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Protein

THO complex subunit 1

Gene

THOC1

Organism
Homo sapiens (Human)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Required for efficient export of polyadenylated RNA. Acts as 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. 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/NFX1 pathway. The TREX complex is essential for the export of Kaposi's sarcoma-associated herpesvirus (KSHV) intronless mRNAs and infectious virus production. Regulates transcriptional elongation of a subset of genes. Involved in genome stability by preventing co-transcriptional R-loop formation.
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.

GO - Molecular functioni

GO - Biological processi

  • apoptotic process Source: UniProtKB
  • mRNA 3'-end processing Source: Reactome
  • mRNA export from nucleus Source: UniProtKB
  • negative regulation of DNA damage checkpoint Source: UniProtKB
  • negative regulation of isotype switching to IgA isotypes Source: UniProtKB
  • positive regulation of DNA-templated transcription, elongation Source: UniProtKB
  • regulation of DNA recombination Source: UniProtKB
  • regulation of DNA-templated transcription, elongation Source: UniProtKB
  • replication fork processing Source: UniProtKB
  • RNA export from nucleus Source: Reactome
  • RNA processing Source: ProtInc
  • RNA splicing Source: UniProtKB-KW
  • signal transduction Source: InterPro
  • termination of RNA polymerase II transcription Source: Reactome
  • viral mRNA export from host cell nucleus Source: UniProtKB
Complete GO annotation...

Keywords - Biological processi

Apoptosis, mRNA processing, mRNA splicing, mRNA transport, Transcription, Transcription regulation, Transport

Keywords - Ligandi

DNA-binding, RNA-binding

Enzyme and pathway databases

BioCyciZFISH:ENSG00000079134-MONOMER.
ReactomeiR-HSA-109688. Cleavage of Growing Transcript in the Termination Region.
R-HSA-159236. Transport of Mature mRNA derived from an Intron-Containing Transcript.
R-HSA-72187. mRNA 3'-end processing.

Names & Taxonomyi

Protein namesi
Recommended name:
THO complex subunit 1
Short name:
Tho1
Alternative name(s):
Nuclear matrix protein p84
Short name:
p84N5
hTREX84
Gene namesi
Name:THOC1
Synonyms:HPR1
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
Proteomesi
  • UP000005640 Componenti: Chromosome 18

Organism-specific databases

HGNCiHGNC:19070. THOC1.

Subcellular locationi

Isoform 1 :

GO - Cellular componenti

  • cytoplasm Source: UniProtKB
  • intercellular bridge Source: HPA
  • nuclear matrix Source: UniProtKB-SubCell
  • nuclear speck Source: UniProtKB-SubCell
  • nucleoplasm Source: HPA
  • nucleus Source: UniProtKB
  • THO complex Source: UniProtKB
  • THO complex part of transcription export complex Source: UniProtKB
  • transcription export complex Source: UniProtKB
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm, Nucleus

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Mutagenesisi617L → P: Loss of ability to induce apoptosis. Interferes with normal response of SaOS-2 cells to radiation. 1 Publication1
Mutagenesisi620W → P or R: Loss of ability to induce apoptosis. Interferes with normal response of SaOS-2 cells to radiation. 1 Publication1

Organism-specific databases

DisGeNETi9984.
OpenTargetsiENSG00000079134.
PharmGKBiPA134887435.

Polymorphism and mutation databases

BioMutaiTHOC1.
DMDMi37999906.

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00000725201 – 657THO complex subunit 1Add BLAST657

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei1N-acetylmethionineCombined sources1
Modified residuei2PhosphoserineCombined sources1
Modified residuei4PhosphothreonineCombined sources1
Cross-linki31Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)Combined sources
Modified residuei133N6-acetyllysineCombined sources1
Modified residuei300N6-acetyllysineCombined sources1
Cross-linki408Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)Combined sources
Modified residuei537PhosphoserineCombined sources1
Modified residuei542PhosphothreonineCombined sources1
Modified residuei560PhosphoserineCombined sources1
Cross-linki595Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO1)Combined sources
Cross-linki595Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)Combined sources

Post-translational modificationi

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 NEDD4.1 Publication

Keywords - PTMi

Acetylation, Isopeptide bond, Phosphoprotein, Ubl conjugation

Proteomic databases

EPDiQ96FV9.
MaxQBiQ96FV9.
PaxDbiQ96FV9.
PeptideAtlasiQ96FV9.
PRIDEiQ96FV9.

