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Protein

THO complex subunit 4

Gene

ALYREF

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

Functioni

Export adapter involved in nuclear export of spliced and unspliced mRNA. Binds mRNA which is thought to be transferred to the NXF1-NXT1 heterodimer for export (TAP/NFX1 pathway). Component of the TREX complex which is thought to couple mRNA transcription, processing and nuclear export, and 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. TREX recruitment occurs via an interaction between ALYREF/THOC4 and the cap-binding protein NCBP1. The TREX complex is essential for the export of Kaposi's sarcoma-associated herpesvirus (KSHV) intronless mRNAs and infectious virus production; ALYREF/THOC4 mediates the recruitment of the TREX complex to the intronless viral mRNA. Required for TREX complex assembly and for linking DDX39B to the cap-binding complex (CBC). In conjunction with THOC5 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 the nuclear export of intronless mRNA; proposed to be recruited to intronless mRNA by ATP-bound DDX39B. Involved in transcription elongation and genome stability.1 Publication
Acts as chaperone and promotes the dimerization of transcription factors containing basic leucine zipper (bZIP) domains and thereby promotes transcriptional activation.

GO - Molecular functioni

  • nucleotide binding Source: InterPro
  • poly(A) RNA binding Source: UniProtKB

GO - Biological processi

  • mRNA 3'-end processing Source: Reactome
  • mRNA export from nucleus Source: UniProtKB
  • mRNA splicing, via spliceosome Source: UniProtKB
  • osteoblast differentiation Source: UniProtKB
  • positive regulation of DNA-templated transcription, elongation Source: UniProtKB
  • regulation of DNA recombination Source: UniProtKB
  • replication fork processing Source: UniProtKB
  • RNA export from nucleus Source: Reactome
  • termination of RNA polymerase II transcription Source: Reactome
  • viral mRNA export from host cell nucleus Source: UniProtKB
Complete GO annotation...

Keywords - Molecular functioni

Chaperone

Keywords - Biological processi

Host-virus interaction, 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-159227. Transport of the SLBP independent Mature mRNA.
R-HSA-159230. Transport of the SLBP Dependant Mature mRNA.
R-HSA-159231. Transport of Mature mRNA Derived from an Intronless Transcript.
R-HSA-159236. Transport of Mature mRNA derived from an Intron-Containing Transcript.
R-HSA-72163. mRNA Splicing - Major Pathway.
R-HSA-72187. mRNA 3'-end processing.
SIGNORiQ86V81.

Names & Taxonomyi

Protein namesi
Recommended name:
THO complex subunit 4
Short name:
Tho4
Alternative name(s):
Ally of AML-1 and LEF-1
Aly/REF export factor
Transcriptional coactivator Aly/REF
bZIP-enhancing factor BEF
Gene namesi
Name:ALYREF
Synonyms:ALY, BEF, THOC4
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
Proteomesi
  • UP000005640 Componenti: Unplaced

Organism-specific databases

HGNCiHGNC:19071. ALYREF.

Subcellular locationi

GO - Cellular componenti

  • catalytic step 2 spliceosome Source: UniProtKB
  • cytosol Source: Reactome
  • extracellular exosome Source: UniProtKB
  • intracellular membrane-bounded organelle Source: HPA
  • membrane Source: UniProtKB
  • nuclear speck Source: UniProtKB-SubCell
  • nucleoplasm Source: HPA
  • nucleus Source: HPA
  • transcription export complex Source: UniProtKB
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm, Nucleus, Spliceosome

Pathology & Biotechi

Organism-specific databases

PharmGKBiPA134925107.

