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Tubulin beta-1 chain

 TBB1_HUMAN              Reviewed;         451 AA.
01-FEB-2005, integrated into UniProtKB/Swiss-Prot.
01-MAR-2001, sequence version 1.
13-FEB-2019, entry version 154.
RecName: Full=Tubulin beta-1 chain;
Homo sapiens (Human).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
Catarrhini; Hominidae; Homo.
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.
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).
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).
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).
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).
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).
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
Cell 137:1076-1087(2009).
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).
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).
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
Blood 106:2356-2362(2005).
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.
-!- SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton
-!- TISSUE SPECIFICITY: Hematopoietic cell-specific. Major isotype in
leukocytes, where it represents 50% of all beta-tubulins.
-!- 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).
-!- 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).
-!- 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.
-!- 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
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; 82.
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; -.
jPOST; 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; ENSGT00940000159809; -.
HOGENOM; HOG000165710; -.
HOVERGEN; HBG000089; -.
InParanoid; Q9H4B7; -.
KO; K07375; -.
OrthoDB; 962471at2759; -.
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-9619483; Activation of AMPK downstream of NMDARs.
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.
Genevisible; Q9H4B7; HS.
GO; GO:0005737; C:cytoplasm; IDA:UniProtKB.
GO; GO:0070062; C:extracellular exosome; HDA:UniProtKB.
GO; GO:0005874; C:microtubule; IBA:GO_Central.
GO; GO:0005525; F:GTP binding; IBA:GO_Central.
GO; GO:0003924; F:GTPase activity; IEA:InterPro.
GO; GO:0005200; F:structural constituent of cytoskeleton; IBA:GO_Central.
GO; GO:0000226; P:microtubule cytoskeleton organization; IBA:GO_Central.
GO; GO:0007017; P:microtubule-based process; IBA:GO_Central.
GO; GO:0000278; P:mitotic cell cycle; IBA:GO_Central.
GO; GO:0051225; P:spindle assembly; IEA:Ensembl.
Gene3D;; -; 1.
Gene3D; 3.30.1330.20; -; 1.
Gene3D;; -; 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.
SMART; SM00864; Tubulin; 1.
SMART; SM00865; Tubulin_C; 1.
SUPFAM; SSF52490; SSF52490; 1.
SUPFAM; SSF55307; SSF55307; 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.
NP_BIND 140 146 GTP. {ECO:0000255}.
MOD_RES 172 172 Phosphoserine; by CDK1.
MOD_RES 440 440 5-glutamyl polyglutamate.
VARIANT 43 43 Q -> H (in dbSNP:rs415064).
VARIANT 43 43 Q -> P (in dbSNP:rs463312).
VARIANT 274 274 T -> M (in dbSNP:rs35565630).
VARIANT 307 307 R -> H (in dbSNP:rs6070697).
VARIANT 318 318 R -> W (in MAD-TUBB1; dbSNP:rs121918555).
SEQUENCE 451 AA; 50327 MW; 6A3E5208C1C89AE4 CRC64;

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Kits Elisa; taq POLYMERASE

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Pathways :
WP1614: 1- and 2-Methylnaphthalene degradation
WP542: Electron Transport Chain
WP1002: Electron Transport Chain
WP1045: TGF-beta Receptor Signaling Pathway
WP1048: TGF Beta Signaling Pathway
WP105: Fatty Acid Beta Oxidation 2
WP1058: Senescence and Autophagy
WP1061: Fatty Acid Beta Oxidation
WP1106: Keap1-Nrf2
WP1107: Mitochondrial LC-Fatty Acid Beta-Oxidation
WP111: Electron Transport Chain
WP1119: Electron Transport Chain
WP113: TGF Beta Signaling Pathway
WP1161: TGF-beta Receptor Signaling Pathway
WP1164: TGF Beta Signaling Pathway
WP1177: Fatty Acid Beta Oxidation
WP1207: Fatty Acid Beta Oxidation
WP1224: EBV LMP1 signaling
WP1225: estrogen signalling
WP1226: Mitochondrial LC-Fatty Acid Beta-Oxidation
WP1237: Fatty Acid Beta Oxidation
WP126: Fatty Acid Beta Oxidation 1
WP1269: Fatty Acid Beta Oxidation
WP1307: Fatty Acid Beta Oxidation
WP1339: Electron Transport Chain

