Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.

UniProtKB - Q13769 (THOC5_HUMAN)

(max 400 entries)x

Your basket is currently empty. i

Select item(s) and click on "Add to basket" to create your own collection here
(400 entries max)

Protein

THO complex subunit 5 homolog

Gene

THOC5

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

Functioni

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. THOC5 in conjunction with ALYREF/THOC4 functions in NXF1-NXT1 mediated nuclear export of HSP70 mRNA; both proteins enhance the RNA binding activity of NXF1 and are required for NXF1 localization to the nuclear rim. Involved in transcription elongation and genome stability. Involved in alternative polyadenylation site choice by recruiting CPSF6 to 5' region of target genes; probably mediates association of the TREX and CFIm complexes.
Regulates the expression of myeloid transcription factors CEBPA, CEBPB and GAB2 by enhancing the levels of phosphatidylinositol 3,4,5-trisphosphate. May be involved in the differentiation of granulocytes and adipocytes. Essential for hematopoietic primitive cell survival and plays an integral role in monocytic development.

GO - Molecular functioni

View the complete GO annotation on QuickGO ...

GO - Biological processi

  • monocyte differentiation Source: UniProtKB
  • mRNA 3'-end processing Source: Reactome
  • mRNA export from nucleus Source: UniProtKB
  • negative regulation of DNA damage checkpoint Source: UniProtKB
  • positive regulation of DNA-templated transcription, elongation Source: UniProtKB
  • primitive hemopoiesis Source: UniProtKB
  • RNA export from nucleus Source: Reactome
  • RNA splicing Source: UniProtKB-KW
  • viral mRNA export from host cell nucleus Source: UniProtKB
View the complete GO annotation on QuickGO ...

Keywordsi

Molecular functionRNA-binding
Biological processDifferentiation, mRNA processing, mRNA splicing, mRNA transport, Transport

Enzyme and pathway databases

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
SIGNORiQ13769

Names & Taxonomyi

Protein namesi
Recommended name:
THO complex subunit 5 homolog
Alternative name(s):
Functional spliceosome-associated protein 79
Short name:
fSAP79
NF2/meningioma region protein pK1.3
Placental protein 39.2
Short name:
PP39.2
hTREX90
Gene namesi
Name:THOC5
Synonyms:C22orf19, KIAA0983
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Primates › Haplorrhini › Catarrhini › Hominidae › Homo
Proteomesi
  • UP000005640 Componenti: Chromosome 22

Organism-specific databases

EuPathDBiHostDB:ENSG00000100296.13
HGNCiHGNC:19074 THOC5
MIMi612733 gene
neXtProtiNX_Q13769

Subcellular locationi

Extracellular region or secreted Cytosol Plasma membrane Cytoskeleton Lysosome Endosome Peroxisome ER Golgi apparatus Nucleus Mitochondrion Manual annotation Automatic computational assertionGraphics by Christian Stolte; Source: COMPARTMENTS

Keywords - Cellular componenti

Cytoplasm, Nucleus

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Mutagenesisi225Y → F: Impairs mRNA binding, enhances CXCL12-dependent cell migration. 1 Publication1

Organism-specific databases

DisGeNETi8563
OpenTargetsiENSG00000100296
PharmGKBiPA38188

Polymorphism and mutation databases

BioMutaiTHOC5
DMDMi259016156

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Initiator methionineiRemovedCombined sources
ChainiPRO_00000795772 – 683THO complex subunit 5 homologAdd BLAST682

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei2N-acetylserineCombined sources1
Modified residuei5PhosphoserineBy similarity1
Modified residuei6PhosphoserineBy similarity1
Cross-linki153Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)Combined sources
Modified residuei225Phosphotyrosine; by SRC2 Publications1
Modified residuei307PhosphoserineCombined sources1
Modified residuei312PhosphoserineCombined sources1
Modified residuei314PhosphoserineCombined sources1
Modified residuei328PhosphothreonineCombined sources1