Polymorphism and mutation databases

BioMutaiALYREF.
DMDMi48429165.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Initiator methionineiRemovedCombined sources2 Publications
Chaini2 – 257256THO complex subunit 4PRO_0000081974Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei2 – 21N-acetylalanineCombined sources2 Publications
Modified residuei8 – 81PhosphoserineCombined sources
Modified residuei86 – 861N6-acetyllysineBy similarity
Modified residuei94 – 941PhosphoserineCombined sources
Modified residuei141 – 1411CitrullineBy similarity
Modified residuei204 – 2041Dimethylated arginine; alternateCombined sources1 Publication
Modified residuei204 – 2041Omega-N-methylated arginine; alternate1 Publication
Modified residuei220 – 2201Omega-N-methylarginine1 Publication
Modified residuei239 – 2391PhosphoserineCombined sources

Post-translational modificationi

Arg-204 is dimethylated, probably to asymmetric dimethylarginine. Arginine methylation reduces RNA binding.2 Publications
Citrullinated by PADI4.By similarity

Keywords - PTMi

Acetylation, Citrullination, Methylation, Phosphoprotein

Proteomic databases

EPDiQ86V81.
MaxQBiQ86V81.
PaxDbiQ86V81.
PRIDEiQ86V81.
TopDownProteomicsiQ86V81.

PTM databases

iPTMnetiQ86V81.
PhosphoSiteiQ86V81.

Miscellaneous databases

PMAP-CutDBQ86V81.

Expressioni

Tissue specificityi

Expressed in a wide variety of cancer types.1 Publication

Gene expression databases

BgeeiQ86V81.
CleanExiHS_THOC4.

Organism-specific databases

HPAiCAB016281.
HPA019799.
HPA061282.

Interactioni

Subunit structurei

Homomultimer. Is part of several complexes involved in mRNA processing and export. Component of the transcription/export (TREX) complex at least composed of ALYREF/THOC4, DDX39B, SARNP/CIP29, CHTOP and the THO subcomplex; TREX seems to have a dynamic structure involving ATP-dependent remodeling; in the complex interacts (via C-terminus) directly with DDX39B and interacts directly with THOC1 and THOC2. Found in mRNA splicing-dependent exon junction complexes (EJC). Identified in the spliceosome C complex. Found in a mRNP complex with UPF3A and UPF3B. Interacts with RBM8A, NCBP1, THOC5, LEF1, RUNX1, EIF4A3, RNPS1, SRRM1, IWS1 and EXOSC1. Interacts with NXF1; the interaction is direct. Interacts with human Kaposi's sarcoma-associated herpesvirus (HHV-8) ORF57 protein; this interaction allows efficient export of HHV-8 early and late intronless transcripts. Interacts with HHV-1 ICP27 protein; this interaction recruits ALYREF to viral replication compartments and probably directs viral mRNA to the TAP/NFX1 pathway.22 Publications

Binary interactionsi

WithEntry#Exp.IntActNotes
CHTOPQ9Y3Y28EBI-347640,EBI-347794
DDX39BQ138384EBI-347640,EBI-348622
NXF1Q9UBU94EBI-347640,EBI-398874

Protein-protein interaction databases

BioGridi115486. 121 interactions.
DIPiDIP-32711N.
IntActiQ86V81. 49 interactions.
MINTiMINT-5001811.
STRINGi9606.ENSP00000421592.

Structurei

Secondary structure

1
257
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi105 – 1128Combined sources
Helixi119 – 1279Combined sources
Beta strandi132 – 1398Combined sources
Beta strandi145 – 15511Combined sources
Helixi156 – 16611Combined sources
Beta strandi177 – 1815Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
3ULHX-ray2.54A78-183[»]
ProteinModelPortaliQ86V81.
SMRiQ86V81. Positions 1-188.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini106 – 18378RRMPROSITE-ProRule annotationAdd
BLAST

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni16 – 3722Sufficient for RNA-binding, interaction with NXF1-NXT1 heterodimerAdd
BLAST
Regioni85 – 186102Interaction with HHV-8 ORF57 protein and with ICP27 from HHV-1By similarityAdd
BLAST

Compositional bias

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Compositional biasi21 – 231211Ala/Arg/Gly-richAdd
BLAST

Sequence similaritiesi

Belongs to the ALYREF family.Curated
Contains 1 RRM (RNA recognition motif) domain.PROSITE-ProRule annotation

Phylogenomic databases

eggNOGiKOG0533. Eukaryota.
ENOG4111JAW. LUCA.
HOGENOMiHOG000239962.
HOVERGENiHBG054806.
InParanoidiQ86V81.
KOiK12881.
PhylomeDBiQ86V81.

