ID TBB2B_MOUSE Reviewed; 445 AA. AC Q9CWF2; Q3TG26; DT 28-NOV-2006, integrated into UniProtKB/Swiss-Prot. DT 01-JUN-2001, sequence version 1. DT 14-DEC-2022, entry version 176. DE RecName: Full=Tubulin beta-2B chain; GN Name=Tubb2b; 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 [LARGE SCALE MRNA]. RC STRAIN=C57BL/6J; TISSUE=Liver; 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 [2] RP PROTEIN SEQUENCE OF 104-121; 217-241; 263-276; 310-318 AND 381-390, AND RP IDENTIFICATION BY MASS SPECTROMETRY. RC TISSUE=Hippocampus; RA Lubec G., Klug S.; RL Submitted (MAR-2007) to UniProtKB. RN [3] 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 [4] 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 [5] RP TISSUE SPECIFICITY. RX PubMed=19465910; DOI=10.1038/ng.380; RA Jaglin X.H., Poirier K., Saillour Y., Buhler E., Tian G., Bahi-Buisson N., RA Fallet-Bianco C., Phan-Dinh-Tuy F., Kong X.P., Bomont P., RA Castelnau-Ptakhine L., Odent S., Loget P., Kossorotoff M., Snoeck I., RA Plessis G., Parent P., Beldjord C., Cardoso C., Represa A., Flint J., RA Keays D.A., Cowan N.J., Chelly J.; RT "Mutations in the beta-tubulin gene TUBB2B result in asymmetrical RT polymicrogyria."; RL Nat. Genet. 41:746-752(2009). RN [6] RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Brain, Heart, Kidney, Lung, Pancreas, 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 [7] 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 [8] 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, a cylinder CC consisting of laterally associated linear protofilaments composed of CC alpha- and beta-tubulin heterodimers. Microtubules grow by the addition CC of GTP-tubulin dimers to the microtubule end, where a stabilizing cap CC forms. Below the cap, tubulin dimers are in GDP-bound state, owing to CC GTPase activity of alpha-tubulin. Plays a critical role in proper axon CC guidance in both central and peripheral axon tracts. Implicated in CC neuronal migration. {ECO:0000250, ECO:0000250|UniProtKB:Q9BVA1}. CC -!- COFACTOR: CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420; CC Evidence={ECO:0000250|UniProtKB:P68363}; 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. {ECO:0000250|UniProtKB:Q9BVA1}. CC -!- SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton CC {ECO:0000250|UniProtKB:Q9BVA1}. CC -!- TISSUE SPECIFICITY: Strong expression is detected in the developing CC cortex and peripheral nervous system, as well as in the adult CC cerebellum, hippocampus and olfactory bulb. CC {ECO:0000269|PubMed:19465910}. 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:0000250|UniProtKB:Q9BVA1}. CC -!- SIMILARITY: Belongs to the tubulin family. {ECO:0000305}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; AK010786; BAB27182.1; -; mRNA. DR EMBL; AK168908; BAE40722.1; -; mRNA. DR CCDS; CCDS26445.1; -. DR RefSeq; NP_076205.1; NM_023716.2. DR AlphaFoldDB; Q9CWF2; -. DR SMR; Q9CWF2; -. DR BioGRID; 216203; 17. DR CORUM; Q9CWF2; -. DR IntAct; Q9CWF2; 8. DR MINT; Q9CWF2; -. DR STRING; 10090.ENSMUSP00000075178; -. DR iPTMnet; Q9CWF2; -. DR PhosphoSitePlus; Q9CWF2; -. DR SwissPalm; Q9CWF2; -. DR EPD; Q9CWF2; -. DR jPOST; Q9CWF2; -. DR MaxQB; Q9CWF2; -. DR PaxDb; Q9CWF2; -. DR ProteomicsDB; 254858; -. DR Antibodypedia; 