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P68363

- TBA1B_HUMAN

UniProt

P68363 - TBA1B_HUMAN

Protein

Tubulin alpha-1B chain

Gene

TUBA1B

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 115 (01 Oct 2014)
      Sequence version 1 (13 Aug 1987)
      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 polymerization

    Regions

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

    GO - Molecular functioni

    1. double-stranded RNA binding Source: MGI
    2. GTPase activity Source: InterPro
    3. GTP binding Source: UniProtKB-KW
    4. protein binding Source: UniProtKB
    5. structural constituent of cytoskeleton Source: Ensembl
    6. structural molecule activity Source: BHF-UCL

    GO - Biological processi

    1. 'de novo' posttranslational protein folding Source: Reactome
    2. cell division Source: BHF-UCL
    3. cellular protein metabolic process Source: Reactome
    4. cellular response to interleukin-4 Source: Ensembl
    5. cytoskeleton-dependent intracellular transport Source: BHF-UCL
    6. microtubule-based process Source: BHF-UCL
    7. microtubule cytoskeleton organization Source: Ensembl
    8. protein folding Source: Reactome
    9. protein polymerization Source: InterPro

    Keywords - Ligandi

    GTP-binding, Nucleotide-binding

    Enzyme and pathway databases

    ReactomeiREACT_11039. Microtubule-dependent trafficking of connexons from Golgi to the plasma membrane.
    REACT_121399. MHC class II antigen presentation.
    REACT_147867. Translocation of GLUT4 to the plasma membrane.
    REACT_150425. Resolution of Sister Chromatid Cohesion.
    REACT_150471. Separation of Sister Chromatids.
    REACT_15510. Recruitment of NuMA to mitotic centrosomes.
    REACT_16956. Formation of tubulin folding intermediates by CCT/TriC.
    REACT_16967. Post-chaperonin tubulin folding pathway.
    REACT_22365. Recycling pathway of L1.
    REACT_25201. Kinesins.
    REACT_682. Mitotic Prometaphase.
    REACT_9509. Gap junction assembly.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Tubulin alpha-1B chain
    Alternative name(s):
    Alpha-tubulin ubiquitous
    Tubulin K-alpha-1
    Tubulin alpha-ubiquitous chain
    Gene namesi
    Name:TUBA1B
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 12

    Organism-specific databases

    HGNCiHGNC:18809. TUBA1B.

    Subcellular locationi

    GO - Cellular componenti

    1. cytoplasm Source: UniProtKB-KW
    2. cytoplasmic microtubule Source: Ensembl
    3. extracellular vesicular exosome Source: UniProt
    4. microtubule Source: UniProtKB

    Keywords - Cellular componenti

    Cytoplasm, Cytoskeleton, Microtubule

    Pathology & Biotechi

    Organism-specific databases

    PharmGKBiPA162407332.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 451451Tubulin alpha-1B chainPRO_0000048108Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei48 – 481Phosphoserine1 Publication
    Modified residuei83 – 831Nitrated tyrosineBy similarity
    Modified residuei232 – 2321Phosphoserine1 Publication
    Modified residuei282 – 2821Nitrated tyrosineBy similarity
    Cross-linki326 – 326Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)
    Modified residuei339 – 3391Omega-N-methylarginine1 Publication
    Cross-linki370 – 370Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)
    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 polyglutamylated. This modification occurs exclusively on glutamate residues and results in polyglutamate chains on the gamma-carboxyl group. Also monoglycylated but not polyglycylated due to the absence of functional TTLL10 in human. Monoglycylation 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 glycylation levels increases polyglutamylation, and reciprocally. The precise function of such modifications is still unclear but they regulate the assembly and dynamics of axonemal microtubules Probable.Curated
    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

    MaxQBiP68363.
    PaxDbiP68363.
    PRIDEiP68363.

    2D gel databases

    OGPiP68363.
    SWISS-2DPAGEP68363.

