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Q56WH1

- TBA3_ARATH

UniProt

Q56WH1 - TBA3_ARATH

Protein

Tubulin alpha-3 chain

Gene

TUBA3

Organism
Arabidopsis thaliana (Mouse-ear cress)
Status
Reviewed - Annotation score: 4 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 62 (01 Oct 2014)
      Sequence version 2 (03 Oct 2012)
      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 polymerization

    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

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Tubulin alpha-3 chain
    Gene namesi
    Name:TUBA3
    Synonyms:TUA3
    Ordered Locus Names:At5g19770
    ORF Names:T29J13.190
    OrganismiArabidopsis thaliana (Mouse-ear cress)
    Taxonomic identifieri3702 [NCBI]
    Taxonomic lineageiEukaryotaViridiplantaeStreptophytaEmbryophytaTracheophytaSpermatophytaMagnoliophytaeudicotyledonsGunneridaePentapetalaerosidsmalvidsBrassicalesBrassicaceaeCamelineaeArabidopsis
    ProteomesiUP000006548: Chromosome 5

    Organism-specific databases

    TAIRiAT5G19770.

    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_0000048138Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei349 – 3491Phosphothreonine1 Publication

    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

    Keywords - PTMi

    Phosphoprotein

    Proteomic databases

    PRIDEiQ56WH1.

    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

    IntActiQ56WH1. 1 interaction.

    Structurei

    3D structure databases

    ProteinModelPortaliQ56WH1.
    SMRiQ56WH1. Positions 1-436.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Sequence similaritiesi

    Belongs to the tubulin family.Curated

    Phylogenomic databases

    eggNOGiCOG5023.
    HOGENOMiHOG000165711.
    KOiK07374.
    PhylomeDBiQ56WH1.

    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.
    IPR013838. Beta-tubulin_BS.
    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.

    Q56WH1-1 [UniParc]FASTAAdd to Basket

    « Hide

    MREIISIHIG QAGIQVGNSC WELYCLEHGI QPDGMMPSDT TVGVAHDAFN    50
    TFFSETGAGK HVPRAVFVDL EPTVIDEVRT GTYRQLFHPE QLISGKEDAA 100
    NNFARGHYTV GKEIVDLCLD RVRKLADNCT GLQGFLVFNA VGGGTGSGLG 150
    SLLLERLSVD YGKKSKLGFT IYPSPQVSTA VVEPYNSVLS THSLLEHTDV 200
    AVLLDNEAIY DICRRSLDIE RPTYTNLNRL ISQIISSLTT SLRFDGAINV 250
    DITEFQTNLV PYPRIHFMLS SYAPVISAAK AYHEQLSVPE ITNAVFEPAS 300
    MMAKCDPRHG KYMACCLMYR GDVVPKDVNA AVGTIKTKRT VQFVDWCPTG 350
    FKCGINYQPP TVVPGGDLAK VQRAVCMISN NTAVAEVFSR IDHKFDLMYA 400
    KRAFVHWYVG EGMEEGEFSE AREDLAALEK DYEEVGAEGG DDEEDEGEDY 450
    Length:450
    Mass (Da):49,654
    Last modified:October 3, 2012 - v2
    Checksum:iB6AD6D00244CFB71
    GO

    Sequence cautioni

    The sequence BAD94893.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally extended.

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti308 – 3081R → K in BAD94893. 1 PublicationCurated

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    M17189 Genomic DNA. Translation: AAA32888.1.
    AF296838 Genomic DNA. No translation available.
    CP002688 Genomic DNA. Translation: AED92747.1.
    AF367301 mRNA. Translation: AAK32888.1.
    AY065164 mRNA. Translation: AAL38340.1.
    AY143895 mRNA. Translation: AAN28834.1.
    BT000718 mRNA. Translation: AAN31860.1.
    BT000719 mRNA. Translation: AAN31861.1.
    BT001197 mRNA. Translation: AAN65084.1.
    AK222069 mRNA. Translation: BAD94893.1. Different initiation.
    PIRiA32712.
    RefSeqiNP_197478.1. NM_121982.3.
    NP_197479.1. NM_121983.3.
    UniGeneiAt.23553.
    At.49039.
    At.75628.

