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P02554

- TBB_PIG

UniProt

P02554 - TBB_PIG

Protein

Tubulin beta chain

Gene
N/A
Organism
Sus scrofa (Pig)
Status
Reviewed - Annotation score: 4 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 117 (01 Oct 2014)
      Sequence version 1 (21 Jul 1986)
      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.

    Regions

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Nucleotide bindingi140 – 1467GTPSequence Analysis

    GO - Molecular functioni

    1. GTPase activity Source: InterPro
    2. GTP binding Source: UniProtKB-KW
    3. protein binding Source: UniProtKB
    4. 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 beta chain
    Alternative name(s):
    Beta-tubulin
    OrganismiSus scrofa (Pig)
    Taxonomic identifieri9823 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaLaurasiatheriaCetartiodactylaSuinaSuidaeSus
    ProteomesiUP000008227: Unplaced

    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 – 445445Tubulin beta chainPRO_0000048261Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei172 – 1721Phosphoserine; by CDK1By similarity

    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

    Keywords - PTMi

    Phosphoprotein

    Proteomic databases

    PaxDbiP02554.
    PRIDEiP02554.

    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

    IntActiP02554. 2 interactions.
    STRINGi9823.ENSSSCP00000001076.

    Structurei

    Secondary structure

    1
    445
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Beta strandi3 – 64
    Helixi10 – 2011
    Turni21 – 255
    Helixi26 – 283
    Beta strandi32 – 343
    Beta strandi39 – 424
    Helixi47 – 493
    Beta strandi53 – 553
    Turni70 – 723
    Helixi73 – 775
    Turni81 – 844
    Helixi101 – 1044
    Turni105 – 1128
    Helixi116 – 1249
    Beta strandi126 – 1283
    Beta strandi130 – 1345
    Beta strandi136 – 1427
    Turni143 – 1453
    Helixi146 – 15510
    Turni156 – 1583
    Beta strandi160 – 1645
    Beta strandi167 – 1704
    Beta strandi177 – 1804
    Helixi181 – 19212
    Turni193 – 1953
    Helixi206 – 2127
    Helixi222 – 23615
    Helixi238 – 2403
    Helixi250 – 2578
    Turni276 – 2783
    Helixi289 – 2935
    Beta strandi295 – 3039
    Helixi305 – 3073
    Beta strandi316 – 3205
    Helixi323 – 33513
    Helixi338 – 3403
    Beta strandi343 – 3453
    Beta strandi352 – 3565
    Beta strandi364 – 3685
    Turni372 – 3765
    Helixi377 – 38913
    Turni390 – 3945
    Helixi395 – 3995
    Helixi407 – 42317

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    1FFXX-ray3.95B/D1-445[»]
    1IA0electron microscopy15.00B1-445[»]
    1JFFX-ray3.50B1-445[»]
    1TUBX-ray3.70B1-427[»]
    2HXFelectron microscopy10.00B1-435[»]
    2HXHelectron microscopy11.00B1-435[»]
    3J6Eelectron microscopy4.70B/D/F/H/J/L/N/P/R1-427[»]
    3J6Felectron microscopy4.90B/D/F/H/J/L/N/P/R1-427[»]
    3J6Gelectron microscopy5.50B/D/F/H/J/L/N/P/R1-427[»]
    4ABOelectron microscopy8.60A/C/E/G1-445[»]
    ProteinModelPortaliP02554.
    SMRiP02554. Positions 1-427.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiP02554.

    Family & Domainsi

    Sequence similaritiesi

    Belongs to the tubulin family.Curated

    Phylogenomic databases

    eggNOGiCOG5023.
    HOGENOMiHOG000165710.
    HOVERGENiHBG000089.

    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.

    P02554-1 [UniParc]FASTAAdd to Basket

    « Hide

    MREIVHIQAG QCGNQIGAKF WEVISDEHGI DPTGSYHGDS DLQLERINVY    50
    YNEAAGNKYV PRAILVDLEP GTMDSVRSGP FGQIFRPDNF VFGQSGAGNN 100
    WAKGHYTEGA ELVDSVLDVV RKESESCDCL QGFQLTHSLG GGTGSGMGTL 150
    LISKIREEYP DRIMNTFSVV PSPKVSDTVV EPYNATLSVH QLVENTDETY 200
    CIDNEALYDI CFRTLKLTTP TYGDLNHLVS ATMSGVTTCL RFPGQLNADL 250
    RKLAVNMVPF PRLHFFMPGF APLTSRGSQQ YRALTVPELT QQMFDAKNMM 300
    AACDPRHGRY LTVAAVFRGR MSMKEVDEQM LNVQNKNSSY FVEWIPNNVK 350
    TAVCDIPPRG LKMSATFIGN STAIQELFKR ISEQFTAMFR RKAFLHWYTG 400
    EGMDEMEFTE AESNMNDLVS EYQQYQDATA DEQGEFEEEG EEDEA 445
    Length:445
    Mass (Da):49,861
    Last modified:July 21, 1986 - v1
    Checksum:iEF71423B12C5E1B2
    GO

