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Protein Page:
THOC4 (human)
p Phosphorylation
a Acetylation
m Methylation
m1 Mono-methylation
m2 Di-methylation
m3 Tri-methylation
u Ubiquitination
s Sumoylation
n Neddylation
g O-GlcNAc
h Palmitoylation
ad Adenylylation
sn S-Nitrosylation
ca Caspase cleavage

Overview
THOC4 a chaperone protein that promotes the dimerization of transcription factors containing basic leucine zipper (bZIP) domains thus promoting transcriptional activation. Plays a role in mRNA processing and export. May function as scaffold that mediates interactions between proteins and/or RNA. Integral part of the THO/TREX complex that is recruited to transcribed genes and travels with the RNA polymerase during elongation. Is part of the exon junction complex that remains associated with spliced mRNA and plays an important role in mRNA export and nonsense-mediated RNA decay. Nuclear localization, translocates to the cytoplasm as part of the exon junction complex (EJC) bound to mRNA. Two differentially spliced isoforms have been described. Note: This description may include information from UniProtKB.
Protein type: RNA binding protein; Transcription, coactivator/corepressor; Chaperone
Cellular Component: nucleoplasm; nucleolus; nuclear speck; nucleus; cytosol
Molecular Function: protein binding; RNA binding; nucleotide binding
Biological Process: transcription from RNA polymerase II promoter; nuclear mRNA splicing, via spliceosome; mRNA export from nucleus; RNA splicing; gene expression; mRNA 3'-end processing; intronless viral mRNA export from host nucleus; termination of RNA polymerase II transcription
Reference #:  Q86V81 (UniProtKB)
Alt. Names/Synonyms: Ally of AML-1 and LEF-1; ALY; BEF; bZIP enhancing factor; bZIP-enhancing factor BEF; THO complex 4; THO complex subunit 4; Tho4; THOC4; Transcriptional coactivator Aly/REF
Gene Symbols: ALYREF
Molecular weight: 26,888 Da
Basal Isoelectric point: 11.15  Predict pI for various phosphorylation states
Protein-Specific Antibodies or siRNAs from Cell Signaling Technology® Total Proteins
Select Structure to View Below

THOC4
Protein Structure Not Found.


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Sites Implicated In
cell growth, altered: T219‑p
activation: T219‑p

Modification Sites and Domains Show Modification Legend
Click here to view phosphorylation modifications only

Modification Sites in Parent Protein, Orthologs, and Isoforms Show Modification Legend
 

Show Multiple Sequence Alignment


 SS 

SS: The number of records in which this modification site was determined using site-specific methods. SS methods include amino acid sequencing, site-directed mutagenesis, modification site-specific antibodies, specific MS strategies, etc.


  MS 

MS: The number of records in which this modification site was assigned using ONLY proteomic discovery-mode mass spectrometry.


        human

 
0 1 K4-a ____MADkMDMsLDD
0 6 S8-p MADkMDMsLDDIIkL
0 1 K14-u MsLDDIIkLNRsQRG
0 1 S18-p DIIkLNRsQRGGRGG
1 2 S34-p RGRGRAGsQGGrGGG
0 21 R38-m1 RAGsQGGrGGGAQAA
0 5 R38-m2 RAGsQGGrGGGAQAA
0 10 R50-m1 QAAARVNrGGGPIrN
0 2 R50-m2 QAAARVNrGGGPIrN
0 1 R56-m1 NrGGGPIrNrPAIAr
0 1 R58-m1 GGGPIrNrPAIArGA
0 1 R58-m2 GGGPIrNrPAIArGA
0 1 R63-m2 rNrPAIArGAAGGGG
0 71 Y77-p GRNRPAPysRPkQLP
0 11 S78-p RNRPAPysRPkQLPD
0 1 K81-u PAPysRPkQLPDkWQ
0 2 K86-a RPkQLPDkWQHDLFd
0 4 K86-u RPkQLPDkWQHDLFd
0 2 D93-ca kWQHDLFdsGFGGGA
0 3 S94-p WQHDLFdsGFGGGAG
0 3 K164-u ADALKAMkQYNGVPL
0 4 S183-p MNIQLVTsQIDAQRR
0 1 S194 AQRRPAQSVNrGGMT
0 30 R197-m1 RPAQSVNrGGMTRNr
0 3 R197-m2 RPAQSVNrGGMTRNr
0 1 R202 VNrGGMTRNrGAGGF
0 15 R204-m1 rGGMTRNrGAGGFGG
0 18 R204-m2 rGGMTRNrGAGGFGG
0 1 T215-p GFGGGGGtrRGtRGG
0 4 R216-m1 FGGGGGtrRGtRGGA
1 1 T219-p GGGtrRGtRGGARGR
0 1 S234 GRGAGRNSkQQLsAE
0 13 K235-u RGAGRNSkQQLsAEE
0 8 S239-p RNSkQQLsAEELDAQ
0 5 Y250-p LDAQLDAyNARMDts
0 13 T256-p AyNARMDts______
0 8 S257-p yNARMDts_______
  mouse

