ID TBA1B_MOUSE Reviewed; 451 AA. AC P05213; Q3TY23; Q3U8B1; Q3UAW8; Q4KMW2; DT 13-AUG-1987, integrated into UniProtKB/Swiss-Prot. DT 23-NOV-2004, sequence version 2. DT 28-JUN-2023, entry version 216. DE RecName: Full=Tubulin alpha-1B chain; DE EC=3.6.5.- {ECO:0000250|UniProtKB:P68363}; DE AltName: Full=Alpha-tubulin 2; DE AltName: Full=Alpha-tubulin isotype M-alpha-2; DE AltName: Full=Tubulin alpha-2 chain; DE Contains: DE RecName: Full=Detyrosinated tubulin alpha-1B chain; GN Name=Tuba1b; Synonyms=Tuba2; 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=3785200; DOI=10.1128/mcb.6.7.2409-2419.1986; RA Villasante A., Wang D., Dobner P., Dolph P., Lewis S.A., Cowan N.J.; RT "Six mouse alpha-tubulin mRNAs encode five distinct isotypes: testis- RT specific expression of two sister genes."; RL Mol. Cell. Biol. 6:2409-2419(1986). RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. RC STRAIN=C57BL/6J, and NOD; RC TISSUE=Amnion, Bone marrow, Eye, Kidney, Liver, Thymus, and Visual cortex; 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 MRNA]. RC STRAIN=C57BL/6J, Czech II, and FVB/N; RC TISSUE=Limb, Mammary tumor, Olfactory epithelium, and Salivary gland; 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 [4] RP PROTEIN SEQUENCE OF 41-60; 65-79; 85-121; 157-163; 216-304; 312-320; RP 327-336; 340-370; 374-390; 395-401 AND 403-432, AND IDENTIFICATION BY MASS RP SPECTROMETRY. RC STRAIN=C57BL/6J, and OF1; TISSUE=Brain, and Hippocampus; RA Lubec G., Kang S.U., Klug S., Sunyer B., Chen W.-Q.; RL Submitted (JAN-2009) to UniProtKB. RN [5] RP NUCLEOTIDE SEQUENCE [MRNA] OF 100-451. 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 [6] RP PROTEIN SEQUENCE OF 440-448, AND GLUTAMYLATION AT GLU-445. RX PubMed=1967194; DOI=10.1126/science.1967194; RA Edde B., Rossier J., Le Caer J.P., Desbruyeres E., Gros F., Denoulet P.; RT "Posttranslational glutamylation of alpha-tubulin."; RL Science 247:83-85(1990). 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 TYROSINATION. RX PubMed=16954346; DOI=10.1083/jcb.200512058; RA Peris L., Thery M., Faure J., Saoudi Y., Lafanechere L., Chilton J.K., RA Gordon-Weeks P., Galjart N., Bornens M., Wordeman L., Wehland J., RA Andrieux A., Job D.; RT "Tubulin tyrosination is a major factor affecting the recruitment of CAP- RT Gly proteins at microtubule plus ends."; RL J. Cell Biol. 174:839-849(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 TYROSINATION. RX PubMed=19564401; DOI=10.1083/jcb.200902142; RA Peris L., Wagenbach M., Lafanechere L., Brocard J., Moore A.T., RA Kozielski F., Job D., Wordeman L., Andrieux A.; RT "Motor-dependent microtubule disassembly driven by tubulin tyrosination."; RL J. Cell Biol. 185:1159-1166(2009). RN [11] 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 [12] RP DETYROSINATION. RX PubMed=26446751; DOI=10.1038/ncomms9526; RA Kerr J.P., Robison P., Shi G., Bogush A.I., Kempema A.M., Hexum J.K., RA Becerra N., Harki D.A., Martin S.S., Raiteri R., Prosser B.L., Ward C.W.; RT "Detyrosinated microtubules modulate mechanotransduction in heart and RT skeletal muscle."; RL Nat. Commun. 