dbPTM

RHG35_MOUSE - PTM Information in dbPTM

Basic Information of Protein

Overview of Protein Modification Sites with Functional and Structural Information
UniProt ID	RHG35_MOUSE
UniProt AC	Q91YM2
Protein Name	Rho GTPase-activating protein 35 {ECO:0000312\|MGI:MGI:1929494}
Gene Name	Arhgap35 {ECO:0000312\|MGI:MGI:1929494}
Organism	Mus musculus (Mouse).
Sequence Length	1499
Subcellular Localization	Cytoplasm, cytoskeleton, cilium basal body . Cytoplasm . Nucleus . Cell membrane . In response to integrins and SDC4 and upon phosphorylation by PKC, relocalizes from the cytoplasm to regions of plasma membrane ruffling where it colocalizes with poly
Protein Description	Rho GTPase-activating protein (GAP). Binds several acidic phospholipids which inhibits the Rho GAP activity to promote the Rac GAP activity. [PubMed: 16971514 This binding is inhibited by phosphorylation by PRKCA (By similarity Involved in cell differentiation as well as cell adhesion and migration, plays an important role in retinal tissue morphogenesis, neural tube fusion, midline fusion of the cerebral hemispheres and mammary gland branching morphogenesis]
Protein Sequence	MMMARKQDVRIPTYNISVVGLSGTEKEKGQCGIGKSCLCNRFVRPSADEFHLDHTSVLSTSDFGGRVVNNDHFLYWGEVSRSLEDCVECKMHIVEQTEFIDDQTFQPHRSTALQPYIKRAAATKLASAEKLMYFCTDQLGLEQDFEQKQMPDGKLLVDGFLLGIDVSRGMNRNFDDQLKFVSNLYNQLAKTKKPIVVVLTKCDEGVERYIRDAHTFALSKKNLQVVETSARSNVNVDLAFSTLVQLIDKSRGKTKIIPYFEALKQQSQQIATAKDKYEWLVSRIVKNHNENWPSVSRKMQASPEYQDYVYLEGTQKAKKLFLQHIHRLKHEHIERRRKLYLAALPLAFEALIPNLDEVDHLSCIKAKKLLETKPEFLKWFVVLEETPWDATSHIDNMENERIPFDLMDTVPAEQLYETHLEKLRNERKRAEMRRAFKENLETSPFITPGKPWEEARSFIMNEDFYQWLEESVYMDIYGKHQKQIIDRAKEEFQELLLEYSELFYELELDAKPSKEKMGVIQDVLGEEQRFKALQKLQAERDALILKHIHFVYHPTKETCPSCPACVDAKIEHLISSRFIRPSDRNQKNSLSDLNIDRINLVILGKDGLARELANEIRALCTNDDKYVIDGKMYELSLRPIEGNVRLPVNSFQTPTFQPHGCLCLYNSKESLSYVVESIEKSRESTLGRRDNHLVHLPLTLILVNKRGDTSGETLHSLIQQGQQIASKLQCVFLDPASAGIGYGRNINEKQISQVLKGLLDSKRNLNLVSSTASIKDLADVDLRIVMCLMCGDPFSADDVLSPVLQSQTCKSSHCGSSNSVLLELPIGLHKKRIELSVLSYHSSFSIRKSRLVHGYIVFYSAKRKASLAMLRAFLCEVQDIIPIQLVALTDGAIDVLDNDLSREQLTEGEEIAQEIDGRFTSIPCSQPQHKLELFHPFFKDVVEKKNIIEATHMYDNVAEACSTTEEVFNSPRAGSPLCNSNLQDSEEDVEPPSYHLFREDATLPSLSKDHSKFSMELEGNDGLSFIMSNFESKLNNKVPPPVKPKPPVHFDITKDLSYLDQGHREGQRKSMSSSPWMPQDGFDPSDYAEPMDAVVKPRNEEENIYSVPHDSTQGKIITIRNINKAQSNGSGNGSDSEMDTSSLERGRKVSAVSKPVLYRTRCTRLGRFASYRTSFSVGSDDELGPIRKKEEDQASQGYKGDNAVIPYETDEDPRRRNILRSLRRNTKKPKPKPRPSITKATWESNYFGVPLTTVVTPEKPIPIFIERCIEYIEATGLSTEGIYRVSGNKSEMESLQRQFDQDHNLDLAEKDFTVNTVAGAMKSFFSELPDPLVPYSMQIDLVEAHKINDREQKLHALKEVLKKFPKENHEVFKYVISHLNKVSHNNKVNLMTSENLSICFWPTLMRPDFSSMDALTATRSYQTIIELFIQQCPFFFYNRPISEPPGAAPGSPSAMAPTVPFLTSTPATSQPSPPQSPPPTPQSPMQPLLSSQLQAEHTL

Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations	Modification	Substrate Peptides & Secondary Structure	ASA (%)	Reference
124	Malonylation	IKRAAATKLASAEKL HHHHHHHHHCCHHHH	37.01	26320211
296	Phosphorylation	NENWPSVSRKMQASP CCCCCCCCHHHCCCH	30.44	22817900
308	Phosphorylation	ASPEYQDYVYLEGTQ CCHHHCCCEEEECHH	3.88	22817900
368	Ubiquitination	LSCIKAKKLLETKPE HHHHHHHHHHHCCHH	64.26	-
442	Phosphorylation	AFKENLETSPFITPG HHHHHHCCCCCCCCC	44.88	28418008
443	Phosphorylation	FKENLETSPFITPGK HHHHHCCCCCCCCCC	14.40	28418008
477	Nitration	ESVYMDIYGKHQKQI HHHCHHHHCHHHHHH	18.83	-
589	Phosphorylation	SDRNQKNSLSDLNID CCCCCCCCHHHCCCC	35.96	25521595
591	Phosphorylation	RNQKNSLSDLNIDRI CCCCCCHHHCCCCCE	39.61	22324799
625	Acetylation	ALCTNDDKYVIDGKM HHHCCCCCEEECCEE	44.26	22826441
636	Phosphorylation	DGKMYELSLRPIEGN CCEEEEEEECCCCCC	15.47	25159016
685	Phosphorylation	IEKSRESTLGRRDNH HHHHHHHHCCCCCCC	28.60	23140645
769	Phosphorylation	KRNLNLVSSTASIKD CCCCCCCCCCCCHHH	25.74	27742792
770	Phosphorylation	RNLNLVSSTASIKDL CCCCCCCCCCCHHHH	22.10	25521595
771	Phosphorylation	NLNLVSSTASIKDLA CCCCCCCCCCHHHHH	19.54	25521595
773	Phosphorylation	NLVSSTASIKDLADV CCCCCCCCHHHHHCC	30.20	25521595
843	Phosphorylation	SVLSYHSSFSIRKSR EEEEECCCCCCCHHH	15.08	30387612
951	Phosphorylation	KKNIIEATHMYDNVA HCCHHHHHCCCHHHH	8.39	25777480
954	Phosphorylation	IIEATHMYDNVAEAC HHHHHCCCHHHHHHH	9.21	25777480
962	Phosphorylation	DNVAEACSTTEEVFN HHHHHHHCCCHHHHC	45.47	25777480
963	Phosphorylation	NVAEACSTTEEVFNS HHHHHHCCCHHHHCC	37.80	25777480
964	Phosphorylation	VAEACSTTEEVFNSP HHHHHCCCHHHHCCC	17.54	25777480
970	Phosphorylation	TTEEVFNSPRAGSPL CCHHHHCCCCCCCCC	12.33	27087446
975	Phosphorylation	FNSPRAGSPLCNSNL HCCCCCCCCCCCCCC	17.45	25521595
980	Phosphorylation	AGSPLCNSNLQDSEE CCCCCCCCCCCCCHH	37.61	24925903
985	Phosphorylation	CNSNLQDSEEDVEPP CCCCCCCCHHCCCCC	29.89	24925903
993	Phosphorylation	EEDVEPPSYHLFRED HHCCCCCCHHHCCCC	35.58	25619855
994	Phosphorylation	EDVEPPSYHLFREDA HCCCCCCHHHCCCCC	14.33	25619855
1002	Phosphorylation	HLFREDATLPSLSKD HHCCCCCCCCCCCCC	52.07	23984901
1005	Phosphorylation	REDATLPSLSKDHSK CCCCCCCCCCCCCCC	48.68	23984901
1007	Phosphorylation	DATLPSLSKDHSKFS CCCCCCCCCCCCCCE	40.13	23984901
1011	Phosphorylation	PSLSKDHSKFSMELE CCCCCCCCCCEEEEC	45.59	29899451
1014	Phosphorylation	SKDHSKFSMELEGND CCCCCCCEEEECCCC	18.32	29899451
1057	Phosphorylation	FDITKDLSYLDQGHR EECCCCHHHHHHCCC	33.51	22817900
1070	Phosphorylation	HREGQRKSMSSSPWM CCCCCCCCCCCCCCC	26.53	22499769
