TBB2B_HUMAN
ID TBB2B_HUMAN Reviewed; 445 AA.
AC Q9BVA1; A8K068;
DT 28-NOV-2006, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2001, sequence version 1.
DT 03-AUG-2022, entry version 190.
DE RecName: Full=Tubulin beta-2B chain;
GN Name=TUBB2B;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RA Kalnine N., Chen X., Rolfs A., Halleck A., Hines L., Eisenstein S.,
RA Koundinya M., Raphael J., Moreira D., Kelley T., LaBaer J., Lin Y.,
RA Phelan M., Farmer A.;
RT "Cloning of human full-length CDSs in BD Creator(TM) system donor vector.";
RL Submitted (OCT-2004) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RA Ebert L., Schick M., Neubert P., Schatten R., Henze S., Korn B.;
RT "Cloning of human full open reading frames in Gateway(TM) system entry
RT vector (pDONR201).";
RL Submitted (JUN-2004) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RX PubMed=14702039; DOI=10.1038/ng1285;
RA Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
RA Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
RA Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
RA Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
RA Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H.,
RA Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M.,
RA Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K.,
RA Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T.,
RA Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M.,
RA Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S.,
RA Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H.,
RA Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K.,
RA Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N.,
RA Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
RA Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
RA Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
RA Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
RA Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y.,
RA Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K.,
RA Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T.,
RA Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T.,
RA Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y.,
RA Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H.,
RA Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y.,
RA Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H.,
RA Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O.,
RA Isogai T., Sugano S.;
RT "Complete sequencing and characterization of 21,243 full-length human
RT cDNAs.";
RL Nat. Genet. 36:40-45(2004).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=14574404; DOI=10.1038/nature02055;
RA Mungall A.J., Palmer S.A., Sims S.K., Edwards C.A., Ashurst J.L.,
RA Wilming L., Jones M.C., Horton R., Hunt S.E., Scott C.E., Gilbert J.G.R.,
RA Clamp M.E., Bethel G., Milne S., Ainscough R., Almeida J.P., Ambrose K.D.,
RA Andrews T.D., Ashwell R.I.S., Babbage A.K., Bagguley C.L., Bailey J.,
RA Banerjee R., Barker D.J., Barlow K.F., Bates K., Beare D.M., Beasley H.,
RA Beasley O., Bird C.P., Blakey S.E., Bray-Allen S., Brook J., Brown A.J.,
RA Brown J.Y., Burford D.C., Burrill W., Burton J., Carder C., Carter N.P.,
RA Chapman J.C., Clark S.Y., Clark G., Clee C.M., Clegg S., Cobley V.,
RA Collier R.E., Collins J.E., Colman L.K., Corby N.R., Coville G.J.,
RA Culley K.M., Dhami P., Davies J., Dunn M., Earthrowl M.E., Ellington A.E.,
RA Evans K.A., Faulkner L., Francis M.D., Frankish A., Frankland J.,
RA French L., Garner P., Garnett J., Ghori M.J., Gilby L.M., Gillson C.J.,
RA Glithero R.J., Grafham D.V., Grant M., Gribble S., Griffiths C.,
RA Griffiths M.N.D., Hall R., Halls K.S., Hammond S., Harley J.L., Hart E.A.,
RA Heath P.D., Heathcott R., Holmes S.J., Howden P.J., Howe K.L., Howell G.R.,
RA Huckle E., Humphray S.J., Humphries M.D., Hunt A.R., Johnson C.M.,
RA Joy A.A., Kay M., Keenan S.J., Kimberley A.M., King A., Laird G.K.,
