THOC4_HUMAN - dbPTM
THOC4_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID THOC4_HUMAN
UniProt AC Q86V81
Protein Name THO complex subunit 4
Gene Name ALYREF
Organism Homo sapiens (Human).
Sequence Length 257
Subcellular Localization Nucleus . Nucleus speckle . Cytoplasm . Colocalizes with the core EJC, ALYREF/THOC4, NXF1 and DDX39B in the nucleus and nuclear speckles. Travels to the cytoplasm as part of the exon junction complex (EJC) bound to mRNA (PubMed:19324961). Localizes t
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. 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.; Acts as chaperone and promotes the dimerization of transcription factors containing basic leucine zipper (bZIP) domains and thereby promotes transcriptional activation..
Protein Sequence MADKMDMSLDDIIKLNRSQRGGRGGGRGRGRAGSQGGRGGGAQAAARVNRGGGPIRNRPAIARGAAGGGGRNRPAPYSRPKQLPDKWQHDLFDSGFGGGAGVETGGKLLVSNLDFGVSDADIQELFAEFGTLKKAAVHYDRSGRSLGTADVHFERKADALKAMKQYNGVPLDGRPMNIQLVTSQIDAQRRPAQSVNRGGMTRNRGAGGFGGGGGTRRGTRGGARGRGRGAGRNSKQQLSAEELDAQLDAYNARMDTS
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		25.7322814378
42-Hydroxyisobutyrylation----MADKMDMSLDD
----CCCCCCCCHHH		27.54-
4Acetylation----MADKMDMSLDD
----CCCCCCCCHHH		27.5425953088
5Sulfoxidation---MADKMDMSLDDI
---CCCCCCCCHHHH		5.5621406390
7Sulfoxidation-MADKMDMSLDDIIK
-CCCCCCCCHHHHHH		3.7128183972
8PhosphorylationMADKMDMSLDDIIKL
CCCCCCCCHHHHHHH		25.1230266825
14UbiquitinationMSLDDIIKLNRSQRG
CCHHHHHHHHHHHCC		39.7921906983
15PhosphorylationSLDDIIKLNRSQRGG
CHHHHHHHHHHHCCC		4.5419651622
18PhosphorylationDIIKLNRSQRGGRGG
HHHHHHHHHCCCCCC		24.1324719451
21UbiquitinationKLNRSQRGGRGGGRG
HHHHHHCCCCCCCCC		23.6321890473
25PhosphorylationSQRGGRGGGRGRGRA
HHCCCCCCCCCCCCC		22.67-
31MethylationGGGRGRGRAGSQGGR
CCCCCCCCCCCCCCC		34.12115918429
34PhosphorylationRGRGRAGSQGGRGGG
CCCCCCCCCCCCCCH		25.3522199227
38Asymmetric dimethylarginineRAGSQGGRGGGAQAA
CCCCCCCCCCHHHHH		47.62-
38MethylationRAGSQGGRGGGAQAA
CCCCCCCCCCHHHHH		47.6224129315
41PhosphorylationSQGGRGGGAQAAARV
CCCCCCCHHHHHHHH		19.8332645325
45MethylationRGGGAQAAARVNRGG
CCCHHHHHHHHCCCC		5.45-
47MethylationGGAQAAARVNRGGGP
CHHHHHHHHCCCCCC		22.86115368285
50DimethylationQAAARVNRGGGPIRN
HHHHHHCCCCCCCCC		42.13-
50MethylationQAAARVNRGGGPIRN
HHHHHHCCCCCCCCC		42.1320678875
54MethylationRVNRGGGPIRNRPAI
HHCCCCCCCCCCHHH		26.16-
56MethylationNRGGGPIRNRPAIAR
CCCCCCCCCCHHHHC		35.9230761357
57MethylationRGGGPIRNRPAIARG
CCCCCCCCCHHHHCC		55.82-
58DimethylationGGGPIRNRPAIARGA
CCCCCCCCHHHHCCC		16.51-
58MethylationGGGPIRNRPAIARGA
CCCCCCCCHHHHCCC		16.5124129315
63MethylationRNRPAIARGAAGGGG
CCCHHHHCCCCCCCC		29.2124129315
63DimethylationRNRPAIARGAAGGGG
CCCHHHHCCCCCCCC		29.21-
65MethylationRPAIARGAAGGGGRN
CHHHHCCCCCCCCCC		9.44-
70MethylationRGAAGGGGRNRPAPY
CCCCCCCCCCCCCCC		27.28-
71MethylationGAAGGGGRNRPAPYS