    PTM databases

    PhosphoSiteiP68363.

    Expressioni

    Gene expression databases

    ArrayExpressiP68363.
    BgeeiP68363.
    CleanExiHS_TUBA1B.
    GenevestigatoriP68363.

    Organism-specific databases

    HPAiCAB011513.
    HPA039247.
    HPA043684.

    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.1 Publication

    Binary interactionsi

    WithEntry#Exp.IntActNotes
    EBNA-LPQ8AZK73EBI-487083,EBI-1185167From a different organism.
    TUBB3Q135093EBI-487083,EBI-350989

    Protein-protein interaction databases

    BioGridi115651. 76 interactions.
    IntActiP68363. 23 interactions.
    MINTiMINT-4998849.
    STRINGi9606.ENSP00000336799.

    Structurei

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    2E4HNMR-B416-451[»]
    ProteinModelPortaliP68363.
    SMRiP68363. Positions 1-440.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiP68363.

    Family & Domainsi

    Sequence similaritiesi

    Belongs to the tubulin family.Curated

    Phylogenomic databases

    eggNOGiCOG5023.
    HOGENOMiHOG000165711.
    HOVERGENiHBG000089.
    InParanoidiP68363.
    KOiK07374.
    OMAiCVRARTI.
    OrthoDBiEOG7TBC1W.
    PhylomeDBiP68363.
    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]

    Sequences (2)i

    Sequence statusi: Complete.

    This entry describes 2 isoformsi produced by alternative splicing. Align

    Isoform 1 (identifier: P68363-1) [UniParc]FASTAAdd to Basket

    This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

    « 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:August 13, 1987 - v1
    Checksum:i94355B4EC2086429
    GO
    Isoform 2 (identifier: P68363-2) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         108-223: Missing.

    Note: No experimental confirmation available.

    Show »
    Length:335
    Mass (Da):37,218
    Checksum:iCEC8DAFE68516D27
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti131 – 1311G → R in AAA91576. (PubMed:6646120)Curated
    Sequence conflicti290 – 2901E → D in AAA91576. (PubMed:6646120)Curated
    Sequence conflicti308 – 3081R → G in AAA91576. (PubMed:6646120)Curated
    Sequence conflicti340 – 3401S → T in AAA91576. (PubMed:6646120)Curated

    Alternative sequence

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Alternative sequencei108 – 223116Missing in isoform 2. 1 PublicationVSP_055764Add
    BLAST

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    K00558 mRNA. Translation: AAA91576.1.
    AF081484 mRNA. Translation: AAC31959.1.
    DQ400107 mRNA. Translation: ABD60581.1.
    BC000696 mRNA. Translation: AAH00696.1.
    BC001128 mRNA. Translation: AAH01128.1.
    BC006379 mRNA. Translation: AAH06379.1.
    BC006481 mRNA. Translation: AAH06481.1.
    BC008659 mRNA. Translation: AAH08659.1.
    BC009314 mRNA. Translation: AAH09314.1.
    BC009509 mRNA. Translation: AAH09509.1.
    BC009512 mRNA. Translation: AAH09512.1.
    BC009513 mRNA. Translation: AAH09513.1.
    BC010494 mRNA. Translation: AAH10494.1.
    BC011572 mRNA. Translation: AAH11572.1.
    BC015883 mRNA. Translation: AAH15883.1.
    BC017004 mRNA. Translation: AAH17004.1.
    BC021564 mRNA. Translation: AAH21564.1.
    BC030820 mRNA. Translation: AAH30820.1.
    BC071904 mRNA. Translation: AAH71904.1.
    CCDSiCCDS31792.1.
    PIRiI77403.
    RefSeqiNP_006073.2. NM_006082.2.
    UniGeneiHs.524390.

    Genome annotation databases

    GeneIDi10376.
    KEGGihsa:10376.
    UCSCiuc001rtl.3. human.

    Polymorphism databases

    DMDMi55977474.