    Genome annotation databases

    EnsemblPlantsiAT5G19770.1; AT5G19770.1; AT5G19770.
    AT5G19780.1; AT5G19780.1; AT5G19780.
    GeneIDi832097.
    832098.
    KEGGiath:AT5G19770.
    ath:AT5G19780.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    M17189 Genomic DNA. Translation: AAA32888.1 .
    AF296838 Genomic DNA. No translation available.
    CP002688 Genomic DNA. Translation: AED92747.1 .
    AF367301 mRNA. Translation: AAK32888.1 .
    AY065164 mRNA. Translation: AAL38340.1 .
    AY143895 mRNA. Translation: AAN28834.1 .
    BT000718 mRNA. Translation: AAN31860.1 .
    BT000719 mRNA. Translation: AAN31861.1 .
    BT001197 mRNA. Translation: AAN65084.1 .
    AK222069 mRNA. Translation: BAD94893.1 . Different initiation.
    PIRi A32712.
    RefSeqi NP_197478.1. NM_121982.3.
    NP_197479.1. NM_121983.3.
    UniGenei At.23553.
    At.49039.
    At.75628.

    3D structure databases

    ProteinModelPortali Q56WH1.
    SMRi Q56WH1. Positions 1-436.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    IntActi Q56WH1. 1 interaction.

    Proteomic databases

    PRIDEi Q56WH1.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    EnsemblPlantsi AT5G19770.1 ; AT5G19770.1 ; AT5G19770 .
    AT5G19780.1 ; AT5G19780.1 ; AT5G19780 .
    GeneIDi 832097.
    832098.
    KEGGi ath:AT5G19770.
    ath:AT5G19780.

    Organism-specific databases

    TAIRi AT5G19770.

    Phylogenomic databases

    eggNOGi COG5023.
    HOGENOMi HOG000165711.
    KOi K07374.
    PhylomeDBi Q56WH1.