Family and domain databases

Gene3Di3.30.70.330. 1 hit.
InterProiIPR025715. FoP_C.
IPR012677. Nucleotide-bd_a/b_plait.
IPR000504. RRM_dom.
[Graphical view]
PfamiPF13865. FoP_duplication. 1 hit.
PF00076. RRM_1. 1 hit.
[Graphical view]
SMARTiSM01218. FoP_duplication. 1 hit.
SM00360. RRM. 1 hit.
[Graphical view]
SUPFAMiSSF54928. SSF54928. 1 hit.
PROSITEiPS50102. RRM. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

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

Q86V81-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MADKMDMSLD DIIKLNRSQR GGRGGGRGRG RAGSQGGRGG GAQAAARVNR
60 70 80 90 100
GGGPIRNRPA IARGAAGGGG RNRPAPYSRP KQLPDKWQHD LFDSGFGGGA
110 120 130 140 150
GVETGGKLLV SNLDFGVSDA DIQELFAEFG TLKKAAVHYD RSGRSLGTAD
160 170 180 190 200
VHFERKADAL KAMKQYNGVP LDGRPMNIQL VTSQIDAQRR PAQSVNRGGM
210 220 230 240 250
TRNRGAGGFG GGGGTRRGTR GGARGRGRGA GRNSKQQLSA EELDAQLDAY

NARMDTS
Length:257
Mass (Da):26,888
Last modified:January 23, 2007 - v3
Checksum:iE2B5021DA579919A
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti26 – 261G → R in AAD09608 (PubMed:9952027).Curated
Sequence conflicti35 – 362QG → RA in AAD09608 (PubMed:9952027).Curated
Sequence conflicti39 – 391G → R in AAD09608 (PubMed:9952027).Curated
Sequence conflicti150 – 1501D → N in AAD09608 (PubMed:9952027).Curated
Sequence conflicti169 – 1691V → F in AAD09608 (PubMed:9952027).Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AC145207 Genomic DNA. No translation available.
BC052302 mRNA. Translation: AAH52302.1.
AF047002 mRNA. Translation: AAD09608.1.
RefSeqiNP_005773.3. NM_005782.3.
UniGeneiHs.534385.

Genome annotation databases

EnsembliENST00000331204; ENSP00000331817; ENSG00000183684.
GeneIDi10189.
KEGGihsa:10189.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AC145207 Genomic DNA. No translation available.
BC052302 mRNA. Translation: AAH52302.1.
AF047002 mRNA. Translation: AAD09608.1.
RefSeqiNP_005773.3. NM_005782.3.
UniGeneiHs.534385.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
3ULHX-ray2.54A78-183[»]
ProteinModelPortaliQ86V81.
SMRiQ86V81. Positions 1-188.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi115486. 121 interactions.
DIPiDIP-32711N.
IntActiQ86V81. 49 interactions.
MINTiMINT-5001811.
STRINGi9606.ENSP00000421592.

PTM databases

iPTMnetiQ86V81.
PhosphoSiteiQ86V81.

Polymorphism and mutation databases

BioMutaiALYREF.
DMDMi48429165.

Proteomic databases

EPDiQ86V81.
MaxQBiQ86V81.
PaxDbiQ86V81.
PRIDEiQ86V81.
TopDownProteomicsiQ86V81.

Protocols and materials databases

DNASUi10189.
Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000331204; ENSP00000331817; ENSG00000183684.
GeneIDi10189.
KEGGihsa:10189.

Organism-specific databases

CTDi10189.
GeneCardsiALYREF.
HGNCiHGNC:19071. ALYREF.
HPAiCAB016281.
HPA019799.
HPA061282.
MIMi604171. gene.
neXtProtiNX_Q86V81.
PharmGKBiPA134925107.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiKOG0533. Eukaryota.
ENOG4111JAW. LUCA.
HOGENOMiHOG000239962.
HOVERGENiHBG054806.
InParanoidiQ86V81.
KOiK12881.
PhylomeDBiQ86V81.

