ID TBB_YEAST Reviewed; 457 AA. AC P02557; D6VTJ3; DT 21-JUL-1986, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1995, sequence version 2. DT 02-JUN-2021, entry version 201. DE RecName: Full=Tubulin beta chain; DE AltName: Full=Beta-tubulin; GN Name=TUB2; OrderedLocusNames=YFL037W; OS Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast). OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes; OC Saccharomycetales; Saccharomycetaceae; Saccharomyces. OX NCBI_TaxID=559292; RN [1] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA]. RX PubMed=6380751; DOI=10.1016/0092-8674(83)90350-1; RA Neff N.F., Thomas J.H., Grisafi P., Botstein D.; RT "Isolation of the beta-tubulin gene from yeast and demonstration of its RT essential function in vivo."; RL Cell 33:211-219(1983). RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 204508 / S288c; RX PubMed=7670463; DOI=10.1038/ng0795-261; RA Murakami Y., Naitou M., Hagiwara H., Shibata T., Ozawa M., Sasanuma S., RA Sasanuma M., Tsuchiya Y., Soeda E., Yokoyama K., Yamazaki M., Tashiro H., RA Eki T.; RT "Analysis of the nucleotide sequence of chromosome VI from Saccharomyces RT cerevisiae."; RL Nat. Genet. 10:261-268(1995). RN [3] RP GENOME REANNOTATION. RC STRAIN=ATCC 204508 / S288c; RX PubMed=24374639; DOI=10.1534/g3.113.008995; RA Engel S.R., Dietrich F.S., Fisk D.G., Binkley G., Balakrishnan R., RA Costanzo M.C., Dwight S.S., Hitz B.C., Karra K., Nash R.S., Weng S., RA Wong E.D., Lloyd P., Skrzypek M.S., Miyasato S.R., Simison M., Cherry J.M.; RT "The reference genome sequence of Saccharomyces cerevisiae: Then and now."; RL G3 (Bethesda) 4:389-398(2014). RN [4] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-8. RX PubMed=6318115; DOI=10.1038/306704a0; RA Gallwitz D., Donath C., Sander C.; RT "A yeast gene encoding a protein homologous to the human c-has/bas proto- RT oncogene product."; RL Nature 306:704-707(1983). RN [5] RP ANTIBIOTIC RESISTANCE TO RHIZOXIN. RX PubMed=2274023; DOI=10.1007/bf00633814; RA Takahashi M., Matsumoto S., Iwasaki S., Yahara I.; RT "Molecular basis for determining the sensitivity of eucaryotes to the RT antimitotic drug rhizoxin."; RL Mol. Gen. Genet. 222:169-175(1990). RN [6] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-278 AND SER-280, AND RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RX PubMed=18407956; DOI=10.1074/mcp.m700468-mcp200; RA Albuquerque C.P., Smolka M.B., Payne S.H., Bafna V., Eng J., Zhou H.; RT "A multidimensional chromatography technology for in-depth phosphoproteome RT analysis."; RL Mol. Cell. Proteomics 7:1389-1396(2008). RN [7] RP SUBCELLULAR LOCATION, AND MUTAGENESIS OF GLU-421. RX PubMed=23001566; DOI=10.1093/hmg/dds393; RA Cederquist G.Y., Luchniak A., Tischfield M.A., Peeva M., Song Y., RA Menezes M.P., Chan W.M., Andrews C., Chew S., Jamieson R.V., Gomes L., RA Flaherty M., Grant P.E., Gupta M.L. Jr., Engle E.C.; RT "An inherited TUBB2B mutation alters a kinesin-binding site and causes RT polymicrogyria, CFEOM and axon dysinnervation."; RL Hum. Mol. Genet. 