ID TBA1_YEAST Reviewed; 447 AA. AC P09733; D6W0J8; DT 01-JUL-1989, integrated into UniProtKB/Swiss-Prot. DT 01-OCT-1996, sequence version 2. DT 02-SEP-2026, entry version 214. DE RecName: Full=Tubulin alpha-1 chain; DE EC=3.6.5.- {ECO:0000250|UniProtKB:P68363}; GN Name=TUB1; OrderedLocusNames=YML085C; 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. RX PubMed=3025610; DOI=10.1128/mcb.6.11.3711-3721.1986; RA Schatz P.J., Pillus L., Grisafi P., Solomon F., Botstein D.; RT "Two functional alpha-tubulin genes of the yeast Saccharomyces cerevisiae RT encode divergent proteins."; RL Mol. Cell. Biol. 6:3711-3721(1986). RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 204508 / S288c; RX PubMed=9169872; DOI=10.1038/387s090; RA Bowman S., Churcher C.M., Badcock K., Brown D., Chillingworth T., RA Connor R., Dedman K., Devlin K., Gentles S., Hamlin N., Hunt S., Jagels K., RA Lye G., Moule S., Odell C., Pearson D., Rajandream M.A., Rice P., RA Skelton J., Walsh S.V., Whitehead S., Barrell B.G.; RT "The nucleotide sequence of Saccharomyces cerevisiae chromosome XIII."; RL Nature 387:90-93(1997). 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 LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS]. RX PubMed=14562106; DOI=10.1038/nature02046; RA Ghaemmaghami S., Huh W.-K., Bower K., Howson R.W., Belle A., Dephoure N., RA O'Shea E.K., Weissman J.S.; RT "Global analysis of protein expression in yeast."; RL Nature 425:737-741(2003). RN [5] RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RX PubMed=19779198; DOI=10.1126/science.1172867; RA Holt L.J., Tuch B.B., Villen J., Johnson A.D., Gygi S.P., Morgan D.O.; RT "Global analysis of Cdk1 substrate phosphorylation sites provides insights RT into evolution."; RL Science 325:1682-1686(2009). RN [6] RP FUNCTION, CATALYTIC ACTIVITY, SUBUNIT, SUBCELLULAR LOCATION, ACTIVE SITE, RP AND MUTAGENESIS OF ASP-252 AND GLU-255. RX PubMed=11739794; DOI=10.1091/mbc.12.12.3973; RA Anders K.R., Botstein D.; RT "Dominant-lethal alpha-tubulin mutants defective in microtubule RT depolymerization in yeast."; RL Mol. Biol. Cell 12:3973-3986(2001). 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:11739794). Microtubules CC grow by the addition of GTP-tubulin dimers to the microtubule end, CC where a stabilizing cap forms. Below the cap, tubulin dimers are in CC GDP-bound state, owing to GTPase activity of alpha-tubulin. CC {ECO:0000269|PubMed:11739794}. CC -!- CATALYTIC ACTIVITY: CC Reaction=GTP + H2O = GDP + phosphate + H(+); Xref=Rhea:RHEA:19669, CC ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:37565, CC ChEBI:CHEBI:43474, ChEBI:CHEBI:58189; CC Evidence={ECO:0000250|UniProtKB:P68363}; CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:19670; CC Evidence={ECO:0000250|UniProtKB:P68363}; 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:11739794). 