Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Basket 0
(max 400 entries)x

Your basket is currently empty.

Select item(s) and click on "Add to basket" to create your own collection here
(400 entries max)

P68371

- TBB4B_HUMAN

UniProt

P68371 - TBB4B_HUMAN

Protein

Tubulin beta-4B chain

Gene

TUBB4B

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
    • BLAST
    • Align
    • Format
    • Add to basket
    • History
      Entry version 111 (01 Oct 2014)
      Sequence version 1 (13 Aug 1987)
      Previous versions | rss
    • Help video
    • Feedback
    • Comment

    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.

    Regions

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

    GO - Molecular functioni

    1. double-stranded RNA binding Source: MGI
    2. GTPase activity Source: InterPro
    3. GTP binding Source: UniProtKB-KW
    4. MHC class I protein binding Source: UniProtKB
    5. structural constituent of cytoskeleton Source: InterPro
    6. unfolded protein binding Source: UniProtKB

    GO - Biological processi

    1. 'de novo' posttranslational protein folding Source: Reactome
    2. cellular component movement Source: ProtInc
    3. cellular protein metabolic process Source: Reactome
    4. G2/M transition of mitotic cell cycle Source: Reactome
    5. microtubule-based process Source: InterPro
    6. mitotic cell cycle Source: Reactome
    7. natural killer cell mediated cytotoxicity Source: UniProtKB
    8. protein folding Source: Reactome
    9. protein polymerization Source: InterPro

    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_15296. Recruitment of mitotic centrosome proteins and complexes.
    REACT_15364. Loss of Nlp from mitotic centrosomes.
    REACT_15451. Loss of proteins required for interphase microtubule organization from the centrosome.
    REACT_15510. Recruitment of NuMA to mitotic centrosomes.
    REACT_160315. Regulation of PLK1 Activity at G2/M Transition.
    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-4B chain
    Alternative name(s):
    Tubulin beta-2 chain
    Tubulin beta-2C chain
    Gene namesi
    Name:TUBB4B
    Synonyms:TUBB2C
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 9

    Organism-specific databases

    HGNCiHGNC:20771. TUBB4B.

    Subcellular locationi

    GO - Cellular componenti

    1. cytoskeleton Source: ProtInc
    2. cytosol Source: Reactome
    3. extracellular vesicular exosome Source: UniProt
    4. microtubule Source: UniProtKB
    5. nucleus Source: UniProt

    Keywords - Cellular componenti

    Cytoplasm, Cytoskeleton, Microtubule

    Pathology & Biotechi

    Organism-specific databases

    PharmGKBiPA142670672.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 445445Tubulin beta-4B chainPRO_0000048248Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei58 – 581N6-acetyllysine1 Publication
    Modified residuei172 – 1721Phosphoserine; by CDK1Curated

    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

    Acetylation, Phosphoprotein

    Proteomic databases

    MaxQBiP68371.
    PeptideAtlasiP68371.
    PRIDEiP68371.

    2D gel databases

    OGPiP05217.
    REPRODUCTION-2DPAGEIPI00007752.
    SWISS-2DPAGEP68371.

    PTM databases

    PhosphoSiteiP68371.

    Expressioni

    Tissue specificityi

    Ubiquitous.1 Publication

    Gene expression databases

    ArrayExpressiP68371.
    BgeeiP68371.
    CleanExiHS_TUBB2C.
    GenevestigatoriP68371.

    Organism-specific databases

    HPAiCAB010880.
    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.

    Protein-protein interaction databases

    BioGridi115656. 94 interactions.
    IntActiP68371. 41 interactions.
    MINTiMINT-1390314.
    STRINGi9606.ENSP00000341289.

    Structurei

    3D structure databases

    ProteinModelPortaliP68371.
    SMRiP68371. Positions 2-427.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Domaini

    The highly acidic C-terminal region may bind cations such as calcium.

    Sequence similaritiesi

    Belongs to the tubulin family.Curated

    Phylogenomic databases

    HOGENOMiHOG000165710.
    HOVERGENiHBG000089.
    InParanoidiP68371.
    KOiK07375.
    OMAiREIVSIQ.
    OrthoDBiEOG71ZP1H.
    PhylomeDBiP68371.
    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.