6:8526-8526(2015). RN [13] RP DETYROSINATION. RX PubMed=27102488; DOI=10.1126/science.aaf0659; RA Robison P., Caporizzo M.A., Ahmadzadeh H., Bogush A.I., Chen C.Y., RA Margulies K.B., Shenoy V.B., Prosser B.L.; RT "Detyrosinated microtubules buckle and bear load in contracting RT cardiomyocytes."; RL Science 352:417-428(2016). RN [14] RP DETYROSINATION. RX PubMed=29146868; DOI=10.1126/science.aao4165; RA Aillaud C., Bosc C., Peris L., Bosson A., Heemeryck P., Van Dijk J., RA Le Friec J., Boulan B., Vossier F., Sanman L.E., Syed S., Amara N., RA Coute Y., Lafanechere L., Denarier E., Delphin C., Pelletier L., RA Humbert S., Bogyo M., Andrieux A., Rogowski K., Moutin M.J.; RT "Vasohibins/SVBP are tubulin carboxypeptidases (TCPs) that regulate neuron RT differentiation."; RL Science 358:1448-1453(2017). RN [15] 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. {ECO:0000250|UniProtKB:P68363}. CC -!- CATALYTIC ACTIVITY: CC Reaction=GTP + H2O = GDP + H(+) + phosphate; Xref=Rhea:RHEA:19669, CC ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:37565, CC ChEBI:CHEBI:43474, ChEBI:CHEBI:58189; CC Evidence={ECO:0000250|UniProtKB:P68363}; CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:19670; CC Evidence={ECO:0000250|UniProtKB:P68363}; 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. Nascent tubulin polypeptide interacts (via beta- CC tubulin MREC motif) with TTC5/STRAP; this interaction may result in CC tubulin mRNA-targeted degradation. {ECO:0000250|UniProtKB:P68363}. CC -!- SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton. CC -!- TISSUE SPECIFICITY: Ubiquitously expressed with highest levels in CC spleen, thymus and immature brain. CC -!- DOMAIN: The MREC motif mediates interaction with TTC5/STRAP and may be CC critical for tubulin autoregulation. {ECO:0000250|UniProtKB:P68363}. 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:1967194, PubMed:15890843). Polyglutamylation plays a key role CC in microtubule severing by spastin (SPAST). SPAST preferentially CC recognizes and acts on microtubules decorated with short polyglutamate CC tails: severing activity by SPAST increases as the number of glutamates CC per tubulin rises from one to eight, but decreases beyond this CC glutamylation threshold (By similarity). Glutamylation is also involved CC in cilia motility (PubMed:23897886). {ECO:0000250|UniProtKB:Q71U36, CC ECO:0000269|PubMed:15890843, ECO:0000269|PubMed:1967194, CC ECO:0000269|PubMed:23897886}. CC -!- PTM: Acetylation of alpha chains at Lys-40 is located inside the CC microtubule lumen. This modification has been correlated with increased CC microtubule stability, intracellular transport and ciliary assembly. CC {ECO:0000269|PubMed:16954346, ECO:0000269|PubMed:19564401}. CC -!- PTM: Methylation of alpha chains at Lys-40 is found in mitotic CC microtubules and is required for normal mitosis and cytokinesis CC contributing to genomic stability. {ECO:0000250|UniProtKB:P68363}. CC -!- PTM: Nitration of Tyr-451 is irreversible and interferes with normal CC dynein intracellular distribution. {ECO:0000250|UniProtKB:Q71U36}. CC -!