ID TBA1C_HUMAN Reviewed; 449 AA. AC Q9BQE3; DT 02-MAY-2002, integrated into UniProtKB/Swiss-Prot. DT 01-JUN-2001, sequence version 1. DT 27-MAR-2024, entry version 208. DE RecName: Full=Tubulin alpha-1C chain; DE EC=3.6.5.- {ECO:0000250|UniProtKB:P68363}; DE AltName: Full=Alpha-tubulin 6; DE AltName: Full=Tubulin alpha-6 chain; DE Contains: DE RecName: Full=Detyrosinated tubulin alpha-1C chain; GN Name=TUBA1C; Synonyms=TUBA6; 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]. RC TISSUE=Bone marrow, Duodenum, Lymph, 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 [2] RP PROTEIN SEQUENCE OF 65-79 AND 244-280, AND IDENTIFICATION BY MASS RP SPECTROMETRY. RC TISSUE=Brain, and Cajal-Retzius cell; RA Lubec G., Afjehi-Sadat L.; RL Submitted (MAR-2007) to UniProtKB. RN [3] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-439, AND IDENTIFICATION BY RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Cervix carcinoma; RX PubMed=17081983; DOI=10.1016/j.cell.2006.09.026; RA Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P., Mann M.; RT "Global, in vivo, and site-specific phosphorylation dynamics in signaling RT networks."; RL Cell 127:635-648(2006). RN [4] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-439, AND IDENTIFICATION BY RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Cervix carcinoma; RX PubMed=18691976; DOI=10.1016/j.molcel.2008.07.007; RA Daub H., Olsen J.V., Bairlein M., Gnad F., Oppermann F.S., Korner R., RA Greff Z., Keri G., Stemmann O., Mann M.; RT "Kinase-selective enrichment enables quantitative phosphoproteomics of the RT kinome across the cell cycle."; RL Mol. Cell 31:438-448(2008). RN [5] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-439, AND IDENTIFICATION BY RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Cervix carcinoma; RX PubMed=18669648; DOI=10.1073/pnas.0805139105; RA Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E., RA Elledge S.J., Gygi S.P.; RT "A quantitative atlas of mitotic phosphorylation."; RL Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008). RN [6] RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RX PubMed=19413330; DOI=10.1021/ac9004309; RA Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J., Mohammed S.; RT "Lys-N and trypsin cover complementary parts of the phosphoproteome in a RT refined SCX-based approach."; RL Anal. Chem. 81:4493-4501(2009). RN [7] 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 [8] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-432 AND SER-439, AND RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Leukemic T-cell; RX PubMed=19690332; DOI=10.1126/scisignal.2000007; RA Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K., RA Rodionov V., Han D.K.; RT "Quantitative phosphoproteomic analysis of T cell receptor signaling RT reveals system-wide modulation of protein-protein interactions."; RL Sci. Signal. 2:RA46-RA46(2009). RN [9] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-439, AND IDENTIFICATION BY RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Cervix carcinoma; RX PubMed=20068231; DOI=10.1126/scisignal.2000475; RA Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L., RA Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S., Mann M.; RT "Quantitative phosphoproteomics reveals widespread full phosphorylation RT site occupancy during mitosis."; RL Sci. Signal. 