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P81947

- TBA1B_BOVIN

UniProt

P81947 - TBA1B_BOVIN

Protein

Tubulin alpha-1B chain

Gene
N/A
Organism
Bos taurus (Bovine)
Status
Reviewed - Annotation score: 4 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 85 (01 Oct 2014)
      Sequence version 2 (10 Feb 2009)
      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
    Sitei451 – 4511Involved in polymerizationBy similarity

    Regions

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Nucleotide bindingi142 – 1487GTPSequence Analysis

    GO - Molecular functioni

    1. double-stranded RNA binding Source: Ensembl
    2. GTPase activity Source: InterPro
    3. GTP binding Source: UniProtKB-KW
    4. structural constituent of cytoskeleton Source: Ensembl

    GO - Biological processi

    1. cellular response to interleukin-4 Source: Ensembl
    2. microtubule cytoskeleton organization Source: Ensembl
    3. protein polymerization Source: InterPro

    Keywords - Ligandi

    GTP-binding, Nucleotide-binding

    Enzyme and pathway databases

    ReactomeiREACT_214148. Formation of tubulin folding intermediates by CCT/TriC.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Tubulin alpha-1B chain
    Alternative name(s):
    Alpha-tubulin ubiquitous
    Tubulin K-alpha-1
    Tubulin alpha-ubiquitous chain
    OrganismiBos taurus (Bovine)Curated
    Taxonomic identifieri9913 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaLaurasiatheriaCetartiodactylaRuminantiaPecoraBovidaeBovinaeBos
    ProteomesiUP000009136: Chromosome 5

    Subcellular locationi

    GO - Cellular componenti

    1. cytoplasmic microtubule Source: Ensembl

    Keywords - Cellular componenti

    Cytoplasm, Cytoskeleton, Microtubule

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 451451Tubulin alpha-1B chainPRO_0000048114Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei48 – 481PhosphoserineBy similarity
    Modified residuei83 – 831Nitrated tyrosineBy similarity
    Modified residuei232 – 2321PhosphoserineBy similarity
    Modified residuei282 – 2821Nitrated tyrosineBy similarity
    Cross-linki326 – 326Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)By similarity
    Modified residuei339 – 3391Omega-N-methylarginineBy similarity
    Cross-linki370 – 370Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)By 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 By similarity.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, Isopeptide bond, Methylation, Nitration, Phosphoprotein, Ubl conjugation

    Proteomic databases

    PaxDbiP81947.
    PRIDEiP81947.

    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

    MINTiMINT-235448.

    Structurei

    Secondary structure

    1
    451
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Beta strandi4 – 96
    Helixi10 – 2819
    Beta strandi41 – 433
    Helixi48 – 514
    Beta strandi53 – 553
    Beta strandi61 – 633
    Beta strandi65 – 728
    Helixi73 – 808
    Helixi84 – 863
    Helixi89 – 913
    Beta strandi92 – 943
    Helixi103 – 1075
    Turni108 – 1103
    Helixi111 – 12616
    Beta strandi134 – 14310
    Helixi144 – 16017
    Turni161 – 1633
    Beta strandi164 – 1729
    Turni175 – 1773
    Helixi183 – 19412
    Helixi195 – 1973
    Beta strandi199 – 2057
    Helixi206 – 21611
    Helixi224 – 24320
    Beta strandi247 – 2493
    Helixi252 – 2598
    Beta strandi261 – 2644
    Beta strandi269 – 2735
    Beta strandi277 – 2793
    Helixi288 – 2936
    Helixi294 – 2963
    Helixi298 – 3003
    Beta strandi301 – 3033
    Helixi307 – 3093
    Beta strandi312 – 32211
    Helixi325 – 33612
    Beta strandi349 – 35810
    Beta strandi366 – 3683
    Beta strandi372 – 38110
    Helixi382 – 3843
    Helixi385 – 39915
    Turni400 – 4045
    Helixi405 – 4095
    Turni410 – 4123
    Helixi415 – 43622

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    3DCOelectron microscopy1.90A1-451[»]
    3EDLelectron microscopy28.00A/F1-451[»]
    3J1Telectron microscopy9.70B1-451[»]
    3J1Uelectron microscopy9.70B1-451[»]
    3J2Uelectron microscopy10.80A/C1-451[»]
    4I4TX-ray1.80A/C1-450[»]
    4I50X-ray2.30A/C1-451[»]
    4I55X-ray2.20A/C1-450[»]
    4IHJX-ray2.00A/C1-450[»]
    4IIJX-ray2.60A/C1-451[»]
    4O2AX-ray2.50A/C1-451[»]
    4O2BX-ray2.30A/C1-451[»]
    4O4HX-ray2.10A/C1-451[»]
    4O4IX-ray2.40A/C1-451[»]
    4O4JX-ray2.20A/C1-451[»]
    4O4LX-ray2.20A/C1-451[»]
    ProteinModelPortaliP81947.
    SMRiP81947. Positions 1-440.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiP81947.

    Family & Domainsi

    Sequence similaritiesi

    Belongs to the tubulin family.Curated

    Phylogenomic databases

    eggNOGiCOG5023.
    GeneTreeiENSGT00750000117333.
    HOGENOMiHOG000165711.
    HOVERGENiHBG000089.
    InParanoidiA6H700.
    KOiK07374.
    OMAiCVRARTI.
    OrthoDBiEOG7TBC1W.
    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.

