GenomeNet

Database: UniProt
Entry: Q13509
LinkDB: Q13509
Original site: Q13509 
ID   TBB3_HUMAN              Reviewed;         450 AA.
AC   Q13509; A8K854; Q9BTZ0; Q9BW10;
DT   15-JUL-1998, integrated into UniProtKB/Swiss-Prot.
DT   02-MAY-2002, sequence version 2.
DT   22-APR-2020, entry version 197.
DE   RecName: Full=Tubulin beta-3 chain;
DE   AltName: Full=Tubulin beta-4 chain;
DE   AltName: Full=Tubulin beta-III;
GN   Name=TUBB3; Synonyms=TUBB4;
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).
RX   PubMed=9473684; DOI=10.1016/s0167-4781(97)00168-1;
RA   Ranganathan S., Dexter D.W., Benetatos C.A., Hudes G.R.;
RT   "Cloning and sequencing of human betaIII-tubulin cDNA: induction of betaIII
RT   isotype in human prostate carcinoma cells by acute exposure to
RT   antimicrotubule agents.";
RL   Biochim. Biophys. Acta 1395:237-245(1998).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
RC   TISSUE=Mammary cancer;
RA   Banerjee A.;
RL   Submitted (OCT-2001) to the EMBL/GenBank/DDBJ databases.
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RC   TISSUE=Brain, and Esophagus;
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=15616553; DOI=10.1038/nature03187;
RA   Martin J., Han C., Gordon L.A., Terry A., Prabhakar S., She X., Xie G.,
RA   Hellsten U., Chan Y.M., Altherr M., Couronne O., Aerts A., Bajorek E.,
RA   Black S., Blumer H., Branscomb E., Brown N.C., Bruno W.J., Buckingham J.M.,
RA   Callen D.F., Campbell C.S., Campbell M.L., Campbell E.W., Caoile C.,
RA   Challacombe J.F., Chasteen L.A., Chertkov O., Chi H.C., Christensen M.,
RA   Clark L.M., Cohn J.D., Denys M., Detter J.C., Dickson M.,
RA   Dimitrijevic-Bussod M., Escobar J., Fawcett J.J., Flowers D., Fotopulos D.,
RA   Glavina T., Gomez M., Gonzales E., Goodstein D., Goodwin L.A., Grady D.L.,
RA   Grigoriev I., Groza M., Hammon N., Hawkins T., Haydu L., Hildebrand C.E.,
RA   Huang W., Israni S., Jett J., Jewett P.B., Kadner K., Kimball H.,
RA   Kobayashi A., Krawczyk M.-C., Leyba T., Longmire J.L., Lopez F., Lou Y.,
RA   Lowry S., Ludeman T., Manohar C.F., Mark G.A., McMurray K.L., Meincke L.J.,
RA   Morgan J., Moyzis R.K., Mundt M.O., Munk A.C., Nandkeshwar R.D.,
RA   Pitluck S., Pollard M., Predki P., Parson-Quintana B., Ramirez L., Rash S.,
RA   Retterer J., Ricke D.O., Robinson D.L., Rodriguez A., Salamov A.,
RA   Saunders E.H., Scott D., Shough T., Stallings R.L., Stalvey M.,
RA   Sutherland R.D., Tapia R., Tesmer J.G., Thayer N., Thompson L.S., Tice H.,
RA   Torney D.C., Tran-Gyamfi M., Tsai M., Ulanovsky L.E., Ustaszewska A.,
RA   Vo N., White P.S., Williams A.L., Wills P.L., Wu J.-R., Wu K., Yang J.,
RA   DeJong P., Bruce D., Doggett N.A., Deaven L., Schmutz J., Grimwood J.,
RA   Richardson P., Rokhsar D.S., Eichler E.E., Gilna P., Lucas S.M.,
RA   Myers R.M., Rubin E.M., Pennacchio L.A.;
RT   "The sequence and analysis of duplication-rich human chromosome 16.";
RL   Nature 432:988-994(2004).
