X-ray; 2.29 A; B/D=1-445. DR PDB; 5S4Q; X-ray; 2.59 A; B/D=1-445. DR PDB; 5S4R; X-ray; 2.35 A; B/D=1-445. DR PDB; 5S4S; X-ray; 2.35 A; B/D=1-445. DR PDB; 5S4T; X-ray; 2.27 A; B/D=1-445. DR PDB; 5S4U; X-ray; 2.39 A; B/D=1-445. DR PDB; 5S4V; X-ray; 2.30 A; B/D=1-445. DR PDB; 5S4W; X-ray; 2.80 A; B/D=1-445. DR PDB; 5S4X; X-ray; 2.53 A; B/D=1-445. DR PDB; 5S4Y; X-ray; 2.30 A; B/D=1-445. DR PDB; 5S4Z; X-ray; 2.10 A; B/D=1-445. DR PDB; 5S50; X-ray; 3.10 A; B/D=1-445. DR PDB; 5S51; X-ray; 2.40 A; B/D=1-445. DR PDB; 5S52; X-ray; 2.83 A; B/D=1-445. DR PDB; 5S53; X-ray; 2.75 A; B/D=1-445. DR PDB; 5S54; X-ray; 2.40 A; B/D=1-445. DR PDB; 5S55; X-ray; 2.30 A; B/D=1-445. DR PDB; 5S56; X-ray; 2.25 A; B/D=1-445. DR PDB; 5S57; X-ray; 2.45 A; B/D=1-445. DR PDB; 5S58; X-ray; 2.30 A; B/D=1-445. DR PDB; 5S59; X-ray; 2.60 A; B/D=1-445. DR PDB; 5S5A; X-ray; 2.35 A; B/D=1-445. DR PDB; 5S5B; X-ray; 2.30 A; B/D=1-445. DR PDB; 5S5C; X-ray; 2.40 A; B/D=1-445. DR PDB; 5S5D; X-ray; 1.90 A; B/D=1-445. DR PDB; 5S5E; X-ray; 2.67 A; B/D=1-445. DR PDB; 5S5F; X-ray; 2.24 A; B/D=1-445. DR PDB; 5S5G; X-ray; 2.69 A; B/D=1-445. DR PDB; 5S5H; X-ray; 2.50 A; B/D=1-445. DR PDB; 5S5I; X-ray; 2.49 A; B/D=1-445. DR PDB; 5S5J; X-ray; 2.25 A; B/D=1-445. DR PDB; 5S5K; X-ray; 2.41 A; B/D=1-445. DR PDB; 5S5L; X-ray; 2.25 A; B/D=1-445. DR PDB; 5S5M; X-ray; 2.70 A; B/D=1-445. DR PDB; 5S5N; X-ray; 2.90 A; B/D=1-445. DR PDB; 5S5O; X-ray; 2.30 A; B/D=1-445. DR PDB; 5S5P; X-ray; 2.79 A; B/D=1-445. DR PDB; 5S5Q; X-ray; 2.05 A; B/D=1-445. DR PDB; 5S5R; X-ray; 2.30 A; B/D=1-445. DR PDB; 5S5S; X-ray; 2.36 A; B/D=1-445. DR PDB; 5S5T; X-ray; 2.53 A; B/D=1-445. DR PDB; 5S5U; X-ray; 2.50 A; B/D=1-445. DR PDB; 5S5V; X-ray; 2.70 A; B/D=1-445. DR PDB; 5S5W; X-ray; 2.35 A; B/D=1-445. DR PDB; 5S5X; X-ray; 2.32 A; B/D=1-445. DR PDB; 5S5Y; X-ray; 2.26 A; B/D=1-445. DR PDB; 5S5Z; X-ray; 2.55 A; B/D=1-445. DR PDB; 5S60; X-ray; 2.30 A; B/D=1-445. DR PDB; 5S61; X-ray; 1.95 A; B/D=1-445. DR PDB; 5S62; X-ray; 2.75 A; B/D=1-445. DR PDB; 5S63; X-ray; 2.60 A; B/D=1-445. DR PDB; 5S64; X-ray; 2.75 A; B/D=1-445. DR PDB; 5S65; X-ray; 2.25 A; B/D=1-445. DR PDB; 5S66; X-ray; 