dbPTM

THOC5_MOUSE - PTM Information in dbPTM

Basic Information of Protein

Overview of Protein Modification Sites with Functional and Structural Information
UniProt ID	THOC5_MOUSE
UniProt AC	Q8BKT7
Protein Name	THO complex subunit 5 homolog
Gene Name	Thoc5
Organism	Mus musculus (Mouse).
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. 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	MSSESSKKRKPKVIRSDGTPTEGKRNRSDTEQEGKYYSEEAEVDLRDPGRDYELYKYTCQELQRLMAEIQDLKSKGSKDVAIEIEERRIQSCVHFMTLKKLNRLAHIRLKKGRDQTHEAKQKVDAYHLQLQNLLYEVMHLQKEITKCLEFKSKHEEIDLVSLEEFYSEAPPSISKAEITMGDPHQQTLARLDWELEQRKRLAEKYRECLSNKEKILKEIEVKRDYLSSLQPRLNSIMQASLPVQEYLFMPFDQAHKQYETARHLPPPLYVLFVQATAYGQACDKTLSVAIEGSVDEAKALFKPPEDSQDDESDSDAEEEQTTKRRRPTLGVQLDDKRKEMLKRHPLSVLLDLKCKDNSVLHLTFYYLMNLNIMTVKAKVTTAVELITPISAGDLLSPDSVLSCLYPGDHGKKTPNPANQYQFDKVGILTLRDYVLELGHPYLWVQKLGGLHFPKEQPQQTVMPDHSQSASHMETTMKLLKTRVQSRLALHKQFASLEHGIVPVTSDCQDLFPAKVVSRLVKWVIITHEDYMELHFTKDIVEAGLAGDTNLYYLALIERGTAKLQAAVVLNPGYSSIPPVFRLCLNWKGEKTNSNDDNIRAMESEVNVCYKELCGPRPSHQLLTNQLQRLCVLLDVYLETESHDDSFEGPKEFPQEKMCLRLFRGPSRMKPFKYNHPQGFFSHR

Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations	Modification	Substrate Peptides & Secondary Structure	ASA (%)	Reference
2	Acetylation	------MSSESSKKR ------CCCCCHHCC	42.69	-
2	Phosphorylation	------MSSESSKKR ------CCCCCHHCC	42.69	26745281
3	Phosphorylation	-----MSSESSKKRK -----CCCCCHHCCC	39.95	26745281
5	Phosphorylation	---MSSESSKKRKPK ---CCCCCHHCCCCC	49.78	15221008
6	Phosphorylation	--MSSESSKKRKPKV --CCCCCHHCCCCCE	37.84	15221008
16	Phosphorylation	RKPKVIRSDGTPTEG CCCCEECCCCCCCCC	29.30	19737024
19	Phosphorylation	KVIRSDGTPTEGKRN CEECCCCCCCCCCCC	31.84	23684622
21	Phosphorylation	IRSDGTPTEGKRNRS ECCCCCCCCCCCCCC	58.15	29550500
24	Acetylation	DGTPTEGKRNRSDTE CCCCCCCCCCCCCCC	40.02	130261
28	Phosphorylation	TEGKRNRSDTEQEGK CCCCCCCCCCCCCCC	53.05	27087446
30	Phosphorylation	GKRNRSDTEQEGKYY CCCCCCCCCCCCCEE	40.59	23684622
59	S-nitrosylation	YELYKYTCQELQRLM HHHHHHHHHHHHHHH	2.41	20925432
59	S-nitrosocysteine	YELYKYTCQELQRLM HHHHHHHHHHHHHHH	2.41	-
74	Phosphorylation	AEIQDLKSKGSKDVA HHHHHHHHCCCCCEE	49.93	24719451
91	Phosphorylation	IEERRIQSCVHFMTL HHHHHHHHHHHHHHH	18.74	28609623
97	Phosphorylation	QSCVHFMTLKKLNRL HHHHHHHHHHHHHHH	34.19	28609623
204	Acetylation	QRKRLAEKYRECLSN HHHHHHHHHHHHHHC	43.96	7631021
225	Phosphorylation	EIEVKRDYLSSLQPR HHHHHHHHHHHCHHH	16.71	19015024
235	Phosphorylation	SLQPRLNSIMQASLP HCHHHHHHHHHHCCC	24.83	25367039
240	Phosphorylation	LNSIMQASLPVQEYL HHHHHHHCCCHHHHC	19.13	25367039
246	Phosphorylation	ASLPVQEYLFMPFDQ HCCCHHHHCCCCHHH	6.53	25367039
285	Phosphorylation	YGQACDKTLSVAIEG HHHHCCCCEEEEEEC	15.83	28285833
307	Phosphorylation	LFKPPEDSQDDESDS HCCCCCCCCCCCCCC	33.57	27087446
312	Phosphorylation	EDSQDDESDSDAEEE CCCCCCCCCCHHHHH	49.78	25521595
314	Phosphorylation	SQDDESDSDAEEEQT CCCCCCCCHHHHHHH	48.26	25521595
321	Phosphorylation	SDAEEEQTTKRRRPT CHHHHHHHHHHCCCC	37.25	21082442
322	Phosphorylation	DAEEEQTTKRRRPTL HHHHHHHHHHCCCCC	23.42	21082442
328	Phosphorylation	TTKRRRPTLGVQLDD HHHHCCCCCCCCCCH	34.04	25521595
336	Acetylation	LGVQLDDKRKEMLKR CCCCCCHHHHHHHHH	66.10	6569167
338	Acetylation	VQLDDKRKEMLKRHP CCCCHHHHHHHHHCC	53.89	6569773
424	Acetylation	ANQYQFDKVGILTLR CCCCCCCCEEEEEHH	43.58	66699129

