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Q9D6F9

- TBB4A_MOUSE

UniProt

Q9D6F9 - TBB4A_MOUSE

Protein

Tubulin beta-4A chain

Gene

Tubb4a

Organism
Mus musculus (Mouse)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 116 (01 Oct 2014)
      Sequence version 3 (01 May 2007)
      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. GTPase activity Source: InterPro
    2. GTP binding Source: UniProtKB-KW
    3. structural constituent of cytoskeleton Source: InterPro

    GO - Biological processi

    1. cell projection organization Source: UniProtKB-KW
    2. microtubule-based process Source: InterPro
    3. protein polymerization Source: InterPro

    Keywords - Biological processi

    Cilium biogenesis/degradation

    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-4A chain
    Alternative name(s):
    Tubulin beta-4 chain
    Gene namesi
    Name:Tubb4a
    Synonyms:Tubb4
    OrganismiMus musculus (Mouse)
    Taxonomic identifieri10090 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
    ProteomesiUP000000589: Chromosome 17

    Organism-specific databases

    MGIiMGI:107848. Tubb4a.

    Subcellular locationi

    GO - Cellular componenti

    1. cell projection Source: MGI
    2. cilium Source: MGI
    3. cytoplasm Source: MGI
    4. internode region of axon Source: MGI
    5. microtubule Source: UniProtKB-KW
    6. myelin sheath Source: MGI
    7. neuronal cell body Source: MGI
    8. plasma membrane Source: Ensembl

    Keywords - Cellular componenti

    Cytoplasm, Cytoskeleton, Microtubule

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 444444Tubulin beta-4A chainPRO_0000048254Add
    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 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

    Phosphoprotein

    Proteomic databases

    MaxQBiQ9D6F9.
    PRIDEiQ9D6F9.

    2D gel databases

    REPRODUCTION-2DPAGEIPI00109073.
    Q9D6F9.

    PTM databases

    PhosphoSiteiQ9D6F9.

    Expressioni

    Gene expression databases

    BgeeiQ9D6F9.
    CleanExiMM_TUBB4.
    GenevestigatoriQ9D6F9.

    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

    BioGridi204380. 6 interactions.
    IntActiQ9D6F9. 8 interactions.
    MINTiMINT-4137071.

    Structurei

    3D structure databases

    ProteinModelPortaliQ9D6F9.
    SMRiQ9D6F9. 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

    GeneTreeiENSGT00750000117394.
    HOGENOMiHOG000165710.
    HOVERGENiHBG000089.
    InParanoidiQ9D6F9.
    KOiK07375.
    OMAiMQLERIN.
    OrthoDBiEOG71ZP1H.
    PhylomeDBiQ9D6F9.
    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.

    Q9D6F9-1 [UniParc]FASTAAdd to Basket

    « Hide

    MREIVHLQAG QCGNQIGAKF WEVISDEHGI DPTGTYHGDS DLQLERINVY    50
    YNEATGGNYV PRAVLVDLEP GTMDSVRSGP FGQIFRPDNF VFGQSGAGNN 100
    WAKGHYTEGA ELVDAVLDVV RKEAESCDCL QGFQLTHSLG GGTGSGMGTL 150
    LISKIREEFP DRIMNTFSVV PSPKVSDTVV EPYNATLSVH QLVENTDETY 200
    CIDNEALYDI CFRTLKLTTP TYGDLNHLVS ATMSGVTTCL RFPGQLNADL 250
    RKLAVNMVPF PRLHFFMPGF APLTSRGSQQ YRALTVPELT QQMFDAKNMM 300
    AACDPRHGRY LTVAAVFRGR MSMKEVDEQM LSVQSKNSSY FVEWIPNNVK 350
    TAVCDIPPRG LKMAATFIGN STAIQELFKR ISEQFTAMFR RKAFLHWYTG 400
    EGMDEMEFTE AESNMNDLVS EYQQYQDATA EEGEFEEEAE EEVA 444
    Length:444
    Mass (Da):49,586
    Last modified:May 1, 2007 - v3
    Checksum:iF7429D057C11A3F5
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti73 – 731M → I in AAA40509. (PubMed:3839797)Curated
    Sequence conflicti111 – 1111E → Q in AAA40509. (PubMed:3839797)Curated
    Sequence conflicti270 – 2701F → L in AAA40509. (PubMed:3839797)Curated
    Sequence conflicti293 – 2931M → V in AAA40509. (PubMed:3839797)Curated
    Sequence conflicti303 – 3031C → S in AAA40509. (PubMed:3839797)Curated
    Sequence conflicti351 – 3511T → A in AAA40509. (PubMed:3839797)Curated
    Sequence conflicti400 – 4001G → A in AAA40509. (PubMed:3839797)Curated
    Sequence conflicti427 – 4271D → G in BAB28967. (PubMed:16141072)Curated

