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P08537

- TBA_XENLA

UniProt

P08537 - TBA_XENLA

Protein

Tubulin alpha chain

Gene

tuba

Organism
Xenopus laevis (African clawed frog)
Status
Reviewed - Annotation score: 4 out of 5- Experimental evidence at transcript leveli
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    • History
      Entry version 93 (01 Oct 2014)
      Sequence version 2 (14 Nov 2006)
      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
    Sitei449 – 4491Involved 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 chain
    Gene namesi
    Name:tuba
    Synonyms:tuba1
    OrganismiXenopus laevis (African clawed frog)
    Taxonomic identifieri8355 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiAmphibiaBatrachiaAnuraPipoideaPipidaeXenopodinaeXenopusXenopus

    Organism-specific databases

    XenbaseiXB-GENE-6464328. tuba3e.

    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 – 449449Tubulin alpha chainPRO_0000048238Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei40 – 401N6-acetyllysineBy 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
    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

    Proteomic databases

    PRIDEiP08537.

    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

    IntActiP08537. 1 interaction.
    MINTiMINT-1204896.

    Structurei

    3D structure databases

    ProteinModelPortaliP08537.
    SMRiP08537. Positions 1-439.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Sequence similaritiesi

    Belongs to the tubulin family.Curated

    Phylogenomic databases

    HOVERGENiHBG000089.
    KOiK07374.

    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.

    P08537-1 [UniParc]FASTAAdd to Basket

    « Hide

    MRECISIHVG QAGVQIGNAC WELYCLEHGI QPDGQMPSDK TIGGGDDSFN    50
    TFFSETGAGK HVPRAVFVDL EPTVIDEVRT GTYRQLFHPE QLITGKEDAA 100
    NNYARGHYTI GKEIIDLVLD RIRKLADQCT GLQGFLVFHS FGGGTGSGFT 150
    SLLMERLSVD YGKKSKLEFA IYPAPQVSTA VVEPYNSILT THTTLEHSDC 200
    AFMVDNEAIY DICRRNLDIE RPTYTNLNRL ISQIVSSITA SLRFDGALNV 250
    DLTEFQTNLV PYPRIHFPLA TYAPVISAEK AYHEQLTVAD ITNACFEPAN 300
    QMVKCDPRHG KYMACCLLYR GDVVPKDVNA AIATIKTKRS IQFVDWCPTG 350
    FKVGINYQPP TVVPGGDLAK VQRAVCMLSN TTAIAEAWAR LDHKFDLMYA 400
    KRAFVHWYVG EGMEEGEFSE AREDMAALEK DYEEVGADSA DAEDEGEEY 449
    Length:449
    Mass (Da):49,879
    Last modified:November 14, 2006 - v2
    Checksum:i9A5B8497FA27FF8C
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti154 – 1541M → L in CAA30094. (PubMed:3342025)Curated

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    X07046 mRNA. Translation: CAA30094.1.
    X07045 Genomic DNA. Translation: CAA30093.1.
    BC097546 mRNA. Translation: AAH97546.1.
    BC106207 mRNA. Translation: AAI06208.1.
    PIRiS00253.
    RefSeqiNP_001095253.1. NM_001101783.1.
    NP_001165669.1. NM_001172198.1.
    UniGeneiXl.13561.
    Xl.66058.

    Genome annotation databases

    GeneIDi100337592.
    399313.
    KEGGixla:100337592.
    xla:399313.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    X07046 mRNA. Translation: CAA30094.1 .
    X07045 Genomic DNA. Translation: CAA30093.1 .
    BC097546 mRNA. Translation: AAH97546.1 .
    BC106207 mRNA. Translation: AAI06208.1 .
    PIRi S00253.
    RefSeqi NP_001095253.1. NM_001101783.1.
    NP_001165669.1. NM_001172198.1.
    UniGenei Xl.13561.
    Xl.66058.

    3D structure databases

    ProteinModelPortali P08537.
    SMRi P08537. Positions 1-439.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    IntActi P08537. 1 interaction.
    MINTi MINT-1204896.

    Proteomic databases

    PRIDEi P08537.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    GeneIDi 100337592.
    399313.
    KEGGi xla:100337592.
    xla:399313.

    Organism-specific databases

    CTDi 10376.
    112714.
    Xenbasei XB-GENE-6464328. tuba3e.

    Phylogenomic databases

    HOVERGENi HBG000089.
    KOi K07374.

    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. "The complete sequence of a frog alpha-tubulin gene and its regulated expression in mouse L-cells."
      Smith D.J.
      Biochem. J. 249:465-472(1988) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA].
    2. NIH - Xenopus Gene Collection (XGC) project
      Submitted (OCT-2005) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
      Tissue: Embryo.

    Entry informationi

    Entry nameiTBA_XENLA
    AccessioniPrimary (citable) accession number: P08537
    Secondary accession number(s): Q4V850
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: August 1, 1988
    Last sequence update: November 14, 2006
    Last modified: October 1, 2014
    This is version 93 of the entry and version 2 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programChordata Protein Annotation Program

    Miscellaneousi

    Documents

    1. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3