THOC3_HUMAN - dbPTM
THOC3_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID THOC3_HUMAN
UniProt AC Q96J01
Protein Name THO complex subunit 3
Gene Name THOC3
Organism Homo sapiens (Human).
Sequence Length 351
Subcellular Localization Nucleus . Nucleus speckle .
Protein Description Required for efficient export of polyadenylated RNA and spliced mRNA. 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..
Protein Sequence MAVPAAAMGPSALGQSGPGSMAPWCSVSSGPSRYVLGMQELFRGHSKTREFLAHSAKVHSVAWSCDGRRLASGSFDKTASVFLLEKDRLVKENNYRGHGDSVDQLCWHPSNPDLFVTASGDKTIRIWDVRTTKCIATVNTKGENINICWSPDGQTIAVGNKDDVVTFIDAKTHRSKAEEQFKFEVNEISWNNDNNMFFLTNGNGCINILSYPELKPVQSINAHPSNCICIKFDPMGKYFATGSADALVSLWDVDELVCVRCFSRLDWPVRTLSFSHDGKMLASASEDHFIDIAEVETGDKLWEVQCESPTFTVAWHPKRPLLAFACDDKDGKYDSSREAGTVKLFGLPNDS
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------MAVPAAAMG
------CCCCCHHCC		18.9222223895
11PhosphorylationPAAAMGPSALGQSGP
CCHHCCCCCCCCCCC		30.3228348404
16PhosphorylationGPSALGQSGPGSMAP
CCCCCCCCCCCCCCC		45.1928348404
20PhosphorylationLGQSGPGSMAPWCSV
CCCCCCCCCCCCEEC		18.2028348404
26PhosphorylationGSMAPWCSVSSGPSR
CCCCCCEECCCCCCC		22.5924043423
28PhosphorylationMAPWCSVSSGPSRYV
CCCCEECCCCCCCEE		17.1824043423
29PhosphorylationAPWCSVSSGPSRYVL
CCCEECCCCCCCEEE		53.2022210691
32PhosphorylationCSVSSGPSRYVLGMQ
EECCCCCCCEEECHH		39.5122210691
34PhosphorylationVSSGPSRYVLGMQEL
CCCCCCCEEECHHHH		12.3624043423
43MethylationLGMQELFRGHSKTRE
ECHHHHHCCCHHHHH		55.31115918421
45UbiquitinationMQELFRGHSKTREFL
HHHHHCCCHHHHHHH		23.1227667366
57UbiquitinationEFLAHSAKVHSVAWS
HHHHHCCCEEEEEEE		43.4229967540
60PhosphorylationAHSAKVHSVAWSCDG
HHCCCEEEEEEEECC		19.2720873877
64PhosphorylationKVHSVAWSCDGRRLA
CEEEEEEEECCCEEC		7.8120873877
65GlutathionylationVHSVAWSCDGRRLAS
EEEEEEEECCCEECC		4.4822555962
72PhosphorylationCDGRRLASGSFDKTA
ECCCEECCCCCCCCE		39.2920873877
74PhosphorylationGRRLASGSFDKTASV
CCEECCCCCCCCEEE		27.9828355574
77MethylationLASGSFDKTASVFLL
ECCCCCCCCEEEEEE		43.9438016267
77UbiquitinationLASGSFDKTASVFLL
ECCCCCCCCEEEEEE		43.9429967540
77UbiquitinationLASGSFDKTASVFLL
ECCCCCCCCEEEEEE		43.9421890473
83UbiquitinationDKTASVFLLEKDRLV
CCCEEEEEEECCCCC		5.9021890473
86UbiquitinationASVFLLEKDRLVKEN
EEEEEEECCCCCCCC		48.3821906983
86AcetylationASVFLLEKDRLVKEN
EEEEEEECCCCCCCC		48.3826051181
862-HydroxyisobutyrylationASVFLLEKDRLVKEN
EEEEEEECCCCCCCC		48.38-
86UbiquitinationASVFLLEKDRLVKEN
EEEEEEECCCCCCCC		48.3821890473
88UbiquitinationVFLLEKDRLVKENNY
EEEEECCCCCCCCCC		53.0723000965
91UbiquitinationLEKDRLVKENNYRGH
EECCCCCCCCCCCCC		60.3521906983
91UbiquitinationLEKDRLVKENNYRGH
EECCCCCCCCCCCCC		60.3521890473
101PhosphorylationNYRGHGDSVDQLCWH
CCCCCCCCHHHEEEC		31.9920873877
104UbiquitinationGHGDSVDQLCWHPSN
CCCCCHHHEEECCCC		36.0421890473
110PhosphorylationDQLCWHPSNPDLFVT
HHEEECCCCCCEEEE		48.3720873877
113UbiquitinationCWHPSNPDLFVTASG
EECCCCCCEEEEECC		57.9221890473
117PhosphorylationSNPDLFVTASGDKTI
CCCCEEEEECCCCEE		14.0520873877
118UbiquitinationNPDLFVTASGDKTIR
CCCEEEEECCCCEEE		13.2521890473
119PhosphorylationPDLFVTASGDKTIRI
CCEEEEECCCCEEEE		37.8520873877
122UbiquitinationFVTASGDKTIRIWDV
EEEECCCCEEEEEEC		49.7529967540
123O-linked_GlycosylationVTASGDKTIRIWDVR
EEECCCCEEEEEECC		21.8930620550
125MethylationASGDKTIRIWDVRTT
ECCCCEEEEEECCCC		29.22115918413
130MethylationTIRIWDVRTTKCIAT
EEEEEECCCCEEEEE		33.92115918417
133UbiquitinationIWDVRTTKCIATVNT
EEECCCCEEEEEECC		24.0327667366
133UbiquitinationIWDVRTTKCIATVNT
EEECCCCEEEEEECC		24.03-
133AcetylationIWDVRTTKCIATVNT
EEECCCCEEEEEECC		24.0325953088
141UbiquitinationCIATVNTKGENINIC
EEEEECCCCCCEEEE		60.0529967540