    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.
    IPR013838. Beta-tubulin_BS.
    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. "Characterization of the alpha-tubulin gene family of Arabidopsis thaliana."
      Ludwig S.R., Oppenheimer D.G., Silflow C.D., Snustad D.P.
      Proc. Natl. Acad. Sci. U.S.A. 84:5833-5837(1987) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    2. "Sequence and analysis of chromosome 5 of the plant Arabidopsis thaliana."
      Tabata S., Kaneko T., Nakamura Y., Kotani H., Kato T., Asamizu E., Miyajima N., Sasamoto S., Kimura T., Hosouchi T., Kawashima K., Kohara M., Matsumoto M., Matsuno A., Muraki A., Nakayama S., Nakazaki N., Naruo K.
      , Okumura S., Shinpo S., Takeuchi C., Wada T., Watanabe A., Yamada M., Yasuda M., Sato S., de la Bastide M., Huang E., Spiegel L., Gnoj L., O'Shaughnessy A., Preston R., Habermann K., Murray J., Johnson D., Rohlfing T., Nelson J., Stoneking T., Pepin K., Spieth J., Sekhon M., Armstrong J., Becker M., Belter E., Cordum H., Cordes M., Courtney L., Courtney W., Dante M., Du H., Edwards J., Fryman J., Haakensen B., Lamar E., Latreille P., Leonard S., Meyer R., Mulvaney E., Ozersky P., Riley A., Strowmatt C., Wagner-McPherson C., Wollam A., Yoakum M., Bell M., Dedhia N., Parnell L., Shah R., Rodriguez M., Hoon See L., Vil D., Baker J., Kirchoff K., Toth K., King L., Bahret A., Miller B., Marra M.A., Martienssen R., McCombie W.R., Wilson R.K., Murphy G., Bancroft I., Volckaert G., Wambutt R., Duesterhoeft A., Stiekema W., Pohl T., Entian K.-D., Terryn N., Hartley N., Bent E., Johnson S., Langham S.-A., McCullagh B., Robben J., Grymonprez B., Zimmermann W., Ramsperger U., Wedler H., Balke K., Wedler E., Peters S., van Staveren M., Dirkse W., Mooijman P., Klein Lankhorst R., Weitzenegger T., Bothe G., Rose M., Hauf J., Berneiser S., Hempel S., Feldpausch M., Lamberth S., Villarroel R., Gielen J., Ardiles W., Bents O., Lemcke K., Kolesov G., Mayer K.F.X., Rudd S., Schoof H., Schueller C., Zaccaria P., Mewes H.-W., Bevan M., Fransz P.F.
      Nature 408:823-826(2000) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
      Strain: cv. Columbia.
    3. The Arabidopsis Information Resource (TAIR)
      Submitted (APR-2011) to the EMBL/GenBank/DDBJ databases
      Cited for: GENOME REANNOTATION.
      Strain: cv. Columbia.
    4. "Empirical analysis of transcriptional activity in the Arabidopsis genome."
      Yamada K., Lim J., Dale J.M., Chen H., Shinn P., Palm C.J., Southwick A.M., Wu H.C., Kim C.J., Nguyen M., Pham P.K., Cheuk R.F., Karlin-Newmann G., Liu S.X., Lam B., Sakano H., Wu T., Yu G.
      , Miranda M., Quach H.L., Tripp M., Chang C.H., Lee J.M., Toriumi M.J., Chan M.M., Tang C.C., Onodera C.S., Deng J.M., Akiyama K., Ansari Y., Arakawa T., Banh J., Banno F., Bowser L., Brooks S.Y., Carninci P., Chao Q., Choy N., Enju A., Goldsmith A.D., Gurjal M., Hansen N.F., Hayashizaki Y., Johnson-Hopson C., Hsuan V.W., Iida K., Karnes M., Khan S., Koesema E., Ishida J., Jiang P.X., Jones T., Kawai J., Kamiya A., Meyers C., Nakajima M., Narusaka M., Seki M., Sakurai T., Satou M., Tamse R., Vaysberg M., Wallender E.K., Wong C., Yamamura Y., Yuan S., Shinozaki K., Davis R.W., Theologis A., Ecker J.R.
      Science 302:842-846(2003) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
      Strain: cv. Columbia.
    5. "Large-scale analysis of RIKEN Arabidopsis full-length (RAFL) cDNAs."
      Totoki Y., Seki M., Ishida J., Nakajima M., Enju A., Kamiya A., Narusaka M., Shin-i T., Nakagawa M., Sakamoto N., Oishi K., Kohara Y., Kobayashi M., Toyoda A., Sakaki Y., Sakurai T., Iida K., Akiyama K.
      , Satou M., Toyoda T., Konagaya A., Carninci P., Kawai J., Hayashizaki Y., Shinozaki K.
      Submitted (MAR-2005) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 255-450.
      Strain: cv. Columbia.
    6. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Root.
    7. "Phosphoproteomic analysis of nuclei-enriched fractions from Arabidopsis thaliana."
      Jones A.M.E., MacLean D., Studholme D.J., Serna-Sanz A., Andreasson E., Rathjen J.P., Peck S.C.
      J. Proteomics 72:439-451(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Strain: cv. Columbia.
    8. "Large-scale Arabidopsis phosphoproteome profiling reveals novel chloroplast kinase substrates and phosphorylation networks."
      Reiland S., Messerli G., Baerenfaller K., Gerrits B., Endler A., Grossmann J., Gruissem W., Baginsky S.
      Plant Physiol. 150:889-903(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-349, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].

    Entry informationi

    Entry nameiTBA3_ARATH
    AccessioniPrimary (citable) accession number: Q56WH1
    Secondary accession number(s): P20363
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: October 3, 2012
    Last sequence update: October 3, 2012
    Last modified: October 1, 2014
    This is version 62 of the entry and version 2 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programPlant Protein Annotation Program

    Miscellaneousi

    Miscellaneous

    There are six genes coding for alpha-tubulin. The sequences coded by genes 3 and 5 are identical.

    Keywords - Technical termi

    Complete proteome, Reference proteome

    Documents

    1. Arabidopsis thaliana
      Arabidopsis thaliana: entries and gene names
    2. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3