TBA1_YEAST
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 03-AUG-2022, entry version 195.
DE RecName: Full=Tubulin alpha-1 chain;
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;
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).
CC -!- FUNCTION: Tubulin is the major constituent of microtubules. It binds
CC two moles of GTP, one at an exchangeable site on the beta chain and one
CC at a non-exchangeable site on the alpha chain.
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 -!- SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton.
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}.
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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 PDBsum; 4FFB; -.
DR PDBsum; 4U3J; -.
DR PDBsum; 5W3F; -.
DR PDBsum; 5W3H; -.
DR PDBsum; 5W3J; -.
DR AlphaFoldDB; P09733; -.
DR SMR; P09733; -.
DR BioGRID; 35056; 174.
DR ComplexPortal; CPX-1424; Tubulin alpha-beta heterodimeric complex, TUB1 variant.
DR DIP; DIP-854N; -.
DR IntAct; P09733; 315.
DR MINT; P09733; -.
DR STRING; 4932.YML085C; -.
DR iPTMnet; P09733; -.
DR SwissPalm; P09733; -.
DR MaxQB; P09733; -.
DR PaxDb; P09733; -.
DR PRIDE; P09733; -.
DR EnsemblFungi; YML085C_mRNA; YML085C; YML085C.
DR GeneID; 854889; -.
DR KEGG; sce:YML085C; -.
DR SGD; S000004550; TUB1.
DR VEuPathDB; FungiDB:YML085C; -.
DR eggNOG; KOG1376; Eukaryota.
DR GeneTree; ENSGT00940000164588; -.
DR HOGENOM; CLU_015718_0_0_1; -.
DR InParanoid; P09733; -.
DR OMA; VDNEACY; -.
DR BioCyc; YEAST:G3O-32674-MON; -.
DR Reactome; R-SCE-114608; Platelet degranulation.
DR Reactome; R-SCE-5617833; Cilium Assembly.
DR Reactome; R-SCE-9646399; Aggrephagy.
DR Reactome; R-SCE-9668328; Sealing of the nuclear envelope (NE) by ESCRT-III.
DR PRO; PR:P09733; -.
DR Proteomes; UP000002311; Chromosome XIII.
DR RNAct; P09733; protein.
DR GO; GO:0005737; C:cytoplasm; HDA:SGD.
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:0034399; C:nuclear periphery; IDA:SGD.
DR GO; GO:0005634; C:nucleus; HDA:SGD.
DR GO; GO:0005827; C:polar microtubule; IC: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: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 Gene3D; 1.10.287.600; -; 1.
DR Gene3D; 3.30.1330.20; -; 1.
DR Gene3D; 3.40.50.1440; -; 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; PTHR11588; 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; SSF52490; SSF52490; 1.
DR SUPFAM; SSF55307; SSF55307; 1.
DR PROSITE; PS00227; TUBULIN; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Cytoplasm; Cytoskeleton; GTP-binding; Microtubule;
KW Nucleotide-binding; Reference proteome.
FT CHAIN 1..447
FT /note="Tubulin alpha-1 chain"
FT /id="PRO_0000048239"
FT BINDING 143..149
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000255"
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 104..108
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 TURN 146..148
FT /evidence="ECO:0007829|PDB:4U3J"
FT HELIX 149..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