RN   [5]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA   Mural R.J., Istrail S., Sutton 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 (SEP-2005) to the EMBL/GenBank/DDBJ databases.
RN   [6]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC   TISSUE=Lung;
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 63-77; 104-121; 242-251; 163-174 AND 381-390, AND
RP   IDENTIFICATION 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   TISSUE SPECIFICITY.
RX   PubMed=14736079; DOI=10.1177/088307380301801205;
RA   Katsetos C.D., Legido A., Perentes E., Mork S.J.;
RT   "Class III beta-tubulin isotype: a key cytoskeletal protein at the
RT   crossroads of developmental neurobiology and tumor neuropathology.";
RL   J. Child Neurol. 18:851-866(2003).
RN   [9]
RP   ERRATUM OF PUBMED:14736079.
RA   Katsetos C.D., Legido A., Perentes E., Mork S.J.;
RL   J. Child Neurol. 19:531-531(2004).
RN   [10]
RP   PHOSPHORYLATION AT SER-172 BY CDK1.
RX   PubMed=16371510; DOI=10.1091/mbc.e05-07-0621;
RA   Fourest-Lieuvin A., Peris L., Gache V., Garcia-Saez I., Juillan-Binard C.,
RA   Lantez V., Job D.;
RT   "Microtubule regulation in mitosis: tubulin phosphorylation by the cyclin-
RT   dependent kinase Cdk1.";
RL   Mol. Biol. Cell 17:1041-1050(2006).
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   FUNCTION, VARIANTS CFEOM3A GLN-62; CYS-262; HIS-262; THR-302; CYS-380;
RP   LYS-410; HIS-417 AND ASN-417, AND CHARACTERIZATION OF VARIANTS CFEOM3A
RP   GLN-62; CYS-262; HIS-262; THR-302; CYS-380 AND LYS-410.
RX   PubMed=20074521; DOI=10.1016/j.cell.2009.12.011;
RA   Tischfield M.A., Baris H.N., Wu C., Rudolph G., Van Maldergem L., He W.,
RA   Chan W.M., Andrews C., Demer J.L., Robertson R.L., Mackey D.A.,
RA   Ruddle J.B., Bird T.D., Gottlob I., Pieh C., Traboulsi E.I., Pomeroy S.L.,
RA   Hunter D.G., Soul J.S., Newlin A., Sabol L.J., Doherty E.J.,
RA   de Uzcategui C.E., de Uzcategui N., Collins M.L., Sener E.C., Wabbels B.,
RA   Hellebrand H., Meitinger T., de Berardinis T., Magli A., Schiavi C.,
RA   Pastore-Trossello M., Koc F., Wong A.M., Levin A.V., Geraghty M.T.,
RA   Descartes M., Flaherty M., Jamieson R.V., Moller H.U., Meuthen I.,
RA   Callen D.F., Kerwin J., Lindsay S., Meindl A., Gupta M.L. Jr., Pellman D.,
RA   Engle E.C.;
RT   "Human TUBB3 mutations perturb microtubule dynamics, kinesin interactions,
RT   and axon guidance.";
RL   Cell 140:74-87(2010).
RN   [13]
RP   TISSUE SPECIFICITY.
RX   PubMed=20191564; DOI=10.1002/cm.20436;
RA   Leandro-Garcia L.J., Leskela S., Landa I., Montero-Conde C.,
RA   Lopez-Jimenez E., Leton R., Cascon A., Robledo M., Rodriguez-Antona C.;
RT   "Tumoral and tissue-specific expression of the major human beta-tubulin
RT   isotypes.";
RL   Cytoskeleton 67:214-223(2010).
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   FUNCTION, AND INTERACTION WITH UNC5C.
RX   PubMed=28483977; DOI=10.1523/jneurosci.2617-16.2017;
RA   Shao Q., Yang T., Huang H., Alarmanazi F., Liu G.;
RT   "Uncoupling of UNC5C with Polymerized TUBB3 in Microtubules Mediates
RT   Netrin-1 Repulsion.";
RL   J. Neurosci. 37:5620-5633(2017).