166PhosphorylationGNKDDVVTFIDAKTH
CCCCCEEEEEECCCC		18.09-
171SumoylationVVTFIDAKTHRSKAE
EEEEEECCCCCHHHH		40.91-
171UbiquitinationVVTFIDAKTHRSKAE
EEEEEECCCCCHHHH		40.9123000965
171SumoylationVVTFIDAKTHRSKAE
EEEEEECCCCCHHHH		40.91-
171UbiquitinationVVTFIDAKTHRSKAE
EEEEEECCCCCHHHH		40.9121890473
176UbiquitinationDAKTHRSKAEEQFKF
ECCCCCHHHHHHHEE		60.8323000965
198UbiquitinationNNDNNMFFLTNGNGC
CCCCCEEEEECCCCE		5.9821890473
244UbiquitinationKYFATGSADALVSLW
CEECCCCCCEEEECC		13.8722505724
255UbiquitinationVSLWDVDELVCVRCF
EECCCCCCEEEEHHH		42.8424816145
264MethylationVCVRCFSRLDWPVRT
EEEHHHHCCCCCEEE		19.2030989529
271PhosphorylationRLDWPVRTLSFSHDG
CCCCCEEEEEECCCC		27.3020873877
273PhosphorylationDWPVRTLSFSHDGKM
CCCEEEEEECCCCCE		24.8820873877
275PhosphorylationPVRTLSFSHDGKMLA
CEEEEEECCCCCEEE		19.7920873877
297 (in isoform 2)Phosphorylation-56.7222210691
304 (in isoform 2)Phosphorylation-5.5122210691
308PhosphorylationLWEVQCESPTFTVAW
EEEEEECCCCEEEEE		36.5525159151
310PhosphorylationEVQCESPTFTVAWHP
EEEECCCCEEEEECC		41.0127251275
312PhosphorylationQCESPTFTVAWHPKR
EECCCCEEEEECCCC		16.2827251275
318UbiquitinationFTVAWHPKRPLLAFA
EEEEECCCCCEEEEE		54.4829967540
329UbiquitinationLAFACDDKDGKYDSS
EEEEEECCCCCCCCC		55.9529967540
329AcetylationLAFACDDKDGKYDSS
EEEEEECCCCCCCCC		55.9526051181
332UbiquitinationACDDKDGKYDSSREA
EEECCCCCCCCCCCC		56.8922505724
332AcetylationACDDKDGKYDSSREA
EEECCCCCCCCCCCC		56.8926051181
333PhosphorylationCDDKDGKYDSSREAG
EECCCCCCCCCCCCE		26.96-
335PhosphorylationDKDGKYDSSREAGTV
CCCCCCCCCCCCEEE		28.36-
343UbiquitinationSREAGTVKLFGLPND
CCCCEEEEEECCCCC		37.6327667366
343SumoylationSREAGTVKLFGLPND
CCCCEEEEEECCCCC		37.63-
370Ubiquitination--------------------------
--------------------------		21890473
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 THOC3_HUMAN !!
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of THOC3_HUMAN !!
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 THOC3_HUMAN !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
THOC5_HUMANTHOC5physical
22939629
THOC7_HUMANTHOC7physical
22939629
THOC6_HUMANTHOC6physical
22939629
ZCRB1_HUMANZCRB1physical
22939629
ZC3HF_HUMANZC3H15physical
22939629
VIME_HUMANVIMphysical
22939629
TTC1_HUMANTTC1physical
22939629
UTRO_HUMANUTRNphysical
22939629
ZKSC5_HUMANZKSCAN5physical
22939629
THOC5_HUMANTHOC5physical
23222130
THOC2_HUMANTHOC2physical
23222130
THOC4_HUMANALYREFphysical
23222130
NCBP1_HUMANNCBP1physical
23222130
PAK2_HUMANPAK2physical
26344197
THOC1_HUMANTHOC1physical
26344197
THOC2_HUMANTHOC2physical
26344197
THOC6_HUMANTHOC6physical
26344197
THOC1_HUMANTHOC1physical
28514442
THOC7_HUMANTHOC7physical
28514442
THOC5_HUMANTHOC5physical
28514442
THOC2_HUMANTHOC2physical
28514442
TCPW_HUMANCCT6Bphysical
28514442
APBP2_HUMANAPPBP2physical
28514442
TCPD_HUMANCCT4physical
28514442
TCPB_HUMANCCT2physical
28514442
TCPA_HUMANTCP1physical
28514442
THOC6_HUMANTHOC6physical
28514442
TCPG_HUMANCCT3physical
28514442
CLU_HUMANCLUHphysical
28514442
TCPZ_HUMANCCT6Aphysical
28514442
TCPE_HUMANCCT5physical
28514442
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 THOC3_HUMAN

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Related Literatures of Post-Translational Modification
Acetylation
ReferencePubMed
"Lys-N and trypsin cover complementary parts of the phosphoproteome ina refined SCX-based approach.";
Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J.,Mohammed S.;
Anal. Chem. 81:4493-4501(2009).
Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, AND MASS SPECTROMETRY.

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