THOC6_HUMAN - dbPTM
THOC6_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID THOC6_HUMAN
UniProt AC Q86W42
Protein Name THO complex subunit 6 homolog
Gene Name THOC6
Organism Homo sapiens (Human).
Sequence Length 341
Subcellular Localization Nucleus . Nucleus speckle .
Protein Description 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. Plays a role in apoptosis negative control involved in brain development..
Protein Sequence MERAVPLAVPLGQTEVFQALQRLHMTIFSQSVSPCGKFLAAGNNYGQIAIFSLSSALSSEAKEESKKPVVTFQAHDGPVYSMVSTDRHLLSAGDGEVKAWLWAEMLKKGCKELWRRQPPYRTSLEVPEINALLLVPKENSLILAGGDCQLHTMDLETGTFTRVLRGHTDYIHCLALRERSPEVLSGGEDGAVRLWDLRTAKEVQTIEVYKHEECSRPHNGRWIGCLATDSDWMVCGGGPALTLWHLRSSTPTTIFPIRAPQKHVTFYQDLILSAGQGRCVNQWQLSGELKAQVPGSSPGLLSLSLNQQPAAPECKVLTAAGNSCRVDVFTNLGYRAFSLSF
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
67UbiquitinationEAKEESKKPVVTFQA
HHHHHHCCCEEEEEC
52.9329967540
83 (in isoform 2)Ubiquitination-4.6021890473
83UbiquitinationDGPVYSMVSTDRHLL
CCCEEEEEECCCCHH
4.6032015554
91PhosphorylationSTDRHLLSAGDGEVK
ECCCCHHCCCCHHHH
36.2420860994
107UbiquitinationWLWAEMLKKGCKELW
HHHHHHHHHHHHHHH
45.8921890473
107 (in isoform 3)Ubiquitination-45.8921890473
107 (in isoform 1)Ubiquitination-45.8921890473
107AcetylationWLWAEMLKKGCKELW
HHHHHHHHHHHHHHH
45.8926051181
122PhosphorylationRRQPPYRTSLEVPEI
HHCCCCCCCCCCCCC
31.6428857561
123PhosphorylationRQPPYRTSLEVPEIN
HCCCCCCCCCCCCCC
17.3428857561
177 (in isoform 2)Ubiquitination-31.5121890473
177UbiquitinationYIHCLALRERSPEVL
EEEEEEEECCCHHHH
31.5133845483
180PhosphorylationCLALRERSPEVLSGG
EEEEECCCHHHHCCC
22.2129255136
185PhosphorylationERSPEVLSGGEDGAV
CCCHHHHCCCCCCCE
50.3420068231
201 (in isoform 1)Ubiquitination-58.7821890473
201UbiquitinationLWDLRTAKEVQTIEV
EEECCCCCEEEEEEE
58.7822817900
201 (in isoform 3)Ubiquitination-58.7821890473
210UbiquitinationVQTIEVYKHEECSRP
EEEEEEEECCCCCCC
50.11-
210AcetylationVQTIEVYKHEECSRP
EEEEEEEECCCCCCC
50.1126051181
248PhosphorylationLTLWHLRSSTPTTIF
EEEEECCCCCCCEEE
44.9423312004
249PhosphorylationTLWHLRSSTPTTIFP
EEEECCCCCCCEEEE
31.7823312004
250PhosphorylationLWHLRSSTPTTIFPI
EEECCCCCCCEEEEC
26.3823312004
262UbiquitinationFPIRAPQKHVTFYQD
EECCCCCCCEEEEHH
38.7017623298
290UbiquitinationWQLSGELKAQVPGSS
EEECCEEEEECCCCC
32.2517623298
330PhosphorylationSCRVDVFTNLGYRAF
CCEEEEEECCCEEEE
29.40-
334PhosphorylationDVFTNLGYRAFSLSF
EEEECCCEEEEEECC
11.26-
338PhosphorylationNLGYRAFSLSF----
CCCEEEEEECC----
23.32-

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 THOC6_HUMAN !!

Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of THOC6_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 THOC6_HUMAN !!

Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
THOC7_HUMANTHOC7physical
22939629
U2AF2_HUMANU2AF2physical
22939629
U5S1_HUMANEFTUD2physical
22939629
U2AF1_HUMANU2AF1physical
22939629
U520_HUMANSNRNP200physical
22939629
ZCHC8_HUMANZCCHC8physical
22939629
ZC3HF_HUMANZC3H15physical
22939629
U3IP2_HUMANRRP9physical
22939629
TPR_HUMANTPRphysical
22939629
UTRO_HUMANUTRNphysical
22939629
ZN326_HUMANZNF326physical
22939629
TRI55_HUMANTRIM55physical
22939629
VDAC2_HUMANVDAC2physical
22939629
2AAA_HUMANPPP2R1Aphysical
26344197
THOC1_HUMANTHOC1physical
26344197
THOC7_HUMANTHOC7physical
26344197

Drug and Disease Associations
Kegg Disease
There are no disease associations of PTM sites.
OMIM Disease
613680Beaulieu-Boycott-Innes syndrome (BBIS)
Kegg Drug
There are no disease associations of PTM sites.
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of THOC6_HUMAN

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Related Literatures of Post-Translational Modification

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