Post-translational modificationi

Phosphorylated on tyrosine upon binding to activated CSF1R; which causes a dissociation of the two proteins. Phosphorylation on Ser-5 and/or Ser-6 is required for nuclear export. Phosphorylated on Thr-328 in insulin-stimulated adipocytes (By similarity). Phosphorylation at Tyr-225 modulates mRNA binding.By similarity2 Publications

Keywords - PTMi

Acetylation, Isopeptide bond, Phosphoprotein, Ubl conjugation

Proteomic databases

EPDiQ13769
MaxQBiQ13769
PaxDbiQ13769
PeptideAtlasiQ13769
PRIDEiQ13769
ProteomicsDBi59680

PTM databases

iPTMnetiQ13769
PhosphoSitePlusiQ13769

Expressioni

Tissue specificityi

Ubiquitously expressed.

Gene expression databases

BgeeiENSG00000100296
CleanExiHS_THOC5
ExpressionAtlasiQ13769 baseline and differential
GenevisibleiQ13769 HS

Organism-specific databases

HPAiHPA048402

Interactioni

Subunit structurei

Interacts with phosphorylated CSF1R (By similarity). 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. Interacts with ALYREF/THOC4, and THOC7. Interacts (via N-terminus) with the NTF2 domain of NXF1. Forms a complex with CEBPB. Interacts with CPSF6; indicative for an association with the cleavage factor Im (CFIm) complex. Interacts with THOC1 (By similarity). Interacts with LUZP4. Interacts with NCBP3 (PubMed:26382858).By similarity8 Publications

Binary interactionsi

Show more details

Protein-protein interaction databases

BioGridi114132, 66 interactors
CORUMiQ13769
IntActiQ13769, 49 interactors
MINTiQ13769
STRINGi9606.ENSP00000380969

Structurei

3D structure databases

ProteinModelPortaliQ13769
SMRiQ13769
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni2 – 199Interaction with THOC71 PublicationAdd BLAST198
Regioni2 – 144Interaction with CSF1RBy similarityAdd BLAST143

Motif

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Motifi7 – 10Nuclear localization signalBy similarity4

Sequence similaritiesi

Belongs to the THOC5 family.Curated

Phylogenomic databases

eggNOGiKOG2216 Eukaryota
ENOG410YCE5 LUCA
GeneTreeiENSGT00390000013777
HOGENOMiHOG000007514
HOVERGENiHBG051271
InParanoidiQ13769
KOiK13174
OMAiECQHLFP
OrthoDBiEOG091G0781
PhylomeDBiQ13769
TreeFamiTF314812

Family and domain databases

InterProiView protein in InterPro
IPR019163 THO_Thoc5
PANTHERiPTHR13375 PTHR13375, 1 hit
PfamiView protein in Pfam
PF09766 FimP, 1 hit

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

Q13769-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MSSESSKKRK PKVIRSDGAP AEGKRNRSDT EQEGKYYSEE AEVDLRDPGR 
        60         70         80         90        100
DYELYKYTCQ ELQRLMAEIQ DLKSRGGKDV AIEIEERRIQ SCVHFMTLKK 
       110        120        130        140        150
LNRLAHIRLK KGRDQTHEAK QKVDAYHLQL QNLLYEVMHL QKEITKCLEF 
       160        170        180        190        200
KSKHEEIDLV SLEEFYKEAP PDISKAEVTM GDPHQQTLAR LDWELEQRKR 
       210        220        230        240        250
LAEKYRECLS NKEKILKEIE VKKEYLSSLQ PRLNSIMQAS LPVQEYLFMP 
       260        270        280        290        300
FDQAHKQYET ARHLPPPLYV LFVQATAYGQ ACDKTLSVAI EGSVDEAKAL 
       310        320        330        340        350
FKPPEDSQDD ESDSDAEEEQ TTKRRRPTLG VQLDDKRKEM LKRHPLSVML 
       360        370        380        390        400
DLKCKDDSVL HLTFYYLMNL NIMTVKAKVT TAMELITPIS AGDLLSPDSV 
       410        420        430        440        450
LSCLYPGDHG KKTPNPANQY QFDKVGILTL SDYVLELGHP YLWVQKLGGL 
       460        470        480        490        500
HFPKEQPQQT VIADHSLSAS HMETTMKLLK TRVQSRLALH KQFASLEHGI 
       510        520        530        540        550
VPVTSDCQYL FPAKVVSRLV KWVTVAHEDY MELHFTKDIV DAGLAGDTNL 
       560        570        580        590        600
YYMALIERGT AKLQAAVVLN PGYSSIPPVF QLCLNWKGEK TNSNDDNIRA 
       610        620        630        640        650
MEGEVNVCYK ELCGPWPSHQ LLTNQLQRLC VLLDVYLETE SHDDSVEGPK 
       660        670        680 
EFPQEKMCLR LFRGPSRMKP FKYNHPQGFF SHR
Length:683
Mass (Da):78,508
Last modified:September 22, 2009 - v2
Checksum:i59550FA548835016
GO

