ID TBB2A_HUMAN Reviewed; 445 AA.
AC Q13885; Q6FGZ8; Q8IWR2;
DT 28-NOV-2006, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1996, sequence version 1.
DT 27-MAR-2024, entry version 208.
DE RecName: Full=Tubulin beta-2A chain;
DE AltName: Full=Tubulin beta class IIa;
GN Name=TUBB2A; Synonyms=TUBB2;
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 [MRNA].
RC TISSUE=Skin;
RA Leffers H., Wiemann S., Ansorge W.;
RT "Cloning and vaccinia virus expression of a cDNA containing the complete
RT coding sequence of human beta tubulin mRNA.";
RL Submitted (JUN-1994) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA].
RA Banerjee A.;
RT "Class II beta tubulin sequence from MCF7 breast cancer cells.";
RL Submitted (OCT-2002) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RA Halleck A., Ebert L., Mkoundinya M., Schick M., Eisenstein S., Neubert P.,
RA Kstrang K., Schatten R., Shen B., Henze S., Mar W., Korn B., Zuo D., Hu Y.,
RA LaBaer J.;
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 [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 MRNA].
RC TISSUE=Eye, and Skin;
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 [6]
RP PROTEIN SEQUENCE OF 3-19; 47-58; 63-121; 163-174; 217-276; 283-306;
RP 310-318; 325-359; 363-379 AND 381-390, AND IDENTIFICATION BY MASS
RP 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 [7]
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 [8]
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 [9]
RP IDENTIFICATION IN A COMPLEX WITH HCFC1; MKI67; EMSY; MATR3; HSPA8; ZNF335;
RP CCAR2; ASH2L; RBBP5 AND WDR5.
RX PubMed=19131338; DOI=10.1074/jbc.m805872200;
RA Garapaty S., Xu C.F., Trojer P., Mahajan M.A., Neubert T.A., Samuels H.H.;
RT "Identification and characterization of a novel nuclear protein complex
RT involved in nuclear hormone receptor-mediated gene regulation.";
RL J. Biol. Chem. 284:7542-7552(2009).
RN [10]
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 [11]
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 [12]
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 [13]
RP VARIANT [LARGE SCALE ANALYSIS] TRP-62.
RX PubMed=16959974; DOI=10.1126/science.1133427;
RA Sjoeblom T., Jones S., Wood L.D., Parsons D.W., Lin J., Barber T.D.,
RA Mandelker D., Leary R.J., Ptak J., Silliman N., Szabo S., Buckhaults P.,
RA Farrell C., Meeh P., Markowitz S.D., Willis J., Dawson D., Willson J.K.V.,
RA Gazdar A.F., Hartigan J., Wu L., Liu C., Parmigiani G., Park B.H.,
RA Bachman K.E., Papadopoulos N., Vogelstein B., Kinzler K.W.,
RA Velculescu V.E.;
RT "The consensus coding sequences of human breast and colorectal cancers.";
RL Science 314:268-274(2006).
RN [14]
RP VARIANTS CDCBM5 LYS-247 AND VAL-248, AND CHARACTERIZATION OF VARIANTS
RP CDCBM5 LYS-247 AND VAL-248.
RX PubMed=24702957; DOI=10.1016/j.ajhg.2014.03.009;
RA Cushion T.D., Paciorkowski A.R., Pilz D.T., Mullins J.G., Seltzer L.E.,
RA Marion R.W., Tuttle E., Ghoneim D., Christian S.L., Chung S.K., Rees M.I.,
RA Dobyns W.B.;
RT "De novo mutations in the beta-tubulin gene TUBB2A cause simplified gyral
RT patterning and infantile-onset epilepsy.";
RL Am. J. Hum. Genet. 94:634-641(2014).
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.
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000250|UniProtKB:P68363};
CC -!- SUBUNIT: Interacts with ZNRF1 (By similarity). Part of a complex
CC composed at least of ASH2L, EMSY, HCFC1, HSPA8, CCAR2, MATR3, MKI67,
CC RBBP5, TUBB2A, WDR5 and ZNF335; this complex may have a histone H3-
CC specific methyltransferase activity (By similarity). Dimer of alpha and
CC beta chains. A typical microtubule is a hollow water-filled tube with
CC an outer 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.