PTM databases

iPTMnetiQ96FV9.
PhosphoSitePlusiQ96FV9.

Expressioni

Tissue specificityi

Ubiquitous. Expressed in various cancer cell lines. Expressed at very low levels in normal breast epithelial cells and highly expressed in breast tumors. Expression is strongly associated with an aggressive phenotype of breast tumors and expression correlates with tumor size and the metastatic state of the tumor progression.2 Publications

Inductioni

Up-regulated during cell proliferation.1 Publication

Gene expression databases

BgeeiENSG00000079134.
CleanExiHS_THOC1.
ExpressionAtlasiQ96FV9. baseline and differential.
GenevisibleiQ96FV9. HS.

Organism-specific databases

HPAiHPA019096.
HPA019687.

Interactioni

Subunit structurei

Component of the THO complex, which is composed of THOC1, THOC2, THOC3, THOC5, THOC6 and THOC7; together with at least ALYREF/THOC4, DDX39B, SARNP/CIP29 and CHTOP, THO forms the transcription/export (TREX) complex which seems to have a dynamic structure involving ATP-dependent remodeling. Binds to the hypophosphorylated form of RB1. Interacts with THOC2, DDX39B and RNA polymerase II. Interacts with THOC5 (By similarity). Interacts with LUZP4.By similarity6 Publications

Binary interactionsi

WithEntry#Exp.IntActNotes
MOAP1Q96BY25EBI-1765605,EBI-739825
RABGEF1Q9UJ413EBI-1765605,EBI-913954
THOC5Q137699EBI-1765605,EBI-5280316
TRIM54Q9BYV23EBI-1765605,EBI-2130429
USHBP1Q8N6Y03EBI-1765605,EBI-739895

Protein-protein interaction databases

BioGridi115305. 87 interactors.
IntActiQ96FV9. 77 interactors.
MINTiMINT-4536762.
STRINGi9606.ENSP00000261600.

Structurei

Secondary structure

1657
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Beta strandi565 – 567Combined sources3
Helixi571 – 581Combined sources11
Turni582 – 584Combined sources3
Helixi585 – 588Combined sources4
Turni589 – 593Combined sources5
Helixi596 – 605Combined sources10
Helixi609 – 624Combined sources16
Helixi625 – 627Combined sources3
Helixi630 – 639Combined sources10
Helixi643 – 650Combined sources8

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1WXPNMR-A561-657[»]
ProteinModelPortaliQ96FV9.
SMRiQ96FV9.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiQ96FV9.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Domaini570 – 653DeathPROSITE-ProRule annotationAdd BLAST84

Motif

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Motifi414 – 430Nuclear localization signal1 PublicationAdd BLAST17

Domaini

An intact death domain is needed for apoptosis.1 Publication

Sequence similaritiesi

Contains 1 death domain.PROSITE-ProRule annotation

Phylogenomic databases

eggNOGiKOG2491. Eukaryota.
ENOG410XQEX. LUCA.
GeneTreeiENSGT00390000016232.
HOGENOMiHOG000008123.
HOVERGENiHBG060294.
InParanoidiQ96FV9.
KOiK12878.
OMAiQACKSEQ.
PhylomeDBiQ96FV9.
TreeFamiTF314796.

Family and domain databases

Gene3Di1.10.533.10. 1 hit.
InterProiIPR011029. DEATH-like_dom.
IPR000488. Death_domain.
IPR021861. THO_THOC1.
[Graphical view]
PfamiPF00531. Death. 1 hit.
PF11957. efThoc1. 1 hit.
[Graphical view]
SMARTiSM00005. DEATH. 1 hit.
[Graphical view]
SUPFAMiSSF47986. SSF47986. 1 hit.
PROSITEiPS50017. DEATH_DOMAIN. 1 hit.
[Graphical view]

Sequences (2)i

Sequence statusi: Complete.

This entry describes 2 isoformsi produced by alternative splicing. AlignAdd to basket

Isoform 1 (identifier: Q96FV9-1) [UniParc]FASTAAdd to basket

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.

