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Tubulin alpha-1A chain (Alpha-tubulin 3) (Tubulin B-alpha-1) (Tubulin alpha-3 chain) [Cleaved into: Detyrosinated tubulin alpha-1A chain]

 TBA1A_HUMAN             Reviewed;         451 AA.
Q71U36; A8K0B8; G3V1U9; P04687; P05209;
13-AUG-1987, integrated into UniProtKB/Swiss-Prot.
05-JUL-2004, sequence version 1.
25-OCT-2017, entry version 147.
RecName: Full=Tubulin alpha-1A chain;
AltName: Full=Alpha-tubulin 3;
AltName: Full=Tubulin B-alpha-1;
AltName: Full=Tubulin alpha-3 chain;
Contains:
RecName: Full=Detyrosinated tubulin alpha-1A chain;
Name=TUBA1A; Synonyms=TUBA3;
Homo sapiens (Human).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
Catarrhini; Hominidae; Homo.
NCBI_TaxID=9606;
[1]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
PubMed=3839072; DOI=10.1093/nar/13.1.207;
Hall J.L., Cowan N.J.;
"Structural features and restricted expression of a human alpha-
tubulin gene.";
Nucleic Acids Res. 13:207-223(1985).
[2]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
TISSUE=Retina;
PubMed=11504633; DOI=10.1016/S0968-0896(01)00103-1;
Crabtree D.V., Ojima I., Geng X., Adler A.J.;
"Tubulins in the primate retina: evidence that xanthophylls may be
endogenous ligands for the paclitaxel-binding site.";
Bioorg. Med. Chem. 9:1967-1976(2001).
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
TISSUE=Cerebellum;
PubMed=14702039; DOI=10.1038/ng1285;
Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A.,
Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M.,
Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y.,
Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M.,
Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K.,
Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S.,
Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J.,
Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y.,
Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N.,
Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S.,
Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y.,
Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T.,
Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y.,
Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S.,
Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T.,
Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M.,
Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T.,
Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K.,
Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R.,
Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.;
"Complete sequencing and characterization of 21,243 full-length human
cDNAs.";
Nat. Genet. 36:40-45(2004).
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
PubMed=16541075; DOI=10.1038/nature04569;
Scherer S.E., Muzny D.M., Buhay C.J., Chen R., Cree A., Ding Y.,
Dugan-Rocha S., Gill R., Gunaratne P., Harris R.A., Hawes A.C.,
Hernandez J., Hodgson A.V., Hume J., Jackson A., Khan Z.M.,
Kovar-Smith C., Lewis L.R., Lozado R.J., Metzker M.L.,
Milosavljevic A., Miner G.R., Montgomery K.T., Morgan M.B.,
Nazareth L.V., Scott G., Sodergren E., Song X.-Z., Steffen D.,
Lovering R.C., Wheeler D.A., Worley K.C., Yuan Y., Zhang Z.,
Adams C.Q., Ansari-Lari M.A., Ayele M., Brown M.J., Chen G., Chen Z.,
Clerc-Blankenburg K.P., Davis C., Delgado O., Dinh H.H., Draper H.,
Gonzalez-Garay M.L., Havlak P., Jackson L.R., Jacob L.S., Kelly S.H.,
Li L., Li Z., Liu J., Liu W., Lu J., Maheshwari M., Nguyen B.-V.,