RN   [16]
RP   VARIANTS CDCBM1 MET-178; LYS-205; VAL-302 AND VAL-323, AND CHARACTERIZATION
RP   OF VARIANTS CDCBM1 MET-178; LYS-205; VAL-302 AND VAL-323.
RX   PubMed=20829227; DOI=10.1093/hmg/ddq377;
RA   Poirier K., Saillour Y., Bahi-Buisson N., Jaglin X.H., Fallet-Bianco C.,
RA   Nabbout R., Castelnau-Ptakhine L., Roubertie A., Attie-Bitach T.,
RA   Desguerre I., Genevieve D., Barnerias C., Keren B., Lebrun N., Boddaert N.,
RA   Encha-Razavi F., Chelly J.;
RT   "Mutations in the neuronal ss-tubulin subunit TUBB3 result in malformation
RT   of cortical development and neuronal migration defects.";
RL   Hum. Mol. Genet. 19:4462-4473(2010).
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. TUBB3 plays a critical
CC       role in proper axon guidance and mantainance. Binding of NTN1/Netrin-1
CC       to its receptor UNC5C might cause dissociation of UNC5C from
CC       polymerized TUBB3 in microtubules and thereby lead to increased
CC       microtubule dynamics and axon repulsion (PubMed:28483977). Plays a role
CC       in dorsal root ganglion axon projection towards the spinal cord
CC       (PubMed:28483977). {ECO:0000269|PubMed:20074521,
CC       ECO:0000269|PubMed:28483977}.
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 UNC5C (via cytoplasmic domain); this
CC       interaction is decreased by NTN1/Netrin-1 (PubMed:28483977).
CC       {ECO:0000269|PubMed:28483977}.
CC   -!- INTERACTION:
CC       Q13509; P54274: TERF1; NbExp=2; IntAct=EBI-350989, EBI-710997;
CC       Q13509; P68363: TUBA1B; NbExp=3; IntAct=EBI-350989, EBI-487083;
CC       Q13509; O95185: UNC5C; NbExp=2; IntAct=EBI-350989, EBI-11343380;
CC   -!- SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton
CC       {ECO:0000250|UniProtKB:Q9ERD7}. Cell projection, lamellipodium
CC       {ECO:0000250|UniProtKB:Q9ERD7}. Cell projection, filopodium
CC       {ECO:0000250|UniProtKB:Q9ERD7}.
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=2;
CC       Name=1;
CC         IsoId=Q13509-1; Sequence=Displayed;
CC       Name=2;
CC         IsoId=Q13509-2; Sequence=VSP_054659;
CC   -!- TISSUE SPECIFICITY: Expression is primarily restricted to central and
CC       peripheral nervous system. Greatly increased expression in most
CC       cancerous tissues. {ECO:0000269|PubMed:14736079,
CC       ECO:0000269|PubMed:20191564}.
CC   -!- DOMAIN: The highly acidic C-terminal region may bind cations such as
CC       calcium.
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). {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 axonemes
CC       (cilia and flagella). Both polyglutamylation and monoglycylation can
CC       coexist on the same protein on adjacent residues, and lowering
CC       glycylation levels increases polyglutamylation, and reciprocally. The
CC       precise function of monoglycylation is still unclear (Probable).
CC       {ECO:0000305|PubMed:19524510}.
CC   -!- PTM: Phosphorylated on Ser-172 by CDK1 during the cell cycle, from
CC       metaphase to telophase, but not in interphase. This phosphorylation
CC       inhibits tubulin incorporation into microtubules.
CC       {ECO:0000269|PubMed:16371510}.