1071	Oxidation	REGQRKSMSSSPWMP CCCCCCCCCCCCCCC	5.16	17242355
1072	Phosphorylation	EGQRKSMSSSPWMPQ CCCCCCCCCCCCCCC	34.45	22499769
1073	Phosphorylation	GQRKSMSSSPWMPQD CCCCCCCCCCCCCCC	31.60	22499769
1074	Phosphorylation	QRKSMSSSPWMPQDG CCCCCCCCCCCCCCC	18.44	25367039
1077	Oxidation	SMSSSPWMPQDGFDP CCCCCCCCCCCCCCH	2.13	17242355
1085	Phosphorylation	PQDGFDPSDYAEPMD CCCCCCHHHCCCCCC	45.13	25338131
1087	Phosphorylation	DGFDPSDYAEPMDAV CCCCHHHCCCCCCEE	19.73	25177544
1105	Phosphorylation	RNEEENIYSVPHDST CCCCCCCEECCCCCC	18.39	26824392
1106	Phosphorylation	NEEENIYSVPHDSTQ CCCCCCEECCCCCCC	25.94	27742792
1111	Phosphorylation	IYSVPHDSTQGKIIT CEECCCCCCCCEEEE	21.42	25619855
1112	Phosphorylation	YSVPHDSTQGKIITI EECCCCCCCCEEEEE	47.61	25619855
1127	Phosphorylation	RNINKAQSNGSGNGS EECCHHHCCCCCCCC	48.28	23984901
1130	Phosphorylation	NKAQSNGSGNGSDSE CHHHCCCCCCCCCCC	33.08	24759943
1134	Phosphorylation	SNGSGNGSDSEMDTS CCCCCCCCCCCCCHH	41.80	25521595
1136	Phosphorylation	GSGNGSDSEMDTSSL CCCCCCCCCCCHHHH	36.20	23527152
1140	Phosphorylation	GSDSEMDTSSLERGR CCCCCCCHHHHHHCC	20.93	23140645
1141	Phosphorylation	SDSEMDTSSLERGRK CCCCCCHHHHHHCCC	28.76	23140645
1142	Phosphorylation	DSEMDTSSLERGRKV CCCCCHHHHHHCCCE	36.02	23527152
1150	Phosphorylation	LERGRKVSAVSKPVL HHHCCCEECCCCCEE	26.45	26824392
1153	Phosphorylation	GRKVSAVSKPVLYRT CCCEECCCCCEECCC	30.84	26239621
1158	Phosphorylation	AVSKPVLYRTRCTRL CCCCCEECCCCCCHH	15.35	29899451
1170	Phosphorylation	TRLGRFASYRTSFSV CHHHCCEECEEEECC	16.67	29899451
1173	Phosphorylation	GRFASYRTSFSVGSD HCCEECEEEECCCCC	26.37	24925903
1174	Phosphorylation	RFASYRTSFSVGSDD CCEECEEEECCCCCC	13.41	24925903
1176	Phosphorylation	ASYRTSFSVGSDDEL EECEEEECCCCCCCC	25.90	25521595
1179	Phosphorylation	RTSFSVGSDDELGPI EEEECCCCCCCCCCC	39.47	24925903
1221	Phosphorylation	RRRNILRSLRRNTKK HHHHHHHHHHHCCCC	23.84	-
1226	Phosphorylation	LRSLRRNTKKPKPKP HHHHHHCCCCCCCCC	38.34	-
1236	Phosphorylation	PKPKPRPSITKATWE CCCCCCCCCCHHHEE	44.14	26824392
1238	Phosphorylation	PKPRPSITKATWESN CCCCCCCCHHHEECC	20.97	29472430
1290	Phosphorylation	YRVSGNKSEMESLQR EEECCCHHHHHHHHH	46.29	20495213
1313	Phosphorylation	DLAEKDFTVNTVAGA CHHHCCCCHHHHHHH	23.99	25521595
1472	Phosphorylation	TPATSQPSPPQSPPP CCCCCCCCCCCCCCC	41.39	18502760
1476	Phosphorylation	SQPSPPQSPPPTPQS CCCCCCCCCCCCCCC	45.18	18502760
1480	Phosphorylation	PPQSPPPTPQSPMQP CCCCCCCCCCCCCHH	39.47	18502760
1483	Phosphorylation	SPPPTPQSPMQPLLS CCCCCCCCCCHHHHH	24.44	26859289