Okwuonu G.O., Pasternak S., Perez L.M., Plopper F.J.H., Santibanez J.,
Shen H., Tabor P.E., Verduzco D., Waldron L., Wang Q., Williams G.A.,
Zhang J., Zhou J., Allen C.C., Amin A.G., Anyalebechi V., Bailey M.,
Barbaria J.A., Bimage K.E., Bryant N.P., Burch P.E., Burkett C.E.,
Burrell K.L., Calderon E., Cardenas V., Carter K., Casias K.,
Cavazos I., Cavazos S.R., Ceasar H., Chacko J., Chan S.N., Chavez D.,
Christopoulos C., Chu J., Cockrell R., Cox C.D., Dang M.,
Dathorne S.R., David R., Davis C.M., Davy-Carroll L., Deshazo D.R.,
Donlin J.E., D'Souza L., Eaves K.A., Egan A., Emery-Cohen A.J.,
Escotto M., Flagg N., Forbes L.D., Gabisi A.M., Garza M., Hamilton C.,
Henderson N., Hernandez O., Hines S., Hogues M.E., Huang M.,
Idlebird D.G., Johnson R., Jolivet A., Jones S., Kagan R., King L.M.,
Leal B., Lebow H., Lee S., LeVan J.M., Lewis L.C., London P.,
Lorensuhewa L.M., Loulseged H., Lovett D.A., Lucier A., Lucier R.L.,
Ma J., Madu R.C., Mapua P., Martindale A.D., Martinez E., Massey E.,
Mawhiney S., Meador M.G., Mendez S., Mercado C., Mercado I.C.,
Merritt C.E., Miner Z.L., Minja E., Mitchell T., Mohabbat F.,
Mohabbat K., Montgomery B., Moore N., Morris S., Munidasa M.,
Ngo R.N., Nguyen N.B., Nickerson E., Nwaokelemeh O.O., Nwokenkwo S.,
Obregon M., Oguh M., Oragunye N., Oviedo R.J., Parish B.J.,
Parker D.N., Parrish J., Parks K.L., Paul H.A., Payton B.A., Perez A.,
Perrin W., Pickens A., Primus E.L., Pu L.-L., Puazo M., Quiles M.M.,
Quiroz J.B., Rabata D., Reeves K., Ruiz S.J., Shao H., Sisson I.,
Sonaike T., Sorelle R.P., Sutton A.E., Svatek A.F., Svetz L.A.,
Tamerisa K.S., Taylor T.R., Teague B., Thomas N., Thorn R.D.,
Trejos Z.Y., Trevino B.K., Ukegbu O.N., Urban J.B., Vasquez L.I.,
Vera V.A., Villasana D.M., Wang L., Ward-Moore S., Warren J.T.,
Wei X., White F., Williamson A.L., Wleczyk R., Wooden H.S.,
Wooden S.H., Yen J., Yoon L., Yoon V., Zorrilla S.E., Nelson D.,
Kucherlapati R., Weinstock G., Gibbs R.A.;
"The finished DNA sequence of human chromosome 12.";
Nature 440:346-351(2006).
[5]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L.,
Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R.,
Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V.,
Hannenhalli S., Turner R., Yooseph S., Lu F., Nusskern D.R.,
Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H.,
Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G.,
Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W.,
Venter J.C.;
Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
[6]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
TISSUE=Muscle, and Skin;
PubMed=15489334; DOI=10.1101/gr.2596504;
The MGC Project Team;
"The status, quality, and expansion of the NIH full-length cDNA
project: the Mammalian Gene Collection (MGC).";
Genome Res. 14:2121-2127(2004).
[7]
PROTEIN SEQUENCE OF 41-60; 65-79; 85-105; 113-121; 157-163; 216-304;
312-320; 327-336; 340-352; 374-390; 395-401 AND 403-430, AND
IDENTIFICATION BY MASS SPECTROMETRY.
TISSUE=Brain, Cajal-Retzius cell, and Fetal brain cortex;
Lubec G., Afjehi-Sadat L., Chen W.-Q., Sun Y.;
Submitted (DEC-2008) to UniProtKB.
[8]
NUCLEOTIDE SEQUENCE [MRNA] OF 110-451.
TISSUE=Fetal brain;
PubMed=6646120; DOI=10.1128/MCB.3.10.1738;
Cowan N.J., Dobner P., Fuchs E.V., Cleveland D.W.;
"Expression of human alpha-tubulin genes: interspecies conservation of
3' untranslated regions.";
Mol. Cell. Biol. 3:1738-1745(1983).
[9]
PROTEIN SEQUENCE OF 439-451, AND NITRATION AT TYR-451.