2.10 A; B/D=1-445. DR PDB; 5S67; X-ray; 2.10 A; B/D=1-445. DR PDB; 5SB3; X-ray; 2.20 A; B/D=1-445. DR PDB; 5SB4; X-ray; 2.50 A; B/D=1-445. DR PDB; 5SB5; X-ray; 2.31 A; B/D=1-445. DR PDB; 5SB6; X-ray; 2.30 A; B/D=1-445. DR PDB; 5SB7; X-ray; 2.10 A; B/D=1-445. DR PDB; 5SB8; X-ray; 2.30 A; B/D=1-445. DR PDB; 5SB9; X-ray; 2.50 A; B/D=1-445. DR PDB; 5SBA; X-ray; 2.25 A; B/D=1-445. DR PDB; 5SBB; X-ray; 2.25 A; B/D=1-445. DR PDB; 5SBC; X-ray; 2.32 A; B/D=1-445. DR PDB; 5SBD; X-ray; 2.25 A; B/D=1-445. DR PDB; 5SBE; X-ray; 2.75 A; B/D=1-445. DR PDB; 5XAF; X-ray; 2.55 A; B/D=1-445. DR PDB; 5XAG; X-ray; 2.56 A; B/D=1-445. DR PDB; 5XLT; X-ray; 2.81 A; B/D=1-445. DR PDB; 5XLZ; X-ray; 2.30 A; B/D=1-445. DR PDB; 5YZ3; X-ray; 2.54 A; B/D=1-445. DR PDB; 5Z4P; X-ray; 2.50 A; B=1-428, D=1-431. DR PDB; 5Z4U; X-ray; 3.18 A; B/D=1-445. DR PDB; 5ZXH; X-ray; 2.80 A; B/D=1-445. DR PDB; 6AGK; X-ray; 2.80 A; B/D=1-445. DR PDB; 6BBN; X-ray; 3.51 A; B/D=1-445. DR PDB; 6EG5; X-ray; 2.45 A; B/D=1-445. DR PDB; 6F7C; X-ray; 2.00 A; B/D=1-445. DR PDB; 6FII; X-ray; 2.40 A; B/D=1-445. DR PDB; 6FJF; X-ray; 2.40 A; B/D=1-445. DR PDB; 6FJM; X-ray; 2.10 A; B/D=1-445. DR PDB; 6FKJ; X-ray; 2.15 A; B/D=1-445. DR PDB; 6FKL; X-ray; 2.10 A; B/D=1-445. DR PDB; 6GF3; X-ray; 2.40 A; B/D=1-445. DR PDB; 6GJ4; X-ray; 2.40 A; B/D=1-445. DR PDB; 6GZE; X-ray; 2.49 A; B/D=1-445. DR PDB; 6HX8; X-ray; 2.40 A; B/D=1-445. DR PDB; 6I5C; X-ray; 2.95 A; B/D=1-445. DR PDB; 6JCJ; X-ray; 2.50 A; B/D=1-445. DR PDB; 6K9V; X-ray; 2.54 A; B/D=1-445. DR PDB; 6KNZ; X-ray; 2.48 A; B/D=1-445. DR PDB; 6N47; X-ray; 2.60 A; B/D=1-445. DR PDB; 6OJQ; EM; 3.67 A; B=1-426. DR PDB; 6QQN; X-ray; 2.30 A; B/D=1-445. DR PDB; 6QTN; X-ray; 1.90 A; B/D=1-445. DR PDB; 6REV; EM; 3.80 A; B/b=1-429. DR PDB; 6RF2; EM; 4.20 A; B/b=1-429. DR PDB; 6RF8; EM; 3.80 A; B/b=1-429. DR PDB; 6RFD; EM; 3.90 A; B/b=1-429. DR PDB; 6S8K; X-ray; 1.52 A; B=1-445. DR PDB; 6S9E; X-ray; 2.25 A; B/D=1-445. DR PDB; 6SES; X-ray; 2.00 A; B/D=1-445. DR PDB; 6WVL; EM; 3.20 A; B/D=1-445. DR PDB; 6WVM; EM; 3.30 A; B/D=1-445. DR PDB; 6WVR; EM; 2.90 A; B/D=1-445. DR PDB; 6Y6D; X-ray; 2.20 A; B/D=1-445. DR PDB; 