TBB5_MOUSE
ID TBB5_MOUSE Reviewed; 444 AA.
AC P99024; B1B178; P05218; Q3TFB6; Q3THH9; Q3TIL1; Q3UAV4; Q3UF52; Q8WUC1;
AC Q9CY33;
DT 13-AUG-1987, integrated into UniProtKB/Swiss-Prot.
DT 13-AUG-1987, sequence version 1.
DT 03-AUG-2022, entry version 173.
DE RecName: Full=Tubulin beta-5 chain;
GN Name=Tubb5;
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RX PubMed=3782288; DOI=10.1083/jcb.103.5.1903;
RA Wang D., Villasante A., Lewis S.A., Cowan N.J.;
RT "The mammalian beta-tubulin repertoire: hematopoietic expression of a
RT novel, heterologous beta-tubulin isotype.";
RL J. Cell Biol. 103:1903-1910(1986).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J, and DBA/2J;
RC TISSUE=Bone marrow, Embryo, Kidney, Liver, Pituitary, Placenta,
RC Spinal ganglion, Spleen, Sympathetic ganglion, and Thymus;
RX PubMed=16141072; DOI=10.1126/science.1112014;
RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT "The transcriptional landscape of the mammalian genome.";
RL Science 309:1559-1563(2005).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=C57BL/6J;
RX PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., She X.,
RA Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., Kapustin Y.,
RA Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., Zhou S.,
RA Teague B., Potamousis K., Churas C., Place M., Herschleb J., Runnheim R.,
RA Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., Lindblad-Toh K.,
RA Eichler E.E., Ponting C.P.;
RT "Lineage-specific biology revealed by a finished genome assembly of the
RT mouse.";
RL PLoS Biol. 7:E1000112-E1000112(2009).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
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 project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [5]
RP PROTEIN SEQUENCE OF 3-19; 63-121; 163-174; 217-241; 242-276; 283-297;
RP 310-318; 321-359 AND 381-390, AND IDENTIFICATION BY MASS SPECTROMETRY.
RC STRAIN=C57BL/6J; TISSUE=Brain, and Hippocampus;
RA Lubec G., Kang S.U., Klug S., Yang J.W., Zigmond M.;
RL Submitted (JUL-2007) to UniProtKB.
RN [6]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 325-444.
RX PubMed=3839797; DOI=10.1083/jcb.101.3.852;
RA Lewis S.A., Lee M.G.-S., Cowan N.J.;
RT "Five mouse tubulin isotypes and their regulated expression during
RT development.";
RL J. Cell Biol. 101:852-861(1985).
RN [7]
RP GLUTAMYLATION.
RX PubMed=15890843; DOI=10.1126/science.1113010;
RA Janke C., Rogowski K., Wloga D., Regnard C., Kajava A.V., Strub J.-M.,
RA Temurak N., van Dijk J., Boucher D., van Dorsselaer A., Suryavanshi S.,
RA Gaertig J., Edde B.;
RT "Tubulin polyglutamylase enzymes are members of the TTL domain protein
RT family.";
RL Science 308:1758-1762(2005).
RN [8]
RP PHOSPHORYLATION AT SER-172 BY CDK1, AND MUTAGENESIS OF SER-172.
RX PubMed=16371510; DOI=10.1091/mbc.e05-07-0621;
RA Fourest-Lieuvin A., Peris L., Gache V., Garcia-Saez I., Juillan-Binard C.,
RA Lantez V., Job D.;
RT "Microtubule regulation in mitosis: tubulin phosphorylation by the cyclin-
RT dependent kinase Cdk1.";
RL Mol. Biol. Cell 17:1041-1050(2006).
RN [9]
RP INTERACTION WITH RANBP10.
RX PubMed=18347012; DOI=10.1074/jbc.m709397200;
RA Schulze H., Dose M., Korpal M., Meyer I., Italiano J.E. Jr.,
RA Shivdasani R.A.;
RT "RanBP10 is a cytoplasmic guanine nucleotide exchange factor that modulates
RT noncentrosomal microtubules.";
RL J. Biol. Chem. 283:14109-14119(2008).