PubMed=10339593; DOI=10.1073/pnas.96.11.6365;
Eiserich J.P., Estevez A.G., Bamberg T.V., Ye Y.Z., Chumley P.H.,
Beckman J.S., Freeman B.A.;
"Microtubule dysfunction by posttranslational nitrotyrosination of
alpha-tubulin: a nitric oxide-dependent mechanism of cellular
injury.";
Proc. Natl. Acad. Sci. U.S.A. 96:6365-6370(1999).
[10]
TISSUE SPECIFICITY, AND VARIANTS LIS3 LEU-188; THR-263; CYS-264;
PHE-286; HIS-402; CYS-402 AND LEU-419.
PubMed=17584854; DOI=10.1002/humu.20572;
Poirier K., Keays D.A., Francis F., Saillour Y., Bahi N.,
Manouvrier S., Fallet-Bianco C., Pasquier L., Toutain A., Tuy F.P.,
Bienvenu T., Joriot S., Odent S., Ville D., Desguerre I.,
Goldenberg A., Moutard M.L., Fryns J.-P., van Esch H., Harvey R.J.,
Siebold C., Flint J., Beldjord C., Chelly J.;
"Large spectrum of lissencephaly and pachygyria phenotypes resulting
from de novo missense mutations in tubulin alpha 1A (TUBA1A).";
Hum. Mutat. 28:1055-1064(2007).
[11]
GLYCYLATION.
PubMed=19524510; DOI=10.1016/j.cell.2009.05.020;
Rogowski K., Juge F., van Dijk J., Wloga D., Strub J.-M.,
Levilliers N., Thomas D., Bre M.-H., Van Dorsselaer A., Gaertig J.,
Janke C.;
"Evolutionary divergence of enzymatic mechanisms for posttranslational
polyglycylation.";
Cell 137:1076-1087(2009).
[12]
ACETYLATION AT LYS-40.
PubMed=24906155; DOI=10.1016/j.cell.2014.03.061;
Szyk A., Deaconescu A.M., Spector J., Goodman B., Valenstein M.L.,
Ziolkowska N.E., Kormendi V., Grigorieff N., Roll-Mecak A.;
"Molecular basis for age-dependent microtubule acetylation by tubulin
acetyltransferase.";
Cell 157:1405-1415(2014).
[13]
DETYROSINATION.
PubMed=25908662; DOI=10.1126/science.aaa5175;
Barisic M., Silva e Sousa R., Tripathy S.K., Magiera M.M.,
Zaytsev A.V., Pereira A.L., Janke C., Grishchuk E.L., Maiato H.;
"Mitosis. Microtubule detyrosination guides chromosomes during
mitosis.";
Science 348:799-803(2015).
[14]
GLUTAMYLATION.
PubMed=26875866; DOI=10.1016/j.cell.2016.01.019;
Valenstein M.L., Roll-Mecak A.;
"Graded control of microtubule severing by tubulin glutamylation.";
Cell 164:911-921(2016).
[15]
INTERACTION WITH SETD2.
PubMed=27518565; DOI=10.1016/j.cell.2016.07.005;
Park I.Y., Powell R.T., Tripathi D.N., Dere R., Ho T.H., Blasius T.L.,
Chiang Y.C., Davis I.J., Fahey C.C., Hacker K.E., Verhey K.J.,
Bedford M.T., Jonasch E., Rathmell W.K., Walker C.L.;
"Dual chromatin and cytoskeletal remodeling by SETD2.";
Cell 166:950-962(2016).
[16]
TYROSINATION.
PubMed=26972003; DOI=10.1016/j.celrep.2016.02.046;
Nirschl J.J., Magiera M.M., Lazarus J.E., Janke C., Holzbaur E.L.;
"Alpha-tubulin tyrosination and CLIP-170 phosphorylation regulate the
initiation of dynein-driven transport in neurons.";
Cell Rep. 14:2637-2652(2016).
[17]
TYROSINATION.
