ID   TBB5_HUMAN              Reviewed;         444 AA.
AC   P07437; P05218; Q8WUC1; Q9CY33;
DT   13-AUG-1987, integrated into UniProtKB/Swiss-Prot.
DT   21-DEC-2004, sequence version 2.
DT   25-JAN-2012, entry version 144.
DE   RecName: Full=Tubulin beta chain;
DE   AltName: Full=Tubulin beta-5 chain;
GN   Name=TUBB; Synonyms=TUBB5; ORFNames=OK/SW-cl.56;
OS   Homo sapiens (Human).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
OC   Catarrhini; Hominidae; Homo.
OX   NCBI_TaxID=9606;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   MEDLINE=83232883; PubMed=6688039; DOI=10.1016/0092-8674(83)90429-4;
RA   Lee M.G.-S., Lewis S.A., Wilde C.D., Cowan N.J.;
RT   "Evolutionary history of a multigene family: an expressed human beta-
RT   tubulin gene and three processed pseudogenes.";
RL   Cell 33:477-487(1983).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   MEDLINE=83244582; PubMed=6865944;
RA   Hall J.L., Dudley L., Dobner P.R., Lewis S.A., Cowan N.J.;
RT   "Identification of two human beta-tubulin isotypes.";
RL   Mol. Cell. Biol. 3:854-862(1983).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   TISSUE=Retina;
RX   MEDLINE=21395848; PubMed=11504633; DOI=10.1016/S0968-0896(01)00103-1;
RA   Crabtree D.V., Ojima I., Geng X., Adler A.J.;
RT   "Tubulins in the primate retina: evidence that xanthophylls may be
RT   endogenous ligands for the paclitaxel-binding site.";
RL   Bioorg. Med. Chem. 9:1967-1976(2001).
RN   [4]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Brain;
RA   Yu W., Gibbs R.A.;
RL   Submitted (JUN-1998) to the EMBL/GenBank/DDBJ databases.
RN   [5]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA   Shiina S., Tamiya G., Oka A., Inoko H.;
RT   "Homo sapiens 2,229,817bp genomic DNA of 6p21.3 HLA class I region.";
RL   Submitted (SEP-1999) to the EMBL/GenBank/DDBJ databases.
RN   [6]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA   Shiina T., Ota M., Katsuyama Y., Hashimoto N., Inoko H.;
RT   "Genome diversity in HLA: a new strategy for detection of genetic
RT   polymorphisms in expressed genes within the HLA class III and class I
RT   regions.";
RL   Submitted (JUL-2002) to the EMBL/GenBank/DDBJ databases.
RN   [7]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Colon adenocarcinoma;
RA   Shichijo S., Itoh K.;
RT   "Identification of immuno-peptidmics that are recognized by tumor-
RT   reactive CTL generated from TIL of colon cancer patients.";
RL   Submitted (MAY-2001) to the EMBL/GenBank/DDBJ databases.
RN   [8]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Brain, Eye, Lung, Muscle, and Placenta;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [9]
RP   PROTEIN SEQUENCE OF 1-19; 47-77; 104-174; 242-276; 283-297; 310-359
RP   AND 363-390, METHYLATION AT ARG-318, AND MASS SPECTROMETRY.
RC   TISSUE=Foreskin fibroblast, and Mammary carcinoma;
RA   Bienvenut W.V., Campbell A., Ozanne B.W., Lourenco F., Olson M.F.;
RL   Submitted (DEC-2009) to UniProtKB.
RN   [10]
RP   PROTEIN SEQUENCE OF 3-19; 47-58; 63-77; 104-121; 163-174; 242-251;
RP   253-276; 283-297; 310-318; 325-336 AND 381-390, AND MASS SPECTROMETRY.
RC   TISSUE=Brain, Cajal-Retzius cell, and Fetal brain cortex;
RA   Lubec G., Vishwanath V., Chen W.-Q., Sun Y.;
RL   Submitted (DEC-2008) to UniProtKB.
RN   [11]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-36, AND MASS
RP   SPECTROMETRY.
RX   PubMed=15592455; DOI=10.1038/nbt1046;
RA   Rush J., Moritz A., Lee K.A., Guo A., Goss V.L., Spek E.J., Zhang H.,
RA   Zha X.-M., Polakiewicz R.D., Comb M.J.;
RT   "Immunoaffinity profiling of tyrosine phosphorylation in cancer
RT   cells.";
RL   Nat. Biotechnol. 23:94-101(2005).
RN   [12]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-48; THR-55 AND THR-429,
RP   AND MASS SPECTROMETRY.
RC   TISSUE=Cervix carcinoma;
RX   PubMed=19007248; DOI=10.1021/ac801708p;
RA   Wang B., Malik R., Nigg E.A., Korner R.;
RT   "Evaluation of the low-specificity protease elastase for large-scale
RT   phosphoproteome analysis.";
RL   Anal. Chem. 80:9526-9533(2008).