6ZWB; X-ray; 1.75 A; B=1-445. DR PDB; 6ZWC; X-ray; 2.04 A; B=1-445. DR PDB; 7AC5; X-ray; 2.26 A; B=1-445. DR PDB; 7AU5; X-ray; 2.20 A; B/D=1-445. DR PDB; 7CPD; X-ray; 2.51 A; B/D=1-445. DR PDB; 7CPQ; X-ray; 2.60 A; B/D=1-445. DR PDB; 7E4P; X-ray; 2.40 A; B/D=1-431. DR PDB; 7E4Q; X-ray; 2.50 A; B/D=1-431. DR PDB; 7E4R; X-ray; 2.60 A; B/D=1-431. DR PDB; 7E4Y; X-ray; 2.71 A; B/D=1-431. DR PDB; 7E4Z; X-ray; 2.69 A; B/D=1-431. DR PDB; 7EN3; X-ray; 2.64 A; B/D=1-445. DR PDB; 7JFR; X-ray; 2.35 A; B/D=1-445. DR PDB; 7OGN; X-ray; 2.20 A; B/D=1-445. DR PDB; 7VMG; X-ray; 2.39 A; B/D=1-445. DR PDB; 7VMJ; X-ray; 2.90 A; B/D=1-445. DR PDB; 7VMK; X-ray; 2.50 A; B/D=1-445. DR PDB; 7YYQ; X-ray; 1.70 A; B=1-445. DR PDB; 7YYV; X-ray; 2.20 A; B=1-445. DR PDB; 7YYW; X-ray; 2.20 A; B=1-445. DR PDB; 7YYX; X-ray; 2.20 A; B=1-445. DR PDB; 7YYY; X-ray; 2.20 A; B=1-445. DR PDB; 7YYZ; X-ray; 2.20 A; B=1-445. DR PDB; 7YZ0; X-ray; 2.20 A; B=1-445. DR PDB; 7YZ1; X-ray; 2.20 A; B=1-445. DR PDB; 7YZ2; X-ray; 2.20 A; B=1-445. DR PDB; 7YZ3; X-ray; 1.80 A; B=1-445. DR PDB; 7YZ5; X-ray; 2.11 A; B=1-445. DR PDB; 7YZ6; X-ray; 2.10 A; B=1-445. DR PDB; 7Z01; X-ray; 1.82 A; B=1-445. DR PDB; 7Z02; X-ray; 2.36 A; B=1-445. DR PDB; 7Z2N; X-ray; 2.17 A; B/D=1-445. DR PDB; 7Z2P; X-ray; 2.00 A; B/D=1-445. DR PDB; 7Z7D; X-ray; 2.00 A; B/D=1-445. DR PDB; 7ZX2; X-ray; 2.50 A; B/D=1-445. DR PDB; 7ZYW; X-ray; 2.45 A; B/D=1-445. DR PDB; 8A0L; X-ray; 2.00 A; B/D=1-445. DR PDB; 8A9T; X-ray; 2.30 A; B/D=1-445. DR PDB; 8A9Z; X-ray; 2.29 A; B/D=1-445. DR PDB; 8AHM; X-ray; 2.42 A; B/D=1-445. DR PDB; 8ASN; X-ray; 2.57 A; B/D=1-445. DR PDB; 8B7A; X-ray; 2.25 A; B/D=1-445. DR PDB; 8B7B; X-ray; 2.25 A; B/D=1-445. DR PDB; 8B7C; X-ray; 1.90 A; B/D=1-445. DR PDB; 8BDE; X-ray; 1.90 A; B/D=1-445. DR PDB; 8BDF; X-ray; 1.95 A; B/D=1-445. DR PDB; 8BDG; X-ray; 2.35 A; B/D=1-445. DR PDB; 8C0F; X-ray; 2.10 A; B/D=1-445. DR PDBsum; 1SA0; -. DR PDBsum; 1SA1; -. DR PDBsum; 1TVK; -. DR PDBsum; 1Z2B; -. DR PDBsum; 2P4N; -. DR PDBsum; 2WBE; -. DR PDBsum; 2XRP; -. DR PDBsum; 3DCO; -. DR PDBsum; 3DU7; -. DR PDBsum; 3E22; -. DR PDBsum; 3IZ0; -. DR PDBsum; 3J1T; -. DR PDBsum; 