GenomeNet

Database: UniProt
Entry: P02557
LinkDB: P02557
Original site: P02557 
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   07-OCT-2020, entry version 197.
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}.
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; 447.
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   EuPathDB; FungiDB:YFL037W; -.
DR   SGD; S000001857; TUB2.
DR   eggNOG; KOG1375; Eukaryota.
DR   GeneTree; ENSGT00940000154394; -.
DR   HOGENOM; CLU_015718_1_1_1; -.
DR   InParanoid; P02557; -.
DR   KO; K07375; -.
DR   OMA; EVGANKY; -.
DR   Reactome; R-SCE-5617833; Cilium Assembly.
DR   Reactome; R-SCE-5626467; RHO GTPases activate IQGAPs.
DR   Reactome; R-SCE-6798695; Neutrophil degranulation.
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: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   MOD_RES         278
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000244|PubMed:18407956"
FT   MOD_RES         280
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000244|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:0000244|PDB:4U3J"
FT   HELIX           10..27
FT                   /evidence="ECO:0000244|PDB:4U3J"
FT   HELIX           42..45
FT                   /evidence="ECO:0000244|PDB:4U3J"
FT   HELIX           46..49
FT                   /evidence="ECO:0000244|PDB:4U3J"
FT   STRAND          51..53
FT                   /evidence="ECO:0000244|PDB:4U3J"
FT   STRAND          59..61
FT                   /evidence="ECO:0000244|PDB:4U3J"
FT   STRAND          63..69
FT                   /evidence="ECO:0000244|PDB:4U3J"
FT   HELIX           70..77
FT                   /evidence="ECO:0000244|PDB:4U3J"
FT   HELIX           80..82
FT                   /evidence="ECO:0000244|PDB:4FFB"
FT   STRAND          83..85
FT                   /evidence="ECO:0000244|PDB:4U3J"
FT   HELIX           87..89
FT                   /evidence="ECO:0000244|PDB:4U3J"
FT   STRAND          90..92
FT                   /evidence="ECO:0000244|PDB:4U3J"
FT   HELIX           101..105
FT                   /evidence="ECO:0000244|PDB:4U3J"
FT   TURN            108..112
FT                   /evidence="ECO:0000244|PDB:4U3J"
FT   HELIX           113..125
FT                   /evidence="ECO:0000244|PDB:4U3J"
FT   STRAND          132..142
FT                   /evidence="ECO:0000244|PDB:4U3J"
FT   HELIX           143..158
FT                   /evidence="ECO:0000244|PDB:4U3J"
FT   STRAND          162..170
FT                   /evidence="ECO:0000244|PDB:4U3J"
FT   HELIX           181..195
FT                   /evidence="ECO:0000244|PDB:4U3J"
FT   STRAND          197..203
FT                   /evidence="ECO:0000244|PDB:4U3J"
FT   HELIX           204..211
FT                   /evidence="ECO:0000244|PDB:4U3J"
FT   HELIX           222..236
FT                   /evidence="ECO:0000244|PDB:4U3J"
FT   HELIX           238..241
FT                   /evidence="ECO:0000244|PDB:4U3J"
FT   STRAND          242..244
FT                   /evidence="ECO:0000244|PDB:4FFB"
FT   STRAND          245..247
FT                   /evidence="ECO:0000244|PDB:4U3J"
FT   HELIX           250..257
FT                   /evidence="ECO:0000244|PDB:4U3J"
FT   STRAND          265..271
FT                   /evidence="ECO:0000244|PDB:4U3J"
FT   HELIX           286..294
FT                   /evidence="ECO:0000244|PDB:4U3J"
FT   HELIX           296..298
FT                   /evidence="ECO:0000244|PDB:4U3J"
FT   STRAND          299..303
FT                   /evidence="ECO:0000244|PDB:4U3J"
FT   HELIX           305..307
FT                   /evidence="ECO:0000244|PDB:4U3J"
FT   STRAND          310..320
FT                   /evidence="ECO:0000244|PDB:4U3J"
FT   HELIX           323..336
FT                   /evidence="ECO:0000244|PDB:4U3J"
FT   HELIX           338..340
FT                   /evidence="ECO:0000244|PDB:4U3J"
FT   STRAND          345..347
FT                   /evidence="ECO:0000244|PDB:4U3J"
FT   STRAND          349..355
FT                   /evidence="ECO:0000244|PDB:4U3J"
FT   STRAND          362..371
FT                   /evidence="ECO:0000244|PDB:4U3J"
FT   HELIX           372..374
FT                   /evidence="ECO:0000244|PDB:4U3J"
FT   HELIX           375..389
FT                   /evidence="ECO:0000244|PDB:4U3J"
FT   TURN            390..395
FT                   /evidence="ECO:0000244|PDB:4U3J"
FT   HELIX           396..399
FT                   /evidence="ECO:0000244|PDB:4U3J"
FT   TURN            400..402
FT                   /evidence="ECO:0000244|PDB:4U3J"
FT   HELIX           405..426
FT                   /evidence="ECO:0000244|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
//
DBGET integrated database retrieval system