CC {ECO:0000250, ECO:0000269|PubMed:19131338}.
CC -!- INTERACTION:
CC Q13885; Q96AP0: ACD; NbExp=2; IntAct=EBI-711595, EBI-717666;
CC Q13885; Q14457: BECN1; NbExp=3; IntAct=EBI-711595, EBI-949378;
CC Q13885; P55212: CASP6; NbExp=3; IntAct=EBI-711595, EBI-718729;
CC Q13885; P00533: EGFR; NbExp=2; IntAct=EBI-711595, EBI-297353;
CC Q13885; P05412: JUN; NbExp=5; IntAct=EBI-711595, EBI-852823;
CC Q13885; Q5S007: LRRK2; NbExp=3; IntAct=EBI-711595, EBI-5323863;
CC Q13885; P08247: SYP; NbExp=3; IntAct=EBI-711595, EBI-9071725;
CC Q13885; Q96MN9-2: ZNF488; NbExp=3; IntAct=EBI-711595, EBI-25831733;
CC -!- SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton {ECO:0000250}.
CC -!- TISSUE SPECIFICITY: High expression in brain, where it represents 30%
CC of all beta-tubulins. {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 5
CC (CDCBM5) [MIM:615763]: A disorder of aberrant neuronal migration and
CC disturbed axonal guidance. Clinical features include seizures, global
CC developmental delay, and various brain malformations such as a diffuse
CC simplified gyral pattern with reduced volume of white matter, globular
CC basal ganglia, thin and dysmorphic corpus callosum, mild brainstem
CC hypoplasia with a flat pons, mild cerebellar vermis hypoplasia, and
CC mildly enlarged posterior fossa. {ECO:0000269|PubMed:24702957}.
CC Note=The disease is caused by variants affecting the gene represented
CC in this entry.
CC -!- SIMILARITY: Belongs to the tubulin family. {ECO:0000305}.
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DR EMBL; X79535; CAA56071.1; -; mRNA.
DR EMBL; AY159127; AAN85571.1; -; mRNA.
DR EMBL; CR541958; CAG46756.1; -; mRNA.
DR EMBL; AL031963; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC001194; AAH01194.1; -; mRNA.
DR EMBL; BC018780; AAH18780.1; -; mRNA.
DR CCDS; CCDS4484.1; -.
DR PIR; T08726; T08726.
DR RefSeq; NP_001060.1; NM_001069.2.
DR RefSeq; NP_001297244.1; NM_001310315.1.
DR PDB; 7NVN; EM; 3.00 A; T=1-445.
DR PDBsum; 7NVN; -.
DR AlphaFoldDB; Q13885; -.
DR EMDB; EMD-12607; -.
DR SMR; Q13885; -.
DR BioGRID; 113131; 357.
DR IntAct; Q13885; 120.
DR MINT; Q13885; -.
DR STRING; 9606.ENSP00000369703; -.
DR ChEMBL; CHEMBL3797012; -.
DR DrugBank; DB05147; CYT997.
DR DrugBank; DB12695; Phenethyl Isothiocyanate.
DR DrugCentral; Q13885; -.
DR GlyGen; Q13885; 7 sites, 1 O-linked glycan (7 sites).
DR iPTMnet; Q13885; -.
DR MetOSite; Q13885; -.
DR PhosphoSitePlus; Q13885; -.
DR SwissPalm; Q13885; -.
DR BioMuta; TUBB2A; -.
DR DMDM; 74762137; -.
DR EPD; Q13885; -.
DR jPOST; Q13885; -.
DR MassIVE; Q13885; -.
DR MaxQB; Q13885; -.
DR PaxDb; 9606-ENSP00000369703; -.
DR PeptideAtlas; Q13885; -.
DR PRIDE; Q13885; -.
DR ProteomicsDB; 59713; -.
DR Pumba; Q13885; -.
DR TopDownProteomics; Q13885; -.
DR ABCD; Q13885; 1 sequenced antibody.
DR Antibodypedia; 9372; 425 antibodies from 31 providers.
DR DNASU; 7280; -.
DR Ensembl; ENST00000333628.4; ENSP00000369703.2; ENSG00000137267.7.