PubMed=26968983; DOI=10.15252/embj.201593071;
McKenney R.J., Huynh W., Vale R.D., Sirajuddin M.;
"Tyrosination of alpha-tubulin controls the initiation of processive
dynein-dynactin motility.";
EMBO J. 35:1175-1185(2016).
[18]
VARIANT LIS3 LEU-402.
PubMed=25818041; DOI=10.1111/epi.12954;
Mercimek-Mahmutoglu S., Patel J., Cordeiro D., Hewson S., Callen D.,
Donner E.J., Hahn C.D., Kannu P., Kobayashi J., Minassian B.A.,
Moharir M., Siriwardena K., Weiss S.K., Weksberg R., Snead O.C. III;
"Diagnostic yield of genetic testing in epileptic encephalopathy in
childhood.";
Epilepsia 56:707-716(2015).
-!- FUNCTION: Tubulin is the major constituent of microtubules. It
binds two moles of GTP, one at an exchangeable site on the beta
chain and one at a non-exchangeable site on the alpha chain.
-!- SUBUNIT: Dimer of alpha and beta chains. A typical microtubule is
a hollow water-filled tube with an outer diameter of 25 nm and an
inner diameter of 15 nM. Alpha-beta heterodimers associate head-
to-tail to form protofilaments running lengthwise along the
microtubule wall with the beta-tubulin subunit facing the
microtubule plus end conferring a structural polarity.
Microtubules usually have 13 protofilaments but different
protofilament numbers can be found in some organisms and
specialized cells. Interacts with SETD2; the interaction is
independent on alpha-tubulin acetylation on Lys-40.
-!- INTERACTION:
P30622-2:CLIP1; NbExp=3; IntAct=EBI-302552, EBI-6479976;
Q9NQC7:CYLD; NbExp=6; IntAct=EBI-302552, EBI-2117940;
P00533:EGFR; NbExp=3; IntAct=EBI-302552, EBI-297353;
P05412:JUN; NbExp=3; IntAct=EBI-302552, EBI-852823;
-!- SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=2;
Name=1;
IsoId=Q71U36-1; Sequence=Displayed;
Name=2;
IsoId=Q71U36-2; Sequence=VSP_046782;
Note=No experimental confirmation available.;
-!- TISSUE SPECIFICITY: Expressed at a high level in fetal brain.
{ECO:0000269|PubMed:17584854}.
-!- PTM: Some glutamate residues at the C-terminus are
polyglutamylated, resulting in polyglutamate chains on the gamma-
carboxyl group (PubMed:26875866). Polyglutamylation plays a key
role in microtubule severing by spastin (SPAST). SPAST
preferentially recognizes and acts on microtubules decorated with
short polyglutamate tails: severing activity by SPAST increases as
the number of glutamates per tubulin rises from one to eight, but
decreases beyond this glutamylation threshold (PubMed:26875866).
{ECO:0000269|PubMed:26875866}.
-!- PTM: Some glutamate residues at the C-terminus are monoglycylated
but not polyglycylated due to the absence of functional TTLL10 in
human. Monoglycylation is mainly limited to tubulin incorporated
into axonemes (cilia and flagella). Both polyglutamylation and
monoglycylation can coexist on the same protein on adjacent
residues, and lowering glycylation levels increases
polyglutamylation, and reciprocally. The precise function of
monoglycylation is still unclear (Probable).
{ECO:0000305|PubMed:19524510}.
-!- PTM: Acetylation of alpha chains at Lys-40 is located inside the
microtubule lumen. This modification has been correlated with
increased microtubule stability, intracellular transport and
ciliary assembly. {ECO:0000269|PubMed:24906155}.
-!- PTM: Methylation of alpha chains at Lys-40 is found in mitotic
microtubules and is required for normal mitosis and cytokinesis
contributing to genomic stability. {ECO:0000250|UniProtKB:P68363}.
-!- PTM: Nitration of Tyr-451 is irreversible and interferes with
normal dynein intracellular distribution.