RA Langford C., Lawlor S., Leongamornlert D.A., Leversha M., Lloyd C.R.,
RA Lloyd D.M., Loveland J.E., Lovell J., Martin S., Mashreghi-Mohammadi M.,
RA Maslen G.L., Matthews L., McCann O.T., McLaren S.J., McLay K., McMurray A.,
RA Moore M.J.F., Mullikin J.C., Niblett D., Nickerson T., Novik K.L.,
RA Oliver K., Overton-Larty E.K., Parker A., Patel R., Pearce A.V., Peck A.I.,
RA Phillimore B.J.C.T., Phillips S., Plumb R.W., Porter K.M., Ramsey Y.,
RA Ranby S.A., Rice C.M., Ross M.T., Searle S.M., Sehra H.K., Sheridan E.,
RA Skuce C.D., Smith S., Smith M., Spraggon L., Squares S.L., Steward C.A.,
RA Sycamore N., Tamlyn-Hall G., Tester J., Theaker A.J., Thomas D.W.,
RA Thorpe A., Tracey A., Tromans A., Tubby B., Wall M., Wallis J.M.,
RA West A.P., White S.S., Whitehead S.L., Whittaker H., Wild A., Willey D.J.,
RA Wilmer T.E., Wood J.M., Wray P.W., Wyatt J.C., Young L., Younger R.M.,
RA Bentley D.R., Coulson A., Durbin R.M., Hubbard T., Sulston J.E., Dunham I.,
RA Rogers J., Beck S.;
RT "The DNA sequence and analysis of human chromosome 6.";
RL Nature 425:805-811(2003).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M.,
RA Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J.,
RA Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S.,
RA Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H.,
RA Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K.,
RA Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D.,
RA Hunkapiller M.W., Myers E.W., Venter J.C.;
RL Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Brain, and Muscle;
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 [7]
RP PROTEIN SEQUENCE OF 47-58; 63-121; 163-174; 217-276; 283-297; 310-318;
RP 325-359; 363-379 AND 381-390, AND IDENTIFICATION BY MASS SPECTROMETRY.
RC TISSUE=Brain, Cajal-Retzius cell, and Fetal brain cortex;
RA Lubec G., Afjehi-Sadat L., Chen W.-Q., Sun Y.;
RL Submitted (DEC-2008) to UniProtKB.
RN [8]
RP PHOSPHORYLATION AT 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 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 [10]
RP FUNCTION, VARIANTS CDCBM7 PRO-172; THR-210; PRO-228; LEU-265 AND MET-312,
RP VARIANT SER-201, AND CHARACTERIZATION OF VARIANTS CDCBM7 PRO-172 AND
RP LEU-265.
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 [11]
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., Rodriguez-Antona C.;
RT "Tumoral and tissue-specific expression of the major human beta-tubulin
RT isotypes.";
RL Cytoskeleton 67:214-223(2010).
RN [12]
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., Buerckstuemmer T.,
RA Bennett K.L., Superti-Furga G., Colinge J.;
RT "Initial characterization of the human central proteome.";
RL BMC Syst. Biol. 5:17-17(2011).
RN [13]
RP GLUTAMYLATION.
RX PubMed=26875866; DOI=10.1016/j.cell.2016.01.019;
RA Valenstein M.L., Roll-Mecak A.;
RT "Graded control of microtubule severing by tubulin glutamylation.";
RL Cell 164:911-921(2016).
RN [14]
RP VARIANTS CDCBM7 PRO-117; SER-256 AND ASN-417, AND INVOLVEMENT IN CDCBM7.
RX PubMed=22333901; DOI=10.1038/ejhg.2012.21;
RA Guerrini R., Mei D., Cordelli D.M., Pucatti D., Franzoni E., Parrini E.;
RT "Symmetric polymicrogyria and pachygyria associated with TUBB2B gene
RT mutations.";
RL Eur. J. Hum. Genet. 20:995-998(2012).
RN [15]
RP VARIANT CDCBM7 LYS-421, CHARACTERIZATION OF VARIANT CDCBM7 LYS-421,
RP FUNCTION, SUBUNIT, AND SUBCELLULAR LOCATION.
RX PubMed=23001566; DOI=10.1093/hmg/dds393;
RA Cederquist G.Y., Luchniak A., Tischfield M.A., Peeva M., Song Y.,
RA Menezes M.P., Chan W.M., Andrews C., Chew S., Jamieson R.V., Gomes L.,
RA Flaherty M., Grant P.E., Gupta M.L. Jr., Engle E.C.;
RT "An inherited TUBB2B mutation alters a kinesin-binding site and causes
RT polymicrogyria, CFEOM and axon dysinnervation.";
RL Hum. Mol. Genet. 21:5484-5499(2012).
RN [16]
RP VARIANT CDCBM7 PHE-239, CHARACTERIZATION OF VARIANT CDCBM7 PHE-239,
RP INVOLVEMENT IN CDCBM7, FUNCTION, AND SUBUNIT.
