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Q9H4B7

- TBB1_HUMAN

UniProt

Q9H4B7 - TBB1_HUMAN

Protein

Tubulin beta-1 chain

Gene

TUBB1

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 112 (01 Oct 2014)
      Sequence version 1 (01 Mar 2001)
      Previous versions | rss
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    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

    1. GTPase activity Source: InterPro
    2. GTP binding Source: UniProtKB-KW
    3. structural constituent of cytoskeleton Source: Ensembl

    GO - Biological processi

    1. 'de novo' posttranslational protein folding Source: Reactome
    2. cellular protein metabolic process Source: Reactome
    3. protein folding Source: Reactome
    4. protein polymerization Source: InterPro
    5. spindle assembly Source: Ensembl

    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_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: Chromosome 20

    Organism-specific databases

    HGNCiHGNC:16257. TUBB1.

    Subcellular locationi

    Cytoplasmcytoskeleton 1 Publication

    GO - Cellular componenti

    1. cytoplasm Source: UniProtKB
    2. microtubule Source: UniProtKB-KW

    Keywords - Cellular componenti

    Cytoplasm, Cytoskeleton, Microtubule

    Pathology & Biotechi

    Involvement in diseasei

    Macrothrombocytopenia, autosomal dominant, TUBB1-related (MAD-TUBB1) [MIM:613112]: A congenital blood disorder characterized by increased platelet size and decreased number of circulating platelets.1 Publication
    Note: The disease is caused by mutations affecting the gene represented in this entry.
    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.

    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.Curated

    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.
    GenevestigatoriQ9H4B7.

    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. 27 interactions.
    DIPiDIP-42487N.
    IntActiQ9H4B7. 20 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.
    HOGENOMiHOG000165710.
    HOVERGENiHBG000089.
    InParanoidiQ9H4B7.
    KOiK07375.
    OMAiACIFRGK.
    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

    MREIVHIQIG QCGNQIGAKF WEMIGEEHGI DLAGSDRGAS ALQLERISVY    50
    YNEAYGRKYV PRAVLVDLEP GTMDSIRSSK LGALFQPDSF VHGNSGAGNN 100
    WAKGHYTEGA ELIENVLEVV RHESESCDCL QGFQIVHSLG GGTGSGMGTL 150
    LMNKIREEYP DRIMNSFSVM PSPKVSDTVV EPYNAVLSIH QLIENADACF 200
    CIDNEALYDI CFRTLKLTTP TYGDLNHLVS LTMSGITTSL RFPGQLNADL 250
    RKLAVNMVPF PRLHFFMPGF APLTAQGSQQ YRALSVAELT QQMFDARNTM 300
    AACDLRRGRY LTVACIFRGK MSTKEVDQQL LSVQTRNSSC FVEWIPNNVK 350
    VAVCDIPPRG LSMAATFIGN NTAIQEIFNR VSEHFSAMFK RKAFVHWYTS 400
    EGMDINEFGE AENNIHDLVS EYQQFQDAKA VLEEDEEVTE EAEMEPEDKG 450
    H 451
    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:
    EMBL
    GenBank
    DDBJ
    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.

    Polymorphism databases

    DMDMi62903515.

    Keywords - Coding sequence diversityi

    Polymorphism

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AJ292757 mRNA. Translation: CAC16605.1 .
    AL109840 Genomic DNA. Translation: CAC09371.2 .
    BC033679 mRNA. Translation: AAH33679.1 .
    CCDSi CCDS13475.1.
    RefSeqi NP_110400.1. NM_030773.3.
    UniGenei Hs.303023.

    3D structure databases

    ProteinModelPortali Q9H4B7.
    SMRi Q9H4B7. Positions 1-430.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 123347. 27 interactions.
    DIPi DIP-42487N.
    IntActi Q9H4B7. 20 interactions.
    MINTi MINT-1891365.
    STRINGi 9606.ENSP00000217133.

    Chemistry

    BindingDBi Q9H4B7.
    ChEMBLi CHEMBL1915.
    DrugBanki DB01394. Colchicine.
    DB01248. Docetaxel.
    DB01229. Paclitaxel.
    DB00309. Vindesine.

    PTM databases

    PhosphoSitei Q9H4B7.

    Polymorphism databases

    DMDMi 62903515.

    2D gel databases

    OGPi Q9H4B7.

    Proteomic databases

    MaxQBi Q9H4B7.
    PaxDbi Q9H4B7.
    PeptideAtlasi Q9H4B7.
    PRIDEi Q9H4B7.

    Protocols and materials databases

    DNASUi 81027.
    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000217133 ; ENSP00000217133 ; ENSG00000101162 .
    GeneIDi 81027.
    KEGGi hsa:81027.
    UCSCi uc002yak.3. human.

    Organism-specific databases

    CTDi 81027.
    GeneCardsi GC20P057594.
    HGNCi HGNC:16257. TUBB1.
    HPAi CAB004286.
    HPA043640.
    HPA046280.
    MIMi 612901. gene.
    613112. phenotype.
    neXtProti NX_Q9H4B7.
    Orphaneti 140957. Autosomal dominant macrothrombocytopenia.
    PharmGKBi PA38100.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi COG5023.
    HOGENOMi HOG000165710.
    HOVERGENi HBG000089.
    InParanoidi Q9H4B7.
    KOi K07375.
    OMAi ACIFRGK.
    OrthoDBi EOG7ZKS9Z.
    PhylomeDBi Q9H4B7.
    TreeFami TF300298.

    Enzyme and pathway databases

    Reactomei REACT_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_682. Mitotic Prometaphase.
    REACT_9509. Gap junction assembly.

    Miscellaneous databases

    GeneWikii TUBB1.
    GenomeRNAii 81027.
    NextBioi 71348.
    PROi Q9H4B7.
    SOURCEi Search...

    Gene expression databases

    Bgeei Q9H4B7.
    CleanExi HS_TUBB1.
    Genevestigatori Q9H4B7.

    Family and domain databases

    Gene3Di 1.10.287.600. 1 hit.
    3.30.1330.20. 1 hit.
    3.40.50.1440. 1 hit.
    InterProi IPR013838. 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 ]
    PANTHERi PTHR11588. PTHR11588. 1 hit.
    Pfami PF00091. Tubulin. 1 hit.
    PF03953. Tubulin_C. 1 hit.
    [Graphical view ]
    PRINTSi PR01163. BETATUBULIN.
    PR01161. TUBULIN.
    SMARTi SM00864. Tubulin. 1 hit.
    SM00865. Tubulin_C. 1 hit.
    [Graphical view ]
    SUPFAMi SSF52490. SSF52490. 1 hit.
    SSF55307. SSF55307. 1 hit.
    PROSITEi PS00227. TUBULIN. 1 hit.
    PS00228. TUBULIN_B_AUTOREG. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    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: October 1, 2014
    This is version 112 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