dbPTM

RHG09_HUMAN - PTM Information in dbPTM

Basic Information of Protein

Overview of Protein Modification Sites with Functional and Structural Information
UniProt ID	RHG09_HUMAN
UniProt AC	Q9BRR9
Protein Name	Rho GTPase-activating protein 9
Gene Name	ARHGAP9
Organism	Homo sapiens (Human).
Sequence Length	750
Subcellular Localization
Protein Description	GTPase activator for the Rho-type GTPases by converting them to an inactive GDP-bound state. Has a substantial GAP activity toward CDC42 and RAC1 and less toward RHOA. Has a role in regulating adhesion of hematopoietic cells to the extracellular matrix. Binds phosphoinositides, and has the highest affinity for phosphatidylinositol 3,4,5-trisphosphate, followed by phosphatidylinositol 3,4-bisphosphate and phosphatidylinositol 4,5-bisphosphate..
Protein Sequence	MLSSRWWPSSWGILGLGPRSPPRGSQLCALYAFTYTGADGQQVSLAEGDRFLLLRKTNSDWWLARRLEAPSTSRPIFVPAAYMIEESIPSQSPTTVIPGQLLWTPGPKLFHGSLEELSQALPSRAQASSEQPPPLPRKMCRSVSTDNLSPSLLKPFQEGPSGRSLSQEDLPSEASASTAGPQPLMSEPPVYCNLVDLRRCPRSPPPGPACPLLQRLDAWEQHLDPNSGRCFYINSLTGCKSWKPPRRSRSETNPGSMEGTQTLKRNNDVLQPQAKGFRSDTGTPEPLDPQGSLSLSQRTSQLDPPALQAPRPLPQLLDDPHEVEKSGLLNMTKIAQGGRKLRKNWGPSWVVLTGNSLVFYREPPPTAPSSGWGPAGSRPESSVDLRGAALAHGRHLSSRRNVLHIRTIPGHEFLLQSDHETELRAWHRALRTVIERLVRWVEARREAPTGRDQGSGDRENPLELRLSGSGPAELSAGEDEEEESELVSKPLLRLSSRRSSIRGPEGTEQNRVRNKLKRLIAKRPPLQSLQERGLLRDQVFGCQLESLCQREGDTVPSFLRLCIAAVDKRGLDVDGIYRVSGNLAVVQKLRFLVDRERAVTSDGRYVFPEQPGQEGRLDLDSTEWDDIHVVTGALKLFLRELPQPLVPPLLLPHFRAALALSESEQCLSQIQELIGSMPKPNHDTLRYLLEHLCRVIAHSDKNRMTPHNLGIVFGPTLFRPEQETSDPAAHALYPGQLVQLMLTNFTSLFP

Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations	Modification	Substrate Peptides & Secondary Structure	ASA (%)	Reference
7 (in isoform 4)	Phosphorylation	-	5.04	27155012
7 (in isoform 3)	Phosphorylation	-	5.04	27155012
20	Phosphorylation	ILGLGPRSPPRGSQL CCCCCCCCCCCHHHH	42.25	17081983
56	Ubiquitination	DRFLLLRKTNSDWWL CEEEEEEECCCCHHH	52.61	-
57	Phosphorylation	RFLLLRKTNSDWWLA EEEEEEECCCCHHHH	33.26	30108239
59	Phosphorylation	LLLRKTNSDWWLARR EEEEECCCCHHHHHH	39.58	30108239
90	Phosphorylation	MIEESIPSQSPTTVI HHHCCCCCCCCCEEE	41.44	22468782
95	Phosphorylation	IPSQSPTTVIPGQLL CCCCCCCEEECCCEE	21.59	22468782
113	Phosphorylation	GPKLFHGSLEELSQA CCCCCCCCHHHHHHH	24.84	22617229
118	Phosphorylation	HGSLEELSQALPSRA CCCHHHHHHHCHHHH	19.38	23403867
123	Phosphorylation	ELSQALPSRAQASSE HHHHHCHHHHHCCCC	40.89	23403867
128	Phosphorylation	LPSRAQASSEQPPPL CHHHHHCCCCCCCCC	23.48	-
142	Phosphorylation	LPRKMCRSVSTDNLS CCHHHHCCCCCCCCC	18.58	30108239
144	Phosphorylation	RKMCRSVSTDNLSPS HHHHCCCCCCCCCHH	31.15	23401153
145	Phosphorylation	KMCRSVSTDNLSPSL HHHCCCCCCCCCHHH	27.10	30108239
149	Phosphorylation	SVSTDNLSPSLLKPF CCCCCCCCHHHCCCC	20.78	30108239
151	Phosphorylation	STDNLSPSLLKPFQE CCCCCCHHHCCCCCC	42.85	24719451
161	Phosphorylation	KPFQEGPSGRSLSQE CCCCCCCCCCCCCHH	58.66	23312004
164	Phosphorylation	QEGPSGRSLSQEDLP CCCCCCCCCCHHHCC	35.58	22210691
166	Phosphorylation	GPSGRSLSQEDLPSE CCCCCCCCHHHCCCH	32.54	22210691
178	Phosphorylation	PSEASASTAGPQPLM CCHHHCCCCCCCCCC	35.04	-
186	Phosphorylation	AGPQPLMSEPPVYCN CCCCCCCCCCCEEEE	55.42	29978859
191	Phosphorylation	LMSEPPVYCNLVDLR CCCCCCEEEEEEECC	4.96	29978859
203	Phosphorylation	DLRRCPRSPPPGPAC ECCCCCCCCCCCCCC	27.22	23401153
232	Phosphorylation	PNSGRCFYINSLTGC CCCCCEEEEECCCCC	11.65	-
248	Phosphorylation	SWKPPRRSRSETNPG CCCCCCCCCCCCCCC	41.24	29978859
250	Phosphorylation	KPPRRSRSETNPGSM CCCCCCCCCCCCCCH	50.44	29209046
252	Phosphorylation	PRRSRSETNPGSMEG CCCCCCCCCCCCHHC	48.21	29209046
256	Phosphorylation	RSETNPGSMEGTQTL CCCCCCCCHHCCHHH	18.21	29209046
260	Phosphorylation	NPGSMEGTQTLKRNN CCCCHHCCHHHHHCC	12.69	29209046
262	Phosphorylation	GSMEGTQTLKRNNDV CCHHCCHHHHHCCCC	33.80	29209046
264	Ubiquitination	MEGTQTLKRNNDVLQ HHCCHHHHHCCCCCC	57.37	-
275	Ubiquitination	DVLQPQAKGFRSDTG CCCCCCCCCCCCCCC	54.02	-
279	Phosphorylation	PQAKGFRSDTGTPEP CCCCCCCCCCCCCCC	36.94	23401153
281	Phosphorylation	AKGFRSDTGTPEPLD CCCCCCCCCCCCCCC	44.17	28450419
283	Phosphorylation	GFRSDTGTPEPLDPQ CCCCCCCCCCCCCCC	26.94	23401153
292	Phosphorylation	EPLDPQGSLSLSQRT CCCCCCCCCCCCCCC	14.99	28450419
294	Phosphorylation	LDPQGSLSLSQRTSQ CCCCCCCCCCCCCCC	27.89	28450419
296	Phosphorylation	PQGSLSLSQRTSQLD CCCCCCCCCCCCCCC	17.78	19690332
325	Ubiquitination	DDPHEVEKSGLLNMT CCHHHHHHCCCCCHH	55.81	-
333	Ubiquitination	SGLLNMTKIAQGGRK CCCCCHHHHCCCCCH	25.85	-
385	Ubiquitination	RPESSVDLRGAALAH CCCCCCCHHHHHHHH	5.22	21890473
386	Dimethylation	PESSVDLRGAALAHG CCCCCCHHHHHHHHC	28.39	-
404 (in isoform 3)	Ubiquitination	-	11.82	21890473
417	Phosphorylation	GHEFLLQSDHETELR CCCEECCCCHHHHHH	40.69	-
448	Phosphorylation	VEARREAPTGRDQGS HHHHHHCCCCCCCCC	30.54	-
456	Phosphorylation	TGRDQGSGDRENPLE CCCCCCCCCCCCCEE	44.83	24719451
465	Phosphorylation	RENPLELRLSGSGPA CCCCEEEEECCCCCC	19.89	-