CC   -!- DISEASE: Fibrosis of extraocular muscles, congenital, 3A (CFEOM3A)
CC       [MIM:600638]: A congenital ocular motility disorder marked by
CC       restrictive ophthalmoplegia affecting extraocular muscles innervated by
CC       the oculomotor and/or trochlear nerves. It is clinically characterized
CC       by anchoring of the eyes in downward gaze, ptosis, and backward tilt of
CC       the head. Congenital fibrosis of extraocular muscles type 3 presents as
CC       a non-progressive, autosomal dominant disorder with variable
CC       expression. Patients may be bilaterally or unilaterally affected, and
CC       their oculo-motility defects range from complete ophthalmoplegia (with
CC       the eyes fixed in a hypo- and exotropic position), to mild asymptomatic
CC       restrictions of ocular movement. Ptosis, refractive error, amblyopia,
CC       and compensatory head positions are associated with the more severe
CC       forms of the disorder. In some cases, the ocular phenotype is
CC       accompanied by additional features including developmental delay,
CC       corpus callosum agenesis, basal ganglia dysmorphism, facial weakness,
CC       polyneuropathy. {ECO:0000269|PubMed:20074521}. Note=The disease is
CC       caused by mutations affecting the gene represented in this entry.
CC   -!- DISEASE: Cortical dysplasia, complex, with other brain malformations 1
CC       (CDCBM1) [MIM:614039]: A disorder of aberrant neuronal migration and
CC       disturbed axonal guidance. Affected individuals have mild to severe
CC       mental retardation, strabismus, axial hypotonia, and spasticity. Brain
CC       imaging shows variable malformations of cortical development, including
CC       polymicrogyria, gyral disorganization, and fusion of the basal ganglia,
CC       as well as thin corpus callosum, hypoplastic brainstem, and dysplastic
CC       cerebellar vermis. Extraocular muscles are not involved.
CC       {ECO:0000269|PubMed:20829227}. Note=The disease is caused by mutations
CC       affecting the gene represented in this entry.
CC   -!- SIMILARITY: Belongs to the tubulin family. {ECO:0000305}.
DR   EMBL; U47634; AAC52035.1; -; mRNA.
DR   EMBL; AF427491; AAL28094.1; -; mRNA.
DR   EMBL; AK122757; BAG53710.1; -; mRNA.
DR   EMBL; AK292219; BAF84908.1; -; mRNA.
DR   EMBL; AC092143; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; CH471184; EAW66674.1; -; Genomic_DNA.
DR   EMBL; BC000748; AAH00748.1; -; mRNA.
DR   EMBL; BC003021; AAH03021.2; -; mRNA.
DR   CCDS; CCDS10988.1; -. [Q13509-1]
DR   CCDS; CCDS56012.1; -. [Q13509-2]
DR   RefSeq; NP_001184110.1; NM_001197181.1. [Q13509-2]
DR   RefSeq; NP_006077.2; NM_006086.3. [Q13509-1]
DR   PDB; 5IJ0; EM; 3.80 A; B=1-426.
DR   PDB; 5IJ9; EM; 3.70 A; B=1-426.
DR   PDB; 5JCO; EM; 4.00 A; C/D/I/J/K/L=1-426.
DR   PDB; 6E7B; EM; 3.50 A; B=1-426.
DR   PDB; 6S8L; X-ray; 1.80 A; B=1-450.
DR   PDBsum; 5IJ0; -.
DR   PDBsum; 5IJ9; -.
DR   PDBsum; 5JCO; -.
DR   PDBsum; 6E7B; -.
DR   PDBsum; 6S8L; -.
DR   SMR; Q13509; -.
DR   BioGrid; 115654; 307.
DR   CORUM; Q13509; -.
DR   DIP; DIP-31505N; -.
DR   IntAct; Q13509; 263.
DR   MINT; Q13509; -.
DR   STRING; 9606.ENSP00000320295; -.
DR   ChEMBL; CHEMBL2597; -.
DR   DrugBank; DB05147; CYT997.
DR   DrugBank; DB01873; Epothilone D.
DR   DrugBank; DB04845; Ixabepilone.
DR   DrugBank; DB03010; Patupilone.
