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    TUBB4B tubulin, beta 4B class IVb [ Homo sapiens ]

    Gene ID: 10383, updated on 11-May-2012

    Summary

    Official Symbol
    TUBB4Bprovided by HGNC
    Official Full Name
    tubulin, beta 4B class IVbprovided by HGNC
    Primary source
    HGNC:20771
    Locus tag
    RP13-122B23.2
    See related
    Ensembl:ENSG00000188229; HPRD:04043; MIM:602660; Vega:OTTHUMG00000131783
    Gene type
    protein coding
    RefSeq status
    VALIDATED
    Organism
    Homo sapiens
    Lineage
    Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae; Homo
    Also known as
    Beta2; TUBB2; TUBB2C

    Genomic context

    Location :
    9q34
    Sequence :
    Chromosome: 9; NC_000009.11 (140135711..140138159)
    See TUBB4B in Epigenomics, MapViewer

    Chromosome 9 - NC_000009.11Genomic Context describing neighboring genes Neighboring gene uncharacterized LOC100130547 Neighboring gene ring finger protein 224 Neighboring gene solute carrier family 34 (sodium phosphate), member 3 Neighboring gene family with sequence similarity 166, member A Neighboring gene uncharacterized LOC100129722 Neighboring gene chromosome 9 open reading frame 173 Neighboring gene cofactor of BRCA1

    Genomic regions, transcripts, and products

    Bibliography

    GeneRIFs: Gene References Into Functions What's a GeneRIF?

    HIV-1 protein interactions

    Protein Gene Interaction Pubs
    Rev rev Rev acts to depolymerize microtubules that are formed by tubulin, an effect that is observed during HIV-1 infection PubMed
    Tat tat In Jurkat cells expressing HIV-1 Tat, decreased expression levels are found for basic cytoskeletal proteins such as actin, beta-tubulin, annexin, cofilin, gelsolin, and Rac/Rho-GDI complex PubMed
    tat HIV-1 Tat (amino acids 36-39) binds tubulin alpha/beta dimers and polymerized microtubules leading to the alteration of microtubule dynamics and activation of a mitochondria-dependent apoptotic pathway that is facilitated by the Bcl-2 relative Bim PubMed
    tat HIV-1 Tat (specifically, amino acids 38-72), enhances tubulin polymerization and triggers the mitochondrial pathway to induce T cell apoptosis as shown in vitro by the release of cytochrome c from isolated mitochondria PubMed

    Go to the HIV-1, Human Protein Interaction Database

    Interactions

    Products Interactant Other Gene Complex Source Pubs Description
    P68371 P36957 DLST    HPRD  PubMed  
    P68371 Q06323 PSME1    HPRD  PubMed  
    P68371 O14544 SOCS6    HPRD  PubMed  
    P68371 O14512 SOCS7    HPRD  PubMed  
    P68371 P23258 TUBG1    HPRD  PubMed  
    P68371 O43261     HPRD  PubMed  
    BioGRID:115656 BioGRID:121497 AICDA    BioGRID  PubMed Affinity Capture-Western 
    BioGRID:115656 BioGRID:107459 CDK9    BioGRID  PubMed Affinity Capture-MS 
    BioGRID:115656 BioGRID:107463 CDKN2A    BioGRID  PubMed Affinity Capture-MS 
    BioGRID:115656 BioGRID:115589 DLEU1    BioGRID  PubMed Two-hybrid 
    BioGRID:115656 BioGRID:108087 DLST    BioGRID  PubMed Two-hybrid 
    BioGRID:115656 BioGRID:128177 EIF2C3    BioGRID  PubMed Affinity Capture-MS 
    BioGRID:115656 BioGRID:128178 EIF2C4    BioGRID  PubMed Affinity Capture-MS 
    BioGRID:115656 BioGRID:115331 HDAC5    BioGRID  PubMed Affinity Capture-MS 
    BioGRID:115656 BioGRID:110411 MGMT    BioGRID  PubMed Affinity Capture-MS 
    BioGRID:115656 BioGRID:111692 PSME1    BioGRID  PubMed Two-hybrid 
    BioGRID:115656 BioGRID:111822 RAD21    BioGRID  PubMed Affinity Capture-Western 
    BioGRID:115656 BioGRID:114719 SOCS6    BioGRID  PubMed Affinity Capture-MS 
    BioGRID:115656 BioGRID:112497 SUMO2    BioGRID  PubMed Affinity Capture-MS 
    BioGRID:115656 BioGRID:113164 UBC    BioGRID  PubMed Affinity Capture-MS 
    BioGRID:115656 BioGRID:113269 VHL    BioGRID  PubMed Affinity Capture-MS 