467	Phosphorylation	NPLELRLSGSGPAEL CCEEEEECCCCCCCC	25.20	28787133
469	Phosphorylation	LELRLSGSGPAELSA EEEEECCCCCCCCCC	37.92	28787133
470	Ubiquitination	ELRLSGSGPAELSAG EEEECCCCCCCCCCC	29.03	-
475	Phosphorylation	GSGPAELSAGEDEEE CCCCCCCCCCCCHHH	26.23	23401153
480	Phosphorylation	ELSAGEDEEEESELV CCCCCCCHHHHHHHH	64.11	24719451
481	Phosphorylation	LSAGEDEEEESELVS CCCCCCHHHHHHHHH	78.40	27251275
484	Phosphorylation	GEDEEEESELVSKPL CCCHHHHHHHHHHHH	39.24	26307563
488	Phosphorylation	EEESELVSKPLLRLS HHHHHHHHHHHHHHH	40.98	28450419
489	Ubiquitination	EESELVSKPLLRLSS HHHHHHHHHHHHHHH	32.00	-
489	Acetylation	EESELVSKPLLRLSS HHHHHHHHHHHHHHH	32.00	25953088
495	Phosphorylation	SKPLLRLSSRRSSIR HHHHHHHHHCCCCCC	18.50	26074081
496	Phosphorylation	KPLLRLSSRRSSIRG HHHHHHHHCCCCCCC	35.98	26074081
499	Phosphorylation	LRLSSRRSSIRGPEG HHHHHCCCCCCCCCC	29.07	23401153
500	Phosphorylation	RLSSRRSSIRGPEGT HHHHCCCCCCCCCCH	17.94	23401153
503	Ubiquitination	SRRSSIRGPEGTEQN HCCCCCCCCCCHHHH	23.96	-
507	Phosphorylation	SIRGPEGTEQNRVRN CCCCCCCHHHHHHHH	32.51	28450419
522	Acetylation	KLKRLIAKRPPLQSL HHHHHHHHCCCCHHH	59.45	25953088
522	Ubiquitination	KLKRLIAKRPPLQSL HHHHHHHHCCCCHHH	59.45	-
549	Ubiquitination	CQLESLCQREGDTVP HHHHHHHHHCCCCHH	52.32	-
568	Ubiquitination	LCIAAVDKRGLDVDG HHHHHHHCCCCCCCC	41.59	-
569	Ubiquitination	CIAAVDKRGLDVDGI HHHHHHCCCCCCCCE	46.58	-
569 (in isoform 2)	Ubiquitination	-	46.58	21890473
569	Ubiquitination	CIAAVDKRGLDVDGI HHHHHHCCCCCCCCE	46.58	21890473
588	Ubiquitination	GNLAVVQKLRFLVDR CCCHHHHHHHHHHCH	29.98	2189047
588 (in isoform 1)	Ubiquitination	-	29.98	21890473
600	Phosphorylation	VDRERAVTSDGRYVF HCHHHEECCCCCEEC	21.81	22210691
601	Phosphorylation	DRERAVTSDGRYVFP CHHHEECCCCCEECC	31.31	22210691
605	Phosphorylation	AVTSDGRYVFPEQPG EECCCCCEECCCCCC	16.39	28796482
706	Phosphorylation	SDKNRMTPHNLGIVF CCCCCCCCCCCEEEE	12.67	24719451
724	Phosphorylation	LFRPEQETSDPAAHA CCCCCCCCCCCHHHH	37.82	24719451
725	Phosphorylation	FRPEQETSDPAAHAL CCCCCCCCCCHHHHH	40.62	24719451
733	Phosphorylation	DPAAHALYPGQLVQL CCHHHHHCHHHHHHH	13.19	26552605
743	Phosphorylation	QLVQLMLTNFTSLFP HHHHHHHHCCHHCCC	17.83	24719451
746	Phosphorylation	QLMLTNFTSLFP--- HHHHHCCHHCCC---	26.96	26552605
747	Phosphorylation	LMLTNFTSLFP---- HHHHCCHHCCC----	24.71	26552605

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 RHG09_HUMAN !!

Functions of PTM Sites

Modified Location	Modified Residue	Modification	Function	Reference
Oops, there are no descriptions of PTM sites of RHG09_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 RHG09_HUMAN !!

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference
A4_HUMAN	APP	physical	21832049
MK01_RAT	Mapk1	physical	17284314
MK01_HUMAN	MAPK1	physical	17284314
MK14_HUMAN	MAPK14	physical	17284314

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 RHG09_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-475, AND MASSSPECTROMETRY.	19690332 [Abstract]
"Phosphorylation analysis of primary human T lymphocytes usingsequential IMAC and titanium oxide enrichment."; Carrascal M., Ovelleiro D., Casas V., Gay M., Abian J.; J. Proteome Res. 7:5167-5176(2008). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-475, AND MASSSPECTROMETRY.	19367720 [Abstract]