Related Genes :
[betaTub56D 1t A1ZBL0_DROME B1t beta BETA 56D beta-Tub beta-tub beta-tub 56D beta-Tub56D beta-tub56D beta-tubulin beta-tubulin56D beta1 beta1-tub beta1-Tubulin beta1t beta1Tub beta1tub beta56D beta[[1]] tubulin beta[[1]]-tubulin betaTub betatub(56D) betaTub1 betatub56D betaTub56D-RA Dmbeta1 Dmel\CG9277 DTB2 l(2)k00705 T TBB1_DROME Tub Tub2D TUB56D Tubulin tubulin CG9277 Dmel_CG9277] Tubulin beta chain
[Tuba1a Tuba1] Tubulin alpha-1A chain (Alpha-tubulin 1) (Alpha-tubulin isotype M-alpha-1) (Tubulin alpha-1 chain) [Cleaved into: Detyrosinated tubulin alpha-1A chain]
[TUBB4B TUBB2C] Tubulin beta-4B chain (Tubulin beta-2 chain) (Tubulin beta-2C chain)
[Tuba1b Tuba2] Tubulin alpha-1B chain (Alpha-tubulin 2) (Alpha-tubulin isotype M-alpha-2) (Tubulin alpha-2 chain) [Cleaved into: Detyrosinated tubulin alpha-1B chain]
[Tuba1c Tuba6] Tubulin alpha-1C chain (Alpha-tubulin 6) (Alpha-tubulin isotype M-alpha-6) (Tubulin alpha-6 chain) [Cleaved into: Detyrosinated tubulin alpha-1C chain]
[TUBB4A TUBB4 TUBB5] Tubulin beta-4A chain (Tubulin 5 beta) (Tubulin beta-4 chain)
[TUBB3 TUBB4] Tubulin beta-3 chain (Tubulin beta-4 chain) (Tubulin beta-III)
[betaTub60D 143391_i_at 3t B3t BETA 60D beta-tub beta-Tub60D beta-Tub6D beta3 beta3 TU beta3-Tub beta3-tubulin beta3t beta3TUB beta3Tub beta3tub beta60C beta[[3]] tubulin beta[[3]]-Tub beta[[3]]-tubulin betaTub betaTub3 betaTub60C betatub60D D.m.BETA-60D Dmbeta3 Dmel\CG3401 DTB3 p50 p53 T Tub Tub2E Tub60D tubulin CG3401 Dmel_CG3401] Tubulin beta chain
[TUBA1B] Tubulin alpha-1B chain (Alpha-tubulin ubiquitous) (Tubulin K-alpha-1) (Tubulin alpha-ubiquitous chain) [Cleaved into: Detyrosinated tubulin alpha-1B chain]
[TUBA1A TUBA3] Tubulin alpha-1A chain (Alpha-tubulin 3) (Tubulin B-alpha-1) (Tubulin alpha-3 chain) [Cleaved into: Detyrosinated tubulin alpha-1A chain]
[mec-7 ZK154.3] Tubulin beta-1 chain (Beta-1-tubulin)
[Tuba1a Tuba1] Tubulin alpha-1A chain (Alpha-tubulin 1) (Tubulin alpha-1 chain) [Cleaved into: Detyrosinated tubulin alpha-1A chain]
[TUBA1C TUBA6] Tubulin alpha-1C chain (Alpha-tubulin 6) (Tubulin alpha-6 chain) [Cleaved into: Detyrosinated tubulin alpha-1C chain]
[TUBB TUBB5 OK/SW-cl.56] Tubulin beta chain (Tubulin beta-5 chain)
[] Tubulin alpha-1B chain (Alpha-tubulin ubiquitous) (Tubulin K-alpha-1) (Tubulin alpha-ubiquitous chain) [Cleaved into: Detyrosinated tubulin alpha-1B chain]
[Tuba1b Tuba2] Tubulin alpha-1B chain (Alpha-tubulin 2) (Tubulin alpha-2 chain) [Cleaved into: Detyrosinated tubulin alpha-1B chain]
[Tubb4a Tubb4] Tubulin beta-4A chain (Tubulin beta-4 chain)
[TUBA4A TUBA1] Tubulin alpha-4A chain (Alpha-tubulin 1) (Testis-specific alpha-tubulin) (Tubulin H2-alpha) (Tubulin alpha-1 chain)
[TUBA1A] Tubulin alpha-1A chain (Alpha-tubulin 1) (Tubulin alpha-1 chain) [Cleaved into: Detyrosinated tubulin alpha-1A chain]
[benA rhiA AN1182] Tubulin beta-1 chain (Beta-1-tubulin)
[TUBB8] Tubulin beta-8 chain (Tubulin beta 8 class VIII)
[TUBB2A TUBB2] Tubulin beta-2A chain (Tubulin beta class IIa)
[TUB2 YFL037W] Tubulin beta chain (Beta-tubulin)
[nda3 alp12 SPBC26H8.07c] Tubulin beta chain (Beta-tubulin)
[Tubb4b Tubb2c] Tubulin beta-4B chain (Tubulin beta-2C chain)
[TUBA3C TUBA2] Tubulin alpha-3C chain (Alpha-tubulin 2) (Alpha-tubulin 3C) (Tubulin alpha-2 chain) [Cleaved into: Detyrosinated tubulin alpha-3C chain]
[Tuba3a Tuba3; Tuba3b Tuba7] Tubulin alpha-3 chain (Alpha-tubulin 3/7) (Alpha-tubulin isotype M-alpha-3/7) (Tubulin alpha-3/alpha-7 chain) [Cleaved into: Detyrosinated tubulin alpha-3 chain]
[TUBB6] Tubulin beta-6 chain (Tubulin beta class V)
[Tubg1 Tubg] Tubulin gamma-1 chain (Gamma-1-tubulin) (Gamma-tubulin complex component 1) (GCP-1)
[Tuba4a Tuba4] Tubulin alpha-4A chain (Alpha-tubulin 4) (Alpha-tubulin isotype M-alpha-4) (Tubulin alpha-4 chain)

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