TBA1C_HUMAN
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 03-AUG-2022, entry version 199.
DE RecName: Full=Tubulin alpha-1C chain;
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).
CC -!- FUNCTION: Tubulin is the major constituent of microtubules. It binds
CC two moles of GTP, one at an exchangeable site on the beta chain and one
CC at a non-exchangeable site on the alpha chain.
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 (VASH1 or VASH2) and tubulin tyrosine ligase
CC (TTL), respectively. {ECO:0000269|PubMed:25908662,
CC ECO:0000269|PubMed:26972003, ECO:0000269|PubMed:29146869}.
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}.
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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; 446.
DR IntAct; Q9BQE3; 226.
DR MINT; Q9BQE3; -.
DR STRING; 9606.ENSP00000301072; -.
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 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; Q9BQE3; -.
DR PeptideAtlas; Q9BQE3; -.
DR PRIDE; Q9BQE3; -.
DR ProteomicsDB; 78661; -.
DR TopDownProteomics; Q9BQE3; -.
DR Antibodypedia; 25908; 369 antibodies from 26 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 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 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 SignaLink; Q9BQE3; -.
DR SIGNOR; Q9BQE3; -.
DR BioGRID-ORCS; 84790; 674 hits in 1020 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 202 other tissues.
DR ExpressionAtlas; Q9BQE3; baseline and differential.
DR Genevisible; Q9BQE3; HS.
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: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 Gene3D; 1.10.287.600; -; 1.
DR Gene3D; 3.30.1330.20; -; 1.
DR Gene3D; 3.40.50.1440; -; 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; PTHR11588; 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; SSF52490; SSF52490; 1.
DR SUPFAM; SSF55307; SSF55307; 1.
DR PROSITE; PS00227; TUBULIN; 1.
PE 1: Evidence at protein level;
KW Acetylation; Cytoplasm; Cytoskeleton; Direct protein sequencing;
KW GTP-binding; Methylation; Microtubule; Nitration; Nucleotide-binding;
KW 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 BINDING 142..148
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000255"
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
