TBB2B_MOUSE
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 03-AUG-2022, entry version 174.
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. 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. Plays a critical role in
CC proper axon guidance in both central and peripheral axon tracts.
CC Implicated in neuronal migration. {ECO:0000250,
CC ECO:0000250|UniProtKB:Q9BVA1}.
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}.
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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 PRIDE; Q9CWF2; -.
DR ProteomicsDB; 254858; -.
DR Antibodypedia; 24394; 363 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 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-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:0046982; F:protein heterodimerization activity; ISS:UniProtKB.
DR GO; GO:0005200; F:structural constituent of cytoskeleton; IBA:GO_Central.
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; 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; Neurogenesis;
KW Nucleotide-binding; Phosphoprotein; 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 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: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