RN [10]
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., Levilliers N.,
RA Thomas D., Bre M.-H., Van Dorsselaer A., Gaertig J., Janke C.;
RT "Evolutionary divergence of enzymatic mechanisms for posttranslational
RT polyglycylation.";
RL Cell 137:1076-1087(2009).
RN [11]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-40, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain, Brown adipose tissue, Heart, Kidney, Liver, Lung, Pancreas,
RC Spleen, and Testis;
RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL Cell 143:1174-1189(2010).
RN [12]
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 asymmetry.";
RL Dev. Cell 19:66-77(2010).
RN [13]
RP DISRUPTION PHENOTYPE, AND TISSUE SPECIFICITY.
RX PubMed=23246003; DOI=10.1016/j.celrep.2012.11.017;
RA Breuss M., Heng J.I., Poirier K., Tian G., Jaglin X.H., Qu Z., Braun A.,
RA Gstrein T., Ngo L., Haas M., Bahi-Buisson N., Moutard M.L., Passemard S.,
RA Verloes A., Gressens P., Xie Y., Robson K.J., Rani D.S., Thangaraj K.,
RA Clausen T., Chelly J., Cowan N.J., Keays D.A.;
RT "Mutations in the beta-tubulin gene TUBB5 cause microcephaly with
RT structural brain abnormalities.";
RL Cell Rep. 2:1554-1562(2012).
RN [14]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-58, SUCCINYLATION [LARGE SCALE
RP ANALYSIS] AT LYS-58, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE
RP ANALYSIS].
RC TISSUE=Embryonic fibroblast;
RX PubMed=23806337; DOI=10.1016/j.molcel.2013.06.001;
RA Park J., Chen Y., Tishkoff D.X., Peng C., Tan M., Dai L., Xie Z., Zhang Y.,
RA Zwaans B.M., Skinner M.E., Lombard D.B., Zhao Y.;
RT "SIRT5-mediated lysine desuccinylation impacts diverse metabolic
RT pathways.";
RL Mol. Cell 50:919-930(2013).
RN [15]
RP SUBCELLULAR LOCATION, AND TISSUE SPECIFICITY.
RX PubMed=26637975; DOI=10.1016/j.ajhg.2015.10.014;
RA Isrie M., Breuss M., Tian G., Hansen A.H., Cristofoli F., Morandell J.,
RA Kupchinsky Z.A., Sifrim A., Rodriguez-Rodriguez C.M., Dapena E.P.,
RA Doonanco K., Leonard N., Tinsa F., Moortgat S., Ulucan H., Koparir E.,
RA Karaca E., Katsanis N., Marton V., Vermeesch J.R., Davis E.E., Cowan N.J.,
RA Keays D.A., Van Esch H.;
RT "Mutations in Either TUBB or MAPRE2 Cause Circumferential Skin Creases
RT Kunze Type.";
RL Am. J. Hum. Genet. 97:790-800(2015).
RN [16]
RP GLYCYLATION, AND GLUTAMYLATION.
RX PubMed=23897886; DOI=10.1083/jcb.201305041;
RA Bosch Grau M., Gonzalez Curto G., Rocha C., Magiera M.M., Marques Sousa P.,
RA Giordano T., Spassky N., Janke C.;
RT "Tubulin glycylases and glutamylases have distinct functions in
RT stabilization and motility of ependymal cilia.";
RL J. Cell Biol. 202:441-451(2013).
RN [17]
RP INTERACTION WITH CFAP157.
RX PubMed=27965440; DOI=10.1242/dev.139626;
RA Weidemann M., Schuster-Gossler K., Stauber M., Wrede C., Hegermann J.,
RA Ott T., Boldt K., Beyer T., Serth K., Kremmer E., Blum M., Ueffing M.,
RA Gossler A.;
RT "CFAP157 is a murine downstream effector of FOXJ1 that is specifically
RT required for flagellum morphogenesis and sperm motility.";
RL Development 143:4736-4748(2016).
