TBA8_HUMAN
ID TBA8_HUMAN Reviewed; 449 AA.
AC Q9NY65; B2RCX2; B3KPW9; B4DWG3; Q2M3N4;
DT 24-JAN-2001, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2000, sequence version 1.
DT 03-AUG-2022, entry version 191.
DE RecName: Full=Tubulin alpha-8 chain;
DE AltName: Full=Alpha-tubulin 8;
DE AltName: Full=Tubulin alpha chain-like 2;
GN Name=TUBA8; Synonyms=TUBAL2;
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 [MRNA] (ISOFORM 1).
RC TISSUE=Skeletal muscle;
RX PubMed=10772959; DOI=10.1006/bbrc.2000.2571;
RA Stanchi F., Corso V., Scannapieco P., Ievolella C., Negrisolo E., Tiso N.,
RA Lanfranchi G., Valle G.;
RT "TUBA8: a new tissue-specific isoform of alpha-tubulin that is highly
RT conserved in human and mouse.";
RL Biochem. Biophys. Res. Commun. 270:1111-1118(2000).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RX PubMed=15461802; DOI=10.1186/gb-2004-5-10-r84;
RA Collins J.E., Wright C.L., Edwards C.A., Davis M.P., Grinham J.A.,
RA Cole C.G., Goward M.E., Aguado B., Mallya M., Mokrab Y., Huckle E.J.,
RA Beare D.M., Dunham I.;
RT "A genome annotation-driven approach to cloning the human ORFeome.";
RL Genome Biol. 5:R84.1-R84.11(2004).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
RC TISSUE=Caudate nucleus, and Skeletal muscle;
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=10591208; DOI=10.1038/990031;
RA Dunham I., Hunt A.R., Collins J.E., Bruskiewich R., Beare D.M., Clamp M.,
RA Smink L.J., Ainscough R., Almeida J.P., Babbage A.K., Bagguley C.,
RA Bailey J., Barlow K.F., Bates K.N., Beasley O.P., Bird C.P., Blakey S.E.,
RA Bridgeman A.M., Buck D., Burgess J., Burrill W.D., Burton J., Carder C.,
RA Carter N.P., Chen Y., Clark G., Clegg S.M., Cobley V.E., Cole C.G.,
RA Collier R.E., Connor R., Conroy D., Corby N.R., Coville G.J., Cox A.V.,
RA Davis J., Dawson E., Dhami P.D., Dockree C., Dodsworth S.J., Durbin R.M.,
RA Ellington A.G., Evans K.L., Fey J.M., Fleming K., French L., Garner A.A.,
RA Gilbert J.G.R., Goward M.E., Grafham D.V., Griffiths M.N.D., Hall C.,
RA Hall R.E., Hall-Tamlyn G., Heathcott R.W., Ho S., Holmes S., Hunt S.E.,
RA Jones M.C., Kershaw J., Kimberley A.M., King A., Laird G.K., Langford C.F.,
RA Leversha M.A., Lloyd C., Lloyd D.M., Martyn I.D., Mashreghi-Mohammadi M.,
RA Matthews L.H., Mccann O.T., Mcclay J., Mclaren S., McMurray A.A.,
RA Milne S.A., Mortimore B.J., Odell C.N., Pavitt R., Pearce A.V., Pearson D.,
RA Phillimore B.J.C.T., Phillips S.H., Plumb R.W., Ramsay H., Ramsey Y.,
RA Rogers L., Ross M.T., Scott C.E., Sehra H.K., Skuce C.D., Smalley S.,
RA Smith M.L., Soderlund C., Spragon L., Steward C.A., Sulston J.E.,
RA Swann R.M., Vaudin M., Wall M., Wallis J.M., Whiteley M.N., Willey D.L.,
RA Williams L., Williams S.A., Williamson H., Wilmer T.E., Wilming L.,
RA Wright C.L., Hubbard T., Bentley D.R., Beck S., Rogers J., Shimizu N.,
