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Q13509

- TBB3_HUMAN

UniProt

Q13509 - TBB3_HUMAN

Protein

Tubulin beta-3 chain

Gene

TUBB3

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 140 (01 Oct 2014)
      Sequence version 2 (02 May 2002)
      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. TUBB3 plays a critical role in proper axon guidance and mantainance.1 Publication

    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: IntAct
    4. structural constituent of cytoskeleton Source: InterPro

    GO - Biological processi

    1. 'de novo' posttranslational protein folding Source: Reactome
    2. axon guidance Source: UniProtKB
    3. cellular protein metabolic process Source: Reactome
    4. microtubule-based process Source: InterPro
    5. protein folding Source: Reactome
    6. 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_16936. Prefoldin mediated transfer of substrate to CCT/TriC.
    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 beta-3 chain
    Alternative name(s):
    Tubulin beta-4 chain
    Tubulin beta-III
    Gene namesi
    Name:TUBB3
    Synonyms:TUBB4
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 16

    Organism-specific databases

    HGNCiHGNC:20772. TUBB3.

    Subcellular locationi

    GO - Cellular componenti

    1. cytoplasm Source: UniProtKB-KW
    2. microtubule Source: UniProtKB
    3. nucleus Source: UniProt

    Keywords - Cellular componenti

    Cytoplasm, Cytoskeleton, Microtubule

    Pathology & Biotechi

    Involvement in diseasei

    Congenital fibrosis of extraocular muscles 3A (CFEOM3A) [MIM:600638]: A congenital ocular motility disorder marked by restrictive ophthalmoplegia affecting extraocular muscles innervated by the oculomotor and/or trochlear nerves. It is clinically characterized by anchoring of the eyes in downward gaze, ptosis, and backward tilt of the head. Congenital fibrosis of extraocular muscles type 3 presents as a non-progressive, autosomal dominant disorder with variable expression. Patients may be bilaterally or unilaterally affected, and their oculo-motility defects range from complete ophthalmoplegia (with the eyes fixed in a hypo- and exotropic position), to mild asymptomatic restrictions of ocular movement. Ptosis, refractive error, amblyopia, and compensatory head positions are associated with the more severe forms of the disorder. In some cases, the ocular phenotype is accompanied by additional features including developmental delay, corpus callosum agenesis, basal ganglia dysmorphism, facial weakness, polyneuropathy.1 Publication
    Note: The disease is caused by mutations affecting the gene represented in this entry.
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti62 – 621R → Q in CFEOM3A; affects heterodimers formation; results in increased stability and reduced dynamics of microtubules. 1 Publication
    VAR_062758
    Natural varianti262 – 2621R → C in CFEOM3A; affects heterodimers formation; affects microtubules polymerization and depolymerization rates. 1 Publication
    VAR_062759
    Natural varianti262 – 2621R → H in CFEOM3A; severe phenotype with congenital facial weakness, congenital wrist and finger contractures; affects microtubules polymerization and depolymerization rates. 1 Publication
    VAR_062760
    Natural varianti302 – 3021A → T in CFEOM3A; affects heterodimers formation; results in increased stability and reduced dynamics of microtubules. 1 Publication
    VAR_062761
    Natural varianti380 – 3801R → C in CFEOM3A; affects heterodimers formation; results in increased stability and reduced dynamics of microtubules. 1 Publication
    VAR_062762
    Natural varianti410 – 4101E → K in CFEOM3A; severe phenotype with congenital facial weakness; lower extremity weakness and sensory loss in the second to third decade of life in one patient; affects microtubules polymerization and depolymerization rates. 1 Publication
    VAR_062763
    Natural varianti417 – 4171D → H in CFEOM3A; severe phenotype with congenital facial weakness, congenital wrist and finger contractures. 1 Publication
    VAR_062764
    Natural varianti417 – 4171D → N in CFEOM3A; some patients with lower extremity weakness and sensory loss in the second to third decade of life; also found in patients without CFEOM3A who developed polyneuropathy. 1 Publication
    VAR_062765
    Cortical dysplasia, complex, with other brain malformations 1 (CDCBM1) [MIM:614039]: A disorder of aberrant neuronal migration and disturbed axonal guidance. Affected individuals have mild to severe mental retardation, strabismus, axial hypotonia, and spasticity. Brain imaging shows variable malformations of cortical development, including polymicrogyria, gyral disorganization, and fusion of the basal ganglia, as well as thin corpus callosum, hypoplastic brainstem, and dysplastic cerebellar vermis. Extraocular muscles are not involved.1 Publication
    Note: The disease is caused by mutations affecting the gene represented in this entry.
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti178 – 1781T → M in CDCBM1; can form tubulin heterodimers that are properly incorporated into microtubules; the microtubules are less stable than wild-type. 1 Publication
    VAR_066206
    Natural varianti205 – 2051E → K in CDCBM1; does not form tubulin heterodimers; patient fibroblasts show no major alterations in the microtubule network, but the microtubules are less stable than wild-type. 1 Publication
    VAR_066207
    Natural varianti302 – 3021A → V in CDCBM1; does not form tubulin heterodimers. 1 Publication
    VAR_066208
    Natural varianti323 – 3231M → V in CDCBM1; reduced heterodimers formation. 1 Publication
    VAR_066209