RN   [13]
RP   UBIQUITINATION [LARGE SCALE ANALYSIS] AT LYS-58 AND LYS-324, AND MASS
RP   SPECTROMETRY.
RX   PubMed=18781797; DOI=10.1021/pr800468j;
RA   Meierhofer D., Wang X., Huang L., Kaiser P.;
RT   "Quantitative analysis of global ubiquitination in HeLa cells by mass
RT   spectrometry.";
RL   J. Proteome Res. 7:4566-4576(2008).
RN   [14]
RP   GLYCYLATION.
RX   PubMed=19524510; DOI=10.1016/j.cell.2009.05.020;
RA   Rogowski K., Juge F., van Dijk J., Wloga D., Strub J.-M.,
RA   Levilliers N., Thomas D., Bre M.-H., Van Dorsselaer A., Gaertig J.,
RA   Janke C.;
RT   "Evolutionary divergence of enzymatic mechanisms for posttranslational
RT   polyglycylation.";
RL   Cell 137:1076-1087(2009).
RN   [15]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-340, AND MASS
RP   SPECTROMETRY.
RC   TISSUE=Mammary epithelium;
RX   PubMed=19534553; DOI=10.1021/pr900044c;
RA   Heibeck T.H., Ding S.-J., Opresko L.K., Zhao R., Schepmoes A.A.,
RA   Yang F., Tolmachev A.V., Monroe M.E., Camp D.G. II, Smith R.D.,
RA   Wiley H.S., Qian W.-J.;
RT   "An extensive survey of tyrosine phosphorylation revealing new sites
RT   in human mammary epithelial cells.";
RL   J. Proteome Res. 8:3852-3861(2009).
RN   [16]
RP   ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-58, AND MASS SPECTROMETRY.
RX   PubMed=19608861; DOI=10.1126/science.1175371;
RA   Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T.,
RA   Olsen J.V., Mann M.;
RT   "Lysine acetylation targets protein complexes and co-regulates major
RT   cellular functions.";
RL   Science 325:834-840(2009).
RN   [17]
RP   TISSUE SPECIFICITY.
RX   PubMed=20191564; DOI=10.1002/cm.20436;
RA   Leandro-Garcia L.J., Leskela S., Landa I., Montero-Conde C.,
RA   Lopez-Jimenez E., Leton R., Cascon A., Robledo M.,
RA   Rodriguez-Antona C.;
RT   "Tumoral and tissue-specific expression of the major human beta-
RT   tubulin isotypes.";
RL   Cytoskeleton 67:214-223(2010).
RN   [18]
RP   INTERACTION WITH PIFO.
RX   PubMed=20643351; DOI=10.1016/j.devcel.2010.06.005;
RA   Kinzel D., Boldt K., Davis E.E., Burtscher I., Trumbach D., Diplas B.,
RA   Attie-Bitach T., Wurst W., Katsanis N., Ueffing M., Lickert H.;
RT   "Pitchfork regulates primary cilia disassembly and left-right
RT   asymmetry.";
RL   Dev. Cell 19:66-77(2010).
RN   [19]
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX   PubMed=21269460; DOI=10.1186/1752-0509-5-17;
RA   Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P.,
RA   Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.;
RT   "Initial characterization of the human central proteome.";
RL   BMC Syst. Biol. 5:17-17(2011).
CC   -!- FUNCTION: Tubulin is the major constituent of microtubules. It
CC       binds two moles of GTP, one at an exchangeable site on the beta
CC       chain and one at a non-exchangeable site on the alpha-chain.
CC   -!- SUBUNIT: Dimer of alpha and beta chains. May interact with RNABP10
CC       (By similarity). Interacts with PIFO/C1orf88.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton.
CC   -!- TISSUE SPECIFICITY: Ubiquitously expressed with highest levels in
CC       spleen, thymus and immature brain.
CC   -!- DOMAIN: The highly acidic C-terminal region may bind cations such
CC       as calcium.
CC   -!- PTM: Some glutamate residues at the C-terminus are
CC       polyglutamylated. This modification occurs exclusively on
CC       glutamate residues and results in polyglutamate chains on the
CC       gamma-carboxyl group. Also monoglycylated but not polyglycylated
CC       due to the absence of functional TTLL10 in human. Monoglycylation
CC       is mainly limited to tubulin incorporated into axonemes (cilia and
CC       flagella) whereas glutamylation is prevalent in neuronal cells,
CC       centrioles, axonemes, and the mitotic spindle. Both modifications
CC       can coexist on the same protein on adjacent residues, and lowering
CC       glycylation levels increases polyglutamylation, and reciprocally.