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 THOC5_MOUSE !!

Functions of PTM Sites

Modified Location	Modified Residue	Modification	Reference
5	S	Phosphorylation	15221008
Phosphorylation on Ser-5 and/or Ser-6 is required for nuclear export.
6	S	Phosphorylation	15221008
Phosphorylation on Ser-5 and/or Ser-6 is required for nuclear export.
328	T	Phosphorylation	15451025
Phosphorylated on Thr-328 in insulin-stimulated adipocytes.

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_MOUSE !!

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference	Domain-Domain Interactions
Oops, there are no PPI records of THOC5_MOUSE !!

Drug and Disease Associations

Kegg Drug
DrugBank
There are no disease associations of PTM sites.

Regulatory Network of THOC5_MOUSE

Related Literatures of Post-Translational Modification

Phosphorylation
Reference	PubMed
"Solid tumor proteome and phosphoproteome analysis by high resolutionmass spectrometry."; Zanivan S., Gnad F., Wickstroem S.A., Geiger T., Macek B., Cox J.,Faessler R., Mann M.; J. Proteome Res. 7:5314-5326(2008). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-312 AND SER-314, ANDMASS SPECTROMETRY.	19367708 [Abstract]
"Large-scale phosphorylation analysis of mouse liver."; Villen J., Beausoleil S.A., Gerber S.A., Gygi S.P.; Proc. Natl. Acad. Sci. U.S.A. 104:1488-1493(2007). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-307; SER-312 ANDSER-314, AND MASS SPECTROMETRY.	17242355 [Abstract]
"Novel insulin-elicited phosphoproteins in adipocytes."; Gridley S., Lane W.S., Garner C.W., Lienhard G.E.; Cell. Signal. 17:59-66(2005). Cited for: PHOSPHORYLATION AT THR-328, TISSUE SPECIFICITY, AND MASS SPECTROMETRY.	15451025 [Abstract]
"THOC5 couples M-CSF receptor signaling to transcription factorexpression."; Carney L., Pierce A., Rijnen M., Gonzalez Sanchez M.B., Hamzah H.G.,Zhang L., Tamura T., Whetton A.D.; Cell. Signal. 21:309-316(2009). Cited for: FUNCTION, INDUCTION, COMPLEX FORMATION WITH CEBPB, AND PHOSPHORYLATIONAT TYR-225.	19015024 [Abstract]

show

show

show