    P68371-1 [UniParc]FASTAAdd to Basket

    « Hide

    MREIVHLQAG QCGNQIGAKF WEVISDEHGI DPTGTYHGDS DLQLERINVY    50
    YNEATGGKYV PRAVLVDLEP GTMDSVRSGP FGQIFRPDNF VFGQSGAGNN 100
    WAKGHYTEGA ELVDSVLDVV RKEAESCDCL QGFQLTHSLG GGTGSGMGTL 150
    LISKIREEYP DRIMNTFSVV PSPKVSDTVV EPYNATLSVH QLVENTDETY 200
    CIDNEALYDI CFRTLKLTTP TYGDLNHLVS ATMSGVTTCL RFPGQLNADL 250
    RKLAVNMVPF PRLHFFMPGF APLTSRGSQQ YRALTVPELT QQMFDAKNMM 300
    AACDPRHGRY LTVAAVFRGR MSMKEVDEQM LNVQNKNSSY FVEWIPNNVK 350
    TAVCDIPPRG LKMSATFIGN STAIQELFKR ISEQFTAMFR RKAFLHWYTG 400
    EGMDEMEFTE AESNMNDLVS EYQQYQDATA EEEGEFEEEA EEEVA 445
    Length:445
    Mass (Da):49,831
    Last modified:August 13, 1987 - v1
    Checksum:iA552C52822AFA072
    GO

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    X02344 Genomic DNA. Translation: CAA26203.1.
    BX255925 Genomic DNA. Translation: CAM24148.1.
    BC001911 mRNA. Translation: AAH01911.1.
    BC002783 mRNA. Translation: AAH02783.1.
    BC002885 mRNA. Translation: AAH02885.1.
    BC004188 mRNA. Translation: AAH04188.1.
    BC007889 mRNA. Translation: AAH07889.1.
    BC012835 mRNA. Translation: AAH12835.1.
    BC019359 mRNA. Translation: AAH19359.1.
    BC019829 mRNA. Translation: AAH19829.1.
    BC039175 mRNA. Translation: AAH39175.1.
    BC071889 mRNA. Translation: AAH71889.1.
    CCDSiCCDS7039.1.
    PIRiI38370.
    RefSeqiNP_006079.1. NM_006088.5.
    UniGeneiHs.433615.

    Genome annotation databases

    EnsembliENST00000340384; ENSP00000341289; ENSG00000188229.
    GeneIDi10383.
    KEGGihsa:10383.
    UCSCiuc004cmg.1. human.

    Polymorphism databases

    DMDMi55977480.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    X02344 Genomic DNA. Translation: CAA26203.1 .
    BX255925 Genomic DNA. Translation: CAM24148.1 .
    BC001911 mRNA. Translation: AAH01911.1 .
    BC002783 mRNA. Translation: AAH02783.1 .
    BC002885 mRNA. Translation: AAH02885.1 .
    BC004188 mRNA. Translation: AAH04188.1 .
    BC007889 mRNA. Translation: AAH07889.1 .
    BC012835 mRNA. Translation: AAH12835.1 .
    BC019359 mRNA. Translation: AAH19359.1 .
    BC019829 mRNA. Translation: AAH19829.1 .
    BC039175 mRNA. Translation: AAH39175.1 .
    BC071889 mRNA. Translation: AAH71889.1 .
    CCDSi CCDS7039.1.
    PIRi I38370.
    RefSeqi NP_006079.1. NM_006088.5.
    UniGenei Hs.433615.

    3D structure databases

    ProteinModelPortali P68371.
    SMRi P68371. Positions 2-427.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 115656. 94 interactions.
    IntActi P68371. 41 interactions.
    MINTi MINT-1390314.
    STRINGi 9606.ENSP00000341289.

    Chemistry

    BindingDBi P68371.
    ChEMBLi CHEMBL2095182.

    PTM databases

    PhosphoSitei P68371.

    Polymorphism databases

    DMDMi 55977480.

    2D gel databases

    OGPi P05217.
    REPRODUCTION-2DPAGE IPI00007752.
    SWISS-2DPAGE P68371.

    Proteomic databases

    MaxQBi P68371.
    PeptideAtlasi P68371.
    PRIDEi P68371.

    Protocols and materials databases

    DNASUi 10383.
    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000340384 ; ENSP00000341289 ; ENSG00000188229 .
    GeneIDi 10383.
    KEGGi hsa:10383.
    UCSCi uc004cmg.1. human.

    Organism-specific databases

    CTDi 10383.
    GeneCardsi GC09P140136.
    HGNCi HGNC:20771. TUBB4B.
    HPAi CAB010880.
    HPA043640.
    HPA046280.
    MIMi 602660. gene.
    neXtProti NX_P68371.
    PharmGKBi PA142670672.
    GenAtlasi Search...