{ECO:0000269|PubMed:10339593}.
-!- PTM: Undergoes a tyrosination/detyrosination cycle, the cyclic
removal and re-addition of a C-terminal tyrosine residue by the
enzymes tubulin tyrosine carboxypeptidase (TTCP) and tubulin
tyrosine ligase (TTL), respectively. {ECO:0000269|PubMed:25908662,
ECO:0000269|PubMed:26968983, ECO:0000269|PubMed:26972003}.
-!- PTM: Tubulin alpha-1A chain: Tyrosination promotes microtubule
interaction with CAP-Gly domain-containing proteins such as CLIP1,
CLIP2 and DCTN1. Tyrosination regulates the initiation of dynein-
dynactin motility via interaction with DCTN1, which brings the
dynein-dynactin complex into contact with microtubules
(PubMed:26972003, PubMed:26968983). In neurons, tyrosinated
tubulins mediate the initiation of retrograde vesicle transport
(PubMed:26968983). {ECO:0000269|PubMed:26968983,
ECO:0000269|PubMed:26972003}.
-!- PTM: Detyrosinated tubulin alpha-1A chain: Detyrosination is
involved in metaphase plate congression by guiding chromosomes
during mitosis: detyrosination promotes interaction with CENPE,
promoting pole-proximal transport of chromosomes toward the
equator (PubMed:25908662). Detyrosination increases microtubules-
dependent mechanotransduction in dystrophic cardiac and skeletal
muscle. In cardiomyocytes, detyrosinated microtubules are required
to resist to contractile compression during contraction:
detyrosination promotes association with desmin (DES) at force-
generating sarcomeres, leading to buckled microtubules and
mechanical resistance to contraction (By similarity).
{ECO:0000250|UniProtKB:P68369, ECO:0000269|PubMed:25908662}.
-!- DISEASE: Lissencephaly 3 (LIS3) [MIM:611603]: A classic type
lissencephaly associated with psychomotor retardation and
seizures. Features include agyria or pachygyria or laminar
heterotopia, severe mental retardation, motor delay, variable
presence of seizures, and abnormalities of corpus callosum,
hippocampus, cerebellar vermis and brainstem.
{ECO:0000269|PubMed:17584854, ECO:0000269|PubMed:25818041}.
Note=The disease is caused by mutations affecting the gene
represented in this entry.
-!- SIMILARITY: Belongs to the tubulin family. {ECO:0000305}.
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EMBL; X01703; CAA25855.1; -; Genomic_DNA.
EMBL; AF141347; AAD33871.1; -; mRNA.
EMBL; AK289483; BAF82172.1; -; mRNA.
EMBL; AC010173; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; CH471111; EAW58052.1; -; Genomic_DNA.
EMBL; CH471111; EAW58054.1; -; Genomic_DNA.
EMBL; CH471111; EAW58055.1; -; Genomic_DNA.
EMBL; BC006468; AAH06468.1; -; mRNA.
EMBL; BC050637; AAH50637.1; -; mRNA.
EMBL; K00557; AAA91575.1; -; mRNA.
CCDS; CCDS58226.1; -. [Q71U36-2]
CCDS; CCDS58227.1; -. [Q71U36-1]
CCDS; CCDS8781.1; -. [Q71U36-1]
RefSeq; NP_001257328.1; NM_001270399.1. [Q71U36-1]
RefSeq; NP_001257329.1; NM_001270400.1. [Q71U36-2]
RefSeq; NP_006000.2; NM_006009.3. [Q71U36-1]
UniGene; Hs.654422; -.
PDB; 5JCO; EM; 4.00 A; A/B/E/F/G/H=1-437.
PDBsum; 5JCO; -.
ProteinModelPortal; Q71U36; -.
SMR; Q71U36; -.
BioGrid; 113603; 261.
CORUM; Q71U36; -.
DIP; DIP-32773N; -.
ELM; Q71U36; -.
IntAct; Q71U36; 243.