Enzyme and pathway databases

ReactomeiR-HSA-109688. Cleavage of Growing Transcript in the Termination Region.
R-HSA-159227. Transport of the SLBP independent Mature mRNA.
R-HSA-159230. Transport of the SLBP Dependant Mature mRNA.
R-HSA-159231. Transport of Mature mRNA Derived from an Intronless Transcript.
R-HSA-159236. Transport of Mature mRNA derived from an Intron-Containing Transcript.
R-HSA-72163. mRNA Splicing - Major Pathway.
R-HSA-72187. mRNA 3'-end processing.
SIGNORiQ86V81.

Miscellaneous databases

ChiTaRSiALYREF. human.
GeneWikiiTHOC4.
GenomeRNAii10189.
PMAP-CutDBQ86V81.
PROiQ86V81.
SOURCEiSearch...

Gene expression databases

BgeeiQ86V81.
CleanExiHS_THOC4.

Family and domain databases

Gene3Di3.30.70.330. 1 hit.
InterProiIPR025715. FoP_C.
IPR012677. Nucleotide-bd_a/b_plait.
IPR000504. RRM_dom.
[Graphical view]
PfamiPF13865. FoP_duplication. 1 hit.
PF00076. RRM_1. 1 hit.
[Graphical view]
SMARTiSM01218. FoP_duplication. 1 hit.
SM00360. RRM. 1 hit.
[Graphical view]
SUPFAMiSSF54928. SSF54928. 1 hit.
PROSITEiPS50102. RRM. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "DNA sequence of human chromosome 17 and analysis of rearrangement in the human lineage."
    Zody M.C., Garber M., Adams D.J., Sharpe T., Harrow J., Lupski J.R., Nicholson C., Searle S.M., Wilming L., Young S.K., Abouelleil A., Allen N.R., Bi W., Bloom T., Borowsky M.L., Bugalter B.E., Butler J., Chang J.L.
    , Chen C.-K., Cook A., Corum B., Cuomo C.A., de Jong P.J., DeCaprio D., Dewar K., FitzGerald M., Gilbert J., Gibson R., Gnerre S., Goldstein S., Grafham D.V., Grocock R., Hafez N., Hagopian D.S., Hart E., Norman C.H., Humphray S., Jaffe D.B., Jones M., Kamal M., Khodiyar V.K., LaButti K., Laird G., Lehoczky J., Liu X., Lokyitsang T., Loveland J., Lui A., Macdonald P., Major J.E., Matthews L., Mauceli E., McCarroll S.A., Mihalev A.H., Mudge J., Nguyen C., Nicol R., O'Leary S.B., Osoegawa K., Schwartz D.C., Shaw-Smith C., Stankiewicz P., Steward C., Swarbreck D., Venkataraman V., Whittaker C.A., Yang X., Zimmer A.R., Bradley A., Hubbard T., Birren B.W., Rogers J., Lander E.S., Nusbaum C.
    Nature 440:1045-1049(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  2. "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
    The MGC Project Team
    Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Tissue: Lung.
  3. Quadroni M.
    Submitted (OCT-2004) to UniProtKB
    Cited for: PROTEIN SEQUENCE OF 2-15 AND 146-156, CLEAVAGE OF INITIATOR METHIONINE, ACETYLATION AT ALA-2, IDENTIFICATION BY MASS SPECTROMETRY.
    Tissue: B-cell lymphoma.
  4. Bienvenut W.V., Lilla S., von Kriegsheim A., Lempens A., Kolch W.
    Submitted (DEC-2008) to UniProtKB
    Cited for: PROTEIN SEQUENCE OF 2-14; 108-134; 145-155; 165-189; 203-216 AND 236-253, CLEAVAGE OF INITIATOR METHIONINE, ACETYLATION AT ALA-2, METHYLATION AT ARG-204 AND ARG-220, IDENTIFICATION BY MASS SPECTROMETRY.
    Tissue: Ovarian carcinoma.
  5. "Autoantibodies to transcriptional regulation proteins DEK and ALY in a patient with systemic lupus erythematosus."
    Wichmann I., Garcia-Lozano J.R., Respaldiza N., Gonzalez-Escribano M.F., Nunez-Roldan A.
    Hum. Immunol. 60:57-62(1999) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 25-257, INVOLVEMENT IN SYSTEMIC LUPUS ERYTHEMATOSUS.
    Tissue: Cervix carcinoma.
  6. "Large-scale proteomic analysis of the human spliceosome."
    Rappsilber J., Ryder U., Lamond A.I., Mann M.
    Genome Res. 12:1231-1245(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: PROTEIN SEQUENCE OF 108-133, IDENTIFICATION BY MASS SPECTROMETRY, INTERACTION WITH THE SPLICEOSOME.
  7. "A human nuclear-localized chaperone that regulates dimerization, DNA binding, and transcriptional activity of bZIP proteins."
