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Database: UniProt
Entry: P09733
LinkDB: P09733
Original site: P09733 
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   07-OCT-2020, entry version 187.
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;
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}.
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   SMR; P09733; -.
DR   BioGRID; 35056; 150.
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   EuPathDB; FungiDB:YML085C; -.
DR   SGD; S000004550; TUB1.
DR   eggNOG; KOG1376; Eukaryota.
DR   GeneTree; ENSGT00940000164588; -.
DR   HOGENOM; CLU_015718_0_0_1; -.
DR   InParanoid; P09733; -.
DR   KO; K07374; -.
DR   OMA; VDNEACY; -.
DR   Reactome; R-SCE-114608; Platelet degranulation.
DR   Reactome; R-SCE-5617833; Cilium Assembly.
DR   Reactome; R-SCE-5626467; RHO GTPases activate IQGAPs.
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:0003924; F:GTPase activity; IEA:InterPro.
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; IBA:GO_Central.
DR   GO; GO:0007017; P:microtubule-based process; IBA:GO_Central.
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; 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; 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   NP_BIND         143..149
FT                   /note="GTP"
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:0000244|PDB:4U3J"
FT   HELIX           10..27
FT                   /evidence="ECO:0000244|PDB:4U3J"
FT   STRAND          34..36
FT                   /evidence="ECO:0000244|PDB:4U3J"
FT   STRAND          47..50
FT                   /evidence="ECO:0000244|PDB:4U3J"
FT   TURN            51..53
FT                   /evidence="ECO:0000244|PDB:4U3J"
FT   STRAND          54..56
FT                   /evidence="ECO:0000244|PDB:4U3J"
FT   STRAND          58..60
FT                   /evidence="ECO:0000244|PDB:4U3J"
FT   STRAND          62..64
FT                   /evidence="ECO:0000244|PDB:4U3J"
FT   STRAND          66..72
FT                   /evidence="ECO:0000244|PDB:4U3J"
FT   HELIX           73..81
FT                   /evidence="ECO:0000244|PDB:4U3J"
FT   TURN            83..87
FT                   /evidence="ECO:0000244|PDB:4U3J"
FT   TURN            90..92
FT                   /evidence="ECO:0000244|PDB:4U3J"
FT   STRAND          93..95
FT                   /evidence="ECO:0000244|PDB:4U3J"
FT   HELIX           104..108
FT                   /evidence="ECO:0000244|PDB:4U3J"
FT   HELIX           112..127
FT                   /evidence="ECO:0000244|PDB:4U3J"
FT   STRAND          135..145
FT                   /evidence="ECO:0000244|PDB:4U3J"
FT   TURN            146..148
FT                   /evidence="ECO:0000244|PDB:4U3J"
FT   HELIX           149..161
FT                   /evidence="ECO:0000244|PDB:4U3J"
FT   TURN            162..164
FT                   /evidence="ECO:0000244|PDB:4U3J"
FT   STRAND          165..173
FT                   /evidence="ECO:0000244|PDB:4U3J"
FT   HELIX           176..178
FT                   /evidence="ECO:0000244|PDB:4U3J"
FT   HELIX           184..195
FT                   /evidence="ECO:0000244|PDB:4U3J"
FT   STRAND          196..198
FT                   /evidence="ECO:0000244|PDB:4U3J"
FT   STRAND          200..206
FT                   /evidence="ECO:0000244|PDB:4U3J"
FT   HELIX           207..216
FT                   /evidence="ECO:0000244|PDB:4U3J"
FT   HELIX           225..239
FT                   /evidence="ECO:0000244|PDB:4U3J"
FT   HELIX           241..244
FT                   /evidence="ECO:0000244|PDB:4U3J"
FT   HELIX           253..260
FT                   /evidence="ECO:0000244|PDB:4U3J"
FT   STRAND          262..265
FT                   /evidence="ECO:0000244|PDB:4FFB"
FT   STRAND          270..274
FT                   /evidence="ECO:0000244|PDB:4U3J"
FT   HELIX           289..295
FT                   /evidence="ECO:0000244|PDB:4U3J"
FT   HELIX           299..301
FT                   /evidence="ECO:0000244|PDB:4U3J"
FT   STRAND          302..306
FT                   /evidence="ECO:0000244|PDB:4U3J"
FT   STRAND          313..323
FT                   /evidence="ECO:0000244|PDB:4U3J"
FT   HELIX           326..338
FT                   /evidence="ECO:0000244|PDB:4U3J"
FT   STRAND          352..357
FT                   /evidence="ECO:0000244|PDB:4U3J"
FT   STRAND          365..369
FT                   /evidence="ECO:0000244|PDB:4U3J"
FT   STRAND          373..382
FT                   /evidence="ECO:0000244|PDB:4U3J"
FT   HELIX           383..385
FT                   /evidence="ECO:0000244|PDB:4U3J"
FT   HELIX           386..400
FT                   /evidence="ECO:0000244|PDB:4U3J"
FT   TURN            401..405
FT                   /evidence="ECO:0000244|PDB:4U3J"
FT   HELIX           406..410
FT                   /evidence="ECO:0000244|PDB:4U3J"
FT   TURN            411..413
FT                   /evidence="ECO:0000244|PDB:4U3J"
FT   HELIX           417..436
FT                   /evidence="ECO:0000244|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
//
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