    Keywords - Coding sequence diversityi

    Alternative splicing

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    K00558 mRNA. Translation: AAA91576.1 .
    AF081484 mRNA. Translation: AAC31959.1 .
    DQ400107 mRNA. Translation: ABD60581.1 .
    BC000696 mRNA. Translation: AAH00696.1 .
    BC001128 mRNA. Translation: AAH01128.1 .
    BC006379 mRNA. Translation: AAH06379.1 .
    BC006481 mRNA. Translation: AAH06481.1 .
    BC008659 mRNA. Translation: AAH08659.1 .
    BC009314 mRNA. Translation: AAH09314.1 .
    BC009509 mRNA. Translation: AAH09509.1 .
    BC009512 mRNA. Translation: AAH09512.1 .
    BC009513 mRNA. Translation: AAH09513.1 .
    BC010494 mRNA. Translation: AAH10494.1 .
    BC011572 mRNA. Translation: AAH11572.1 .
    BC015883 mRNA. Translation: AAH15883.1 .
    BC017004 mRNA. Translation: AAH17004.1 .
    BC021564 mRNA. Translation: AAH21564.1 .
    BC030820 mRNA. Translation: AAH30820.1 .
    BC071904 mRNA. Translation: AAH71904.1 .
    CCDSi CCDS31792.1.
    PIRi I77403.
    RefSeqi NP_006073.2. NM_006082.2.
    UniGenei Hs.524390.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    2E4H NMR - B 416-451 [» ]
    ProteinModelPortali P68363.
    SMRi P68363. Positions 1-440.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 115651. 76 interactions.
    IntActi P68363. 23 interactions.
    MINTi MINT-4998849.
    STRINGi 9606.ENSP00000336799.

    Chemistry

    ChEMBLi CHEMBL2095182.

    PTM databases

    PhosphoSitei P68363.

    Polymorphism databases

    DMDMi 55977474.

    2D gel databases

    OGPi P68363.
    SWISS-2DPAGE P68363.

    Proteomic databases

    MaxQBi P68363.
    PaxDbi P68363.
    PRIDEi P68363.

    Protocols and materials databases

    DNASUi 10376.
    Structural Biology Knowledgebase Search...

    Genome annotation databases

    GeneIDi 10376.
    KEGGi hsa:10376.
    UCSCi uc001rtl.3. human.

    Organism-specific databases

    CTDi 10376.
    GeneCardsi GC12M049523.
    H-InvDB HIX0079488.
    HGNCi HGNC:18809. TUBA1B.
    HPAi CAB011513.
    HPA039247.
    HPA043684.
    MIMi 602530. gene.
    neXtProti NX_P68363.
    PharmGKBi PA162407332.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi COG5023.
    HOGENOMi HOG000165711.
    HOVERGENi HBG000089.
    InParanoidi P68363.
    KOi K07374.
    OMAi CVRARTI.
    OrthoDBi EOG7TBC1W.
    PhylomeDBi P68363.
    TreeFami TF300314.

    Enzyme and pathway databases

    Reactomei REACT_11039. Microtubule-dependent trafficking of connexons from Golgi to the plasma membrane.
    REACT_121399. MHC class II antigen presentation.
    REACT_147867. Translocation of GLUT4 to the plasma membrane.
    REACT_150425. Resolution of Sister Chromatid Cohesion.
    REACT_150471. Separation of Sister Chromatids.
    REACT_15510. Recruitment of NuMA to mitotic centrosomes.
    REACT_16956. Formation of tubulin folding intermediates by CCT/TriC.
    REACT_16967. Post-chaperonin tubulin folding pathway.
    REACT_22365. Recycling pathway of L1.
    REACT_25201. Kinesins.
    REACT_682. Mitotic Prometaphase.
    REACT_9509. Gap junction assembly.