3J1U; -. DR PDBsum; 3J2U; -. DR PDBsum; 4AQV; -. DR PDBsum; 4AQW; -. DR PDBsum; 4ATU; -. DR PDBsum; 4ATX; -. DR PDBsum; 4CK5; -. DR PDBsum; 4CK6; -. DR PDBsum; 4CK7; -. DR PDBsum; 4I4T; -. DR PDBsum; 4I50; -. DR PDBsum; 4I55; -. DR PDBsum; 4IHJ; -. DR PDBsum; 4IIJ; -. DR PDBsum; 4O2A; -. DR PDBsum; 4O2B; -. DR PDBsum; 4O4H; -. DR PDBsum; 4O4I; -. DR PDBsum; 4O4J; -. DR PDBsum; 4O4L; -. DR PDBsum; 4TUY; -. DR PDBsum; 4TV8; -. DR PDBsum; 4TV9; -. DR PDBsum; 4UXO; -. DR PDBsum; 4UXP; -. DR PDBsum; 4UXR; -. DR PDBsum; 4UXS; -. DR PDBsum; 4UXT; -. DR PDBsum; 4UXY; -. DR PDBsum; 4UY0; -. DR PDBsum; 4YJ2; -. DR PDBsum; 4YJ3; -. DR PDBsum; 5EIB; -. DR PDBsum; 5EZY; -. DR PDBsum; 5GON; -. DR PDBsum; 5H74; -. DR PDBsum; 5H7O; -. DR PDBsum; 5ITZ; -. DR PDBsum; 5IYZ; -. DR PDBsum; 5J2T; -. DR PDBsum; 5J2U; -. DR PDBsum; 5JH7; -. DR PDBsum; 5JVD; -. DR PDBsum; 5LA6; -. DR PDBsum; 5LOV; -. DR PDBsum; 5LP6; -. DR PDBsum; 5LXS; -. DR PDBsum; 5LXT; -. DR PDBsum; 5LYJ; -. DR PDBsum; 5M50; -. DR PDBsum; 5M54; -. DR PDBsum; 5M5C; -. DR PDBsum; 5M5I; -. DR PDBsum; 5M5L; -. DR PDBsum; 5M5M; -. DR PDBsum; 5M5N; -. DR PDBsum; 5M5O; -. DR PDBsum; 5M7E; -. DR PDBsum; 5M7G; -. DR PDBsum; 5M8D; -. DR PDBsum; 5M8G; -. DR PDBsum; 5MF4; -. DR PDBsum; 5ND2; -. DR PDBsum; 5ND3; -. DR PDBsum; 5ND4; -. DR PDBsum; 5ND7; -. DR PDBsum; 5NFZ; -. DR PDBsum; 5NG1; -. DR PDBsum; 5NJH; -. DR PDBsum; 5NM5; -. DR PDBsum; 5NQT; -. DR PDBsum; 5NQU; -. DR PDBsum; 5O7A; -. DR PDBsum; 5OSK; -. DR PDBsum; 5OV7; -. DR PDBsum; 5S4L; -. DR PDBsum; 5S4M; -. DR PDBsum; 5S4N; -. DR PDBsum; 5S4O; -. DR PDBsum; 5S4P; -. DR PDBsum; 5S4Q; -. DR PDBsum; 5S4R; -. DR PDBsum; 5S4S; -. DR PDBsum; 5S4T; -. DR PDBsum; 5S4U; -. DR PDBsum; 5S4V; -. DR PDBsum; 5S4W; -. DR PDBsum; 5S4X; -. DR PDBsum; 5S4Y; -. DR PDBsum; 5S4Z; -. DR PDBsum; 5S50; -. DR PDBsum; 5S51; -. DR PDBsum; 5S52; -. DR PDBsum; 5S53; -. DR PDBsum; 5S54; -. DR PDBsum; 5S55; -. DR PDBsum; 5S56; -. DR PDBsum; 5S57; -. DR PDBsum; 5S58; -. DR PDBsum; 5S59; -. DR PDBsum; 5S5A; -. DR PDBsum; 5S5B; -. DR PDBsum; 5S5C; -. DR PDBsum; 5S5D; -. DR PDBsum; 5S5E; -. DR PDBsum; 5S5F; -. DR PDBsum; 