RX PubMed=26732629; DOI=10.1016/j.ejmg.2015.12.007;
RA Laquerriere A., Gonzales M., Saillour Y., Cavallin M., Joye N., Quelin C.,
RA Bidat L., Dommergues M., Plessis G., Encha-Razavi F., Chelly J.,
RA Bahi-Buisson N., Poirier K.;
RT "De novo TUBB2B mutation causes fetal akinesia deformation sequence with
RT microlissencephaly: An unusual presentation of tubulinopathy.";
RL Eur. J. Med. Genet. 59:249-256(2016).
RN [17]
RP VARIANT GLN-390, CHARACTERIZATION OF VARIANT GLN-390, FUNCTION, SUBUNIT,
RP AND SUBCELLULAR LOCATION.
RX PubMed=28013290; DOI=10.1093/hmg/ddw383;
RA Breuss M.W., Nguyen T., Srivatsan A., Leca I., Tian G., Fritz T.,
RA Hansen A.H., Musaev D., McEvoy-Venneri J., James K.N., Rosti R.O.,
RA Scott E., Tan U., Kolodner R.D., Cowan N.J., Keays D.A., Gleeson J.G.;
RT "Uner Tan syndrome caused by a homozygous TUBB2B mutation affecting
RT microtubule stability.";
RL Hum. Mol. Genet. 26:258-269(2017).
CC -!- FUNCTION: Tubulin is the major constituent of microtubules
CC (PubMed:23001566, PubMed:28013290, PubMed:26732629). It binds two moles
CC of GTP, one at an exchangeable site on the beta chain and one at a non-
CC exchangeable site on the alpha chain (By similarity). Plays a critical
CC role in proper axon guidance in both central and peripheral axon tracts
CC (PubMed:23001566). Implicated in neuronal migration (PubMed:19465910).
CC {ECO:0000250, ECO:0000269|PubMed:19465910, ECO:0000269|PubMed:23001566,
CC ECO:0000269|PubMed:26732629, ECO:0000269|PubMed:28013290}.
CC -!- SUBUNIT: Dimer of alpha and beta chains (PubMed:23001566,
CC PubMed:28013290, PubMed:26732629). A typical microtubule is a hollow
CC water-filled tube with an outer diameter of 25 nm and an inner diameter
CC of 15 nM. Alpha-beta heterodimers associate head-to-tail to form
CC protofilaments running lengthwise along the microtubule wall with the
CC 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:0000269|PubMed:23001566,
CC ECO:0000269|PubMed:26732629, ECO:0000269|PubMed:28013290}.
CC -!- INTERACTION:
CC Q9BVA1; O00555: CACNA1A; NbExp=2; IntAct=EBI-355665, EBI-766279;
CC -!- SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton
CC {ECO:0000269|PubMed:23001566, ECO:0000269|PubMed:28013290}.
CC -!- TISSUE SPECIFICITY: High expression in brain.
CC {ECO:0000269|PubMed:20191564}.
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 polyglutamylated,
CC resulting in polyglutamate chains on the gamma-carboxyl group
CC (PubMed:26875866). 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 (PubMed:26875866). Glutamylation is also involved in cilia
CC motility (By similarity). {ECO:0000250|UniProtKB:P99024,
CC ECO:0000269|PubMed:26875866}.
CC -!- PTM: Some glutamate residues at the C-terminus are monoglycylated but
CC not polyglycylated due to the absence of functional TTLL10 in human.
CC Monoglycylation is mainly limited to tubulin incorporated into cilia
CC and flagella axonemes, which is required for their stability and
CC maintenance. Flagella glycylation controls sperm motility. Both
CC polyglutamylation and monoglycylation can coexist on the same protein
CC on adjacent residues, and lowering glycylation levels increases
CC polyglutamylation, and reciprocally. {ECO:0000250|UniProtKB:P07437,
CC ECO:0000305|PubMed:19524510}.
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 -!- DISEASE: Cortical dysplasia, complex, with other brain malformations 7
CC (CDCBM7) [MIM:610031]: A malformation of the cortex in which the brain
CC surface is irregular and characterized by an excessive number of small
CC gyri with abnormal lamination. Polymicrogyria is a heterogeneous
CC disorder, considered to be the result of postmigratory abnormal
CC cortical organization. {ECO:0000269|PubMed:19465910,
CC ECO:0000269|PubMed:22333901, ECO:0000269|PubMed:23001566,
CC ECO:0000269|PubMed:26732629}. Note=The disease is caused by variants
CC affecting the gene represented in this entry.
