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P68372

- TBB4B_MOUSE

UniProt

P68372 - TBB4B_MOUSE

Protein

Tubulin beta-4B chain

Gene

Tubb4b

Organism
Mus musculus (Mouse)
Status
Reviewed - Annotation score: 4 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 105 (01 Oct 2014)
      Sequence version 1 (13 Aug 1987)
      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.

    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
    4. structural constituent of cytoskeleton Source: InterPro

    GO - Biological processi

    1. microtubule-based process Source: UniProtKB
    2. protein polymerization Source: InterPro

    Keywords - Ligandi

    GTP-binding, Nucleotide-binding

    Enzyme and pathway databases

    ReactomeiREACT_196550. MHC class II antigen presentation.
    REACT_196635. Regulation of PLK1 Activity at G2/M Transition.
    REACT_198961. Resolution of Sister Chromatid Cohesion.
    REACT_199054. Translocation of GLUT4 to the plasma membrane.
    REACT_199117. Kinesins.
    REACT_207679. Separation of Sister Chromatids.
    REACT_218773. Microtubule-dependent trafficking of connexons from Golgi to the plasma membrane.
    REACT_227366. Gap junction assembly.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Tubulin beta-4B chain
    Alternative name(s):
    Tubulin beta-2C chain
    Gene namesi
    Name:Tubb4b
    Synonyms:Tubb2c
    OrganismiMus musculus (Mouse)
    Taxonomic identifieri10090 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
    ProteomesiUP000000589: Chromosome 2

    Organism-specific databases

    MGIiMGI:1915472. Tubb4b.

    Subcellular locationi

    GO - Cellular componenti

    1. cytoplasm Source: UniProtKB-KW
    2. microtubule Source: UniProtKB-KW
    3. tubulin complex Source: UniProtKB

    Keywords - Cellular componenti

    Cytoplasm, Cytoskeleton, Microtubule

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 445445Tubulin beta-4B chainPRO_0000048249Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei58 – 581N6-acetyllysine1 Publication
    Modified residuei172 – 1721Phosphoserine; by CDK1By similarity

    Post-translational modificationi

    Some glutamate residues at the C-terminus are either polyglutamylated or polyglycylated. These 2 modifications occur exclusively on glutamate residues and result in either polyglutamate or polyglycine chains on the gamma-carboxyl group. Glycylation 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 polyglycylation levels increases polyglutamylation, and reciprocally. The precise function of such modifications is still unclear but they are regulate the assembly and dynamics of axonemal microtubules.

    Keywords - PTMi

    Acetylation, Phosphoprotein

    Proteomic databases

    MaxQBiP68372.
    PaxDbiP68372.
    PRIDEiP68372.

    2D gel databases

    REPRODUCTION-2DPAGEIPI00169463.
    P68372.
    UCD-2DPAGEP05217.
    P68372.

    PTM databases

    PhosphoSiteiP68372.

    Expressioni

    Gene expression databases

    BgeeiP68372.
    CleanExiMM_TUBB2C.
    GenevestigatoriP68372.

    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

    BioGridi230642. 28 interactions.
    IntActiP68372. 39 interactions.
    MINTiMINT-4137100.

    Structurei

    3D structure databases

    ProteinModelPortaliP68372.
    SMRiP68372. 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

    eggNOGiCOG5023.
    GeneTreeiENSGT00750000117394.
    HOGENOMiHOG000165710.
    HOVERGENiHBG000089.
    InParanoidiP68372.
    KOiK07375.
    OMAiREIVSIQ.
    OrthoDBiEOG71ZP1H.
    PhylomeDBiP68372.
    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.

    P68372-1 [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

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti207 – 2071L → P in AAH05547. (PubMed:15489334)Curated
    Sequence conflicti342 – 3421V → A in BAE27282. (PubMed:16141072)Curated

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AK146587 mRNA. Translation: BAE27282.1.
    AK167022 mRNA. Translation: BAE39195.1.
    AL732309 Genomic DNA. Translation: CAM14671.1.
    BC005547 mRNA. Translation: AAH05547.1.
    BC022919 mRNA. Translation: AAH22919.1.
    BC083319 mRNA. Translation: AAH83319.1.
    CCDSiCCDS15753.1.
    PIRiC25437.
    RefSeqiNP_666228.1. NM_146116.2.
    UniGeneiMm.227260.
    Mm.491119.

