TBA1A_HUMAN
ID TBA1A_HUMAN Reviewed; 451 AA.
AC Q71U36; A8K0B8; G3V1U9; P04687; P05209;
DT 13-AUG-1987, integrated into UniProtKB/Swiss-Prot.
DT 05-JUL-2004, sequence version 1.
DT 03-AUG-2022, entry version 180.
DE RecName: Full=Tubulin alpha-1A chain;
DE AltName: Full=Alpha-tubulin 3;
DE AltName: Full=Tubulin B-alpha-1;
DE AltName: Full=Tubulin alpha-3 chain;
DE Contains:
DE RecName: Full=Detyrosinated tubulin alpha-1A chain;
GN Name=TUBA1A; Synonyms=TUBA3;
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 [GENOMIC DNA].
RX PubMed=3839072; DOI=10.1093/nar/13.1.207;
RA Hall J.L., Cowan N.J.;
RT "Structural features and restricted expression of a human alpha-tubulin
RT gene.";
RL Nucleic Acids Res. 13:207-223(1985).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
RC TISSUE=Retina;
RX PubMed=11504633; DOI=10.1016/s0968-0896(01)00103-1;
RA Crabtree D.V., Ojima I., Geng X., Adler A.J.;
RT "Tubulins in the primate retina: evidence that xanthophylls may be
RT endogenous ligands for the paclitaxel-binding site.";
RL Bioorg. Med. Chem. 9:1967-1976(2001).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=Cerebellum;
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=16541075; DOI=10.1038/nature04569;
RA Scherer S.E., Muzny D.M., Buhay C.J., Chen R., Cree A., Ding Y.,
RA Dugan-Rocha S., Gill R., Gunaratne P., Harris R.A., Hawes A.C.,
RA Hernandez J., Hodgson A.V., Hume J., Jackson A., Khan Z.M., Kovar-Smith C.,
RA Lewis L.R., Lozado R.J., Metzker M.L., Milosavljevic A., Miner G.R.,
RA Montgomery K.T., Morgan M.B., Nazareth L.V., Scott G., Sodergren E.,
RA Song X.-Z., Steffen D., Lovering R.C., Wheeler D.A., Worley K.C., Yuan Y.,
RA Zhang Z., Adams C.Q., Ansari-Lari M.A., Ayele M., Brown M.J., Chen G.,
RA Chen Z., Clerc-Blankenburg K.P., Davis C., Delgado O., Dinh H.H.,
RA Draper H., Gonzalez-Garay M.L., Havlak P., Jackson L.R., Jacob L.S.,
RA Kelly S.H., Li L., Li Z., Liu J., Liu W., Lu J., Maheshwari M.,
RA Nguyen B.-V., Okwuonu G.O., Pasternak S., Perez L.M., Plopper F.J.H.,
RA Santibanez J., Shen H., Tabor P.E., Verduzco D., Waldron L., Wang Q.,
RA Williams G.A., Zhang J., Zhou J., Allen C.C., Amin A.G., Anyalebechi V.,
RA Bailey M., Barbaria J.A., Bimage K.E., Bryant N.P., Burch P.E.,
RA Burkett C.E., Burrell K.L., Calderon E., Cardenas V., Carter K., Casias K.,
RA Cavazos I., Cavazos S.R., Ceasar H., Chacko J., Chan S.N., Chavez D.,
RA Christopoulos C., Chu J., Cockrell R., Cox C.D., Dang M., Dathorne S.R.,
RA David R., Davis C.M., Davy-Carroll L., Deshazo D.R., Donlin J.E.,
RA D'Souza L., Eaves K.A., Egan A., Emery-Cohen A.J., Escotto M., Flagg N.,
RA Forbes L.D., Gabisi A.M., Garza M., Hamilton C., Henderson N.,
RA Hernandez O., Hines S., Hogues M.E., Huang M., Idlebird D.G., Johnson R.,
RA Jolivet A., Jones S., Kagan R., King L.M., Leal B., Lebow H., Lee S.,
RA LeVan J.M., Lewis L.C., London P., Lorensuhewa L.M., Loulseged H.,
RA Lovett D.A., Lucier A., Lucier R.L., Ma J., Madu R.C., Mapua P.,
RA Martindale A.D., Martinez E., Massey E., Mawhiney S., Meador M.G.,
