dbPTM

RHOA_HUMAN - PTM Information in dbPTM

Basic Information of Protein

Overview of Protein Modification Sites with Functional and Structural Information
UniProt ID	RHOA_HUMAN
UniProt AC	P61586
Protein Name	Transforming protein RhoA
Gene Name	RHOA
Organism	Homo sapiens (Human).
Sequence Length	193
Subcellular Localization	Cell membrane Lipid-anchor Cytoplasmic side. Cytoplasm, cytoskeleton. Cleavage furrow. Cytoplasm, cell cortex . Midbody. Cell projection, lamellipodium. Localized to cell-cell contacts in calcium-treated keratinocytes (By similarity). Translocates
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. Required for the apical junction formation of keratinocyte cell-cell adhesion. Stimulates PKN2 kinase activity. 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. 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. Required for the apical junction formation of keratinocyte cell-cell adhesion. 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). 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	MAAIRKKLVIVGDGACGKTCLLIVFSKDQFPEVYVPTVFENYVADIEVDGKQVELALWDTAGQEDYDRLRPLSYPDTDVILMCFSIDSPDSLENIPEKWTPEVKHFCPNVPIILVGNKKDLRNDEHTRRELAKMKQEPVKPEEGRDMANRIGAFGYMECSAKTKDGVREVFEMATRAALQARRGKKKSGCLVL

Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations	Modification	Substrate Peptides & Secondary Structure	ASA (%)	Reference
6	Ubiquitination	--MAAIRKKLVIVGD --CCCCCCEEEEECC	44.33	-
7	Ubiquitination	-MAAIRKKLVIVGDG -CCCCCCEEEEECCC	37.83	-
16	S-palmitoylation	VIVGDGACGKTCLLI EEECCCCCCCEEEEE	7.60	29575903
19	Phosphorylation	GDGACGKTCLLIVFS CCCCCCCEEEEEEEE	8.15	19060867
26	Phosphorylation	TCLLIVFSKDQFPEV EEEEEEEECCCCCCE	25.16	19060867
27	Sumoylation	CLLIVFSKDQFPEVY EEEEEEECCCCCCEE	44.05	-
34	Phosphorylation	KDQFPEVYVPTVFEN CCCCCCEECCCEECC	10.07	23532336
34	O-linked_Glycosylation	KDQFPEVYVPTVFEN CCCCCCEECCCEECC	10.07	24141704
34	Nitration	KDQFPEVYVPTVFEN CCCCCCEECCCEECC	10.07	-
34	AMPylation	KDQFPEVYVPTVFEN CCCCCCEECCCEECC	10.07	19362538
34	O-AMP-tyrosine	KDQFPEVYVPTVFEN CCCCCCEECCCEECC	10.07	-
37	O-AMP-threonine	FPEVYVPTVFENYVA CCCEECCCEECCEEE	27.99	-
37	Phosphorylation	FPEVYVPTVFENYVA CCCEECCCEECCEEE	27.99	25106551
37	O-linked_Glycosylation	FPEVYVPTVFENYVA CCCEECCCEECCEEE	27.99	7775453
37	AMPylation	FPEVYVPTVFENYVA CCCEECCCEECCEEE	27.99	19039103
41	ADP-ribosylation	YVPTVFENYVADIEV ECCCEECCEEEEEEE	25.72	1328215
41	ADP-ribosylation	YVPTVFENYVADIEV ECCCEECCEEEEEEE	25.72	-
42	Phosphorylation	VPTVFENYVADIEVD CCCEECCEEEEEEEC	6.99	-
60	Phosphorylation	VELALWDTAGQEDYD EEEEEEECCCCCCHH	22.55	29978859
63	Serotonylation	ALWDTAGQEDYDRLR EEEECCCCCCHHHCC	37.61	-
66	Phosphorylation	DTAGQEDYDRLRPLS ECCCCCCHHHCCCCC	11.38	25884760
73	Phosphorylation	YDRLRPLSYPDTDVI HHHCCCCCCCCCCEE	36.98	-
88	Phosphorylation	LMCFSIDSPDSLENI EEEEECCCCHHHHCC	29.01	-
100	Phosphorylation	ENIPEKWTPEVKHFC HCCCCCCCHHHHHHC	22.19	-
104	Ubiquitination	EKWTPEVKHFCPNVP CCCCHHHHHHCCCCC	29.33	21890473
104	Ubiquitination	EKWTPEVKHFCPNVP CCCCHHHHHHCCCCC	29.33	21890473
107	S-palmitoylation	TPEVKHFCPNVPIIL CHHHHHHCCCCCEEE	2.10	29575903
118	Ubiquitination	PIILVGNKKDLRNDE CEEEECCHHHHCCCH	41.56	-
119	Methylation	IILVGNKKDLRNDEH EEEECCHHHHCCCHH	67.03	23644510
119	Ubiquitination	IILVGNKKDLRNDEH EEEECCHHHHCCCHH	67.03	-
128	Methylation	LRNDEHTRRELAKMK HCCCHHHHHHHHHHH	31.80	115491229
133	Ubiquitination	HTRRELAKMKQEPVK HHHHHHHHHHCCCCC	60.29	21890473
135	Ubiquitination	RRELAKMKQEPVKPE HHHHHHHHCCCCCCH	51.29	21890473
135	Acetylation	RRELAKMKQEPVKPE HHHHHHHHCCCCCCH	51.29	26051181
140	Ubiquitination	KMKQEPVKPEEGRDM HHHCCCCCCHHCCCH	58.38	21890473
156	Phosphorylation	NRIGAFGYMECSAKT HHHCCCEEEECCCCC	5.36	28152594
157	Sulfoxidation	RIGAFGYMECSAKTK HHCCCEEEECCCCCC	4.24	21406390
159	Glutathionylation	GAFGYMECSAKTKDG CCCEEEECCCCCCCH	2.46	22555962
159	S-nitrosylation	GAFGYMECSAKTKDG CCCEEEECCCCCCCH	2.46	2212679
160	Phosphorylation	AFGYMECSAKTKDGV CCEEEECCCCCCCHH	21.35	28152594
162	Ubiquitination	GYMECSAKTKDGVRE EEEECCCCCCCHHHH	39.55	-
162	Acetylation	GYMECSAKTKDGVRE EEEECCCCCCCHHHH	39.55	25953088
164	Ubiquitination	MECSAKTKDGVREVF EECCCCCCCHHHHHH	52.34	-
173	Sulfoxidation	GVREVFEMATRAALQ HHHHHHHHHHHHHHH	2.91	30846556
188	Phosphorylation	ARRGKKKSGCLVL-- HHCCCCCCCCEEC--	43.55	15890975
190	Geranylgeranylation	RGKKKSGCLVL---- CCCCCCCCEEC----	2.83	-
190	Methylation	RGKKKSGCLVL---- CCCCCCCCEEC----	2.83	-