    Mutagenesis

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Mutagenesisi172 – 1721S → A: Loss of CDK1-mediated phosphorylation. 1 Publication
    Mutagenesisi172 – 1721S → D or E: Mimics phosphorylation, unable to incorporate into microtubules. 1 Publication

    Keywords - Diseasei

    Disease mutation

    Organism-specific databases

    MIMi600638. phenotype.
    614039. phenotype.
    Orphaneti45358. Congenital fibrosis of extraocular muscles.
    300570. Cortical dysgenesis with pontocerebellar hypoplasia due to TUBB3 mutation.
    PharmGKBiPA134953867.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 450450Tubulin beta-3 chainPRO_0000048250Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei172 – 1721Phosphoserine; by CDK11 Publication

    Post-translational modificationi

    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
    Phosphorylated on Ser-172 by CDK1 during the cell cycle, from metaphase to telophase, but not in interphase. This phosphorylation inhibits tubulin incorporation into microtubules.1 Publication

    Keywords - PTMi

    Phosphoprotein

    Proteomic databases

    MaxQBiQ13509.
    PRIDEiQ13509.

    2D gel databases

    OGPiQ13509.

    PTM databases

    PhosphoSiteiQ13509.

    Expressioni

    Tissue specificityi

    Expression is primarily restricted to central and peripheral nervous system. Greatly increased expression in most cancerous tissues.2 Publications

    Gene expression databases

    BgeeiQ13509.
    CleanExiHS_TUBB3.
    HS_TUBB4.
    GenevestigatoriQ13509.

    Organism-specific databases

    HPAiCAB011512.
    HPA043640.
    HPA046280.

    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.

    Binary interactionsi

    WithEntry#Exp.IntActNotes
    TUBA1BP683633EBI-350989,EBI-487083

    Protein-protein interaction databases

    BioGridi115654. 71 interactions.
    DIPiDIP-31505N.
    IntActiQ13509. 19 interactions.
    MINTiMINT-1163245.
    STRINGi9606.ENSP00000320295.

    Structurei

    3D structure databases

    ProteinModelPortaliQ13509.
    SMRiQ13509. Positions 2-427.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Domaini

    The highly acidic C-terminal region may bind cations such as calcium.

    Sequence similaritiesi

    Belongs to the tubulin family.Curated

    Phylogenomic databases

    HOGENOMiHOG000165710.
    HOVERGENiHBG000089.
    KOiK07375.
    PhylomeDBiQ13509.
    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]

    Sequences (2)i

    Sequence statusi: Complete.

    This entry describes 2 isoformsi produced by alternative splicing. Align

    Isoform 1 (identifier: Q13509-1) [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

    MREIVHIQAG QCGNQIGAKF WEVISDEHGI DPSGNYVGDS DLQLERISVY    50
    YNEASSHKYV PRAILVDLEP GTMDSVRSGA FGHLFRPDNF IFGQSGAGNN 100
    WAKGHYTEGA ELVDSVLDVV RKECENCDCL QGFQLTHSLG GGTGSGMGTL 150
    LISKVREEYP DRIMNTFSVV PSPKVSDTVV EPYNATLSIH QLVENTDETY 200
    CIDNEALYDI CFRTLKLATP TYGDLNHLVS ATMSGVTTSL RFPGQLNADL 250
    RKLAVNMVPF PRLHFFMPGF APLTARGSQQ YRALTVPELT QQMFDAKNMM 300
    AACDPRHGRY LTVATVFRGR MSMKEVDEQM LAIQSKNSSY FVEWIPNNVK 350
    VAVCDIPPRG LKMSSTFIGN STAIQELFKR ISEQFTAMFR RKAFLHWYTG 400
    EGMDEMEFTE AESNMNDLVS EYQQYQDATA EEEGEMYEDD EEESEAQGPK 450
    Length:450
    Mass (Da):50,433
    Last modified:May 2, 2002 - v2
    Checksum:i4B9CDE7DBA102949
    GO
    Isoform 2 (identifier: Q13509-2) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         1-72: Missing.