 
K4 ____MADKMDMsLDD
S8-p MADKMDMsLDDIIKL
K14 MsLDDIIKLNRSQRG
S18 DIIKLNRSQRGGRGG
S34-p RGRGRAGsQGGrGGA
R38-m1 RAGsQGGrGGAVQAA
R38-m2 RAGsQGGrGGAVQAA
R50-m1 QAAARVNrGGGPMRN
R50 QAAARVNRGGGPMRN
R56 NrGGGPMRNRPAIAR
R58 GGGPMRNRPAIARGA
R58 GGGPMRNRPAIARGA
R63 RNRPAIARGAAGGGR
Y76 GRNRPAPYSRPKQLP
S77 RNRPAPYSRPKQLPD
K80 PAPYSRPKQLPDkWQ
K85 RPKQLPDKWQHDLFD
K85-u RPKQLPDkWQHDLFD
D92 kWQHDLFDSGFGGGA
S93 WQHDLFDSGFGGGAG
K163-u ADALKAMkQYNGVPL
S182 MNIQLVTSQIDTQRR
S193-p TQRRPAQsINrGGMT
R196-m1 RPAQsINrGGMTrNr
R196-m2 RPAQsINrGGMTrNr
R201-m1 INrGGMTrNrGSGGF
R203-m1 rGGMTrNrGSGGFGG
R203-m2 rGGMTrNrGSGGFGG
T213 GGFGGGGTrRGTRGG
R214-m1 GFGGGGTrRGTRGGS
T217 GGGTrRGTRGGSRGR
S232-p GRGTGRNskQQLsAE
K233-u RGTGRNskQQLsAEE
S237-p RNskQQLsAEELDAQ
Y248 LDAQLDAYNARMDTS
T254 AYNARMDTS______
S255 YNARMDTS_______
  rat

 
K4 ____MADKMDMSLDD
S8 MADKMDMSLDDIIKL
K14 MSLDDIIKLNRSQRG
S18 DIIKLNRSQRGGRGG
S34 RGRGRAGSQGGrGGA
R38-m1 RAGSQGGrGGAVQAA
R38 RAGSQGGRGGAVQAA
R50 QAAARVNRGGGPMRN
R50 QAAARVNRGGGPMRN
R56 NRGGGPMRNRPAIAR
R58 GGGPMRNRPAIARGA
R58 GGGPMRNRPAIARGA
R63 RNRPAIARGAAGGGG
Y77 GRNRPAPYSRPKQLP
S78 RNRPAPYSRPKQLPD
K81 PAPYSRPKQLPDKWQ
K86 RPKQLPDKWQHDLFD
K86 RPKQLPDKWQHDLFD
D93 KWQHDLFDSGFGGGA
S94 WQHDLFDSGFGGGAG
K164 ADALKAMKQYNGVPL
S183 MNIQLVTSQIDTQRR
S194 TQRRPAQSINrGGMT
R197-m1 RPAQSINrGGMTRNR
R197 RPAQSINRGGMTRNR
R202 INrGGMTRNRGSGSF
R204 rGGMTRNRGSGSFGG
R204 rGGMTRNRGSGSFGG
T214 GSFGGGGTRRGTRGG
R215 SFGGGGTRRGTRGGS
T218 GGGTRRGTRGGSRGR
S233 GRGTGRNSKQQLSAE
K234 RGTGRNSKQQLSAEE
S238 RNSKQQLSAEELDAQ
Y249 LDAQLDAYNARMDTS
T255 AYNARMDTS______
S256 YNARMDTS_______
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