DR GeneID; 7280; -.
DR KEGG; hsa:7280; -.
DR MANE-Select; ENST00000333628.4; ENSP00000369703.2; NM_001069.3; NP_001060.1.
DR UCSC; uc003mvc.5; human.
DR AGR; HGNC:12412; -.
DR CTD; 7280; -.
DR DisGeNET; 7280; -.
DR GeneCards; TUBB2A; -.
DR GeneReviews; TUBB2A; -.
DR HGNC; HGNC:12412; TUBB2A.
DR HPA; ENSG00000137267; Group enriched (brain, skin).
DR MalaCards; TUBB2A; -.
DR MIM; 615101; gene.
DR MIM; 615763; phenotype.
DR neXtProt; NX_Q13885; -.
DR OpenTargets; ENSG00000137267; -.
DR PharmGKB; PA142670670; -.
DR VEuPathDB; HostDB:ENSG00000137267; -.
DR eggNOG; KOG1375; Eukaryota.
DR GeneTree; ENSGT00940000154150; -.
DR HOGENOM; CLU_015718_1_1_1; -.
DR InParanoid; Q13885; -.
DR OMA; DQMRSIQ; -.
DR OrthoDB; 3124041at2759; -.
DR PhylomeDB; Q13885; -.
DR TreeFam; TF300298; -.
DR PathwayCommons; Q13885; -.
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 Reactome; R-HSA-9833482; PKR-mediated signaling.
DR SignaLink; Q13885; -.
DR SIGNOR; Q13885; -.
DR BioGRID-ORCS; 7280; 20 hits in 1062 CRISPR screens.
DR ChiTaRS; TUBB2A; human.
DR GeneWiki; TUBB2A; -.
DR GenomeRNAi; 7280; -.
DR Pharos; Q13885; Tclin.
DR PRO; PR:Q13885; -.
DR Proteomes; UP000005640; Chromosome 6.
DR RNAct; Q13885; Protein.
DR Bgee; ENSG00000137267; Expressed in endothelial cell and 205 other cell types or tissues.
DR Genevisible; Q13885; HS.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0070062; C:extracellular exosome; HDA:UniProtKB.
DR GO; GO:1903561; C:extracellular vesicle; HDA:UniProtKB.
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:HPA.
DR GO; GO:0072686; C:mitotic spindle; IDA:HPA.
DR GO; GO:0005634; C:nucleus; HDA:UniProtKB.
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:0005200; F:structural constituent of cytoskeleton; IBA:GO_Central.
DR GO; GO:0021987; P:cerebral cortex development; IEA:Ensembl.
DR GO; GO:0000226; P:microtubule cytoskeleton organization; IBA:GO_Central.
DR GO; GO:0000278; P:mitotic cell cycle; IBA:GO_Central.
DR CDD; cd02187; beta_tubulin; 1.
DR Gene3D; 1.10.287.600; Helix hairpin bin; 1.
DR Gene3D; 3.30.1330.20; Tubulin/FtsZ, C-terminal domain; 1.
DR Gene3D; 3.40.50.1440; Tubulin/FtsZ, GTPase domain; 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 PANTHER; PTHR11588:SF488; TUBULIN BETA-2A CHAIN; 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 3D-structure; Acetylation; Cytoplasm; Cytoskeleton;
KW Direct protein sequencing; Disease variant; GTP-binding; Isopeptide bond;
KW Magnesium; Metal-binding; Methylation; Microtubule; Nucleotide-binding;
KW Phosphoprotein; Reference proteome; Ubl conjugation.