    Note: No experimental confirmation available.

    Show »
    Length:378
    Mass (Da):42,433
    Checksum:iA190AB5B6264F2AB
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti275 – 2751A → R in AAC52035. (PubMed:9473684)Curated

    Natural variant

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti62 – 621R → Q in CFEOM3A; affects heterodimers formation; results in increased stability and reduced dynamics of microtubules. 1 Publication
    VAR_062758
    Natural varianti178 – 1781T → M in CDCBM1; can form tubulin heterodimers that are properly incorporated into microtubules; the microtubules are less stable than wild-type. 1 Publication
    VAR_066206
    Natural varianti205 – 2051E → K in CDCBM1; does not form tubulin heterodimers; patient fibroblasts show no major alterations in the microtubule network, but the microtubules are less stable than wild-type. 1 Publication
    VAR_066207
    Natural varianti262 – 2621R → C in CFEOM3A; affects heterodimers formation; affects microtubules polymerization and depolymerization rates. 1 Publication
    VAR_062759
    Natural varianti262 – 2621R → H in CFEOM3A; severe phenotype with congenital facial weakness, congenital wrist and finger contractures; affects microtubules polymerization and depolymerization rates. 1 Publication
    VAR_062760
    Natural varianti302 – 3021A → T in CFEOM3A; affects heterodimers formation; results in increased stability and reduced dynamics of microtubules. 1 Publication
    VAR_062761
    Natural varianti302 – 3021A → V in CDCBM1; does not form tubulin heterodimers. 1 Publication
    VAR_066208
    Natural varianti323 – 3231M → V in CDCBM1; reduced heterodimers formation. 1 Publication
    VAR_066209
    Natural varianti380 – 3801R → C in CFEOM3A; affects heterodimers formation; results in increased stability and reduced dynamics of microtubules. 1 Publication
    VAR_062762
    Natural varianti410 – 4101E → K in CFEOM3A; severe phenotype with congenital facial weakness; lower extremity weakness and sensory loss in the second to third decade of life in one patient; affects microtubules polymerization and depolymerization rates. 1 Publication
    VAR_062763
    Natural varianti417 – 4171D → H in CFEOM3A; severe phenotype with congenital facial weakness, congenital wrist and finger contractures. 1 Publication
    VAR_062764
    Natural varianti417 – 4171D → N in CFEOM3A; some patients with lower extremity weakness and sensory loss in the second to third decade of life; also found in patients without CFEOM3A who developed polyneuropathy. 1 Publication
    VAR_062765

    Alternative sequence

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Alternative sequencei1 – 7272Missing in isoform 2. 1 PublicationVSP_054659Add
    BLAST

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    U47634 mRNA. Translation: AAC52035.1.
    AF427491 mRNA. Translation: AAL28094.1.
    AK122757 mRNA. Translation: BAG53710.1.
    AK292219 mRNA. Translation: BAF84908.1.
    AC092143 Genomic DNA. No translation available.
    CH471184 Genomic DNA. Translation: EAW66674.1.
    BC000748 mRNA. Translation: AAH00748.1.
    BC003021 mRNA. Translation: AAH03021.2.
    CCDSiCCDS10988.1. [Q13509-1]
    CCDS56012.1. [Q13509-2]
    RefSeqiNP_001184110.1. NM_001197181.1. [Q13509-2]
    NP_006077.2. NM_006086.3. [Q13509-1]
    UniGeneiHs.511743.

    Genome annotation databases

    EnsembliENST00000304984; ENSP00000302777; ENSG00000258947.
    ENST00000315491; ENSP00000320295; ENSG00000198211.
    GeneIDi10381.
    KEGGihsa:10381.
    UCSCiuc002fpf.2. human. [Q13509-1]

    Polymorphism databases

    DMDMi20455526.

