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Q6B856

- TBB2B_BOVIN

UniProt

Q6B856 - TBB2B_BOVIN

Protein

Tubulin beta-2B chain

Gene

TUBB2B

Organism
Bos taurus (Bovine)
Status
Reviewed - Annotation score: 3 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 89 (01 Oct 2014)
      Sequence version 2 (28 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 By similarity.By similarity

    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. neuron migration Source: Ensembl
    3. protein polymerization Source: InterPro

    Keywords - Ligandi

    GTP-binding, Nucleotide-binding

    Enzyme and pathway databases

    ReactomeiREACT_209545. Resolution of Sister Chromatid Cohesion.
    REACT_211133. MHC class II antigen presentation.
    REACT_212887. Separation of Sister Chromatids.
    REACT_214148. Formation of tubulin folding intermediates by CCT/TriC.
    REACT_215331. Recruitment of NuMA to mitotic centrosomes.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Tubulin beta-2B chain
    Gene namesi
    Name:TUBB2B
    OrganismiBos taurus (Bovine)
    Taxonomic identifieri9913 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaLaurasiatheriaCetartiodactylaRuminantiaPecoraBovidaeBovinaeBos
    ProteomesiUP000009136: Chromosome 23

    Subcellular locationi

    Cytoplasmcytoskeleton By similarity

    GO - Cellular componenti

    1. cytoplasm Source: UniProtKB-KW
    2. microtubule Source: UniProtKB-KW
    3. plasma membrane Source: Ensembl

    Keywords - Cellular componenti

    Cytoplasm, Cytoskeleton, Microtubule

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 445445Tubulin beta-2B chainPRO_0000262654Add
    BLAST

    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 By similarity.By similarity

    Proteomic databases

    PaxDbiQ6B856.
    PRIDEiQ6B856.

    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

    BioGridi158875. 1 interaction.
    IntActiQ6B856. 6 interactions.
    MINTiMINT-6604256.

    Structurei

    Secondary structure

    1
    445
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Beta strandi4 – 96
    Helixi10 – 2718
    Beta strandi34 – 363
    Beta strandi39 – 413
    Helixi42 – 454
    Helixi47 – 493
    Beta strandi51 – 544
    Turni55 – 573
    Beta strandi58 – 614
    Beta strandi63 – 708
    Helixi71 – 788
    Helixi82 – 843
    Helixi87 – 893
    Beta strandi90 – 923
    Helixi101 – 1055
    Helixi108 – 12518
    Beta strandi132 – 14211
    Helixi143 – 15816
    Beta strandi162 – 1709
    Helixi173 – 1753
    Helixi181 – 19515
    Beta strandi197 – 2037
    Helixi204 – 21310
    Helixi222 – 23615
    Helixi238 – 2414
    Beta strandi245 – 2473
    Helixi250 – 2578
    Beta strandi265 – 2717
    Beta strandi276 – 2783
    Beta strandi280 – 2823
    Helixi286 – 2938
    Helixi296 – 2983
    Beta strandi299 – 3024
    Helixi305 – 3073
    Beta strandi310 – 32011
    Helixi323 – 33614
    Helixi338 – 3403
    Beta strandi343 – 3453
    Beta strandi349 – 3557
    Beta strandi362 – 37110
    Helixi372 – 3743
    Helixi375 – 38915
    Turni390 – 3956
    Helixi396 – 3994
    Turni400 – 4023
    Helixi405 – 42622

