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TUBB3 tubulin, beta 3 class III [ Homo sapiens (human) ]

Gene ID: 10381, updated on 24-Aug-2015
Official Symbol
TUBB3provided by HGNC
Official Full Name
tubulin, beta 3 class IIIprovided by HGNC
Primary source
HGNC:HGNC:20772
See related
Ensembl:ENSG00000258947; HPRD:04044; MIM:602661; Vega:OTTHUMG00000138985
Gene type
protein coding
RefSeq status
REVIEWED
Organism
Homo sapiens
Lineage
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae; Homo
Also known as
CDCBM; FEOM3; TUBB4; CDCBM1; CFEOM3; beta-4; CFEOM3A
Summary
This gene encodes a class III member of the beta tubulin protein family. Beta tubulins are one of two core protein families (alpha and beta tubulins) that heterodimerize and assemble to form microtubules. This protein is primarily expressed in neurons and may be involved in neurogenesis and axon guidance and maintenance. Mutations in this gene are the cause of congenital fibrosis of the extraocular muscles type 3. Alternate splicing results in multiple transcript variants. A pseudogene of this gene is found on chromosome 6. [provided by RefSeq, Oct 2010]
Orthologs
See TUBB3 in Epigenomics, MapViewer
Location:
16q24.3
Exon count:
5
Annotation release Status Assembly Chr Location
107 current GRCh38.p2 (GCF_000001405.28) 16 NC_000016.10 (89922009..89936097)
105 previous assembly GRCh37.p13 (GCF_000001405.25) 16 NC_000016.9 (89988417..90002505)

Chromosome 16 - NC_000016.10Genomic Context describing neighboring genes Neighboring gene uncharacterized LOC101927910 Neighboring gene melanocortin 1 receptor (alpha melanocyte stimulating hormone receptor) Neighboring gene differentially expressed in FDCP 8 homolog (mouse) Neighboring gene CENPB DNA-binding domains containing 1 Neighboring gene AFG3-like AAA ATPase 1, pseudogene

GeneRIFs: Gene References Into FunctionsWhat's a GeneRIF?

Protein interactions

Protein Gene Interaction Pubs
Envelope surface glycoprotein gp160, precursor env Treatment of cells with actin-depolymerizing agents or tubulin polymerization inhibitors largely reduces the percentage of cells with capped HIV-1 Gag and Env, indicating an intact actin and tubulin cytoskeleton is required for efficient assembly of HIV-1 PubMed
Pr55(Gag) gag Treatment of cells with actin-depolymerizing agents or tubulin polymerization inhibitors largely reduces the percentage of cells with capped HIV-1 Gag and Env, indicating an intact actin and tubulin cytoskeleton is required for efficient assembly of HIV-1 PubMed
Rev rev HIV-1 Rev interacting protein, TUBB3, is identified by the in-vitro binding experiments involving cytosolic or nuclear extracts from HeLa cells PubMed
rev Rev acts to depolymerize microtubules that are formed by tubulin, an effect that is observed during HIV-1 infection PubMed
Tat tat HIV-1 Tat K29A, K50R, and K51R lysine mutations downregulate the proportion of soluble tubulin in cells, while the majority of other lysine mutations upregulate the percentage of soluble tubulin compared with the wild-type PubMed
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 (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
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
Vpr vpr Concurrent exposure of HIV-1 Vpr with HCV core protein causes significantly increased human fetal neuron (HFN) injury, as indicated by reduced beta-III-tubulin, than HFN treated with HIV-1 Vpr alone PubMed

Go to the HIV-1, Human Interaction Database

  • 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).
  • Diurnally regulated genes with circadian orthologs, organism-specific biosystem (from WikiPathways)
    Diurnally regulated genes with circadian orthologs, organism-specific biosystemHuman genes regulated in the diurnal comparison with orthologues that display circadian regulation in mouse heart and liver (Panda 2002, Storch 2002), and SCN (Panda 2002). The 608 significantly regu...
  • 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...
  • 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'...
  • 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.
  • Parkin-Ubiquitin Proteasomal System pathway, organism-specific biosystem (from WikiPathways)
    Parkin-Ubiquitin Proteasomal System pathway, organism-specific biosystemThis pathway describes the Parkin-Ubiquitin proteasome degradation system.
  • 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, organism-specific biosystem (from WikiPathways)
    Pathogenic Escherichia coli infection, organism-specific biosystemSources: [http://www.genome.jp/kegg/pathway/hsa/hsa05130.html KEGG]
  • 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 ATP-dependent interaction with TriC/CCT. In order to form a functional heterodimer, these folding intermediates undergo a series of i...
  • 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...
Products Interactant Other Gene Complex Source Pubs Description

