TBB1_DROME
ID TBB1_DROME Reviewed; 447 AA.
AC Q24560; Q53YG6; Q9V8V4;
DT 15-NOV-2002, integrated into UniProtKB/Swiss-Prot.
DT 15-NOV-2002, sequence version 2.
DT 03-AUG-2022, entry version 166.
DE RecName: Full=Tubulin beta-1 chain;
DE AltName: Full=Beta-1-tubulin;
GN Name=betaTub56D; ORFNames=CG9277;
OS Drosophila melanogaster (Fruit fly).
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; Ephydroidea;
OC Drosophilidae; Drosophila; Sophophora.
OX NCBI_TaxID=7227;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RX PubMed=3119300; DOI=10.1007/bf00333989;
RA Michiels F., Falkenburg D., Mueller A.M., Hinz U., Otto U., Bellmann R.,
RA Glaetzer K.H., Brand R., Bialojan S., Renkawitz-Pohl R.;
RT "Testis-specific beta 2 tubulins are identical in Drosophila melanogaster
RT and D. hydei but differ from the ubiquitous beta 1 tubulin.";
RL Chromosoma 95:387-395(1987).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Berkeley;
RX PubMed=10731132; DOI=10.1126/science.287.5461.2185;
RA Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D.,
RA Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F.,
RA George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N.,
RA Sutton G.G., Wortman J.R., Yandell M.D., Zhang Q., Chen L.X., Brandon R.C.,
RA Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D., Wan K.H., Doyle C.,
RA Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G., Abril J.F., Agbayani A.,
RA An H.-J., Andrews-Pfannkoch C., Baldwin D., Ballew R.M., Basu A.,
RA Baxendale J., Bayraktaroglu L., Beasley E.M., Beeson K.Y., Benos P.V.,
RA Berman B.P., Bhandari D., Bolshakov S., Borkova D., Botchan M.R., Bouck J.,
RA Brokstein P., Brottier P., Burtis K.C., Busam D.A., Butler H., Cadieu E.,
RA Center A., Chandra I., Cherry J.M., Cawley S., Dahlke C., Davenport L.B.,
RA Davies P., de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I.,
RA Dietz S.M., Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C.,
RA Dunn P., Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S.,
RA Fleischmann W., Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M.,
RA Glasser K., Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M.,
RA Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J., Hostin D.,
RA Houston K.A., Howland T.J., Wei M.-H., Ibegwam C., Jalali M., Kalush F.,
RA Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A., Kimmel B.E., Kodira C.D.,
RA Kraft C.L., Kravitz S., Kulp D., Lai Z., Lasko P., Lei Y., Levitsky A.A.,
RA Li J.H., Li Z., Liang Y., Lin X., Liu X., Mattei B., McIntosh T.C.,
RA McLeod M.P., McPherson D., Merkulov G., Milshina N.V., Mobarry C.,
RA Morris J., Moshrefi A., Mount S.M., Moy M., Murphy B., Murphy L.,
RA Muzny D.M., Nelson D.L., Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R.,
RA Pacleb J.M., Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V.,
RA Reese M.G., Reinert K., Remington K., Saunders R.D.C., Scheeler F.,
RA Shen H., Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T.J.,
RA Spier E., Spradling A.C., Stapleton M., Strong R., Sun E., Svirskas R.,
RA Tector C., Turner R., Venter E., Wang A.H., Wang X., Wang Z.-Y.,
RA Wassarman D.A., Weinstock G.M., Weissenbach J., Williams S.M., Woodage T.,
RA Worley K.C., Wu D., Yang S., Yao Q.A., Ye J., Yeh R.-F., Zaveri J.S.,
RA Zhan M., Zhang G., Zhao Q., Zheng L., Zheng X.H., Zhong F.N., Zhong W.,
RA Zhou X., Zhu S.C., Zhu X., Smith H.O., Gibbs R.A., Myers E.W., Rubin G.M.,
RA Venter J.C.;
RT "The genome sequence of Drosophila melanogaster.";
RL Science 287:2185-2195(2000).