5S5G; -. DR PDBsum; 5S5H; -. DR PDBsum; 5S5I; -. DR PDBsum; 5S5J; -. DR PDBsum; 5S5K; -. DR PDBsum; 5S5L; -. DR PDBsum; 5S5M; -. DR PDBsum; 5S5N; -. DR PDBsum; 5S5O; -. DR PDBsum; 5S5P; -. DR PDBsum; 5S5Q; -. DR PDBsum; 5S5R; -. DR PDBsum; 5S5S; -. DR PDBsum; 5S5T; -. DR PDBsum; 5S5U; -. DR PDBsum; 5S5V; -. DR PDBsum; 5S5W; -. DR PDBsum; 5S5X; -. DR PDBsum; 5S5Y; -. DR PDBsum; 5S5Z; -. DR PDBsum; 5S60; -. DR PDBsum; 5S61; -. DR PDBsum; 5S62; -. DR PDBsum; 5S63; -. DR PDBsum; 5S64; -. DR PDBsum; 5S65; -. DR PDBsum; 5S66; -. DR PDBsum; 5S67; -. DR PDBsum; 5SB3; -. DR PDBsum; 5SB4; -. DR PDBsum; 5SB5; -. DR PDBsum; 5SB6; -. DR PDBsum; 5SB7; -. DR PDBsum; 5SB8; -. DR PDBsum; 5SB9; -. DR PDBsum; 5SBA; -. DR PDBsum; 5SBB; -. DR PDBsum; 5SBC; -. DR PDBsum; 5SBD; -. DR PDBsum; 5SBE; -. DR PDBsum; 5XAF; -. DR PDBsum; 5XAG; -. DR PDBsum; 5XLT; -. DR PDBsum; 5XLZ; -. DR PDBsum; 5YZ3; -. DR PDBsum; 5Z4P; -. DR PDBsum; 5Z4U; -. DR PDBsum; 5ZXH; -. DR PDBsum; 6AGK; -. DR PDBsum; 6BBN; -. DR PDBsum; 6EG5; -. DR PDBsum; 6F7C; -. DR PDBsum; 6FII; -. DR PDBsum; 6FJF; -. DR PDBsum; 6FJM; -. DR PDBsum; 6FKJ; -. DR PDBsum; 6FKL; -. DR PDBsum; 6GF3; -. DR PDBsum; 6GJ4; -. DR PDBsum; 6GZE; -. DR PDBsum; 6HX8; -. DR PDBsum; 6I5C; -. DR PDBsum; 6JCJ; -. DR PDBsum; 6K9V; -. DR PDBsum; 6KNZ; -. DR PDBsum; 6N47; -. DR PDBsum; 6OJQ; -. DR PDBsum; 6QQN; -. DR PDBsum; 6QTN; -. DR PDBsum; 6REV; -. DR PDBsum; 6RF2; -. DR PDBsum; 6RF8; -. DR PDBsum; 6RFD; -. DR PDBsum; 6S8K; -. DR PDBsum; 6S9E; -. DR PDBsum; 6SES; -. DR PDBsum; 6WVL; -. DR PDBsum; 6WVM; -. DR PDBsum; 6WVR; -. DR PDBsum; 6Y6D; -. DR PDBsum; 6ZWB; -. DR PDBsum; 6ZWC; -. DR PDBsum; 7AC5; -. DR PDBsum; 7AU5; -. DR PDBsum; 7CPD; -. DR PDBsum; 7CPQ; -. DR PDBsum; 7E4P; -. DR PDBsum; 7E4Q; -. DR PDBsum; 7E4R; -. DR PDBsum; 7E4Y; -. DR PDBsum; 7E4Z; -. DR PDBsum; 7EN3; -. DR PDBsum; 7JFR; -. DR PDBsum; 7OGN; -. DR PDBsum; 7VMG; -. DR PDBsum; 7VMJ; -. DR PDBsum; 7VMK; -. DR PDBsum; 7YYQ; -. DR PDBsum; 7YYV; -. DR PDBsum; 7YYW; -. DR PDBsum; 7YYX; -. DR PDBsum; 7YYY; -. DR PDBsum; 7YYZ; -. DR PDBsum; 7YZ0; -. DR PDBsum; 7YZ1; -. DR PDBsum; 7YZ2; -. DR PDBsum; 7YZ3; -. DR