24394; 364 antibodies from 24 providers. DR DNASU; 73710; -. DR Ensembl; ENSMUST00000075774; ENSMUSP00000075178; ENSMUSG00000045136. DR GeneID; 73710; -. DR KEGG; mmu:73710; -. DR UCSC; uc007qbd.1; mouse. DR AGR; MGI:1920960; -. DR CTD; 347733; -. DR MGI; MGI:1920960; Tubb2b. DR VEuPathDB; HostDB:ENSMUSG00000045136; -. DR eggNOG; KOG1375; Eukaryota. DR GeneTree; ENSGT00940000154150; -. DR HOGENOM; CLU_015718_1_1_1; -. DR InParanoid; Q9CWF2; -. DR OMA; SYVGNSH; -. DR OrthoDB; 962471at2759; -. DR PhylomeDB; Q9CWF2; -. DR TreeFam; TF300298; -. DR Reactome; R-MMU-190840; Microtubule-dependent trafficking of connexons from Golgi to the plasma membrane. DR Reactome; R-MMU-2132295; MHC class II antigen presentation. DR Reactome; R-MMU-2467813; Separation of Sister Chromatids. DR Reactome; R-MMU-2500257; Resolution of Sister Chromatid Cohesion. DR Reactome; R-MMU-3371497; HSP90 chaperone cycle for steroid hormone receptors (SHR) in the presence of ligand. DR Reactome; R-MMU-380320; Recruitment of NuMA to mitotic centrosomes. DR Reactome; R-MMU-437239; Recycling pathway of L1. DR Reactome; R-MMU-5610787; Hedgehog 'off' state. DR Reactome; R-MMU-5617833; Cilium Assembly. DR Reactome; R-MMU-5620924; Intraflagellar transport. DR Reactome; R-MMU-5626467; RHO GTPases activate IQGAPs. DR Reactome; R-MMU-5663220; RHO GTPases Activate Formins. DR Reactome; R-MMU-6807878; COPI-mediated anterograde transport. DR Reactome; R-MMU-6811434; COPI-dependent Golgi-to-ER retrograde traffic. DR Reactome; R-MMU-6811436; COPI-independent Golgi-to-ER retrograde traffic. DR Reactome; R-MMU-68877; Mitotic Prometaphase. DR Reactome; R-MMU-8852276; The role of GTSE1 in G2/M progression after G2 checkpoint. DR Reactome; R-MMU-8955332; Carboxyterminal post-translational modifications of tubulin. DR Reactome; R-MMU-9646399; Aggrephagy. DR Reactome; R-MMU-9648025; EML4 and NUDC in mitotic spindle formation. DR Reactome; R-MMU-9668328; Sealing of the nuclear envelope (NE) by ESCRT-III. DR Reactome; R-MMU-983189; Kinesins. DR BioGRID-ORCS; 73710; 2 hits in 72 CRISPR screens. DR ChiTaRS; Tubb2b; mouse. DR PRO; PR:Q9CWF2; -. DR Proteomes; UP000000589; Chromosome 13. DR RNAct; Q9CWF2; protein. DR Bgee; ENSMUSG00000045136; Expressed in cortical plate and 183 other tissues. DR ExpressionAtlas; Q9CWF2; baseline and differential. DR Genevisible; Q9CWF2; MM. DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central. DR GO; GO:0045171; C:intercellular bridge; ISO:MGI. DR GO; GO:0005874; C:microtubule; ISO:MGI. DR GO; GO:0015630; C:microtubule cytoskeleton; ISS:UniProtKB. DR GO; GO:0072686; C:mitotic spindle; ISO:MGI. DR GO; GO:0098685; C:Schaffer collateral - CA1 synapse; IDA:SynGO. DR GO; GO:0005525; F:GTP binding; IBA:GO_Central. DR GO; GO:0003924; F:GTPase activity; IEA:InterPro. DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW. DR GO; GO:0046982; F:protein heterodimerization activity; ISS:UniProtKB. DR GO; GO:0005200; F:structural constituent of cytoskeleton; IBA:GO_Central. DR GO; GO:0021987; P:cerebral cortex development; IMP:MGI. DR GO; GO:1990403; P:embryonic brain development; IMP:MGI. DR GO; GO:0000226; P:microtubule cytoskeleton organization; IBA:GO_Central. DR GO; GO:0007017; P:microtubule-based process; ISS:UniProtKB. DR GO; GO:0000278; P:mitotic cell cycle; IBA:GO_Central. DR GO; GO:0050804; P:modulation of chemical synaptic transmission; IDA:SynGO. DR GO; GO:0001764; P:neuron migration; ISO:MGI. DR GO; GO:1902669; P:positive regulation of axon guidance; ISS:UniProtKB. 