MINT; MINT-156132; -.
STRING; 9606.ENSP00000301071; -.
ChEMBL; CHEMBL3661; -.
DrugBank; DB00518; Albendazole.
DrugBank; DB05147; CYT997.
DrugBank; DB03010; Epothilone B.
DrugBank; DB01873; Epothilone D.
DrugBank; DB00643; Mebendazole.
DrugBank; DB00570; Vinblastine.
iPTMnet; Q71U36; -.
PhosphoSitePlus; Q71U36; -.
SwissPalm; Q71U36; -.
BioMuta; TUBA1A; -.
DMDM; 55977864; -.
EPD; Q71U36; -.
MaxQB; Q71U36; -.
PaxDb; Q71U36; -.
PeptideAtlas; Q71U36; -.
PRIDE; Q71U36; -.
TopDownProteomics; Q71U36-1; -. [Q71U36-1]
DNASU; 7846; -.
Ensembl; ENST00000295766; ENSP00000439020; ENSG00000167552. [Q71U36-1]
Ensembl; ENST00000301071; ENSP00000301071; ENSG00000167552. [Q71U36-1]
Ensembl; ENST00000550767; ENSP00000446637; ENSG00000167552. [Q71U36-2]
GeneID; 7846; -.
KEGG; hsa:7846; -.
UCSC; uc001rtp.5; human. [Q71U36-1]
CTD; 7846; -.
DisGeNET; 7846; -.
EuPathDB; HostDB:ENSG00000167552.13; -.
GeneCards; TUBA1A; -.
HGNC; HGNC:20766; TUBA1A.
HPA; CAB008686; -.
HPA; HPA039247; -.
HPA; HPA043684; -.
HPA; HPA063394; -.
MalaCards; TUBA1A; -.
MIM; 602529; gene.
MIM; 611603; phenotype.
neXtProt; NX_Q71U36; -.
OpenTargets; ENSG00000167552; -.
Orphanet; 171680; Lissencephaly due to TUBA1A mutation.
PharmGKB; PA162407319; -.
eggNOG; KOG1376; Eukaryota.
eggNOG; COG5023; LUCA.
GeneTree; ENSGT00760000119060; -.
HOGENOM; HOG000165711; -.
HOVERGEN; HBG000089; -.
InParanoid; Q71U36; -.
KO; K07374; -.
OMA; ENNSHIA; -.
OrthoDB; EOG091G0736; -.
PhylomeDB; Q71U36; -.
TreeFam; TF300314; -.
Reactome; R-HSA-1445148; Translocation of GLUT4 to the plasma membrane.
Reactome; R-HSA-190840; Microtubule-dependent trafficking of connexons from Golgi to the plasma membrane.
Reactome; R-HSA-190861; Gap junction assembly.
Reactome; R-HSA-2132295; MHC class II antigen presentation.
Reactome; R-HSA-2467813; Separation of Sister Chromatids.
Reactome; R-HSA-2500257; Resolution of Sister Chromatid Cohesion.
Reactome; R-HSA-2565942; Regulation of PLK1 Activity at G2/M Transition.
Reactome; R-HSA-3371497; HSP90 chaperone cycle for steroid hormone receptors (SHR).
Reactome; R-HSA-380259; Loss of Nlp from mitotic centrosomes.
Reactome; R-HSA-380270; Recruitment of mitotic centrosome proteins and complexes.
Reactome; R-HSA-380284; Loss of proteins required for interphase microtubule organization from the centrosome.
Reactome; R-HSA-380320; Recruitment of NuMA to mitotic centrosomes.
Reactome; R-HSA-389957; Prefoldin mediated transfer of substrate to CCT/TriC.
Reactome; R-HSA-389960; Formation of tubulin folding intermediates by CCT/TriC.
Reactome; R-HSA-389977; Post-chaperonin tubulin folding pathway.
Reactome; R-HSA-437239; Recycling pathway of L1.
Reactome; R-HSA-5610787; Hedgehog 'off' state.