RA Mendez S., Mercado C., Mercado I.C., Merritt C.E., Miner Z.L., Minja E.,
RA Mitchell T., Mohabbat F., Mohabbat K., Montgomery B., Moore N., Morris S.,
RA Munidasa M., Ngo R.N., Nguyen N.B., Nickerson E., Nwaokelemeh O.O.,
RA Nwokenkwo S., Obregon M., Oguh M., Oragunye N., Oviedo R.J., Parish B.J.,
RA Parker D.N., Parrish J., Parks K.L., Paul H.A., Payton B.A., Perez A.,
RA Perrin W., Pickens A., Primus E.L., Pu L.-L., Puazo M., Quiles M.M.,
RA Quiroz J.B., Rabata D., Reeves K., Ruiz S.J., Shao H., Sisson I.,
RA Sonaike T., Sorelle R.P., Sutton A.E., Svatek A.F., Svetz L.A.,
RA Tamerisa K.S., Taylor T.R., Teague B., Thomas N., Thorn R.D., Trejos Z.Y.,
RA Trevino B.K., Ukegbu O.N., Urban J.B., Vasquez L.I., Vera V.A.,
RA Villasana D.M., Wang L., Ward-Moore S., Warren J.T., Wei X., White F.,
RA Williamson A.L., Wleczyk R., Wooden H.S., Wooden S.H., Yen J., Yoon L.,
RA Yoon V., Zorrilla S.E., Nelson D., Kucherlapati R., Weinstock G.,
RA Gibbs R.A.;
RT "The finished DNA sequence of human chromosome 12.";
RL Nature 440:346-351(2006).
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] (ISOFORM 1).
RC TISSUE=Muscle, 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 [7]
RP PROTEIN SEQUENCE OF 41-60; 65-79; 85-105; 113-121; 157-163; 216-304;
RP 312-320; 327-336; 340-352; 374-390; 395-401 AND 403-430, AND IDENTIFICATION
RP 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 NUCLEOTIDE SEQUENCE [MRNA] OF 110-451.
RC TISSUE=Fetal brain;
RX PubMed=6646120; DOI=10.1128/mcb.3.10.1738-1745.1983;
RA Cowan N.J., Dobner P., Fuchs E.V., Cleveland D.W.;
RT "Expression of human alpha-tubulin genes: interspecies conservation of 3'
RT untranslated regions.";
RL Mol. Cell. Biol. 3:1738-1745(1983).
RN [9]
RP PROTEIN SEQUENCE OF 439-451, AND NITRATION AT TYR-451.
RX PubMed=10339593; DOI=10.1073/pnas.96.11.6365;
RA Eiserich J.P., Estevez A.G., Bamberg T.V., Ye Y.Z., Chumley P.H.,
RA Beckman J.S., Freeman B.A.;
RT "Microtubule dysfunction by posttranslational nitrotyrosination of alpha-
RT tubulin: a nitric oxide-dependent mechanism of cellular injury.";
RL Proc. Natl. Acad. Sci. U.S.A. 96:6365-6370(1999).
RN [10]
RP TISSUE SPECIFICITY, AND VARIANTS LIS3 LEU-188; THR-263; CYS-264; PHE-286;
RP HIS-402; CYS-402 AND LEU-419.
RX PubMed=17584854; DOI=10.1002/humu.20572;
RA Poirier K., Keays D.A., Francis F., Saillour Y., Bahi N., Manouvrier S.,
RA Fallet-Bianco C., Pasquier L., Toutain A., Tuy F.P., Bienvenu T.,
RA Joriot S., Odent S., Ville D., Desguerre I., Goldenberg A., Moutard M.L.,
RA Fryns J.-P., van Esch H., Harvey R.J., Siebold C., Flint J., Beldjord C.,
RA Chelly J.;
RT "Large spectrum of lissencephaly and pachygyria phenotypes resulting from
RT de novo missense mutations in tubulin alpha 1A (TUBA1A).";
RL Hum. Mutat. 28:1055-1064(2007).
RN [11]
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 [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 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 [14]
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 [15]
RP INTERACTION WITH SETD2.
