Format

Send to:

Choose Destination

TUBA3C tubulin alpha 3c [ Homo sapiens (human) ]

Gene ID: 7278, updated on 12-May-2016
Official Symbol
TUBA3Cprovided by HGNC
Official Full Name
tubulin alpha 3cprovided by HGNC
Primary source
HGNC:HGNC:12408
See related
Ensembl:ENSG00000198033 HPRD:03958; MIM:602528; Vega:OTTHUMG00000016481
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
TUBA2; bA408E5.3
Summary
Microtubules of the eukaryotic cytoskeleton perform essential and diverse functions and are composed of a heterodimer of alpha and beta tubulin. The genes encoding these microtubule constituents are part of the tubulin superfamily, which is composed of six distinct families. Genes from the alpha, beta and gamma tubulin families are found in all eukaryotes. The alpha and beta tubulins represent the major components of microtubules, while gamma tubulin plays a critical role in the nucleation of microtubule assembly. There are multiple alpha and beta tubulin genes and they are highly conserved among and between species. This gene is an alpha tubulin gene that encodes a protein 99% identical to the mouse testis-specific Tuba3 and Tuba7 gene products. This gene is located in the 13q11 region, which is associated with the genetic diseases Clouston hidrotic ectodermal dysplasia and Kabuki syndrome. [provided by RefSeq, Jul 2008]
Orthologs
Location:
13q11
Exon count:
5
Annotation release Status Assembly Chr Location
107 current GRCh38.p2 (GCF_000001405.28) 13 NC_000013.11 (19173770..19181852, complement)
105 previous assembly GRCh37.p13 (GCF_000001405.25) 13 NC_000013.10 (19747910..19755992, complement)

Chromosome 13 - NC_000013.11Genomic Context describing neighboring genes Neighboring gene RNA, U6 small nuclear 52, pseudogene Neighboring gene sphingomyelin phosphodiesterase 4 pseudogene 2 Neighboring gene uncharacterized LOC101928697 Neighboring gene paraspeckle component 1 pseudogene 1

NHGRI GWAS Catalog

Description
A genome-wide approach accounting for body mass index identifies genetic variants influencing fasting glycemic traits and insulin resistance.
NHGRI GWA Catalog

Protein interactions

Protein Gene Interaction Pubs
Envelope surface glycoprotein gp120 env The mRNA expression levels for alpha-tubulin, TRADD, IFN-gamma R2, GAS1, MADD, NF-kappaB, I-kappa B, 14-3-3 protein, APaf1, PARP, IGF-1 receptor, RB1, Rb2/p130, ARC, and caspase 6 are upregulated in human neuronal cells after treatment with HIV-1 gp120 PubMed
env The binding of HIV-1 gp120 to CD4+-permissive cells increases the level of acetylated alpha-tubulin in a CD4-dependent manner; overexpression of Histone Deacetylase 6 (HDAC6) inhibits the acetylation of alpha-tubulin and prevents HIV-1-cell fusion PubMed
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
Envelope transmembrane glycoprotein gp41 env Expression of HIV-1 gp41 cytoplasmic domain reduces acetylated tubulin alpha and interferes with virus-cell fusion 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 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 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 causes a dramatic decrease in alpha-tubulin staining, which indicates disruption of the cytoskeleton organization in human intestinal epithelial cells 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
integrase gag-pol Co-immunoprecipitation shows interaction of HIV-1 IN with alpha-tubulin PubMed

Go to the HIV-1, Human Interaction Database

  • Apoptosis, organism-specific biosystem (from KEGG)
    Apoptosis, organism-specific biosystemApoptosis is a genetically programmed process for the elimination of damaged or redundant cells by activation of caspases (aspartate-specific cysteine proteases). The onset of apoptosis is controlled...
  • Apoptosis, conserved biosystem (from KEGG)
    Apoptosis, conserved biosystemApoptosis is a genetically programmed process for the elimination of damaged or redundant cells by activation of caspases (aspartate-specific cysteine proteases). The onset of apoptosis is controlled...
  • 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...
  • 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
 
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
microtubule-based process IEA
Inferred from Electronic Annotation
more info
 
Component Evidence Code Pubs
cytoplasm IEA
Inferred from Electronic Annotation
more info
 
microtubule IEA
Inferred from Electronic Annotation
more info
 
nucleus IDA
Inferred from Direct Assay
more info
PubMed 
Preferred Names
tubulin alpha-3C/D chain
Names
alpha-tubulin 2
alpha-tubulin 3C/D
tubulin alpha-2 chain
tubulin, alpha 2
tubulin, alpha 3c

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_006001.2NP_005992.1  tubulin alpha-3C/D chain

    See identical proteins and their annotated locations for NP_005992.1

    Status: REVIEWED

    Source sequence(s)
    AA412719, AL139327, DB026664, DB524026
    Consensus CDS
    CCDS9284.1
    UniProtKB/Swiss-Prot
    Q13748
    UniProtKB/TrEMBL
    Q1ZYQ1
    Related
    ENSP00000382982, OTTHUMP00000018071, ENST00000400113, OTTHUMT00000044007
    Conserved Domains (2) summary
    PTZ00335
    Location:1440
    PTZ00335; tubulin alpha chain; Provisional
    cd02186
    Location:2435
    alpha_tubulin; The alpha-tubulin family

RefSeqs of Annotated Genomes: Homo sapiens Annotation Release 107 details...

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

Reference GRCh38.p2 Primary Assembly

Genomic

  1. NC_000013.11 Reference GRCh38.p2 Primary Assembly

    Range
    19173770..19181852 complement
    Download
    GenBank, FASTA, Sequence Viewer (Graphics)

Alternate CHM1_1.1

Genomic

  1. NC_018924.2 Alternate CHM1_1.1

    Range
    19715021..19723554 complement
    Download
    GenBank, FASTA, Sequence Viewer (Graphics)

Suppressed Reference Sequence(s)

The following Reference Sequences have been suppressed. Explain

  1. NM_079836.1: Suppressed sequence

    Description
    NM_079836.1: This RefSeq was permanently suppressed because currently there is not sufficient data to support this transcript.