RN [3]
RP GENOME REANNOTATION.
RC STRAIN=Berkeley;
RX PubMed=12537572; DOI=10.1186/gb-2002-3-12-research0083;
RA Misra S., Crosby M.A., Mungall C.J., Matthews B.B., Campbell K.S.,
RA Hradecky P., Huang Y., Kaminker J.S., Millburn G.H., Prochnik S.E.,
RA Smith C.D., Tupy J.L., Whitfield E.J., Bayraktaroglu L., Berman B.P.,
RA Bettencourt B.R., Celniker S.E., de Grey A.D.N.J., Drysdale R.A.,
RA Harris N.L., Richter J., Russo S., Schroeder A.J., Shu S.Q., Stapleton M.,
RA Yamada C., Ashburner M., Gelbart W.M., Rubin G.M., Lewis S.E.;
RT "Annotation of the Drosophila melanogaster euchromatic genome: a systematic
RT review.";
RL Genome Biol. 3:RESEARCH0083.1-RESEARCH0083.22(2002).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=Berkeley; TISSUE=Embryo;
RA Stapleton M., Brokstein P., Hong L., Agbayani A., Carlson J.W., Champe M.,
RA Chavez C., Dorsett V., Dresnek D., Farfan D., Frise E., George R.A.,
RA Gonzalez M., Guarin H., Kronmiller B., Li P.W., Liao G., Miranda A.,
RA Mungall C.J., Nunoo J., Pacleb J.M., Paragas V., Park S., Patel S.,
RA Phouanenavong S., Wan K.H., Yu C., Lewis S.E., Rubin G.M., Celniker S.E.;
RL Submitted (JAN-2003) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-40 AND SER-339, AND
RP IDENTIFICATION BY MASS SPECTROMETRY.
RC TISSUE=Embryo;
RX PubMed=18327897; DOI=10.1021/pr700696a;
RA Zhai B., Villen J., Beausoleil S.A., Mintseris J., Gygi S.P.;
RT "Phosphoproteome analysis of Drosophila melanogaster embryos.";
RL J. Proteome Res. 7:1675-1682(2008).
RN [6]
RP INTERACTION WITH MGR AND VHL.
RX PubMed=22451918; DOI=10.1073/pnas.1108537109;
RA Delgehyr N., Wieland U., Rangone H., Pinson X., Mao G., Dzhindzhev N.S.,
RA McLean D., Riparbelli M.G., Llamazares S., Callaini G., Gonzalez C.,
RA Glover D.M.;
RT "Drosophila Mgr, a Prefoldin subunit cooperating with von Hippel Lindau to
RT regulate tubulin stability.";
RL Proc. Natl. Acad. Sci. U.S.A. 109:5729-5734(2012).
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 (By similarity).
CC {ECO:0000250}.
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. Interacts with mgr and Vhl.
CC {ECO:0000269|PubMed:22451918}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the tubulin family. {ECO:0000305}.
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DR EMBL; M20419; AAA28989.1; -; mRNA.
DR EMBL; AE013599; AAF57555.1; -; Genomic_DNA.
DR EMBL; BT003242; AAO24999.1; -; mRNA.
DR RefSeq; NP_523795.2; NM_079071.3.
DR PDB; 6TIS; X-ray; 2.30 A; B/D=1-447.
DR PDB; 6TIU; X-ray; 3.57 A; B/D=1-447.
DR PDB; 6TIY; X-ray; 2.29 A; B/D=1-447.
DR PDB; 6TIZ; X-ray; 2.20 A; B/D=1-447.
DR PDBsum; 6TIS; -.
DR PDBsum; 6TIU; -.
DR PDBsum; 6TIY; -.
DR PDBsum; 6TIZ; -.
DR AlphaFoldDB; Q24560; -.
DR SMR; Q24560; -.
DR BioGRID; 62900; 89.
DR DIP; DIP-43956N; -.