FT CHAIN 1..445
FT /note="Tubulin beta-2A chain"
FT /id="PRO_0000262648"
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 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 62
FT /note="R -> W (in a colorectal cancer sample; somatic
FT mutation; dbSNP:rs774124807)"
FT /evidence="ECO:0000269|PubMed:16959974"
FT /id="VAR_036197"
FT VARIANT 247
FT /note="N -> K (in CDCBM5; abolishes coassembly with tubulin
FT subunits and incorporation into the microtubule polymer
FT network; dbSNP:rs886037663)"
FT /evidence="ECO:0000269|PubMed:24702957"
FT /id="VAR_071168"
FT VARIANT 248
FT /note="A -> V (in CDCBM5; reduces coassembly with tubulin
FT subunits and incorporation into the microtubule polymer
FT network; dbSNP:rs2808001)"
FT /evidence="ECO:0000269|PubMed:24702957"
FT /id="VAR_071169"
FT CONFLICT 191
FT /note="Q -> H (in Ref. 2; AAN85571)"
FT /evidence="ECO:0000305"
FT CONFLICT 202
FT /note="I -> H (in Ref. 3; CAG46756)"
FT /evidence="ECO:0000305"
FT CONFLICT 263
FT /note="L -> V (in Ref. 3; CAG46756)"
FT /evidence="ECO:0000305"
FT STRAND 3..9
FT /evidence="ECO:0007829|PDB:7NVN"
FT HELIX 10..26
FT /evidence="ECO:0007829|PDB:7NVN"
FT HELIX 42..45
FT /evidence="ECO:0007829|PDB:7NVN"
FT TURN 48..50
FT /evidence="ECO:0007829|PDB:7NVN"
FT STRAND 51..53
FT /evidence="ECO:0007829|PDB:7NVN"
FT STRAND 57..61
FT /evidence="ECO:0007829|PDB:7NVN"
FT STRAND 63..69
FT /evidence="ECO:0007829|PDB:7NVN"
FT HELIX 70..78
FT /evidence="ECO:0007829|PDB:7NVN"
FT STRAND 83..85
FT /evidence="ECO:0007829|PDB:7NVN"
FT STRAND 89..92
FT /evidence="ECO:0007829|PDB:7NVN"
FT HELIX 101..105
FT /evidence="ECO:0007829|PDB:7NVN"
FT HELIX 113..124
FT /evidence="ECO:0007829|PDB:7NVN"
FT STRAND 128..141
FT /evidence="ECO:0007829|PDB:7NVN"
FT HELIX 142..158
FT /evidence="ECO:0007829|PDB:7NVN"
FT STRAND 162..169
FT /evidence="ECO:0007829|PDB:7NVN"
FT STRAND 178..180
FT /evidence="ECO:0007829|PDB:7NVN"
FT HELIX 181..195
FT /evidence="ECO:0007829|PDB:7NVN"
FT STRAND 197..201
FT /evidence="ECO:0007829|PDB:7NVN"
FT HELIX 204..215
FT /evidence="ECO:0007829|PDB:7NVN"
FT HELIX 223..228
FT /evidence="ECO:0007829|PDB:7NVN"
FT HELIX 230..236
FT /evidence="ECO:0007829|PDB:7NVN"
FT HELIX 374..391
FT /evidence="ECO:0007829|PDB:7NVN"
FT TURN 392..394
FT /evidence="ECO:0007829|PDB:7NVN"
FT HELIX 396..400
FT /evidence="ECO:0007829|PDB:7NVN"
FT HELIX 405..423
FT /evidence="ECO:0007829|PDB:7NVN"
SQ SEQUENCE 445 AA; 49907 MW; 93B3213EB2A9367B CRC64;
MREIVHIQAG QCGNQIGAKF WEVISDEHGI DPTGSYHGDS DLQLERINVY YNEAAGNKYV
PRAILVDLEP GTMDSVRSGP FGQIFRPDNF VFGQSGAGNN WAKGHYTEGA ELVDSVLDVV
RKESESCDCL QGFQLTHSLG GGTGSGMGTL LISKIREEYP DRIMNTFSVM PSPKVSDTVV
EPYNATLSVH QLVENTDETY SIDNEALYDI CFRTLKLTTP TYGDLNHLVS ATMSGVTTCL
RFPGQLNADL RKLAVNMVPF PRLHFFMPGF APLTSRGSQQ YRALTVPELT QQMFDSKNMM
AACDPRHGRY LTVAAIFRGR MSMKEVDEQM LNVQNKNSSY FVEWIPNNVK TAVCDIPPRG
LKMSATFIGN STAIQELFKR ISEQFTAMFR RKAFLHWYTG EGMDEMEFTE AESNMNDLVS
EYQQYQDATA DEQGEFEEEE GEDEA
//
