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TUBA1C tubulin, alpha 1c [ Homo sapiens (human) ]

Gene ID: 84790, updated on 7-Dec-2014
Official Symbol
TUBA1Cprovided by HGNC
Official Full Name
tubulin, alpha 1cprovided by HGNC
Primary source
HGNC:HGNC:20768
See related
Ensembl:ENSG00000167553; HPRD:06747; Vega:OTTHUMG00000169497
Gene type
protein coding
RefSeq status
PROVISIONAL
Organism
Homo sapiens
Lineage
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae; Homo
Also known as
TUBA6; bcm948
See TUBA1C in Epigenomics, MapViewer
Location:
12q13.12
Exon count:
4
Annotation release Status Assembly Chr Location
106 current GRCh38 (GCF_000001405.26) 12 NC_000012.12 (49265082..49273330)
105 previous assembly GRCh37.p13 (GCF_000001405.25) 12 NC_000012.11 (49621715..49667117)

Chromosome 12 - NC_000012.12Genomic Context describing neighboring genes Neighboring gene tubulin, alpha 1a Neighboring gene uncharacterized LOC102723916 Neighboring gene uncharacterized LOC101927267 Neighboring gene peripherin Neighboring gene trophinin associated protein

Replication interactions

Interaction Pubs
Knockdown of tubulin, alpha 1c (TUBA1C) by shRNA library screening inhibits HIV-1 replication in cultured Jurkat T-cells PubMed

Protein interactions

Protein Gene Interaction Pubs
Envelope surface glycoprotein gp120 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 HIV-1 Rev interacting protein, tubulin alpha 1c (TUBA1C), 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 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 (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
integrase gag-pol Co-immunoprecipitation shows interaction of HIV-1 IN with alpha-tubulin 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).
  • 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

Clone Names

  • MGC10851, MGC14580

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
 
structural molecule activity TAS
Traceable Author Statement
more info
PubMed 
Process Evidence Code Pubs
'de novo' posttranslational protein folding TAS
Traceable Author Statement
more info
 
GTP catabolic process IEA
Inferred from Electronic Annotation
more info
 
cell division TAS
Traceable Author Statement
more info
PubMed 
cellular protein metabolic process TAS
Traceable Author Statement
more info
 
cytoskeleton-dependent intracellular transport TAS
Traceable Author Statement
more info
PubMed 
microtubule-based process TAS
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
cytoplasmic microtubule IEA
Inferred from Electronic Annotation
more info
 
microtubule TAS
Traceable Author Statement
more info
PubMed 
nucleus IDA
Inferred from Direct Assay
more info
PubMed 
vesicle IDA
Inferred from Direct Assay
more info
PubMed 
Preferred Names
tubulin alpha-1C chain
Names
tubulin alpha-1C chain
alpha-tubulin 6
tubulin, alpha 6
tubulin alpha-6 chain

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_032704.3NP_116093.1  tubulin alpha-1C chain

    See proteins identical to NP_116093.1

    Status: PROVISIONAL

    Source sequence(s)
    BC005946
    Consensus CDS
    CCDS8782.1
    UniProtKB/Swiss-Prot
    Q9BQE3
    Related
    ENSP00000443475, OTTHUMP00000241322, ENST00000541364, OTTHUMT00000404420
    Conserved Domains (2) summary
    cd02186
    Location:2435
    alpha_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 ...
    PTZ00335
    Location:1448
    PTZ00335; tubulin alpha chain; Provisional

RefSeqs of Annotated Genomes: Homo sapiens Annotation Release 106

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

Reference GRCh38 Primary Assembly

Genomic

  1. NC_000012.12 

    Range
    49265082..49273330
    Download
    GenBank, FASTA, Sequence Viewer (Graphics)

Alternate CHM1_1.1

Genomic

  1. NC_018923.2 

    Range
    49624585..49632833
    Download
    GenBank, FASTA, Sequence Viewer (Graphics)

Alternate HuRef

Genomic

  1. AC_000144.1 

    Range
    46689983..46698231
    Download
    GenBank, FASTA, Sequence Viewer (Graphics)