    Virbasius C.-M., Wagner S., Green M.R.
    Mol. Cell 4:219-228(1999) [PubMed] [Europe PMC] [Abstract]
    Cited for: PROTEIN SEQUENCE OF 127-131; 182-189; 239-245 AND 249-251, FUNCTION, SUBCELLULAR LOCATION.
  8. "Mass spectrometry and EST-database searching allows characterization of the multi-protein spliceosome complex."
    Neubauer G., King A., Rappsilber J., Calvio C., Watson M., Ajuh P., Sleeman J., Lamond A.I., Mann M.
    Nat. Genet. 20:46-50(1998) [PubMed] [Europe PMC] [Abstract]
    Cited for: PARTIAL PROTEIN SEQUENCE, IDENTIFICATION BY MASS SPECTROMETRY, INTERACTION WITH THE SPLICEOSOME.
  9. "The spliceosome deposits multiple proteins 20-24 nucleotides upstream of mRNA exon-exon junctions."
    Le Hir H., Izaurralde E., Maquat L.E., Moore M.J.
    EMBO J. 19:6860-6869(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION IN A MRNA SPLICING-DEPENDENT EXON JUNCTION COMPLEX (EJC) WITH DEK; RBM8A; RNPS1 AND SRRM1.
  10. "Magoh, a human homolog of Drosophila mago nashi protein, is a component of the splicing-dependent exon-exon junction complex."
    Kataoka N., Diem M.D., Kim V.N., Yong J., Dreyfuss G.
    EMBO J. 20:6424-6433(2001) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, INTERACTION WITH RBM8A; NXF1 AND THE EXON JUNCTION COMPLEX.
  11. "Pre-mRNA splicing and mRNA export linked by direct interactions between UAP56 and Aly."
    Luo M.-J., Zhou Z., Magni K., Christoforides C., Rappsilber J., Mann M., Reed R.
    Nature 413:644-647(2001) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, INTERACTION WITH NXF1.
  12. "Role of the nonsense-mediated decay factor hUpf3 in the splicing-dependent exon-exon junction complex."
    Kim V.N., Kataoka N., Dreyfuss G.
    Science 293:1832-1836(2001) [PubMed] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION IN A MRNP COMPLEX WITH UPF3A AND UPF3B.
  13. "ICP27 interacts with the RNA export factor Aly/REF to direct herpes simplex virus type 1 intronless mRNAs to the TAP export pathway."
    Chen I.-H.B., Sciabica K.S., Sandri-Goldin R.M.
    J. Virol. 76:12877-12889(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, INTERACTION WITH HHV-1 ICP27.
  14. Cited for: FUNCTION, INTERACTION WITH THE TREX COMPLEX.
  15. "Purification and characterization of native spliceosomes suitable for three-dimensional structural analysis."
    Jurica M.S., Licklider L.J., Gygi S.P., Grigorieff N., Moore M.J.
    RNA 8:426-439(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION BY MASS SPECTROMETRY, IDENTIFICATION IN THE SPLICEOSOMAL C COMPLEX.
  16. "An evolutionarily conserved role for SRm160 in 3'-end processing that functions independently of exon junction complex formation."
    McCracken S., Longman D., Johnstone I.L., Caceres J.F., Blencowe B.J.
    J. Biol. Chem. 278:44153-44160(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH DDX39B; RBM8A; RNPS1 AND SRRM1.
  17. "Identifying and quantifying in vivo methylation sites by heavy methyl SILAC."
    Ong S.E., Mittler G., Mann M.
    Nat. Methods 1:119-126(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: METHYLATION [LARGE SCALE ANALYSIS] AT ARG-204, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  18. "eIF4A3 is a novel component of the exon junction complex."
    Chan C.C., Dostie J., Diem M.D., Feng W., Mann M., Rappsilber J., Dreyfuss G.
    RNA 10:200-209(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH EIF4A3 AND NXF1.
  19. "Linking transcriptional elongation and messenger RNA export to metastatic breast cancers."
    Guo S., Hakimi M.A., Baillat D., Chen X., Farber M.J., Klein-Szanto A.J., Cooch N.S., Godwin A.K., Shiekhattar R.
