Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Protein

Tubulin beta-1 chain

Gene

TUBB1

Organism
Homo sapiens (Human)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

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).By similarity

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi140 – 1467GTPSequence Analysis

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Ligandi

GTP-binding, Nucleotide-binding

Enzyme and pathway databases

ReactomeiREACT_11039. Microtubule-dependent trafficking of connexons from Golgi to the plasma membrane.
REACT_121399. MHC class II antigen presentation.
REACT_147867. Translocation of GLUT4 to the plasma membrane.
REACT_150425. Resolution of Sister Chromatid Cohesion.
REACT_150471. Separation of Sister Chromatids.
REACT_15510. Recruitment of NuMA to mitotic centrosomes.
REACT_16936. Prefoldin mediated transfer of substrate to CCT/TriC.
REACT_16956. Formation of tubulin folding intermediates by CCT/TriC.
REACT_16967. Post-chaperonin tubulin folding pathway.
REACT_22365. Recycling pathway of L1.
REACT_25201. Kinesins.
REACT_268024. Intraflagellar transport.
REACT_268265. Assembly of the primary cilium.
REACT_268323. Hedgehog 'off' state.
REACT_355252. RHO GTPases Activate Formins.
REACT_355469. RHO GTPases activate IQGAPs.
REACT_682. Mitotic Prometaphase.
REACT_9509. Gap junction assembly.

Names & Taxonomyi

Protein namesi
Recommended name:
Tubulin beta-1 chain
Gene namesi
Name:TUBB1
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640 Componenti: Chromosome 20

Organism-specific databases

HGNCiHGNC:16257. TUBB1.

Subcellular locationi

GO - Cellular componenti

  • cytoplasm Source: UniProtKB
  • extracellular exosome Source: UniProtKB
  • microtubule Source: UniProtKB-KW
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm, Cytoskeleton, Microtubule

Pathology & Biotechi

Involvement in diseasei

Macrothrombocytopenia, autosomal dominant, TUBB1-related (MAD-TUBB1)1 Publication

The disease is caused by mutations affecting the gene represented in this entry.

Disease descriptionA congenital blood disorder characterized by increased platelet size and decreased number of circulating platelets.

See also OMIM:613112
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti318 – 3181R → W in MAD-TUBB1. 1 Publication
Corresponds to variant rs121918555 [ dbSNP | Ensembl ].
VAR_063411

Keywords - Diseasei

Disease mutation

Organism-specific databases

MIMi613112. phenotype.
Orphaneti140957. Autosomal dominant macrothrombocytopenia.
PharmGKBiPA38100.

Chemistry

DrugBankiDB06772. Cabazitaxel.
DB01394. Colchicine.
DB01248. Docetaxel.
DB01229. Paclitaxel.
DB00309. Vindesine.

Polymorphism and mutation databases

BioMutaiTUBB1.
DMDMi62903515.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 451451Tubulin beta-1 chainPRO_0000048242Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei172 – 1721Phosphoserine; by CDK1By similarity

Post-translational modificationi

Some glutamate residues at the C-terminus are polyglutamylated. This modification occurs exclusively on glutamate residues and results in polyglutamate chains on the gamma-carboxyl group. Also 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) whereas glutamylation is prevalent in neuronal cells, centrioles, axonemes, and the mitotic spindle. Both modifications can coexist on the same protein on adjacent residues, and lowering glycylation levels increases polyglutamylation, and reciprocally. The precise function of such modifications is still unclear but they regulate the assembly and dynamics of axonemal microtubules (Probable).1 Publication

Keywords - PTMi

Phosphoprotein

Proteomic databases

MaxQBiQ9H4B7.
PaxDbiQ9H4B7.
PeptideAtlasiQ9H4B7.
PRIDEiQ9H4B7.

2D gel databases

OGPiQ9H4B7.

PTM databases

PhosphoSiteiQ9H4B7.

Expressioni

Tissue specificityi

Hematopoietic cell-specific. Major isotype in leukocytes, where it represents 50% of all beta-tubulins.1 Publication

Gene expression databases

BgeeiQ9H4B7.
CleanExiHS_TUBB1.
GenevisibleiQ9H4B7. HS.