PDBsum; 7YZ5; -. DR PDBsum; 7YZ6; -. DR PDBsum; 7Z01; -. DR PDBsum; 7Z02; -. DR PDBsum; 7Z2N; -. DR PDBsum; 7Z2P; -. DR PDBsum; 7Z7D; -. DR PDBsum; 7ZX2; -. DR PDBsum; 7ZYW; -. DR PDBsum; 8A0L; -. DR PDBsum; 8A9T; -. DR PDBsum; 8A9Z; -. DR PDBsum; 8AHM; -. DR PDBsum; 8ASN; -. DR PDBsum; 8B7A; -. DR PDBsum; 8B7B; -. DR PDBsum; 8B7C; -. DR PDBsum; 8BDE; -. DR PDBsum; 8BDF; -. DR PDBsum; 8BDG; -. DR PDBsum; 8C0F; -. DR AlphaFoldDB; Q6B856; -. DR EMDB; EMD-1340; -. DR EMDB; EMD-1788; -. DR EMDB; EMD-20092; -. DR EMDB; EMD-2078; -. DR EMDB; EMD-2095; -. DR EMDB; EMD-2098; -. DR EMDB; EMD-21919; -. DR EMDB; EMD-21922; -. DR EMDB; EMD-21923; -. DR EMDB; EMD-21924; -. DR EMDB; EMD-2533; -. DR EMDB; EMD-2534; -. DR EMDB; EMD-2535; -. DR EMDB; EMD-2536; -. DR EMDB; EMD-2537; -. DR EMDB; EMD-2538; -. DR EMDB; EMD-2539; -. DR EMDB; EMD-2540; -. DR EMDB; EMD-2541; -. DR EMDB; EMD-2542; -. DR EMDB; EMD-2765; -. DR EMDB; EMD-2766; -. DR EMDB; EMD-2767; -. DR EMDB; EMD-2768; -. DR EMDB; EMD-2769; -. DR EMDB; EMD-2770; -. DR EMDB; EMD-2771; -. DR EMDB; EMD-3444; -. DR EMDB; EMD-3445; -. DR EMDB; EMD-3620; -. DR EMDB; EMD-3621; -. DR EMDB; EMD-3622; -. DR EMDB; EMD-3623; -. DR EMDB; EMD-4154; -. DR EMDB; EMD-4156; -. DR EMDB; EMD-4858; -. DR EMDB; EMD-4861; -. DR EMDB; EMD-4862; -. DR EMDB; EMD-4863; -. DR EMDB; EMD-5565; -. DR SASBDB; Q6B856; -. DR SMR; Q6B856; -. DR BioGRID; 158875; 3. DR DIP; DIP-47524N; -. DR IntAct; Q6B856; 6. DR MINT; Q6B856; -. DR STRING; 9913.ENSBTAP00000030869; -. DR BindingDB; Q6B856; -. DR ChEMBL; CHEMBL3394; -. DR DrugCentral; Q6B856; -. DR iPTMnet; Q6B856; -. DR PaxDb; 9913-ENSBTAP00000005346; -. DR PeptideAtlas; Q6B856; -. DR ABCD; Q6B856; 1 sequenced antibody. DR GeneID; 281555; -. DR KEGG; bta:281555; -. DR CTD; 347733; -. DR eggNOG; KOG1375; Eukaryota. DR InParanoid; Q6B856; -. DR OrthoDB; 3124041at2759; -. DR TreeFam; TF300298; -. DR EvolutionaryTrace; Q6B856; -. DR PRO; PR:Q6B856; -. DR Proteomes; UP000009136; Unplaced. DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central. DR GO; GO:0005874; C:microtubule; IBA:GO_Central. DR GO; GO:0015630; C:microtubule cytoskeleton; ISS:UniProtKB. 