« Hide

        10         20         30         40         50
MSPTPPLFSL PEARTRFTKS TREALNNKNI KPLLSTFSQV PGSENEKKCT
60 70 80 90 100
LDQAFRGILE EEIINHSSCE NVLAIISLAI GGVTEGICTA STPFVLLGDV
110 120 130 140 150
LDCLPLDQCD TIFTFVEKNV ATWKSNTFYS AGKNYLLRMC NDLLRRLSKS
160 170 180 190 200
QNTVFCGRIQ LFLARLFPLS EKSGLNLQSQ FNLENVTVFN TNEQESTLGQ
210 220 230 240 250
KHTEDREEGM DVEEGEMGDE EAPTTCSIPI DYNLYRKFWS LQDYFRNPVQ
260 270 280 290 300
CYEKISWKTF LKYSEEVLAV FKSYKLDDTQ ASRKKMEELK TGGEHVYFAK
310 320 330 340 350
FLTSEKLMDL QLSDSNFRRH ILLQYLILFQ YLKGQVKFKS SNYVLTDEQS
360 370 380 390 400
LWIEDTTKSV YQLLSENPPD GERFSKMVEH ILNTEENWNS WKNEGCPSFV
410 420 430 440 450
KERTSDTKPT RIIRKRTAPE DFLGKGPTKK ILMGNEELTR LWNLCPDNME
460 470 480 490 500
ACKSETREHM PTLEEFFEEA IEQADPENMV ENEYKAVNNS NYGWRALRLL
510 520 530 540 550
ARRSPHFFQP TNQQFKSLPE YLENMVIKLA KELPPPSEEI KTGEDEDEED
560 570 580 590 600
NDALLKENES PDVRRDKPVT GEQIEVFANK LGEQWKILAP YLEMKDSEIR
610 620 630 640 650
QIECDSEDMK MRAKQLLVAW QDQEGVHATP ENLINALNKS GLSDLAESLT

NDNETNS
Length:657
Mass (Da):75,666
Last modified:December 1, 2001 - v1
Checksum:iDB7980BD0F252DAB
GO
Isoform 2 (identifier: Q96FV9-2) [UniParc]FASTAAdd to basket
Also known as: p84N5s

The sequence of this isoform differs from the canonical sequence as follows:
     363-377: LLSENPPDGERFSKM → VSSTRNKPMIEKMEI
     378-657: Missing.

Note: May be due to an intron retention.
Show »
Length:377
Mass (Da):43,359
Checksum:i313FCF7E19C03FFC
GO

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sequence conflicti71N → H in AAT81408 (PubMed:15358532).Curated1
Sequence conflicti86G → A in AAT81408 (PubMed:15358532).Curated1
Sequence conflicti130S → A in AAA53571 (PubMed:7525595).Curated1
Sequence conflicti134N → S in BAG37293 (PubMed:14702039).Curated1
Sequence conflicti433M → T in AAA53571 (PubMed:7525595).Curated1
Sequence conflicti480V → A in AAA53571 (PubMed:7525595).Curated1
Sequence conflicti487V → M in AAA53571 (PubMed:7525595).Curated1
Sequence conflicti498R → K in AAA53571 (PubMed:7525595).Curated1
Sequence conflicti519P → Q in AAA53571 (PubMed:7525595).Curated1

Alternative sequence

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Alternative sequenceiVSP_038073363 – 377LLSEN…RFSKM → VSSTRNKPMIEKMEI in isoform 2. 1 PublicationAdd BLAST15
Alternative sequenceiVSP_038074378 – 657Missing in isoform 2. 1 PublicationAdd BLAST280

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
L36529 mRNA. Translation: AAA53571.1.
AY573302 mRNA. Translation: AAT81408.1.
AY573303 mRNA. Translation: AAT81409.1.
AK314755 mRNA. Translation: BAG37293.1.
AP000845 Genomic DNA. No translation available.
CH471113 Genomic DNA. Translation: EAX01732.1.
BC010381 mRNA. Translation: AAH10381.1.
CCDSiCCDS45820.1. [Q96FV9-1]
PIRiA53545.
RefSeqiNP_005122.2. NM_005131.2. [Q96FV9-1]
UniGeneiHs.712543.