RX PubMed=27518565; DOI=10.1016/j.cell.2016.07.005;
RA Park I.Y., Powell R.T., Tripathi D.N., Dere R., Ho T.H., Blasius T.L.,
RA Chiang Y.C., Davis I.J., Fahey C.C., Hacker K.E., Verhey K.J.,
RA Bedford M.T., Jonasch E., Rathmell W.K., Walker C.L.;
RT "Dual chromatin and cytoskeletal remodeling by SETD2.";
RL Cell 166:950-962(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 TYROSINATION.
RX PubMed=26968983; DOI=10.15252/embj.201593071;
RA McKenney R.J., Huynh W., Vale R.D., Sirajuddin M.;
RT "Tyrosination of alpha-tubulin controls the initiation of processive
RT dynein-dynactin motility.";
RL EMBO J. 35:1175-1185(2016).
RN [18]
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 [19]
RP GLUTAMYLATION AT GLU-443.
RX PubMed=32747782; DOI=10.1038/s41594-020-0462-0;
RA Mahalingan K.K., Keith Keenan E., Strickland M., Li Y., Liu Y., Ball H.L.,
RA Tanner M.E., Tjandra N., Roll-Mecak A.;
RT "Structural basis for polyglutamate chain initiation and elongation by TTLL
RT family enzymes.";
RL Nat. Struct. Mol. Biol. 27:802-813(2020).
RN [20]
RP VARIANT LIS3 LEU-402.
RX PubMed=25818041; DOI=10.1111/epi.12954;
RA Mercimek-Mahmutoglu S., Patel J., Cordeiro D., Hewson S., Callen D.,
RA Donner E.J., Hahn C.D., Kannu P., Kobayashi J., Minassian B.A., Moharir M.,
RA Siriwardena K., Weiss S.K., Weksberg R., Snead O.C. III;
RT "Diagnostic yield of genetic testing in epileptic encephalopathy in
RT childhood.";
RL Epilepsia 56:707-716(2015).
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. Interacts with SETD2; the interaction is independent
CC on alpha-tubulin acetylation on Lys-40.
CC -!- INTERACTION:
CC Q71U36; P05067: APP; NbExp=3; IntAct=EBI-302552, EBI-77613;
CC Q71U36; P30622-2: CLIP1; NbExp=3; IntAct=EBI-302552, EBI-6479976;
CC Q71U36; Q9NQC7: CYLD; NbExp=6; IntAct=EBI-302552, EBI-2117940;
CC Q71U36; P00533: EGFR; NbExp=4; IntAct=EBI-302552, EBI-297353;
CC Q71U36; P42858: HTT; NbExp=3; IntAct=EBI-302552, EBI-466029;
CC Q71U36; P05412: JUN; NbExp=3; IntAct=EBI-302552, EBI-852823;
CC Q71U36; P10636-8: MAPT; NbExp=4; IntAct=EBI-302552, EBI-366233;
CC Q71U36; Q71U36: TUBA1A; NbExp=5; IntAct=EBI-302552, EBI-302552;
CC Q71U36; P07437: TUBB; NbExp=4; IntAct=EBI-302552, EBI-350864;
CC -!- SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q71U36-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q71U36-2; Sequence=VSP_046782;
CC -!- TISSUE SPECIFICITY: Expressed at a high level in fetal brain.
CC {ECO:0000269|PubMed:17584854}.
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-451 is irreversible and interferes with normal
CC dynein intracellular distribution. {ECO:0000269|PubMed:10339593}.
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:26968983, ECO:0000269|PubMed:26972003,
CC ECO:0000269|PubMed:29146869}.
CC -!- PTM: [Tubulin alpha-1A chain]: Tyrosination promotes microtubule
CC interaction with CAP-Gly domain-containing proteins such as CLIP1,
CC CLIP2 and DCTN1. Tyrosination regulates the initiation of dynein-
CC dynactin motility via interaction with DCTN1, which brings the dynein-
CC dynactin complex into contact with microtubules (PubMed:26972003,
CC PubMed:26968983). In neurons, tyrosinated tubulins mediate the
CC initiation of retrograde vesicle transport (PubMed:26968983).
CC {ECO:0000269|PubMed:26968983, ECO:0000269|PubMed:26972003}.
CC -!- PTM: [Detyrosinated tubulin alpha-1A 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:P68369, ECO:0000269|PubMed:25908662}.
