Q96FV9 · THOC1_HUMAN
- 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
Required for efficient export of polyadenylated RNA (PubMed:23222130).
The THOC1-THOC2-THOC3 core complex alone is sufficient to bind export factor NXF1-NXT1 and promote ATPase activity of DDX39B/UAP56 (PubMed:33191911).
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 (PubMed:15833825, PubMed:15998806, PubMed:17190602).
Regulates transcriptional elongation of a subset of genes (PubMed:22144908).
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).
GO annotations
Aspect | Term | |
---|---|---|
Cellular Component | cytoplasm | |
Cellular Component | nuclear matrix | |
Cellular Component | nuclear speck | |
Cellular Component | nucleoplasm | |
Cellular Component | nucleus | |
Cellular Component | THO complex | |
Cellular Component | THO complex part of transcription export complex | |
Cellular Component | 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
Protein family/group databases
Names & Taxonomy
Protein names
- Recommended nameTHO complex subunit 1
- Alternative names
Gene names
Organism names
- Organism
- Taxonomic lineageEukaryota > Metazoa > Chordata > Craniata > Vertebrata > Euteleostomi > Mammalia > Eutheria > Euarchontoglires > Primates > Haplorrhini > Catarrhini > Hominidae > Homo
Accessions
- Primary accessionQ96FV9
- Secondary accessions
Proteomes
Organism-specific databases
Subcellular Location
Isoform 1
Isoform 2
Keywords
- Cellular component
Disease & Variants
Involvement in disease
Deafness, autosomal dominant, 86 (DFNA86)
- Note
- DescriptionA form of non-syndromic, sensorineural hearing loss. Sensorineural hearing loss results from damage to the neural receptors of the inner ear, the nerve pathways to the brain, or the area of the brain that receives sound information. DFNA86 is characterized by progressive, bilateral hearing loss that is most predominant in the high frequencies, begins mildly during the fourth decade and gradually progresses to severe-to-profound deafness in the seventh and eighth decades. Affected subjects have tinnitus, while vestibular dysfunction or other clinical abnormalities are not present.
- See alsoMIM:620280
Natural variants in DFNA86
Variant ID | Position(s) | Change | Description | |
---|---|---|---|---|
VAR_088179 | 183 | L>V | in DFNA86; impaired function in hair cell formation, when tested in a heterologous system |
Features
Showing features for natural variant, mutagenesis.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Natural variant | VAR_088179 | 183 | in DFNA86; impaired function in hair cell formation, when tested in a heterologous system | |||
Sequence: L → V | ||||||
Mutagenesis | 617 | Loss of ability to induce apoptosis. Interferes with normal response of SaOS-2 cells to radiation. | ||||
Sequence: L → P | ||||||
Mutagenesis | 620 | Loss of ability to induce apoptosis. Interferes with normal response of SaOS-2 cells to radiation. | ||||
Sequence: W → P or R |
Variants
We now provide the "Disease & Variants" viewer in its own tab.
The viewer provides 504 variants from UniProt as well as other sources including ClinVar and dbSNP.
Keywords
- Disease
Organism-specific databases
Miscellaneous
Genetic variation databases
PTM/Processing
Features
Showing features for modified residue, chain, modified residue (large scale data), cross-link.