    Miscellaneous databases

    ChiTaRSi TUBA1B. human.
    EvolutionaryTracei P68363.
    GeneWikii TUBA1B.
    GenomeRNAii 10376.
    NextBioi 39315.
    PROi P68363.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi P68363.
    Bgeei P68363.
    CleanExi HS_TUBA1B.
    Genevestigatori P68363.

    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. "Expression of human alpha-tubulin genes: interspecies conservation of 3' untranslated regions."
      Cowan N.J., Dobner P., Fuchs E.V., Cleveland D.W.
      Mol. Cell. Biol. 3:1738-1745(1983) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
      Tissue: Keratinocyte.
    2. de Hostos E.L.
      Submitted (JUL-1998) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
    3. "Gene response of gangliocytes stimulated by Herpes simplex virus type 1."
      Li Q., Liu L., Ma S.
      Submitted (FEB-2006) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
    4. "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
      The MGC Project Team
      Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
      Tissue: Brain, Colon, Eye, Kidney, Lung, Muscle, Placenta, Prostate, Skin and Uterus.
    5. Lubec G., Afjehi-Sadat L., Vishwanath V., Chen W.-Q., Sun Y.
      Submitted (DEC-2008) to UniProtKB
      Cited for: PROTEIN SEQUENCE OF 41-60; 65-79; 113-121; 230-280; 312-320; 327-336; 340-370; 374-390; 395-401 AND 403-422, IDENTIFICATION BY MASS SPECTROMETRY.
      Tissue: Brain, Cajal-Retzius cell and Fetal brain cortex.
    6. Bienvenut W.V., Waridel P., Quadroni M.
      Submitted (MAR-2009) to UniProtKB
      Cited for: PROTEIN SEQUENCE OF 41-79; 65-79; 85-121; 125-164; 216-304; 312-370 AND 374-451, PHOSPHORYLATION AT SER-48 AND SER-232, METHYLATION AT ARG-339, IDENTIFICATION BY MASS SPECTROMETRY.
      Tissue: Embryonic kidney.
    7. "C-terminal fragments of alpha- and beta-tubulin form amyloid fibrils in vitro and associate with amyloid deposits of familial cerebral amyloid angiopathy, British type."
      Baumann M.H., Wisniewski T., Levy E., Plant G.T., Ghiso J.
      Biochem. Biophys. Res. Commun. 219:238-242(1996) [PubMed] [Europe PMC] [Abstract]
      Cited for: PROTEIN SEQUENCE OF 353-370 AND 395-401.
      Tissue: Brain.
    8. "Evolutionary divergence of enzymatic mechanisms for posttranslational polyglycylation."
      Rogowski K., Juge F., van Dijk J., Wloga D., Strub J.-M., Levilliers N., Thomas D., Bre M.-H., Van Dorsselaer A., Gaertig J., Janke C.
      Cell 137:1076-1087(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: GLYCYLATION.
    9. "Structural basis for tubulin recognition by cytoplasmic linker protein 170 and its autoinhibition."
      Mishima M., Maesaki R., Kasa M., Watanabe T., Fukata M., Kaibuchi K., Hakoshima T.
      Proc. Natl. Acad. Sci. U.S.A. 104:10346-10351(2007) [PubMed] [Europe PMC] [Abstract]
      Cited for: STRUCTURE BY NMR OF 416-451 IN COMPLEX WITH CLIP1.

    Entry informationi

    Entry nameiTBA1B_HUMAN
    AccessioniPrimary (citable) accession number: P68363
    Secondary accession number(s): P04687
    , P05209, Q27I68, Q8WU19
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: August 13, 1987
    Last sequence update: August 13, 1987
    Last modified: October 1, 2014
    This is version 115 of the entry and version 1 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programChordata Protein Annotation Program
    DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

    Miscellaneousi

    Keywords - Technical termi

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

    Documents

    1. Human chromosome 12
      Human chromosome 12: entries, gene names and cross-references to MIM
    2. MIM cross-references
      Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
    3. PDB cross-references
      Index of Protein Data Bank (PDB) cross-references
    4. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3