    Cancer Res. 65:3011-3016(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION IN THE TREX COMPLEX, FUNCTION OF THE TREX COMPLEX, IDENTIFICATION BY MASS SPECTROMETRY.
  20. "Recruitment of the human TREX complex to mRNA during splicing."
    Masuda S., Das R., Cheng H., Hurt E., Dorman N., Reed R.
    Genes Dev. 19:1512-1517(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION IN THE TREX COMPLEX, FUNCTION OF THE TREX COMPLEX, IDENTIFICATION BY MASS SPECTROMETRY, INTERACTION WITH DDX39B.
  21. "Biochemical analysis of the EJC reveals two new factors and a stable tetrameric protein core."
    Tange T.O., Shibuya T., Jurica M.S., Moore M.J.
    RNA 11:1869-1883(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION IN A MRNA SPLICING-DEPENDENT EXON JUNCTION COMPLEX, HETERODIMERIZATION, IDENTIFICATION BY MASS SPECTROMETRY.
  22. "Human mRNA export machinery recruited to the 5' end of mRNA."
    Cheng H., Dufu K., Lee C.-S., Hsu J.L., Dias A., Reed R.
    Cell 127:1389-1400(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION OF THE TREX COMPLEX, INTERACTION WITH NCBP1.
  23. "The Spt6 SH2 domain binds Ser2-P RNAPII to direct Iws1-dependent mRNA splicing and export."
    Yoh S.M., Cho H., Pickle L., Evans R.M., Jones K.A.
    Genes Dev. 21:160-174(2007) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH IWS1 AND EXOSC10.
  24. "ATP-dependent recruitment of export factor Aly/REF onto intronless mRNAs by RNA helicase UAP56."
    Taniguchi I., Ohno M.
    Mol. Cell. Biol. 28:601-608(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, INTERACTION WITH DDX39B.
  25. "Recruitment of the complete hTREX complex is required for Kaposi's sarcoma-associated herpesvirus intronless mRNA nuclear export and virus replication."
    Boyne J.R., Colgan K.J., Whitehouse A.
    PLoS Pathog. 4:E1000194-E1000194(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION OF THE TREX COMPLEX, SUBUNIT, SUBCELLULAR LOCATION, INTERACTION WITH NXF1; DDX39B AND HUMAN KAPOSI'S SARCOMA-ASSOCIATED HERPESVIRUS ORF57 PROTEIN.
  26. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  27. "Mutually exclusive interactions drive handover of mRNA from export adaptors to TAP."
    Hautbergue G.M., Hung M.L., Golovanov A.P., Lian L.Y., Wilson S.A.
    Proc. Natl. Acad. Sci. U.S.A. 105:5154-5159(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION.
  28. "Lys-N and trypsin cover complementary parts of the phosphoproteome in a refined SCX-based approach."
    Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J., Mohammed S.
    Anal. Chem. 81:4493-4501(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, CLEAVAGE OF INITIATOR METHIONINE [LARGE SCALE ANALYSIS], IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  29. "Adaptor Aly and co-adaptor Thoc5 function in the Tap-p15-mediated nuclear export of HSP70 mRNA."
    Katahira J., Inoue H., Hurt E., Yoneda Y.
    EMBO J. 28:556-567(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, INTERACTION WITH THOC5 AND NXF1.
  30. "Assembly and mobility of exon-exon junction complexes in living cells."
    Schmidt U., Im K.-B., Benzing C., Janjetovic S., Rippe K., Lichter P., Wachsmuth M.
    RNA 15:862-876(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: SUBCELLULAR LOCATION.
  31. "Quantitative phosphoproteomic analysis of T cell receptor signaling reveals system-wide modulation of protein-protein interactions."
    Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K., Rodionov V., Han D.K.
    Sci. Signal. 2:RA46-RA46(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-239, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Leukemic T-cell.
