dbPTM

RHG01_HUMAN - PTM Information in dbPTM

Basic Information of Protein

Overview of Protein Modification Sites with Functional and Structural Information
UniProt ID	RHG01_HUMAN
UniProt AC	Q07960
Protein Name	Rho GTPase-activating protein 1
Gene Name	ARHGAP1
Organism	Homo sapiens (Human).
Sequence Length	439
Subcellular Localization	Cytoplasm.
Protein Description	GTPase activator for the Rho, Rac and Cdc42 proteins, converting them to the putatively inactive GDP-bound state. Cdc42 seems to be the preferred substrate..
Protein Sequence	MDPLSELQDDLTLDDTSEALNQLKLASIDEKNWPSDEMPDFPKSDDSKSSSPELVTHLKWDDPYYDIARHQIVEVAGDDKYGRKIIVFSACRMPPSHQLDHSKLLGYLKHTLDQYVESDYTLLYLHHGLTSDNKPSLSWLRDAYREFDRKYKKNIKALYIVHPTMFIKTLLILFKPLISFKFGQKIFYVNYLSELSEHVKLEQLGIPRQVLKYDDFLKSTQKSPATAPKPMPPRPPLPNQQFGVSLQHLQEKNPEQEPIPIVLRETVAYLQAHALTTEGIFRRSANTQVVREVQQKYNMGLPVDFDQYNELHLPAVILKTFLRELPEPLLTFDLYPHVVGFLNIDESQRVPATLQVLQTLPEENYQVLRFLTAFLVQISAHSDQNKMTNTNLAVVFGPNLLWAKDAAITLKAINPINTFTKFLLDHQGELFPSPDPSGL

Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations	Modification	Substrate Peptides & Secondary Structure	ASA (%)	Reference
1	Acetylation	-------MDPLSELQ -------CCHHHHHC	12.35	22223895
5	Phosphorylation	---MDPLSELQDDLT ---CCHHHHHCCCCC	41.47	20873877
12	Phosphorylation	SELQDDLTLDDTSEA HHHCCCCCCCCHHHH	34.83	28348404
16	Phosphorylation	DDLTLDDTSEALNQL CCCCCCCHHHHHHHH	28.29	22199227
17	Phosphorylation	DLTLDDTSEALNQLK CCCCCCHHHHHHHHH	28.06	22199227
27	Phosphorylation	LNQLKLASIDEKNWP HHHHHHHCCCCCCCC	40.80	29255136
31	Ubiquitination	KLASIDEKNWPSDEM HHHCCCCCCCCCCCC	61.64	29967540
35	Phosphorylation	IDEKNWPSDEMPDFP CCCCCCCCCCCCCCC	37.51	22199227
43	Ubiquitination	DEMPDFPKSDDSKSS CCCCCCCCCCCCCCC	67.52	22817900
44	Phosphorylation	EMPDFPKSDDSKSSS CCCCCCCCCCCCCCC	47.06	23927012
47	Phosphorylation	DFPKSDDSKSSSPEL CCCCCCCCCCCCHHH	39.15	25159151
48	Ubiquitination	FPKSDDSKSSSPELV CCCCCCCCCCCHHHH	62.44	21906983
49	Phosphorylation	PKSDDSKSSSPELVT CCCCCCCCCCHHHHH	39.75	29255136
50	Phosphorylation	KSDDSKSSSPELVTH CCCCCCCCCHHHHHH	54.36	29255136
51	Phosphorylation	SDDSKSSSPELVTHL CCCCCCCCHHHHHHC	29.50	29255136
56	Phosphorylation	SSSPELVTHLKWDDP CCCHHHHHHCCCCCC	33.83	23927012
56	O-linked_Glycosylation	SSSPELVTHLKWDDP CCCHHHHHHCCCCCC	33.83	OGP
59	Ubiquitination	PELVTHLKWDDPYYD HHHHHHCCCCCCCHH	40.76	29967540
64	Phosphorylation	HLKWDDPYYDIARHQ HCCCCCCCHHHHHHH	22.29	28152594
65	Phosphorylation	LKWDDPYYDIARHQI CCCCCCCHHHHHHHE	13.27	28152594
80	Ubiquitination	VEVAGDDKYGRKIIV EEECCCCCCCCEEEE	55.11	22817900
80	Acetylation	VEVAGDDKYGRKIIV EEECCCCCCCCEEEE	55.11	19608861
80	2-Hydroxyisobutyrylation	VEVAGDDKYGRKIIV EEECCCCCCCCEEEE	55.11	-
81	Phosphorylation	EVAGDDKYGRKIIVF EECCCCCCCCEEEEE	29.20	-
84	Ubiquitination	GDDKYGRKIIVFSAC CCCCCCCEEEEEEEC	32.21	22817900
89	Phosphorylation	GRKIIVFSACRMPPS CCEEEEEEECCCCCH	18.63	28857561
93	Sulfoxidation	IVFSACRMPPSHQLD EEEEECCCCCHHHCC	6.02	30846556
144	Phosphorylation	LSWLRDAYREFDRKY HHHHHHHHHHHHHHH	18.24	-
156	Ubiquitination	RKYKKNIKALYIVHP HHHHHHCCEEEECCH	41.55	33845483
159	Phosphorylation	KKNIKALYIVHPTMF HHHCCEEEECCHHHH	13.03	-
168	Ubiquitination	VHPTMFIKTLLILFK CCHHHHHHHHHHHHH	23.12	21890473
169	Phosphorylation	HPTMFIKTLLILFKP CHHHHHHHHHHHHHH	23.21	20068231
174	Ubiquitination	IKTLLILFKPLISFK HHHHHHHHHHHHHHC	6.41	23000965
175	Ubiquitination	KTLLILFKPLISFKF HHHHHHHHHHHHHCC	35.15	33845483
178	Ubiquitination	LILFKPLISFKFGQK HHHHHHHHHHCCCCE	6.54	22817900
179	Phosphorylation	ILFKPLISFKFGQKI HHHHHHHHHCCCCEE	30.02	24719451
212	Ubiquitination	GIPRQVLKYDDFLKS CCCHHHHCHHHHHHH	48.02	23000965
212	Acetylation	GIPRQVLKYDDFLKS CCCHHHHCHHHHHHH	48.02	23236377
218	Methylation	LKYDDFLKSTQKSPA HCHHHHHHHCCCCCC	51.99	-
218	Ubiquitination	LKYDDFLKSTQKSPA HCHHHHHHHCCCCCC	51.99	23000965
219	Phosphorylation	KYDDFLKSTQKSPAT CHHHHHHHCCCCCCC	37.91	26699800
220	Phosphorylation	YDDFLKSTQKSPATA HHHHHHHCCCCCCCC	38.13	26699800
222	Ubiquitination	DFLKSTQKSPATAPK HHHHHCCCCCCCCCC	59.50	33845483
223	Phosphorylation	FLKSTQKSPATAPKP HHHHCCCCCCCCCCC	15.22	26055452
226	Phosphorylation	STQKSPATAPKPMPP HCCCCCCCCCCCCCC	47.04	30576142
245	Phosphorylation	PNQQFGVSLQHLQEK CCCCCCCCHHHHHHH	23.77	22115753
284	Phosphorylation	TEGIFRRSANTQVVR CCCCHHHCCCHHHHH	22.93	28857561
299	Sulfoxidation	EVQQKYNMGLPVDFD HHHHHHCCCCCCCHH	5.46	30846556
365	Phosphorylation	QTLPEENYQVLRFLT HHCCHHHHHHHHHHH	11.86	-
379	Phosphorylation	TAFLVQISAHSDQNK HHHHHHHHHCCCCCC	11.66	22210691
382	Phosphorylation	LVQISAHSDQNKMTN HHHHHHCCCCCCCCC	40.38	22210691
388	Phosphorylation	HSDQNKMTNTNLAVV CCCCCCCCCCCEEEE	40.27	22210691
390	Phosphorylation	DQNKMTNTNLAVVFG CCCCCCCCCEEEEEC	23.57	24505115
409	Phosphorylation	WAKDAAITLKAINPI CHHCHHHHHHHCCCC	19.92	22210691
411	Ubiquitination	KDAAITLKAINPINT HCHHHHHHHCCCCHH	38.27	32015554
420	Phosphorylation	INPINTFTKFLLDHQ CCCCHHHHHHHHHCC	20.88	24505115
433	Phosphorylation	HQGELFPSPDPSGL- CCCCCCCCCCCCCC-	34.30	24076635
437	Phosphorylation	LFPSPDPSGL----- CCCCCCCCCC-----	61.17	27251275

