Q8R3N6 · THOC1_MOUSE

  • Protein
    THO complex subunit 1
  • Gene
    Thoc1
  • Status
    UniProtKB reviewed (Swiss-Prot)
  • Amino acids
  • Protein existence
    Evidence at protein level
  • Annotation score
    5/5

Function

function

Component of the THO subcomplex of the TREX complex which is thought to couple mRNA transcription, processing and nuclear export, and which specifically associates with spliced mRNA and not with unspliced pre-mRNA (By similarity).
Required for efficient export of polyadenylated RNA (By similarity).
The THOC1-THOC2-THOC3 core complex alone is sufficient to bind export factor NXF1-NXT1 and promote ATPase activity of DDX39B (By similarity).
TREX is recruited to spliced mRNAs by a transcription-independent mechanism, binds to mRNA upstream of the exon-junction complex (EJC) and is recruited in a splicing- and cap-dependent manner to a region near the 5' end of the mRNA where it functions in mRNA export to the cytoplasm via the TAP/NXF1 pathway (By similarity).
Regulates transcriptional elongation of a subset of genes (By similarity).
Involved in genome stability by preventing co-transcriptional R-loop formation (By similarity).
May play a role in hair cell formation, hence may be involved in hearing (By similarity).
Participates in an apoptotic pathway which is characterized by activation of caspase-6, increases in the expression of BAK1 and BCL2L1 and activation of NF-kappa-B. This pathway does not require p53/TP53, nor does the presence of p53/TP53 affect the efficiency of cell killing. Activates a G2/M cell cycle checkpoint prior to the onset of apoptosis. Apoptosis is inhibited by association with RB1 (By similarity).
Essential for early embryonic development. Required for normal gene expression during postnatal testis development

GO annotations

AspectTerm
Cellular Componentchromosome, telomeric region
Cellular Componentcytosol
Cellular Componentnuclear matrix
Cellular Componentnuclear speck
Cellular ComponentTHO complex part of transcription export complex
Molecular FunctionDNA binding
Molecular FunctionRNA binding
Biological Processapoptotic process
Biological ProcessmRNA export from nucleus
Biological ProcessmRNA processing
Biological ProcessRNA splicing
Biological Processsignal transduction

Keywords

Enzyme and pathway databases

Names & Taxonomy

Protein names

  • Recommended name
    THO complex subunit 1
  • Alternative names
    • Nuclear matrix protein p84

Gene names

    • Name
      Thoc1
    • Synonyms
      Hpr1

Organism names

  • Taxonomic identifier
  • Strains
    • C57BL/6J
    • Czech II
  • Taxonomic lineage
    Eukaryota > Metazoa > Chordata > Craniata > Vertebrata > Euteleostomi > Mammalia > Eutheria > Euarchontoglires > Glires > Rodentia > Myomorpha > Muroidea > Muridae > Murinae > Mus > Mus

Accessions

  • Primary accession
    Q8R3N6
  • Secondary accessions
    • Q8BWD5
    • Q8BXY3

Proteomes

Organism-specific databases

Subcellular Location

Nucleus
Nucleus, nucleoplasm
Nucleus matrix
Cytoplasm, cytosol
Note: Predominantly localized in the nucleus (PubMed:32776944).
Shuttles between the nucleus and cytosol. Nuclear localization is required for induction of apoptotic cell death. Translocates to the cytoplasm during the early phase of apoptosis execution (By similarity).

Keywords

Phenotypes & Variants

Disruption phenotype

Mice show early embryonic lethality and severely diminished fertility.

Variants

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The viewer provides 23 variants from UniProt as well as other sources including ClinVar and dbSNP.

Go to variant viewer

PTM/Processing

Features

Showing features for modified residue, chain, cross-link.

TypeIDPosition(s)Description
Modified residue1N-acetylmethionine
ChainPRO_00000725211-657THO complex subunit 1
Modified residue2Phosphoserine
Modified residue4Phosphothreonine
Cross-link31Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)
Modified residue133N6-acetyllysine
Modified residue300N6-acetyllysine
Cross-link408Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)
Modified residue537Phosphoserine
Modified residue542Phosphothreonine
Modified residue560Phosphoserine
Cross-link580Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)
Cross-link595Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO1); alternate
Cross-link595Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2); alternate

Post-translational modification

Expression is altered specifically during apoptosis and is accompanied by the appearance of novel forms with smaller apparent molecular mass.
Polyubiquitinated, leading to proteasomal degradation; probably involves NEDD4.