RN [18]
RP GLYCYLATION.
RX PubMed=33414192; DOI=10.1126/science.abd4914;
RA Gadadhar S., Alvarez Viar G., Hansen J.N., Gong A., Kostarev A.,
RA Ialy-Radio C., Leboucher S., Whitfield M., Ziyyat A., Toure A., Alvarez L.,
RA Pigino G., Janke C.;
RT "Tubulin glycylation controls axonemal dynein activity, flagellar beat, and
RT male fertility.";
RL Science 371:0-0(2021).
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: Heterodimer of alpha and beta chains (By similarity). A
CC typical microtubule is a hollow water-filled tube with an outer
CC diameter of 25 nm and an inner diameter of 15 nM. Alpha-beta
CC heterodimers associate head-to-tail to form protofilaments running
CC lengthwise along the microtubule wall with the beta-tubulin subunit
CC facing the microtubule plus end conferring a structural polarity.
CC Microtubules usually have 13 protofilaments but different protofilament
CC numbers can be found in some organisms and specialized cells. Interacts
CC with PIFO (PubMed:20643351). Interacts with DIAPH1 (By similarity).
CC Interacts with MX1 (By similarity). May interact with RNABP10
CC (PubMed:18347012). Interacts with CFAP157 (PubMed:27965440). Nascent
CC tubulin polypeptide interacts (via beta-tubulin MREI motif) with
CC TTC5/STRAP; this interaction results in tubulin mRNA-targeted
CC degradation (By similarity). {ECO:0000250|UniProtKB:P07437,
CC ECO:0000250|UniProtKB:P69893, ECO:0000269|PubMed:18347012,
CC ECO:0000269|PubMed:20643351, ECO:0000269|PubMed:27965440}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton
CC {ECO:0000269|PubMed:26637975}.
CC -!- TISSUE SPECIFICITY: Ubiquitously expressed with highest levels in
CC spleen, thymus and immature brain. Expressed in embryonic brain,
CC including throughout the developing cortex and in the subventricular
CC zone. Also found in radial glial cells, intermediate progenitors,
CC migrating neurons and postmitotic neurons (PubMed:23246003). Expressed
CC in skin and developing hair follicle (PubMed:26637975).
CC {ECO:0000269|PubMed:23246003, ECO:0000269|PubMed:26637975}.
CC -!- DOMAIN: The MREI motif is common among all beta-tubulin isoforms and
CC may be critical for tubulin autoregulation.
CC {ECO:0000250|UniProtKB:P07437}.
CC -!- PTM: Some glutamate residues at the C-terminus are polyglycylated,
CC resulting in polyglycine chains on the gamma-carboxyl group.
CC Glycylation is mainly limited to tubulin incorporated into axonemes
CC (cilia and flagella) whereas glutamylation is prevalent in neuronal
CC cells, centrioles, axonemes, and the mitotic spindle. Both
CC modifications can coexist on the same protein on adjacent residues, and
CC lowering polyglycylation levels increases polyglutamylation, and
CC reciprocally. Cilia and flagella glycylation is required for their
CC stability and maintenance. Flagella glycylation controls sperm motility
CC (PubMed:33414192). {ECO:0000269|PubMed:19524510,
CC ECO:0000269|PubMed:23897886, ECO:0000269|PubMed:33414192}.
CC -!- PTM: Some glutamate residues at the C-terminus are polyglutamylated,
CC resulting in polyglutamate chains on the gamma-carboxyl group
CC (PubMed:15890843). Polyglutamylation plays a key role in microtubule
CC severing by spastin (SPAST). SPAST preferentially recognizes and acts
CC on microtubules decorated with short polyglutamate tails: severing
CC activity by SPAST increases as the number of glutamates per tubulin
CC rises from one to eight, but decreases beyond this glutamylation
CC threshold (By similarity). Glutamylation is also involved in cilia
CC motility (PubMed:23897886). {ECO:0000250|UniProtKB:Q71U36,
CC ECO:0000269|PubMed:15890843, ECO:0000269|PubMed:23897886}.