RA Minoshima S., Kawasaki K., Sasaki T., Asakawa S., Kudoh J., Shintani A.,
RA Shibuya K., Yoshizaki Y., Aoki N., Mitsuyama S., Roe B.A., Chen F., Chu L.,
RA Crabtree J., Deschamps S., Do A., Do T., Dorman A., Fang F., Fu Y., Hu P.,
RA Hua A., Kenton S., Lai H., Lao H.I., Lewis J., Lewis S., Lin S.-P., Loh P.,
RA Malaj E., Nguyen T., Pan H., Phan S., Qi S., Qian Y., Ray L., Ren Q.,
RA Shaull S., Sloan D., Song L., Wang Q., Wang Y., Wang Z., White J.,
RA Willingham D., Wu H., Yao Z., Zhan M., Zhang G., Chissoe S., Murray J.,
RA Miller N., Minx P., Fulton R., Johnson D., Bemis G., Bentley D.,
RA Bradshaw H., Bourne S., Cordes M., Du Z., Fulton L., Goela D., Graves T.,
RA Hawkins J., Hinds K., Kemp K., Latreille P., Layman D., Ozersky P.,
RA Rohlfing T., Scheet P., Walker C., Wamsley A., Wohldmann P., Pepin K.,
RA Nelson J., Korf I., Bedell J.A., Hillier L.W., Mardis E., Waterston R.,
RA Wilson R., Emanuel B.S., Shaikh T., Kurahashi H., Saitta S., Budarf M.L.,
RA McDermid H.E., Johnson A., Wong A.C.C., Morrow B.E., Edelmann L., Kim U.J.,
RA Shizuya H., Simon M.I., Dumanski J.P., Peyrard M., Kedra D., Seroussi E.,
RA Fransson I., Tapia I., Bruder C.E., O'Brien K.P., Wilkinson P.,
RA Bodenteich A., Hartman K., Hu X., Khan A.S., Lane L., Tilahun Y.,
RA Wright H.;
RT "The DNA sequence of human chromosome 22.";
RL Nature 402:489-495(1999).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA] (ISOFORM 1).
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=Brain;
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 INVOLVEMENT IN CDCBM8.
RX PubMed=19896110; DOI=10.1016/j.ajhg.2009.10.007;
RA Abdollahi M.R., Morrison E., Sirey T., Molnar Z., Hayward B.E., Carr I.M.,
RA Springell K., Woods C.G., Ahmed M., Hattingh L., Corry P., Pilz D.T.,
RA Stoodley N., Crow Y., Taylor G.R., Bonthron D.T., Sheridan E.;
RT "Mutation of the variant alpha-tubulin TUBA8 results in polymicrogyria with
RT optic nerve hypoplasia.";
RL Am. J. Hum. Genet. 85:737-744(2009).
RN [8]
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 [9]
RP TISSUE SPECIFICITY.
RX PubMed=20466094; DOI=10.1016/j.ajhg.2010.03.019;
RA Braun A., Breuss M., Salzer M.C., Flint J., Cowan N.J., Keays D.A.;
RT "Tuba8 is expressed at low levels in the developing mouse and human
RT brain.";
RL Am. J. Hum. Genet. 86:819-822(2010).
RN [10]
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).
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 Q9NY65; Q8N4U5: TCP11L2; NbExp=3; IntAct=EBI-356246, EBI-11897462;
CC -!- SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q9NY65-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q9NY65-2; Sequence=VSP_042810;
CC -!- TISSUE SPECIFICITY: Preferentially expressed in heart, skeletal muscle
CC and testis. Expressed at low levels in the developing brain.
CC {ECO:0000269|PubMed:20466094}.
