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Q9H4B7 (TBB1_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 110. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (5) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Tubulin beta-1 chain
Gene names
Name:TUBB1
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length451 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

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.

Subunit structure

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. Ref.5

Subcellular location

Cytoplasmcytoskeleton Ref.9.

Tissue specificity

Hematopoietic cell-specific. Major isotype in leukocytes, where it represents 50% of all beta-tubulins. Ref.7

Post-translational modification

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.

Involvement in 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.
Note: The disease is caused by mutations affecting the gene represented in this entry. Ref.9

Sequence similarities

Belongs to the tubulin family.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 451451Tubulin beta-1 chain
PRO_0000048242

Regions

Nucleotide binding140 – 1467GTP Potential

Amino acid modifications

Modified residue1721Phosphoserine; by CDK1 By similarity

Natural variations

Natural variant431Q → H.
Corresponds to variant rs415064 [ dbSNP | Ensembl ].
VAR_034542
Natural variant431Q → P. Ref.8 Ref.9
Corresponds to variant rs463312 [ dbSNP | Ensembl ].
VAR_034543
Natural variant2741T → M.
Corresponds to variant rs35565630 [ dbSNP | Ensembl ].
VAR_052671
Natural variant3071R → H. Ref.9
Corresponds to variant rs6070697 [ dbSNP | Ensembl ].
VAR_052672
Natural variant3181R → W in MAD-TUBB1. Ref.9
Corresponds to variant rs121918555 [ dbSNP | Ensembl ].
VAR_063411

Sequences

Sequence LengthMass (Da)Tools
Q9H4B7 [UniParc].

Last modified March 1, 2001. Version 1.
Checksum: 6A3E5208C1C89AE4

FASTA45150,327
        10         20         30         40         50         60 
MREIVHIQIG QCGNQIGAKF WEMIGEEHGI DLAGSDRGAS ALQLERISVY YNEAYGRKYV 

        70         80         90        100        110        120 
PRAVLVDLEP GTMDSIRSSK LGALFQPDSF VHGNSGAGNN WAKGHYTEGA ELIENVLEVV 

       130        140        150        160        170        180 
RHESESCDCL QGFQIVHSLG GGTGSGMGTL LMNKIREEYP DRIMNSFSVM PSPKVSDTVV 

       190        200        210        220        230        240 
EPYNAVLSIH QLIENADACF CIDNEALYDI CFRTLKLTTP TYGDLNHLVS LTMSGITTSL 

       250        260        270        280        290        300 
RFPGQLNADL RKLAVNMVPF PRLHFFMPGF APLTAQGSQQ YRALSVAELT QQMFDARNTM 

       310        320        330        340        350        360 
AACDLRRGRY LTVACIFRGK MSTKEVDQQL LSVQTRNSSC FVEWIPNNVK VAVCDIPPRG 

       370        380        390        400        410        420 
LSMAATFIGN NTAIQEIFNR VSEHFSAMFK RKAFVHWYTS EGMDINEFGE AENNIHDLVS 

       430        440        450 
EYQQFQDAKA VLEEDEEVTE EAEMEPEDKG H 

« Hide

References

« Hide 'large scale' references
[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. expand/collapse author list , 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]"Tumoral and tissue-specific expression of the major human beta-tubulin isotypes."
Leandro-Garcia L.J., Leskela S., Landa I., Montero-Conde C., Lopez-Jimenez E., Leton R., Cascon A., Robledo M., Rodriguez-Antona C.
Cytoskeleton 67:214-223(2010) [PubMed] [Europe PMC] [Abstract]
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.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AJ292757 mRNA. Translation: CAC16605.1.
AL109840 Genomic DNA. Translation: CAC09371.2.
BC033679 mRNA. Translation: AAH33679.1.
CCDSCCDS13475.1.
RefSeqNP_110400.1. NM_030773.3.
UniGeneHs.303023.

3D structure databases

ProteinModelPortalQ9H4B7.
SMRQ9H4B7. Positions 1-430.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid123347. 28 interactions.
IntActQ9H4B7. 13 interactions.
MINTMINT-1891365.
STRING9606.ENSP00000217133.

Chemistry

BindingDBQ9H4B7.
ChEMBLCHEMBL1915.
DrugBankDB01394. Colchicine.
DB01248. Docetaxel.
DB01229. Paclitaxel.
DB00309. Vindesine.

PTM databases

PhosphoSiteQ9H4B7.

Polymorphism databases

DMDM62903515.

2D gel databases

OGPQ9H4B7.

Proteomic databases

MaxQBQ9H4B7.
PaxDbQ9H4B7.
PeptideAtlasQ9H4B7.
PRIDEQ9H4B7.

Protocols and materials databases

DNASU81027.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000217133; ENSP00000217133; ENSG00000101162.
GeneID81027.
KEGGhsa:81027.
UCSCuc002yak.3. human.

Organism-specific databases

CTD81027.
GeneCardsGC20P057594.
HGNCHGNC:16257. TUBB1.
HPACAB004286.
HPA043640.
HPA046280.
MIM612901. gene.
613112. phenotype.
neXtProtNX_Q9H4B7.
Orphanet140957. Autosomal dominant macrothrombocytopenia.
PharmGKBPA38100.
GenAtlasSearch...

Phylogenomic databases

eggNOGCOG5023.
HOGENOMHOG000165710.
HOVERGENHBG000089.
InParanoidQ9H4B7.
KOK07375.
OMAACIFRGK.
OrthoDBEOG7ZKS9Z.
PhylomeDBQ9H4B7.
TreeFamTF300298.

Enzyme and pathway databases

ReactomeREACT_111045. Developmental Biology.
REACT_11123. Membrane Trafficking.
REACT_115566. Cell Cycle.
REACT_17015. Metabolism of proteins.
REACT_21300. Mitotic M-M/G1 phases.
REACT_604. Hemostasis.
REACT_6900. Immune System.

Gene expression databases

BgeeQ9H4B7.
CleanExHS_TUBB1.
GenevestigatorQ9H4B7.

Family and domain databases

Gene3D1.10.287.600. 1 hit.
3.30.1330.20. 1 hit.
3.40.50.1440. 1 hit.
InterProIPR013838. 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]
PANTHERPTHR11588. PTHR11588. 1 hit.
PfamPF00091. Tubulin. 1 hit.
PF03953. Tubulin_C. 1 hit.
[Graphical view]
PRINTSPR01163. BETATUBULIN.
PR01161. TUBULIN.
SMARTSM00864. Tubulin. 1 hit.
SM00865. Tubulin_C. 1 hit.
[Graphical view]
SUPFAMSSF52490. SSF52490. 1 hit.
SSF55307. SSF55307. 1 hit.
PROSITEPS00227. TUBULIN. 1 hit.
PS00228. TUBULIN_B_AUTOREG. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

GeneWikiTUBB1.
GenomeRNAi81027.
NextBio71348.
PROQ9H4B7.
SOURCESearch...

Entry information

Entry nameTBB1_HUMAN
AccessionPrimary (citable) accession number: Q9H4B7
Entry history
Integrated into UniProtKB/Swiss-Prot: February 1, 2005
Last sequence update: March 1, 2001
Last modified: July 9, 2014
This is version 110 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (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.

Relevant documents

SIMILARITY comments

Index of protein domains and families

MIM cross-references

Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot

Human polymorphisms and disease mutations

Index of human polymorphisms and disease mutations

Human entries with polymorphisms or disease mutations

List of human entries with polymorphisms or disease mutations

Human chromosome 20

Human chromosome 20: entries, gene names and cross-references to MIM