Organism-specific databases

HPAiCAB004286.
HPA043640.
HPA046280.

Interactioni

Subunit structurei

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 RANBP10.1 Publication

Protein-protein interaction databases

BioGridi123347. 45 interactions.
DIPiDIP-42487N.
IntActiQ9H4B7. 22 interactions.
MINTiMINT-1891365.
STRINGi9606.ENSP00000217133.

Structurei

3D structure databases

ProteinModelPortaliQ9H4B7.
SMRiQ9H4B7. Positions 1-430.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Belongs to the tubulin family.Curated

Phylogenomic databases

eggNOGiCOG5023.
GeneTreeiENSGT00760000119061.
HOGENOMiHOG000165710.
HOVERGENiHBG000089.
InParanoidiQ9H4B7.
KOiK07375.
OMAiFDARNIM.
OrthoDBiEOG7ZKS9Z.
PhylomeDBiQ9H4B7.
TreeFamiTF300298.

Family and domain databases

Gene3Di1.10.287.600. 1 hit.
3.30.1330.20. 1 hit.
3.40.50.1440. 1 hit.
InterProiIPR013838. Beta-tubulin_BS.
IPR002453. Beta_tubulin.
IPR008280. Tub_FtsZ_C.
IPR000217. Tubulin.
IPR018316. Tubulin/FtsZ_2-layer-sand-dom.
IPR023123. Tubulin_C.
IPR017975. Tubulin_CS.
IPR003008. Tubulin_FtsZ_GTPase.
[Graphical view]
PANTHERiPTHR11588. PTHR11588. 1 hit.
PfamiPF00091. Tubulin. 1 hit.
PF03953. Tubulin_C. 1 hit.
[Graphical view]
PRINTSiPR01163. BETATUBULIN.
PR01161. TUBULIN.
SMARTiSM00864. Tubulin. 1 hit.
SM00865. Tubulin_C. 1 hit.
[Graphical view]
SUPFAMiSSF52490. SSF52490. 1 hit.
SSF55307. SSF55307. 1 hit.
PROSITEiPS00227. TUBULIN. 1 hit.
PS00228. TUBULIN_B_AUTOREG. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Q9H4B7-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MREIVHIQIG QCGNQIGAKF WEMIGEEHGI DLAGSDRGAS ALQLERISVY
60 70 80 90 100
YNEAYGRKYV PRAVLVDLEP GTMDSIRSSK LGALFQPDSF VHGNSGAGNN
110 120 130 140 150
WAKGHYTEGA ELIENVLEVV RHESESCDCL QGFQIVHSLG GGTGSGMGTL
160 170 180 190 200
LMNKIREEYP DRIMNSFSVM PSPKVSDTVV EPYNAVLSIH QLIENADACF
210 220 230 240 250
CIDNEALYDI CFRTLKLTTP TYGDLNHLVS LTMSGITTSL RFPGQLNADL
260 270 280 290 300
RKLAVNMVPF PRLHFFMPGF APLTAQGSQQ YRALSVAELT QQMFDARNTM
310 320 330 340 350
AACDLRRGRY LTVACIFRGK MSTKEVDQQL LSVQTRNSSC FVEWIPNNVK
360 370 380 390 400
VAVCDIPPRG LSMAATFIGN NTAIQEIFNR VSEHFSAMFK RKAFVHWYTS
410 420 430 440 450
EGMDINEFGE AENNIHDLVS EYQQFQDAKA VLEEDEEVTE EAEMEPEDKG

H
Length:451
Mass (Da):50,327
Last modified:March 1, 2001 - v1
Checksum:i6A3E5208C1C89AE4
GO

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti43 – 431Q → H.
Corresponds to variant rs415064 [ dbSNP | Ensembl ].
VAR_034542
Natural varianti43 – 431Q → P.2 Publications
Corresponds to variant rs463312 [ dbSNP | Ensembl ].
VAR_034543
Natural varianti274 – 2741T → M.
Corresponds to variant rs35565630 [ dbSNP | Ensembl ].
VAR_052671
Natural varianti307 – 3071R → H.1 Publication
Corresponds to variant rs6070697 [ dbSNP | Ensembl ].
VAR_052672
Natural varianti318 – 3181R → W in MAD-TUBB1. 1 Publication
Corresponds to variant rs121918555 [ dbSNP | Ensembl ].
VAR_063411

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AJ292757 mRNA. Translation: CAC16605.1.
AL109840 Genomic DNA. Translation: CAC09371.2.
BC033679 mRNA. Translation: AAH33679.1.
CCDSiCCDS13475.1.
RefSeqiNP_110400.1. NM_030773.3.
UniGeneiHs.303023.