Sequence cautioni

The sequence BAA76827 differs from that shown. Reason: Erroneous initiation. Translation N-terminally shortened.Curated

Natural variant

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Natural variantiVAR_035692380T → K in a breast cancer sample; somatic mutation. 1 Publication1
Natural variantiVAR_037134475T → S. Corresponds to variant dbSNP:rs8141153Ensembl.1
Natural variantiVAR_035693499G → S in a breast cancer sample; somatic mutation. 1 Publication1
Natural variantiVAR_037135525V → I4 PublicationsCorresponds to variant dbSNP:rs737976Ensembl.1
Natural variantiVAR_021410579V → I3 PublicationsCorresponds to variant dbSNP:rs1049534Ensembl.1

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
L18972 Genomic DNA Translation: AAC26837.1
AB023200 mRNA Translation: BAA76827.2 Different initiation.
CR456542 mRNA Translation: CAG30428.1
AC005529 Genomic DNA No translation available.
BC003615 mRNA Translation: AAH03615.1
AJ006069 mRNA Translation: CAA06841.1
CCDSiCCDS13859.1
PIRiI39463
RefSeqiNP_001002877.1, NM_001002877.1
NP_001002878.1, NM_001002878.1
NP_001002879.1, NM_001002879.1
NP_003669.4, NM_003678.4
UniGeneiHs.75361

Genome annotation databases

EnsembliENST00000397871; ENSP00000380969; ENSG00000100296
ENST00000397872; ENSP00000380970; ENSG00000100296
ENST00000397873; ENSP00000380971; ENSG00000100296
ENST00000490103; ENSP00000420306; ENSG00000100296
GeneIDi8563
KEGGihsa:8563
UCSCiuc003afr.4 human

Keywords - Coding sequence diversityi

Polymorphism

Similar proteinsi

Entry informationi

Entry nameiTHOC5_HUMAN
AccessioniPrimary (citable) accession number: Q13769
Secondary accession number(s): O60839, Q9UPZ5
Entry historyiIntegrated into UniProtKB/Swiss-Prot: May 2, 2002
Last sequence update: September 22, 2009
Last modified: June 20, 2018
This is version 145 of the entry and version 2 of the sequence. See 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

Complete proteome, Reference proteome

Documents

  1. Human chromosome 22
    Human chromosome 22: entries, gene names and cross-references to MIM
  2. Human entries with polymorphisms or disease mutations
    List of human entries with polymorphisms or disease mutations
  3. Human polymorphisms and disease mutations
    Index of human polymorphisms and disease mutations
  4. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  5. SIMILARITY comments
    Index of protein domains and families

We'd like to inform you that we have updated our Privacy Notice to comply with Europe’s new General Data Protection Regulation (GDPR) that applies since 25 May 2018.

Do not show this banner again
UniProt is an ELIXIR core data resource
Main funding by: National Institutes of Health