    Natural variant

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti37 – 371H → V in 2nd form.
    Natural varianti48 – 481N → S in 2nd form.
    Natural varianti55 – 573AGN → SSH in 2nd form.
    Natural varianti275 – 2751S → A in 2nd form.

    Sequence databases

    PIRiA02973. UBPGB.

    Cross-referencesi

    Sequence databases

    PIRi A02973. UBPGB.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    1FFX X-ray 3.95 B/D 1-445 [» ]
    1IA0 electron microscopy 15.00 B 1-445 [» ]
    1JFF X-ray 3.50 B 1-445 [» ]
    1TUB X-ray 3.70 B 1-427 [» ]
    2HXF electron microscopy 10.00 B 1-435 [» ]
    2HXH electron microscopy 11.00 B 1-435 [» ]
    3J6E electron microscopy 4.70 B/D/F/H/J/L/N/P/R 1-427 [» ]
    3J6F electron microscopy 4.90 B/D/F/H/J/L/N/P/R 1-427 [» ]
    3J6G electron microscopy 5.50 B/D/F/H/J/L/N/P/R 1-427 [» ]
    4ABO electron microscopy 8.60 A/C/E/G 1-445 [» ]
    ProteinModelPortali P02554.
    SMRi P02554. Positions 1-427.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    IntActi P02554. 2 interactions.
    STRINGi 9823.ENSSSCP00000001076.

    Chemistry

    BindingDBi P02554.
    ChEMBLi CHEMBL2111354.

    Proteomic databases

    PaxDbi P02554.
    PRIDEi P02554.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Phylogenomic databases

    eggNOGi COG5023.
    HOGENOMi HOG000165710.
    HOVERGENi HBG000089.

    Miscellaneous databases

    EvolutionaryTracei P02554.

    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. Cited for: PROTEIN SEQUENCE.
      Tissue: Brain.
    2. "The GTP-binding peptide of beta-tubulin. Localization by direct photoaffinity labeling and comparison with nucleotide-binding proteins."
      Linse K., Mandelkow E.M.
      J. Biol. Chem. 263:15205-15210(1988) [PubMed] [Europe PMC] [Abstract]
      Cited for: PROTEIN SEQUENCE OF 63-77.
    3. "Localization of the ATP binding site on alpha-tubulin."
      Zabrecky J.R., Cole R.D.
      Arch. Biochem. Biophys. 225:475-481(1983) [PubMed] [Europe PMC] [Abstract]
      Cited for: GUANINE NUCLEOTIDE-BINDING SITES.
    4. Cited for: X-RAY CRYSTALLOGRAPHY (3.95 ANGSTROMS).
    5. "Structure of the alpha beta tubulin dimer by electron crystallography."
      Nogales E., Wolf S.G., Downing K.H.
      Nature 391:199-203(1998) [PubMed] [Europe PMC] [Abstract]
      Cited for: STRUCTURE BY ELECTRON MICROSCOPY (3.7 ANGSTROMS) OF 1-427.
    6. "15 A resolution model of the monomeric kinesin motor, KIF1A."
      Kikkawa M., Okada Y., Hirokawa N.
      Cell 100:241-252(2000) [PubMed] [Europe PMC] [Abstract]
      Cited for: STRUCTURE BY ELECTRON MICROSCOPY (15.0 ANGSTROMS).
    7. "Refined structure of alpha beta-tubulin at 3.5 A resolution."
      Loewe J., Li H., Downing K.H., Nogales E.
      J. Mol. Biol. 313:1045-1057(2001) [PubMed] [Europe PMC] [Abstract]
      Cited for: STRUCTURE BY ELECTRON MICROSCOPY (3.5 ANGSTROMS).

    Entry informationi

    Entry nameiTBB_PIG
    AccessioniPrimary (citable) accession number: P02554
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: July 21, 1986
    Last sequence update: July 21, 1986
    Last modified: October 1, 2014
    This is version 117 of the entry and version 1 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programChordata Protein Annotation Program

    Miscellaneousi

    Miscellaneous

    The highly acidic C-terminal region may bind cations such as calcium.
    Pig brain contains at least two forms of this protein.

    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