CC       The precise function of such modifications is still unclear but
CC       they regulate the assembly and dynamics of axonemal microtubules
CC       (Probable).
CC   -!- SIMILARITY: Belongs to the tubulin family.
CC   -!- WEB RESOURCE: Name=Wikipedia; Note=Tubulin entry;
CC       URL="http://en.wikipedia.org/wiki/Tubulin";
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DR   EMBL; J00314; AAB59507.1; -; Genomic_DNA.
DR   EMBL; AF141349; AAD33873.1; -; mRNA.
DR   EMBL; AF070561; AAC28642.1; -; mRNA.
DR   EMBL; AF070593; AAC28650.1; -; mRNA.
DR   EMBL; AF070600; AAC28654.1; -; mRNA.
DR   EMBL; BA000025; BAB63321.1; -; Genomic_DNA.
DR   EMBL; AB088100; BAC54932.1; -; Genomic_DNA.
DR   EMBL; AB062393; BAB93480.1; -; mRNA.
DR   EMBL; BC001938; AAH01938.1; -; mRNA.
DR   EMBL; BC002347; AAH02347.1; -; mRNA.
DR   EMBL; BC005838; AAH05838.1; -; mRNA.
DR   EMBL; BC007605; AAH07605.1; -; mRNA.
DR   EMBL; BC013374; AAH13374.1; -; mRNA.
DR   EMBL; BC019924; AAH19924.1; -; mRNA.
DR   EMBL; BC020946; AAH20946.1; -; mRNA.
DR   EMBL; BC021909; AAH21909.1; -; mRNA.
DR   EMBL; BC070326; AAH70326.1; -; mRNA.
DR   IPI; IPI01019113; -.
DR   PIR; A26561; A26561.
DR   RefSeq; NP_821133.1; NM_178014.2.
DR   UniGene; Hs.636480; -.
DR   UniGene; Hs.706187; -.
DR   UniGene; Hs.714425; -.
DR   ProteinModelPortal; P07437; -.
DR   SMR; P07437; 2-427.
DR   IntAct; P07437; 28.
DR   MINT; MINT-1146393; -.
DR   STRING; P07437; -.
DR   PhosphoSite; P07437; -.
DR   DMDM; 56757569; -.
DR   SWISS-2DPAGE; P07437; -.
DR   Cornea-2DPAGE; P07437; -.
DR   OGP; P07437; -.
DR   REPRODUCTION-2DPAGE; P07437; -.
DR   UCD-2DPAGE; P07437; -.
DR   PRIDE; P07437; -.
DR   Ensembl; ENST00000327892; ENSP00000339001; ENSG00000196230.
DR   Ensembl; ENST00000383564; ENSP00000373058; ENSG00000183311.
DR   Ensembl; ENST00000419792; ENSP00000401317; ENSG00000235067.
DR   Ensembl; ENST00000421473; ENSP00000399155; ENSG00000224156.
DR   Ensembl; ENST00000422650; ENSP00000400663; ENSG00000229684.
DR   Ensembl; ENST00000422674; ENSP00000406811; ENSG00000227739.
DR   Ensembl; ENST00000432462; ENSP00000410829; ENSG00000232421.
DR   Ensembl; ENST00000436628; ENSP00000410071; ENSG00000232575.
DR   GeneID; 203068; -.
DR   KEGG; hsa:203068; -.
DR   UCSC; uc003nrl.1; human.
DR   CTD; 203068; -.
DR   GeneCards; GC06P030687; -.
DR   H-InvDB; HIX0057935; -.
DR   HGNC; HGNC:20778; TUBB.
DR   HPA; CAB005417; -.
DR   HPA; CAB012406; -.
DR   MIM; 191130; gene.
DR   neXtProt; NX_P07437; -.
DR   PharmGKB; PA358; -.
DR   eggNOG; maNOG18649; -.
DR   HOVERGEN; HBG000089; -.
DR   InParanoid; P07437; -.
DR   OMA; RYQGEND; -.
DR   OrthoDB; EOG4DFPNJ; -.
DR   PhylomeDB; P07437; -.
DR   Reactome; REACT_152; Cell Cycle, Mitotic.
DR   DrugBank; DB01394; Colchicine.
DR   DrugBank; DB00570; Vinblastine.
DR   DrugBank; DB00541; Vincristine.
DR   DrugBank; DB00361; Vinorelbine.
DR   NextBio; 90324; -.
DR   CleanEx; HS_TUBB; -.
DR   Genevestigator; P07437; -.
DR   GermOnline; ENSG00000196230; Homo sapiens.
DR   GO; GO:0044297; C:cell body; IDA:DFLAT.
DR   GO; GO:0005829; C:cytosol; TAS:Reactome.
DR   GO; GO:0005874; C:microtubule; TAS:BHF-UCL.