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    1SA0X-ray3.58B/D1-439[»]
    1SA1X-ray4.20B/D1-439[»]
    1TVKX-ray2.89B1-427[»]
    1Z2BX-ray4.10B/D1-445[»]
    2P4Nelectron microscopy9.00B1-445[»]
    2WBEelectron microscopy9.40B1-445[»]
    2XRPelectron microscopy8.20A/C/E/G1-445[»]
    3DCOelectron microscopy1.90B1-445[»]
    3DU7X-ray4.10B/D1-445[»]
    3E22X-ray3.80B/D1-445[»]
    3IZ0electron microscopy8.60B1-445[»]
    3J1Telectron microscopy9.70C1-427[»]
    3J1Uelectron microscopy9.70C1-427[»]
    3J2Uelectron microscopy10.80B/D1-445[»]
    4AQVelectron microscopy9.70B1-445[»]
    4AQWelectron microscopy9.50B1-445[»]
    4ATUelectron microscopy8.30A/C/E/G1-445[»]
    4ATXelectron microscopy8.20A1-445[»]
    4CK5electron microscopy10.00B1-445[»]
    4CK6electron microscopy9.20B1-445[»]
    4CK7electron microscopy9.20B1-445[»]
    4I4TX-ray1.80B/D1-445[»]
    4I50X-ray2.30B/D1-445[»]
    4I55X-ray2.20B/D1-445[»]
    4IHJX-ray2.00B/D1-445[»]
    4IIJX-ray2.60B/D1-445[»]
    4O2AX-ray2.50B/D1-445[»]
    4O2BX-ray2.30B/D1-445[»]
    4O4HX-ray2.10B/D1-445[»]
    4O4IX-ray2.40B/D1-445[»]
    4O4JX-ray2.20B/D1-445[»]
    4O4LX-ray2.20B/D1-445[»]
    ProteinModelPortaliQ6B856.
    SMRiQ6B856. Positions 1-431.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiQ6B856.

    Family & Domainsi

    Sequence similaritiesi

    Belongs to the tubulin family.Curated

    Phylogenomic databases

    eggNOGiCOG5023.
    GeneTreeiENSGT00740000115320.
    HOGENOMiHOG000165710.
    HOVERGENiHBG000089.
    KOiK07375.
    OMAiYQQEEEY.
    OrthoDBiEOG71ZP1H.
    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.

    Q6B856-1 [UniParc]FASTAAdd to Basket

    « Hide

    MREIVHIQAG QCGNQIGAKF WEVISDEHGI DPTGSYHGDS DLQLERINVY    50
    YNEATGNKYV PRAILVDLEP GTMDSVRSGP FGQIFRPDNF VFGQSGAGNN 100
    WAKGHYTEGA ELVDSVLDVV RKESESCDCL QGFQLTHSLG GGTGSGMGTL 150
    LISKIREEYP DRIMNTFSVM PSPKVSDTVV EPYNATLSVH QLVENTDETY 200
    CIDNEALYDI CFRTLKLTTP TYGDLNHLVS ATMSGVTTCL RFPGQLNADL 250
    RKLAVNMVPF PRLHFFMPGF APLTSRGSQQ YRALTVPELT QQMFDSKNMM 300
    AACDPRHGRY LTVAAIFRGR MSMKEVDEQM LNVQNKNSSY FVEWIPNNVK 350
    TAVCDIPPRG LKMSATFIGN STAIQELFKR ISEQFTAMFR RKAFLHWYTG 400
    EGMDEMEFTE AESNMNDLVS EYQQYQDATA DEQGEFEEEE GEDEA 445
    Length:445
    Mass (Da):49,953
    Last modified:November 28, 2006 - v2
    Checksum:i4DC3956EFF880746
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti201 – 2011C → S in AAT84374. 1 PublicationCurated

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AY675081 mRNA. Translation: AAT84374.1.
    RefSeqiNP_001003900.1. NM_001003900.1.
    UniGeneiBt.105119.