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:0046982; F:protein heterodimerization activity; ISS:UniProtKB. 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; ISS:UniProtKB. DR GO; GO:0000278; P:mitotic cell cycle; IBA:GO_Central. DR GO; GO:0007399; P:nervous system development; IEA:UniProtKB-KW. DR GO; GO:1902669; P:positive regulation of axon guidance; ISS:UniProtKB. 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:SF100; TUBULIN BETA-2 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; GTP-binding; KW Isopeptide bond; Magnesium; Metal-binding; Methylation; Microtubule; KW Neurogenesis; Nucleotide-binding; Phosphoprotein; Reference proteome; KW Ubl conjugation. FT CHAIN 1..445 FT /note="Tubulin beta-2B chain" FT /id="PRO_0000262654" FT REGION 422..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 55 FT /note="Phosphothreonine" FT /evidence="ECO:0000250|UniProtKB:Q3KRE8" 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:Q9BVA1" 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 CONFLICT 201 FT /note="C -> S (in Ref. 1; AAT84374)" FT /evidence="ECO:0000305" FT STRAND 4..9 FT /evidence="ECO:0007829|PDB:6S8K" FT HELIX 10..28 FT /evidence="ECO:0007829|PDB:6S8K" FT STRAND 34..36 FT /evidence="ECO:0007829|PDB:6S8K" FT STRAND 39..41 FT /evidence="ECO:0007829|PDB:4IIJ" FT HELIX 42..45 FT /evidence="ECO:0007829|PDB:6S8K" FT HELIX 47..49 FT /evidence="ECO:0007829|PDB:6S8K" FT STRAND 51..53 FT /evidence="ECO:0007829|PDB:6S8K" FT STRAND 57..61 FT /evidence="ECO:0007829|PDB:6S8K" FT STRAND 63..69 FT /evidence="ECO:0007829|PDB:6S8K" FT HELIX 70..78 FT /evidence="ECO:0007829|PDB:6S8K" FT STRAND 79..81 FT /evidence="ECO:0007829|PDB:5S5Q" FT HELIX 82..84 FT /evidence="ECO:0007829|PDB:6S8K" FT HELIX 87..89 FT /evidence="ECO:0007829|PDB:6S8K" FT STRAND 90..92 FT /evidence="ECO:0007829|PDB:6S8K" FT HELIX 101..106 FT /evidence="ECO:0007829|PDB:6S8K" FT HELIX 108..125 FT /evidence="ECO:0007829|PDB:6S8K" FT STRAND 126..128 FT /evidence="ECO:0007829|PDB:1TVK" FT STRAND 132..142 FT /evidence="ECO:0007829|PDB:6S8K" FT HELIX 143..158 FT /evidence="ECO:0007829|PDB:6S8K" FT