CC -!- DISEASE: Lissencephaly 3 (LIS3) [MIM:611603]: A classic type
CC lissencephaly associated with psychomotor retardation and seizures.
CC Features include agyria or pachygyria or laminar heterotopia, severe
CC intellectual disability, motor delay, variable presence of seizures,
CC and abnormalities of corpus callosum, hippocampus, cerebellar vermis
CC and brainstem. {ECO:0000269|PubMed:17584854,
CC ECO:0000269|PubMed:25818041}. Note=The disease is caused by variants
CC affecting the gene represented in this entry.
CC -!- SIMILARITY: Belongs to the tubulin family. {ECO:0000305}.
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DR EMBL; X01703; CAA25855.1; -; Genomic_DNA.
DR EMBL; AF141347; AAD33871.1; -; mRNA.
DR EMBL; AK289483; BAF82172.1; -; mRNA.
DR EMBL; AC010173; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH471111; EAW58052.1; -; Genomic_DNA.
DR EMBL; CH471111; EAW58054.1; -; Genomic_DNA.
DR EMBL; CH471111; EAW58055.1; -; Genomic_DNA.
DR EMBL; BC006468; AAH06468.1; -; mRNA.
DR EMBL; BC050637; AAH50637.1; -; mRNA.
DR EMBL; K00557; AAA91575.1; -; mRNA.
DR CCDS; CCDS58226.1; -. [Q71U36-2]
DR CCDS; CCDS58227.1; -. [Q71U36-1]
DR CCDS; CCDS8781.1; -. [Q71U36-1]
DR RefSeq; NP_001257328.1; NM_001270399.1. [Q71U36-1]
DR RefSeq; NP_001257329.1; NM_001270400.1. [Q71U36-2]
DR RefSeq; NP_006000.2; NM_006009.3. [Q71U36-1]
DR PDB; 5JCO; EM; 4.00 A; A/B/E/F/G/H=1-437.
DR PDB; 6J8F; X-ray; 2.28 A; C=444-451.
DR PDB; 6WSL; EM; 3.10 A; A/E=1-451.
DR PDB; 7C1M; NMR; -; B=440-451.
DR PDBsum; 5JCO; -.
DR PDBsum; 6J8F; -.
DR PDBsum; 6WSL; -.
DR PDBsum; 7C1M; -.
DR AlphaFoldDB; Q71U36; -.
DR SASBDB; Q71U36; -.
DR SMR; Q71U36; -.
DR BioGRID; 113603; 939.
DR CORUM; Q71U36; -.
DR DIP; DIP-32773N; -.
DR ELM; Q71U36; -.
DR IntAct; Q71U36; 406.
DR MINT; Q71U36; -.
DR STRING; 9606.ENSP00000301071; -.
DR ChEMBL; CHEMBL3661; -.
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; DB00518; Albendazole.
DR DrugBank; DB11638; Artenimol.
DR DrugBank; DB15534; Colchiceine.
DR DrugBank; DB05147; CYT997.
DR DrugBank; DB01873; Epothilone D.
DR DrugBank; DB00643; Mebendazole.
DR DrugBank; DB03010; Patupilone.
DR DrugBank; DB12695; Phenethyl Isothiocyanate.
DR DrugBank; DB00570; Vinblastine.
DR DrugCentral; Q71U36; -.
DR TCDB; 8.A.173.1.1; the tubulin (tubulin) family.
DR GlyGen; Q71U36; 1 site, 1 O-linked glycan (1 site).
DR iPTMnet; Q71U36; -.
DR PhosphoSitePlus; Q71U36; -.
DR SwissPalm; Q71U36; -.
DR BioMuta; TUBA1A; -.
DR DMDM; 55977864; -.
DR EPD; Q71U36; -.
DR jPOST; Q71U36; -.
DR MassIVE; Q71U36; -.
DR MaxQB; Q71U36; -.
DR PaxDb; Q71U36; -.
DR PeptideAtlas; Q71U36; -.
DR PRIDE; Q71U36; -.
DR TopDownProteomics; Q71U36-1; -. [Q71U36-1]
DR Antibodypedia; 3282; 680 antibodies from 39 providers.
DR DNASU; 7846; -.