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
1105	Y	Phosphorylation	Kinase	ABL2	Q4JIM5	Uniprot
1105	Y	Phosphorylation	Kinase	EGFR	P00533	PSP
1105	Y	Phosphorylation	Kinase	PTK6	Q64434	Uniprot
1105	Y	Phosphorylation	Kinase	SRC	P00523	PSP
1105	Y	Phosphorylation	Kinase	SRC	P12931	PSP

Functions of PTM Sites

Modified Location	Modified Residue	Modification	Reference
1221	S	Phosphorylation	11044403
Phosphorylated by PRKCA at Ser-1221 and Thr-1226, induces relocalization from the cytoplasm to regions of plasma membrane ruffling and prevents the binding and substrate specificity regulation by phospholipids.
1226	T	Phosphorylation	11044403
Phosphorylated by PRKCA at Ser-1221 and Thr-1226, induces relocalization from the cytoplasm to regions of plasma membrane ruffling and prevents the binding and substrate specificity regulation by phospholipids.
1451	S	Phosphorylation	11283609
During focal adhesion formation, phosphorylated by MAPK1 and MAPK3 at the C-terminal region, probably at Ser-1451, Ser-1476, Thr-1480 and Ser-1483.
1476	S	Phosphorylation	18502760
During focal adhesion formation, phosphorylated by MAPK1 and MAPK3 at the C-terminal region, probably at Ser-1451, Ser-1476, Thr-1480 and Ser-1483.
1476	S	Phosphorylation	18502760
Phosphorylation at Ser-1476 and Thr-1480 by GSK3B requires priming by MAPK and inhibits RhoGAP activity and modulates polarized cell migration.
1480	T	Phosphorylation	18502760
During focal adhesion formation, phosphorylated by MAPK1 and MAPK3 at the C-terminal region, probably at Ser-1451, Ser-1476, Thr-1480 and Ser-1483.
1480	T	Phosphorylation	18502760
Phosphorylation at Ser-1476 and Thr-1480 by GSK3B requires priming by MAPK and inhibits RhoGAP activity and modulates polarized cell migration.
1483	S	Phosphorylation	18502760
During focal adhesion formation, phosphorylated by MAPK1 and MAPK3 at the C-terminal region, probably at Ser-1451, Ser-1476, Thr-1480 and Ser-1483.

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 RHG35_MOUSE !!

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference	Domain-Domain Interactions
FZR1_MOUSE	Fzr1	physical	20530197

Drug and Disease Associations

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

Regulatory Network of RHG35_MOUSE

Related Literatures of Post-Translational Modification

Phosphorylation
Reference	PubMed
"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-773 AND SER-980, ANDMASS SPECTROMETRY.	17242355 [Abstract]
"Integrin signaling through Arg activates p190RhoGAP by promoting itsbinding to p120RasGAP and recruitment to the membrane."; Bradley W.D., Hernandez S.E., Settleman J., Koleske A.J.; Mol. Biol. Cell 17:4827-4836(2006). Cited for: PHOSPHORYLATION AT TYR-1105, INTERACTION WITH RASA1, AND FUNCTION.	16971514 [Abstract]
"Large-scale identification and evolution indexing of tyrosinephosphorylation sites from murine brain."; Ballif B.A., Carey G.R., Sunyaev S.R., Gygi S.P.; J. Proteome Res. 7:311-318(2008). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-1087 AND TYR-1105, ANDMASS SPECTROMETRY.	18034455 [Abstract]
"Quantitative time-resolved phosphoproteomic analysis of mast cellsignaling."; Cao L., Yu K., Banh C., Nguyen V., Ritz A., Raphael B.J., Kawakami Y.,Kawakami T., Salomon A.R.; J. Immunol. 179:5864-5876(2007). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-1105, AND MASSSPECTROMETRY.	17947660 [Abstract]
"Comprehensive identification of phosphorylation sites in postsynapticdensity preparations."; Trinidad J.C., Specht C.G., Thalhammer A., Schoepfer R.,Burlingame A.L.; Mol. Cell. Proteomics 5:914-922(2006). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-1105, AND MASSSPECTROMETRY.	16452087 [Abstract]

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