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AK013717 mRNA. Translation: BAB28967.1.
    BC049112 mRNA. Translation: AAH49112.1.
    BC054831 mRNA. Translation: AAH54831.1.
    M28730 mRNA. Translation: AAA40509.1.
    CCDSiCCDS28925.1.
    RefSeqiNP_033477.2. NM_009451.3.
    UniGeneiMm.7420.

    Genome annotation databases

    EnsembliENSMUST00000071135; ENSMUSP00000071135; ENSMUSG00000062591.
    GeneIDi22153.
    KEGGimmu:22153.
    UCSCiuc008dea.1. mouse.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AK013717 mRNA. Translation: BAB28967.1 .
    BC049112 mRNA. Translation: AAH49112.1 .
    BC054831 mRNA. Translation: AAH54831.1 .
    M28730 mRNA. Translation: AAA40509.1 .
    CCDSi CCDS28925.1.
    RefSeqi NP_033477.2. NM_009451.3.
    UniGenei Mm.7420.

    3D structure databases

    ProteinModelPortali Q9D6F9.
    SMRi Q9D6F9. Positions 2-427.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 204380. 6 interactions.
    IntActi Q9D6F9. 8 interactions.
    MINTi MINT-4137071.

    Chemistry

    BindingDBi Q9D6F9.

    PTM databases

    PhosphoSitei Q9D6F9.

    2D gel databases

    REPRODUCTION-2DPAGE IPI00109073.
    Q9D6F9.

    Proteomic databases

    MaxQBi Q9D6F9.
    PRIDEi Q9D6F9.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENSMUST00000071135 ; ENSMUSP00000071135 ; ENSMUSG00000062591 .
    GeneIDi 22153.
    KEGGi mmu:22153.
    UCSCi uc008dea.1. mouse.

    Organism-specific databases

    CTDi 10382.
    MGIi MGI:107848. Tubb4a.

    Phylogenomic databases

    GeneTreei ENSGT00750000117394.
    HOGENOMi HOG000165710.
    HOVERGENi HBG000089.
    InParanoidi Q9D6F9.
    KOi K07375.
    OMAi MQLERIN.
    OrthoDBi EOG71ZP1H.
    PhylomeDBi Q9D6F9.
    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 302070.
    PROi Q9D6F9.
    SOURCEi Search...

    Gene expression databases

    Bgeei Q9D6F9.
    CleanExi MM_TUBB4.
    Genevestigatori Q9D6F9.

    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 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.
      Tissue: Hippocampus.
    2. "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.
      Tissue: Brain and Olfactory epithelium.
    3. Lubec G., Klug S., Kang S.U.
      Submitted (MAR-2007) to UniProtKB
      Cited for: PROTEIN SEQUENCE OF 3-19; 47-77; 104-121; 163-174; 242-276; 283-297; 310-318; 321-359; 363-379 AND 381-390, IDENTIFICATION BY MASS SPECTROMETRY.
      Strain: C57BL/6.
      Tissue: Brain and Hippocampus.
    4. "Five mouse tubulin isotypes and their regulated expression during development."
      Lewis S.A., Lee M.G.-S., Cowan N.J.
      J. Cell Biol. 101:852-861(1985) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 66-444.
    5. Cited for: POLYGLUTAMYLATION.
    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: POLYGLYCYLATION.

    Entry informationi

    Entry nameiTBB4A_MOUSE
    AccessioniPrimary (citable) accession number: Q9D6F9
    Secondary accession number(s): Q62364, Q80Y54
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: February 28, 2003
    Last sequence update: May 1, 2007
    Last modified: October 1, 2014
    This is version 116 of the entry and version 3 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