- PTM: Undergoes a tyrosination/detyrosination cycle, the cyclic removal CC and re-addition of a C-terminal tyrosine residue by the enzymes tubulin CC tyrosine carboxypeptidase (MATCAP, VASH1 or VASH2) and tubulin tyrosine CC ligase (TTL), respectively. {ECO:0000269|PubMed:16954346, CC ECO:0000269|PubMed:19564401, ECO:0000269|PubMed:26446751, CC ECO:0000269|PubMed:27102488, ECO:0000269|PubMed:29146868}. CC -!- PTM: [Tubulin alpha-1B chain]: Tyrosination promotes microtubule CC interaction with CAP-Gly domain-containing proteins such as CLIP1, CC CLIP2 and DCTN1 (PubMed:16954346, PubMed:19564401). Tyrosination CC regulates the initiation of dynein-dynactin motility via interaction CC with DCTN1, which brings the dynein-dynactin complex into contact with CC microtubules. In neurons, tyrosinated tubulins mediate the initiation CC of retrograde vesicle transport (By similarity). CC {ECO:0000250|UniProtKB:Q71U36, ECO:0000269|PubMed:16954346, CC ECO:0000269|PubMed:19564401}. CC -!- PTM: [Detyrosinated tubulin alpha-1B chain]: Detyrosination is involved CC in metaphase plate congression by guiding chromosomes during mitosis: CC detyrosination promotes interaction with CENPE, promoting pole-proximal CC transport of chromosomes toward the equator (By similarity). CC Detyrosination increases microtubules-dependent mechanotransduction in CC dystrophic cardiac and skeletal muscle (PubMed:26446751). In CC cardiomyocytes, detyrosinated microtubules are required to resist to CC contractile compression during contraction: detyrosination promotes CC association with desmin (DES) at force-generating sarcomeres, leading CC to buckled microtubules and mechanical resistance to contraction CC (PubMed:27102488). {ECO:0000250|UniProtKB:P68363, CC ECO:0000269|PubMed:26446751, ECO:0000269|PubMed:27102488}. 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; M13446; AAA40500.1; -; mRNA. DR EMBL; AK075955; BAC36080.1; -; mRNA. DR EMBL; AK137885; BAE23512.1; -; mRNA. DR EMBL; AK150128; BAE29327.1; -; mRNA. DR EMBL; AK150179; BAE29362.1; -; mRNA. DR EMBL; AK150968; BAE29999.1; -; mRNA. DR EMBL; AK151199; BAE30196.1; -; mRNA. DR EMBL; AK151809; BAE30708.1; -; mRNA. DR EMBL; AK152298; BAE31107.1; -; mRNA. DR EMBL; AK153064; BAE31690.1; -; mRNA. DR EMBL; AK153254; BAE31845.1; -; mRNA. DR EMBL; AK158958; BAE34741.1; -; mRNA. DR EMBL; AK164428; BAE37783.1; -; mRNA. DR EMBL; AK168770; BAE40606.1; -; mRNA. DR EMBL; AK169075; BAE40860.1; -; mRNA. DR EMBL; AK169092; BAE40875.1; -; mRNA. DR EMBL; AK169130; BAE40909.1; -; mRNA. DR EMBL; AK169665; BAE41287.1; -; mRNA. DR EMBL; BC002219; AAH02219.1; -; mRNA. DR EMBL; BC008117; AAH08117.1; -; mRNA. DR EMBL; BC063777; AAH63777.1; -; mRNA. DR EMBL; BC083120; AAH83120.1; -; mRNA. DR EMBL; BC098321; AAH98321.1; -; mRNA. DR EMBL; BC108337; AAI08338.1; -; mRNA. DR EMBL; BC108394; AAI08395.1; -; mRNA. DR EMBL; M28727; AAA40507.1; -; mRNA. DR CCDS; CCDS37195.1; -. DR PIR; I77425; I77425. DR PIR; S29013; A61275. DR RefSeq; NP_035784.1; NM_011654.2. DR AlphaFoldDB; P05213; -. DR SMR; P05213; -. DR BioGRID; 204373; 51. DR CORUM; P05213; -. DR IntAct; P05213; 21. DR MINT; P05213; -. DR STRING; 10090.ENSMUSP00000076777; -. DR GlyGen; P05213; 1 site, 1 O-linked glycan (1 site). DR