CC -!- DISEASE: Note=Defects in TUBB2B may be involved in cerebellar ataxia,
CC intellectual disability, and dysequilibrium syndrome (CAMRQ).
CC {ECO:0000269|PubMed:28013290}.
CC -!- SIMILARITY: Belongs to the tubulin family. {ECO:0000305}.
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DR EMBL; BT019930; AAV38733.1; -; mRNA.
DR EMBL; CR456788; CAG33069.1; -; mRNA.
DR EMBL; AK289433; BAF82122.1; -; mRNA.
DR EMBL; AL445309; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH471087; EAW55125.1; -; Genomic_DNA.
DR EMBL; BC001352; AAH01352.1; -; mRNA.
DR EMBL; BC063610; AAH63610.1; -; mRNA.
DR CCDS; CCDS4485.1; -.
DR RefSeq; NP_821080.1; NM_178012.4.
DR PDB; 6E7C; EM; 3.65 A; B=1-426.
DR PDBsum; 6E7C; -.
DR AlphaFoldDB; Q9BVA1; -.
DR SMR; Q9BVA1; -.
DR BioGRID; 131483; 195.
DR CORUM; Q9BVA1; -.
DR IntAct; Q9BVA1; 66.
DR MINT; Q9BVA1; -.
DR STRING; 9606.ENSP00000259818; -.
DR ChEMBL; CHEMBL2095182; -.
DR DrugBank; DB07574; 2-MERCAPTO-N-[1,2,3,10-TETRAMETHOXY-9-OXO-5,6,7,9-TETRAHYDRO-BENZO[A]HEPTALEN-7-YL]ACETAMIDE.
DR DrugBank; DB05147; CYT997.
DR DrugCentral; Q9BVA1; -.
DR GlyGen; Q9BVA1; 1 site, 1 O-linked glycan (1 site).
DR iPTMnet; Q9BVA1; -.
DR PhosphoSitePlus; Q9BVA1; -.
DR SwissPalm; Q9BVA1; -.
DR BioMuta; TUBB2B; -.
DR DMDM; 74761283; -.
DR EPD; Q9BVA1; -.
DR jPOST; Q9BVA1; -.
DR MassIVE; Q9BVA1; -.
DR MaxQB; Q9BVA1; -.
DR PaxDb; Q9BVA1; -.
DR PeptideAtlas; Q9BVA1; -.
DR PRIDE; Q9BVA1; -.
DR ProteomicsDB; 79190; -.
DR TopDownProteomics; Q9BVA1; -.
DR Antibodypedia; 24394; 363 antibodies from 24 providers.
DR DNASU; 347733; -.
DR Ensembl; ENST00000259818.8; ENSP00000259818.6; ENSG00000137285.11.
DR GeneID; 347733; -.
DR KEGG; hsa:347733; -.
DR MANE-Select; ENST00000259818.8; ENSP00000259818.6; NM_178012.5; NP_821080.1.
DR UCSC; uc003mvg.4; human.
DR CTD; 347733; -.
DR DisGeNET; 347733; -.
DR GeneCards; TUBB2B; -.
DR GeneReviews; TUBB2B; -.
DR HGNC; HGNC:30829; TUBB2B.
DR HPA; ENSG00000137285; Group enriched (brain, choroid plexus).
DR MalaCards; TUBB2B; -.
DR MIM; 610031; phenotype.
DR MIM; 612850; gene.
DR neXtProt; NX_Q9BVA1; -.
DR OpenTargets; ENSG00000137285; -.
DR Orphanet; 45358; Congenital fibrosis of extraocular muscles.
DR Orphanet; 1766; Dysequilibrium syndrome.
DR Orphanet; 300573; Polymicrogyria due to TUBB2B mutation.
DR Orphanet; 467166; Tubulinopathy-associated dysgyria.
DR PharmGKB; PA142670671; -.
DR VEuPathDB; HostDB:ENSG00000137285; -.
DR eggNOG; KOG1375; Eukaryota.
DR GeneTree; ENSGT00940000154150; -.
