ID C9JJQ8_HUMAN Unreviewed; 198 AA. AC C9JJQ8; DT 03-NOV-2009, integrated into UniProtKB/TrEMBL. DT 03-NOV-2009, sequence version 1. DT 24-JUL-2024, entry version 94. DE RecName: Full=Tubulin alpha chain {ECO:0000256|RuleBase:RU000352}; DE Flags: Fragment; GN Name=TUBA4A {ECO:0000313|Ensembl:ENSP00000416992.1}; 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 {ECO:0000313|Ensembl:ENSP00000416992.1, ECO:0000313|Proteomes:UP000005640}; RN [1] {ECO:0000313|Proteomes:UP000005640} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RX PubMed=15815621; DOI=10.1038/nature03466; RA Hillier L.W., Graves T.A., Fulton R.S., Fulton L.A., Pepin K.H., Minx P., RA Wagner-McPherson C., Layman D., Wylie K., Sekhon M., Becker M.C., RA Fewell G.A., Delehaunty K.D., Miner T.L., Nash W.E., Kremitzki C., Oddy L., RA Du H., Sun H., Bradshaw-Cordum H., Ali J., Carter J., Cordes M., Harris A., RA Isak A., van Brunt A., Nguyen C., Du F., Courtney L., Kalicki J., RA Ozersky P., Abbott S., Armstrong J., Belter E.A., Caruso L., Cedroni M., RA Cotton M., Davidson T., Desai A., Elliott G., Erb T., Fronick C., Gaige T., RA Haakenson W., Haglund K., Holmes A., Harkins R., Kim K., Kruchowski S.S., RA Strong C.M., Grewal N., Goyea E., Hou S., Levy A., Martinka S., Mead K., RA McLellan M.D., Meyer R., Randall-Maher J., Tomlinson C., RA Dauphin-Kohlberg S., Kozlowicz-Reilly A., Shah N., Swearengen-Shahid S., RA Snider J., Strong J.T., Thompson J., Yoakum M., Leonard S., Pearman C., RA Trani L., Radionenko M., Waligorski J.E., Wang C., Rock S.M., RA Tin-Wollam A.-M., Maupin R., Latreille P., Wendl M.C., Yang S.-P., Pohl C., RA Wallis J.W., Spieth J., Bieri T.A., Berkowicz N., Nelson J.O., Osborne J., RA Ding L., Meyer R., Sabo A., Shotland Y., Sinha P., Wohldmann P.E., RA Cook L.L., Hickenbotham M.T., Eldred J., Williams D., Jones T.A., She X., RA Ciccarelli F.D., Izaurralde E., Taylor J., Schmutz J., Myers R.M., RA Cox D.R., Huang X., McPherson J.D., Mardis E.R., Clifton S.W., Warren W.C., RA Chinwalla A.T., Eddy S.R., Marra M.A., Ovcharenko I., Furey T.S., RA Miller W., Eichler E.E., Bork P., Suyama M., Torrents D., Waterston R.H., RA Wilson R.K.; RT "Generation and annotation of the DNA sequences of human chromosomes 2 and RT 4."; RL Nature 434:724-731(2005). RN [2] {ECO:0007829|PubMed:18691976} RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. 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 [3] {ECO:0007829|PubMed:18669648} RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. 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 [4] {ECO:0007829|PubMed:21269460} 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., Burckstummer 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 [5] {ECO:0007829|PubMed:23186163} RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RX PubMed=23186163; RA Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J., RA Mohammed S.; RT "Toward a comprehensive characterization of a human cancer cell RT phosphoproteome."; RL J. Proteome Res. 12:260-271(2013). RN [6] {ECO:0007829|PubMed:24275569} RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. 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 [7] {ECO:0007829|PubMed:25944712} RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RX PubMed=25944712; RA Vaca Jacome A.S., Rabilloud T., Schaeffer-Reiss C., Rompais M., Ayoub D., RA Lane L., Bairoch A., Van Dorsselaer A., Carapito C.; RT "N-terminome analysis of the human mitochondrial proteome."; RL Proteomics 15:2519-2524(2015). RN [8] {ECO:0000313|Ensembl:ENSP00000416992.1} RP IDENTIFICATION. RG Ensembl; RL Submitted (APR-2024) to UniProtKB. CC -!