iPTMnet; P05213; -. DR PhosphoSitePlus; P05213; -. DR SwissPalm; P05213; -. DR REPRODUCTION-2DPAGE; P05213; -. DR EPD; P05213; -. DR jPOST; P05213; -. DR MaxQB; P05213; -. DR PaxDb; P05213; -. DR PeptideAtlas; P05213; -. DR TopDownProteomics; P05213; -. DR ABCD; P05213; 1 sequenced antibody. DR Antibodypedia; 3156; 719 antibodies from 41 providers. DR DNASU; 22143; -. DR Ensembl; ENSMUST00000077577; ENSMUSP00000076777; ENSMUSG00000023004. DR GeneID; 22143; -. DR KEGG; mmu:22143; -. DR UCSC; uc007xoj.1; mouse. DR AGR; MGI:107804; -. DR CTD; 10376; -. DR MGI; MGI:107804; Tuba1b. DR VEuPathDB; HostDB:ENSMUSG00000023004; -. DR eggNOG; KOG1376; Eukaryota. DR GeneTree; ENSGT00950000182825; -. DR HOGENOM; CLU_015718_0_0_1; -. DR InParanoid; P05213; -. DR OMA; ESCYDIC; -. DR OrthoDB; 899149at2759; -. DR PhylomeDB; P05213; -. DR TreeFam; TF300314; -. 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-9013407; RHOH GTPase cycle. 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; 22143; 15 hits in 45 CRISPR screens. DR ChiTaRS; Tuba1b; mouse. DR PRO; PR:P05213; -. DR Proteomes; UP000000589; Chromosome 15. DR RNAct; P05213; protein. DR Bgee; ENSMUSG00000023004; Expressed in ventricular zone and 66 other tissues. DR Genevisible; P05213; MM. DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central. DR GO; GO:0005881; C:cytoplasmic microtubule; IDA:MGI. DR GO; GO:0005829; C:cytosol; TAS:Reactome. 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:0043209; C:myelin sheath; HDA:UniProtKB. DR GO; GO:0003725; F:double-stranded RNA binding; ISO:MGI. DR GO; GO:0005525; F:GTP binding; ISS:UniProtKB. DR GO; GO:0003924; F:GTPase activity; ISS:UniProtKB. DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW. 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:0071353; P:cellular response to interleukin-4; IDA:MGI. DR GO; GO:0000226; P:microtubule cytoskeleton organization; IDA:MGI. DR GO; GO:0000278; P:mitotic cell cycle; IBA:GO_Central. DR CDD; cd02186; alpha_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; IPR002452; Alpha_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:SF251; TUBULIN ALPHA-1B CHAIN; 1. DR Pfam; PF00091; Tubulin; 1. DR Pfam; PF03953; Tubulin_C; 1. DR PRINTS; PR01162; ALPHATUBULIN. 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. PE 1: Evidence at protein level; KW Acetylation; Cytoplasm; Cytoskeleton; Direct protein sequencing; KW GTP-binding; Hydrolase; Isopeptide bond; Magnesium; Metal-binding; KW Methylation; Microtubule; Nitration; Nucleotide-binding; Phosphoprotein; KW Reference proteome; Ubl conjugation. FT CHAIN 1..451 FT /note="Tubulin alpha-1B chain" FT /id="PRO_0000048121" FT CHAIN 1..450 FT /note="Detyrosinated tubulin alpha-1B chain" FT /evidence="ECO:0000305|PubMed:26446751, FT ECO:0000305|PubMed:27102488, ECO:0000305|PubMed:29146868" FT /id="PRO_0000437387" FT REGION 432..451 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT MOTIF 1..4 FT /note="MREC motif" FT /evidence="ECO:0000250|UniProtKB:P68363" FT ACT_SITE 254 FT /evidence="ECO:0000250|UniProtKB:P68363" FT BINDING 11 FT /ligand="GTP" FT /ligand_id="ChEBI:CHEBI:37565" FT /evidence="ECO:0000250|UniProtKB:P68363" FT BINDING 71 FT /ligand="GTP" FT /ligand_id="ChEBI:CHEBI:37565" FT /evidence="ECO:0000250|UniProtKB:P68363" FT BINDING 71 FT /ligand="Mg(2+)" FT /ligand_id="ChEBI:CHEBI:18420" FT /evidence="ECO:0000250|UniProtKB:P68363" FT BINDING 140 FT /ligand="GTP" FT /ligand_id="ChEBI:CHEBI:37565" FT /evidence="ECO:0000250|UniProtKB:P68363" FT BINDING 144 FT /ligand="GTP" FT /ligand_id="ChEBI:CHEBI:37565" FT /evidence="ECO:0000250|UniProtKB:P68363" FT BINDING 145 FT /ligand="GTP" FT /ligand_id="ChEBI:CHEBI:37565" FT /evidence="ECO:0000250|UniProtKB:P68363" FT BINDING 179 FT /ligand="GTP" FT /ligand_id="ChEBI:CHEBI:37565" FT /evidence="ECO:0000250|UniProtKB:P68363" FT BINDING 206 FT /ligand="GTP" FT /ligand_id="ChEBI:CHEBI:37565" FT /evidence="ECO:0000250|UniProtKB:P68363" FT BINDING 228 FT /ligand="GTP" FT /ligand_id="ChEBI:CHEBI:37565" FT /evidence="ECO:0000250|UniProtKB:P68363" FT SITE 451 FT /note="Involved in polymerization" FT MOD_RES 40 FT /note="N6,N6,N6-trimethyllysine; alternate" FT /evidence="ECO:0000250|UniProtKB:P68363" FT MOD_RES 40 FT /note="N6-acetyllysine; alternate" FT /evidence="ECO:0000250|UniProtKB:P68363" FT MOD_RES 48 FT /note="Phosphoserine" FT /evidence="ECO:0000250|UniProtKB:P68363" FT MOD_RES 232 FT /note="Phosphoserine" FT /evidence="ECO:0000250|UniProtKB:P68363" FT MOD_RES 282 FT /note="3'-nitrotyrosine" FT /evidence="ECO:0000250|UniProtKB:P68373" FT MOD_RES 339 FT /note="Omega-N-methylarginine" FT /evidence="ECO:0000250|UniProtKB:P68363" FT MOD_RES 439 FT /note="Phosphoserine" FT /evidence="ECO:0000250|UniProtKB:P68373" FT MOD_RES 443 FT /note="5-glutamyl polyglutamate" FT /evidence="ECO:0000250|UniProtKB:P68363" FT MOD_RES 445 FT /note="5-glutamyl polyglutamate" FT /evidence="ECO:0000269|PubMed:1967194" FT MOD_RES 451 FT /note="3'-nitrotyrosine" FT /evidence="ECO:0000250|UniProtKB:Q71U36" FT CROSSLNK 326 FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with FT G-Cter in ubiquitin)" FT /evidence="ECO:0000250|UniProtKB:P68363" FT CROSSLNK 370 FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with FT G-Cter in ubiquitin)" FT /evidence="ECO:0000250|UniProtKB:P68363" FT CONFLICT 55 FT /note="E -> G (in Ref. 2; BAE30708/BAE31107)" FT /evidence="ECO:0000305" FT CONFLICT 114 FT /note="I -> T (in Ref. 2; BAE34741)" FT /evidence="ECO:0000305" FT CONFLICT 119 FT /note="L -> P (in Ref. 2; BAE29999/BAE30196)" FT /evidence="ECO:0000305" FT CONFLICT 135..136 FT /note="FL -> LF (in Ref. 5; AAA40507)" FT /evidence="ECO:0000305" FT CONFLICT 340 FT /note="S -> T (in Ref. 1 and 5; AAA40507)" FT /evidence="ECO:0000305" SQ SEQUENCE 451 AA; 50152 MW; 94355B4EC2086429 CRC64; MRECISIHVG QAGVQIGNAC WELYCLEHGI QPDGQMPSDK TIGGGDDSFN TFFSETGAGK HVPRAVFVDL EPTVIDEVRT GTYRQLFHPE QLITGKEDAA NNYARGHYTI GKEIIDLVLD RIRKLADQCT GLQGFLVFHS FGGGTGSGFT SLLMERLSVD YGKKSKLEFS IYPAPQVSTA VVEPYNSILT THTTLEHSDC AFMVDNEAIY DICRRNLDIE RPTYTNLNRL ISQIVSSITA SLRFDGALNV DLTEFQTNLV PYPRIHFPLA TYAPVISAEK AYHEQLSVAE ITNACFEPAN QMVKCDPRHG KYMACCLLYR GDVVPKDVNA AIATIKTKRS IQFVDWCPTG FKVGINYQPP TVVPGGDLAK VQRAVCMLSN TTAIAEAWAR LDHKFDLMYA KRAFVHWYVG EGMEEGEFSE AREDMAALEK DYEEVGVDSV EGEGEEEGEE Y //