Reactome; R-HSA-5617833; Cilium Assembly.
Reactome; R-HSA-5620912; Anchoring of the basal body to the plasma membrane.
Reactome; R-HSA-5620924; Intraflagellar transport.
Reactome; R-HSA-5626467; RHO GTPases activate IQGAPs.
Reactome; R-HSA-5663220; RHO GTPases Activate Formins.
Reactome; R-HSA-6807878; COPI-mediated anterograde transport.
Reactome; R-HSA-6811434; COPI-dependent Golgi-to-ER retrograde traffic.
Reactome; R-HSA-6811436; COPI-independent Golgi-to-ER retrograde traffic.
Reactome; R-HSA-68877; Mitotic Prometaphase.
Reactome; R-HSA-8852276; The role of GTSE1 in G2/M progression after G2 checkpoint.
Reactome; R-HSA-8854518; AURKA Activation by TPX2.
Reactome; R-HSA-8955332; Carboxyterminal post-translational modifications of tubulin.
Reactome; R-HSA-983189; Kinesins.
SIGNOR; Q71U36; -.
ChiTaRS; TUBA1A; human.
GeneWiki; TUBA1A; -.
GenomeRNAi; 7846; -.
PMAP-CutDB; Q71U36; -.
PRO; PR:Q71U36; -.
Proteomes; UP000005640; Chromosome 12.
Bgee; ENSG00000167552; -.
CleanEx; HS_TUBA1A; -.
ExpressionAtlas; Q71U36; baseline and differential.
Genevisible; Q71U36; HS.
GO; GO:0005881; C:cytoplasmic microtubule; IEA:Ensembl.
GO; GO:0036464; C:cytoplasmic ribonucleoprotein granule; IDA:ParkinsonsUK-UCL.
GO; GO:0005829; C:cytosol; TAS:Reactome.
GO; GO:0070062; C:extracellular exosome; IDA:UniProtKB.
GO; GO:0045121; C:membrane raft; IEA:Ensembl.
GO; GO:0005874; C:microtubule; IDA:UniProtKB.
GO; GO:0015630; C:microtubule cytoskeleton; IDA:HPA.
GO; GO:0043209; C:myelin sheath; IEA:Ensembl.
GO; GO:0005634; C:nucleus; IDA:UniProtKB.
GO; GO:0055037; C:recycling endosome; IDA:UniProtKB.
GO; GO:0005525; F:GTP binding; IEA:UniProtKB-KW.
GO; GO:0003924; F:GTPase activity; IEA:InterPro.
GO; GO:0019904; F:protein domain specific binding; IEA:Ensembl.
GO; GO:0005200; F:structural constituent of cytoskeleton; IEA:InterPro.
GO; GO:0005198; F:structural molecule activity; TAS:BHF-UCL.
GO; GO:0051301; P:cell division; TAS:BHF-UCL.
GO; GO:0097711; P:ciliary basal body-plasma membrane docking; TAS:Reactome.
GO; GO:0030705; P:cytoskeleton-dependent intracellular transport; TAS:BHF-UCL.
GO; GO:0000086; P:G2/M transition of mitotic cell cycle; TAS:Reactome.
GO; GO:0007017; P:microtubule-based process; TAS:BHF-UCL.
GO; GO:0010389; P:regulation of G2/M transition of mitotic cell cycle; TAS:Reactome.
Gene3D; 3.30.1330.20; -; 1.
Gene3D; 3.40.50.1440; -; 1.
InterPro; IPR002452; Alpha_tubulin.
InterPro; IPR008280; Tub_FtsZ_C.
InterPro; IPR000217; Tubulin.
InterPro; IPR018316; Tubulin/FtsZ_2-layer-sand-dom.
InterPro; IPR037103; Tubulin/FtsZ_C_sf.
InterPro; IPR036525; Tubulin/FtsZ_GTPase_sf.
InterPro; IPR017975; Tubulin_CS.
