dbPTM

GPKOW_HUMAN - PTM Information in dbPTM

Basic Information of Protein

Overview of Protein Modification Sites with Functional and Structural Information
UniProt ID	GPKOW_HUMAN
UniProt AC	Q92917
Protein Name	G-patch domain and KOW motifs-containing protein
Gene Name	GPKOW
Organism	Homo sapiens (Human).
Sequence Length	476
Subcellular Localization	Nucleus .
Protein Description	RNA-binding protein involved in pre-mRNA splicing..
Protein Sequence	MADSKEGVLPLTAASTAPISFGFTRTSARRRLADSGDGAGPSPEEKDFLKTVEGRELQSVKPQEAPKELVIPLIQNGHRRQPPARPPGPSTDTGALADGVVSQAVKELIAESKKSLEERENAGVDPTLAIPMIQKGCTPSGEGADSEPRAETVPEEANYEAVPVEAYGLAMLRGMGWKPGEGIGRTFNQVVKPRVNSLRPKGLGLGANLTEAQALTPTGPSRMPRPDEEQEKDKEDQPQGLVPGGAVVVLSGPHRGLYGKVEGLDPDNVRAMVRLAVGSRVVTVSEYYLRPVSQQEFDKNTLDLRQQNGTASSRKTLWNQELYIQQDNSERKRKHLPDRQDGPAAKSEKAAPRSQHWLHRDLRVRFVDNMYKGGQYYNTKMIIEDVLSPDTCVCRTDEGRVLEGLREDMLETLVPKAEGDRVMVVLGPQTGRVGHLLSRDRARSRALVQLPRENQVVELHYDAICQYMGPSDTDDD

Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations	Modification	Substrate Peptides & Secondary Structure	ASA (%)	Reference
2	Acetylation	------MADSKEGVL ------CCCCCCCCE	29.77	22814378
4	Phosphorylation	----MADSKEGVLPL ----CCCCCCCCEEC	24.06	25072903
5	Sumoylation	---MADSKEGVLPLT ---CCCCCCCCEECC	60.06	28112733
12	Phosphorylation	KEGVLPLTAASTAPI CCCCEECCCCCCCCC	20.45	29396449
12	O-linked_Glycosylation	KEGVLPLTAASTAPI CCCCEECCCCCCCCC	20.45	30059200
15	Phosphorylation	VLPLTAASTAPISFG CEECCCCCCCCCCCC	23.72	29396449
15	O-linked_Glycosylation	VLPLTAASTAPISFG CEECCCCCCCCCCCC	23.72	30059200
16	Phosphorylation	LPLTAASTAPISFGF EECCCCCCCCCCCCC	31.55	29396449
20	O-linked_Glycosylation	AASTAPISFGFTRTS CCCCCCCCCCCCCHH	20.47	30059200
20	Phosphorylation	AASTAPISFGFTRTS CCCCCCCCCCCCCHH	20.47	25159151
24	Phosphorylation	APISFGFTRTSARRR CCCCCCCCCHHHHHH	33.16	25159151
26	Phosphorylation	ISFGFTRTSARRRLA CCCCCCCHHHHHHHH	24.55	26503892
27	Phosphorylation	SFGFTRTSARRRLAD CCCCCCHHHHHHHHH	19.25	21712546
35	Phosphorylation	ARRRLADSGDGAGPS HHHHHHHCCCCCCCC	32.93	23927012
42	Phosphorylation	SGDGAGPSPEEKDFL CCCCCCCCHHHHHHH	43.98	29255136
46	Ubiquitination	AGPSPEEKDFLKTVE CCCCHHHHHHHHHHC	52.71	24816145
46	Acetylation	AGPSPEEKDFLKTVE CCCCHHHHHHHHHHC	52.71	26051181
50	Ubiquitination	PEEKDFLKTVEGREL HHHHHHHHHHCCCCC	50.98	29967540
51	Phosphorylation	EEKDFLKTVEGRELQ HHHHHHHHHCCCCCC	26.41	25002506
59	Phosphorylation	VEGRELQSVKPQEAP HCCCCCCCCCCCCCC	44.74	22210691
61	Acetylation	GRELQSVKPQEAPKE CCCCCCCCCCCCCHH	46.35	25953088
61	Ubiquitination	GRELQSVKPQEAPKE CCCCCCCCCCCCCHH	46.35	24816145
82	Phosphorylation	QNGHRRQPPARPPGP HCCCCCCCCCCCCCC	23.78	32645325
90	Phosphorylation	PARPPGPSTDTGALA CCCCCCCCCCHHHHC	44.84	18491316
91	Phosphorylation	ARPPGPSTDTGALAD CCCCCCCCCHHHHCH	40.49	18491316
102	Phosphorylation	ALADGVVSQAVKELI HHCHHHHHHHHHHHH	15.26	18491316
106	Ubiquitination	GVVSQAVKELIAESK HHHHHHHHHHHHHHH	50.23	29967540
115	Phosphorylation	LIAESKKSLEERENA HHHHHHHHHHHHHHC	44.76	25159151
127	Phosphorylation	ENAGVDPTLAIPMIQ HHCCCCCCHHHHHHH	25.10	26074081
132	Sulfoxidation	DPTLAIPMIQKGCTP CCCHHHHHHHCCCCC	4.07	21406390
138	Phosphorylation	PMIQKGCTPSGEGAD HHHHCCCCCCCCCCC	29.20	21815630
140	Phosphorylation	IQKGCTPSGEGADSE HHCCCCCCCCCCCCC	31.18	21815630
146	Phosphorylation	PSGEGADSEPRAETV CCCCCCCCCCCCCCC	49.30	21815630
152	Phosphorylation	DSEPRAETVPEEANY CCCCCCCCCCCHHCC	40.14	27642862
159	Phosphorylation	TVPEEANYEAVPVEA CCCCHHCCCCCCHHH	16.59	26552605
167	Phosphorylation	EAVPVEAYGLAMLRG CCCCHHHHHHHHHHC	10.12	27642862
173	Methylation	AYGLAMLRGMGWKPG HHHHHHHHCCCCCCC	21.70	-
178	Acetylation	MLRGMGWKPGEGIGR HHHCCCCCCCCCCCC	37.10	23954790
192	Ubiquitination	RTFNQVVKPRVNSLR CHHHHHCCCCCCCCC	28.40	22817900
192	Acetylation	RTFNQVVKPRVNSLR CHHHHHCCCCCCCCC	28.40	23749302
197	Phosphorylation	VVKPRVNSLRPKGLG HCCCCCCCCCCCCCC	23.93	29396449
201	Acetylation	RVNSLRPKGLGLGAN CCCCCCCCCCCCCCC	61.40	26051181
201	Ubiquitination	RVNSLRPKGLGLGAN CCCCCCCCCCCCCCC	61.40	23000965
207	Ubiquitination	PKGLGLGANLTEAQA CCCCCCCCCCCHHHC	16.95	21890473
210	Phosphorylation	LGLGANLTEAQALTP CCCCCCCCHHHCCCC	29.14	29255136
216	Ubiquitination	LTEAQALTPTGPSRM CCHHHCCCCCCCCCC	23.09	23000965
216	Phosphorylation	LTEAQALTPTGPSRM CCHHHCCCCCCCCCC	23.09	23401153
218	Phosphorylation	EAQALTPTGPSRMPR HHHCCCCCCCCCCCC	57.39	29255136
221	Phosphorylation	ALTPTGPSRMPRPDE CCCCCCCCCCCCCCH	42.42	29255136
251	Phosphorylation	GGAVVVLSGPHRGLY CCEEEEECCCCCCCC	38.37	25159151
258	Phosphorylation	SGPHRGLYGKVEGLD CCCCCCCCCCCCCCC	20.09	-
260	Ubiquitination	PHRGLYGKVEGLDPD CCCCCCCCCCCCCHH	24.45	24816145
275	Ubiquitination	NVRAMVRLAVGSRVV HHHHHHHHHCCCEEE	2.85	24816145
299	Ubiquitination	VSQQEFDKNTLDLRQ CCHHHHCCCCCCHHH	58.09	33845483
315	Ubiquitination	NGTASSRKTLWNQEL CCCCCHHHHHHCEEE	50.33	22817900
316	Phosphorylation	GTASSRKTLWNQELY CCCCHHHHHHCEEEE	35.58	21880142
323	Phosphorylation	TLWNQELYIQQDNSE HHHCEEEEEECCCCH	8.91	29978859
329	Phosphorylation	LYIQQDNSERKRKHL EEEECCCCHHHHHCC	47.25	25159151
330	Ubiquitination	YIQQDNSERKRKHLP EEECCCCHHHHHCCC	69.36	21890473
346	Acetylation	RQDGPAAKSEKAAPR CCCCCCHHCCCCCCC	62.34	23749302
346	Ubiquitination	RQDGPAAKSEKAAPR CCCCCCHHCCCCCCC	62.34	24816145
349	Ubiquitination	GPAAKSEKAAPRSQH CCCHHCCCCCCCCCC	57.87	24816145
361	Ubiquitination	SQHWLHRDLRVRFVD CCCCCCHHHHHHHHH	28.25	24816145
364	Ubiquitination	WLHRDLRVRFVDNMY CCCHHHHHHHHHCCC	7.87	24816145
372	Ubiquitination	RFVDNMYKGGQYYNT HHHHCCCCCCCEECC	45.88	21890473
372	Acetylation	RFVDNMYKGGQYYNT HHHHCCCCCCCEECC	45.88	25953088
387	Ubiquitination	KMIIEDVLSPDTCVC EEEEECCCCCCCEEE	10.73	21890473
388	Phosphorylation	MIIEDVLSPDTCVCR EEEECCCCCCCEEEE	22.15	25159151
391	Phosphorylation	EDVLSPDTCVCRTDE ECCCCCCCEEEECCC	15.38	20068231
412	Phosphorylation	LREDMLETLVPKAEG HHHHHHHHHCCCCCC	29.15	26074081
423	Sulfoxidation	KAEGDRVMVVLGPQT CCCCCEEEEEECCCC	1.47	21406390
461	Phosphorylation	NQVVELHYDAICQYM CCCEEEEHHHHHHHC	21.50	27251275
467	Phosphorylation	HYDAICQYMGPSDTD EHHHHHHHCCCCCCC	10.30	30576142
471	Phosphorylation	ICQYMGPSDTDDD-- HHHHCCCCCCCCC--	47.62	28102081
473	Phosphorylation	QYMGPSDTDDD---- HHCCCCCCCCC----	45.74	28102081