21:5484-5499(2012). RN [8] RP FUNCTION, AND MUTAGENESIS OF LYS-390. RX PubMed=28013290; DOI=10.1093/hmg/ddw383; RA Breuss M.W., Nguyen T., Srivatsan A., Leca I., Tian G., Fritz T., RA Hansen A.H., Musaev D., McEvoy-Venneri J., James K.N., Rosti R.O., RA Scott E., Tan U., Kolodner R.D., Cowan N.J., Keays D.A., Gleeson J.G.; RT "Uner Tan syndrome caused by a homozygous TUBB2B mutation affecting RT microtubule stability."; RL Hum. Mol. Genet. 26:258-269(2017). CC -!- FUNCTION: Tubulin is the major constituent of microtubules CC (PubMed:28013290). It binds two moles of GTP, one at an exchangeable CC site on the beta chain and one at a non-exchangeable site on the alpha CC chain. {ECO:0000269|PubMed:28013290}. 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. CC -!- INTERACTION: CC P02557; P48606: RBL2; NbExp=2; IntAct=EBI-18986, EBI-18991; CC -!- SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton CC {ECO:0000269|PubMed:23001566}. Note=Colocalizes with kinesin KIP3 at CC the plus ends of growing microtubules and along the microtubule CC lattice. {ECO:0000269|PubMed:23001566}. CC -!- MISCELLANEOUS: Rhizoxin, an antibiotic that exhibits potent anti- CC mitotic activity against most eukaryotic cells except for yeasts, binds CC to beta tubulin. 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; V01296; CAA24603.1; -; Genomic_DNA. DR EMBL; D50617; BAA09202.1; -; Genomic_DNA. DR EMBL; X00209; CAA25035.1; -; Genomic_DNA. DR EMBL; BK006940; DAA12403.1; -; Genomic_DNA. DR PIR; S56217; UBBYB. DR RefSeq; NP_116616.1; NM_001179929.1. DR PDB; 4FFB; X-ray; 2.88 A; B=1-457. DR PDB; 4U3J; X-ray; 2.81 A; B=1-457. DR PDB; 5W3F; EM; 3.70 A; B=1-457. DR PDB; 5W3H; EM; 4.00 A; B=1-457. DR PDB; 5W3J; EM; 4.00 A; B=1-457. DR PDBsum; 4FFB; -. DR PDBsum; 4U3J; -. DR PDBsum; 5W3F; -. DR PDBsum; 5W3H; -. DR PDBsum; 5W3J; -. DR SMR; P02557; -. DR BioGRID; 31109; 448. DR ComplexPortal; CPX-1424; Tubulin alpha-beta heterodimeric complex, TUB1 variant. DR ComplexPortal; CPX-1425; Tubulin alpha-beta heterodimeric complex, TUB3 variant. DR DIP; DIP-2340N; -. DR IntAct; P02557; 339. DR MINT; P02557; -. DR STRING; 4932.YFL037W; -. DR iPTMnet; P02557; -. DR MaxQB; P02557; -. DR PaxDb; P02557; -. DR PRIDE; P02557; -. DR EnsemblFungi; YFL037W_mRNA; YFL037W; YFL037W. DR GeneID; 850506; -. DR KEGG; sce:YFL037W; -. DR SGD; S000001857; TUB2. DR VEuPathDB; FungiDB:YFL037W; -. DR eggNOG; KOG1375; Eukaryota. DR GeneTree; ENSGT00940000154394; -. DR HOGENOM; CLU_015718_1_1_1; -. DR InParanoid; P02557; -. DR OMA; EVGANKY; -. DR Reactome; R-SCE-5617833; Cilium Assembly. DR Reactome; R-SCE-6798695; Neutrophil degranulation. DR PRO; PR:P02557; -. DR Proteomes; UP000002311; Chromosome VI. DR