DR   DrugBank; DB12695; Phenethyl Isothiocyanate.
DR   DrugBank; DB06042; ZEN-012.
DR   DrugCentral; Q13509; -.
DR   GuidetoPHARMACOLOGY; 2752; -.
DR   iPTMnet; Q13509; -.
DR   MetOSite; Q13509; -.
DR   PhosphoSitePlus; Q13509; -.
DR   SwissPalm; Q13509; -.
DR   BioMuta; TUBB3; -.
DR   DMDM; 20455526; -.
DR   OGP; Q13509; -.
DR   EPD; Q13509; -.
DR   jPOST; Q13509; -.
DR   MassIVE; Q13509; -.
DR   MaxQB; Q13509; -.
DR   PaxDb; Q13509; -.
DR   PeptideAtlas; Q13509; -.
DR   PRIDE; Q13509; -.
DR   ProteomicsDB; 1874; -.
DR   ProteomicsDB; 59510; -. [Q13509-1]
DR   TopDownProteomics; Q13509-1; -. [Q13509-1]
DR   Antibodypedia; 54822; 986 antibodies.
DR   DNASU; 10381; -.
DR   Ensembl; ENST00000315491; ENSP00000320295; ENSG00000258947. [Q13509-1]
DR   Ensembl; ENST00000554444; ENSP00000451617; ENSG00000258947. [Q13509-2]
DR   GeneID; 10381; -.
DR   KEGG; hsa:10381; -.
DR   UCSC; uc002fph.2; human. [Q13509-1]
DR   CTD; 10381; -.
DR   DisGeNET; 10381; -.
DR   GeneCards; TUBB3; -.
DR   GeneReviews; TUBB3; -.
DR   HGNC; HGNC:20772; TUBB3.
DR   HPA; ENSG00000258947; Tissue enriched (brain).
DR   MalaCards; TUBB3; -.
DR   MIM; 600638; phenotype.
DR   MIM; 602661; gene.
DR   MIM; 614039; phenotype.
DR   neXtProt; NX_Q13509; -.
DR   OpenTargets; ENSG00000258947; -.
DR   Orphanet; 45358; Congenital fibrosis of extraocular muscles.
DR   Orphanet; 300570; Cortical dysgenesis with pontocerebellar hypoplasia due to TUBB3 mutation.
DR   Orphanet; 467166; Tubulinopathy-associated dysgyria.
DR   PharmGKB; PA134953867; -.
DR   eggNOG; KOG1375; Eukaryota.
DR   eggNOG; COG5023; LUCA.
DR   GeneTree; ENSGT00940000159115; -.
DR   HOGENOM; CLU_015718_0_0_1; -.
DR   InParanoid; Q13509; -.
DR   KO; K07375; -.
DR   PhylomeDB; Q13509; -.
DR   TreeFam; TF300298; -.
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).
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-983189; Kinesins.
DR   SIGNOR; Q13509; -.
DR   ChiTaRS; TUBB3; human.
DR   GeneWiki; TUBB3; -.
DR   GenomeRNAi; 10381; -.
DR   Pharos; Q13509; Tclin.
DR   PRO; PR:Q13509; -.
DR   Proteomes; UP000005640; Chromosome 16.
DR   RNAct; Q13509; protein.
DR   Bgee; ENSG00000258947; Expressed in hypothalamus and 86 other tissues.
DR   ExpressionAtlas; Q13509; baseline and differential.
DR   Genevisible; Q13509; HS.
DR   GO; GO:0030424; C:axon; ISS:ARUK-UCL.
DR   GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR   GO; GO:0030425; C:dendrite; ISS:ParkinsonsUK-UCL.
DR   GO; GO:0070062; C:extracellular exosome; HDA:UniProtKB.
DR   GO; GO:0030175; C:filopodium; ISS:UniProtKB.
DR   GO; GO:0030426; C:growth cone; ISS:UniProtKB.
