dbPTM

RHG17_HUMAN - PTM Information in dbPTM

Basic Information of Protein

Overview of Protein Modification Sites with Functional and Structural Information
UniProt ID	RHG17_HUMAN
UniProt AC	Q68EM7
Protein Name	Rho GTPase-activating protein 17
Gene Name	ARHGAP17
Organism	Homo sapiens (Human).
Sequence Length	881
Subcellular Localization	Membrane Peripheral membrane protein. Cytoplasm. Cell junction, tight junction. Associates with membranes and concentrates at sites of cell-cell contact.
Protein Description	Rho GTPase-activating protein involved in the maintenance of tight junction by regulating the activity of CDC42, thereby playing a central role in apical polarity of epithelial cells. Specifically acts as a GTPase activator for the CDC42 GTPase by converting it to an inactive GDP-bound state. The complex formed with AMOT acts by regulating the uptake of polarity proteins at tight junctions, possibly by deciding whether tight junction transmembrane proteins are recycled back to the plasma membrane or sent elsewhere. Participates in the Ca(2+)-dependent regulation of exocytosis, possibly by catalyzing GTPase activity of Rho family proteins and by inducing the reorganization of the cortical actin filaments. Acts as a GTPase activator in vitro for RAC1..
Protein Sequence	MKKQFNRMKQLANQTVGRAEKTEVLSEDLLQIERRLDTVRSICHHSHKRLVACFQGQHGTDAERRHKKLPLTALAQNMQEASTQLEDSLLGKMLETCGDAENQLALELSQHEVFVEKEIVDPLYGIAEVEIPNIQKQRKQLARLVLDWDSVRARWNQAHKSSGTNFQGLPSKIDTLKEEMDEAGNKVEQCKDQLAADMYNFMAKEGEYGKFFVTLLEAQADYHRKALAVLEKTLPEMRAHQDKWAEKPAFGTPLEEHLKRSGREIALPIEACVMLLLETGMKEEGLFRIGAGASKLKKLKAALDCSTSHLDEFYSDPHAVAGALKSYLRELPEPLMTFNLYEEWTQVASVQDQDKKLQDLWRTCQKLPPQNFVNFRYLIKFLAKLAQTSDVNKMTPSNIAIVLGPNLLWARNEGTLAEMAAATSVHVVAVIEPIIQHADWFFPEEVEFNVSEAFVPLTTPSSNHSFHTGNDSDSGTLERKRPASMAVMEGDLVKKESFGVKLMDFQAHRRGGTLNRKHISPAFQPPLPPTDGSTVVPAGPEPPPQSSRAESSSGGGTVPSSAGILEQGPSPGDGSPPKPKDPVSAAVPAPGRNNSQIASGQNQPQAAAGSHQLSMGQPHNAAGPSPHTLRRAVKKPAPAPPKPGNPPPGHPGGQSSSGTSQHPPSLSPKPPTRSPSPPTQHTGQPPGQPSAPSQLSAPRRYSSSLSPIQAPNHPPPQPPTQATPLMHTKPNSQGPPNPMALPSEHGLEQPSHTPPQTPTPPSTPPLGKQNPSLPAPQTLAGGNPETAQPHAGTLPRPRPVPKPRNRPSVPPPPQPPGVHSAGDSSLTNTAPTASKIVTDSNSRVSEPHRSIFPEMHSDSASKDVPGRILLDIDNDTESTAL

Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations	Modification	Substrate Peptides & Secondary Structure	ASA (%)	Reference
2	Ubiquitination	------MKKQFNRMK ------CHHHHHHHH	56.11	24816145
3	Methylation	-----MKKQFNRMKQ -----CHHHHHHHHH	59.84	-
9	Ubiquitination	KKQFNRMKQLANQTV HHHHHHHHHHHHHHC	38.63	29967540
21	Ubiquitination	QTVGRAEKTEVLSED HHCCCHHHHHHCCHH	49.34	29967540
48	Acetylation	SICHHSHKRLVACFQ HHHHCCCHHHHHHHC	50.90	7407557
72	Phosphorylation	RHKKLPLTALAQNMQ HHHHCCHHHHHHHHH	20.06	-
82	Phosphorylation	AQNMQEASTQLEDSL HHHHHHHHHHHHHHH	18.88	-
83	Phosphorylation	QNMQEASTQLEDSLL HHHHHHHHHHHHHHH	44.19	-
95	Ubiquitination	SLLGKMLETCGDAEN HHHHHHHHHCCCHHH	38.26	27667366
124	Phosphorylation	KEIVDPLYGIAEVEI HHHCCCCHHCEEEEC	16.33	27642862
136	Ubiquitination	VEIPNIQKQRKQLAR EECCCHHHHHHHHHH	48.55	29967540
160	Ubiquitination	ARWNQAHKSSGTNFQ HHHHHHHHHCCCCCC	49.70	29967540
161	Phosphorylation	RWNQAHKSSGTNFQG HHHHHHHHCCCCCCC	24.92	23401153
161 (in isoform 2)	Phosphorylation	-	24.92	-
162	Phosphorylation	WNQAHKSSGTNFQGL HHHHHHHCCCCCCCC	55.21	25159151
164	Phosphorylation	QAHKSSGTNFQGLPS HHHHHCCCCCCCCCH	34.50	30278072
171	Phosphorylation	TNFQGLPSKIDTLKE CCCCCCCHHHHHHHH	47.49	23403867
171	Ubiquitination	TNFQGLPSKIDTLKE CCCCCCCHHHHHHHH	47.49	27667366
172	Ubiquitination	NFQGLPSKIDTLKEE CCCCCCHHHHHHHHH	42.53	27667366
191	Ubiquitination	GNKVEQCKDQLAADM HHHHHHHHHHHHHHH	48.48	29967540
199	Phosphorylation	DQLAADMYNFMAKEG HHHHHHHHHHHHHCC	13.04	23879269
204	Ubiquitination	DMYNFMAKEGEYGKF HHHHHHHHCCCCHHH	55.23	29967540
232	Ubiquitination	KALAVLEKTLPEMRA HHHHHHHHHHHHHHH	51.72	29967540
243	Ubiquitination	EMRAHQDKWAEKPAF HHHHCHHHHHCCCCC	41.56	29967540
247	Ubiquitination	HQDKWAEKPAFGTPL CHHHHHCCCCCCCCH	33.62	29967540
252	Phosphorylation	AEKPAFGTPLEEHLK HCCCCCCCCHHHHHH	20.46	27067055
259	Ubiquitination	TPLEEHLKRSGREIA CCHHHHHHHCCCCCC	46.56	33845483
295	Acetylation	RIGAGASKLKKLKAA ECCCCHHHHHHHHHH	64.89	19608861
295	Ubiquitination	RIGAGASKLKKLKAA ECCCCHHHHHHHHHH	64.89	19608861
295 (in isoform 2)	Acetylation	-	64.89	-
306	Phosphorylation	LKAALDCSTSHLDEF HHHHHCCCCCCHHHH	32.39	28857561
307	Phosphorylation	KAALDCSTSHLDEFY HHHHCCCCCCHHHHC	26.88	28857561
308	Phosphorylation	AALDCSTSHLDEFYS HHHCCCCCCHHHHCC	13.03	28857561
314	Phosphorylation	TSHLDEFYSDPHAVA CCCHHHHCCCHHHHH	15.32	27642862
325	Ubiquitination	HAVAGALKSYLRELP HHHHHHHHHHHHHCC	36.20	29967540
377	Phosphorylation	QNFVNFRYLIKFLAK CCCCCHHHHHHHHHH	14.51	-
384	Ubiquitination	YLIKFLAKLAQTSDV HHHHHHHHHHCCCCC	46.64	29967540
459	Phosphorylation	EAFVPLTTPSSNHSF CCCCCCCCCCCCCCE	28.93	26074081
461	Phosphorylation	FVPLTTPSSNHSFHT CCCCCCCCCCCCEEC	41.50	26074081
462	Phosphorylation	VPLTTPSSNHSFHTG CCCCCCCCCCCEECC	39.50	26074081
465	Phosphorylation	TTPSSNHSFHTGNDS CCCCCCCCEECCCCC	23.99	26074081
468	Phosphorylation	SSNHSFHTGNDSDSG CCCCCEECCCCCCCC	35.35	26074081
472	Phosphorylation	SFHTGNDSDSGTLER CEECCCCCCCCCCCC	37.36	26074081