DR   GO; GO:0005641; C:nuclear envelope lumen; IDA:DFLAT.
DR   GO; GO:0005525; F:GTP binding; IEA:UniProtKB-KW.
DR   GO; GO:0003924; F:GTPase activity; IEA:InterPro.
DR   GO; GO:0042288; F:MHC class I protein binding; IDA:UniProtKB.
DR   GO; GO:0051301; P:cell division; TAS:BHF-UCL.
DR   GO; GO:0030705; P:cytoskeleton-dependent intracellular transport; TAS:BHF-UCL.
DR   GO; GO:0000086; P:G2/M transition of mitotic cell cycle; TAS:Reactome.
DR   GO; GO:0007018; P:microtubule-based movement; IEA:InterPro.
DR   GO; GO:0042267; P:natural killer cell mediated cytotoxicity; NAS:UniProtKB.
DR   GO; GO:0051258; P:protein polymerization; IEA:InterPro.
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; IPR023123; Tubulin_C.
DR   InterPro; IPR017975; Tubulin_CS.
DR   InterPro; IPR003008; Tubulin_FtsZ_GTPase.
DR   Gene3D; G3DSA:3.30.1330.20; Tubulin/FtsZ_2-layer-sand-dom; 1.
DR   Gene3D; G3DSA:1.10.287.600; Tubulin_C; 1.
DR   Gene3D; G3DSA:3.40.50.1440; Tubulin_FtsZ; 1.
DR   KO; K07375; -.
DR   PANTHER; PTHR11588; Tubulin; 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; SSF55307; Tub_FtsZ_C; 1.
DR   SUPFAM; SSF52490; Tubulin_FtsZ; 1.
DR   PROSITE; PS00227; TUBULIN; 1.
DR   PROSITE; PS00228; TUBULIN_B_AUTOREG; 1.
PE   1: Evidence at protein level;
KW   Acetylation; Complete proteome; Cytoplasm; Cytoskeleton;
KW   Direct protein sequencing; GTP-binding; Isopeptide bond; Methylation;
KW   Microtubule; Nucleotide-binding; Phosphoprotein; Reference proteome;
KW   Ubl conjugation.
FT   CHAIN         1    444       Tubulin beta chain.
FT                                /FTId=PRO_0000048243.
FT   NP_BIND     140    146       GTP (Potential).
FT   MOD_RES      36     36       Phosphotyrosine.
FT   MOD_RES      48     48       Phosphoserine.
FT   MOD_RES      55     55       Phosphothreonine.
FT   MOD_RES      58     58       N6-acetyllysine.
FT   MOD_RES     172    172       Phosphoserine; by CDK1 (By similarity).
FT   MOD_RES     318    318       Omega-N-methylarginine.
FT   MOD_RES     340    340       Phosphotyrosine.
FT   MOD_RES     429    429       Phosphothreonine.
FT   CROSSLNK     58     58       Glycyl lysine isopeptide (Lys-Gly)
FT                                (interchain with G-Cter in ubiquitin).
FT   CROSSLNK    324    324       Glycyl lysine isopeptide (Lys-Gly)
FT                                (interchain with G-Cter in ubiquitin).
FT   CONFLICT    216    216       K -> R (in Ref. 1 and 2).
FT   CONFLICT    231    231       A -> G (in Ref. 1 and 2).
FT   CONFLICT    234    235       SG -> EC (in Ref. 1 and 2).
FT   CONFLICT    288    288       E -> D (in Ref. 1 and 2).
FT   CONFLICT    298    298       N -> D (in Ref. 8; AAH20946).
SQ   SEQUENCE   444 AA;  49671 MW;  1E6CD0A36773A103 CRC64;
     MREIVHIQAG QCGNQIGAKF WEVISDEHGI DPTGTYHGDS DLQLDRISVY YNEATGGKYV
     PRAILVDLEP GTMDSVRSGP FGQIFRPDNF VFGQSGAGNN WAKGHYTEGA ELVDSVLDVV
     RKEAESCDCL QGFQLTHSLG GGTGSGMGTL LISKIREEYP DRIMNTFSVV PSPKVSDTVV
     EPYNATLSVH QLVENTDETY CIDNEALYDI CFRTLKLTTP TYGDLNHLVS ATMSGVTTCL
     RFPGQLNADL RKLAVNMVPF PRLHFFMPGF APLTSRGSQQ YRALTVPELT QQVFDAKNMM
     AACDPRHGRY LTVAAVFRGR MSMKEVDEQM LNVQNKNSSY FVEWIPNNVK TAVCDIPPRG
     LKMAVTFIGN STAIQELFKR ISEQFTAMFR RKAFLHWYTG EGMDEMEFTE AESNMNDLVS
     EYQQYQDATA EEEEDFGEEA EEEA
//