Type | ID | Position(s) | Source | Description | |||
---|---|---|---|---|---|---|---|
Modified residue | 1 | UniProt | N-acetylmethionine | ||||
Sequence: M | |||||||
Chain | PRO_0000072520 | 1-657 | UniProt | THO complex subunit 1 | |||
Sequence: MSPTPPLFSLPEARTRFTKSTREALNNKNIKPLLSTFSQVPGSENEKKCTLDQAFRGILEEEIINHSSCENVLAIISLAIGGVTEGICTASTPFVLLGDVLDCLPLDQCDTIFTFVEKNVATWKSNTFYSAGKNYLLRMCNDLLRRLSKSQNTVFCGRIQLFLARLFPLSEKSGLNLQSQFNLENVTVFNTNEQESTLGQKHTEDREEGMDVEEGEMGDEEAPTTCSIPIDYNLYRKFWSLQDYFRNPVQCYEKISWKTFLKYSEEVLAVFKSYKLDDTQASRKKMEELKTGGEHVYFAKFLTSEKLMDLQLSDSNFRRHILLQYLILFQYLKGQVKFKSSNYVLTDEQSLWIEDTTKSVYQLLSENPPDGERFSKMVEHILNTEENWNSWKNEGCPSFVKERTSDTKPTRIIRKRTAPEDFLGKGPTKKILMGNEELTRLWNLCPDNMEACKSETREHMPTLEEFFEEAIEQADPENMVENEYKAVNNSNYGWRALRLLARRSPHFFQPTNQQFKSLPEYLENMVIKLAKELPPPSEEIKTGEDEDEEDNDALLKENESPDVRRDKPVTGEQIEVFANKLGEQWKILAPYLEMKDSEIRQIECDSEDMKMRAKQLLVAWQDQEGVHATPENLINALNKSGLSDLAESLTNDNETNS | |||||||
Modified residue | 2 | UniProt | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 2 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue | 4 | UniProt | Phosphothreonine | ||||
Sequence: T | |||||||
Modified residue (large scale data) | 4 | PRIDE | Phosphothreonine | ||||
Sequence: T | |||||||
Cross-link | 31 | UniProt | Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2) | ||||
Sequence: K | |||||||
Modified residue | 133 | UniProt | N6-acetyllysine | ||||
Sequence: K | |||||||
Modified residue | 300 | UniProt | N6-acetyllysine | ||||
Sequence: K | |||||||
Cross-link | 408 | UniProt | Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2) | ||||
Sequence: K | |||||||
Modified residue | 537 | UniProt | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 537 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue | 542 | UniProt | Phosphothreonine | ||||
Sequence: T | |||||||
Modified residue (large scale data) | 542 | PRIDE | Phosphothreonine | ||||
Sequence: T | |||||||
Modified residue | 560 | UniProt | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 560 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Cross-link | 580 | UniProt | Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2) | ||||
Sequence: K | |||||||
Cross-link | 595 | UniProt | Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO1); alternate | ||||
Sequence: K | |||||||
Cross-link | 595 | UniProt | Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2); alternate | ||||
Sequence: K | |||||||
Modified residue (large scale data) | 640 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 657 | PRIDE | Phosphoserine | ||||
Sequence: S |
Post-translational modification
Keywords
- PTM
Proteomic databases
PTM databases
Expression
Tissue specificity
Induction
Gene expression databases
Organism-specific databases
Interaction
Subunit
The THO subcomplex interacts with DDX39B to form the THO-DDX39B complex which multimerizes into a 28-subunit tetrameric assembly (PubMed:33191911, PubMed:37020021).
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 (PubMed:33191911, PubMed:37020021).
TREX seems to have a dynamic structure involving ATP-dependent remodeling (PubMed:23222130, PubMed:37020021).
Binds to the hypophosphorylated form of RB1. Interacts with RNA polymerase II. Interacts with LUZP4
Binary interactions
Type | Entry 1 | Entry 2 | Number of experiments | Intact | |
---|---|---|---|---|---|
BINARY | Q96FV9 | AGR2 O95994 | 3 | EBI-1765605, EBI-712648 | |
BINARY | Q96FV9 | AKAP9 Q6PJH3 | 3 | EBI-1765605, EBI-11745576 | |
BINARY | Q96FV9 | CTAG1B P78358 | 3 | EBI-1765605, EBI-1188472 | |
BINARY | Q96FV9 | EXOC5 O00471 | 3 | EBI-1765605, EBI-949824 | |
BINARY | Q96FV9 | GPRASP3 Q6PI77 | 3 | EBI-1765605, EBI-11519926 | |
BINARY | Q96FV9 | MAGEB4 O15481 | 3 | EBI-1765605, EBI-751857 | |
BINARY | Q96FV9 | MOAP1 Q96BY2 | 7 | EBI-1765605, EBI-739825 | |