STRAND 162..170 FT /evidence="ECO:0007829|PDB:6S8K" FT TURN 173..175 FT /evidence="ECO:0007829|PDB:7YYQ" FT STRAND 177..179 FT /evidence="ECO:0007829|PDB:6GF3" FT HELIX 181..195 FT /evidence="ECO:0007829|PDB:6S8K" FT STRAND 197..203 FT /evidence="ECO:0007829|PDB:6S8K" FT HELIX 204..213 FT /evidence="ECO:0007829|PDB:6S8K" FT HELIX 222..241 FT /evidence="ECO:0007829|PDB:6S8K" FT TURN 244..246 FT /evidence="ECO:0007829|PDB:6ZWB" FT HELIX 250..257 FT /evidence="ECO:0007829|PDB:6S8K" FT STRAND 259..262 FT /evidence="ECO:0007829|PDB:5S4S" FT STRAND 265..272 FT /evidence="ECO:0007829|PDB:6S8K" FT HELIX 278..280 FT /evidence="ECO:0007829|PDB:4I4T" FT HELIX 286..294 FT /evidence="ECO:0007829|PDB:6S8K" FT HELIX 296..298 FT /evidence="ECO:0007829|PDB:6S8K" FT STRAND 299..302 FT /evidence="ECO:0007829|PDB:6S8K" FT HELIX 305..307 FT /evidence="ECO:0007829|PDB:6S8K" FT STRAND 310..320 FT /evidence="ECO:0007829|PDB:6S8K" FT HELIX 323..336 FT /evidence="ECO:0007829|PDB:6S8K" FT HELIX 338..340 FT /evidence="ECO:0007829|PDB:6S8K" FT STRAND 345..347 FT /evidence="ECO:0007829|PDB:7Z01" FT STRAND 349..356 FT /evidence="ECO:0007829|PDB:6S8K" FT TURN 359..361 FT /evidence="ECO:0007829|PDB:5LOV" FT STRAND 362..371 FT /evidence="ECO:0007829|PDB:6S8K" FT HELIX 372..374 FT /evidence="ECO:0007829|PDB:6S8K" FT HELIX 375..390 FT /evidence="ECO:0007829|PDB:6S8K" FT TURN 391..395 FT /evidence="ECO:0007829|PDB:6S8K" FT HELIX 396..399 FT /evidence="ECO:0007829|PDB:6S8K" FT TURN 400..402 FT /evidence="ECO:0007829|PDB:6S8K" FT HELIX 405..426 FT /evidence="ECO:0007829|PDB:6S8K" SQ SEQUENCE 445 AA; 49953 MW; 4DC3956EFF880746 CRC64; MREIVHIQAG QCGNQIGAKF WEVISDEHGI DPTGSYHGDS DLQLERINVY YNEATGNKYV PRAILVDLEP GTMDSVRSGP FGQIFRPDNF VFGQSGAGNN WAKGHYTEGA ELVDSVLDVV RKESESCDCL QGFQLTHSLG GGTGSGMGTL LISKIREEYP DRIMNTFSVM PSPKVSDTVV EPYNATLSVH QLVENTDETY CIDNEALYDI CFRTLKLTTP TYGDLNHLVS ATMSGVTTCL RFPGQLNADL RKLAVNMVPF PRLHFFMPGF APLTSRGSQQ YRALTVPELT QQMFDSKNMM AACDPRHGRY LTVAAIFRGR MSMKEVDEQM LNVQNKNSSY FVEWIPNNVK TAVCDIPPRG LKMSATFIGN STAIQELFKR ISEQFTAMFR RKAFLHWYTG EGMDEMEFTE AESNMNDLVS EYQQYQDATA DEQGEFEEEE GEDEA //