DR HOGENOM; CLU_015718_1_1_1; -.
DR InParanoid; Q9BVA1; -.
DR OMA; SYVGNSH; -.
DR OrthoDB; 962471at2759; -.
DR PhylomeDB; Q9BVA1; -.
DR TreeFam; TF300298; -.
DR PathwayCommons; Q9BVA1; -.
DR Reactome; R-HSA-1445148; Translocation of SLC2A4 (GLUT4) to the plasma membrane.
DR Reactome; R-HSA-190840; Microtubule-dependent trafficking of connexons from Golgi to the plasma membrane.
DR Reactome; R-HSA-190861; Gap junction assembly.
DR Reactome; R-HSA-2132295; MHC class II antigen presentation.
DR Reactome; R-HSA-2467813; Separation of Sister Chromatids.
DR Reactome; R-HSA-2500257; Resolution of Sister Chromatid Cohesion.
DR Reactome; R-HSA-3371497; HSP90 chaperone cycle for steroid hormone receptors (SHR) in the presence of ligand.
DR Reactome; R-HSA-380320; Recruitment of NuMA to mitotic centrosomes.
DR Reactome; R-HSA-389957; Prefoldin mediated transfer of substrate to CCT/TriC.
DR Reactome; R-HSA-389960; Formation of tubulin folding intermediates by CCT/TriC.
DR Reactome; R-HSA-389977; Post-chaperonin tubulin folding pathway.
DR Reactome; R-HSA-437239; Recycling pathway of L1.
DR Reactome; R-HSA-5610787; Hedgehog 'off' state.
DR Reactome; R-HSA-5617833; Cilium Assembly.
DR Reactome; R-HSA-5620924; Intraflagellar transport.
DR Reactome; R-HSA-5626467; RHO GTPases activate IQGAPs.
DR Reactome; R-HSA-5663220; RHO GTPases Activate Formins.
DR Reactome; R-HSA-6807878; COPI-mediated anterograde transport.
DR Reactome; R-HSA-6811434; COPI-dependent Golgi-to-ER retrograde traffic.
DR Reactome; R-HSA-6811436; COPI-independent Golgi-to-ER retrograde traffic.
DR Reactome; R-HSA-68877; Mitotic Prometaphase.
DR Reactome; R-HSA-8852276; The role of GTSE1 in G2/M progression after G2 checkpoint.
DR Reactome; R-HSA-8955332; Carboxyterminal post-translational modifications of tubulin.
DR Reactome; R-HSA-9609690; HCMV Early Events.
DR Reactome; R-HSA-9609736; Assembly and cell surface presentation of NMDA receptors.
DR Reactome; R-HSA-9619483; Activation of AMPK downstream of NMDARs.
DR Reactome; R-HSA-9646399; Aggrephagy.
DR Reactome; R-HSA-9648025; EML4 and NUDC in mitotic spindle formation.
DR Reactome; R-HSA-9668328; Sealing of the nuclear envelope (NE) by ESCRT-III.
DR Reactome; R-HSA-983189; Kinesins.
DR SignaLink; Q9BVA1; -.
DR BioGRID-ORCS; 347733; 36 hits in 1007 CRISPR screens.
DR ChiTaRS; TUBB2B; human.
DR GenomeRNAi; 347733; -.
DR Pharos; Q9BVA1; Tclin.
DR PRO; PR:Q9BVA1; -.
DR Proteomes; UP000005640; Chromosome 6.
DR RNAct; Q9BVA1; protein.
DR Bgee; ENSG00000137285; Expressed in cortical plate and 179 other tissues.
DR ExpressionAtlas; Q9BVA1; baseline and differential.
DR Genevisible; Q9BVA1; HS.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0045171; C:intercellular bridge; IDA:HPA.
DR GO; GO:0005874; C:microtubule; IDA:UniProtKB.
DR GO; GO:0015630; C:microtubule cytoskeleton; IDA:UniProtKB.
DR GO; GO:0072686; C:mitotic spindle; IDA:HPA.
DR GO; GO:0005634; C:nucleus; HDA:UniProtKB.
DR GO; GO:0098685; C:Schaffer collateral - CA1 synapse; IEA:Ensembl.
DR GO; GO:0005525; F:GTP binding; IBA:GO_Central.
