dbPTM

ARHG7_MOUSE - PTM Information in dbPTM

Basic Information of Protein

Overview of Protein Modification Sites with Functional and Structural Information
UniProt ID	ARHG7_MOUSE
UniProt AC	Q9ES28
Protein Name	Rho guanine nucleotide exchange factor 7
Gene Name	Arhgef7
Organism	Mus musculus (Mouse).
Sequence Length	862
Subcellular Localization	Cell junction, focal adhesion. Cell projection, ruffle. Cytoplasm, cell cortex. Cell projection, lamellipodium. Detected at cell adhesions. A small proportion is detected at focal adhesions.
Protein Description	Acts as a RAC1 guanine nucleotide exchange factor (GEF) and can induce membrane ruffling. May function as a positive regulator of apoptosis. Functions in cell migration, attachment and cell spreading. Promotes targeting of RAC1 to focal adhesions. Downstream of NMDA receptors and CaMKK-CaMK1 signaling cascade, promotes the formation of spines and synapses in hippocampal neurons (By similarity)..
Protein Sequence	MNSAEQTVTWLITLGVLESPKKTISDPEVFLQASLKDGVVLCRLLERLLPGTIEKVYPEPRNESECLSNIREFLRACGASLRLETFDANDLYQGQNFNKVLSSLVTLNKVTADIGLGSDSVCARPSSHRIKSFDSLGSQSSHSRTSKLLQSQYRSLDMTDNTNSQLVVRAKFNFQQTNEDELSFSKGDVIHVTRVEEGGWWEGTHNGRTGWFPSNYVREIKPSEKPVSPKSGTLKSPPKGFDTTAINKSYYNVVLQNILETEHEYSKELQSVLSTYLRPLQTSDKLSSANTSYLMGNLEEISSFQQVLVQSLEECTKSPEAQQRVGGCFLSLMPQMRTLYLAYCANHPSAVSVLTEHSEDLGEFMETKGASSPGILVLTTGLSKPFMRLDKYPTLLKELERHMEDYHPDRQDIQKSMTAFKNLSAQCQEVRKRKELELQILTEPIRSWEGDDIKTLGSVTYMSQVTIQCAGSEEKNERYLLLFPNLLLMLSASPRMSGFIYQGKLPTTGMTITKLEDSENHRNAFEISGSMIERILVSCTSQQDLHEWVEHLQKQTKVTSVSNPTIKPHSVPSHTLPSHPLTPSSKHADSKPVALTPAYHTLPHPSHHGTPHTTISWGPLEPPKTPKPWSLSCLRPAPPLRPSAALCYKEDLSKSPKTMKKLLPKRKPERKPSDEEFAVRKSTAALEEDAQILKVIEAYCTSAKTRQTLNSTWQGTDLMHNHVLADDDQSSLDSLGRRSSLSRLEPSDLSEDSEYDSIWTAHSYRMGSASRSRKESAPQVLLPEEEKIIVEETKSNGQTVIEEKSLVDTVYALKDEVQELRQDNKKMKKSLEEEQRARKDLEKLVRKVLKNMNDPAWDETNL

Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations	Modification	Substrate Peptides & Secondary Structure	ASA (%)	Reference
2 (in isoform 8)	Phosphorylation	-	50.34	29514104
5 (in isoform 8)	Phosphorylation	-	46.75	27566939
7 (in isoform 8)	Phosphorylation	-	16.06	26824392
23	Phosphorylation	VLESPKKTISDPEVF CCCCCCCCCCCHHHH	31.66	19060867
25	Phosphorylation	ESPKKTISDPEVFLQ CCCCCCCCCHHHHHH	52.96	19060867
55	Ubiquitination	LLPGTIEKVYPEPRN HCCCCCCHHCCCCCC	43.12	22790023
92	Phosphorylation	TFDANDLYQGQNFNK ECCHHHHHCCCCHHH	17.29	-
102	Phosphorylation	QNFNKVLSSLVTLNK CCHHHHHHHHHHHCC	25.31	25521595
103	Phosphorylation	NFNKVLSSLVTLNKV CHHHHHHHHHHHCCE	23.77	23984901
126	Phosphorylation	DSVCARPSSHRIKSF CCCCCCCCCCCCCCC	32.97	21183079
127	Phosphorylation	SVCARPSSHRIKSFD CCCCCCCCCCCCCCC	21.33	19060867
132	Phosphorylation	PSSHRIKSFDSLGSQ CCCCCCCCCCCCCCC	31.73	26824392
135	Phosphorylation	HRIKSFDSLGSQSSH CCCCCCCCCCCCCCC	32.40	22324799
138	Phosphorylation	KSFDSLGSQSSHSRT CCCCCCCCCCCCHHH	31.98	22324799
140	Phosphorylation	FDSLGSQSSHSRTSK CCCCCCCCCCHHHHH	31.54	22324799
141	Phosphorylation	DSLGSQSSHSRTSKL CCCCCCCCCHHHHHH	20.18	22324799
143	Phosphorylation	LGSQSSHSRTSKLLQ CCCCCCCHHHHHHHH	38.92	22324799
145	Phosphorylation	SQSSHSRTSKLLQSQ CCCCCHHHHHHHHHH	32.98	22324799
146	Phosphorylation	QSSHSRTSKLLQSQY CCCCHHHHHHHHHHH	21.86	22324799
151	Phosphorylation	RTSKLLQSQYRSLDM HHHHHHHHHHHHCCC	29.20	23984901
153	Phosphorylation	SKLLQSQYRSLDMTD HHHHHHHHHHCCCCC	13.86	23984901
155	Phosphorylation	LLQSQYRSLDMTDNT HHHHHHHHCCCCCCC	24.64	25521595
159	Phosphorylation	QYRSLDMTDNTNSQL HHHHCCCCCCCCCCE	26.26	26745281
162	Phosphorylation	SLDMTDNTNSQLVVR HCCCCCCCCCCEEEE	38.77	25266776
164	Phosphorylation	DMTDNTNSQLVVRAK CCCCCCCCCEEEEEE	23.89	25521595
223	Phosphorylation	YVREIKPSEKPVSPK HEEECCCCCCCCCCC	53.93	18388127
228	Phosphorylation	KPSEKPVSPKSGTLK CCCCCCCCCCCCCCC	34.83	18388127
231	Phosphorylation	EKPVSPKSGTLKSPP CCCCCCCCCCCCCCC	40.15	25619855
233	Phosphorylation	PVSPKSGTLKSPPKG CCCCCCCCCCCCCCC	37.80	25619855
236	Phosphorylation	PKSGTLKSPPKGFDT CCCCCCCCCCCCCCC	49.93	22942356
243	Phosphorylation	SPPKGFDTTAINKSY CCCCCCCCCCCCHHH	18.83	25619855
244	Phosphorylation	PPKGFDTTAINKSYY CCCCCCCCCCCHHHH	27.64	25619855
249	Phosphorylation	DTTAINKSYYNVVLQ CCCCCCHHHHHHHHH	28.50	29899451
274	Phosphorylation	KELQSVLSTYLRPLQ HHHHHHHHHHHCCCC	16.92	29514104
276	Phosphorylation	LQSVLSTYLRPLQTS HHHHHHHHHCCCCCC	9.42	21183079
328	S-nitrosylation	AQQRVGGCFLSLMPQ HHHHHHHHHHHHCHH	2.26	20925432
328	S-nitrosocysteine	AQQRVGGCFLSLMPQ HHHHHHHHHHHHCHH	2.26	-
371	Phosphorylation	FMETKGASSPGILVL HHHHCCCCCCCEEEE	45.81	25159016
372	Phosphorylation	METKGASSPGILVLT HHHCCCCCCCEEEEE	26.98	25159016
379	Phosphorylation	SPGILVLTTGLSKPF CCCEEEEECCCCCCC	16.02	25159016
380	Phosphorylation	PGILVLTTGLSKPFM CCEEEEECCCCCCCC	31.78	25159016
383	Phosphorylation	LVLTTGLSKPFMRLD EEEECCCCCCCCHHH	39.36	25159016