    General gene information

    Markers

    Homology

    Pathways from BioSystems

    • Cell Cycle, organism-specific biosystem (from REACTOME)
      Cell Cycle, organism-specific biosystem
      Cell Cycle
    • Cell Cycle, Mitotic, organism-specific biosystem (from REACTOME)
      Cell Cycle, Mitotic, organism-specific biosystemThe replication of the genome and the subsequent segregation of chromosomes into daughter cells are controlled by a series of events collectively known as the cell cycle. DNA replication is carried o...
    • Centrosome maturation, organism-specific biosystem (from REACTOME)
      Centrosome maturation, organism-specific biosystemThe centrosome is the primary microtubule organizing center (MTOC) in vertebrate cells and plays an important role in orchestrating the formation of the mitotic spindle. Centrosome maturation is an ...
    • Chaperonin-mediated protein folding, organism-specific biosystem (from REACTOME)
      Chaperonin-mediated protein folding, organism-specific biosystemThe eukaryotic chaperonin TCP-1 ring complex (TRiC/ CCT) plays an essential role in the folding of a subset of proteins prominent among which are the actins and tubulins (reviewed in Altschuler and...
    • Cooperation of Prefoldin and TriC/CCT in actin and tubulin folding, organism-specific biosystem (from REACTOME)
      Cooperation of Prefoldin and TriC/CCT in actin and tubulin folding, organism-specific biosystemIn the case of actin and tubulin folding, and perhaps other substrates, the emerging polypeptide chain is transferred from the ribosome to TRiC via Prefoldin (Vainberg et al., 1998).
    • Formation of tubulin folding intermediates by CCT/TriC, organism-specific biosystem (from REACTOME)
      Formation of tubulin folding intermediates by CCT/TriC, organism-specific biosystemTriC/CCT forms a binary complex with unfolded alpha- or beta-tubulin (Frydman et al., 1992; Gao et al., 1993). The tubulin folding intermediates produced by TriC are unstable (Gao et al., 1993). Fiv...
    • G2/M Transition, organism-specific biosystem (from REACTOME)
      G2/M Transition, organism-specific biosystemCyclin A can also form complexes with Cdc2 (Cdk1). Together with three B-type cyclins, Cdc2 (Cdk1) regulates the transition from G2 into mitosis. These complexes are activated by dephosphorylation of...
    • Gap junction, organism-specific biosystem (from KEGG)
      Gap junction, organism-specific biosystemGap junctions contain intercellular channels that allow direct communication between the cytosolic compartments of adjacent cells. Each gap junction channel is formed by docking of two 'hemichannels'...
    • Gap junction, conserved biosystem (from KEGG)
      Gap junction, conserved biosystemGap junctions contain intercellular channels that allow direct communication between the cytosolic compartments of adjacent cells. Each gap junction channel is formed by docking of two 'hemichannels'...
    • Loss of Nlp from mitotic centrosomes, organism-specific biosystem (from REACTOME)
      Loss of Nlp from mitotic centrosomes, organism-specific biosystemDuring interphase, Nlp interacts with gamma-tubulin ring complexes (gamma-TuRC), and is thought to contribute to the organization of interphase microtubules (Casenghi et al.,2003). Plk1 is activated...
    • Loss of proteins required for interphase microtubule organization from the centrosome, organism-specific biosystem (from REACTOME)
      Loss of proteins required for interphase microtubule organization from the centrosome, organism-specific biosystemIn addition to recruiting proteins and complexes necessary for increased microtubule nucleation, centrosomal maturation involves the loss of proteins involved in interphase microtubule organization ...
    • Metabolism of proteins, organism-specific biosystem (from REACTOME)
      Metabolism of proteins, organism-specific biosystemProtein metabolism comprises the pathways of translation, post-translational modification and protein folding.
    • Mitotic G2-G2/M phases, organism-specific biosystem (from REACTOME)
      Mitotic G2-G2/M phases, organism-specific biosystem
      Mitotic G2-G2/M phases
    • Pathogenic Escherichia coli infection, organism-specific biosystem (from KEGG)
      Pathogenic Escherichia coli infection, organism-specific biosystemEnteropathogenic E. coli (EPEC) and enterohemorrhagic E. coli (EHEC) are closely related pathogenic strains of Escherichia coli. The hallmark of EPEC/EHEC infections [DS:H00278 H00277] is induction o...
    • Pathogenic Escherichia coli infection, conserved biosystem (from KEGG)
      Pathogenic Escherichia coli infection, conserved biosystemEnteropathogenic E. coli (EPEC) and enterohemorrhagic E. coli (EHEC) are closely related pathogenic strains of Escherichia coli. The hallmark of EPEC/EHEC infections [DS:H00278 H00277] is induction o...
    • Phagosome, organism-specific biosystem (from KEGG)
      Phagosome, organism-specific biosystemPhagocytosis is the process of taking in relatively large particles by a cell, and is a central mechanism in the tissue remodeling, inflammation, and defense against infectious agents. A phagosome is...
    • Phagosome, conserved biosystem (from KEGG)
      Phagosome, conserved biosystemPhagocytosis is the process of taking in relatively large particles by a cell, and is a central mechanism in the tissue remodeling, inflammation, and defense against infectious agents. A phagosome is...
    • Post-chaperonin tubulin folding pathway, organism-specific biosystem (from REACTOME)
      Post-chaperonin tubulin folding pathway, organism-specific biosystemAlpha and beta tubulin folding intermediates are formed through ATPâ??dependent interaction with TriC/CCT. In order to form a functional heterodimer, these folding intermediates undergo a series of...
    • Prefoldin mediated transfer of substrate to CCT/TriC, organism-specific biosystem (from REACTOME)
      Prefoldin mediated transfer of substrate to CCT/TriC, organism-specific biosystemUnfolded actins and tubulins bound to prefoldin are transferred to CCT via a docking mechanism (McCormack and Willison, 2001).
    • Protein folding, organism-specific biosystem (from REACTOME)
      Protein folding, organism-specific biosystemDue to the crowded envirnoment within the cell, many proteins must interact with molecular chaperones to attain their native conformation (reviewed in Young et al., 2004). Chaperones recognize and...
    • Recruitment of mitotic centrosome proteins and complexes, organism-specific biosystem (from REACTOME)
      Recruitment of mitotic centrosome proteins and complexes, organism-specific biosystemThe mitotic spindle becomes established once centrosomes have migrated to opposite poles and the nuclear envelope has broken down. During this stage, interphase centrosomes mature into mitotic centro...