  32. "Arginine methylation of REF/ALY promotes efficient handover of mRNA to TAP/NXF1."
    Hung M.L., Hautbergue G.M., Snijders A.P., Dickman M.J., Wilson S.A.
    Nucleic Acids Res. 38:3351-3361(2010) [PubMed] [Europe PMC] [Abstract]
    Cited for: METHYLATION, MRNA-BINDING.
  33. "Quantitative phosphoproteomics reveals widespread full phosphorylation site occupancy during mitosis."
    Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L., Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S., Mann M.
    Sci. Signal. 3:RA3-RA3(2010) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-8; SER-94 AND SER-239, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  34. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  35. "Genome instability and transcription elongation impairment in human cells depleted of THO/TREX."
    Dominguez-Sanchez M.S., Barroso S., Gomez-Gonzalez B., Luna R., Aguilera A.
    PLoS Genet. 7:E1002386-E1002386(2011) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION.
  36. "Structural basis for the recognition of cellular mRNA export factor REF by herpes viral proteins HSV-1 ICP27 and HVS ORF57."
    Tunnicliffe R.B., Hautbergue G.M., Kalra P., Jackson B.R., Whitehouse A., Wilson S.A., Golovanov A.P.
    PLoS Pathog. 7:E1001244-E1001244(2011) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH HUMAN KAPOSI'S SARCOMA-ASSOCIATED HERPESVIRUS ORF57 PROTEIN, INTERACTION WITH HUMAN HERPESVIRUS 1 ICP27 PROTEIN.
  37. "System-wide temporal characterization of the proteome and phosphoproteome of human embryonic stem cell differentiation."
    Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J., Johansen P.T., Kratchmarova I., Kassem M., Mann M., Olsen J.V., Blagoev B.
    Sci. Signal. 4:RS3-RS3(2011) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-239, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  38. Cited for: FUNCTION.
  39. Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, CLEAVAGE OF INITIATOR METHIONINE [LARGE SCALE ANALYSIS], IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  40. "Aly and THO are required for assembly of the human TREX complex and association of TREX components with the spliced mRNA."
    Chi B., Wang Q., Wu G., Tan M., Wang L., Shi M., Chang X., Cheng H.
    Nucleic Acids Res. 41:1294-1306(2013) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, INTERACTION WITH THOC1 AND THOC2.
  41. "Mapping interactions between mRNA export factors in living cells."
    Teng I.F., Wilson S.A.
    PLoS ONE 8:E67676-E67676(2013) [PubMed] [Europe PMC] [Abstract]
    Cited for: SUBCELLULAR LOCATION, INTERACTION WITH NXF1 AND CHTOP.
  42. "An enzyme assisted RP-RPLC approach for in-depth analysis of human liver phosphoproteome."
    Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., Wang L., Ye M., Zou H.
    J. Proteomics 96:253-262(2014) [PubMed] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Liver.
  43. Cited for: FUNCTION, TISSUE SPECIFICITY.
  44. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].

Entry informationi

Entry nameiTHOC4_HUMAN
AccessioniPrimary (citable) accession number: Q86V81
Secondary accession number(s): O43672
Entry historyi
Integrated into UniProtKB/Swiss-Prot: October 10, 2003
Last sequence update: January 23, 2007
Last modified: June 8, 2016
This is version 148 of the entry and version 3 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

Miscellaneous

Antibodies against ALYREF/THOC4 are found in sera of patients with systemic lupus erythematosus (SLE).

Keywords - Technical termi

3D-structure, Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. Human chromosome 17
    Human chromosome 17: 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.