384	Ubiquitination	VLTTGLSKPFMRLDK EEECCCCCCCCHHHH	47.52	22790023
434	Acetylation	CQEVRKRKELELQIL HHHHHHHHHHHHHHH	70.46	7614629
493	Phosphorylation	LLLMLSASPRMSGFI HHHHHCCCCCCCCEE	15.06	26643407
496	Oxidation	MLSASPRMSGFIYQG HHCCCCCCCCEEECC	5.36	17242355
497	Phosphorylation	LSASPRMSGFIYQGK HCCCCCCCCEEECCC	31.65	18388127
501	Phosphorylation	PRMSGFIYQGKLPTT CCCCCEEECCCCCCC	14.67	25619855
570	Phosphorylation	NPTIKPHSVPSHTLP CCCCCCCCCCCCCCC	44.22	26060331
573 (in isoform 3)	Phosphorylation	-	27.27	25777480
573	Phosphorylation	IKPHSVPSHTLPSHP CCCCCCCCCCCCCCC	27.27	26060331
575 (in isoform 3)	Phosphorylation	-	44.71	25777480
575	Phosphorylation	PHSVPSHTLPSHPLT CCCCCCCCCCCCCCC	44.71	26060331
578 (in isoform 3)	Phosphorylation	-	40.63	25777480
578	Phosphorylation	VPSHTLPSHPLTPSS CCCCCCCCCCCCCCC	40.63	26643407
580 (in isoform 3)	Phosphorylation	-	42.12	25266776
582	Phosphorylation	TLPSHPLTPSSKHAD CCCCCCCCCCCCCCC	26.10	26643407
584	Phosphorylation	PSHPLTPSSKHADSK CCCCCCCCCCCCCCC	46.94	26643407
585	Phosphorylation	SHPLTPSSKHADSKP CCCCCCCCCCCCCCC	29.66	26643407
601	Phosphorylation	ALTPAYHTLPHPSHH EEECCCCCCCCCCCC	29.34	22807455
613	Phosphorylation	SHHGTPHTTISWGPL CCCCCCCCEEECCCC	27.33	21183079
653	Phosphorylation	LCYKEDLSKSPKTMK EECCHHHCCCHHHHH	43.33	26745281
655	Phosphorylation	YKEDLSKSPKTMKKL CCHHHCCCHHHHHHH	28.40	24453211
659 (in isoform 4)	Phosphorylation	-	4.50	25338131
660 (in isoform 4)	Phosphorylation	-	45.56	29514104
665 (in isoform 4)	Phosphorylation	-	73.37	25195567
673	Phosphorylation	RKPERKPSDEEFAVR CCCCCCCCHHHHHHH	61.77	18388127
682	Phosphorylation	EEFAVRKSTAALEED HHHHHHHHHHHHHHH	16.83	25521595
683	Phosphorylation	EFAVRKSTAALEEDA HHHHHHHHHHHHHHH	20.98	25521595
699	Phosphorylation	ILKVIEAYCTSAKTR HHHHHHHHHCCCCHH	5.40	25367039
700	Glutathionylation	LKVIEAYCTSAKTRQ HHHHHHHHCCCCHHH	2.90	24333276
711 (in isoform 2)	Phosphorylation	-	33.85	25338131
712 (in isoform 2)	Phosphorylation	-	22.27	29514104
717 (in isoform 2)	Phosphorylation	-	49.14	25195567
739	Phosphorylation	LDSLGRRSSLSRLEP HHHHCCHHHHHCCCC	33.98	29899451
740	Phosphorylation	DSLGRRSSLSRLEPS HHHCCHHHHHCCCCC	28.66	23140645
742	Phosphorylation	LGRRSSLSRLEPSDL HCCHHHHHCCCCCCC	36.45	22324799
747	Phosphorylation	SLSRLEPSDLSEDSE HHHCCCCCCCCCCCC	41.63	29899451
750	Phosphorylation	RLEPSDLSEDSEYDS CCCCCCCCCCCCCCC	44.33	19060867
773 (in isoform 5)	Phosphorylation	-	45.72	29899451
776	Phosphorylation	ASRSRKESAPQVLLP CCCCCCCCCCCCCCC	48.56	25521595
793	Phosphorylation	EKIIVEETKSNGQTV HCEEEEECHHCCCEE	26.68	26745281
794	Ubiquitination	KIIVEETKSNGQTVI CEEEEECHHCCCEEE	45.24	22790023
795	Phosphorylation	IIVEETKSNGQTVIE EEEEECHHCCCEEEE	54.32	25521595
799	Phosphorylation	ETKSNGQTVIEEKSL ECHHCCCEEEEEHHH	25.50	23984901
811	Phosphorylation	KSLVDTVYALKDEVQ HHHHHHHHHHHHHHH	14.33	-
814	Ubiquitination	VDTVYALKDEVQELR HHHHHHHHHHHHHHH	43.61	-
830	Phosphorylation	DNKKMKKSLEEEQRA HHHHHHHHHHHHHHH	35.18	28066266