InterPro; IPR003008; Tubulin_FtsZ_GTPase.
PANTHER; PTHR11588; PTHR11588; 1.
Pfam; PF00091; Tubulin; 1.
Pfam; PF03953; Tubulin_C; 1.
PRINTS; PR01162; ALPHATUBULIN.
PRINTS; PR01161; TUBULIN.
SMART; SM00864; Tubulin; 1.
SMART; SM00865; Tubulin_C; 1.
SUPFAM; SSF52490; SSF52490; 1.
SUPFAM; SSF55307; SSF55307; 1.
PROSITE; PS00227; TUBULIN; 1.
1: Evidence at protein level;
3D-structure; Acetylation; Alternative splicing; Complete proteome;
Cytoplasm; Cytoskeleton; Direct protein sequencing; Disease mutation;
GTP-binding; Isopeptide bond; Lissencephaly; Methylation; Microtubule;
Nitration; Nucleotide-binding; Phosphoprotein; Polymorphism;
Reference proteome.
CHAIN 1 451 Tubulin alpha-1A chain.
/FTId=PRO_0000048111.
CHAIN 1 450 Detyrosinated tubulin alpha-1A chain.
{ECO:0000305|PubMed:25908662}.
/FTId=PRO_0000437378.
NP_BIND 142 148 GTP. {ECO:0000255}.
SITE 451 451 Involved in polymerization.
{ECO:0000250}.
MOD_RES 40 40 N6-acetyllysine.
{ECO:0000269|PubMed:24906155}.
MOD_RES 282 282 Nitrated tyrosine.
{ECO:0000250|UniProtKB:P68373}.
MOD_RES 439 439 Phosphoserine.
{ECO:0000250|UniProtKB:P68373}.
MOD_RES 445 445 5-glutamyl polyglutamate.
{ECO:0000250|UniProtKB:P68369}.
MOD_RES 451 451 3'-nitrotyrosine.
{ECO:0000269|PubMed:10339593}.
VAR_SEQ 1 35 Missing (in isoform 2). {ECO:0000305}.
/FTId=VSP_046782.
VARIANT 188 188 I -> L (in LIS3; dbSNP:rs137853045).
{ECO:0000269|PubMed:17584854}.
/FTId=VAR_039332.
VARIANT 263 263 P -> T (in LIS3; dbSNP:rs137853046).
{ECO:0000269|PubMed:17584854}.
/FTId=VAR_039333.
VARIANT 264 264 R -> C (in LIS3; dbSNP:rs137853043).
{ECO:0000269|PubMed:17584854}.
/FTId=VAR_039334.
VARIANT 286 286 L -> F (in LIS3).
{ECO:0000269|PubMed:17584854}.
/FTId=VAR_039335.
VARIANT 402 402 R -> C (in LIS3; dbSNP:rs587784483).
{ECO:0000269|PubMed:17584854}.
/FTId=VAR_039336.
VARIANT 402 402 R -> H (in LIS3; dbSNP:rs137853044).
{ECO:0000269|PubMed:17584854}.
/FTId=VAR_039337.
VARIANT 402 402 R -> L (in LIS3; dbSNP:rs137853044).
{ECO:0000269|PubMed:25818041}.
/FTId=VAR_078711.
VARIANT 419 419 S -> L (in LIS3; dbSNP:rs137853047).
{ECO:0000269|PubMed:17584854}.
/FTId=VAR_039338.
VARIANT 447 447 E -> K (in dbSNP:rs1065730).
/FTId=VAR_034540.
CONFLICT 131 131 G -> R (in Ref. 1; CAA25855 and 8;
AAA91575). {ECO:0000305}.
CONFLICT 290 290 E -> D (in Ref. 8; AAA91575).
{ECO:0000305}.
CONFLICT 308 308 R -> G (in Ref. 1; CAA25855 and 8;
AAA91575). {ECO:0000305}.
CONFLICT 438 438 D -> H (in Ref. 1; CAA25855).
{ECO:0000305}.
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


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