3:RA3-RA3(2010). RN [10] 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 [11] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-439, AND IDENTIFICATION BY RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RX PubMed=21406692; DOI=10.1126/scisignal.2001570; RA Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J., Johansen P.T., RA Kratchmarova I., Kassem M., Mann M., Olsen J.V., Blagoev B.; RT "System-wide temporal characterization of the proteome and phosphoproteome RT of human embryonic stem cell differentiation."; RL Sci. Signal. 4:RS3-RS3(2011). RN [12] RP ACETYLATION AT LYS-40. RX PubMed=24906155; DOI=10.1016/j.cell.2014.03.061; RA Szyk A., Deaconescu A.M., Spector J., Goodman B., Valenstein M.L., RA Ziolkowska N.E., Kormendi V., Grigorieff N., Roll-Mecak A.; RT "Molecular basis for age-dependent microtubule acetylation by tubulin RT acetyltransferase."; RL Cell 157:1405-1415(2014). RN [13] RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Liver; RX PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014; RA Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., Wang L., RA Ye M., Zou H.; RT "An enzyme assisted RP-RPLC approach for in-depth analysis of human liver RT phosphoproteome."; RL J. Proteomics 96:253-262(2014). RN [14] RP DETYROSINATION. RX PubMed=25908662; DOI=10.1126/science.aaa5175; RA Barisic M., Silva e Sousa R., Tripathy S.K., Magiera M.M., Zaytsev A.V., RA Pereira A.L., Janke C., Grishchuk E.L., Maiato H.; RT "Mitosis. Microtubule detyrosination guides chromosomes during mitosis."; RL Science 348:799-803(2015). RN [15] 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 [16] RP TYROSINATION. RX PubMed=26972003; DOI=10.1016/j.celrep.2016.02.046; RA Nirschl J.J., Magiera M.M., Lazarus J.E., Janke C., Holzbaur E.L.; RT "Alpha-tubulin tyrosination and CLIP-170 phosphorylation regulate the RT initiation of dynein-driven transport in neurons."; RL Cell Rep. 14:2637-2652(2016). RN [17] RP DETYROSINATION. RX PubMed=29146869; DOI=10.1126/science.aao5676; RA Nieuwenhuis J., Adamopoulos A., Bleijerveld O.B., Mazouzi A., Stickel E., RA Celie P., Altelaar M., Knipscheer P., Perrakis A., Blomen V.A., RA Brummelkamp T.R.; RT "Vasohibins encode tubulin detyrosinating activity."; RL Science 358:1453-1456(2017). RN [18] RP DETYROSINATION. RX PubMed=35482892; DOI=10.1126/science.abn6020; RA Landskron L., Bak J., Adamopoulos A., Kaplani K., Moraiti M., RA van den Hengel L.G., Song J.Y., Bleijerveld O.B., Nieuwenhuis J., RA Heidebrecht T., Henneman L., Moutin M.J., Barisic M., Taraviras S., RA Perrakis A., Brummelkamp T.R.; RT "Posttranslational modification of microtubules by the MATCAP RT detyrosinase."; RL Science 376:eabn6020-eabn6020(2022). 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 -!- 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. CC -!- INTERACTION: CC Q9BQE3; P13473-2: LAMP2; NbExp=3; IntAct=EBI-1103245, EBI-21591415; CC Q9BQE3; O75400-2: PRPF40A; NbExp=3; IntAct=EBI-1103245, EBI-5280197; CC Q9BQE3; Q9Y371: SH3GLB1; NbExp=3; IntAct=EBI-1103245, EBI-2623095; CC Q9BQE3; P13693: TPT1; NbExp=4; IntAct=EBI-1103245, EBI-1783169; CC Q9BQE3; P08670: VIM; NbExp=3; IntAct=EBI-1103245, EBI-353844; CC -!- SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton. CC -!- DOMAIN: The MREC motif may be critical for tubulin autoregulation. CC {ECO:0000250|UniProtKB:P68363}. 