DR Ensembl; ENST00000295766.9; ENSP00000439020.2; ENSG00000167552.15. [Q71U36-1]
DR Ensembl; ENST00000301071.12; ENSP00000301071.7; ENSG00000167552.15. [Q71U36-1]
DR Ensembl; ENST00000547939.6; ENSP00000450268.2; ENSG00000167552.15. [Q71U36-2]
DR Ensembl; ENST00000550767.6; ENSP00000446637.1; ENSG00000167552.15. [Q71U36-2]
DR Ensembl; ENST00000552924.2; ENSP00000448725.2; ENSG00000167552.15. [Q71U36-2]
DR GeneID; 7846; -.
DR KEGG; hsa:7846; -.
DR MANE-Select; ENST00000301071.12; ENSP00000301071.7; NM_006009.4; NP_006000.2.
DR UCSC; uc001rtp.5; human. [Q71U36-1]
DR CTD; 7846; -.
DR DisGeNET; 7846; -.
DR GeneCards; TUBA1A; -.
DR GeneReviews; TUBA1A; -.
DR HGNC; HGNC:20766; TUBA1A.
DR HPA; ENSG00000167552; Tissue enhanced (brain).
DR MalaCards; TUBA1A; -.
DR MIM; 602529; gene.
DR MIM; 611603; phenotype.
DR neXtProt; NX_Q71U36; -.
DR OpenTargets; ENSG00000167552; -.
DR Orphanet; 171680; Lissencephaly due to TUBA1A mutation.
DR Orphanet; 467166; Tubulinopathy-associated dysgyria.
DR PharmGKB; PA162407319; -.
DR VEuPathDB; HostDB:ENSG00000167552; -.
DR eggNOG; KOG1376; Eukaryota.
DR GeneTree; ENSGT00950000182825; -.
DR HOGENOM; CLU_015718_0_0_1; -.
DR InParanoid; Q71U36; -.
DR OMA; VDNEACY; -.
DR OrthoDB; 514396at2759; -.
DR PhylomeDB; Q71U36; -.
DR TreeFam; TF300314; -.
DR PathwayCommons; Q71U36; -.
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-2565942; Regulation of PLK1 Activity at G2/M Transition.
DR Reactome; R-HSA-3371497; HSP90 chaperone cycle for steroid hormone receptors (SHR) in the presence of ligand.
DR Reactome; R-HSA-380259; Loss of Nlp from mitotic centrosomes.
DR Reactome; R-HSA-380270; Recruitment of mitotic centrosome proteins and complexes.
DR Reactome; R-HSA-380284; Loss of proteins required for interphase microtubule organization from the centrosome.
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-5620912; Anchoring of the basal body to the plasma membrane.
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-8854518; AURKA Activation by TPX2.
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; Q71U36; -.
DR SIGNOR; Q71U36; -.
DR BioGRID-ORCS; 7846; 182 hits in 1012 CRISPR screens.
DR ChiTaRS; TUBA1A; human.
DR GeneWiki; TUBA1A; -.
DR GenomeRNAi; 7846; -.
DR Pharos; Q71U36; Tchem.
DR PRO; PR:Q71U36; -.
DR Proteomes; UP000005640; Chromosome 12.
DR RNAct; Q71U36; protein.
DR Bgee; ENSG00000167552; Expressed in endothelial cell and 201 other tissues.
DR ExpressionAtlas; Q71U36; baseline and differential.
DR Genevisible; Q71U36; HS.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0005881; C:cytoplasmic microtubule; IEA:Ensembl.
DR GO; GO:0036464; C:cytoplasmic ribonucleoprotein granule; IDA:ParkinsonsUK-UCL.
DR GO; GO:0005829; C:cytosol; TAS:Reactome.
DR GO; GO:0070062; C:extracellular exosome; HDA:UniProtKB.
DR GO; GO:0005874; C:microtubule; IDA:UniProtKB.
DR GO; GO:0015630; C:microtubule cytoskeleton; IDA:HPA.
DR GO; GO:0031594; C:neuromuscular junction; IEA:Ensembl.
DR GO; GO:0005634; C:nucleus; HDA:UniProtKB.
DR GO; GO:0055037; C:recycling endosome; IDA:UniProtKB.
DR GO; GO:0005525; F:GTP binding; IBA:GO_Central.
DR GO; GO:0042802; F:identical protein binding; IPI:IntAct.
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 GO; GO:0050807; P:regulation of synapse organization; IEA:Ensembl.
