GENTAUR Molecular Products.

 TBB1_HUMAN              Reviewed;         451 AA.
 Q9H4B7;
 01-FEB-2005, integrated into UniProtKB/Swiss-Prot.
 01-MAR-2001, sequence version 1.
 12-SEP-2018, entry version 149.
 RecName: Full=Tubulin beta-1 chain;
 Name=TUBB1;
 Homo sapiens (Human).
 Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
 Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
 Catarrhini; Hominidae; Homo.
 NCBI_TaxID=9606;
 [1]
 NUCLEOTIDE SEQUENCE [MRNA].
 Gross C., Kussmann S., Hehr A., Hansmann I., Schlote D.;
 "Mapping and characterization of the human TUBB1 gene.";
 Submitted (JUL-2000) to the EMBL/GenBank/DDBJ databases.
 [2]
 NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
 PubMed=11780052; DOI=10.1038/414865a;
 Deloukas P., Matthews L.H., Ashurst J.L., Burton J., Gilbert J.G.R.,
 Jones M., Stavrides G., Almeida J.P., Babbage A.K., Bagguley C.L.,
 Bailey J., Barlow K.F., Bates K.N., Beard L.M., Beare D.M.,
 Beasley O.P., Bird C.P., Blakey S.E., Bridgeman A.M., Brown A.J.,
 Buck D., Burrill W.D., Butler A.P., Carder C., Carter N.P.,
 Chapman J.C., Clamp M., Clark G., Clark L.N., Clark S.Y., Clee C.M.,
 Clegg S., Cobley V.E., Collier R.E., Connor R.E., Corby N.R.,
 Coulson A., Coville G.J., Deadman R., Dhami P.D., Dunn M.,
 Ellington A.G., Frankland J.A., Fraser A., French L., Garner P.,
 Grafham D.V., Griffiths C., Griffiths M.N.D., Gwilliam R., Hall R.E.,
 Hammond S., Harley J.L., Heath P.D., Ho S., Holden J.L., Howden P.J.,
 Huckle E., Hunt A.R., Hunt S.E., Jekosch K., Johnson C.M., Johnson D.,
 Kay M.P., Kimberley A.M., King A., Knights A., Laird G.K., Lawlor S.,
 Lehvaeslaiho M.H., Leversha M.A., Lloyd C., Lloyd D.M., Lovell J.D.,
 Marsh V.L., Martin S.L., McConnachie L.J., McLay K., McMurray A.A.,
 Milne S.A., Mistry D., Moore M.J.F., Mullikin J.C., Nickerson T.,
 Oliver K., Parker A., Patel R., Pearce T.A.V., Peck A.I.,
 Phillimore B.J.C.T., Prathalingam S.R., Plumb R.W., Ramsay H.,
 Rice C.M., Ross M.T., Scott C.E., Sehra H.K., Shownkeen R., Sims S.,
 Skuce C.D., Smith M.L., Soderlund C., Steward C.A., Sulston J.E.,
 Swann R.M., Sycamore N., Taylor R., Tee L., Thomas D.W., Thorpe A.,
 Tracey A., Tromans A.C., Vaudin M., Wall M., Wallis J.M.,
 Whitehead S.L., Whittaker P., Willey D.L., Williams L., Williams S.A.,
 Wilming L., Wray P.W., Hubbard T., Durbin R.M., Bentley D.R., Beck S.,
 Rogers J.;
 "The DNA sequence and comparative analysis of human chromosome 20.";
 Nature 414:865-871(2001).
 [3]
 NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
 TISSUE=Brain;
 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).
 [4]
 PROTEIN SEQUENCE OF 38-46 AND 263-281.
 TISSUE=Platelet;
 PubMed=12665801; DOI=10.1038/nbt810;
 Gevaert K., Goethals M., Martens L., Van Damme J., Staes A.,
 Thomas G.R., Vandekerckhove J.;
 "Exploring proteomes and analyzing protein processing by mass
 spectrometric identification of sorted N-terminal peptides.";
 Nat. Biotechnol. 21:566-569(2003).
