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P05214

- TBA3_MOUSE

UniProt

P05214 - TBA3_MOUSE

Protein

Tubulin alpha-3 chain

Gene

Tuba3a

more
Organism
Mus musculus (Mouse)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 133 (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.

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sitei450 – 4501Involved in polymerizationBy similarity

    Regions

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Nucleotide bindingi142 – 1487GTPSequence 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. microtubule-based process Source: InterPro
    2. protein polymerization Source: InterPro

    Keywords - Ligandi

    GTP-binding, Nucleotide-binding

    Enzyme and pathway databases

    ReactomeiREACT_196550. MHC class II antigen presentation.
    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 alpha-3 chain
    Alternative name(s):
    Alpha-tubulin 3/7
    Alpha-tubulin isotype M-alpha-3/7
    Tubulin alpha-3/alpha-7 chain
    Gene namesi
    Name:Tuba3a
    Synonyms:Tuba3
    AND
    Name:Tuba3b
    Synonyms:Tuba7
    OrganismiMus musculus (Mouse)
    Taxonomic identifieri10090 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
    ProteomesiUP000000589: Chromosome 6

    Organism-specific databases

    MGIiMGI:1095406. Tuba3a.
    MGI:1095408. Tuba3b.

    Subcellular locationi

    GO - Cellular componenti

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

    Keywords - Cellular componenti

    Cytoplasm, Cytoskeleton, Microtubule

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 450450Tubulin alpha-3 chainPRO_0000048122Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei48 – 481PhosphoserineBy similarity
    Modified residuei83 – 831Nitrated tyrosineBy similarity
    Modified residuei282 – 2821Nitrated tyrosineBy similarity
    Modified residuei432 – 4321PhosphotyrosineBy similarity
    Modified residuei439 – 4391PhosphoserineBy similarity

    Post-translational modificationi

    Undergoes a tyrosination/detyrosination cycle, the cyclic removal and re-addition of a C-terminal tyrosine residue by the enzymes tubulin tyrosine carboxypeptidase (TTCP) and tubulin tyrosine ligase (TTL), respectively.By similarity
    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.
    Acetylation of alpha chains at Lys-40 stabilizes microtubules and affects affinity and processivity of microtubule motors. This modification has a role in multiple cellular functions, ranging from cell motility, cell cycle progression or cell differentiation to intracellular trafficking and signaling By similarity.By similarity

    Keywords - PTMi

    Acetylation, Nitration, Phosphoprotein

    Proteomic databases

    PRIDEiP05214.

    2D gel databases

    REPRODUCTION-2DPAGEP05214.

    PTM databases

    PhosphoSiteiP05214.

    Expressioni

    Tissue specificityi

    Alpha-3 and alpha-7 are identical but coded by two different genes, they are testis-specific.1 Publication

    Gene expression databases

    BgeeiP05214.
    CleanExiMM_TUBA3A.
    MM_TUBA3B.
    GenevestigatoriP05214.

    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

    BioGridi204374. 2 interactions.
    STRINGi10090.ENSMUSP00000084713.

    Structurei

    3D structure databases

    ProteinModelPortaliP05214.
    SMRiP05214. Positions 1-440.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Sequence similaritiesi

    Belongs to the tubulin family.Curated

    Phylogenomic databases

    HOGENOMiHOG000165711.
    HOVERGENiHBG000089.
    InParanoidiP05214.
    KOiK07374.
    OMAiGTERECI.
    OrthoDBiEOG7TBC1W.
    PhylomeDBiP05214.
    TreeFamiTF300314.

    Family and domain databases

    Gene3Di1.10.287.600. 1 hit.
    3.30.1330.20. 1 hit.
    3.40.50.1440. 1 hit.
    InterProiIPR002452. Alpha_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]
    PRINTSiPR01162. ALPHATUBULIN.
    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.
    [Graphical view]

    Sequencei

    Sequence statusi: Complete.

    P05214-1 [UniParc]FASTAAdd to Basket

    « Hide

    MRECISIHVG QAGVQIGNAC WELYCLEHGI QPDGQMPSDK TIGGGDDSFN    50
    TFFSETGAGK HVPRAVFVDL EPTVVDEVRT GTYRQLFHPE QLITGKEDAA 100
    NNYARGHYTI GKEIVDLVLD RIRKLADLCT GLQGFLIFHS FGGGTGSGFA 150
    SLLMERLSVD YGKKSKLEFA IYPAPQVSTA VVEPYNSILT THTTLEHSDC 200
    AFMVDNEAIY DICRRNLDIE RPTYTNLNRL IGQIVSSITA SLRFDGALNV 250
    DLTEFQTNLV PYPRIHFPLA TYAPVISAEK AYHEQLSVAE ITNACFEPAN 300
    QMVKCDPRHG KYMACCMLYR GDVVPKDVNA AIATIKTKRT IQFVDWCPTG 350
    FKVGINYQPP TVVPGGDLAK VQRAVCMLSN TTAIAEAWAR LDHKFDLMYA 400
    KRAFVHWYVG EGMEEGEFSE AREDLAALEK DYEEVGVDSV EAEAEEGEEY 450
    Length:450
    Mass (Da):49,960
    Last modified:August 13, 1987 - v1
    Checksum:i2A78714CBA782D55
    GO