CC -!- PTM: Phosphorylated on Ser-172 by CDK1 during the cell cycle, from
CC metaphase to telophase, but not in interphase. This phosphorylation
CC inhibits tubulin incorporation into microtubules.
CC {ECO:0000269|PubMed:16371510}.
CC -!- DISRUPTION PHENOTYPE: Results in a perturbation of the cell cycle of
CC neurogenic progenitors as well as an alteration in the position of
CC migrating neurons. There is a decrease in neurons in the cortical plate
CC and an accumulation of cells within the ventricular and intermediate
CC zones. {ECO:0000269|PubMed:23246003}.
CC -!- SIMILARITY: Belongs to the tubulin family. {ECO:0000305}.
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DR EMBL; X04663; CAA28369.1; -; mRNA.
DR EMBL; AK010960; BAB27292.1; -; mRNA.
DR EMBL; AK011263; BAB27504.1; -; mRNA.
DR EMBL; AK051164; BAC34541.1; -; mRNA.
DR EMBL; AK051393; BAC34623.1; -; mRNA.
DR EMBL; AK083327; BAC38866.1; -; mRNA.
DR EMBL; AK146567; BAE27265.1; -; mRNA.
DR EMBL; AK148978; BAE28709.1; -; mRNA.
DR EMBL; AK151215; BAE30210.1; -; mRNA.
DR EMBL; AK151670; BAE30596.1; -; mRNA.
DR EMBL; AK160225; BAE35700.1; -; mRNA.
DR EMBL; AK161575; BAE36471.1; -; mRNA.
DR EMBL; AK165249; BAE38103.1; -; mRNA.
DR EMBL; AK167691; BAE39738.1; -; mRNA.
DR EMBL; AK167779; BAE39811.1; -; mRNA.
DR EMBL; AK167808; BAE39835.1; -; mRNA.
DR EMBL; AK167926; BAE39931.1; -; mRNA.
DR EMBL; AK168271; BAE40217.1; -; mRNA.
DR EMBL; AK169123; BAE40903.1; -; mRNA.
DR EMBL; AK169210; BAE40982.1; -; mRNA.
DR EMBL; AK169295; BAE41051.1; -; mRNA.
DR EMBL; CR974451; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC003825; AAH03825.1; -; mRNA.
DR EMBL; M28732; AAA40510.1; -; mRNA.
DR CCDS; CCDS28706.1; -.
DR PIR; E25437; E25437.
DR RefSeq; NP_035785.1; NM_011655.5.
DR AlphaFoldDB; P99024; -.
DR SMR; P99024; -.
DR BioGRID; 204381; 83.
DR CORUM; P99024; -.
DR ELM; P99024; -.
DR IntAct; P99024; 42.
DR MINT; P99024; -.
DR STRING; 10090.ENSMUSP00000001566; -.
DR ChEMBL; CHEMBL4739682; -.
DR CarbonylDB; P99024; -.
DR iPTMnet; P99024; -.
DR PhosphoSitePlus; P99024; -.
DR SwissPalm; P99024; -.
DR REPRODUCTION-2DPAGE; IPI00117352; -.
DR REPRODUCTION-2DPAGE; P99024; -.
DR SWISS-2DPAGE; P99024; -.
DR CPTAC; non-CPTAC-3881; -.
DR EPD; P99024; -.
DR jPOST; P99024; -.
DR MaxQB; P99024; -.
DR PaxDb; P99024; -.
DR PeptideAtlas; P99024; -.
DR PRIDE; P99024; -.
DR ProteomicsDB; 254861; -.
DR TopDownProteomics; P99024; -.
DR Antibodypedia; 48344; 1040 antibodies from 44 providers.
DR DNASU; 22154; -.
DR Ensembl; ENSMUST00000001566; ENSMUSP00000001566; ENSMUSG00000001525.
DR GeneID; 22154; -.
DR KEGG; mmu:22154; -.
DR UCSC; uc008ciq.2; mouse.
DR CTD; 22154; -.