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. {ECO:0000269|PubMed:11739794}. CC -!- INTERACTION: CC P09733; P02557: TUB2; NbExp=2; IntAct=EBI-18976, EBI-18986; CC -!- SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton CC {ECO:0000269|PubMed:11739794}. CC -!- MISCELLANEOUS: Present with 5590 molecules/cell in log phase SD medium. CC {ECO:0000269|PubMed:14562106}. 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; M28429; AAA35180.1; -; mRNA. DR EMBL; Z46660; CAA86653.1; -; Genomic_DNA. DR EMBL; BK006946; DAA09812.1; -; Genomic_DNA. DR PIR; S50871; S50871. DR RefSeq; NP_013625.1; NM_001182444.1. DR PDB; 4FFB; X-ray; 2.88 A; A=1-447. DR PDB; 4U3J; X-ray; 2.81 A; A=1-447. DR PDB; 5W3F; EM; 3.70 A; A=1-447. DR PDB; 5W3H; EM; 4.00 A; A=1-447. DR PDB; 5W3J; EM; 4.00 A; A=1-447. DR PDB; 8QV0; EM; 6.60 A; A/C/D/E/F/G/H/I/J/K/L/M/N=1-447. DR PDB; 8QV2; EM; 9.20 A; Ab/Ac/Ad/Ae/Af/Ag/Ah/Ai/Aj/Ak/Al/Am/An/Ao/Ap/Aq/Ar=1-447. DR PDB; 8QV3; EM; 8.20 A; Ac/Ad=1-447. DR AlphaFoldDB; P09733; -. DR EMDB; EMD-18664; -. DR EMDB; EMD-18665; -. DR EMDB; EMD-18666; -. DR EMDB; EMD-8755; -. DR EMDB; EMD-8756; -. DR EMDB; EMD-8757; -. DR EMDB; EMD-8758; -. DR EMDB; EMD-8759; -. DR SMR; P09733; -. DR BioGRID; 35056; 390. DR ComplexPortal; CPX-1424; Tubulin alpha-beta heterodimeric complex, TUB1 variant. DR DIP; DIP-854N; -. DR FunCoup; P09733; 1615. DR IntAct; P09733; 344. DR MINT; P09733; -. DR STRING; 4932.YML085C; -. DR iPTMnet; P09733; -. DR SwissPalm; P09733; -. DR PaxDb; 4932-YML085C; -. DR PeptideAtlas; P09733; -. DR EnsemblFungi; YML085C_mRNA; YML085C; YML085C. DR GeneID; 854889; -. DR KEGG; sce:YML085C; -. DR AGR; SGD:S000004550; -. DR SGD; S000004550; TUB1. DR VEuPathDB; FungiDB:YML085C; -. DR eggNOG; KOG1376; Eukaryota. DR HOGENOM; CLU_015718_0_0_1; -. DR InParanoid; P09733; -. DR OMA; ESCYDIC; -. DR OrthoDB; 1662883at2759; -. DR BioCyc; YEAST:G3O-32674-MONOMER; -. DR BioGRID-ORCS; 854889; 4 hits in 10 CRISPR screens. DR CD-CODE; 876000F7; Centrosome. DR CD-CODE; E03F929F; Stress granule. DR EvolutionaryTrace; P09733; -. DR PRO; PR:P09733; -. DR Proteomes; UP000002311; Chromosome XIII. DR RNAct; P09733; protein. DR GO; GO:0005737; C:cytoplasm; HDA:SGD. DR GO; GO:0005874; C:microtubule; IEA:InterPro. DR GO; GO:0034399; C:nuclear periphery; IDA:SGD. DR GO; GO:0005634; C:nucleus; HDA:SGD. DR GO; GO:0005819; C:spindle; IBA:GO_Central. 