    Keywords - Coding sequence diversityi

    Alternative splicing

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    U47634 mRNA. Translation: AAC52035.1 .
    AF427491 mRNA. Translation: AAL28094.1 .
    AK122757 mRNA. Translation: BAG53710.1 .
    AK292219 mRNA. Translation: BAF84908.1 .
    AC092143 Genomic DNA. No translation available.
    CH471184 Genomic DNA. Translation: EAW66674.1 .
    BC000748 mRNA. Translation: AAH00748.1 .
    BC003021 mRNA. Translation: AAH03021.2 .
    CCDSi CCDS10988.1. [Q13509-1 ]
    CCDS56012.1. [Q13509-2 ]
    RefSeqi NP_001184110.1. NM_001197181.1. [Q13509-2 ]
    NP_006077.2. NM_006086.3. [Q13509-1 ]
    UniGenei Hs.511743.

    3D structure databases

    ProteinModelPortali Q13509.
    SMRi Q13509. Positions 2-427.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 115654. 71 interactions.
    DIPi DIP-31505N.
    IntActi Q13509. 19 interactions.
    MINTi MINT-1163245.
    STRINGi 9606.ENSP00000320295.

    Chemistry

    BindingDBi Q13509.
    ChEMBLi CHEMBL2597.

    PTM databases

    PhosphoSitei Q13509.

    Polymorphism databases

    DMDMi 20455526.

    2D gel databases

    OGPi Q13509.

    Proteomic databases

    MaxQBi Q13509.
    PRIDEi Q13509.

    Protocols and materials databases

    DNASUi 10381.
    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000304984 ; ENSP00000302777 ; ENSG00000258947 .
    ENST00000315491 ; ENSP00000320295 ; ENSG00000198211 .
    GeneIDi 10381.
    KEGGi hsa:10381.
    UCSCi uc002fpf.2. human. [Q13509-1 ]

    Organism-specific databases

    CTDi 10381.
    GeneCardsi GC16P089996.
    GC16P089997.
    GeneReviewsi TUBB3.
    HGNCi HGNC:20772. TUBB3.
    HPAi CAB011512.
    HPA043640.
    HPA046280.
    MIMi 600638. phenotype.
    602661. gene.
    614039. phenotype.
    neXtProti NX_Q13509.
    Orphaneti 45358. Congenital fibrosis of extraocular muscles.
    300570. Cortical dysgenesis with pontocerebellar hypoplasia due to TUBB3 mutation.
    PharmGKBi PA134953867.
    GenAtlasi Search...

    Phylogenomic databases

    HOGENOMi HOG000165710.
    HOVERGENi HBG000089.
    KOi K07375.
    PhylomeDBi Q13509.
    TreeFami TF300298.

    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_16936. Prefoldin mediated transfer of substrate to CCT/TriC.
    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 TUBB3. human.
    GeneWikii TUBB3.
    GenomeRNAii 10381.
    NextBioi 39327.
    PROi Q13509.
    SOURCEi Search...

    Gene expression databases

    Bgeei Q13509.
    CleanExi HS_TUBB3.
    HS_TUBB4.
    Genevestigatori Q13509.