DR MGI; MGI:107812; Tubb5.
DR VEuPathDB; HostDB:ENSMUSG00000001525; -.
DR eggNOG; KOG1375; Eukaryota.
DR GeneTree; ENSGT00940000154370; -.
DR HOGENOM; CLU_015718_1_1_1; -.
DR InParanoid; P99024; -.
DR OMA; RYQGEND; -.
DR OrthoDB; 962471at2759; -.
DR PhylomeDB; P99024; -.
DR TreeFam; TF300298; -.
DR Reactome; R-MMU-2565942; Regulation of PLK1 Activity at G2/M Transition.
DR Reactome; R-MMU-380259; Loss of Nlp from mitotic centrosomes.
DR Reactome; R-MMU-380270; Recruitment of mitotic centrosome proteins and complexes.
DR Reactome; R-MMU-380284; Loss of proteins required for interphase microtubule organization from the centrosome.
DR Reactome; R-MMU-380320; Recruitment of NuMA to mitotic centrosomes.
DR Reactome; R-MMU-5620912; Anchoring of the basal body to the plasma membrane.
DR Reactome; R-MMU-6798695; Neutrophil degranulation.
DR Reactome; R-MMU-8854518; AURKA Activation by TPX2.
DR BioGRID-ORCS; 22154; 30 hits in 70 CRISPR screens.
DR ChiTaRS; Tubb5; mouse.
DR PRO; PR:P99024; -.
DR Proteomes; UP000000589; Chromosome 17.
DR RNAct; P99024; protein.
DR Bgee; ENSMUSG00000001525; Expressed in medial ganglionic eminence and 284 other tissues.
DR ExpressionAtlas; P99024; baseline and differential.
DR Genevisible; P99024; MM.
DR GO; GO:0044297; C:cell body; ISO:MGI.
DR GO; GO:0005737; C:cytoplasm; ISO:MGI.
DR GO; GO:0036464; C:cytoplasmic ribonucleoprotein granule; ISO:MGI.
DR GO; GO:0005829; C:cytosol; TAS:Reactome.
DR GO; GO:0045171; C:intercellular bridge; ISO:MGI.
DR GO; GO:0045121; C:membrane raft; ISO:MGI.
DR GO; GO:0005874; C:microtubule; IDA:MGI.
DR GO; GO:0015630; C:microtubule cytoskeleton; ISO:MGI.
DR GO; GO:0072686; C:mitotic spindle; ISO:MGI.
DR GO; GO:0005641; C:nuclear envelope lumen; ISO:MGI.
DR GO; GO:0005634; C:nucleus; IDA:MGI.
DR GO; GO:0032991; C:protein-containing complex; ISO:MGI.
DR GO; GO:0045298; C:tubulin complex; NAS:UniProtKB.
DR GO; GO:0005525; F:GTP binding; IBA:GO_Central.
DR GO; GO:0032794; F:GTPase activating protein binding; ISO:MGI.
DR GO; GO:0042288; F:MHC class I protein binding; ISO:MGI.
DR GO; GO:0019904; F:protein domain specific binding; ISO:MGI.
DR GO; GO:0044877; F:protein-containing complex binding; ISO:MGI.
DR GO; GO:0005200; F:structural constituent of cytoskeleton; IDA:MGI.
DR GO; GO:0031625; F:ubiquitin protein ligase binding; ISO:MGI.
DR GO; GO:0000226; P:microtubule cytoskeleton organization; IBA:GO_Central.
DR GO; GO:0007017; P:microtubule-based process; IDA:MGI.
DR GO; GO:0000278; P:mitotic cell cycle; IBA:GO_Central.
DR GO; GO:0071895; P:odontoblast differentiation; ISO:MGI.
DR GO; GO:0050807; P:regulation of synapse organization; IDA:SynGO.
DR GO; GO:0051225; P:spindle assembly; IDA:MGI.
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 Acetylation; Cytoplasm; Cytoskeleton; Direct protein sequencing;
KW GTP-binding; Isopeptide bond; Methylation; Microtubule; Nucleotide-binding;
KW Phosphoprotein; Reference proteome; Ubl conjugation.
