Q8R3N6 · THOC1_MOUSE
- ProteinTHO complex subunit 1
- GeneThoc1
- StatusUniProtKB reviewed (Swiss-Prot)
- Organism
- Amino acids657 (go to sequence)
- Protein existenceEvidence at protein level
- Annotation score5/5
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).
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
Essential for early embryonic development. Required for normal gene expression during postnatal testis development
GO annotations
Aspect | Term | |
---|---|---|
Cellular Component | chromosome, telomeric region | |
Cellular Component | cytosol | |
Cellular Component | nuclear matrix | |
Cellular Component | nuclear speck | |
Cellular Component | THO complex part of transcription export complex | |
Molecular Function | DNA binding | |
Molecular Function | RNA binding | |
Biological Process | apoptotic process | |
Biological Process | mRNA export from nucleus | |
Biological Process | mRNA processing | |
Biological Process | RNA splicing | |
Biological Process | signal transduction |
Keywords
- Molecular function
- Biological process
Enzyme and pathway databases
Names & Taxonomy
Protein names
- Recommended nameTHO complex subunit 1
- Alternative names
Gene names
Organism names
- Organism
- Strains
- Taxonomic lineageEukaryota > Metazoa > Chordata > Craniata > Vertebrata > Euteleostomi > Mammalia > Eutheria > Euarchontoglires > Glires > Rodentia > Myomorpha > Muroidea > Muridae > Murinae > Mus > Mus
Accessions
- Primary accessionQ8R3N6
- Secondary accessions
Proteomes
Organism-specific databases
Subcellular Location
UniProt Annotation
GO Annotation
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).
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
- Cellular component
Phenotypes & Variants
Disruption phenotype
Mice show early embryonic lethality and severely diminished fertility.
Variants
We now provide the "Disease & Variants" viewer in its own tab.
The viewer provides 23 variants from UniProt as well as other sources including ClinVar and dbSNP.
PTM/Processing
Features
Showing features for modified residue, chain, cross-link.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Modified residue | 1 | N-acetylmethionine | ||||
Sequence: M | ||||||
Chain | PRO_0000072521 | 1-657 | THO complex subunit 1 | |||
Sequence: MSPTPALFSLPEARTRFTKSTREALNNKNIKPLLTAFSQLPGSENEKKCTLDQAFRGVLEEEIINHSACENVLAIISLAIGGVTESVCTASTPFVLLGDVLDCLPLDQCDTIFTFVEKNVATWKSNTFYSAGKNYLLRMCNDLLRRLSKSQNTVFCGRIQLFLARLFPLSEKSGLNLQSQFNLENVTVFNTNEQESTLGQKHTEDREEGMDVEEGEMGDDEAPTTCSIPIDYNLYRKFWSLQDYFRNPVQCYEKISWKTFLKYSEEVLAVFKSYKLDDTQASRKKMEELKTGGEHVYFAKFLTSEKLMDLQLSDSNFRRHILLQYLILFQYLKGQVKFKSSNYVLTDEQSLWIEDTTKSVYQLLSENPPDGERFSKMVEHILNTEENWNSWKNEGCPSFVKERASDTKPTRVVRKRAAPEDFLGKGPNKKILIGNEELTRLWNLCPDNMEACKSETREYMPTLEEFFEEAIEQADPENMVESEYKAVNNSNYGWRALRLLARRSPHFFQPTNQQFKSLPEYLENMVIKLAKELPPPSEEIKTGEDEDEEDNDALLKENESPDVRRDKPITGEQIESFANKLGEQWKILAPYLEIKDSDIRQIECDSEDMKMRAKQLLVAWQDQEGVHATTDNLISALNKSGLSDLAESLTNDTETNS | ||||||
Modified residue | 2 | Phosphoserine | ||||
Sequence: S | ||||||
Modified residue | 4 | Phosphothreonine | ||||
Sequence: T | ||||||
Cross-link | 31 | Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2) | ||||
Sequence: K | ||||||
Modified residue | 133 | N6-acetyllysine | ||||
Sequence: K | ||||||
Modified residue | 300 | N6-acetyllysine | ||||
Sequence: K | ||||||
Cross-link | 408 | Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2) | ||||
Sequence: K | ||||||
Modified residue | 537 | Phosphoserine | ||||
Sequence: S | ||||||
Modified residue | 542 | Phosphothreonine | ||||
Sequence: T | ||||||
Modified residue | 560 | Phosphoserine | ||||
Sequence: S | ||||||
Cross-link | 580 | Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2) | ||||
Sequence: K | ||||||
Cross-link | 595 | Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO1); alternate | ||||
Sequence: K | ||||||
Cross-link | 595 | Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2); alternate | ||||
Sequence: K |
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
- PTM
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).
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.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Region | 133-167 | Dock domain; interaction with THOC2 | ||||
Sequence: KNYLLRMCNDLLRRLSKSQNTVFCGRIQLFLARLF | ||||||
Region | 194-221 | Disordered | ||||
Sequence: QESTLGQKHTEDREEGMDVEEGEMGDDE | ||||||
Region | 227-397 | Dock domain; interaction with THOC2 | ||||
Sequence: SIPIDYNLYRKFWSLQDYFRNPVQCYEKISWKTFLKYSEEVLAVFKSYKLDDTQASRKKMEELKTGGEHVYFAKFLTSEKLMDLQLSDSNFRRHILLQYLILFQYLKGQVKFKSSNYVLTDEQSLWIEDTTKSVYQLLSENPPDGERFSKMVEHILNTEENWNSWKNEGCP | ||||||
Motif | 414-430 | Nuclear localization signal | ||||
Sequence: RKRAAPEDFLGKGPNKK | ||||||
Region | 533-569 | Disordered | ||||
Sequence: LPPPSEEIKTGEDEDEEDNDALLKENESPDVRRDKPI | ||||||
Compositional bias | 541-555 | Acidic residues | ||||
Sequence: KTGEDEDEEDNDALL | ||||||
Domain | 570-653 | Death | ||||
Sequence: TGEQIESFANKLGEQWKILAPYLEIKDSDIRQIECDSEDMKMRAKQLLVAWQDQEGVHATTDNLISALNKSGLSDLAESLTNDT |
Domain
An intact death domain is needed for apoptosis.
Sequence similarities
Belongs to the THOC1 family.
Phylogenomic databases
Family and domain databases
Sequence
- Sequence statusComplete
- Length657
- Mass (Da)75,436
- Last updated2002-06-01 v1
- ChecksumE4235E395B5A82BC
Computationally mapped potential isoform sequences
There is 1 potential isoform mapped to this entry
Entry | Entry name | Gene name | Length | ||
---|---|---|---|---|---|
A0A3Q4EBV8 | A0A3Q4EBV8_MOUSE | Thoc1 | 385 |
Features
Showing features for compositional bias.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Compositional bias | 541-555 | Acidic residues | ||||
Sequence: KTGEDEDEEDNDALL |
Keywords
- Technical term
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
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 |