    Phylogenomic databases

    HOGENOMi HOG000165710.
    HOVERGENi HBG000089.
    InParanoidi P68371.
    KOi K07375.
    OMAi REIVSIQ.
    OrthoDBi EOG71ZP1H.
    PhylomeDBi P68371.
    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_15296. Recruitment of mitotic centrosome proteins and complexes.
    REACT_15364. Loss of Nlp from mitotic centrosomes.
    REACT_15451. Loss of proteins required for interphase microtubule organization from the centrosome.
    REACT_15510. Recruitment of NuMA to mitotic centrosomes.
    REACT_160315. Regulation of PLK1 Activity at G2/M Transition.
    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

    ChiTaRSi TUBB4B. human.
    GeneWikii TUBB2C.
    GenomeRNAii 10383.
    NextBioi 39335.
    PROi P68371.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi P68371.
    Bgeei P68371.
    CleanExi HS_TUBB2C.
    Genevestigatori P68371.

    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. "Three expressed sequences within the human beta-tubulin multigene family each define a distinct isotype."
      Lewis S.A., Gilmartin M.E., Hall J.L., Cowan N.J.
      J. Mol. Biol. 182:11-20(1985) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    2. "DNA sequence and analysis of human chromosome 9."
      Humphray S.J., Oliver K., Hunt A.R., Plumb R.W., Loveland J.E., Howe K.L., Andrews T.D., Searle S., Hunt S.E., Scott C.E., Jones M.C., Ainscough R., Almeida J.P., Ambrose K.D., Ashwell R.I.S., Babbage A.K., Babbage S., Bagguley C.L.
      , Bailey J., Banerjee R., Barker D.J., Barlow K.F., Bates K., Beasley H., Beasley O., Bird C.P., Bray-Allen S., Brown A.J., Brown J.Y., Burford D., Burrill W., Burton J., Carder C., Carter N.P., Chapman J.C., Chen Y., Clarke G., Clark S.Y., Clee C.M., Clegg S., Collier R.E., Corby N., Crosier M., Cummings A.T., Davies J., Dhami P., Dunn M., Dutta I., Dyer L.W., Earthrowl M.E., Faulkner L., Fleming C.J., Frankish A., Frankland J.A., French L., Fricker D.G., Garner P., Garnett J., Ghori J., Gilbert J.G.R., Glison C., Grafham D.V., Gribble S., Griffiths C., Griffiths-Jones S., Grocock R., Guy J., Hall R.E., Hammond S., Harley J.L., Harrison E.S.I., Hart E.A., Heath P.D., Henderson C.D., Hopkins B.L., Howard P.J., Howden P.J., Huckle E., Johnson C., Johnson D., Joy A.A., Kay M., Keenan S., Kershaw J.K., Kimberley A.M., King A., Knights A., Laird G.K., Langford C., Lawlor S., Leongamornlert D.A., Leversha M., Lloyd C., Lloyd D.M., Lovell J., Martin S., Mashreghi-Mohammadi M., Matthews L., McLaren S., McLay K.E., McMurray A., Milne S., Nickerson T., Nisbett J., Nordsiek G., Pearce A.V., Peck A.I., Porter K.M., Pandian R., Pelan S., Phillimore B., Povey S., Ramsey Y., Rand V., Scharfe M., Sehra H.K., Shownkeen R., Sims S.K., Skuce C.D., Smith M., Steward C.A., Swarbreck D., Sycamore N., Tester J., Thorpe A., Tracey A., Tromans A., Thomas D.W., Wall M., Wallis J.M., West A.P., Whitehead S.L., Willey D.L., Williams S.A., Wilming L., Wray P.W., Young L., Ashurst J.L., Coulson A., Blocker H., Durbin R.M., Sulston J.E., Hubbard T., Jackson M.J., Bentley D.R., Beck S., Rogers J., Dunham I.
      Nature 429:369-374(2004) [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, Cervix, Lung, Lymph, Muscle, Skin and Uterus.
    4. "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.
    5. "Lysine acetylation targets protein complexes and co-regulates major cellular functions."
      Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T.C., Olsen J.V., Mann M.
      Science 325:834-840(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-58, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    6. Cited for: TISSUE SPECIFICITY.
    7. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].

    Entry informationi

    Entry nameiTBB4B_HUMAN
    AccessioniPrimary (citable) accession number: P68371
    Secondary accession number(s): A2BFA2, P05217
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: August 13, 1987
    Last sequence update: August 13, 1987
    Last modified: October 1, 2014
    This is version 111 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, Reference proteome

    Documents

    1. Human chromosome 9
      Human chromosome 9: entries, gene names and cross-references to MIM
    2. MIM cross-references
      Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
    3. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3