DR   GO; GO:0030027; C:lamellipodium; ISS:UniProtKB.
DR   GO; GO:0005874; C:microtubule; IDA:UniProtKB.
DR   GO; GO:0005634; C:nucleus; HDA:UniProtKB.
DR   GO; GO:0005525; F:GTP binding; IBA:GO_Central.
DR   GO; GO:0003924; F:GTPase activity; IEA:InterPro.
DR   GO; GO:1990890; F:netrin receptor binding; IPI:UniProtKB.
DR   GO; GO:0005200; F:structural constituent of cytoskeleton; IBA:GO_Central.
DR   GO; GO:0007411; P:axon guidance; IMP:UniProtKB.
DR   GO; GO:1990791; P:dorsal root ganglion development; IDA:UniProtKB.
DR   GO; GO:0000226; P:microtubule cytoskeleton organization; IBA:GO_Central.
DR   GO; GO:0007017; P:microtubule-based process; IBA:GO_Central.
DR   GO; GO:0000278; P:mitotic cell cycle; IBA:GO_Central.
DR   GO; GO:0030182; P:neuron differentiation; 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; IPR013838; Beta-tubulin_BS.
DR   InterPro; IPR002453; Beta_tubulin.
DR   InterPro; IPR008280; Tub_FtsZ_C.
DR   InterPro; IPR000217; Tubulin.
DR   InterPro; IPR018316; Tubulin/FtsZ_2-layer-sand-dom.
DR   InterPro; IPR037103; Tubulin/FtsZ_C_sf.
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; PR01163; BETATUBULIN.
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.
DR   PROSITE; PS00228; TUBULIN_B_AUTOREG; 1.
PE   1: Evidence at protein level;
KW   3D-structure; Alternative splicing; Cell projection; Cytoplasm;
KW   Cytoskeleton; Direct protein sequencing; Disease mutation; GTP-binding;
KW   Isopeptide bond; Microtubule; Nucleotide-binding; Phosphoprotein;
KW   Reference proteome.
FT   CHAIN           1..450
FT                   /note="Tubulin beta-3 chain"
FT                   /id="PRO_0000048250"
FT   NP_BIND         140..146
FT                   /note="GTP"
FT                   /evidence="ECO:0000255"
FT   MOD_RES         172
FT                   /note="Phosphoserine; by CDK1"
FT                   /evidence="ECO:0000269|PubMed:16371510"
FT   MOD_RES         438
FT                   /note="5-glutamyl polyglutamate"
FT                   /evidence="ECO:0000250|UniProtKB:Q2T9S0"
FT   MOD_RES         444
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q2T9S0"
FT   VAR_SEQ         1..72
FT                   /note="Missing (in isoform 2)"
FT                   /evidence="ECO:0000303|PubMed:14702039"
FT                   /id="VSP_054659"
FT   VARIANT         62
FT                   /note="R -> Q (in CFEOM3A; affects heterodimers formation;
FT                   results in increased stability and reduced dynamics of
FT                   microtubules; dbSNP:rs864321714)"
FT                   /evidence="ECO:0000269|PubMed:20074521"
FT                   /id="VAR_062758"
FT   VARIANT         178
FT                   /note="T -> M (in CDCBM1; can form tubulin heterodimers
FT                   that are properly incorporated into microtubules; the
FT                   microtubules are less stable than wild-type;
FT                   dbSNP:rs747480526)"
FT                   /evidence="ECO:0000269|PubMed:20829227"
FT                   /id="VAR_066206"
FT   VARIANT         205
FT                   /note="E -> K (in CDCBM1; does not form tubulin
FT                   heterodimers; patient fibroblasts show no major alterations
FT                   in the microtubule network, but the microtubules are less
FT                   stable than wild-type; dbSNP:rs878853257)"
FT                   /evidence="ECO:0000269|PubMed:20829227"
FT                   /id="VAR_066207"
FT   VARIANT         262