BINARY | Q96FV9 | PAX6 P26367 | 3 | EBI-1765605, EBI-747278 | |
BINARY | Q96FV9 | PPP1R12C Q9BZL4 | 3 | EBI-1765605, EBI-721802 | |
BINARY | Q96FV9 | RABGEF1 Q9UJ41 | 3 | EBI-1765605, EBI-913954 | |
BINARY | Q96FV9 | REL Q04864-2 | 3 | EBI-1765605, EBI-10829018 | |
BINARY | Q96FV9 | TADA2A O75478 | 3 | EBI-1765605, EBI-742268 | |
BINARY | Q96FV9 | THOC5 Q13769 | 12 | EBI-1765605, EBI-5280316 | |
BINARY | Q96FV9 | TRIM27 P14373 | 3 | EBI-1765605, EBI-719493 | |
BINARY | Q96FV9 | TRIM54 Q9BYV2 | 3 | EBI-1765605, EBI-2130429 | |
BINARY | Q96FV9 | USHBP1 Q8N6Y0 | 3 | EBI-1765605, EBI-739895 | |
BINARY | Q96FV9 | ZMYND12 Q9H0C1 | 3 | EBI-1765605, EBI-12030590 |
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 | 194-222 | Disordered | ||||
Sequence: QESTLGQKHTEDREEGMDVEEGEMGDEEA | ||||||
Region | 227-397 | Dock domain; interaction with THOC2 | ||||
Sequence: SIPIDYNLYRKFWSLQDYFRNPVQCYEKISWKTFLKYSEEVLAVFKSYKLDDTQASRKKMEELKTGGEHVYFAKFLTSEKLMDLQLSDSNFRRHILLQYLILFQYLKGQVKFKSSNYVLTDEQSLWIEDTTKSVYQLLSENPPDGERFSKMVEHILNTEENWNSWKNEGCP | ||||||
Motif | 414-430 | Nuclear localization signal | ||||
Sequence: RKRTAPEDFLGKGPTKK | ||||||
Region | 533-569 | Disordered | ||||
Sequence: LPPPSEEIKTGEDEDEEDNDALLKENESPDVRRDKPV | ||||||
Compositional bias | 541-555 | Acidic residues | ||||
Sequence: KTGEDEDEEDNDALL | ||||||
Domain | 570-653 | Death | ||||
Sequence: TGEQIEVFANKLGEQWKILAPYLEMKDSEIRQIECDSEDMKMRAKQLLVAWQDQEGVHATPENLINALNKSGLSDLAESLTNDN |
Domain
Sequence similarities
Phylogenomic databases
Family and domain databases
Sequence & Isoform
- Sequence statusComplete
This entry describes 2 isoforms produced by Alternative splicing.
Q96FV9-1
This isoform has been chosen as the canonical sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.
- Name1
- Length657
- Mass (Da)75,666
- Last updated2001-12-01 v1
- ChecksumDB7980BD0F252DAB
Q96FV9-2
- Name2
- Synonymsp84N5s
- NoteMay be due to an intron retention.
Computationally mapped potential isoform sequences
There are 5 potential isoforms mapped to this entry
Features
Showing features for sequence conflict, alternative sequence, compositional bias.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Sequence conflict | 71 | in Ref. 2; AAT81408 | ||||
Sequence: N → H | ||||||
Sequence conflict | 86 | in Ref. 2; AAT81408 | ||||
Sequence: G → A | ||||||
Sequence conflict | 130 | in Ref. 1; AAA53571 | ||||
Sequence: S → A | ||||||
Sequence conflict | 134 | in Ref. 3; BAG37293 | ||||
Sequence: N → S | ||||||
Alternative sequence | VSP_038073 | 363-377 | in isoform 2 | |||
Sequence: LLSENPPDGERFSKM → VSSTRNKPMIEKMEI | ||||||
Alternative sequence | VSP_038074 | 378-657 | in isoform 2 | |||
Sequence: Missing | ||||||
Sequence conflict | 433 | in Ref. 1; AAA53571 | ||||
Sequence: M → T | ||||||
Sequence conflict | 480 | in Ref. 1; AAA53571 | ||||
Sequence: V → A | ||||||
Sequence conflict | 487 | in Ref. 1; AAA53571 | ||||
Sequence: V → M | ||||||
Sequence conflict | 498 | in Ref. 1; AAA53571 | ||||
Sequence: R → K | ||||||
Sequence conflict | 519 | in Ref. 1; AAA53571 | ||||
Sequence: P → Q | ||||||
Compositional bias | 541-555 | Acidic residues | ||||
Sequence: KTGEDEDEEDNDALL |
Keywords
- Coding sequence diversity
- Technical term
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
L36529 EMBL· GenBank· DDBJ | AAA53571.1 EMBL· GenBank· DDBJ | mRNA | ||
AY573302 EMBL· GenBank· DDBJ | AAT81408.1 EMBL· GenBank· DDBJ | mRNA | ||
AY573303 EMBL· GenBank· DDBJ | AAT81409.1 EMBL· GenBank· DDBJ | mRNA | ||
AK314755 EMBL· GenBank· DDBJ | BAG37293.1 EMBL· GenBank· DDBJ | mRNA | ||
AP000845 EMBL· GenBank· DDBJ | - | Genomic DNA | No translation available. | |
CH471113 EMBL· GenBank· DDBJ | EAX01732.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
BC010381 EMBL· GenBank· DDBJ | AAH10381.1 EMBL· GenBank· DDBJ | mRNA |