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: 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:24906155}. 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-449 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 (KIAA0895L/MATCAP, VASH1 or VASH2) and CC tubulin tyrosine ligase (TTL), respectively. CC {ECO:0000269|PubMed:25908662, ECO:0000269|PubMed:26972003, CC ECO:0000269|PubMed:29146869, ECO:0000269|PubMed:35482892}. CC -!- PTM: [Tubulin alpha-1C chain]: Tyrosination promotes microtubule CC interaction with CAP-Gly domain-containing proteins such as CLIP1, CC CLIP2 and DCTN1 (By similarity). Tyrosination regulates the initiation CC of dynein-dynactin motility via interaction with DCTN1, which brings CC the dynein-dynactin complex into contact with microtubules CC (PubMed:26972003). In neurons, tyrosinated tubulins mediate the CC initiation of retrograde vesicle transport (By similarity). CC {ECO:0000250|UniProtKB:P68369, ECO:0000250|UniProtKB:Q71U36, CC ECO:0000269|PubMed:26972003}. CC -!- PTM: [Detyrosinated tubulin alpha-1C 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 (PubMed:25908662). CC Detyrosination increases microtubules-dependent mechanotransduction in CC dystrophic cardiac and skeletal muscle. In cardiomyocytes, CC detyrosinated microtubules are required to resist to contractile CC compression during contraction: detyrosination promotes association CC with desmin (DES) at force-generating sarcomeres, leading to buckled CC microtubules and mechanical resistance to contraction (By similarity). CC {ECO:0000250|UniProtKB:P68373, ECO:0000269|PubMed:25908662}. 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; BC004949; AAH04949.1; -; mRNA. DR EMBL; BC005946; AAH05946.1; -; mRNA. DR EMBL; BC011790; AAH11790.1; -; mRNA. DR EMBL; BC019298; AAH19298.1; -; mRNA. DR EMBL; BC021088; AAH21088.1; -; mRNA. DR EMBL; BC051297; AAH51297.1; -; mRNA. DR EMBL; BC063036; AAH63036.1; -; mRNA. DR CCDS; CCDS8782.1; -. DR RefSeq; NP_116093.1; NM_032704.4. DR AlphaFoldDB; Q9BQE3; -. DR SMR; Q9BQE3; -. DR BioGRID; 124259; 491. DR IntAct; Q9BQE3; 227. DR MINT; Q9BQE3; -. DR STRING; 9606.ENSP00000443475; -. DR BindingDB; Q9BQE3; -. DR ChEMBL; CHEMBL3797011; -. 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 DrugBank; DB01873; Epothilone D. DR DrugBank; DB03010; Patupilone. DR DrugCentral; Q9BQE3; -. DR GlyCosmos; Q9BQE3; 18 sites, 1 glycan. DR GlyGen; Q9BQE3; 18 sites, 1 O-linked glycan (18 sites). DR iPTMnet; Q9BQE3; -. DR MetOSite; Q9BQE3; -. DR PhosphoSitePlus; Q9BQE3; -. DR SwissPalm; Q9BQE3; -. DR BioMuta; TUBA1C; -. DR DMDM; 20455322; -. DR REPRODUCTION-2DPAGE; Q9BQE3; -. DR EPD; Q9BQE3; -. DR jPOST; Q9BQE3; -. DR MassIVE; Q9BQE3; -. DR MaxQB; Q9BQE3; -. DR PaxDb; 9606-ENSP00000301072; -. DR PeptideAtlas; Q9BQE3; -. DR PRIDE; Q9BQE3; -. DR ProteomicsDB; 78661; -. DR Pumba; Q9BQE3; -. DR TopDownProteomics; Q9BQE3; -. DR Antibodypedia; 25908; 426 antibodies from 27 providers. DR DNASU; 84790; -. DR Ensembl; ENST00000301072.11; ENSP00000301072.7; ENSG00000167553.17. DR GeneID; 84790; -. DR KEGG; hsa:84790; -. DR MANE-Select; ENST00000301072.11; ENSP00000301072.7; NM_032704.5; NP_116093.1. DR UCSC; uc001rtt.2; human. DR AGR; HGNC:20768; -. DR CTD; 84790; -. DR DisGeNET; 84790; -. DR GeneCards; TUBA1C; -. DR HGNC; HGNC:20768; TUBA1C. DR HPA; ENSG00000167553; Tissue enhanced (esophagus). DR neXtProt; NX_Q9BQE3; -. DR OpenTargets; ENSG00000167553; -. DR PharmGKB; PA162407345; -. DR VEuPathDB; HostDB:ENSG00000167553; -. DR eggNOG; KOG1376; Eukaryota. DR GeneTree; ENSGT00950000182825; -. DR HOGENOM; CLU_015718_0_0_1; -. DR InParanoid; Q9BQE3; -. DR OMA; FYTRECI; -. DR OrthoDB; 4649019at2759; -. DR PhylomeDB; Q9BQE3; -. DR TreeFam; TF300314; -. DR PathwayCommons; Q9BQE3; -. 