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
34	Y	Phosphorylation	Kinase	BCR-ABL1	A9UF07	PSP
34	Y	Phosphorylation	Kinase	SRC	P12931	PSP
42	Y	Phosphorylation	Kinase	MET	P08581	PSP
66	Y	Phosphorylation	Kinase	BCR-ABL1	A9UF07	PSP
66	Y	Phosphorylation	Kinase	SRC	P12931	PSP
88	S	Phosphorylation	Kinase	MAPK3	P27361	GPS
100	T	Phosphorylation	Kinase	MAPK3	P27361	GPS
188	S	Phosphorylation	Kinase	PKACA	P17612	PSP
188	S	Phosphorylation	Kinase	PRKACA	P05132	GPS
188	S	Phosphorylation	Kinase	PKG1	Q13976	PSP
188	S	Phosphorylation	Kinase	PKA-FAMILY	-	GPS
188	S	Phosphorylation	Kinase	PKA_GROUP	-	PhosphoELM
-	K	Ubiquitination	E3 ubiquitin ligase	KCTD13	Q8WZ19	PMID:19782033
-	K	Ubiquitination	E3 ubiquitin ligase	TNFAIP1	Q13829	PMID:19782033
-	K	Ubiquitination	E3 ubiquitin ligase	SMURF2	Q9HAU4	PMID:21402695
-	K	Ubiquitination	E3 ubiquitin ligase	FBXL19	Q6PCT2	PMID:24658274
-	K	Ubiquitination	E3 ubiquitin ligase	SMURF1	Q9HCE7	PMID:14657501

Functions of PTM Sites

Modified Location	Modified Residue	Modification	Reference
37	T	Glycosylation	7777059
(Microbial infection) Glycosylated (O-GlcNAcylated) at Thr-37 by C.novyi toxin TcdA.
188	S	Phosphorylation	11162591
Phosphorylation by PRKG1 at Ser-188 inactivates RHOA signaling.
188	S	Phosphorylation	11162591
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.