FT                   /note="R -> C (in CFEOM3A; affects heterodimers formation;
FT                   affects microtubules polymerization and depolymerization
FT                   rates; dbSNP:rs267607162)"
FT                   /evidence="ECO:0000269|PubMed:20074521"
FT                   /id="VAR_062759"
FT   VARIANT         262
FT                   /note="R -> H (in CFEOM3A; severe phenotype with congenital
FT                   facial weakness, congenital wrist and finger contractures;
FT                   affects microtubules polymerization and depolymerization
FT                   rates; dbSNP:rs864321716)"
FT                   /evidence="ECO:0000269|PubMed:20074521"
FT                   /id="VAR_062760"
FT   VARIANT         302
FT                   /note="A -> T (in CFEOM3A; affects heterodimers formation;
FT                   results in increased stability and reduced dynamics of
FT                   microtubules; dbSNP:rs267607163)"
FT                   /evidence="ECO:0000269|PubMed:20074521"
FT                   /id="VAR_062761"
FT   VARIANT         302
FT                   /note="A -> V (in CDCBM1; does not form tubulin
FT                   heterodimers; dbSNP:rs878853258)"
FT                   /evidence="ECO:0000269|PubMed:20829227"
FT                   /id="VAR_066208"
FT   VARIANT         323
FT                   /note="M -> V (in CDCBM1; reduced heterodimers formation;
FT                   dbSNP:rs878853256)"
FT                   /evidence="ECO:0000269|PubMed:20829227"
FT                   /id="VAR_066209"
FT   VARIANT         380
FT                   /note="R -> C (in CFEOM3A; affects heterodimers formation;
FT                   results in increased stability and reduced dynamics of
FT                   microtubules; dbSNP:rs864321717)"
FT                   /evidence="ECO:0000269|PubMed:20074521"
FT                   /id="VAR_062762"
FT   VARIANT         410
FT                   /note="E -> K (in CFEOM3A; severe phenotype with congenital
FT                   facial weakness; lower extremity weakness and sensory loss
FT                   in the second to third decade of life in one patient;
FT                   affects microtubules polymerization and depolymerization
FT                   rates; dbSNP:rs267607165)"
FT                   /evidence="ECO:0000269|PubMed:20074521"
FT                   /id="VAR_062763"
FT   VARIANT         417
FT                   /note="D -> H (in CFEOM3A; severe phenotype with congenital
FT                   facial weakness, congenital wrist and finger contractures;
FT                   dbSNP:rs267607164)"
FT                   /evidence="ECO:0000269|PubMed:20074521"
FT                   /id="VAR_062764"
FT   VARIANT         417
FT                   /note="D -> N (in CFEOM3A; some patients with lower
FT                   extremity weakness and sensory loss in the second to third
FT                   decade of life; also found in patients without CFEOM3A who
FT                   developed polyneuropathy; dbSNP:rs267607164)"
FT                   /evidence="ECO:0000269|PubMed:20074521"
FT                   /id="VAR_062765"
FT   CONFLICT        275
FT                   /note="A -> R (in Ref. 1; AAC52035)"
FT                   /evidence="ECO:0000305"
FT   STRAND          4..9
FT                   /evidence="ECO:0000244|PDB:6S8L"
FT   HELIX           10..28
FT                   /evidence="ECO:0000244|PDB:6S8L"
FT   HELIX           42..45
FT                   /evidence="ECO:0000244|PDB:6S8L"