RNAct; P02557; protein. DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central. DR GO; GO:0005881; C:cytoplasmic microtubule; IC:SGD. DR GO; GO:0005828; C:kinetochore microtubule; IC:SGD. DR GO; GO:0005874; C:microtubule; IBA:GO_Central. DR GO; GO:0005880; C:nuclear microtubule; IC:SGD. DR GO; GO:0045298; C:tubulin complex; IDA:SGD. DR GO; GO:0005525; F:GTP binding; IBA:GO_Central. DR GO; GO:0003924; F:GTPase activity; IEA:InterPro. DR GO; GO:0005200; F:structural constituent of cytoskeleton; IBA:GO_Central. DR GO; GO:0031122; P:cytoplasmic microtubule organization; IMP:SGD. DR GO; GO:0007010; P:cytoskeleton organization; IMP:UniProtKB. DR GO; GO:0045143; P:homologous chromosome segregation; IC:SGD. DR GO; GO:0000226; P:microtubule cytoskeleton organization; IBA:GO_Central. DR GO; GO:0007017; P:microtubule-based process; IMP:UniProtKB. DR GO; GO:0000278; P:mitotic cell cycle; IBA:GO_Central. DR GO; GO:0000070; P:mitotic sister chromatid segregation; IC:SGD. DR GO; GO:0090307; P:mitotic spindle assembly; IMP:SGD. DR GO; GO:0000022; P:mitotic spindle elongation; IMP:SGD. DR GO; GO:0030473; P:nuclear migration along microtubule; IC:SGD. DR GO; GO:0090316; P:positive regulation of intracellular protein transport; IMP:UniProtKB. DR GO; GO:0046677; P:response to antibiotic; IEA:UniProtKB-KW. 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; IPR018316; Tubulin/FtsZ_2-layer-sand-dom. DR InterPro; IPR037103; Tubulin/FtsZ_C_sf. 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; Antibiotic resistance; Cytoplasm; Cytoskeleton; GTP-binding; KW Microtubule; Nucleotide-binding; Phosphoprotein; Reference proteome. FT CHAIN 1..457 FT /note="Tubulin beta chain" FT /id="PRO_0000048443" FT NP_BIND 140..146 FT /note="GTP" FT /evidence="ECO:0000255" FT REGION 423..457 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT MOD_RES 278 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:18407956" FT MOD_RES 280 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:18407956" FT MUTAGEN 100 FT /note="V->N: Becomes sensitive to rhizoxin." FT MUTAGEN 390 FT /note="K->Q: Decreased microtubule stability." FT /evidence="ECO:0000269|PubMed:28013290" FT MUTAGEN 421 FT /note="E->K: Increased microtubule polymerization and FT depolymerization rates. Increased microtubule stability. FT Decreased kinesin KIP3 subcellular location at microtubule FT plus ends." FT /evidence="ECO:0000269|PubMed:23001566" FT CONFLICT 9 FT /note="T -> A (in Ref. 1; CAA24603)" FT /evidence="ECO:0000305" FT CONFLICT 12 FT /note="C -> Y (in Ref. 1; CAA24603)" FT /evidence="ECO:0000305" FT CONFLICT 71 FT /note="G -> W (in Ref. 1; CAA24603)" FT /evidence="ECO:0000305" FT CONFLICT 152 FT /note="I -> F (in Ref. 1; CAA24603)" FT /evidence="ECO:0000305" FT CONFLICT 156 FT /note="R -> K (in Ref. 1; CAA24603)" FT /evidence="ECO:0000305" FT CONFLICT 159 FT /note="F -> L (in Ref. 1; CAA24603)" FT /evidence="ECO:0000305" FT STRAND 4..9 FT /evidence="ECO:0007829|PDB:4U3J" FT HELIX 10..27 FT /evidence="ECO:0007829|PDB:4U3J" FT HELIX 42..45 FT /evidence="ECO:0007829|PDB:4U3J" FT HELIX 46..49 FT /evidence="ECO:0007829|PDB:4U3J" FT STRAND 51..53 FT /evidence="ECO:0007829|PDB:4U3J" FT STRAND 59..61 FT /evidence="ECO:0007829|PDB:4U3J" FT STRAND 63..69 FT /evidence="ECO:0007829|PDB:4U3J" FT HELIX 70..77 FT /evidence="ECO:0007829|PDB:4U3J" FT HELIX 80..82 FT /evidence="ECO:0007829|PDB:4FFB" FT STRAND 83..85 FT /evidence="ECO:0007829|PDB:4U3J" FT HELIX 87..89 FT /evidence="ECO:0007829|PDB:4U3J" FT STRAND 90..92 FT /evidence="ECO:0007829|PDB:4U3J" FT HELIX 101..105 FT /evidence="ECO:0007829|PDB:4U3J" FT TURN 108..112 FT /evidence="ECO:0007829|PDB:4U3J" FT HELIX 113..125 FT /evidence="ECO:0007829|PDB:4U3J" FT STRAND 132..142 FT /evidence="ECO:0007829|PDB:4U3J" FT HELIX 143..158 FT /evidence="ECO:0007829|PDB:4U3J" FT STRAND 162..170 FT /evidence="ECO:0007829|PDB:4U3J" FT HELIX 181..195 FT /evidence="ECO:0007829|PDB:4U3J" FT STRAND 197..203 FT /evidence="ECO:0007829|PDB:4U3J" FT HELIX 204..211 FT /evidence="ECO:0007829|PDB:4U3J" FT HELIX 222..236 FT /evidence="ECO:0007829|PDB:4U3J" FT HELIX 238..241 FT /evidence="ECO:0007829|PDB:4U3J" FT STRAND 242..244 FT /evidence="ECO:0007829|PDB:4FFB" FT STRAND 245..247 FT /evidence="ECO:0007829|PDB:4U3J" FT HELIX 250..257 FT /evidence="ECO:0007829|PDB:4U3J" FT STRAND 265..271 FT /evidence="ECO:0007829|PDB:4U3J" FT HELIX 286..294 FT /evidence="ECO:0007829|PDB:4U3J" FT HELIX 296..298 FT /evidence="ECO:0007829|PDB:4U3J" FT STRAND 299..303 FT /evidence="ECO:0007829|PDB:4U3J" FT HELIX 305..307 FT /evidence="ECO:0007829|PDB:4U3J" FT STRAND 310..320 FT /evidence="ECO:0007829|PDB:4U3J" FT HELIX 323..336 FT /evidence="ECO:0007829|PDB:4U3J" FT HELIX 338..340 FT /evidence="ECO:0007829|PDB:4U3J" FT STRAND 345..347 FT /evidence="ECO:0007829|PDB:4U3J" FT STRAND 349..355 FT /evidence="ECO:0007829|PDB:4U3J" FT STRAND 362..371 FT /evidence="ECO:0007829|PDB:4U3J" FT HELIX 372..374 FT /evidence="ECO:0007829|PDB:4U3J" FT HELIX 375..389 FT /evidence="ECO:0007829|PDB:4U3J" FT TURN 390..395 FT /evidence="ECO:0007829|PDB:4U3J" FT HELIX 396..399 FT /evidence="ECO:0007829|PDB:4U3J" FT TURN 400..402 FT /evidence="ECO:0007829|PDB:4U3J" FT HELIX 405..426 FT /evidence="ECO:0007829|PDB:4U3J" SQ SEQUENCE 457 AA; 50923 MW; 68EBEA7D7A5B8EA1 CRC64; MREIIHISTG QCGNQIGAAF WETICGEHGL DFNGTYHGHD DIQKERLNVY FNEASSGKWV PRSINVDLEP GTIDAVRNSA IGNLFRPDNY IFGQSSAGNV WAKGHYTEGA ELVDSVMDVI RREAEGCDSL QGFQITHSLG GGTGSGMGTL LISKIREEFP DRMMATFSVL PSPKTSDTVV EPYNATLSVH QLVEHSDETF CIDNEALYDI CQRTLKLNQP SYGDLNNLVS SVMSGVTTSL RYPGQLNSDL RKLAVNLVPF PRLHFFMVGY APLTAIGSQS FRSLTVPELT QQMFDAKNMM AAADPRNGRY LTVAAFFRGK VSVKEVEDEM HKVQSKNSDY FVEWIPNNVQ TAVCSVAPQG LDMAATFIAN STSIQELFKR VGDQFSAMFK RKAFLHWYTS EGMDELEFSE AESNMNDLVS EYQQYQEATV EDDEEVDENG DFGAPQNQDE PITENFE //