    Gene Ontology Provided by GOA

    Function Evidence Code Pubs
    GTP binding IEA
    Inferred from Electronic Annotation
    more info
     
    GTPase activity IEA
    Inferred from Electronic Annotation
    more info
     
    MHC class I protein binding TAS
    Traceable Author Statement
    more info
    PubMed 
    nucleotide binding IEA
    Inferred from Electronic Annotation
    more info
     
    structural molecule activity IEA
    Inferred from Electronic Annotation
    more info
     
    unfolded protein binding NAS
    Non-traceable Author Statement
    more info
    PubMed 
    Process Evidence Code Pubs
    'de novo' posttranslational protein folding TAS
    Traceable Author Statement
    more info
     
    G2/M transition of mitotic cell cycle TAS
    Traceable Author Statement
    more info
     
    cellular component movement TAS
    Traceable Author Statement
    more info
    PubMed 
    cellular protein metabolic process TAS
    Traceable Author Statement
    more info
     
    microtubule-based movement IEA
    Inferred from Electronic Annotation
    more info
     
    mitotic cell cycle TAS
    Traceable Author Statement
    more info
     
    natural killer cell mediated cytotoxicity NAS
    Non-traceable Author Statement
    more info
    PubMed 
    protein folding TAS
    Traceable Author Statement
    more info
     
    protein polymerization IEA
    Inferred from Electronic Annotation
    more info
     
    Component Evidence Code Pubs
    cytoplasm IEA
    Inferred from Electronic Annotation
    more info
     
    cytoskeleton IEA
    Inferred from Electronic Annotation
    more info
     
    cytosol TAS
    Traceable Author Statement
    more info
     
    microtubule IEA
    Inferred from Electronic Annotation
    more info
     

    General protein information

    Preferred Names
    tubulin beta-4B chain
    Names
    tubulin beta-4B chain
    tubulin, beta 2C
    tubulin, beta, 2
    tubulin beta-2 chain
    tubulin beta-2C chain
    class IVb beta tubulin
    class IVb beta-tubulin

    NCBI Reference Sequences (RefSeq)

    RefSeqs maintained independently of Annotated Genomes

    These reference sequences exist independently of genome builds. Explain

    These reference sequences are curated independently of the genome annotation cycle, so their versions may not match the RefSeq versions in the current genome build. Identify version mismatches by comparing the version of the RefSeq in this section to the one reported in Genomic regions, transcripts, and products above.

    mRNA and Protein(s)

    1. NM_006088.5NP_006079.1  tubulin beta-4B chain

      Status: VALIDATED

      Source sequence(s)
      BC004188, CB139156
      Consensus CDS
      CCDS7039.1
      UniProtKB/Swiss-Prot
      P68371
      Related
      ENSP00000341289, OTTHUMP00000162590, ENST00000340384, OTTHUMT00000254715
      Conserved Domains (2) summary
      cd02187
      Location:2426
      Blast Score: 2460
      beta_tubulin; The tubulin superfamily includes five distinct families, the alpha-, beta-, gamma-, delta-, and epsilon-tubulins and a sixth family (zeta-tubulin) which is present only in kinetoplastid protozoa. The alpha- and beta-tubulins are the major components of ...
      PLN00220
      Location:1427
      Blast Score: 2371
      PLN00220; tubulin beta chain; Provisional

    RefSeqs of Annotated Genomes: Build 37.3

    The following sections contain reference sequences that belong to a specific genome build. Explain

    Reference GRCh37.p5 Primary Assembly

    Genomic

    1. NC_000009.11 Reference GRCh37.p5 Primary Assembly

      Range
      140135711..140138159
      Download
      GenBank, FASTA, Sequence Viewer (Graphics)

    Alternate HuRef

    Genomic

    1. AC_000141.1 Alternate HuRef

      Range
      109595024..109597472
      Download
      GenBank, FASTA, Sequence Viewer (Graphics)

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