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 -!- DISEASE: Cortical dysplasia, complex, with other brain malformations 8
CC (CDCBM8) [MIM:613180]: A disease characterized by extensive
CC polymicrogyria, optic nerve hypoplasia, severe developmental delay,
CC hypotonia, seizures, a dysplastic or absent corpus callosum and
CC colpocephaly. Polymicrogyria is a malformation of the cortex in which
CC the brain surface is irregular and characterized by an excessive number
CC of small gyri with abnormal lamination. Polymicrogyria is a
CC heterogeneous disorder, considered to be the result of postmigratory
CC abnormal cortical organization. {ECO:0000269|PubMed:19896110}. Note=The
CC disease is caused by variants affecting the gene represented in this
CC entry.
CC -!- MISCELLANEOUS: This tubulin does not have a C-terminal tyrosine.
CC -!- SIMILARITY: Belongs to the tubulin family. {ECO:0000305}.
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DR EMBL; AJ245922; CAB88036.1; -; mRNA.
DR EMBL; CR456600; CAG30486.1; -; mRNA.
DR EMBL; AK056947; BAG51831.1; -; mRNA.
DR EMBL; AK315316; BAG37719.1; -; mRNA.
DR EMBL; AC007934; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AC128680; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH471193; EAW57788.1; -; Genomic_DNA.
DR EMBL; CH471193; EAW57789.1; -; Genomic_DNA.
DR EMBL; BC074827; AAH74827.1; -; mRNA.
DR EMBL; BC104845; AAI04846.1; -; mRNA.
DR CCDS; CCDS13751.1; -. [Q9NY65-1]
DR CCDS; CCDS54495.1; -. [Q9NY65-2]
DR RefSeq; NP_001180343.1; NM_001193414.1. [Q9NY65-2]
DR RefSeq; NP_061816.1; NM_018943.2. [Q9NY65-1]
DR AlphaFoldDB; Q9NY65; -.
DR SMR; Q9NY65; -.
DR BioGRID; 108282; 152.
DR BioGRID; 119733; 72.
DR DIP; DIP-40751N; -.
DR IntAct; Q9NY65; 28.
DR MINT; Q9NY65; -.
DR STRING; 9606.ENSP00000333326; -.
DR BindingDB; Q9NY65; -.
DR ChEMBL; CHEMBL3714503; -.
DR DrugBank; DB01873; Epothilone D.
DR DrugBank; DB03010; Patupilone.
DR GlyGen; Q9NY65; 1 site, 1 O-linked glycan (1 site).
DR iPTMnet; Q9NY65; -.
DR PhosphoSitePlus; Q9NY65; -.
DR SwissPalm; Q9NY65; -.
DR BioMuta; TUBA8; -.
DR DMDM; 12585376; -.
DR EPD; Q9NY65; -.
DR jPOST; Q9NY65; -.
DR MassIVE; Q9NY65; -.
DR MaxQB; Q9NY65; -.
DR PaxDb; Q9NY65; -.
DR PeptideAtlas; Q9NY65; -.
DR PRIDE; Q9NY65; -.
DR ProteomicsDB; 83183; -. [Q9NY65-1]
DR ProteomicsDB; 83184; -. [Q9NY65-2]
DR Antibodypedia; 22762; 208 antibodies from 25 providers.
DR DNASU; 51807; -.
DR Ensembl; ENST00000316027.10; ENSP00000318575.6; ENSG00000183785.16. [Q9NY65-2]
DR Ensembl; ENST00000330423.8; ENSP00000333326.3; ENSG00000183785.16. [Q9NY65-1]
DR Ensembl; ENST00000416740.2; ENSP00000412646.2; ENSG00000183785.16. [Q9NY65-2]
DR GeneID; 51807; -.
DR KEGG; hsa:51807; -.
DR MANE-Select; ENST00000330423.8; ENSP00000333326.3; NM_018943.3; NP_061816.1.
DR UCSC; uc002znv.3; human. [Q9NY65-1]
DR CTD; 51807; -.
DR DisGeNET; 51807; -.
DR GeneCards; TUBA8; -.
DR HGNC; HGNC:12410; TUBA8.