    Genome annotation databases

    EnsembliENSBTAT00000005346; ENSBTAP00000005346; ENSBTAG00000004093.
    GeneIDi281555.
    KEGGibta:281555.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AY675081 mRNA. Translation: AAT84374.1 .
    RefSeqi NP_001003900.1. NM_001003900.1.
    UniGenei Bt.105119.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    1SA0 X-ray 3.58 B/D 1-439 [» ]
    1SA1 X-ray 4.20 B/D 1-439 [» ]
    1TVK X-ray 2.89 B 1-427 [» ]
    1Z2B X-ray 4.10 B/D 1-445 [» ]
    2P4N electron microscopy 9.00 B 1-445 [» ]
    2WBE electron microscopy 9.40 B 1-445 [» ]
    2XRP electron microscopy 8.20 A/C/E/G 1-445 [» ]
    3DCO electron microscopy 1.90 B 1-445 [» ]
    3DU7 X-ray 4.10 B/D 1-445 [» ]
    3E22 X-ray 3.80 B/D 1-445 [» ]
    3IZ0 electron microscopy 8.60 B 1-445 [» ]
    3J1T electron microscopy 9.70 C 1-427 [» ]
    3J1U electron microscopy 9.70 C 1-427 [» ]
    3J2U electron microscopy 10.80 B/D 1-445 [» ]
    4AQV electron microscopy 9.70 B 1-445 [» ]
    4AQW electron microscopy 9.50 B 1-445 [» ]
    4ATU electron microscopy 8.30 A/C/E/G 1-445 [» ]
    4ATX electron microscopy 8.20 A 1-445 [» ]
    4CK5 electron microscopy 10.00 B 1-445 [» ]
    4CK6 electron microscopy 9.20 B 1-445 [» ]
    4CK7 electron microscopy 9.20 B 1-445 [» ]
    4I4T X-ray 1.80 B/D 1-445 [» ]
    4I50 X-ray 2.30 B/D 1-445 [» ]
    4I55 X-ray 2.20 B/D 1-445 [» ]
    4IHJ X-ray 2.00 B/D 1-445 [» ]
    4IIJ X-ray 2.60 B/D 1-445 [» ]
    4O2A X-ray 2.50 B/D 1-445 [» ]
    4O2B X-ray 2.30 B/D 1-445 [» ]
    4O4H X-ray 2.10 B/D 1-445 [» ]
    4O4I X-ray 2.40 B/D 1-445 [» ]
    4O4J X-ray 2.20 B/D 1-445 [» ]
    4O4L X-ray 2.20 B/D 1-445 [» ]
    ProteinModelPortali Q6B856.
    SMRi Q6B856. Positions 1-431.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 158875. 1 interaction.
    IntActi Q6B856. 6 interactions.
    MINTi MINT-6604256.

    Chemistry

    BindingDBi Q6B856.
    ChEMBLi CHEMBL3394.

    Proteomic databases

    PaxDbi Q6B856.
    PRIDEi Q6B856.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENSBTAT00000005346 ; ENSBTAP00000005346 ; ENSBTAG00000004093 .
    GeneIDi 281555.
    KEGGi bta:281555.

    Organism-specific databases

    CTDi 347733.

    Phylogenomic databases

    eggNOGi COG5023.
    GeneTreei ENSGT00740000115320.
    HOGENOMi HOG000165710.
    HOVERGENi HBG000089.
    KOi K07375.
    OMAi YQQEEEY.
    OrthoDBi EOG71ZP1H.
    TreeFami TF300298.

    Enzyme and pathway databases

    Reactomei REACT_209545. Resolution of Sister Chromatid Cohesion.
    REACT_211133. MHC class II antigen presentation.
    REACT_212887. Separation of Sister Chromatids.
    REACT_214148. Formation of tubulin folding intermediates by CCT/TriC.
    REACT_215331. Recruitment of NuMA to mitotic centrosomes.

    Miscellaneous databases

    EvolutionaryTracei Q6B856.
    NextBioi 20805506.

    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. "Differentially expressed genes in bovine 8-cell embryo."
      Hwang K.C., Park S.Y., Cui X.S., Kim N.H.
      Submitted (JUL-2004) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [MRNA].
    2. "The genome sequence of taurine cattle: a window to ruminant biology and evolution."
      The bovine genome sequencing and analysis consortium
      Science 324:522-528(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
      Strain: Hereford.

    Entry informationi

    Entry nameiTBB2B_BOVIN
    AccessioniPrimary (citable) accession number: Q6B856
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: November 28, 2006
    Last sequence update: November 28, 2006
    Last modified: October 1, 2014
    This is version 89 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, 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