DR GO; GO:0046982; F:protein heterodimerization activity; IDA:UniProtKB.
DR GO; GO:0005200; F:structural constituent of cytoskeleton; IBA:GO_Central.
DR GO; GO:1990403; P:embryonic brain development; IEA:Ensembl.
DR GO; GO:0000226; P:microtubule cytoskeleton organization; IBA:GO_Central.
DR GO; GO:0007017; P:microtubule-based process; IMP:UniProtKB.
DR GO; GO:0000278; P:mitotic cell cycle; IBA:GO_Central.
DR GO; GO:0050804; P:modulation of chemical synaptic transmission; IEA:Ensembl.
DR GO; GO:0001764; P:neuron migration; IMP:UniProtKB.
DR GO; GO:1902669; P:positive regulation of axon guidance; IMP: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 3D-structure; Acetylation; Cytoplasm; Cytoskeleton;
KW Direct protein sequencing; Disease variant; GTP-binding;
KW Intellectual disability; Isopeptide bond; Methylation; Microtubule;
KW Neurogenesis; Nucleotide-binding; Phosphoprotein; Reference proteome;
KW Ubl conjugation.
FT CHAIN 1..445
FT /note="Tubulin beta-2B chain"
FT /id="PRO_0000262651"
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: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 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 VARIANT 117
FT /note="L -> P (in CDCBM7; dbSNP:rs397514569)"
FT /evidence="ECO:0000269|PubMed:22333901"
FT /id="VAR_078186"
FT VARIANT 172
FT /note="S -> P (in CDCBM7; affects microtubules assembly;
FT dbSNP:rs137853194)"
FT /evidence="ECO:0000269|PubMed:19465910"
FT /id="VAR_063389"
FT VARIANT 201
FT /note="C -> S (in dbSNP:rs201922441)"
FT /evidence="ECO:0000269|PubMed:19465910"
FT /id="VAR_063390"
FT VARIANT 210
FT /note="I -> T (in CDCBM7)"
FT /evidence="ECO:0000269|PubMed:19465910"
FT /id="VAR_063391"
FT VARIANT 228
FT /note="L -> P (in CDCBM7; dbSNP:rs137853195)"
FT /evidence="ECO:0000269|PubMed:19465910"
FT /id="VAR_063392"
FT VARIANT 239
FT /note="C -> F (in CDCBM7; decreased tubulin heterodimer
FT formation; decreased ability to incorporate into the
FT cytoskeleton; no effect on microtubules disintegration;
FT increased ability to repolymerize; dbSNP:rs878853284)"
FT /evidence="ECO:0000269|PubMed:26732629"
FT /id="VAR_078187"
FT VARIANT 256
FT /note="N -> S (in CDCBM7; dbSNP:rs397514568)"
FT /evidence="ECO:0000269|PubMed:22333901"
FT /id="VAR_078188"
FT VARIANT 265
FT /note="F -> L (in CDCBM7; affects microtubules assembly;
FT dbSNP:rs137853196)"
FT /evidence="ECO:0000269|PubMed:19465910"
FT /id="VAR_063393"
FT VARIANT 312
FT /note="T -> M (in CDCBM7)"
FT /evidence="ECO:0000269|PubMed:19465910"
FT /id="VAR_063394"
FT VARIANT 390
FT /note="R -> Q (found in a patient with cerebellar ataxia
FT intellectual disability and dysequilibrium syndrome;
FT unknown pathological significance; no effect on protein
FT folding; no effect on tubulin heterodimer formation; no
FT effect on integration into the microtubule lattice; no
FT effect on cytoskeleton subcellular location)"
FT /evidence="ECO:0000269|PubMed:28013290"
FT /id="VAR_078189"
FT VARIANT 417
FT /note="D -> N (in CDCBM7; dbSNP:rs397514567)"
FT /evidence="ECO:0000269|PubMed:22333901"
FT /id="VAR_078190"
FT VARIANT 421
FT /note="E -> K (in CDCBM7; decreased protein expression;
FT decreased tubulin heterodimer formation; no effect on
FT integration into the microtubule lattice; no effect on
FT microtubule cytoskeleton subcellular location; loss of axon
FT guidance; dbSNP:rs398122369)"
FT /evidence="ECO:0000269|PubMed:23001566"
FT /id="VAR_078191"
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