 [5]
 PHOSPHORYLATION AT SER-172.
 PubMed=16371510; DOI=10.1091/mbc.E05-07-0621;
 Fourest-Lieuvin A., Peris L., Gache V., Garcia-Saez I.,
 Juillan-Binard C., Lantez V., Job D.;
 "Microtubule regulation in mitosis: tubulin phosphorylation by the
 cyclin-dependent kinase Cdk1.";
 Mol. Biol. Cell 17:1041-1050(2006).
 [6]
 INTERACTION WITH RANBP10.
 PubMed=18347012; DOI=10.1074/jbc.M709397200;
 Schulze H., Dose M., Korpal M., Meyer I., Italiano J.E. Jr.,
 Shivdasani R.A.;
 "RanBP10 is a cytoplasmic guanine nucleotide exchange factor that
 modulates noncentrosomal microtubules.";
 J. Biol. Chem. 283:14109-14119(2008).
 [7]
 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).
 [8]
 TISSUE SPECIFICITY.
 PubMed=20191564; DOI=10.1002/cm.20436;
 Leandro-Garcia L.J., Leskela S., Landa I., Montero-Conde C.,
 Lopez-Jimenez E., Leton R., Cascon A., Robledo M.,
 Rodriguez-Antona C.;
 "Tumoral and tissue-specific expression of the major human beta-
 tubulin isotypes.";
 Cytoskeleton 67:214-223(2010).
 [9]
 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).
 [10]
 VARIANT PRO-43.
 PubMed=15956286; DOI=10.1182/blood-2005-02-0723;
 Freson K., De Vos R., Wittevrongel C., Thys C., Defoor J., Vanhees L.,
 Vermylen J., Peerlinck K., Van Geet C.;
 "The TUBB1 Q43P functional polymorphism reduces the risk of
 cardiovascular disease in men by modulating platelet function and
 structure.";
 Blood 106:2356-2362(2005).
 [11]
 VARIANTS PRO-43 AND HIS-307, VARIANT MAD-TUBB1 TRP-318, AND
 SUBCELLULAR LOCATION.
 PubMed=18849486; DOI=10.1182/blood-2008-06-162610;
 Kunishima S., Kobayashi R., Itoh T.J., Hamaguchi M., Saito H.;
 "Mutation of the beta1-tubulin gene associated with congenital
 macrothrombocytopenia affecting microtubule assembly.";
 Blood 113:458-461(2009).
 -!- 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 (By
     similarity). {ECO:0000250}.
 -!- 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 RANBP10.
     {ECO:0000269|PubMed:18347012}.
 -!- SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton
     {ECO:0000269|PubMed:18849486}.
 -!- TISSUE SPECIFICITY: Hematopoietic cell-specific. Major isotype in
     leukocytes, where it represents 50% of all beta-tubulins.
     {ECO:0000269|PubMed:20191564}.
 -!- 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: Phosphorylated on Ser-172 by CDK1 during the cell cycle, from
     metaphase to telophase, but not in interphase. This
     phosphorylation inhibits tubulin incorporation into microtubules.
     {ECO:0000269|PubMed:16371510}.
 -!- DISEASE: Macrothrombocytopenia, autosomal dominant, TUBB1-related
     (MAD-TUBB1) [MIM:613112]: A congenital blood disorder
     characterized by increased platelet size and decreased number of
     circulating platelets. {ECO:0000269|PubMed:18849486}. Note=The
     disease is caused by mutations affecting the gene represented in
     this entry.
 -!- SIMILARITY: Belongs to the tubulin family. {ECO:0000305}.
 -----------------------------------------------------------------------
 Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
 Distributed under the Creative Commons Attribution (CC BY 4.0) License
 -----------------------------------------------------------------------
 EMBL; AJ292757; CAC16605.1; -; mRNA.
 EMBL; AL109840; -; NOT_ANNOTATED_CDS; Genomic_DNA.
 EMBL; BC033679; AAH33679.1; -; mRNA.
 CCDS; CCDS13475.1; -.
 RefSeq; NP_110400.1; NM_030773.3.
