RHOA_MOUSE - PTM Information in dbPTM

Basic Information of Protein

• UniProt ID: RHOA_MOUSE
• UniProt AC: Q9QUI0
• Protein Name: Transforming protein RhoA
• Gene Name: Rhoa
• Organism: Mus musculus (Mouse).
• Sequence Length: 193
• Subcellular Localization: Cell membrane; Lipid-anchor; Cytoplasmic side. Cytoplasm, cytoskeleton. Cleavage furrow. Cytoplasm, cell cortex. Midbody. Cell projection, lamellipodium . Translocates to the equatorial region before furrow formation in a ECT2-dependent manner. Local
• Protein Description: Regulates a signal transduction pathway linking plasma membrane receptors to the assembly of focal adhesions and actin stress fibers. Involved in a microtubule-dependent signal that is required for the myosin contractile ring formation during cell cycle cytokinesis. Plays an essential role in cleavage furrow formation. May be an activator of PLCE1. Activated by ARHGEF2, which promotes the exchange of GDP for GTP. Essential for the SPATA13-mediated regulation of cell migration and adhesion assembly and disassembly. The MEMO1-RHOA-DIAPH1 signaling pathway plays an important role in ERBB2-dependent stabilization of microtubules at the cell cortex. It controls the localization of APC and CLASP2 to the cell membrane, via the regulation of GSK3B activity. In turn, membrane-bound APC allows the localization of the MACF1 to the cell membrane, which is required for microtubule capture and stabilization (By similarity). Required for the apical junction formation of keratinocyte cell-cell adhesion. Regulates KCNA2 potassium channel activity by reducing its location at the cell surface in response to CHRM1 activation; promotes KCNA2 endocytosis. [PubMed: 9635436]
• Protein Sequence: MAAIRKKLVIVGDGACGKTCLLIVFSKDQFPEVYVPTVFENYVADIEVDGKQVELALWDTAGQEDYDRLRPLSYPDTDVILMCFSIDSPDSLENIPEKWTPEVKHFCPNVPIILVGNKKDLRNDEHTRRELAKMKQEPVKPEEGRDMANRIGAFGYMECSAKTKDGVREVFEMATRAALQARRGKKKSGCLIL

Overview of Protein Modification Sites with Functional and Structural Information

Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations	Modification	Substrate Peptides & Secondary Structure	ASA (%)	Reference
16	S-nitrosocysteine	VIVGDGACGKTCLLI EEECCCCCCCEEEEE	7.60	-
16	S-palmitoylation	VIVGDGACGKTCLLI EEECCCCCCCEEEEE	7.60	28526873
16	S-nitrosylation	VIVGDGACGKTCLLI EEECCCCCCCEEEEE	7.60	21278135
19	Phosphorylation	GDGACGKTCLLIVFS CCCCCCCEEEEEEEE	8.15	17203969
26	Phosphorylation	TCLLIVFSKDQFPEV EEEEEEEECCCCCCE	25.16	17203969
34	Phosphorylation	KDQFPEVYVPTVFEN CCCCCCEECCCEECC	10.07	29514104
42	Phosphorylation	VPTVFENYVADIEVD CCCEECCEEEEEEEC	6.99	-
63	Serotonylation	ALWDTAGQEDYDRLR EEEECCCCCCHHHCC	37.61	14697203
66	Phosphorylation	DTAGQEDYDRLRPLS ECCCCCCHHHCCCCC	11.38	25159016
104	Ubiquitination	EKWTPEVKHFCPNVP CCCCHHHHHHCCCCC	29.33	-
107	S-palmitoylation	TPEVKHFCPNVPIIL CHHHHHHCCCCCEEE	2.10	28526873
107	S-nitrosylation	TPEVKHFCPNVPIIL CHHHHHHCCCCCEEE	2.10	21278135
107	S-nitrosocysteine	TPEVKHFCPNVPIIL CHHHHHHCCCCCEEE	2.10	-
118	Ubiquitination	PIILVGNKKDLRNDE CEEEECCHHHHCCCH	41.56	-
119	Ubiquitination	IILVGNKKDLRNDEH EEEECCHHHHCCCHH	67.03	-
135	Malonylation	RRELAKMKQEPVKPE HHHHHHHHCCCCCCH	51.29	26320211
135	Acetylation	RRELAKMKQEPVKPE HHHHHHHHCCCCCCH	51.29	22826441
135	Ubiquitination	RRELAKMKQEPVKPE HHHHHHHHCCCCCCH	51.29	-
156	Phosphorylation	NRIGAFGYMECSAKT HHHCCCEEEECCCCC	5.36	-
159	S-nitrosocysteine	GAFGYMECSAKTKDG CCCEEEECCCCCCCH	2.46	-
159	S-nitrosylation	GAFGYMECSAKTKDG CCCEEEECCCCCCCH	2.46	21278135
159	S-palmitoylation	GAFGYMECSAKTKDG CCCEEEECCCCCCCH	2.46	28526873
162	Ubiquitination	GYMECSAKTKDGVRE EEEECCCCCCCHHHH	39.55	-
188	Phosphorylation	ARRGKKKSGCLIL-- HHCCCCCCCCEEC--	43.55	15102857
190	Geranylgeranylation	RGKKKSGCLIL---- CCCCCCCCEEC----	2.49	-
190	Methylation	RGKKKSGCLIL---- CCCCCCCCEEC----	2.49	-