DR IntAct; Q24560; 3.
DR MINT; Q24560; -.
DR iPTMnet; Q24560; -.
DR PaxDb; Q24560; -.
DR PRIDE; Q24560; -.
DR DNASU; 37238; -.
DR EnsemblMetazoa; FBtr0086536; FBpp0085720; FBgn0284243.
DR GeneID; 37238; -.
DR KEGG; dme:Dmel_CG9277; -.
DR CTD; 37238; -.
DR FlyBase; FBgn0284243; betaTub56D.
DR VEuPathDB; VectorBase:FBgn0284243; -.
DR eggNOG; KOG1375; Eukaryota.
DR GeneTree; ENSGT00940000154394; -.
DR HOGENOM; CLU_015718_1_1_1; -.
DR InParanoid; Q24560; -.
DR OMA; LQFWEII; -.
DR PhylomeDB; Q24560; -.
DR Reactome; R-DME-3371497; HSP90 chaperone cycle for steroid hormone receptors (SHR) in the presence of ligand.
DR Reactome; R-DME-5620924; Intraflagellar transport.
DR Reactome; R-DME-6798695; Neutrophil degranulation.
DR Reactome; R-DME-6807878; COPI-mediated anterograde transport.
DR Reactome; R-DME-6811434; COPI-dependent Golgi-to-ER retrograde traffic.
DR Reactome; R-DME-6811436; COPI-independent Golgi-to-ER retrograde traffic.
DR Reactome; R-DME-983189; Kinesins.
DR SignaLink; Q24560; -.
DR ChiTaRS; betaTub56D; fly.
DR GenomeRNAi; 37238; -.
DR PRO; PR:Q24560; -.
DR Proteomes; UP000000803; Chromosome 2R.
DR Bgee; FBgn0284243; Expressed in cleaving embryo and 43 other tissues.
DR ExpressionAtlas; Q24560; baseline and differential.
DR Genevisible; Q24560; DM.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0005874; C:microtubule; IBA:GO_Central.
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:0000226; P:microtubule cytoskeleton organization; IBA:GO_Central.
DR GO; GO:0007017; P:microtubule-based process; IEA:InterPro.
DR GO; GO:0000278; P:mitotic cell cycle; 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; 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; Cytoplasm; Cytoskeleton; GTP-binding; Microtubule;
KW Nucleotide-binding; Phosphoprotein; Reference proteome.
FT CHAIN 1..447
FT /note="Tubulin beta-1 chain"
FT /id="PRO_0000048276"
FT REGION 427..447
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 428..447
FT /note="Acidic residues"
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 40
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:18327897"
FT MOD_RES 339
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:18327897"
FT CONFLICT 35
FT /note="A -> T (in Ref. 1; AAA28989)"
FT /evidence="ECO:0000305"
FT CONFLICT 163
FT /note="I -> S (in Ref. 1; AAA28989)"
FT /evidence="ECO:0000305"
FT STRAND 3..9
FT /evidence="ECO:0007829|PDB:6TIZ"
FT HELIX 10..27
FT /evidence="ECO:0007829|PDB:6TIZ"
FT STRAND 34..36
FT /evidence="ECO:0007829|PDB:6TIZ"
FT HELIX 42..45
FT /evidence="ECO:0007829|PDB:6TIZ"