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; Q9BQE3; -. DR SIGNOR; Q9BQE3; -. DR BioGRID-ORCS; 84790; 699 hits in 1097 CRISPR screens. DR ChiTaRS; TUBA1C; human. DR GeneWiki; TUBA1C; -. DR GenomeRNAi; 84790; -. DR Pharos; Q9BQE3; Tchem. DR PRO; PR:Q9BQE3; -. DR Proteomes; UP000005640; Chromosome 12. DR RNAct; Q9BQE3; Protein. DR Bgee; ENSG00000167553; Expressed in secondary oocyte and 204 other cell types or tissues. DR ExpressionAtlas; Q9BQE3; baseline and differential. DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central. DR GO; GO:0005881; C:cytoplasmic microtubule; IEA:Ensembl. DR GO; GO:0005874; C:microtubule; IBA:GO_Central. DR GO; GO:0015630; C:microtubule cytoskeleton; IDA:HPA. DR GO; GO:0005634; C:nucleus; IDA:UniProtKB. DR GO; GO:0031982; C:vesicle; HDA:UniProtKB. DR GO; GO:0005525; F:GTP binding; IBA:GO_Central. DR GO; GO:0016787; F:hydrolase activity; IEA:UniProtKB-KW. 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:0005198; F:structural molecule activity; TAS:BHF-UCL. DR GO; GO:0051301; P:cell division; TAS:BHF-UCL. DR GO; GO:0030705; P:cytoskeleton-dependent intracellular transport; TAS:BHF-UCL. DR GO; GO:0000226; P:microtubule cytoskeleton organization; IBA:GO_Central. DR GO; GO:0007017; P:microtubule-based process; TAS:BHF-UCL. 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:SF298; TUBULIN ALPHA-1C 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. DR Genevisible; Q9BQE3; HS. PE 1: Evidence at protein level; KW Acetylation; Cytoplasm; Cytoskeleton; Direct protein sequencing; KW GTP-binding; Hydrolase; Magnesium; Metal-binding; Methylation; Microtubule; KW Nitration; Nucleotide-binding; Phosphoprotein; Reference proteome. FT CHAIN 1..449 FT /note="Tubulin alpha-1C chain" FT /id="PRO_0000048112" FT CHAIN 1..448 FT /note="Detyrosinated tubulin alpha-1C chain" FT /evidence="ECO:0000305|PubMed:25908662, FT ECO:0000305|PubMed:29146869" FT /id="PRO_0000437394" FT REGION 429..449 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 449 FT /note="Involved in polymerization" FT MOD_RES 40 FT /note="N6-acetyllysine" FT /evidence="ECO:0000269|PubMed:24906155" FT MOD_RES 282 FT /note="3'-nitrotyrosine" FT /evidence="ECO:0000250|UniProtKB:P68373" FT MOD_RES 432 FT /note="Phosphotyrosine" FT /evidence="ECO:0007744|PubMed:19690332" FT MOD_RES 439 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:17081983, FT ECO:0007744|PubMed:18669648, ECO:0007744|PubMed:18691976, FT ECO:0007744|PubMed:19690332, ECO:0007744|PubMed:20068231, FT ECO:0007744|PubMed:21406692" FT MOD_RES 449 FT /note="3'-nitrotyrosine" FT /evidence="ECO:0000250|UniProtKB:Q71U36" SQ SEQUENCE 449 AA; 49895 MW; 0CFE7212CB5E14F9 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 AYHEQLTVAE ITNACFEPAN QMVKCDPRHG KYMACCLLYR GDVVPKDVNA AIATIKTKRT IQFVDWCPTG FKVGINYQPP TVVPGGDLAK VQRAVCMLSN TTAVAEAWAR LDHKFDLMYA KRAFVHWYVG EGMEEGEFSE AREDMAALEK DYEEVGADSA DGEDEGEEY //