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
26	S	Phosphorylation	Kinase	STK24	Q99KH8	GPS
42	Y	Phosphorylation	Kinase	SRC	P12931	PSP
188	S	Phosphorylation	Kinase	PKG1	P0C605	PSP
188	S	Phosphorylation	Kinase	CHAK1	Q96QT4	PSP
-	K	Ubiquitination	E3 ubiquitin ligase	Kctd13	Q8BGV7	PMID:22199232
-	K	Ubiquitination	E3 ubiquitin ligase	Smurf1	Q9CUN6	PMID:22199232
-	K	Ubiquitination	E3 ubiquitin ligase	Tnfaip1	O70479	PMID:22199232

Functions of PTM Sites

Modified Location	Modified Residue	Modification	Function	Reference
188	S	Phosphorylation	Phosphorylation by PRKG1 at Ser-188 inactivates RHOA signaling (By similarity).	-
188	S	Phosphorylation	Phosphorylation by SLK at Ser-188 in response to AGTR2 activation (By similarity).	-

Disease-associated PTM Sites based on SAP

* Distance = the distance between SAP position and PTM sites.

Oops, there are no SNP-PTM records of RHOA_MOUSE !!

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference
RHOA_HUMAN	RHOA	physical	20360068
SMUF1_HUMAN	SMURF1	physical	15710384
PKHG5_MOUSE	Plekhg5	physical	16467373
SRGP1_MOUSE	Srgap1	physical	11672528
RGRF1_MOUSE	Rasgrf1	physical	17993462
CTND1_MOUSE	Ctnnd1	physical	17993462
C4BPA_HUMAN	C4BPA	physical	26496610
CLK2_HUMAN	CLK2	physical	26496610
GLGB_HUMAN	GBE1	physical	26496610
PEPL_HUMAN	PPL	physical	26496610
MKNK1_HUMAN	MKNK1	physical	26496610
PAPS1_HUMAN	PAPSS1	physical	26496610
COX5A_HUMAN	COX5A	physical	26496610
Z518A_HUMAN	ZNF518A	physical	26496610
TRI16_HUMAN	TRIM16	physical	26496610
TXN4A_HUMAN	TXNL4A	physical	26496610
POLK_HUMAN	POLK	physical	26496610
F208B_HUMAN	FAM208B	physical	26496610
GPAM1_HUMAN	GPALPP1	physical	26496610
FGD6_HUMAN	FGD6	physical	26496610
SYRM_HUMAN	RARS2	physical	26496610
SCYL1_HUMAN	SCYL1	physical	26496610
GPBP1_HUMAN	GPBP1	physical	26496610
CORO7_HUMAN	CORO7	physical	26496610
COG7_HUMAN	COG7	physical	26496610
PDE12_HUMAN	PDE12	physical	26496610
KPRP_HUMAN	KPRP	physical	26496610

Drug and Disease Associations

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