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; ISS:UniProtKB. DR GO; GO:0005200; F:structural constituent of cytoskeleton; IBA:GO_Central. DR GO; GO:0045143; P:homologous chromosome segregation; IMP:SGD. DR GO; GO:0000226; P:microtubule cytoskeleton organization; IMP:ComplexPortal. DR GO; GO:0000278; P:mitotic cell cycle; IBA:GO_Central. DR GO; GO:0000070; P:mitotic sister chromatid segregation; IMP:SGD. DR GO; GO:0000280; P:nuclear division; IBA:GO_Central. DR GO; GO:0030473; P:nuclear migration along microtubule; IMP:SGD. DR GO; GO:0098863; P:nuclear migration by microtubule mediated pushing forces; IBA:GO_Central. DR CDD; cd02186; alpha_tubulin; 1. DR FunFam; 1.10.287.600:FF:000005; Tubulin alpha chain; 1. DR FunFam; 3.30.1330.20:FF:000001; Tubulin alpha chain; 1. DR FunFam; 3.40.50.1440:FF:000008; Tubulin alpha chain; 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; IPR002452; Alpha_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 Pfam; PF00091; Tubulin; 1. DR Pfam; PF03953; Tubulin_C; 1. DR PRINTS; PR01162; ALPHATUBULIN. 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 PDBsum; 4FFB; -. DR PDBsum; 4U3J; -. DR PDBsum; 5W3F; -. DR PDBsum; 5W3H; -. DR PDBsum; 5W3J; -. DR PDBsum; 8QV0; -. DR PDBsum; 8QV2; -. DR PDBsum; 8QV3; -. PE 1: Evidence at protein level; KW 3D-structure; Cytoplasm; Cytoskeleton; GTP-binding; Hydrolase; Magnesium; KW Metal-binding; Microtubule; Nucleotide-binding; Reference proteome. FT CHAIN 1..447 FT /note="Tubulin alpha-1 chain" FT /id="PRO_0000048239" FT ACT_SITE 255 FT /evidence="ECO:0000305|PubMed:11739794" FT BINDING 11 FT /ligand="GTP" FT /ligand_id="ChEBI:CHEBI:37565" FT /evidence="ECO:0000250|UniProtKB:P68363" FT BINDING 72 FT /ligand="GTP" FT /ligand_id="ChEBI:CHEBI:37565" FT /evidence="ECO:0000250|UniProtKB:P68363" FT BINDING 72 FT /ligand="Mg(2+)" FT /ligand_id="ChEBI:CHEBI:18420" FT /evidence="ECO:0000250|UniProtKB:P68363" FT BINDING 141 FT /ligand="GTP" FT /ligand_id="ChEBI:CHEBI:37565" FT /evidence="ECO:0000250|UniProtKB:P68363" FT BINDING 145 FT /ligand="GTP" FT /ligand_id="ChEBI:CHEBI:37565" FT /evidence="ECO:0000250|UniProtKB:P68363" FT BINDING 146 FT /ligand="GTP" FT /ligand_id="ChEBI:CHEBI:37565" FT /evidence="ECO:0000250|UniProtKB:P68363" FT BINDING 180 FT /ligand="GTP" FT /ligand_id="ChEBI:CHEBI:37565" FT /evidence="ECO:0000250|UniProtKB:P68363" FT BINDING 207 FT /ligand="GTP" FT /ligand_id="ChEBI:CHEBI:37565" FT /evidence="ECO:0000250|UniProtKB:P68363" FT BINDING 229 FT /ligand="GTP" FT /ligand_id="ChEBI:CHEBI:37565" FT /evidence="ECO:0000250|UniProtKB:P68363" FT MUTAGEN 252 FT /note="D->A: Poisonous alpha-tubulins that cause lethality. FT Microtubules do not depolymerize." FT /evidence="ECO:0000269|PubMed:11739794" FT MUTAGEN 255 FT /note="E->A: Poisonous alpha-tubulins that cause lethality. FT Microtubules do not depolymerize." FT /evidence="ECO:0000269|PubMed:11739794" FT CONFLICT 94 FT /note="I -> L (in Ref. 1; AAA35180)" FT /evidence="ECO:0000305" FT CONFLICT 327 FT /note="R -> G (in Ref. 1; AAA35180)" 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 STRAND 34..36 FT /evidence="ECO:0007829|PDB:4U3J" FT STRAND 47..50 FT /evidence="ECO:0007829|PDB:4U3J" FT TURN 51..53 FT /evidence="ECO:0007829|PDB:4U3J" FT STRAND 54..56 FT /evidence="ECO:0007829|PDB:4U3J" FT STRAND 58..60 FT /evidence="ECO:0007829|PDB:4U3J" FT STRAND 62..64 FT /evidence="ECO:0007829|PDB:4U3J" FT STRAND 66..72 FT /evidence="ECO:0007829|PDB:4U3J" FT HELIX 73..81 FT /evidence="ECO:0007829|PDB:4U3J" FT TURN 83..87 FT /evidence="ECO:0007829|PDB:4U3J" FT TURN 90..92 FT /evidence="ECO:0007829|PDB:4U3J" FT STRAND 93..95 FT /evidence="ECO:0007829|PDB:4U3J" FT HELIX 106..110 FT /evidence="ECO:0007829|PDB:4U3J" FT HELIX 112..127 FT /evidence="ECO:0007829|PDB:4U3J" FT STRAND 135..145 FT /evidence="ECO:0007829|PDB:4U3J" FT HELIX 146..150 FT /evidence="ECO:0007829|PDB:4U3J" FT HELIX 151..161 FT /evidence="ECO:0007829|PDB:4U3J" FT TURN 162..164 FT /evidence="ECO:0007829|PDB:4U3J" FT STRAND 165..173 FT /evidence="ECO:0007829|PDB:4U3J" FT HELIX 176..178 FT /evidence="ECO:0007829|PDB:4U3J" FT HELIX 184..195 FT /evidence="ECO:0007829|PDB:4U3J" FT STRAND 196..198 FT /evidence="ECO:0007829|PDB:4U3J" FT STRAND 200..206 FT /evidence="ECO:0007829|PDB:4U3J" FT HELIX 207..216 FT /evidence="ECO:0007829|PDB:4U3J" FT HELIX 225..239 FT /evidence="ECO:0007829|PDB:4U3J" FT HELIX 241..244 FT /evidence="ECO:0007829|PDB:4U3J" FT HELIX 253..260 FT /evidence="ECO:0007829|PDB:4U3J" FT STRAND 262..265 FT /evidence="ECO:0007829|PDB:4FFB" FT STRAND 270..274 FT /evidence="ECO:0007829|PDB:4U3J" FT HELIX 289..295 FT /evidence="ECO:0007829|PDB:4U3J" FT HELIX 299..301 FT /evidence="ECO:0007829|PDB:4U3J" FT STRAND 302..306 FT /evidence="ECO:0007829|PDB:4U3J" FT STRAND 313..323 FT /evidence="ECO:0007829|PDB:4U3J" FT HELIX 326..338 FT /evidence="ECO:0007829|PDB:4U3J" FT STRAND 352..357 FT /evidence="ECO:0007829|PDB:4U3J" FT STRAND 365..369 FT /evidence="ECO:0007829|PDB:4U3J" FT STRAND 373..382 FT /evidence="ECO:0007829|PDB:4U3J" FT HELIX 383..385 FT /evidence="ECO:0007829|PDB:4U3J" FT HELIX 386..400 FT /evidence="ECO:0007829|PDB:4U3J" FT TURN 401..405 FT /evidence="ECO:0007829|PDB:4U3J" FT HELIX 406..410 FT /evidence="ECO:0007829|PDB:4U3J" FT TURN 411..413 FT /evidence="ECO:0007829|PDB:4U3J" FT HELIX 417..436 FT /evidence="ECO:0007829|PDB:4U3J" SQ SEQUENCE 447 AA; 49800 MW; E263B49440F71889 CRC64; MREVISINVG QAGCQIGNAC WELYSLEHGI KPDGHLEDGL SKPKGGEEGF STFFHETGYG KFVPRAIYVD LEPNVIDEVR NGPYKDLFHP EQLISGKEDA ANNYARGHYT VGREILGDVL DRIRKLADQC DGLQGFLFTH SLGGGTGSGL GSLLLEELSA EYGKKSKLEF AVYPAPQVST SVVEPYNTVL TTHTTLEHAD CTFMVDNEAI YDMCKRNLDI PRPSFANLNN LIAQVVSSVT ASLRFDGSLN VDLNEFQTNL VPYPRIHFPL VSYSPVLSKS KAFHESNSVS EITNACFEPG NQMVKCDPRD GKYMATCLLY RGDVVTRDVQ RAVEQVKNKK TVQLVDWCPT GFKIGICYEP PTATPNSQLA TVDRAVCMLS NTTSIAEAWK RIDRKFDLMY AKRAFVHWYV GEGMEEGEFT EAREDLAALE RDYIEVGADS YAEEEEF //