    P81947-1 [UniParc]FASTAAdd to Basket

    « Hide

    MRECISIHVG QAGVQIGNAC WELYCLEHGI QPDGQMPSDK TIGGGDDSFN    50
    TFFSETGAGK HVPRAVFVDL EPTVIDEVRT GTYRQLFHPE QLITGKEDAA 100
    NNYARGHYTI GKEIIDLVLD RIRKLADQCT GLQGFLVFHS FGGGTGSGFT 150
    SLLMERLSVD YGKKSKLEFS IYPAPQVSTA VVEPYNSILT THTTLEHSDC 200
    AFMVDNEAIY DICRRNLDIE RPTYTNLNRL ISQIVSSITA SLRFDGALNV 250
    DLTEFQTNLV PYPRIHFPLA TYAPVISAEK AYHEQLSVAE ITNACFEPAN 300
    QMVKCDPRHG KYMACCLLYR GDVVPKDVNA AIATIKTKRS IQFVDWCPTG 350
    FKVGINYQPP TVVPGGDLAK VQRAVCMLSN TTAIAEAWAR LDHKFDLMYA 400
    KRAFVHWYVG EGMEEGEFSE AREDMAALEK DYEEVGVDSV EGEGEEEGEE 450
    Y 451
    Length:451
    Mass (Da):50,152
    Last modified:February 10, 2009 - v2
    Checksum:i94355B4EC2086429
    GO

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    BC146060 mRNA. Translation: AAI46061.1.
    RefSeqiNP_001108328.1. NM_001114856.1.
    UniGeneiBt.106995.
    Bt.109492.

    Genome annotation databases

    EnsembliENSBTAT00000016242; ENSBTAP00000016242; ENSBTAG00000012244.
    GeneIDi539882.
    KEGGibta:539882.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    BC146060 mRNA. Translation: AAI46061.1 .
    RefSeqi NP_001108328.1. NM_001114856.1.
    UniGenei Bt.106995.
    Bt.109492.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    3DCO electron microscopy 1.90 A 1-451 [» ]
    3EDL electron microscopy 28.00 A/F 1-451 [» ]
    3J1T electron microscopy 9.70 B 1-451 [» ]
    3J1U electron microscopy 9.70 B 1-451 [» ]
    3J2U electron microscopy 10.80 A/C 1-451 [» ]
    4I4T X-ray 1.80 A/C 1-450 [» ]
    4I50 X-ray 2.30 A/C 1-451 [» ]
    4I55 X-ray 2.20 A/C 1-450 [» ]
    4IHJ X-ray 2.00 A/C 1-450 [» ]
    4IIJ X-ray 2.60 A/C 1-451 [» ]
    4O2A X-ray 2.50 A/C 1-451 [» ]
    4O2B X-ray 2.30 A/C 1-451 [» ]
    4O4H X-ray 2.10 A/C 1-451 [» ]
    4O4I X-ray 2.40 A/C 1-451 [» ]
    4O4J X-ray 2.20 A/C 1-451 [» ]
    4O4L X-ray 2.20 A/C 1-451 [» ]
    ProteinModelPortali P81947.
    SMRi P81947. Positions 1-440.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    MINTi MINT-235448.

    Proteomic databases

    PaxDbi P81947.
    PRIDEi P81947.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENSBTAT00000016242 ; ENSBTAP00000016242 ; ENSBTAG00000012244 .
    GeneIDi 539882.
    KEGGi bta:539882.

    Organism-specific databases

    CTDi 10376.

    Phylogenomic databases

    eggNOGi COG5023.
    GeneTreei ENSGT00750000117333.
    HOGENOMi HOG000165711.
    HOVERGENi HBG000089.
    InParanoidi A6H700.
    KOi K07374.
    OMAi CVRARTI.
    OrthoDBi EOG7TBC1W.
    TreeFami TF300314.

    Enzyme and pathway databases

    Reactomei REACT_214148. Formation of tubulin folding intermediates by CCT/TriC.

    Miscellaneous databases

    EvolutionaryTracei P81947.
    NextBioi 20878279.

    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. NIH - Mammalian Gene Collection (MGC) project
      Submitted (JUN-2007) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
      Strain: Hereford.
      Tissue: Uterus.
    2. "Differential assembly kinetics of alpha-tubulin isoforms in the presence of paclitaxel."
      Banerjee A., Kasmala L.T.
      Biochem. Biophys. Res. Commun. 245:349-351(1998) [PubMed] [Europe PMC] [Abstract]
      Cited for: PROTEIN SEQUENCE OF 430-451.
      Tissue: Brain cortex.

    Entry informationi

    Entry nameiTBA1B_BOVIN
    AccessioniPrimary (citable) accession number: P81947
    Secondary accession number(s): A6H700
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: August 31, 2004
    Last sequence update: February 10, 2009
    Last modified: October 1, 2014
    This is version 85 of the entry and version 2 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programChordata Protein Annotation Program

    Miscellaneousi

    Keywords - Technical termi

    3D-structure, Complete proteome, Direct protein sequencing, Reference proteome

    Documents

    1. PDB cross-references
      Index of Protein Data Bank (PDB) cross-references
    2. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3