CCCCCCCCCCCCCCC		38.9824129315
73MethylationAGGGGRNRPAPYSRP
CCCCCCCCCCCCCCC		27.6554559967
77PhosphorylationGRNRPAPYSRPKQLP
CCCCCCCCCCCCCCC		21.3028152594
78MethylationRNRPAPYSRPKQLPD
CCCCCCCCCCCCCCC		40.84-
78PhosphorylationRNRPAPYSRPKQLPD
CCCCCCCCCCCCCCC		40.8428152594
80MethylationRPAPYSRPKQLPDKW
CCCCCCCCCCCCCHH		23.86-
81UbiquitinationPAPYSRPKQLPDKWQ
CCCCCCCCCCCCHHC		64.4621890473
86UbiquitinationRPKQLPDKWQHDLFD
CCCCCCCHHCCCCCC		46.9821890473
86AcetylationRPKQLPDKWQHDLFD
CCCCCCCHHCCCCCC		46.9823954790
862-HydroxyisobutyrylationRPKQLPDKWQHDLFD
CCCCCCCHHCCCCCC		46.98-
88UbiquitinationKQLPDKWQHDLFDSG
CCCCCHHCCCCCCCC		26.4221890473
93UbiquitinationKWQHDLFDSGFGGGA
HHCCCCCCCCCCCCC		55.9721890473
93AcetylationKWQHDLFDSGFGGGA
HHCCCCCCCCCCCCC		55.97-
94PhosphorylationWQHDLFDSGFGGGAG
HCCCCCCCCCCCCCC		28.7825159151
101PhosphorylationSGFGGGAGVETGGKL
CCCCCCCCCCCCCEE		22.5220068231
104PhosphorylationGGGAGVETGGKLLVS
CCCCCCCCCCEEEEE		49.1525159151
111PhosphorylationTGGKLLVSNLDFGVS
CCCEEEEECCCCCCC		31.48-
131PhosphorylationELFAEFGTLKKAAVH
HHHHHHCCHHHEEEE		40.5028464451
1342-HydroxyisobutyrylationAEFGTLKKAAVHYDR
HHHCCHHHEEEEECC		44.69-
141MethylationKAAVHYDRSGRSLGT
HEEEEECCCCCCCCC		33.57115918425
141UbiquitinationKAAVHYDRSGRSLGT
HEEEEECCCCCCCCC		33.57-
141CitrullinationKAAVHYDRSGRSLGT
HEEEEECCCCCCCCC		33.57-
141CitrullinationKAAVHYDRSGRSLGT
HEEEEECCCCCCCCC		33.57-
142PhosphorylationAAVHYDRSGRSLGTA
EEEEECCCCCCCCCC		35.3428348404
145PhosphorylationHYDRSGRSLGTADVH
EECCCCCCCCCCCCH		34.3828985074
148PhosphorylationRSGRSLGTADVHFER
CCCCCCCCCCCHHHH		25.6121406692
148MethylationRSGRSLGTADVHFER
CCCCCCCCCCCHHHH		25.61-
149PhosphorylationSGRSLGTADVHFERK
CCCCCCCCCCHHHHH		18.28-
152PhosphorylationSLGTADVHFERKADA
CCCCCCCHHHHHHHH		21.28-
155PhosphorylationTADVHFERKADALKA
CCCCHHHHHHHHHHH		38.22-
1612-HydroxyisobutyrylationERKADALKAMKQYNG
HHHHHHHHHHHHHCC		48.43-
161AcetylationERKADALKAMKQYNG
HHHHHHHHHHHHHCC		48.4325953088
1642-HydroxyisobutyrylationADALKAMKQYNGVPL
HHHHHHHHHHCCCCC		55.26-
164UbiquitinationADALKAMKQYNGVPL
HHHHHHHHHHCCCCC		55.2621890473
164AcetylationADALKAMKQYNGVPL
HHHHHHHHHHCCCCC		55.2625953088
168UbiquitinationKAMKQYNGVPLDGRP
HHHHHHCCCCCCCCC		19.93-
171UbiquitinationKQYNGVPLDGRPMNI
HHHCCCCCCCCCCEE		11.5121890473
183PhosphorylationMNIQLVTSQIDAQRR
CEEEEECCHHHCCCC		20.0517525332
190PhosphorylationSQIDAQRRPAQSVNR
CHHHCCCCCCCCCCC		20.8717525332
190MethylationSQIDAQRRPAQSVNR
CHHHCCCCCCCCCCC		20.8781121841
194PhosphorylationAQRRPAQSVNRGGMT
CCCCCCCCCCCCCCC		24.3822210691
197Asymmetric dimethylarginineRPAQSVNRGGMTRNR
CCCCCCCCCCCCCCC		40.67-
197MethylationRPAQSVNRGGMTRNR
CCCCCCCCCCCCCCC		40.6712019549
202MethylationVNRGGMTRNRGAGGF
CCCCCCCCCCCCCCC		23.1930989535
204Asymmetric dimethylarginineRGGMTRNRGAGGFGG
CCCCCCCCCCCCCCC		32.80-
204MethylationRGGMTRNRGAGGFGG