DR HPA; ENSG00000183785; Tissue enhanced (heart muscle, skeletal muscle, tongue).
DR MalaCards; TUBA8; -.
DR MIM; 605742; gene.
DR MIM; 613180; phenotype.
DR neXtProt; NX_Q9NY65; -.
DR OpenTargets; ENSG00000183785; -.
DR Orphanet; 250972; Polymicrogyria with optic nerve hypoplasia.
DR PharmGKB; PA37074; -.
DR VEuPathDB; HostDB:ENSG00000183785; -.
DR eggNOG; KOG1376; Eukaryota.
DR GeneTree; ENSGT00940000159668; -.
DR HOGENOM; CLU_015718_0_1_1; -.
DR InParanoid; Q9NY65; -.
DR OMA; AQASKVN; -.
DR OrthoDB; 514396at2759; -.
DR PhylomeDB; Q9NY65; -.
DR TreeFam; TF300314; -.
DR PathwayCommons; Q9NY65; -.
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-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-5617833; Cilium Assembly.
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; Q9NY65; -.
DR SIGNOR; Q9NY65; -.
DR BioGRID-ORCS; 1962; 10 hits in 1082 CRISPR screens.
DR BioGRID-ORCS; 51807; 15 hits in 1071 CRISPR screens.
DR ChiTaRS; TUBA8; human.
DR GeneWiki; TUBA8; -.
DR Pharos; Q9NY65; Tbio.
DR PRO; PR:Q9NY65; -.
DR Proteomes; UP000005640; Chromosome 22.
DR RNAct; Q9NY65; protein.
DR Bgee; ENSG00000183785; Expressed in hindlimb stylopod muscle and 93 other tissues.
DR ExpressionAtlas; Q9NY65; baseline and differential.
DR Genevisible; Q9NY65; HS.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0005874; C:microtubule; IBA:GO_Central.
DR GO; GO:0015630; C:microtubule cytoskeleton; IDA:HPA.
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:0000226; P:microtubule cytoskeleton organization; IBA:GO_Central.
DR GO; GO:0007017; P:microtubule-based process; IEA:InterPro.
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 Alternative splicing; Cytoplasm; Cytoskeleton; GTP-binding; Microtubule;
KW Nucleotide-binding; Reference proteome.
FT CHAIN 1..449
FT /note="Tubulin alpha-8 chain"
FT /id="PRO_0000048113"
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 VAR_SEQ 1..66
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_042810"
FT VARIANT 128
FT /note="A -> V (in dbSNP:rs2234331)"
FT /id="VAR_052670"
FT VARIANT 301
FT /note="Q -> R (in dbSNP:rs2234333)"
FT /id="VAR_024680"
SQ SEQUENCE 449 AA; 50094 MW; 8D1AFB9D131529BD CRC64;
MRECISVHVG QAGVQIGNAC WELFCLEHGI QADGTFDAQA SKINDDDSFT TFFSETGNGK
HVPRAVMIDL EPTVVDEVRA GTYRQLFHPE QLITGKEDAA NNYARGHYTV GKESIDLVLD
RIRKLTDACS GLQGFLIFHS FGGGTGSGFT SLLMERLSLD YGKKSKLEFA IYPAPQVSTA
VVEPYNSILT THTTLEHSDC AFMVDNEAIY DICRRNLDIE RPTYTNLNRL ISQIVSSITA
SLRFDGALNV DLTEFQTNLV PYPRIHFPLV TYAPIISAEK AYHEQLSVAE ITSSCFEPNS
QMVKCDPRHG KYMACCMLYR GDVVPKDVNV AIAAIKTKRT IQFVDWCPTG FKVGINYQPP
TVVPGGDLAK VQRAVCMLSN TTAIAEAWAR LDHKFDLMYA KRAFVHWYVG EGMEEGEFSE
AREDLAALEK DYEEVGTDSF EEENEGEEF
