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Protein

THO complex subunit 5 homolog

Gene

THOC5

Organism
Homo sapiens (Human)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-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

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
  • termination of RNA polymerase II transcription Source: Reactome
  • viral mRNA export from host cell nucleus Source: UniProtKB
Complete GO annotation...

Keywords - Biological processi

Differentiation, mRNA processing, mRNA splicing, mRNA transport, Transport

Keywords - Ligandi

RNA-binding

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 lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
Proteomesi
  • UP000005640 Componenti: Chromosome 22

Organism-specific databases

HGNCiHGNC:19074. THOC5.

Subcellular locationi

GO - Cellular componenti

  • cytoplasm 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)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi225 – 2251Y → F: Impairs mRNA binding, enhances CXCL12-dependent cell migration. 1 Publication

Organism-specific databases

PharmGKBiPA38188.

Polymorphism and mutation databases

BioMutaiTHOC5.
DMDMi259016156.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Initiator methionineiRemovedCombined sources
Chaini2 – 683682THO complex subunit 5 homologPRO_0000079577Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei2 – 21N-acetylserineCombined sources
Modified residuei225 – 2251Phosphotyrosine; by SRC2 Publications
Modified residuei307 – 3071PhosphoserineCombined sources
Modified residuei312 – 3121PhosphoserineCombined sources
Modified residuei314 – 3141PhosphoserineCombined sources
Modified residuei328 – 3281PhosphothreonineCombined sources

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, Phosphoprotein

Proteomic databases

EPDiQ13769.
MaxQBiQ13769.
PaxDbiQ13769.
PeptideAtlasiQ13769.
PRIDEiQ13769.

PTM databases

iPTMnetiQ13769.
PhosphoSiteiQ13769.

Expressioni

Tissue specificityi

Ubiquitously expressed.

Gene expression databases

BgeeiENSG00000100296.
CleanExiHS_THOC5.
ExpressionAtlasiQ13769. baseline and differential.
GenevisibleiQ13769. HS.

Organism-specific databases

HPAiHPA029812.
HPA048402.

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

WithEntry#Exp.IntActNotes
TAP1Q035184EBI-5280316,EBI-747259
THOC1Q96FV99EBI-5280316,EBI-1765605
THOC7Q6I9Y29EBI-5280316,EBI-716286

Protein-protein interaction databases

BioGridi114132. 65 interactions.
IntActiQ13769. 49 interactions.
MINTiMINT-4532759.
STRINGi9606.ENSP00000380969.

Structurei

3D structure databases

ProteinModelPortaliQ13769.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni2 – 199198Interaction with THOC7Add
BLAST
Regioni2 – 144143Interaction with CSF1RBy similarityAdd
BLAST

Motif

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Motifi7 – 104Nuclear localization signalBy similarity

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

InterProiIPR019163. THO_Thoc5.
[Graphical view]
PfamiPF09766. FimP. 1 hit.
[Graphical view]

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)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti380 – 3801T → K in a breast cancer sample; somatic mutation. 1 Publication
VAR_035692
Natural varianti475 – 4751T → S.
Corresponds to variant rs8141153 [ dbSNP | Ensembl ].
VAR_037134
Natural varianti499 – 4991G → S in a breast cancer sample; somatic mutation. 1 Publication
VAR_035693
Natural varianti525 – 5251V → I.4 Publications
Corresponds to variant rs737976 [ dbSNP | Ensembl ].
VAR_037135
Natural varianti579 – 5791V → I.3 Publications
Corresponds to variant rs1049534 [ dbSNP | Ensembl ].
VAR_021410

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

Cross-referencesi

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.

3D structure databases

ProteinModelPortaliQ13769.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi114132. 65 interactions.
IntActiQ13769. 49 interactions.
MINTiMINT-4532759.
STRINGi9606.ENSP00000380969.

PTM databases

iPTMnetiQ13769.
PhosphoSiteiQ13769.

Polymorphism and mutation databases

BioMutaiTHOC5.
DMDMi259016156.

Proteomic databases

EPDiQ13769.
MaxQBiQ13769.
PaxDbiQ13769.
PeptideAtlasiQ13769.
PRIDEiQ13769.

Protocols and materials databases

DNASUi8563.
Structural Biology KnowledgebaseSearch...

Genome annotation databases

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

Organism-specific databases

CTDi8563.
GeneCardsiTHOC5.
HGNCiHGNC:19074. THOC5.
HPAiHPA029812.
HPA048402.
MIMi612733. gene.
neXtProtiNX_Q13769.
PharmGKBiPA38188.
HUGEiSearch...
GenAtlasiSearch...

Phylogenomic databases

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

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.

Miscellaneous databases

ChiTaRSiTHOC5. human.
GeneWikiiTHOC5.
GenomeRNAii8563.
PROiQ13769.
SOURCEiSearch...

Gene expression databases

BgeeiENSG00000100296.
CleanExiHS_THOC5.
ExpressionAtlasiQ13769. baseline and differential.
GenevisibleiQ13769. HS.

Family and domain databases

InterProiIPR019163. THO_Thoc5.
[Graphical view]
PfamiPF09766. FimP. 1 hit.
[Graphical view]
ProtoNetiSearch...

Entry informationi

Entry nameiTHOC5_HUMAN
AccessioniPrimary (citable) accession number: Q13769
Secondary accession number(s): O60839, Q9UPZ5
Entry historyi
Integrated into UniProtKB/Swiss-Prot: May 2, 2002
Last sequence update: September 22, 2009
Last modified: September 7, 2016
This is version 136 of the entry and version 2 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

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

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.