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
755	Y	Phosphorylation	Kinase	SRC	P05480	PSP

Functions of PTM Sites

Modified Location	Modified Residue	Modification	Function	Reference
673	S	Phosphorylation		19144319
Phosphorylated on Ser-673 by CaMK1; enhancement of GEF activity and downstream activation of RAC1 (By similarity).

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 ARHG7_MOUSE !!

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference
1433B_MOUSE	Ywhab	physical	20338996
EGFR_MOUSE	Egfr	physical	16892055
1433Z_MOUSE	Ywhaz	physical	16959763
GIT1_MOUSE	Git1	physical	16959763

Drug and Disease Associations

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

Regulatory Network of ARHG7_MOUSE

Related Literatures of Post-Translational Modification

Phosphorylation
Reference	PubMed
"Large scale localization of protein phosphorylation by use ofelectron capture dissociation mass spectrometry."; Sweet S.M., Bailey C.M., Cunningham D.L., Heath J.K., Cooper H.J.; Mol. Cell. Proteomics 8:904-912(2009). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-164, AND MASSSPECTROMETRY.	19131326 [Abstract]
"The phagosomal proteome in interferon-gamma-activated macrophages."; Trost M., English L., Lemieux S., Courcelles M., Desjardins M.,Thibault P.; Immunity 30:143-154(2009). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-497 AND SER-673, ANDMASS SPECTROMETRY.	19144319 [Abstract]
"Solid tumor proteome and phosphoproteome analysis by high resolutionmass spectrometry."; Zanivan S., Gnad F., Wickstroem S.A., Geiger T., Macek B., Cox J.,Faessler R., Mann M.; J. Proteome Res. 7:5314-5326(2008). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-132; SER-673 ANDSER-776, AND MASS SPECTROMETRY.	19367708 [Abstract]
"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-155, AND MASSSPECTROMETRY.	17242355 [Abstract]
"Qualitative and quantitative analyses of protein phosphorylation innaive and stimulated mouse synaptosomal preparations."; Munton R.P., Tweedie-Cullen R., Livingstone-Zatchej M., Weinandy F.,Waidelich M., Longo D., Gehrig P., Potthast F., Rutishauser D.,Gerrits B., Panse C., Schlapbach R., Mansuy I.M.; Mol. Cell. Proteomics 6:283-293(2007). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-497, AND MASSSPECTROMETRY.	17114649 [Abstract]

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