FT HELIX 47..49
FT /evidence="ECO:0007829|PDB:6TIZ"
FT STRAND 51..53
FT /evidence="ECO:0007829|PDB:6TIZ"
FT STRAND 55..61
FT /evidence="ECO:0007829|PDB:6TIZ"
FT STRAND 63..69
FT /evidence="ECO:0007829|PDB:6TIZ"
FT HELIX 70..78
FT /evidence="ECO:0007829|PDB:6TIZ"
FT HELIX 82..84
FT /evidence="ECO:0007829|PDB:6TIZ"
FT HELIX 87..89
FT /evidence="ECO:0007829|PDB:6TIZ"
FT STRAND 90..92
FT /evidence="ECO:0007829|PDB:6TIZ"
FT HELIX 101..106
FT /evidence="ECO:0007829|PDB:6TIZ"
FT HELIX 108..125
FT /evidence="ECO:0007829|PDB:6TIZ"
FT STRAND 128..142
FT /evidence="ECO:0007829|PDB:6TIZ"
FT HELIX 143..158
FT /evidence="ECO:0007829|PDB:6TIZ"
FT STRAND 162..170
FT /evidence="ECO:0007829|PDB:6TIZ"
FT HELIX 173..175
FT /evidence="ECO:0007829|PDB:6TIZ"
FT HELIX 181..195
FT /evidence="ECO:0007829|PDB:6TIZ"
FT STRAND 197..203
FT /evidence="ECO:0007829|PDB:6TIZ"
FT HELIX 204..213
FT /evidence="ECO:0007829|PDB:6TIZ"
FT HELIX 222..241
FT /evidence="ECO:0007829|PDB:6TIZ"
FT STRAND 245..247
FT /evidence="ECO:0007829|PDB:6TIZ"
FT HELIX 250..257
FT /evidence="ECO:0007829|PDB:6TIZ"
FT STRAND 265..272
FT /evidence="ECO:0007829|PDB:6TIZ"
FT HELIX 286..291
FT /evidence="ECO:0007829|PDB:6TIZ"
FT HELIX 292..294
FT /evidence="ECO:0007829|PDB:6TIZ"
FT HELIX 296..298
FT /evidence="ECO:0007829|PDB:6TIZ"
FT STRAND 299..302
FT /evidence="ECO:0007829|PDB:6TIZ"
FT HELIX 305..307
FT /evidence="ECO:0007829|PDB:6TIZ"
FT STRAND 310..320
FT /evidence="ECO:0007829|PDB:6TIZ"
FT HELIX 323..336
FT /evidence="ECO:0007829|PDB:6TIZ"
FT HELIX 337..340
FT /evidence="ECO:0007829|PDB:6TIZ"
FT STRAND 349..356
FT /evidence="ECO:0007829|PDB:6TIZ"
FT STRAND 362..371
FT /evidence="ECO:0007829|PDB:6TIZ"
FT HELIX 372..374
FT /evidence="ECO:0007829|PDB:6TIZ"
FT HELIX 375..389
FT /evidence="ECO:0007829|PDB:6TIZ"
FT TURN 390..395
FT /evidence="ECO:0007829|PDB:6TIZ"
FT HELIX 396..399
FT /evidence="ECO:0007829|PDB:6TIZ"
FT TURN 400..402
FT /evidence="ECO:0007829|PDB:6TIZ"
FT HELIX 405..427
FT /evidence="ECO:0007829|PDB:6TIZ"
SQ SEQUENCE 447 AA; 50147 MW; 9E6F66C5C96731DB CRC64;
MREIVHIQAG QCGNQIGAKF WEIISDEHGI DATGAYHGDS DLQLERINVY YNEASGGKYV
PRAVLVDLEP GTMDSVRSGP FGQIFRPDNF VFGQSGAGNN WAKGHYTEGA ELVDSVLDVV
RKEAESCDCL QGFQLTHSLG GGTGSGMGTL LISKIREEYP DRIMNTYSVV PSPKVSDTVV
EPYNATLSVH QLVENTDETY CIDNEALYDI CFRTLKLTTP TYGDLNHLVS LTMSGVTTCL
RFPGQLNADL RKLAVNMVPF PRLHFFMPGF APLTSRGSQQ YRALTVPELT QQMFDAKNMM
AACDPRHGRY LTVAAIFRGR MSMKEVDEQM LNIQNKNSSY FVEWIPNNVK TAVCDIPPRG
LKMSATFIGN STAIQELFKR ISEQFTAMFR RKAFLHWYTG EGMDEMEFTE AESNMNDLVS
EYQQYQEATA DEDAEFEEEQ EAEVDEN