Keywords

Proteomic databases

PTM databases

Expression

Tissue specificity

In the inner ear, specifically expressed in inner and outer hair cells (at protein level).

Developmental stage

Widely expressed during embryonic development.

Gene expression databases

Interaction

Subunit

Component of the THO subcomplex, which is composed of THOC1, THOC2, THOC3, THOC5, THOC6 and THOC7 (By similarity).
The THO subcomplex interacts with DDX39B to form the THO-DDX39B complex which multimerizes into a 28-subunit tetrameric assembly (By similarity).
Component of the transcription/export (TREX) complex at least composed of ALYREF/THOC4, DDX39B, SARNP/CIP29, CHTOP and the THO subcomplex; in the complex interacts with THOC2, THOC5 and THOC7 (By similarity).
TREX seems to have a dynamic structure involving ATP-dependent remodeling (By similarity).
Binds to the hypophosphorylated form of RB1. Interacts with RNA polymerase II. Interacts with LUZP4 (By similarity).
Interacts with THOC5 (PubMed:16909111).

Protein-protein interaction databases

Miscellaneous

Structure

Family & Domains

Features

Showing features for region, motif, compositional bias, domain.

TypeIDPosition(s)Description
Region133-167Dock domain; interaction with THOC2
Region194-221Disordered
Region227-397Dock domain; interaction with THOC2
Motif414-430Nuclear localization signal
Region533-569Disordered
Compositional bias541-555Acidic residues
Domain570-653Death

Domain

An intact death domain is needed for apoptosis.

Sequence similarities

Belongs to the THOC1 family.

Phylogenomic databases

Family and domain databases

Sequence

  • Sequence status
    Complete
  • Length
    657
  • Mass (Da)
    75,436
  • Last updated
    2002-06-01 v1
  • Checksum
    E4235E395B5A82BC
MSPTPALFSLPEARTRFTKSTREALNNKNIKPLLTAFSQLPGSENEKKCTLDQAFRGVLEEEIINHSACENVLAIISLAIGGVTESVCTASTPFVLLGDVLDCLPLDQCDTIFTFVEKNVATWKSNTFYSAGKNYLLRMCNDLLRRLSKSQNTVFCGRIQLFLARLFPLSEKSGLNLQSQFNLENVTVFNTNEQESTLGQKHTEDREEGMDVEEGEMGDDEAPTTCSIPIDYNLYRKFWSLQDYFRNPVQCYEKISWKTFLKYSEEVLAVFKSYKLDDTQASRKKMEELKTGGEHVYFAKFLTSEKLMDLQLSDSNFRRHILLQYLILFQYLKGQVKFKSSNYVLTDEQSLWIEDTTKSVYQLLSENPPDGERFSKMVEHILNTEENWNSWKNEGCPSFVKERASDTKPTRVVRKRAAPEDFLGKGPNKKILIGNEELTRLWNLCPDNMEACKSETREYMPTLEEFFEEAIEQADPENMVESEYKAVNNSNYGWRALRLLARRSPHFFQPTNQQFKSLPEYLENMVIKLAKELPPPSEEIKTGEDEDEEDNDALLKENESPDVRRDKPITGEQIESFANKLGEQWKILAPYLEIKDSDIRQIECDSEDMKMRAKQLLVAWQDQEGVHATTDNLISALNKSGLSDLAESLTNDTETNS

Computationally mapped potential isoform sequences

There is 1 potential isoform mapped to this entry

View all
EntryEntry nameGene nameLength
A0A3Q4EBV8A0A3Q4EBV8_MOUSEThoc1385

Features

Showing features for compositional bias.

TypeIDPosition(s)Description
Compositional bias541-555Acidic residues

Keywords

Sequence databases

Nucleotide SequenceProtein SequenceMolecule TypeStatus
AK031785
EMBL· GenBank· DDBJ
BAC27548.1
EMBL· GenBank· DDBJ
mRNA
AK032200
EMBL· GenBank· DDBJ
BAC27754.1
EMBL· GenBank· DDBJ
mRNA
AK042867
EMBL· GenBank· DDBJ
BAC31387.2
EMBL· GenBank· DDBJ
mRNA
BC024951
EMBL· GenBank· DDBJ
AAH24951.1
EMBL· GenBank· DDBJ
mRNA

Genome annotation databases

Similar Proteins

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