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 RHG01_HUMAN !!

Functions of PTM Sites

Modified Location	Modified Residue	Modification	Function	Reference
Oops, there are no descriptions of PTM sites of RHG01_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 RHG01_HUMAN !!

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference
RHG01_HUMAN	ARHGAP1	physical	10954711
BNIP2_HUMAN	BNIP2	physical	10954711
RHOA_HUMAN	RHOA	physical	9548756
RHOA_HUMAN	RHOA	physical	9407060
CDC42_HUMAN	CDC42	physical	9407060
BNIP2_HUMAN	BNIP2	physical	10551883
RAC1_HUMAN	RAC1	physical	9535855
CDC42_HUMAN	CDC42	physical	9535855
RHOA_HUMAN	RHOA	physical	9535855
RHOA_HUMAN	RHOA	physical	20660160
CHK2_HUMAN	CHEK2	physical	21988832
GFPT1_HUMAN	GFPT1	physical	26344197
RUVB2_HUMAN	RUVBL2	physical	26344197
CDC42_HUMAN	CDC42	physical	14749388
RAC1_HUMAN	RAC1	physical	14749388
RHOA_HUMAN	RHOA	physical	14749388
ATRAP_HUMAN	AGTRAP	physical	21516116

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 RHG01_HUMAN

Related Literatures of Post-Translational Modification

Acetylation
Reference	PubMed
"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: ACETYLATION [LARGE SCALE ANALYSIS] AT MET-1, AND MASS SPECTROMETRY.	19413330 [Abstract]
"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-80 AND LYS-212, AND MASSSPECTROMETRY.	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-51, AND MASSSPECTROMETRY.	18669648 [Abstract]
"Phosphoproteome of resting human platelets."; Zahedi R.P., Lewandrowski U., Wiesner J., Wortelkamp S., Moebius J.,Schuetz C., Walter U., Gambaryan S., Sickmann A.; J. Proteome Res. 7:526-534(2008). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-51, AND MASSSPECTROMETRY.	18088087 [Abstract]
"Global proteomic profiling of phosphopeptides using electron transferdissociation tandem mass spectrometry."; Molina H., Horn D.M., Tang N., Mathivanan S., Pandey A.; Proc. Natl. Acad. Sci. U.S.A. 104:2199-2204(2007). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-51, AND MASSSPECTROMETRY.	17287340 [Abstract]