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Tubulin beta-1 chain

 TBB1_HUMAN              Reviewed;         451 AA.
Q9H4B7;
01-FEB-2005, integrated into UniProtKB/Swiss-Prot.
01-MAR-2001, sequence version 1.
20-JUN-2018, entry version 147.
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}.
-----------------------------------------------------------------------
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-----------------------------------------------------------------------
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 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; -.
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


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