CCCCCCCCCCCCCCC		32.8024129315
209MethylationRNRGAGGFGGGGGTR
CCCCCCCCCCCCCCC		8.87-
211MethylationRGAGGFGGGGGTRRG
CCCCCCCCCCCCCCC		29.34-
215PhosphorylationGFGGGGGTRRGTRGG
CCCCCCCCCCCCCCC		22.0722817900
216MethylationFGGGGGTRRGTRGGA
CCCCCCCCCCCCCCC		38.0030761363
219PhosphorylationGGGTRRGTRGGARGR
CCCCCCCCCCCCCCC		25.0822817900
220MethylationGGTRRGTRGGARGRG
CCCCCCCCCCCCCCC		44.35-
222PhosphorylationTRRGTRGGARGRGRG
CCCCCCCCCCCCCCC		14.60-
223MethylationRRGTRGGARGRGRGA
CCCCCCCCCCCCCCC		17.36-
226PhosphorylationTRGGARGRGRGAGRN
CCCCCCCCCCCCCCC		26.53-
227MethylationRGGARGRGRGAGRNS
CCCCCCCCCCCCCCC		34.89-
234PhosphorylationGRGAGRNSKQQLSAE
CCCCCCCCCCCCCHH		30.4020873877
235AcetylationRGAGRNSKQQLSAEE
CCCCCCCCCCCCHHH		45.6823749302
235MethylationRGAGRNSKQQLSAEE
CCCCCCCCCCCCHHH		45.6824129315
235UbiquitinationRGAGRNSKQQLSAEE
CCCCCCCCCCCCHHH		45.682190698
239PhosphorylationRNSKQQLSAEELDAQ
CCCCCCCCHHHHHHH		29.3325159151
242AcetylationKQQLSAEELDAQLDA
CCCCCHHHHHHHHHH		52.22-
242MethylationKQQLSAEELDAQLDA
CCCCCHHHHHHHHHH		52.22-
242UbiquitinationKQQLSAEELDAQLDA
CCCCCHHHHHHHHHH		52.2221890473
246PhosphorylationSAEELDAQLDAYNAR
CHHHHHHHHHHHHHH		39.2719413330
250PhosphorylationLDAQLDAYNARMDTS
HHHHHHHHHHHCCCC		14.7128152594
256PhosphorylationAYNARMDTS------
HHHHHCCCC------		27.3025849741
257PhosphorylationYNARMDTS-------
HHHHCCCC-------		33.6825849741
263PhosphorylationTS-------------
CC-------------		-
264PhosphorylationS--------------
C--------------		-
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
34SPhosphorylationKinaseAKT1P31749
PSP
219TPhosphorylationKinaseAKT1P31749
PSP
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference
204RMethylation


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_HUMAN !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
DX39A_HUMANDDX39Aphysical
15047853
DX39B_HUMANDDX39Bphysical
15047853
LEF1_HUMANLEF1physical
9119228
RUNX2_HUMANRUNX2physical
9119228
THOC4_HUMANALYREFphysical
9119228
ICP27_HHV8PORF57physical
18974867
NCBP1_HUMANNCBP1physical
18974867
THOC2_HUMANTHOC2physical
15998806
THOC5_HUMANTHOC5physical
15998806
THOC1_HUMANTHOC1physical
15998806
THOC3_HUMANTHOC3physical
15998806
THOC6_HUMANTHOC6physical
15998806
THOC7_HUMANTHOC7physical
15998806
DX39B_HUMANDDX39Bphysical
15998806
ZC3HD_HUMANZC3H13physical
15998806
VIR_HUMANKIAA1429physical
15998806
ACINU_HUMANACIN1physical
15998806
SRRM1_HUMANSRRM1physical
15998806
SRRT_HUMANSRRTphysical
15998806
U5S1_HUMANEFTUD2physical
15998806
RBM15_HUMANRBM15physical
15998806
DDX3X_HUMANDDX3Xphysical
15998806
U2AF2_HUMANU2AF2physical
15998806
SRSF2_HUMANSRSF2physical
15998806
SRSF7_HUMANSRSF7physical
15998806
SRSF1_HUMANSRSF1physical
15998806
STF1_HUMANNR5A1physical
17190602
SMAD4_HUMANSMAD4physical
17190602
NCBP1_HUMANNCBP1physical
17190602
DX39B_HUMANDDX39Bphysical
17190602