 UniGene; Hs.303023; -.
 ProteinModelPortal; Q9H4B7; -.
 SMR; Q9H4B7; -.
 BioGrid; 123347; 78.
 CORUM; Q9H4B7; -.
 DIP; DIP-42487N; -.
 IntAct; Q9H4B7; 34.
 MINT; Q9H4B7; -.
 STRING; 9606.ENSP00000217133; -.
 BindingDB; Q9H4B7; -.
 ChEMBL; CHEMBL1915; -.
 DrugBank; DB06772; Cabazitaxel.
 DrugBank; DB01394; Colchicine.
 DrugBank; DB05147; CYT997.
 DrugBank; DB01248; Docetaxel.
 DrugBank; DB04940; E7389.
 DrugBank; DB03010; Epothilone B.
 DrugBank; DB01873; Epothilone D.
 DrugBank; DB01229; Paclitaxel.
 DrugBank; DB00309; Vindesine.
 DrugBank; DB06042; ZEN-012.
 iPTMnet; Q9H4B7; -.
 PhosphoSitePlus; Q9H4B7; -.
 BioMuta; TUBB1; -.
 DMDM; 62903515; -.
 OGP; Q9H4B7; -.
 EPD; Q9H4B7; -.
 MaxQB; Q9H4B7; -.
 PaxDb; Q9H4B7; -.
 PeptideAtlas; Q9H4B7; -.
 PRIDE; Q9H4B7; -.
 ProteomicsDB; 80819; -.
 TopDownProteomics; Q9H4B7; -.
 DNASU; 81027; -.
 Ensembl; ENST00000217133; ENSP00000217133; ENSG00000101162.
 GeneID; 81027; -.
 KEGG; hsa:81027; -.
 UCSC; uc002yak.3; human.
 CTD; 81027; -.
 DisGeNET; 81027; -.
 EuPathDB; HostDB:ENSG00000101162.3; -.
 GeneCards; TUBB1; -.
 HGNC; HGNC:16257; TUBB1.
 HPA; CAB004286; -.
 HPA; HPA043640; -.
 HPA; HPA046280; -.
 MalaCards; TUBB1; -.
 MIM; 612901; gene.
 MIM; 613112; phenotype.
 neXtProt; NX_Q9H4B7; -.
 OpenTargets; ENSG00000101162; -.
 Orphanet; 140957; Autosomal dominant macrothrombocytopenia.
 PharmGKB; PA38100; -.
 eggNOG; KOG1375; Eukaryota.
 eggNOG; COG5023; LUCA.
 GeneTree; ENSGT00760000119061; -.
 HOGENOM; HOG000165710; -.
 HOVERGEN; HBG000089; -.
 InParanoid; Q9H4B7; -.
 KO; K07375; -.
 OMA; DNFIHGN; -.
 OrthoDB; EOG091G06U2; -.
 PhylomeDB; Q9H4B7; -.
 TreeFam; TF300298; -.
 Reactome; R-HSA-1445148; Translocation of SLC2A4 (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-3371497; HSP90 chaperone cycle for steroid hormone receptors (SHR).
 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-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-8955332; Carboxyterminal post-translational modifications of tubulin.
 Reactome; R-HSA-983189; Kinesins.
 SIGNOR; Q9H4B7; -.
 ChiTaRS; TUBB1; human.
 GeneWiki; TUBB1; -.
 GenomeRNAi; 81027; -.
 PRO; PR:Q9H4B7; -.
 Proteomes; UP000005640; Chromosome 20.
 Bgee; ENSG00000101162; Expressed in 85 organ(s), highest expression level in leukocyte.
 CleanEx; HS_TUBB1; -.
 Genevisible; Q9H4B7; HS.
 GO; GO:0005737; C:cytoplasm; IDA:UniProtKB.
 GO; GO:0070062; C:extracellular exosome; HDA:UniProtKB.
 GO; GO:0005874; C:microtubule; IEA:UniProtKB-KW.
 GO; GO:0005525; F:GTP binding; IEA:UniProtKB-KW.
 GO; GO:0003924; F:GTPase activity; IEA:InterPro.
