dbPTM

THOC5_HUMAN - PTM Information in dbPTM

Basic Information of Protein

Overview of Protein Modification Sites with Functional and Structural Information
UniProt ID	THOC5_HUMAN
UniProt AC	Q13769
Protein Name	THO complex subunit 5 homolog
Gene Name	THOC5
Organism	Homo sapiens (Human).
Sequence Length	683
Subcellular Localization	Nucleus . Cytoplasm . Shuttles between nucleus and cytoplasm.
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. THOC5 in conjunction with ALYREF/THOC4 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 transcription elongation and genome stability. Involved in alternative polyadenylation site choice by recruiting CPSF6 to 5' region of target genes; probably mediates association of the TREX and CFIm complexes.; Regulates the expression of myeloid transcription factors CEBPA, CEBPB and GAB2 by enhancing the levels of phosphatidylinositol 3,4,5-trisphosphate. May be involved in the differentiation of granulocytes and adipocytes. Essential for hematopoietic primitive cell survival and plays an integral role in monocytic development..
Protein Sequence	MSSESSKKRKPKVIRSDGAPAEGKRNRSDTEQEGKYYSEEAEVDLRDPGRDYELYKYTCQELQRLMAEIQDLKSRGGKDVAIEIEERRIQSCVHFMTLKKLNRLAHIRLKKGRDQTHEAKQKVDAYHLQLQNLLYEVMHLQKEITKCLEFKSKHEEIDLVSLEEFYKEAPPDISKAEVTMGDPHQQTLARLDWELEQRKRLAEKYRECLSNKEKILKEIEVKKEYLSSLQPRLNSIMQASLPVQEYLFMPFDQAHKQYETARHLPPPLYVLFVQATAYGQACDKTLSVAIEGSVDEAKALFKPPEDSQDDESDSDAEEEQTTKRRRPTLGVQLDDKRKEMLKRHPLSVMLDLKCKDDSVLHLTFYYLMNLNIMTVKAKVTTAMELITPISAGDLLSPDSVLSCLYPGDHGKKTPNPANQYQFDKVGILTLSDYVLELGHPYLWVQKLGGLHFPKEQPQQTVIADHSLSASHMETTMKLLKTRVQSRLALHKQFASLEHGIVPVTSDCQYLFPAKVVSRLVKWVTVAHEDYMELHFTKDIVDAGLAGDTNLYYMALIERGTAKLQAAVVLNPGYSSIPPVFQLCLNWKGEKTNSNDDNIRAMEGEVNVCYKELCGPWPSHQLLTNQLQRLCVLLDVYLETESHDDSVEGPKEFPQEKMCLRLFRGPSRMKPFKYNHPQGFFSHR

Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations	Modification	Substrate Peptides & Secondary Structure	ASA (%)	Reference
2	Phosphorylation	------MSSESSKKR ------CCCCHHHCC	42.69	20068231
2	Acetylation	------MSSESSKKR ------CCCCHHHCC	42.69	22814378
2	O-linked_Glycosylation	------MSSESSKKR ------CCCCHHHCC	42.69	30379171
3	Phosphorylation	-----MSSESSKKRK -----CCCCHHHCCC	39.95	20068231
5	Phosphorylation	---MSSESSKKRKPK ---CCCCHHHCCCCC	49.78	15221008
6	Phosphorylation	--MSSESSKKRKPKV --CCCCHHHCCCCCE	37.84	15221008
16	Phosphorylation	RKPKVIRSDGAPAEG CCCCEECCCCCCCCC	29.31	20068231
24	Acetylation	DGAPAEGKRNRSDTE CCCCCCCCCCCCCCH	37.70	23954790
28	Phosphorylation	AEGKRNRSDTEQEGK CCCCCCCCCCHHCCC	53.05	28176443
30	Phosphorylation	GKRNRSDTEQEGKYY CCCCCCCCHHCCCEE	40.59	30576142
37	Phosphorylation	TEQEGKYYSEEAEVD CHHCCCEECCCEEEC	17.06	-
56	Ubiquitination	GRDYELYKYTCQELQ CCCHHHHHHHHHHHH	46.86	-
66	Sulfoxidation	CQELQRLMAEIQDLK HHHHHHHHHHHHHHH	3.24	21406390
73	2-Hydroxyisobutyrylation	MAEIQDLKSRGGKDV HHHHHHHHHCCCCCE	46.53	-
74	O-linked_Glycosylation	AEIQDLKSRGGKDVA HHHHHHHHCCCCCEE	43.38	30379171
78	Acetylation	DLKSRGGKDVAIEIE HHHHCCCCCEEEEEH	52.43	26051181
146	Ubiquitination	HLQKEITKCLEFKSK HHHHHHHHHHHHHHC	42.35	-
153	Sumoylation	KCLEFKSKHEEIDLV HHHHHHHCCCCCCEE	56.47	28112733
175	Ubiquitination	EAPPDISKAEVTMGD HCCCCCCCCEECCCC	49.23	-
180	Sulfoxidation	ISKAEVTMGDPHQQT CCCCEECCCCHHHHH	7.47	21406390
204	Acetylation	QRKRLAEKYRECLSN HHHHHHHHHHHHHHC	43.96	26051181
210	Phosphorylation	EKYRECLSNKEKILK HHHHHHHHCHHHHHH	58.47	-
212	Acetylation	YRECLSNKEKILKEI HHHHHHCHHHHHHHH	57.94	26051181
217	2-Hydroxyisobutyrylation	SNKEKILKEIEVKKE HCHHHHHHHHHHHHH	61.18	-
217	Acetylation	SNKEKILKEIEVKKE HCHHHHHHHHHHHHH	61.18	26051181
217	Ubiquitination	SNKEKILKEIEVKKE HCHHHHHHHHHHHHH	61.18	-
222	Ubiquitination	ILKEIEVKKEYLSSL HHHHHHHHHHHHHHC	27.39	-
223	2-Hydroxyisobutyrylation	LKEIEVKKEYLSSLQ HHHHHHHHHHHHHCH	57.69	-
223	Ubiquitination	LKEIEVKKEYLSSLQ HHHHHHHHHHHHHCH	57.69	-
225	Phosphorylation	EIEVKKEYLSSLQPR HHHHHHHHHHHCHHH	22.29	18373705
293	Phosphorylation	LSVAIEGSVDEAKAL EEEEEECCHHHHHHH	17.38	-
307	Phosphorylation	LFKPPEDSQDDESDS HCCCCCCCCCCCCCC	33.57	26846344
312	Phosphorylation	EDSQDDESDSDAEEE CCCCCCCCCCHHHHH	49.78	26846344
314	Phosphorylation	SQDDESDSDAEEEQT CCCCCCCCHHHHHHH	48.26	26846344
321	Phosphorylation	SDAEEEQTTKRRRPT CHHHHHHHHHHCCCC	37.25	23927012
322	Phosphorylation	DAEEEQTTKRRRPTL HHHHHHHHHHCCCCC	23.42	23927012
328	Phosphorylation	TTKRRRPTLGVQLDD HHHHCCCCCCCCCCH	34.04	29255136
336	Ubiquitination	LGVQLDDKRKEMLKR CCCCCCHHHHHHHHH	66.10	-
347	Phosphorylation	MLKRHPLSVMLDLKC HHHHCCCEEEEEEEE	15.21	20068231
412	Ubiquitination	YPGDHGKKTPNPANQ CCCCCCCCCCCCCCC	74.03	-
420	Phosphorylation	TPNPANQYQFDKVGI CCCCCCCCCCCCEEE	15.79	-
477	Ubiquitination	SHMETTMKLLKTRVQ HHHHHHHHHHHHHHH	48.88	-
477	Acetylation	SHMETTMKLLKTRVQ HHHHHHHHHHHHHHH	48.88	25953088
491	Acetylation	QSRLALHKQFASLEH HHHHHHHHHHHCCCC	48.22	26051181
514	Ubiquitination	CQYLFPAKVVSRLVK CCEECCHHHHHHHHH	43.33	-
517	Phosphorylation	LFPAKVVSRLVKWVT ECCHHHHHHHHHHHH	23.92	27174698
524	Phosphorylation	SRLVKWVTVAHEDYM HHHHHHHHHCCHHHH	15.74	27174698
530	Phosphorylation	VTVAHEDYMELHFTK HHHCCHHHHHHEECC	6.90	27174698
536	Phosphorylation	DYMELHFTKDIVDAG HHHHHEECCCCHHCC	19.63	27174698
610	Acetylation	GEVNVCYKELCGPWP CCEEEEHHHHHCCCC	38.80	26051181

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
5	S	Phosphorylation	Kinase	PRKCA	P17252	GPS
6	S	Phosphorylation	Kinase	PRKCA	P17252	GPS
225	Y	Phosphorylation	Kinase	PDGFRB	P09619	PSP
225	Y	Phosphorylation	Kinase	SRC	P12931	Uniprot
307	S	Phosphorylation	Kinase	ATM	Q13315	PSP
312	S	Phosphorylation	Kinase	ATM	Q13315	PSP
314	S	Phosphorylation	Kinase	ATM	Q13315	PSP

Functions of PTM Sites

Modified Location	Modified Residue	Modification	Reference
5	S	Phosphorylation	23032722
Phosphorylation on Ser-5 and/or Ser-6 is required for nuclear export.
6	S	Phosphorylation	23032722
Phosphorylation on Ser-5 and/or Ser-6 is required for nuclear export.
328	T	Phosphorylation	20068231
Phosphorylated on Thr-328 in insulin-stimulated adipocytes (By similarity).

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 THOC5_HUMAN !!