Genome annotation databases

EnsembliENST00000217133; ENSP00000217133; ENSG00000101162.
GeneIDi81027.
KEGGihsa:81027.
UCSCiuc002yak.3. human.

Keywords - Coding sequence diversityi

Polymorphism

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AJ292757 mRNA. Translation: CAC16605.1.
AL109840 Genomic DNA. Translation: CAC09371.2.
BC033679 mRNA. Translation: AAH33679.1.
CCDSiCCDS13475.1.
RefSeqiNP_110400.1. NM_030773.3.
UniGeneiHs.303023.

3D structure databases

ProteinModelPortaliQ9H4B7.
SMRiQ9H4B7. Positions 1-430.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi123347. 45 interactions.
DIPiDIP-42487N.
IntActiQ9H4B7. 22 interactions.
MINTiMINT-1891365.
STRINGi9606.ENSP00000217133.

Chemistry

BindingDBiQ9H4B7.
ChEMBLiCHEMBL1915.
DrugBankiDB06772. Cabazitaxel.
DB01394. Colchicine.
DB01248. Docetaxel.
DB01229. Paclitaxel.
DB00309. Vindesine.

PTM databases

PhosphoSiteiQ9H4B7.

Polymorphism and mutation databases

BioMutaiTUBB1.
DMDMi62903515.

2D gel databases

OGPiQ9H4B7.

Proteomic databases

MaxQBiQ9H4B7.
PaxDbiQ9H4B7.
PeptideAtlasiQ9H4B7.
PRIDEiQ9H4B7.

Protocols and materials databases

DNASUi81027.
Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000217133; ENSP00000217133; ENSG00000101162.
GeneIDi81027.
KEGGihsa:81027.
UCSCiuc002yak.3. human.

Organism-specific databases

CTDi81027.
GeneCardsiGC20P057594.
HGNCiHGNC:16257. TUBB1.
HPAiCAB004286.
HPA043640.
HPA046280.
MIMi612901. gene.
613112. phenotype.
neXtProtiNX_Q9H4B7.
Orphaneti140957. Autosomal dominant macrothrombocytopenia.
PharmGKBiPA38100.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiCOG5023.
GeneTreeiENSGT00760000119061.
HOGENOMiHOG000165710.
HOVERGENiHBG000089.
InParanoidiQ9H4B7.
KOiK07375.
OMAiFDARNIM.
OrthoDBiEOG7ZKS9Z.
PhylomeDBiQ9H4B7.
TreeFamiTF300298.

Enzyme and pathway databases

ReactomeiREACT_11039. Microtubule-dependent trafficking of connexons from Golgi to the plasma membrane.
REACT_121399. MHC class II antigen presentation.
REACT_147867. Translocation of GLUT4 to the plasma membrane.
REACT_150425. Resolution of Sister Chromatid Cohesion.
REACT_150471. Separation of Sister Chromatids.
REACT_15510. Recruitment of NuMA to mitotic centrosomes.
REACT_16936. Prefoldin mediated transfer of substrate to CCT/TriC.
REACT_16956. Formation of tubulin folding intermediates by CCT/TriC.
REACT_16967. Post-chaperonin tubulin folding pathway.
REACT_22365. Recycling pathway of L1.
REACT_25201. Kinesins.
REACT_268024. Intraflagellar transport.
REACT_268265. Assembly of the primary cilium.
REACT_268323. Hedgehog 'off' state.
REACT_355252. RHO GTPases Activate Formins.
REACT_355469. RHO GTPases activate IQGAPs.
REACT_682. Mitotic Prometaphase.
REACT_9509. Gap junction assembly.

