THOC7_HUMAN - dbPTM
THOC7_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID THOC7_HUMAN
UniProt AC Q6I9Y2
Protein Name THO complex subunit 7 homolog
Gene Name THOC7
Organism Homo sapiens (Human).
Sequence Length 204
Subcellular Localization Cytoplasm . Nucleus . Nucleus speckle . Interaction with THOC5 is required for nuclear localization.
Protein Description Required for efficient export of polyadenylated RNA. 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 MGAVTDDEVIRKRLLIDGDGAGDDRRINLLVKSFIKWCNSGSQEEGYSQYQRMLSTLSQCEFSMGKTLLVYDMNLREMENYEKIYKEIECSIAGAHEKIAECKKQILQAKRIRKNRQEYDALAKVIQHHPDRHETLKELEALGKELEHLSHIKESVEDKLELRRKQFHVLLSTIHELQQTLENDEKLSEVEEAQEASMETDPKP
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------MGAVTDDEV
------CCCCCCHHH		28.8419413330
5Phosphorylation---MGAVTDDEVIRK
---CCCCCCHHHHHH		36.8825159151
32AcetylationRRINLLVKSFIKWCN
HHHHHHHHHHHHHHC		39.3525953088
32UbiquitinationRRINLLVKSFIKWCN
HHHHHHHHHHHHHHC		39.3521890473
33PhosphorylationRINLLVKSFIKWCNS
HHHHHHHHHHHHHCC		25.4024719451
36AcetylationLLVKSFIKWCNSGSQ
HHHHHHHHHHCCCCC		43.6219608861
36UbiquitinationLLVKSFIKWCNSGSQ
HHHHHHHHHHCCCCC		43.6219608861
67PhosphorylationCEFSMGKTLLVYDMN
CCHHCCCEEEEEECC		21.4229083192
71PhosphorylationMGKTLLVYDMNLREM
CCCEEEEEECCHHHH		14.9427762562
83UbiquitinationREMENYEKIYKEIEC
HHHHHHHHHHHHHHH		40.76-
85PhosphorylationMENYEKIYKEIECSI
HHHHHHHHHHHHHHH		17.4027642862
86AcetylationENYEKIYKEIECSIA
HHHHHHHHHHHHHHC		56.5425825284
86UbiquitinationENYEKIYKEIECSIA
HHHHHHHHHHHHHHC		56.54-
90GlutathionylationKIYKEIECSIAGAHE
HHHHHHHHHHCCHHH		4.3622555962
91PhosphorylationIYKEIECSIAGAHEK
HHHHHHHHHCCHHHH		11.5926074081
98AcetylationSIAGAHEKIAECKKQ
HHCCHHHHHHHHHHH		37.0326051181
98UbiquitinationSIAGAHEKIAECKKQ
HHCCHHHHHHHHHHH		37.03-
104UbiquitinationEKIAECKKQILQAKR
HHHHHHHHHHHHHHH		54.98-
110AcetylationKKQILQAKRIRKNRQ
HHHHHHHHHHHHHHH		35.0825953088
110UbiquitinationKKQILQAKRIRKNRQ
HHHHHHHHHHHHHHH		35.08-
1102-HydroxyisobutyrylationKKQILQAKRIRKNRQ
HHHHHHHHHHHHHHH		35.08-
114UbiquitinationLQAKRIRKNRQEYDA
HHHHHHHHHHHHHHH		54.86-
119PhosphorylationIRKNRQEYDALAKVI
HHHHHHHHHHHHHHH		9.7428796482
124UbiquitinationQEYDALAKVIQHHPD
HHHHHHHHHHHHCCC		40.49-
135PhosphorylationHHPDRHETLKELEAL
HCCCHHHHHHHHHHH		36.68-
137UbiquitinationPDRHETLKELEALGK
CCHHHHHHHHHHHHH		68.61-
144UbiquitinationKELEALGKELEHLSH
HHHHHHHHHHHHHHH		61.04-
1442-HydroxyisobutyrylationKELEALGKELEHLSH
HHHHHHHHHHHHHHH		61.04-
153UbiquitinationLEHLSHIKESVEDKL
HHHHHHHHHHHHHHH		38.21-
155PhosphorylationHLSHIKESVEDKLEL
HHHHHHHHHHHHHHH		26.2920068231
1592-HydroxyisobutyrylationIKESVEDKLELRRKQ
HHHHHHHHHHHHHHH		30.29-
159UbiquitinationIKESVEDKLELRRKQ
HHHHHHHHHHHHHHH		30.29-
188PhosphorylationLENDEKLSEVEEAQE
HHCCHHHHHHHHHHH		51.1420068231
197PhosphorylationVEEAQEASMETDPKP
HHHHHHHHHCCCCCC		19.1925159151
200PhosphorylationAQEASMETDPKP---
HHHHHHCCCCCC---		49.3027251275
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 THOC7_HUMAN !!
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of THOC7_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 THOC7_HUMAN !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
CHD3_HUMANCHD3physical
16169070
ZCRB1_HUMANZCRB1physical
22939629
UBP13_HUMANUSP13physical
22939629
ZC3HF_HUMANZC3H15physical
22939629
UBE3C_HUMANUBE3Cphysical
22939629
VIP2_HUMANPPIP5K2physical
22939629
VIME_HUMANVIMphysical
22939629
WDR36_HUMANWDR36physical
22939629
ZN606_HUMANZNF606physical
22939629
ZPR1_HUMANZPR1physical
22939629
TR112_HUMANTRMT112physical
22939629
THOC1_HUMANTHOC1physical
26344197
THOC3_HUMANTHOC3physical
26344197
DSRAD_HUMANADARphysical
26496610
B2CL2_HUMANBCL2L2physical
26496610
DHX9_HUMANDHX9physical
26496610
IPP2_HUMANPPP1R2physical
26496610
DX39B_HUMANDDX39Bphysical
26496610
AK17A_HUMANAKAP17Aphysical
26496610
THOC5_HUMANTHOC5physical
26496610
IF4A3_HUMANEIF4A3physical
26496610
ZC11A_HUMANZC3H11Aphysical
26496610
THOC1_HUMANTHOC1physical
26496610
THOC4_HUMANALYREFphysical
26496610
DX39A_HUMANDDX39Aphysical
26496610
DDX17_HUMANDDX17physical
26496610
CCDC9_HUMANCCDC9physical
26496610
CHTOP_HUMANCHTOPphysical
26496610
RBM27_HUMANRBM27physical
26496610
ALKB5_HUMANALKBH5physical
26496610
NCBP3_HUMANC17orf85physical
26496610
THOC2_HUMANTHOC2physical
26496610
SFR19_HUMANSCAF1physical
26496610
THOC6_HUMANTHOC6physical
26496610
ZC3HE_HUMANZC3H14physical
26496610
UIF_HUMANFYTTD1physical
26496610
PDIP3_HUMANPOLDIP3physical
26496610
THOC3_HUMANTHOC3physical
26496610
SARNP_HUMANSARNPphysical
26496610
CS047_HUMANC19orf47physical
26496610
RBM33_HUMANRBM33physical
26496610
CO052_HUMANC15orf52physical
26496610
Drug and Disease Associations
Kegg Disease
OMIM Disease
There are no disease associations of PTM sites.
Kegg Drug
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of THOC7_HUMAN

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Related Literatures of Post-Translational Modification
Acetylation
ReferencePubMed
"Lysine acetylation targets protein complexes and co-regulates majorcellular functions.";
Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T.,Olsen J.V., Mann M.;
Science 325:834-840(2009).
Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-36, AND MASS SPECTROMETRY.

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