THOC4_MOUSE - dbPTM
THOC4_MOUSE - PTM Information in dbPTM
Basic Information of Protein
UniProt ID THOC4_MOUSE
UniProt AC O08583
Protein Name THO complex subunit 4
Gene Name Alyref
Organism Mus musculus (Mouse).
Sequence Length 255
Subcellular Localization Nucleus . Nucleus speckle . Cytoplasm . Colocalizes with the core EJC, ALYREF/THOC4, NXF1 and DDX39B in the nucleus and nuclear speckles. Localizes to regions surrounding nuclear speckles known as perispeckles in which TREX complex assembly seems to
Protein Description 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. 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.; Acts as chaperone and promotes the dimerization of transcription factors containing basic leucine zipper (bZIP) domains and thereby promotes transcriptional activation..
Protein Sequence MADKMDMSLDDIIKLNRSQRGGRGGGRGRGRAGSQGGRGGAVQAAARVNRGGGPMRNRPAIARGAAGGGRNRPAPYSRPKQLPDKWQHDLFDSGFGGGAGVETGGKLLVSNLDFGVSDADIQELFAEFGTLKKAAVHYDRSGRSLGTADVHFERKADALKAMKQYNGVPLDGRPMNIQLVTSQIDTQRRPAQSINRGGMTRNRGSGGFGGGGTRRGTRGGSRGRGRGTGRNSKQQLSAEELDAQLDAYNARMDTS
Overview of Protein Modification Sites with Functional and Structural Information
Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations Modification Substrate Peptides
&
Secondary Structure		 ASA (%) Reference Orthologous
Protein Cluster
2Acetylation------MADKMDMSL
------CCCCCCCCH		25.73-
4Acetylation----MADKMDMSLDD
----CCCCCCCCHHH		27.5423806337
8PhosphorylationMADKMDMSLDDIIKL
CCCCCCCCHHHHHHH		25.1221082442
34PhosphorylationRGRGRAGSQGGRGGA
CCCCCCCCCCCCCHH		25.3526824392
38Asymmetric dimethylarginineRAGSQGGRGGAVQAA
CCCCCCCCCHHHHHH		47.39-
38MethylationRAGSQGGRGGAVQAA
CCCCCCCCCHHHHHH		47.3924129315
50DimethylationQAAARVNRGGGPMRN
HHHHHCCCCCCCCCC		42.13-
50MethylationQAAARVNRGGGPMRN
HHHHHCCCCCCCCCC		42.1316188611
56MethylationNRGGGPMRNRPAIAR
CCCCCCCCCCHHHHC		38.8630761359
58MethylationGGGPMRNRPAIARGA
CCCCCCCCHHHHCCC		16.2152723731
63DimethylationRNRPAIARGAAGGGR
CCCHHHHCCCCCCCC		29.21-
63MethylationRNRPAIARGAAGGGR
CCCHHHHCCCCCCCC		29.2154559985
70MethylationRGAAGGGRNRPAPYS
CCCCCCCCCCCCCCC		38.98-
76PhosphorylationGRNRPAPYSRPKQLP
CCCCCCCCCCCCCCC		21.3029514104
80MalonylationPAPYSRPKQLPDKWQ
CCCCCCCCCCCCHHC		64.4626320211
80AcetylationPAPYSRPKQLPDKWQ
CCCCCCCCCCCCHHC		64.4623806337
85UbiquitinationRPKQLPDKWQHDLFD
CCCCCCCHHCCCCCC		46.9822790023
85AcetylationRPKQLPDKWQHDLFD
CCCCCCCHHCCCCCC		46.9823806337
93PhosphorylationWQHDLFDSGFGGGAG
HCCCCCCCCCCCCCC		28.7825266776
103PhosphorylationGGGAGVETGGKLLVS
CCCCCCCCCCEEEEE		49.1523140645
140CitrullinationKAAVHYDRSGRSLGT
HEEEEECCCCCCCCC		33.57-
140CitrullinationKAAVHYDRSGRSLGT
HEEEEECCCCCCCCC		33.5724463520
141PhosphorylationAAVHYDRSGRSLGTA
EEEEECCCCCCCCCC		35.3425338131
163AcetylationADALKAMKQYNGVPL
HHHHHHHHHHCCCCC		55.2622902405
163UbiquitinationADALKAMKQYNGVPL
HHHHHHHHHHCCCCC		55.2622790023
193PhosphorylationTQRRPAQSINRGGMT
CCCCCCHHHCCCCCC		24.7622817900
196MethylationRPAQSINRGGMTRNR
CCCHHHCCCCCCCCC		41.1824129315
196Asymmetric dimethylarginineRPAQSINRGGMTRNR
CCCHHHCCCCCCCCC		41.18-
201MethylationINRGGMTRNRGSGGF
HCCCCCCCCCCCCCC		23.1930989533
203MethylationRGGMTRNRGSGGFGG
CCCCCCCCCCCCCCC		37.0524129315
203Asymmetric dimethylarginineRGGMTRNRGSGGFGG
CCCCCCCCCCCCCCC		37.05-
205PhosphorylationGMTRNRGSGGFGGGG
CCCCCCCCCCCCCCC		32.2925266776
214MethylationGFGGGGTRRGTRGGS
CCCCCCCCCCCCCCC		38.0030761365
218MethylationGGTRRGTRGGSRGRG
CCCCCCCCCCCCCCC		50.75-
232PhosphorylationGRGTGRNSKQQLSAE
CCCCCCCHHHCCCHH		30.4022817900
233UbiquitinationRGTGRNSKQQLSAEE
CCCCCCHHHCCCHHH		45.6822790023
233AcetylationRGTGRNSKQQLSAEE
CCCCCCHHHCCCHHH		45.6823236377
233MethylationRGTGRNSKQQLSAEE
CCCCCCHHHCCCHHH		45.68-
237PhosphorylationRNSKQQLSAEELDAQ
CCHHHCCCHHHHHHH		29.3325521595
254PhosphorylationAYNARMDTS------
HHHHHCCCC------		27.3026745281
255PhosphorylationYNARMDTS-------
HHHHCCCC-------		33.6826745281
Upstream regulatory proteins (kinases for phosphorylation sites, E3 ubiquitin ligases of ubiquitination sites, ...)
Modified Location Modified Residue Modification Type of Upstream Proteins Gene Name of Upstream Proteins UniProt AC of Upstream Proteins Sources

Oops, there are no upstream regulatory protein records of THOC4_MOUSE !!
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference
50RMethylation

-
203RMethylation

24129315
Disease-associated PTM Sites based on SAP

* Distance = the distance between SAP position and PTM sites.

Modified Location Modification Variant Position
(Distance <= 10) 		Residue Change SAP Related Disease Reference

Oops, there are no SNP-PTM records of THOC4_MOUSE !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions

Oops, there are no PPI records of THOC4_MOUSE !!
Drug and Disease Associations
Kegg Drug
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of THOC4_MOUSE

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Related Literatures of Post-Translational Modification
Phosphorylation
ReferencePubMed
"The phagosomal proteome in interferon-gamma-activated macrophages.";
Trost M., English L., Lemieux S., Courcelles M., Desjardins M.,Thibault P.;
Immunity 30:143-154(2009).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-237, AND MASSSPECTROMETRY.

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