- FUNCTION: Tubulin is the major constituent of microtubules, a cylinder CC consisting of laterally associated linear protofilaments composed of CC alpha- and beta-tubulin heterodimers. Microtubules grow by the addition CC of GTP-tubulin dimers to the microtubule end, where a stabilizing cap CC forms. Below the cap, tubulin dimers are in GDP-bound state, owing to CC GTPase activity of alpha-tubulin. {ECO:0000256|RuleBase:RU000352}. CC -!- CATALYTIC ACTIVITY: CC Reaction=GTP + H2O = GDP + H(+) + phosphate; Xref=Rhea:RHEA:19669, CC ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:37565, CC ChEBI:CHEBI:43474, ChEBI:CHEBI:58189; CC Evidence={ECO:0000256|ARBA:ARBA00001702}; CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:19670; CC Evidence={ECO:0000256|ARBA:ARBA00001702}; CC -!- COFACTOR: CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420; CC Evidence={ECO:0000256|ARBA:ARBA00001946}; 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. {ECO:0000256|RuleBase:RU000352}. CC -!- SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton CC {ECO:0000256|ARBA:ARBA00004245}. CC -!- SIMILARITY: Belongs to the tubulin family. CC {ECO:0000256|ARBA:ARBA00009636, ECO:0000256|RuleBase:RU000352}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; AC068946; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR AlphaFoldDB; C9JJQ8; -. DR SMR; C9JJQ8; -. DR SwissPalm; C9JJQ8; -. DR MassIVE; C9JJQ8; -. DR PRIDE; C9JJQ8; -. DR ProteomicsDB; 10490; -. DR Antibodypedia; 3138; 541 antibodies from 39 providers. DR Ensembl; ENST00000456818.5; ENSP00000416992.1; ENSG00000127824.15. DR UCSC; uc061suz.1; human. DR HGNC; HGNC:12407; TUBA4A. DR VEuPathDB; HostDB:ENSG00000127824; -. DR GeneTree; ENSGT00950000183165; -. DR ChiTaRS; TUBA4A; human. DR Proteomes; UP000005640; Chromosome 2. DR Bgee; ENSG00000127824; Expressed in gingival epithelium and 205 other cell types or tissues. DR ExpressionAtlas; C9JJQ8; baseline and differential. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-KW. DR GO; GO:0005874; C:microtubule; IEA:UniProtKB-KW. DR GO; GO:0015630; C:microtubule cytoskeleton; IDA:HPA. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-UniRule. DR GO; GO:0016787; F:hydrolase activity; IEA:UniProtKB-KW. DR GO; GO:0005200; F:structural constituent of cytoskeleton; IEA:InterPro. DR GO; GO:0007017; P:microtubule-based process; IEA:InterPro. DR Gene3D; 3.40.50.1440; Tubulin/FtsZ, GTPase domain; 1. DR InterPro; IPR002452; Alpha_tubulin. DR InterPro; IPR000217; Tubulin. DR InterPro; IPR036525; Tubulin/FtsZ_GTPase_sf. DR InterPro; IPR017975; Tubulin_CS. DR InterPro; IPR003008; Tubulin_FtsZ_GTPase. DR PANTHER; PTHR11588; TUBULIN; 1. DR PANTHER; PTHR11588:SF53; TUBULIN ALPHA-4A CHAIN; 1. DR Pfam; PF00091; Tubulin; 1. DR PRINTS; PR01162; ALPHATUBULIN. DR PRINTS; PR01161; TUBULIN. DR SMART; SM00864; Tubulin; 1. DR SUPFAM; SSF52490; Tubulin nucleotide-binding domain-like; 1. DR PROSITE; PS00227; TUBULIN; 1. PE 1: Evidence at protein level; KW Cytoplasm {ECO:0000256|ARBA:ARBA00022490}; KW Cytoskeleton {ECO:0000256|ARBA:ARBA00023212}; KW GTP-binding {ECO:0000256|ARBA:ARBA00023134, ECO:0000256|RuleBase:RU000352}; KW Hydrolase {ECO:0000256|ARBA:ARBA00022801}; KW Microtubule {ECO:0000256|ARBA:ARBA00022701, ECO:0000256|RuleBase:RU000352}; KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, KW ECO:0000256|RuleBase:RU000352}; KW Proteomics identification {ECO:0007829|PeptideAtlas:C9JJQ8, KW ECO:0007829|ProteomicsDB:C9JJQ8}; KW Reference proteome {ECO:0000313|Proteomes:UP000005640}. FT DOMAIN 72..198 FT /note="Tubulin/FtsZ GTPase" FT /evidence="ECO:0000259|SMART:SM00864" FT NON_TER 198 FT /evidence="ECO:0000313|Ensembl:ENSP00000416992.1" SQ SEQUENCE 198 AA; 21678 MW; E311C05987F08A25 CRC64; MAPILPGTRR VTSGASPQVP LPFWRECISV HVGQAGVQMG NACWELYCLE HGIQPDGQMP SDKTIGGGDD SFTTFFCETG AGKHVPRAVF VDLEPTVIDE IRNGPYRQLF HPEQLITGKE DAANNYARGH YTIGKEIIDP VLDRIRKLSD QCTGLQGFLV FHSFGGGTGS GFTSLLMERL SVDYGKKSKL EFSIYPAP //