474	Phosphorylation	HTGNDSDSGTLERKR ECCCCCCCCCCCCCC	37.31	26074081
476	Phosphorylation	GNDSDSGTLERKRPA CCCCCCCCCCCCCCC	29.42	26074081
484	Phosphorylation	LERKRPASMAVMEGD CCCCCCCCEEEEECC	15.23	25159151
484 (in isoform 2)	Phosphorylation	-	15.23	25849741
497	Phosphorylation	GDLVKKESFGVKLMD CCEECCHHHCCEEEE	35.86	28857561
497 (in isoform 2)	Phosphorylation	-	35.86	25159151
501	Acetylation	KKESFGVKLMDFQAH CCHHHCCEEEEHHHH	38.17	25953088
503	Sulfoxidation	ESFGVKLMDFQAHRR HHHCCEEEEHHHHCC	3.93	30846556
506 (in isoform 2)	Phosphorylation	-	31.81	20068231
513	Phosphorylation	QAHRRGGTLNRKHIS HHHCCCCCCCCCCCC	24.55	24706070
520	Phosphorylation	TLNRKHISPAFQPPL CCCCCCCCCCCCCCC	15.19	25159151
547	Phosphorylation	PEPPPQSSRAESSSG CCCCCCCCCCCCCCC	30.20	20068231
547 (in isoform 2)	Phosphorylation	-	30.20	-
551	Phosphorylation	PQSSRAESSSGGGTV CCCCCCCCCCCCCCC	28.90	23927012
552	Phosphorylation	QSSRAESSSGGGTVP CCCCCCCCCCCCCCC	25.22	23927012
553	Phosphorylation	SSRAESSSGGGTVPS CCCCCCCCCCCCCCC	51.22	23927012
557	Phosphorylation	ESSSGGGTVPSSAGI CCCCCCCCCCCCCCH	32.30	23927012
560	Phosphorylation	SGGGTVPSSAGILEQ CCCCCCCCCCCHHCC	28.60	30266825
561	Phosphorylation	GGGTVPSSAGILEQG CCCCCCCCCCHHCCC	25.17	30266825
570	Phosphorylation	GILEQGPSPGDGSPP CHHCCCCCCCCCCCC	48.62	22167270
575	Phosphorylation	GPSPGDGSPPKPKDP CCCCCCCCCCCCCCC	42.65	29255136
584	Phosphorylation	PKPKDPVSAAVPAPG CCCCCCCCCCCCCCC	18.85	22167270
587 (in isoform 2)	Phosphorylation	-	4.09	-
594 (in isoform 2)	Phosphorylation	-	33.65	-
595	Phosphorylation	PAPGRNNSQIASGQN CCCCCCHHHCCCCCC	26.89	20068231
596 (in isoform 2)	Phosphorylation	-	37.07	-
598	Phosphorylation	GRNNSQIASGQNQPQ CCCHHHCCCCCCCCC	10.44	32142685
598 (in isoform 2)	Phosphorylation	-	10.44	-
599	Phosphorylation	RNNSQIASGQNQPQA CCHHHCCCCCCCCCC	42.41	23927012
601	Phosphorylation	NSQIASGQNQPQAAA HHHCCCCCCCCCCCC	42.78	32142685
601 (in isoform 2)	Phosphorylation	-	42.78	-
604 (in isoform 2)	Phosphorylation	-	33.07	-
610	Phosphorylation	QPQAAAGSHQLSMGQ CCCCCCCCCCCCCCC	11.88	23401153
612 (in isoform 2)	Phosphorylation	-	36.61	-
614	Phosphorylation	AAGSHQLSMGQPHNA CCCCCCCCCCCCCCC	17.81	23927012
623	Phosphorylation	GQPHNAAGPSPHTLR CCCCCCCCCCHHHHH	22.32	32142685
624 (in isoform 2)	Phosphorylation	-	39.70	-
625	Phosphorylation	PHNAAGPSPHTLRRA CCCCCCCCHHHHHHH	28.53	23401153
628	Phosphorylation	AAGPSPHTLRRAVKK CCCCCHHHHHHHHCC	25.91	23401153
642 (in isoform 2)	Phosphorylation	-	65.58	-
650 (in isoform 2)	Phosphorylation	-	24.49	-
655	Phosphorylation	PGHPGGQSSSGTSQH CCCCCCCCCCCCCCC	29.73	30108239
656	Phosphorylation	GHPGGQSSSGTSQHP CCCCCCCCCCCCCCC	25.54	30108239
657	Phosphorylation	HPGGQSSSGTSQHPP CCCCCCCCCCCCCCC	51.87	30108239
659	Phosphorylation	GGQSSSGTSQHPPSL CCCCCCCCCCCCCCC	27.45	30108239
660	Phosphorylation	GQSSSGTSQHPPSLS CCCCCCCCCCCCCCC	29.98	30108239
665	Phosphorylation	GTSQHPPSLSPKPPT CCCCCCCCCCCCCCC	46.02	25159151