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference
DX39B_HUMAN	DDX39B	physical	15998806
THOC2_HUMAN	THOC2	physical	15998806
THOC1_HUMAN	THOC1	physical	15998806
THOC3_HUMAN	THOC3	physical	15998806
THOC6_HUMAN	THOC6	physical	15998806
THOC7_HUMAN	THOC7	physical	15998806
THOC4_HUMAN	ALYREF	physical	15998806
SMAD4_HUMAN	SMAD4	physical	17190602
NCBP1_HUMAN	NCBP1	physical	17190602
THOC4_HUMAN	ALYREF	physical	17190602
DX39B_HUMAN	DDX39B	physical	17190602
THOC2_HUMAN	THOC2	physical	17190602
THOC7_HUMAN	THOC7	physical	22939629
THOC6_HUMAN	THOC6	physical	22939629
ZC3HF_HUMAN	ZC3H15	physical	22939629
XPO4_HUMAN	XPO4	physical	22939629
ZKSC5_HUMAN	ZKSCAN5	physical	22939629
VIME_HUMAN	VIM	physical	22939629
U3IP2_HUMAN	RRP9	physical	22939629
UTRO_HUMAN	UTRN	physical	22939629
ZPR1_HUMAN	ZPR1	physical	22939629
ZN606_HUMAN	ZNF606	physical	22939629
ZO2_HUMAN	TJP2	physical	22939629
UBR7_HUMAN	UBR7	physical	22939629
LSM3_HUMAN	LSM3	physical	22365833
PPIL1_HUMAN	PPIL1	physical	22365833
THOC1_HUMAN	THOC1	physical	22365833
ZN830_HUMAN	ZNF830	physical	22365833
THOC2_HUMAN	THOC2	physical	26344197
THOC3_HUMAN	THOC3	physical	26344197
THOC6_HUMAN	THOC6	physical	26344197
THOC7_HUMAN	THOC7	physical	26344197
ZO1_HUMAN	TJP1	physical	26344197
FMNL1_HUMAN	FMNL1	physical	26496610
T2FA_HUMAN	GTF2F1	physical	26496610
PGFRA_HUMAN	PDGFRA	physical	26496610
RL6_HUMAN	RPL6	physical	26496610
RL22_HUMAN	RPL22	physical	26496610
RL27A_HUMAN	RPL27A	physical	26496610
DX39B_HUMAN	DDX39B	physical	26496610
IF4A3_HUMAN	EIF4A3	physical	26496610
ZC11A_HUMAN	ZC3H11A	physical	26496610
THOC1_HUMAN	THOC1	physical	26496610
THOC4_HUMAN	ALYREF	physical	26496610
DX39A_HUMAN	DDX39A	physical	26496610
KIF1C_HUMAN	KIF1C	physical	26496610
RT27_HUMAN	MRPS27	physical	26496610
SIR1_HUMAN	SIRT1	physical	26496610
CCDC9_HUMAN	CCDC9	physical	26496610
CHTOP_HUMAN	CHTOP	physical	26496610
WDR74_HUMAN	WDR74	physical	26496610
MGN2_HUMAN	MAGOHB	physical	26496610
NCBP3_HUMAN	C17orf85	physical	26496610
DDX24_HUMAN	DDX24	physical	26496610
THOC2_HUMAN	THOC2	physical	26496610
K1522_HUMAN	KIAA1522	physical	26496610
MYO1G_HUMAN	MYO1G	physical	26496610
THOC6_HUMAN	THOC6	physical	26496610
ZC3HE_HUMAN	ZC3H14	physical	26496610
THOC7_HUMAN	THOC7	physical	26496610
KLF16_HUMAN	KLF16	physical	26496610
UIF_HUMAN	FYTTD1	physical	26496610
PDIP3_HUMAN	POLDIP3	physical	26496610
THOC3_HUMAN	THOC3	physical	26496610
SPB12_HUMAN	SERPINB12	physical	26496610
IMP4_HUMAN	IMP4	physical	26496610
CS047_HUMAN	C19orf47	physical	26496610

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 THOC5_HUMAN

Related Literatures of Post-Translational Modification

Phosphorylation
Reference	PubMed
"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-307; SER-312 ANDSER-314, AND MASS SPECTROMETRY.	19690332 [Abstract]
"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: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-312 AND SER-314, ANDMASS SPECTROMETRY.	19413330 [Abstract]
"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-307; SER-312 ANDSER-314, AND MASS SPECTROMETRY.	18669648 [Abstract]
"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-307; SER-312 ANDSER-314, AND MASS SPECTROMETRY.	17525332 [Abstract]
"Global, in vivo, and site-specific phosphorylation dynamics insignaling networks."; Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P.,Mann M.; Cell 127:635-648(2006). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-312 AND SER-314, ANDMASS SPECTROMETRY.	17081983 [Abstract]
"THOC5 spliceosome protein: a target for leukaemogenic tyrosinekinases that affects inositol lipid turnover."; Pierce A., Carney L., Hamza H.G., Griffiths J.R., Zhang L.,Whetton B.A., Gonzalez Sanchez M.B., Tamura T., Sternberg D.,Whetton A.D.; Br. J. Haematol. 141:641-650(2008). Cited for: MASS SPECTROMETRY, AND PHOSPHORYLATION AT TYR-225.	18373705 [Abstract]

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