Miscellaneous databases

GeneWikiiTUBB1.
GenomeRNAii81027.
NextBioi71348.
PROiQ9H4B7.
SOURCEiSearch...

Gene expression databases

BgeeiQ9H4B7.
CleanExiHS_TUBB1.
GenevisibleiQ9H4B7. HS.

Family and domain databases

Gene3Di1.10.287.600. 1 hit.
3.30.1330.20. 1 hit.
3.40.50.1440. 1 hit.
InterProiIPR013838. Beta-tubulin_BS.
IPR002453. Beta_tubulin.
IPR008280. Tub_FtsZ_C.
IPR000217. Tubulin.
IPR018316. Tubulin/FtsZ_2-layer-sand-dom.
IPR023123. Tubulin_C.
IPR017975. Tubulin_CS.
IPR003008. Tubulin_FtsZ_GTPase.
[Graphical view]
PANTHERiPTHR11588. PTHR11588. 1 hit.
PfamiPF00091. Tubulin. 1 hit.
PF03953. Tubulin_C. 1 hit.
[Graphical view]
PRINTSiPR01163. BETATUBULIN.
PR01161. TUBULIN.
SMARTiSM00864. Tubulin. 1 hit.
SM00865. Tubulin_C. 1 hit.
[Graphical view]
SUPFAMiSSF52490. SSF52490. 1 hit.
SSF55307. SSF55307. 1 hit.
PROSITEiPS00227. TUBULIN. 1 hit.
PS00228. TUBULIN_B_AUTOREG. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "Mapping and characterization of the human TUBB1 gene."
    Gross C., Kussmann S., Hehr A., Hansmann I., Schlote D.
    Submitted (JUL-2000) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
  2. "The DNA sequence and comparative analysis of human chromosome 20."
    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.
    Nature 414:865-871(2001) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  3. "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
    The MGC Project Team
    Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Tissue: Brain.
  4. "Exploring proteomes and analyzing protein processing by mass spectrometric identification of sorted N-terminal peptides."
    Gevaert K., Goethals M., Martens L., Van Damme J., Staes A., Thomas G.R., Vandekerckhove J.
    Nat. Biotechnol. 21:566-569(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: PROTEIN SEQUENCE OF 38-46 AND 263-281.
    Tissue: Platelet.
  5. "RanBP10 is a cytoplasmic guanine nucleotide exchange factor that modulates noncentrosomal microtubules."
    Schulze H., Dose M., Korpal M., Meyer I., Italiano J.E. Jr., Shivdasani R.A.
    J. Biol. Chem. 283:14109-14119(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH RANBP10.
  6. "Evolutionary divergence of enzymatic mechanisms for posttranslational polyglycylation."
    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.
    Cell 137:1076-1087(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: GLYCYLATION.
  7. Cited for: TISSUE SPECIFICITY.
  8. "The TUBB1 Q43P functional polymorphism reduces the risk of cardiovascular disease in men by modulating platelet function and structure."
    Freson K., De Vos R., Wittevrongel C., Thys C., Defoor J., Vanhees L., Vermylen J., Peerlinck K., Van Geet C.
    Blood 106:2356-2362(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: VARIANT PRO-43.
  9. "Mutation of the beta1-tubulin gene associated with congenital macrothrombocytopenia affecting microtubule assembly."
    Kunishima S., Kobayashi R., Itoh T.J., Hamaguchi M., Saito H.
    Blood 113:458-461(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: VARIANTS PRO-43 AND HIS-307, VARIANT MAD-TUBB1 TRP-318, SUBCELLULAR LOCATION.

Entry informationi

Entry nameiTBB1_HUMAN
AccessioniPrimary (citable) accession number: Q9H4B7
Entry historyi
Integrated into UniProtKB/Swiss-Prot: February 1, 2005
Last sequence update: March 1, 2001
Last modified: July 22, 2015
This is version 121 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

Miscellaneousi

Keywords - Technical termi

Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. Human chromosome 20
    Human chromosome 20: entries, gene names and cross-references to MIM
  2. Human entries with polymorphisms or disease mutations
    List of human entries with polymorphisms or disease mutations
  3. Human polymorphisms and disease mutations
    Index of human polymorphisms and disease mutations
  4. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  5. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into Uniref entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.