TBB_YEAST
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 03-AUG-2022, entry version 205.
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}.
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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 AlphaFoldDB; P02557; -.
DR SMR; P02557; -.
DR BioGRID; 31109; 472.
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; VCSVAPK; -.
DR BioCyc; YEAST:G3O-30425-MON; -.
DR Reactome; R-SCE-5617833; Cilium Assembly.
DR Reactome; R-SCE-6798695; Neutrophil degranulation.
DR Reactome; R-SCE-9646399; Aggrephagy.
DR Reactome; R-SCE-9668328; Sealing of the nuclear envelope (NE) by ESCRT-III.
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: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; IMP:ComplexPortal.
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; 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; 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 REGION 423..457
FT /note="Disordered"
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 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