Markers

Homology

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
 
peptide binding IEA
Inferred from Electronic Annotation
more info
 
protein binding IPI
Inferred from Physical Interaction
more info
PubMed 
structural constituent of cytoskeleton IEA
Inferred from Electronic Annotation
more info
 
Process Evidence Code Pubs
'de novo' posttranslational protein folding TAS
Traceable Author Statement
more info
 
axon guidance IMP
Inferred from Mutant Phenotype
more info
PubMed 
cellular protein metabolic process TAS
Traceable Author Statement
more info
 
microtubule-based process IEA
Inferred from Electronic Annotation
more info
 
mitotic nuclear division IEA
Inferred from Electronic Annotation
more info
 
protein folding TAS
Traceable Author Statement
more info
 
protein polymerization IEA
Inferred from Electronic Annotation
more info
 
Component Evidence Code Pubs
axon IEA
Inferred from Electronic Annotation
more info
 
cell periphery IEA
Inferred from Electronic Annotation
more info
 
cytoplasm IEA
Inferred from Electronic Annotation
more info
 
dendrite ISS
Inferred from Sequence or Structural Similarity
more info
 
extracellular exosome IDA
Inferred from Direct Assay
more info
PubMed 
microtubule IDA
Inferred from Direct Assay
more info
PubMed 
neuronal cell body IEA
Inferred from Electronic Annotation
more info
 
nucleus IDA
Inferred from Direct Assay
more info
PubMed 
Preferred Names
tubulin beta-3 chain
Names
class III beta-tubulin
tubulin beta-4 chain
tubulin beta-III

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.

Genomic

  1. NG_027810.1 RefSeqGene

    Range
    5001..19089
    Download
    GenBank, FASTA, Sequence Viewer (Graphics)

mRNA and Protein(s)

  1. NM_001197181.1NP_001184110.1  tubulin beta-3 chain isoform 2

    See identical proteins and their annotated locations for NP_001184110.1

    Status: REVIEWED

    Description
    Transcript Variant: This variant (2) differs in the 5' UTR, lacks a portion of the 5' coding region, and initiates translation at a downstream start codon, compared to variant 1. The encoded isoform (2) is shorter at the N-terminus, compared to isoform 1.
    Source sequence(s)
    AC092143, AK292219, BC003021
    Consensus CDS
    CCDS56012.1
    UniProtKB/Swiss-Prot
    Q13509
    Related
    ENSP00000451617, OTTHUMP00000245288, ENST00000554444, OTTHUMT00000412017
    Conserved Domains (2) summary
    PLN00220
    Location:1375
    PLN00220; tubulin beta chain; Provisional
    cd02187
    Location:1354
    beta_tubulin; The beta-tubulin family
  2. NM_006086.3NP_006077.2  tubulin beta-3 chain isoform 1

    See identical proteins and their annotated locations for NP_006077.2

    Status: REVIEWED

    Description
    Transcript Variant: This variant (1) encodes the longest isoform (1).
    Source sequence(s)
    AK223039, BC003021, DA054466
    Consensus CDS
    CCDS10988.1
    UniProtKB/Swiss-Prot
    Q13509
    UniProtKB/TrEMBL
    Q53G92
    Related
    ENSP00000320295, OTTHUMP00000176846, ENST00000315491, OTTHUMT00000272874
    Conserved Domains (2) summary
    PLN00220
    Location:1447
    PLN00220; tubulin beta chain; Provisional
    cd02187
    Location:2426
    beta_tubulin; The beta-tubulin family

RefSeqs of Annotated Genomes: Homo sapiens Annotation Release 107

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

Reference GRCh38.p2 Primary Assembly

Genomic

  1. NC_000016.10 Reference GRCh38.p2 Primary Assembly

    Range
    89922009..89936097
    Download
    GenBank, FASTA, Sequence Viewer (Graphics)

Alternate CHM1_1.1

Genomic

  1. NC_018927.2 Alternate CHM1_1.1

    Range
    91400537..91414621
    Download
    GenBank, FASTA, Sequence Viewer (Graphics)