THOC2_HUMANTHOC2physical
17190602
THOC5_HUMANTHOC5physical
17190602
THOC1_HUMANTHOC1physical
17190602
THOC3_HUMANTHOC3physical
17190602
THOC6_HUMANTHOC6physical
17190602
THOC7_HUMANTHOC7physical
17190602
THOC5_HUMANTHOC5physical
19165146
NXF1_HUMANNXF1physical
19165146
DX39B_HUMANDDX39Bphysical
22939629
YBOX1_HUMANYBX1physical
22939629
TLE3_HUMANTLE3physical
22939629
WDR35_HUMANWDR35physical
22939629
UGGG1_HUMANUGGT1physical
22939629
TRIPC_HUMANTRIP12physical
22939629
VATE1_HUMANATP6V1E1physical
22939629
PCH2_HUMANTRIP13physical
22939629
UBA5_HUMANUBA5physical
22939629
UBC9_HUMANUBE2Iphysical
22939629
XPF_HUMANERCC4physical
22939629
IL7RA_HUMANIL7Rphysical
23151878
THOC2_HUMANTHOC2physical
23222130
DX39B_HUMANDDX39Bphysical
23222130
THOC3_HUMANTHOC3physical
23222130
THOC5_HUMANTHOC5physical
23222130
NCBP1_HUMANNCBP1physical
23222130
AKT1_HUMANAKT1physical
18562279
KC1E_HUMANCSNK1Ephysical
26344197
GNL1_HUMANGNL1physical
26344197
NAA16_HUMANNAA16physical
26344197
NP1L1_HUMANNAP1L1physical
26344197
NOP2_HUMANNOP2physical
26344197
PABP1_HUMANPABPC1physical
26344197
PABP4_HUMANPABPC4physical
26344197
XRN1_HUMANXRN1physical
26344197
LSM4_HUMANLSM4physical
27173435
LSM8_HUMANLSM8physical
27173435
UBIM_HUMANFAUphysical
27173435
LSM6_HUMANLSM6physical
27173435
Drug and Disease Associations
Kegg Disease
There are no disease associations of PTM sites.
OMIM Disease
There are no disease associations of PTM sites.
Kegg Drug
There are no disease associations of PTM sites.
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of THOC4_HUMAN

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Related Literatures of Post-Translational Modification
Methylation
ReferencePubMed
"Identifying and quantifying in vivo methylation sites by heavy methylSILAC.";
Ong S.E., Mittler G., Mann M.;
Nat. Methods 1:119-126(2004).
Cited for: METHYLATION [LARGE SCALE ANALYSIS] AT ARG-50 AND ARG-204, AND MASSSPECTROMETRY.
Phosphorylation
ReferencePubMed
"Quantitative phosphoproteomic analysis of T cell receptor signalingreveals 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).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-239, AND MASSSPECTROMETRY.
"A quantitative atlas of mitotic phosphorylation.";
Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,Elledge S.J., Gygi S.P.;
Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-8, AND MASSSPECTROMETRY.
"ATM and ATR substrate analysis reveals extensive protein networksresponsive to DNA damage.";
Matsuoka S., Ballif B.A., Smogorzewska A., McDonald E.R. III,Hurov K.E., Luo J., Bakalarski C.E., Zhao Z., Solimini N.,Lerenthal Y., Shiloh Y., Gygi S.P., Elledge S.J.;
Science 316:1160-1166(2007).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-183, AND MASSSPECTROMETRY.

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