 GO; GO:0005200; F:structural constituent of cytoskeleton; IEA:Ensembl.
 GO; GO:0051225; P:spindle assembly; IEA:Ensembl.
 Gene3D; 1.10.287.600; -; 1.
 Gene3D; 3.30.1330.20; -; 1.
 Gene3D; 3.40.50.1440; -; 1.
 InterPro; IPR013838; Beta-tubulin_BS.
 InterPro; IPR002453; Beta_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; IPR023123; Tubulin_C.
 InterPro; IPR017975; Tubulin_CS.
 InterPro; IPR003008; Tubulin_FtsZ_GTPase.
 PANTHER; PTHR11588; PTHR11588; 1.
 Pfam; PF00091; Tubulin; 1.
 Pfam; PF03953; Tubulin_C; 1.
 PRINTS; PR01163; BETATUBULIN.
 PRINTS; PR01161; TUBULIN.
 SMART; SM00864; Tubulin; 1.
 SMART; SM00865; Tubulin_C; 1.
 SUPFAM; SSF52490; SSF52490; 1.
 SUPFAM; SSF55307; SSF55307; 1.
 PROSITE; PS00227; TUBULIN; 1.
 PROSITE; PS00228; TUBULIN_B_AUTOREG; 1.
 1: Evidence at protein level;
 Complete proteome; Cytoplasm; Cytoskeleton; Direct protein sequencing;
 Disease mutation; GTP-binding; Isopeptide bond; Microtubule;
 Nucleotide-binding; Phosphoprotein; Polymorphism; Reference proteome.
 CHAIN         1    451       Tubulin beta-1 chain.
                              /FTId=PRO_0000048242.
 NP_BIND     140    146       GTP. {ECO:0000255}.
 MOD_RES     172    172       Phosphoserine; by CDK1.
                              {ECO:0000269|PubMed:16371510}.
 MOD_RES     440    440       5-glutamyl polyglutamate.
                              {ECO:0000250|UniProtKB:Q2T9S0}.
 VARIANT      43     43       Q -> H (in dbSNP:rs415064).
                              /FTId=VAR_034542.
 VARIANT      43     43       Q -> P (in dbSNP:rs463312).
                              {ECO:0000269|PubMed:15956286,
                              ECO:0000269|PubMed:18849486}.
                              /FTId=VAR_034543.
 VARIANT     274    274       T -> M (in dbSNP:rs35565630).
                              /FTId=VAR_052671.
 VARIANT     307    307       R -> H (in dbSNP:rs6070697).
                              {ECO:0000269|PubMed:18849486}.
                              /FTId=VAR_052672.
 VARIANT     318    318       R -> W (in MAD-TUBB1; dbSNP:rs121918555).
                              {ECO:0000269|PubMed:18849486}.
                              /FTId=VAR_063411.
 SEQUENCE   451 AA;  50327 MW;  6A3E5208C1C89AE4 CRC64;
 MREIVHIQIG QCGNQIGAKF WEMIGEEHGI DLAGSDRGAS ALQLERISVY YNEAYGRKYV
 PRAVLVDLEP GTMDSIRSSK LGALFQPDSF VHGNSGAGNN WAKGHYTEGA ELIENVLEVV
 RHESESCDCL QGFQIVHSLG GGTGSGMGTL LMNKIREEYP DRIMNSFSVM PSPKVSDTVV
 EPYNAVLSIH QLIENADACF CIDNEALYDI CFRTLKLTTP TYGDLNHLVS LTMSGITTSL
 RFPGQLNADL RKLAVNMVPF PRLHFFMPGF APLTAQGSQQ YRALSVAELT QQMFDARNTM
 AACDLRRGRY LTVACIFRGK MSTKEVDQQL LSVQTRNSSC FVEWIPNNVK VAVCDIPPRG
 LSMAATFIGN NTAIQEIFNR VSEHFSAMFK RKAFVHWYTS EGMDINEFGE AENNIHDLVS
 EYQQFQDAKA VLEEDEEVTE EAEMEPEDKG H

Related products :