    Genome annotation databases

    EnsembliENSMUST00000043584; ENSMUSP00000042342; ENSMUSG00000036752.
    GeneIDi227613.
    KEGGimmu:227613.
    UCSCiuc008iqs.2. mouse.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AK146587 mRNA. Translation: BAE27282.1 .
    AK167022 mRNA. Translation: BAE39195.1 .
    AL732309 Genomic DNA. Translation: CAM14671.1 .
    BC005547 mRNA. Translation: AAH05547.1 .
    BC022919 mRNA. Translation: AAH22919.1 .
    BC083319 mRNA. Translation: AAH83319.1 .
    CCDSi CCDS15753.1.
    PIRi C25437.
    RefSeqi NP_666228.1. NM_146116.2.
    UniGenei Mm.227260.
    Mm.491119.

    3D structure databases

    ProteinModelPortali P68372.
    SMRi P68372. Positions 2-427.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 230642. 28 interactions.
    IntActi P68372. 39 interactions.
    MINTi MINT-4137100.

    Chemistry

    BindingDBi P68372.

    PTM databases

    PhosphoSitei P68372.

    2D gel databases

    REPRODUCTION-2DPAGE IPI00169463.
    P68372.
    UCD-2DPAGE P05217.
    P68372.

    Proteomic databases

    MaxQBi P68372.
    PaxDbi P68372.
    PRIDEi P68372.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENSMUST00000043584 ; ENSMUSP00000042342 ; ENSMUSG00000036752 .
    GeneIDi 227613.
    KEGGi mmu:227613.
    UCSCi uc008iqs.2. mouse.

    Organism-specific databases

    CTDi 10383.
    MGIi MGI:1915472. Tubb4b.

    Phylogenomic databases

    eggNOGi COG5023.
    GeneTreei ENSGT00750000117394.
    HOGENOMi HOG000165710.
    HOVERGENi HBG000089.
    InParanoidi P68372.
    KOi K07375.
    OMAi REIVSIQ.
    OrthoDBi EOG71ZP1H.
    PhylomeDBi P68372.
    TreeFami TF300298.

    Enzyme and pathway databases

    Reactomei REACT_196550. MHC class II antigen presentation.
    REACT_196635. Regulation of PLK1 Activity at G2/M Transition.
    REACT_198961. Resolution of Sister Chromatid Cohesion.
    REACT_199054. Translocation of GLUT4 to the plasma membrane.
    REACT_199117. Kinesins.
    REACT_207679. Separation of Sister Chromatids.
    REACT_218773. Microtubule-dependent trafficking of connexons from Golgi to the plasma membrane.
    REACT_227366. Gap junction assembly.

    Miscellaneous databases

    NextBioi 378658.
    PROi P68372.
    SOURCEi Search...

    Gene expression databases

    Bgeei P68372.
    CleanExi MM_TUBB2C.
    Genevestigatori P68372.

    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. "The mammalian beta-tubulin repertoire: hematopoietic expression of a novel, heterologous beta-tubulin isotype."
      Wang D., Villasante A., Lewis S.A., Cowan N.J.
      J. Cell Biol. 103:1903-1910(1986) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA].
    2. "The transcriptional landscape of the mammalian genome."
      Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.
      , Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.
      Science 309:1559-1563(2005) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
      Strain: C57BL/6J.
    3. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
      Strain: C57BL/6J.
    4. "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].
      Strain: C57BL/6 and FVB/N.
      Tissue: Brain, Kidney and Mammary tumor.
    5. Lubec G., Klug S., Kang S.U., Sunyer B., Chen W.-Q.
      Submitted (JAN-2009) to UniProtKB
      Cited for: PROTEIN SEQUENCE OF 3-19; 47-58; 63-121; 163-174; 217-276; 283-297; 310-318; 321-359; 363-379 AND 381-390, IDENTIFICATION BY MASS SPECTROMETRY.
      Strain: C57BL/6 and OF1.
      Tissue: Brain and Hippocampus.
    6. Cited for: POLYGLUTAMYLATION.
    7. "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: POLYGLYCYLATION.
    8. "SIRT5-mediated lysine desuccinylation impacts diverse metabolic pathways."
      Park J., Chen Y., Tishkoff D.X., Peng C., Tan M., Dai L., Xie Z., Zhang Y., Zwaans B.M., Skinner M.E., Lombard D.B., Zhao Y.
      Mol. Cell 50:919-930(2013) [PubMed] [Europe PMC] [Abstract]
      Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-58, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Embryonic fibroblast.

    Entry informationi

    Entry nameiTBB4B_MOUSE
    AccessioniPrimary (citable) accession number: P68372
    Secondary accession number(s): P05217
    , Q3TKF0, Q3UJ73, Q99JZ6
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: August 13, 1987
    Last sequence update: August 13, 1987
    Last modified: October 1, 2014
    This is version 105 of the entry and version 1 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programChordata Protein Annotation Program

    Miscellaneousi

    Keywords - Technical termi

    Complete proteome, Direct protein sequencing, Reference proteome

    Documents

    1. MGD cross-references
      Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
    2. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3