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
27	S	Phosphorylation	Kinase	PRKACA	P17612	GPS
27	S	Phosphorylation	Kinase	PKA	-	Uniprot
316	T	Phosphorylation	Kinase	PRKACA	P17612	GPS
316	T	Phosphorylation	Kinase	PKA	-	Uniprot

Functions of PTM Sites

Modified Location	Modified Residue	Modification	Function	Reference
Oops, there are no descriptions of PTM sites of GPKOW_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 GPKOW_HUMAN !!

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference
A4_HUMAN	APP	physical	21832049
RBM10_HUMAN	RBM10	physical	22365833
PRP8_HUMAN	PRPF8	physical	22365833
PRP4_HUMAN	PRPF4	physical	22365833
BUD13_HUMAN	BUD13	physical	22365833
DHX16_HUMAN	DHX16	physical	22365833
PRP16_HUMAN	DHX38	physical	22365833
WDR83_HUMAN	WDR83	physical	22365833
PP1A_HUMAN	PPP1CA	physical	22365833
MEP50_HUMAN	WDR77	physical	22365833
ROP1A_HUMAN	ROPN1	physical	25416956
BUD13_HUMAN	BUD13	physical	25416956
CCD57_HUMAN	CCDC57	physical	25416956
DHX16_HUMAN	DHX16	physical	25296192
TLN1_HUMAN	TLN1	physical	26344197
SH3G1_HUMAN	SH3GL1	physical	21516116
DHX16_HUMAN	DHX16	physical	28514442
BUD13_HUMAN	BUD13	physical	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 GPKOW_HUMAN

Related Literatures of Post-Translational Modification

Phosphorylation
Reference	PubMed
"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-42 AND THR-216, AND MASSSPECTROMETRY.	18669648 [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-471, AND MASSSPECTROMETRY.	17081983 [Abstract]
"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 THR-216, AND MASSSPECTROMETRY.	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 THR-216, AND MASSSPECTROMETRY.	19413330 [Abstract]
"Combining protein-based IMAC, peptide-based IMAC, and MudPIT forefficient phosphoproteomic analysis."; Cantin G.T., Yi W., Lu B., Park S.K., Xu T., Lee J.-D.,Yates J.R. III; J. Proteome Res. 7:1346-1351(2008). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-216, AND MASSSPECTROMETRY.	18220336 [Abstract]