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; 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; Tubulin C-terminal domain-like; 1. DR SUPFAM; SSF52490; Tubulin nucleotide-binding domain-like; 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; Magnesium; Metal-binding; Methylation; KW Microtubule; Neurogenesis; Nucleotide-binding; Phosphoprotein; KW Reference proteome; Ubl conjugation. FT CHAIN 1..445 FT /note="Tubulin beta-2B chain" FT /id="PRO_0000262652" FT REGION 422..445 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 431..445 FT /note="Acidic residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT BINDING 11 FT /ligand="GTP" FT /ligand_id="ChEBI:CHEBI:37565" FT /evidence="ECO:0000250|UniProtKB:Q13509" FT BINDING 69 FT /ligand="GTP" FT /ligand_id="ChEBI:CHEBI:37565" FT /evidence="ECO:0000250|UniProtKB:P68363" FT BINDING 69 FT /ligand="Mg(2+)" FT /ligand_id="ChEBI:CHEBI:18420" FT /evidence="ECO:0000250|UniProtKB:P68363" FT BINDING 138 FT /ligand="GTP" FT /ligand_id="ChEBI:CHEBI:37565" FT /evidence="ECO:0000250|UniProtKB:Q13509" FT BINDING 142 FT /ligand="GTP" FT /ligand_id="ChEBI:CHEBI:37565" FT /evidence="ECO:0000250|UniProtKB:Q13509" FT BINDING 143 FT /ligand="GTP" FT /ligand_id="ChEBI:CHEBI:37565" FT /evidence="ECO:0000250|UniProtKB:Q13509" FT BINDING 144 FT /ligand="GTP" FT /ligand_id="ChEBI:CHEBI:37565" FT /evidence="ECO:0000250|UniProtKB:Q13509" FT BINDING 204 FT /ligand="GTP" FT /ligand_id="ChEBI:CHEBI:37565" FT /evidence="ECO:0000250|UniProtKB:Q13509" FT BINDING 226 FT /ligand="GTP" FT /ligand_id="ChEBI:CHEBI:37565" FT /evidence="ECO:0000250|UniProtKB:Q13509" FT MOD_RES 40 FT /note="Phosphoserine" FT /evidence="ECO:0000250|UniProtKB:P99024" FT MOD_RES 55 FT /note="Phosphothreonine" FT /evidence="ECO:0000250|UniProtKB:Q3KRE8" FT MOD_RES 58 FT /note="N6-acetyllysine; alternate" FT /evidence="ECO:0000250|UniProtKB:P07437" FT MOD_RES 58 FT /note="N6-succinyllysine; alternate" FT /evidence="ECO:0000250|UniProtKB:P99024" FT MOD_RES 172 FT /note="Phosphoserine; by CDK1" FT /evidence="ECO:0000250|UniProtKB:Q9BVA1" 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 438 FT /note="5-glutamyl polyglutamate" FT /evidence="ECO:0000250|UniProtKB:Q2T9S0" 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 CONFLICT 123 FT /note="E -> G (in Ref. 1; BAE40722)" FT /evidence="ECO:0000305" FT CONFLICT 358 FT /note="P -> H (in Ref. 1; BAE40722)" FT /evidence="ECO:0000305" SQ SEQUENCE 445 AA; 49953 MW; 4DC3956EFF880746 CRC64; MREIVHIQAG QCGNQIGAKF WEVISDEHGI DPTGSYHGDS DLQLERINVY YNEATGNKYV PRAILVDLEP GTMDSVRSGP FGQIFRPDNF VFGQSGAGNN WAKGHYTEGA ELVDSVLDVV RKESESCDCL QGFQLTHSLG GGTGSGMGTL LISKIREEYP DRIMNTFSVM PSPKVSDTVV EPYNATLSVH QLVENTDETY CIDNEALYDI CFRTLKLTTP TYGDLNHLVS ATMSGVTTCL RFPGQLNADL RKLAVNMVPF PRLHFFMPGF APLTSRGSQQ YRALTVPELT QQMFDSKNMM AACDPRHGRY LTVAAIFRGR MSMKEVDEQM LNVQNKNSSY FVEWIPNNVK TAVCDIPPRG LKMSATFIGN STAIQELFKR ISEQFTAMFR RKAFLHWYTG EGMDEMEFTE AESNMNDLVS EYQQYQDATA DEQGEFEEEE GEDEA //