FT   HELIX           47..49
FT                   /evidence="ECO:0000244|PDB:6S8L"
FT   STRAND          51..53
FT                   /evidence="ECO:0000244|PDB:6S8L"
FT   STRAND          59..61
FT                   /evidence="ECO:0000244|PDB:6S8L"
FT   STRAND          63..69
FT                   /evidence="ECO:0000244|PDB:6S8L"
FT   HELIX           71..77
FT                   /evidence="ECO:0000244|PDB:6S8L"
FT   HELIX           82..84
FT                   /evidence="ECO:0000244|PDB:6S8L"
FT   HELIX           87..89
FT                   /evidence="ECO:0000244|PDB:6S8L"
FT   STRAND          90..92
FT                   /evidence="ECO:0000244|PDB:6S8L"
FT   HELIX           101..106
FT                   /evidence="ECO:0000244|PDB:6S8L"
FT   HELIX           108..125
FT                   /evidence="ECO:0000244|PDB:6S8L"
FT   STRAND          132..142
FT                   /evidence="ECO:0000244|PDB:6S8L"
FT   HELIX           143..158
FT                   /evidence="ECO:0000244|PDB:6S8L"
FT   STRAND          162..170
FT                   /evidence="ECO:0000244|PDB:6S8L"
FT   HELIX           181..195
FT                   /evidence="ECO:0000244|PDB:6S8L"
FT   STRAND          197..203
FT                   /evidence="ECO:0000244|PDB:6S8L"
FT   HELIX           204..213
FT                   /evidence="ECO:0000244|PDB:6S8L"
FT   HELIX           222..241
FT                   /evidence="ECO:0000244|PDB:6S8L"
FT   HELIX           250..257
FT                   /evidence="ECO:0000244|PDB:6S8L"
FT   STRAND          265..272
FT                   /evidence="ECO:0000244|PDB:6S8L"
FT   HELIX           286..294
FT                   /evidence="ECO:0000244|PDB:6S8L"
FT   HELIX           296..298
FT                   /evidence="ECO:0000244|PDB:6S8L"
FT   STRAND          299..302
FT                   /evidence="ECO:0000244|PDB:6S8L"
FT   HELIX           305..307
FT                   /evidence="ECO:0000244|PDB:6S8L"
FT   STRAND          310..320
FT                   /evidence="ECO:0000244|PDB:6S8L"
FT   HELIX           323..335
FT                   /evidence="ECO:0000244|PDB:6S8L"
FT   HELIX           338..340
FT                   /evidence="ECO:0000244|PDB:6S8L"
FT   STRAND          349..356
FT                   /evidence="ECO:0000244|PDB:6S8L"
FT   STRAND          364..371
FT                   /evidence="ECO:0000244|PDB:6S8L"
FT   HELIX           372..374
FT                   /evidence="ECO:0000244|PDB:6S8L"
FT   HELIX           375..390
FT                   /evidence="ECO:0000244|PDB:6S8L"
FT   TURN            391..394
FT                   /evidence="ECO:0000244|PDB:6S8L"
FT   HELIX           395..399
FT                   /evidence="ECO:0000244|PDB:6S8L"
FT   TURN            400..402
FT                   /evidence="ECO:0000244|PDB:6S8L"
FT   HELIX           405..427
FT                   /evidence="ECO:0000244|PDB:6S8L"
SQ   SEQUENCE   450 AA;  50433 MW;  4B9CDE7DBA102949 CRC64;
     MREIVHIQAG QCGNQIGAKF WEVISDEHGI DPSGNYVGDS DLQLERISVY YNEASSHKYV
     PRAILVDLEP GTMDSVRSGA FGHLFRPDNF IFGQSGAGNN WAKGHYTEGA ELVDSVLDVV
     RKECENCDCL QGFQLTHSLG GGTGSGMGTL LISKVREEYP DRIMNTFSVV PSPKVSDTVV
     EPYNATLSIH QLVENTDETY CIDNEALYDI CFRTLKLATP TYGDLNHLVS ATMSGVTTSL
     RFPGQLNADL RKLAVNMVPF PRLHFFMPGF APLTARGSQQ YRALTVPELT QQMFDAKNMM
     AACDPRHGRY LTVATVFRGR MSMKEVDEQM LAIQSKNSSY FVEWIPNNVK VAVCDIPPRG
     LKMSSTFIGN STAIQELFKR ISEQFTAMFR RKAFLHWYTG EGMDEMEFTE AESNMNDLVS
     EYQQYQDATA EEEGEMYEDD EEESEAQGPK
//
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