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 3D-structure; Acetylation; Alternative splicing; Cytoplasm; Cytoskeleton;
KW Direct protein sequencing; Disease variant; GTP-binding; Isopeptide bond;
KW Lissencephaly; Methylation; Microtubule; Nitration; Nucleotide-binding;
KW Phosphoprotein; Reference proteome.
FT CHAIN 1..451
FT /note="Tubulin alpha-1A chain"
FT /id="PRO_0000048111"
FT CHAIN 1..450
FT /note="Detyrosinated tubulin alpha-1A chain"
FT /evidence="ECO:0000305|PubMed:25908662,
FT ECO:0000305|PubMed:29146869"
FT /id="PRO_0000437378"
FT REGION 432..451
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 142..148
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000255"
FT SITE 451
FT /note="Involved in polymerization"
FT /evidence="ECO:0000250"
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 439
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P68373"
FT MOD_RES 443
FT /note="5-glutamyl polyglutamate"
FT /evidence="ECO:0000269|PubMed:32747782"
FT MOD_RES 445
FT /note="5-glutamyl polyglutamate"
FT /evidence="ECO:0000250|UniProtKB:P68369"
FT MOD_RES 451
FT /note="3'-nitrotyrosine"
FT /evidence="ECO:0000269|PubMed:10339593"
FT VAR_SEQ 1..35
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000305"
FT /id="VSP_046782"
FT VARIANT 188
FT /note="I -> L (in LIS3; dbSNP:rs137853045)"
FT /evidence="ECO:0000269|PubMed:17584854"
FT /id="VAR_039332"
FT VARIANT 263
FT /note="P -> T (in LIS3; dbSNP:rs137853046)"
FT /evidence="ECO:0000269|PubMed:17584854"
FT /id="VAR_039333"
FT VARIANT 264
FT /note="R -> C (in LIS3; dbSNP:rs137853043)"
FT /evidence="ECO:0000269|PubMed:17584854"
FT /id="VAR_039334"
FT VARIANT 286
FT /note="L -> F (in LIS3)"
FT /evidence="ECO:0000269|PubMed:17584854"
FT /id="VAR_039335"
FT VARIANT 402
FT /note="R -> C (in LIS3; dbSNP:rs587784483)"
FT /evidence="ECO:0000269|PubMed:17584854"
FT /id="VAR_039336"
FT VARIANT 402
FT /note="R -> H (in LIS3; dbSNP:rs137853044)"
FT /evidence="ECO:0000269|PubMed:17584854"
FT /id="VAR_039337"
FT VARIANT 402
FT /note="R -> L (in LIS3; dbSNP:rs137853044)"
FT /evidence="ECO:0000269|PubMed:25818041"
FT /id="VAR_078711"
FT VARIANT 419
FT /note="S -> L (in LIS3; dbSNP:rs137853047)"
FT /evidence="ECO:0000269|PubMed:17584854"
FT /id="VAR_039338"
FT VARIANT 447
FT /note="E -> K (in dbSNP:rs1065730)"
FT /id="VAR_034540"
FT CONFLICT 131
FT /note="G -> R (in Ref. 1; CAA25855 and 8; AAA91575)"
FT /evidence="ECO:0000305"
FT CONFLICT 290
FT /note="E -> D (in Ref. 8; AAA91575)"
FT /evidence="ECO:0000305"
FT CONFLICT 308
FT /note="R -> G (in Ref. 1; CAA25855 and 8; AAA91575)"
FT /evidence="ECO:0000305"
FT CONFLICT 438
FT /note="D -> H (in Ref. 1; CAA25855)"
FT /evidence="ECO:0000305"
FT STRAND 3..10