    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. "Cloning and sequencing of human betaIII-tubulin cDNA: induction of betaIII isotype in human prostate carcinoma cells by acute exposure to antimicrotubule agents."
      Ranganathan S., Dexter D.W., Benetatos C.A., Hudes G.R.
      Biochim. Biophys. Acta 1395:237-245(1998) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
    2. Banerjee A.
      Submitted (OCT-2001) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
      Tissue: Mammary cancer.
    3. "Complete sequencing and characterization of 21,243 full-length human cDNAs."
      Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.
      , Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.
      Nat. Genet. 36:40-45(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
      Tissue: Brain and Esophagus.
    4. "The sequence and analysis of duplication-rich human chromosome 16."
      Martin J., Han C., Gordon L.A., Terry A., Prabhakar S., She X., Xie G., Hellsten U., Chan Y.M., Altherr M., Couronne O., Aerts A., Bajorek E., Black S., Blumer H., Branscomb E., Brown N.C., Bruno W.J.
      , Buckingham J.M., Callen D.F., Campbell C.S., Campbell M.L., Campbell E.W., Caoile C., Challacombe J.F., Chasteen L.A., Chertkov O., Chi H.C., Christensen M., Clark L.M., Cohn J.D., Denys M., Detter J.C., Dickson M., Dimitrijevic-Bussod M., Escobar J., Fawcett J.J., Flowers D., Fotopulos D., Glavina T., Gomez M., Gonzales E., Goodstein D., Goodwin L.A., Grady D.L., Grigoriev I., Groza M., Hammon N., Hawkins T., Haydu L., Hildebrand C.E., Huang W., Israni S., Jett J., Jewett P.B., Kadner K., Kimball H., Kobayashi A., Krawczyk M.-C., Leyba T., Longmire J.L., Lopez F., Lou Y., Lowry S., Ludeman T., Manohar C.F., Mark G.A., McMurray K.L., Meincke L.J., Morgan J., Moyzis R.K., Mundt M.O., Munk A.C., Nandkeshwar R.D., Pitluck S., Pollard M., Predki P., Parson-Quintana B., Ramirez L., Rash S., Retterer J., Ricke D.O., Robinson D.L., Rodriguez A., Salamov A., Saunders E.H., Scott D., Shough T., Stallings R.L., Stalvey M., Sutherland R.D., Tapia R., Tesmer J.G., Thayer N., Thompson L.S., Tice H., Torney D.C., Tran-Gyamfi M., Tsai M., Ulanovsky L.E., Ustaszewska A., Vo N., White P.S., Williams A.L., Wills P.L., Wu J.-R., Wu K., Yang J., DeJong P., Bruce D., Doggett N.A., Deaven L., Schmutz J., Grimwood J., Richardson P., Rokhsar D.S., Eichler E.E., Gilna P., Lucas S.M., Myers R.M., Rubin E.M., Pennacchio L.A.
      Nature 432:988-994(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    5. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    6. "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] (ISOFORM 1).
      Tissue: Lung.
    7. Lubec G., Afjehi-Sadat L., Chen W.-Q., Sun Y.
      Submitted (DEC-2008) to UniProtKB
      Cited for: PROTEIN SEQUENCE OF 63-77; 104-121; 242-251; 163-174 AND 381-390, IDENTIFICATION BY MASS SPECTROMETRY.
      Tissue: Brain, Cajal-Retzius cell and Fetal brain cortex.
    8. "Class III beta-tubulin isotype: a key cytoskeletal protein at the crossroads of developmental neurobiology and tumor neuropathology."
      Katsetos C.D., Legido A., Perentes E., Mork S.J.
      J. Child Neurol. 18:851-866(2003) [PubMed] [Europe PMC] [Abstract]
      Cited for: TISSUE SPECIFICITY.
    9. Erratum
      Katsetos C.D., Legido A., Perentes E., Mork S.J.
      J. Child Neurol. 19:531-531(2004)
    10. "Microtubule regulation in mitosis: tubulin phosphorylation by the cyclin-dependent kinase Cdk1."
      Fourest-Lieuvin A., Peris L., Gache V., Garcia-Saez I., Juillan-Binard C., Lantez V., Job D.
      Mol. Biol. Cell 17:1041-1050(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION AT SER-172 BY CDK1, MUTAGENESIS OF SER-172.
    11. "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.
    12. Cited for: FUNCTION, VARIANTS CFEOM3A GLN-62; CYS-262; HIS-262; THR-302; CYS-380; LYS-410; HIS-417 AND ASN-417, CHARACTERIZATION OF VARIANTS CFEOM3A GLN-62; CYS-262; HIS-262; THR-302; CYS-380 AND LYS-410.
    13. Cited for: TISSUE SPECIFICITY.
    14. Cited for: VARIANTS CDCBM1 MET-178; LYS-205; VAL-302 AND VAL-323, CHARACTERIZATION OF VARIANTS CDCBM1 MET-178; LYS-205; VAL-302 AND VAL-323.

    Entry informationi

    Entry nameiTBB3_HUMAN
    AccessioniPrimary (citable) accession number: Q13509
    Secondary accession number(s): A8K854, Q9BTZ0, Q9BW10
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: July 15, 1998
    Last sequence update: May 2, 2002
    Last modified: October 1, 2014
    This is version 140 of the entry and version 2 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

    Complete proteome, Direct protein sequencing, Reference proteome

    Documents

    1. Human chromosome 16
      Human chromosome 16: entries, gene names and cross-references to MIM
    2. Human entries with polymorphisms or disease mutations
      List of human entries with polymorphisms or disease mutations
    3. Human polymorphisms and disease mutations
      Index of human polymorphisms and disease mutations
    4. MIM cross-references
      Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
    5. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3