667	Phosphorylation	SQHPPSLSPKPPTRS CCCCCCCCCCCCCCC	34.90	30108239
672	Phosphorylation	SLSPKPPTRSPSPPT CCCCCCCCCCCCCCC	52.91	30108239
674	Phosphorylation	SPKPPTRSPSPPTQH CCCCCCCCCCCCCCC	32.01	22167270
676	Phosphorylation	KPPTRSPSPPTQHTG CCCCCCCCCCCCCCC	44.77	22167270
679	Phosphorylation	TRSPSPPTQHTGQPP CCCCCCCCCCCCCCC	36.04	22167270
682	Phosphorylation	PSPPTQHTGQPPGQP CCCCCCCCCCCCCCC	27.91	22167270
690	Phosphorylation	GQPPGQPSAPSQLSA CCCCCCCCCCCCCCC	44.94	22167270
693	Phosphorylation	PGQPSAPSQLSAPRR CCCCCCCCCCCCCCC	43.39	22167270
696	Phosphorylation	PSAPSQLSAPRRYSS CCCCCCCCCCCCCCC	28.70	22167270
701	Phosphorylation	QLSAPRRYSSSLSPI CCCCCCCCCCCCCCC	17.74	27251275
702	Phosphorylation	LSAPRRYSSSLSPIQ CCCCCCCCCCCCCCC	16.19	25159151
703	Phosphorylation	SAPRRYSSSLSPIQA CCCCCCCCCCCCCCC	26.77	25159151
704	Phosphorylation	APRRYSSSLSPIQAP CCCCCCCCCCCCCCC	27.25	26657352
706	Phosphorylation	RRYSSSLSPIQAPNH CCCCCCCCCCCCCCC	23.16	26657352
720	Phosphorylation	HPPPQPPTQATPLMH CCCCCCCCCCCCCCC	37.20	23312004
723	Phosphorylation	PQPPTQATPLMHTKP CCCCCCCCCCCCCCC	13.72	25159151
728	Phosphorylation	QATPLMHTKPNSQGP CCCCCCCCCCCCCCC	33.94	23312004
732	Phosphorylation	LMHTKPNSQGPPNPM CCCCCCCCCCCCCCC	45.07	28270605
743	Phosphorylation	PNPMALPSEHGLEQP CCCCCCCCCCCCCCC	42.97	30576142
751	Phosphorylation	EHGLEQPSHTPPQTP CCCCCCCCCCCCCCC	39.42	26657352
753	Phosphorylation	GLEQPSHTPPQTPTP CCCCCCCCCCCCCCC	40.79	26657352
757	Phosphorylation	PSHTPPQTPTPPSTP CCCCCCCCCCCCCCC	34.60	26657352
759	Phosphorylation	HTPPQTPTPPSTPPL CCCCCCCCCCCCCCC	51.74	26657352
762	Phosphorylation	PQTPTPPSTPPLGKQ CCCCCCCCCCCCCCC	55.54	25137130
763	Phosphorylation	QTPTPPSTPPLGKQN CCCCCCCCCCCCCCC	34.40	26657352
778	Phosphorylation	PSLPAPQTLAGGNPE CCCCCCCCCCCCCCC	19.95	28122231
786	Phosphorylation	LAGGNPETAQPHAGT CCCCCCCCCCCCCCC	31.67	25850435
793	Phosphorylation	TAQPHAGTLPRPRPV CCCCCCCCCCCCCCC	34.08	29255136
808	Phosphorylation	PKPRNRPSVPPPPQP CCCCCCCCCCCCCCC	43.98	25159151
820	O-linked_Glycosylation	PQPPGVHSAGDSSLT CCCCCCCCCCCCCCC	31.38	30379171
820	Phosphorylation	PQPPGVHSAGDSSLT CCCCCCCCCCCCCCC	31.38	28555341
824	Phosphorylation	GVHSAGDSSLTNTAP CCCCCCCCCCCCCCC	26.74	27251275
825	Phosphorylation	VHSAGDSSLTNTAPT CCCCCCCCCCCCCCC	43.91	28555341
827	Phosphorylation	SAGDSSLTNTAPTAS CCCCCCCCCCCCCCH	32.25	28555341
829	Phosphorylation	GDSSLTNTAPTASKI CCCCCCCCCCCCHHH	28.86	28555341
840	Phosphorylation	ASKIVTDSNSRVSEP CHHHCCCCCCCCCCC	27.60	25627689
842	Phosphorylation	KIVTDSNSRVSEPHR HHCCCCCCCCCCCCH	37.70	28555341
845	Phosphorylation	TDSNSRVSEPHRSIF CCCCCCCCCCCHHCC	44.28	25627689
850	Phosphorylation	RVSEPHRSIFPEMHS CCCCCCHHCCCCCCC	26.08	21406692
855	Sulfoxidation	HRSIFPEMHSDSASK CHHCCCCCCCCCCCC	3.59	30846556
857	Phosphorylation	SIFPEMHSDSASKDV HCCCCCCCCCCCCCC	31.76	30108239
859	Phosphorylation	FPEMHSDSASKDVPG CCCCCCCCCCCCCCC	37.14	30108239
861	Phosphorylation	EMHSDSASKDVPGRI CCCCCCCCCCCCCCE	33.08	21406692