FT CHAIN 1..444
FT /note="Tubulin beta-5 chain"
FT /id="PRO_0000048246"
FT REGION 423..444
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 1..4
FT /note="MREI motif"
FT /evidence="ECO:0000250|UniProtKB:P07437"
FT COMPBIAS 427..444
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:0007744|PubMed:21183079"
FT MOD_RES 55
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:P07437"
FT MOD_RES 58
FT /note="N6-acetyllysine; alternate"
FT /evidence="ECO:0007744|PubMed:23806337"
FT MOD_RES 58
FT /note="N6-succinyllysine; alternate"
FT /evidence="ECO:0007744|PubMed:23806337"
FT MOD_RES 172
FT /note="Phosphoserine; by CDK1"
FT /evidence="ECO:0000269|PubMed:16371510"
FT MOD_RES 285
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:P07437"
FT MOD_RES 290
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:P07437"
FT MOD_RES 318
FT /note="Omega-N-methylarginine"
FT /evidence="ECO:0000250|UniProtKB:P07437"
FT MOD_RES 434
FT /note="5-glutamyl polyglutamate"
FT /evidence="ECO:0000250|UniProtKB:P07437"
FT MOD_RES 438
FT /note="5-glutamyl polyglutamate"
FT /evidence="ECO:0000250|UniProtKB:Q2T9S0"
FT MOD_RES 438
FT /note="5-glutamyl polyglycine"
FT /evidence="ECO:0000250|UniProtKB:P07437"
FT MOD_RES 439
FT /note="5-glutamyl polyglutamate"
FT /evidence="ECO:0000250|UniProtKB:P07437"
FT MOD_RES 439
FT /note="5-glutamyl polyglycine"
FT /evidence="ECO:0000250|UniProtKB:P07437"
FT MOD_RES 441
FT /note="5-glutamyl polyglutamate"
FT /evidence="ECO:0000250|UniProtKB:P07437"
FT MOD_RES 441
FT /note="5-glutamyl polyglycine"
FT /evidence="ECO:0000250|UniProtKB:P07437"
FT MOD_RES 442
FT /note="5-glutamyl polyglycine"
FT /evidence="ECO:0000250|UniProtKB:P07437"
FT MOD_RES 443
FT /note="5-glutamyl polyglycine"
FT /evidence="ECO:0000250|UniProtKB:P07437"
FT CROSSLNK 58
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in ubiquitin); alternate"
FT /evidence="ECO:0000250|UniProtKB:P07437"
FT CROSSLNK 324
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in ubiquitin)"
FT /evidence="ECO:0000250|UniProtKB:P07437"
FT MUTAGEN 172
FT /note="S->A: Loss of CDK1-mediated phosphorylation."
FT /evidence="ECO:0000269|PubMed:16371510"
FT MUTAGEN 172
FT /note="S->D,E: Mimics phosphorylation, unable to
FT incorporate into microtubules."
FT /evidence="ECO:0000269|PubMed:16371510"
FT CONFLICT 15
FT /note="Q -> P (in Ref. 2; BAB27292)"
FT /evidence="ECO:0000305"
FT CONFLICT 114
FT /note="D -> N (in Ref. 2; BAE40217)"
FT /evidence="ECO:0000305"
FT CONFLICT 143
FT /note="T -> N (in Ref. 2; BAE28709)"
FT /evidence="ECO:0000305"
FT CONFLICT 264
FT /note="H -> D (in Ref. 2; BAE40217)"
FT /evidence="ECO:0000305"
FT CONFLICT 307
FT /note="H -> N (in Ref. 2; BAE39835)"
FT /evidence="ECO:0000305"
FT CONFLICT 357
FT /note="P -> T (in Ref. 2; BAE40217)"
FT /evidence="ECO:0000305"
FT CONFLICT 400
FT /note="G -> A (in Ref. 6; AAA40510)"
FT /evidence="ECO:0000305"
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