FT /evidence="ECO:0007829|PDB:6WSL"
FT HELIX 11..26
FT /evidence="ECO:0007829|PDB:6WSL"
FT TURN 27..29
FT /evidence="ECO:0007829|PDB:6WSL"
FT TURN 50..52
FT /evidence="ECO:0007829|PDB:6WSL"
FT STRAND 53..55
FT /evidence="ECO:0007829|PDB:6WSL"
FT STRAND 61..71
FT /evidence="ECO:0007829|PDB:6WSL"
FT TURN 72..74
FT /evidence="ECO:0007829|PDB:6WSL"
FT HELIX 75..78
FT /evidence="ECO:0007829|PDB:6WSL"
FT TURN 82..86
FT /evidence="ECO:0007829|PDB:6WSL"
FT TURN 89..91
FT /evidence="ECO:0007829|PDB:6WSL"
FT HELIX 104..107
FT /evidence="ECO:0007829|PDB:6WSL"
FT HELIX 111..123
FT /evidence="ECO:0007829|PDB:6WSL"
FT TURN 124..127
FT /evidence="ECO:0007829|PDB:6WSL"
FT STRAND 130..137
FT /evidence="ECO:0007829|PDB:6WSL"
FT STRAND 140..143
FT /evidence="ECO:0007829|PDB:6WSL"
FT HELIX 145..160
FT /evidence="ECO:0007829|PDB:6WSL"
FT STRAND 165..171
FT /evidence="ECO:0007829|PDB:6WSL"
FT HELIX 185..196
FT /evidence="ECO:0007829|PDB:6WSL"
FT STRAND 199..204
FT /evidence="ECO:0007829|PDB:6WSL"
FT HELIX 207..210
FT /evidence="ECO:0007829|PDB:6WSL"
FT TURN 211..216
FT /evidence="ECO:0007829|PDB:6WSL"
FT TURN 224..229
FT /evidence="ECO:0007829|PDB:6WSL"
FT HELIX 230..238
FT /evidence="ECO:0007829|PDB:6WSL"
FT STRAND 241..244
FT /evidence="ECO:0007829|PDB:6WSL"
FT TURN 252..259
FT /evidence="ECO:0007829|PDB:6WSL"
FT STRAND 269..273
FT /evidence="ECO:0007829|PDB:6WSL"
FT STRAND 281..284
FT /evidence="ECO:0007829|PDB:6WSL"
FT HELIX 288..294
FT /evidence="ECO:0007829|PDB:6WSL"
FT STRAND 302..304
FT /evidence="ECO:0007829|PDB:6WSL"
FT TURN 307..309
FT /evidence="ECO:0007829|PDB:6WSL"
FT STRAND 319..322
FT /evidence="ECO:0007829|PDB:6WSL"
FT HELIX 325..336
FT /evidence="ECO:0007829|PDB:6WSL"
FT STRAND 338..340
FT /evidence="ECO:0007829|PDB:6WSL"
FT STRAND 366..368
FT /evidence="ECO:0007829|PDB:6WSL"
FT STRAND 372..379
FT /evidence="ECO:0007829|PDB:6WSL"
FT HELIX 384..386
FT /evidence="ECO:0007829|PDB:6WSL"
FT HELIX 388..399
FT /evidence="ECO:0007829|PDB:6WSL"
FT TURN 400..405
FT /evidence="ECO:0007829|PDB:6WSL"
FT HELIX 406..409
FT /evidence="ECO:0007829|PDB:6WSL"
FT TURN 410..412
FT /evidence="ECO:0007829|PDB:6WSL"
FT HELIX 417..434
FT /evidence="ECO:0007829|PDB:6WSL"
SQ SEQUENCE 451 AA; 50136 MW; 00F8429A4A10E5FE CRC64;
MRECISIHVG QAGVQIGNAC WELYCLEHGI QPDGQMPSDK TIGGGDDSFN TFFSETGAGK
HVPRAVFVDL EPTVIDEVRT GTYRQLFHPE QLITGKEDAA NNYARGHYTI GKEIIDLVLD
RIRKLADQCT GLQGFLVFHS FGGGTGSGFT SLLMERLSVD YGKKSKLEFS IYPAPQVSTA
VVEPYNSILT THTTLEHSDC AFMVDNEAIY DICRRNLDIE RPTYTNLNRL IGQIVSSITA
SLRFDGALNV DLTEFQTNLV PYPRIHFPLA TYAPVISAEK AYHEQLSVAE ITNACFEPAN
QMVKCDPRHG KYMACCLLYR GDVVPKDVNA AIATIKTKRT IQFVDWCPTG FKVGINYQPP
TVVPGGDLAK VQRAVCMLSN TTAIAEAWAR LDHKFDLMYA KRAFVHWYVG EGMEEGEFSE
AREDMAALEK DYEEVGVDSV EGEGEEEGEE Y