Genome annotation databases

EnsembliENST00000261600; ENSP00000261600; ENSG00000079134. [Q96FV9-1]
GeneIDi9984.
KEGGihsa:9984.
UCSCiuc002kkj.5. human. [Q96FV9-1]

Keywords - Coding sequence diversityi

Alternative splicing

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
L36529 mRNA. Translation: AAA53571.1.
AY573302 mRNA. Translation: AAT81408.1.
AY573303 mRNA. Translation: AAT81409.1.
AK314755 mRNA. Translation: BAG37293.1.
AP000845 Genomic DNA. No translation available.
CH471113 Genomic DNA. Translation: EAX01732.1.
BC010381 mRNA. Translation: AAH10381.1.
CCDSiCCDS45820.1. [Q96FV9-1]
PIRiA53545.
RefSeqiNP_005122.2. NM_005131.2. [Q96FV9-1]
UniGeneiHs.712543.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1WXPNMR-A561-657[»]
ProteinModelPortaliQ96FV9.
SMRiQ96FV9.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi115305. 87 interactors.
IntActiQ96FV9. 77 interactors.
MINTiMINT-4536762.
STRINGi9606.ENSP00000261600.

PTM databases

iPTMnetiQ96FV9.
PhosphoSitePlusiQ96FV9.

Polymorphism and mutation databases

BioMutaiTHOC1.
DMDMi37999906.

Proteomic databases

EPDiQ96FV9.
MaxQBiQ96FV9.
PaxDbiQ96FV9.
PeptideAtlasiQ96FV9.
PRIDEiQ96FV9.

Protocols and materials databases

DNASUi9984.
Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000261600; ENSP00000261600; ENSG00000079134. [Q96FV9-1]
GeneIDi9984.
KEGGihsa:9984.
UCSCiuc002kkj.5. human. [Q96FV9-1]

Organism-specific databases

CTDi9984.
DisGeNETi9984.
GeneCardsiTHOC1.
HGNCiHGNC:19070. THOC1.
HPAiHPA019096.
HPA019687.
MIMi606930. gene.
neXtProtiNX_Q96FV9.
OpenTargetsiENSG00000079134.
PharmGKBiPA134887435.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiKOG2491. Eukaryota.
ENOG410XQEX. LUCA.
GeneTreeiENSGT00390000016232.
HOGENOMiHOG000008123.
HOVERGENiHBG060294.
InParanoidiQ96FV9.
KOiK12878.
OMAiQACKSEQ.
PhylomeDBiQ96FV9.
TreeFamiTF314796.

Enzyme and pathway databases

BioCyciZFISH:ENSG00000079134-MONOMER.
ReactomeiR-HSA-109688. Cleavage of Growing Transcript in the Termination Region.
R-HSA-159236. Transport of Mature mRNA derived from an Intron-Containing Transcript.
R-HSA-72187. mRNA 3'-end processing.

Miscellaneous databases

ChiTaRSiTHOC1. human.
EvolutionaryTraceiQ96FV9.
GeneWikiiTHOC1.
GenomeRNAii9984.
PROiQ96FV9.
SOURCEiSearch...

Gene expression databases

BgeeiENSG00000079134.
CleanExiHS_THOC1.
ExpressionAtlasiQ96FV9. baseline and differential.
GenevisibleiQ96FV9. HS.

Family and domain databases

Gene3Di1.10.533.10. 1 hit.
InterProiIPR011029. DEATH-like_dom.
IPR000488. Death_domain.
IPR021861. THO_THOC1.
[Graphical view]
PfamiPF00531. Death. 1 hit.
PF11957. efThoc1. 1 hit.
[Graphical view]
SMARTiSM00005. DEATH. 1 hit.
[Graphical view]
SUPFAMiSSF47986. SSF47986. 1 hit.
PROSITEiPS50017. DEATH_DOMAIN. 1 hit.
[Graphical view]
ProtoNetiSearch...

Entry informationi

Entry nameiTHOC1_HUMAN
AccessioniPrimary (citable) accession number: Q96FV9
Secondary accession number(s): B2RBP6
, Q15219, Q64I72, Q64I73
Entry historyi
Integrated into UniProtKB/Swiss-Prot: October 10, 2003
Last sequence update: December 1, 2001
Last modified: November 30, 2016
This is version 144 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

Documents

  1. Human chromosome 18
    Human chromosome 18: entries, gene names and cross-references to MIM
  2. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  3. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  4. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.