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    M13442 mRNA. Translation: AAA40501.1.
    M13443 mRNA. Translation: AAA40504.1.
    BC050769 mRNA. Translation: AAH50769.1.
    BC050770 mRNA. Translation: AAH50770.1.
    CCDSiCCDS39640.1.
    CCDS39707.1.
    PIRiI77426.
    RefSeqiNP_033472.1. NM_009446.2.
    NP_033475.1. NM_009449.3.
    UniGeneiMm.270295.
    Mm.287784.

    Genome annotation databases

    EnsembliENSMUST00000087445; ENSMUSP00000084713; ENSMUSG00000067338.
    ENSMUST00000088246; ENSMUSP00000085580; ENSMUSG00000067702.
    GeneIDi22144.
    22147.
    KEGGimmu:22144.
    mmu:22147.
    UCSCiuc009dui.1. mouse.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    M13442 mRNA. Translation: AAA40501.1 .
    M13443 mRNA. Translation: AAA40504.1 .
    BC050769 mRNA. Translation: AAH50769.1 .
    BC050770 mRNA. Translation: AAH50770.1 .
    CCDSi CCDS39640.1.
    CCDS39707.1.
    PIRi I77426.
    RefSeqi NP_033472.1. NM_009446.2.
    NP_033475.1. NM_009449.3.
    UniGenei Mm.270295.
    Mm.287784.

    3D structure databases

    ProteinModelPortali P05214.
    SMRi P05214. Positions 1-440.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 204374. 2 interactions.
    STRINGi 10090.ENSMUSP00000084713.

    PTM databases

    PhosphoSitei P05214.

    2D gel databases

    REPRODUCTION-2DPAGE P05214.

    Proteomic databases

    PRIDEi P05214.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENSMUST00000087445 ; ENSMUSP00000084713 ; ENSMUSG00000067338 .
    ENSMUST00000088246 ; ENSMUSP00000085580 ; ENSMUSG00000067702 .
    GeneIDi 22144.
    22147.
    KEGGi mmu:22144.
    mmu:22147.
    UCSCi uc009dui.1. mouse.

    Organism-specific databases

    CTDi 22144.
    22147.
    MGIi MGI:1095406. Tuba3a.
    MGI:1095408. Tuba3b.

    Phylogenomic databases

    HOGENOMi HOG000165711.
    HOVERGENi HBG000089.
    InParanoidi P05214.
    KOi K07374.
    OMAi GTERECI.
    OrthoDBi EOG7TBC1W.
    PhylomeDBi P05214.
    TreeFami TF300314.

    Enzyme and pathway databases

    Reactomei REACT_196550. MHC class II antigen presentation.
    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 302046.
    PROi P05214.
    SOURCEi Search...

    Gene expression databases

    Bgeei P05214.
    CleanExi MM_TUBA3A.
    MM_TUBA3B.
    Genevestigatori P05214.

    Family and domain databases

    Gene3Di 1.10.287.600. 1 hit.
    3.30.1330.20. 1 hit.
    3.40.50.1440. 1 hit.
    InterProi IPR002452. Alpha_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 PR01162. ALPHATUBULIN.
    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.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "Six mouse alpha-tubulin mRNAs encode five distinct isotypes: testis-specific expression of two sister genes."
      Villasante A., Wang D., Dobner P., Dolph P., Lewis S.A., Cowan N.J.
      Mol. Cell. Biol. 6:2409-2419(1986) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA], TISSUE SPECIFICITY.
    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].
      Tissue: Testis.
    3. Lubec G., Klug S., Yang J.W., Zigmond M.
      Submitted (JUL-2007) to UniProtKB
      Cited for: PROTEIN SEQUENCE OF 230-280, IDENTIFICATION BY MASS SPECTROMETRY.
      Tissue: Brain and Hippocampus.
    4. Cited for: POLYGLUTAMYLATION.
    5. "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 nameiTBA3_MOUSE
    AccessioniPrimary (citable) accession number: P05214
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: August 13, 1987
    Last sequence update: August 13, 1987
    Last modified: October 1, 2014
    This is version 133 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