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
702	S	Phosphorylation	Kinase	PRKACA	P17612	GPS

Functions of PTM Sites

Modified Location	Modified Residue	Modification	Function	Reference
Oops, there are no descriptions of PTM sites of RHG17_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 RHG17_HUMAN !!

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference
SRC_HUMAN	SRC	physical	11431473
CRK_HUMAN	CRK	physical	11431473
GRB2_HUMAN	GRB2	physical	11431473
P85A_HUMAN	PIK3R1	physical	11431473
LCK_HUMAN	LCK	physical	11431473
FNBP1_HUMAN	FNBP1	physical	11431473
CIP4_HUMAN	TRIP10	physical	11431473
PACN1_HUMAN	PACSIN1	physical	11431473
SRC8_HUMAN	CTTN	physical	11431473
SHLB1_HUMAN	SH3GLB1	physical	11431473
BTK_HUMAN	BTK	physical	11431473
ABL1_HUMAN	ABL1	physical	11431473
RAC1_HUMAN	RAC1	physical	11431473
CDC42_HUMAN	CDC42	physical	11431473
INADL_HUMAN	INADL	physical	16678097
AMOT_HUMAN	AMOT	physical	16678097
MPP5_HUMAN	MPP5	physical	16678097
SH3K1_HUMAN	SH3KBP1	physical	16678097
CD2AP_HUMAN	CD2AP	physical	16678097
CAZA1_HUMAN	CAPZA1	physical	16678097
CAPZB_HUMAN	CAPZB	physical	16678097
PARD3_HUMAN	PARD3	physical	16678097
PAR6A_HUMAN	PARD6A	physical	16678097
KPCI_HUMAN	PRKCI	physical	16678097
A4_HUMAN	APP	physical	21832049
ARPC2_HUMAN	ARPC2	physical	26344197
4EBP2_HUMAN	EIF4EBP2	physical	26344197
NLRP3_HUMAN	NLRP3	physical	26344197
OPA1_HUMAN	OPA1	physical	26344197
3BP1_HUMAN	SH3BP1	physical	28514442
KLC1_HUMAN	KLC1	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 RHG17_HUMAN

Related Literatures of Post-Translational Modification

Acetylation
Reference	PubMed
"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-295, AND MASS SPECTROMETRY.	19608861 [Abstract]
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-575, AND MASSSPECTROMETRY.	18669648 [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-679, 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-679, AND MASSSPECTROMETRY.	19413330 [Abstract]