Modified Location	Modification	Variant Position (Distance <= 10)	Residue Change	SAP	Related Disease	Reference
Oops, there are no SNP-PTM records of RHOA_HUMAN !!

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference
RHG01_HUMAN	ARHGAP1	physical	16189514
BID_HUMAN	BID	physical	15659383
TR10B_HUMAN	TNFRSF10B	physical	15659383
EZRI_HUMAN	EZR	physical	15659383
FADD_HUMAN	FADD	physical	15659383
TNFL6_HUMAN	FASLG	physical	15659383
MK08_HUMAN	MAPK8	physical	15659383
MOES_HUMAN	MSN	physical	15659383
CASPA_HUMAN	CASP10	physical	15659383
CASP8_HUMAN	CASP8	physical	15659383
TNR1A_HUMAN	TNFRSF1A	physical	15659383
ARHGP_HUMAN	ARHGEF25	physical	15069594
RHG05_HUMAN	ARHGAP5	physical	12842009
ROCK1_HUMAN	ROCK1	physical	12773565
PKN1_HUMAN	PKN1	physical	12773565
DIAP1_HUMAN	DIAPH1	physical	12773565
CTRO_HUMAN	CIT	physical	12773565
RHPN2_HUMAN	RHPN2	physical	12773565
KTN1_HUMAN	KTN1	physical	12773565
ITPR1_HUMAN	ITPR1	physical	12766172
TRPC1_HUMAN	TRPC1	physical	12766172
ROCK1_MOUSE	Rock1	physical	9535835
ARHG8_MOUSE	Net1	physical	9535835
DIAP3_MOUSE	Diap3	physical	9535835
DIAP1_MOUSE	Diap1	physical	9535835
KTN1_MOUSE	Ktn1	physical	9535835
ARHG8_HUMAN	NET1	physical	9535835
SKN7_YEAST	SKN7	physical	9535835
DPYL1_HUMAN	CRMP1	genetic	12482610
DPYL2_HUMAN	DPYSL2	genetic	12482610
CTRO_HUMAN	CIT	physical	8543060
ARHGC_HUMAN	ARHGEF12	physical	11373293
KTN1_HUMAN	KTN1	physical	11162552
PLCG1_HUMAN	PLCG1	physical	12071848
ARHG3_HUMAN	ARHGEF3	physical	12221096
PKN2_HUMAN	PKN2	physical	8910519
VAV3_HUMAN	VAV3	physical	10523675
GDIR1_HUMAN	ARHGDIA	physical	11149925
ARHGI_HUMAN	ARHGEF18	physical	11085924
KCNA2_HUMAN	KCNA2	physical	9635436
KTN1_HUMAN	KTN1	physical	8769096
KTN1_HUMAN	KTN1	physical	11689693
RHG01_HUMAN	ARHGAP1	physical	9548756
RHG35_HUMAN	ARHGAP35	physical	9548756
ARHGB_HUMAN	ARHGEF11	physical	10526156
MPRIP_HUMAN	MPRIP	physical	9199174
DGKQ_HUMAN	DGKQ	physical	10066731
PKN1_HUMAN	PKN1	physical	9446575
ROCK2_HUMAN	ROCK2	physical	11350930
ROCK1_HUMAN	ROCK1	physical	8798490
TRIO_HUMAN	TRIO	physical	10948190
MCF2_HUMAN	MCF2	physical	10854437
PKHG2_HUMAN	PLEKHG2	physical	11839748
SMUF1_HUMAN	SMURF1	physical	16622418
RHG35_HUMAN	ARHGAP35	physical	15102857
SRGP1_HUMAN	SRGAP1	physical	20856855
CAV1_HUMAN	CAV1	physical	20460433
5HT1A_HUMAN	HTR1A	physical	17142836
MDM2_HUMAN	MDM2	physical	22907703
MARK2_HUMAN	MARK2	physical	22072711
ARHG2_HUMAN	ARHGEF2	physical	22072711
RS27A_HUMAN	RPS27A	physical	22939629
RL18_HUMAN	RPL18	physical	22939629
CDN1B_HUMAN	CDKN1B	physical	19470470
RPN2_HUMAN	RPN2	physical	21988832
SMAD2_HUMAN	SMAD2	physical	20195357
BIRC2_HUMAN	BIRC2	physical	24276241
BACD1_HUMAN	KCTD13	physical	19782033
BACD2_HUMAN	TNFAIP1	physical	19782033
GDIR1_HUMAN	ARHGDIA	physical	25416956
TRIP6_HUMAN	TRIP6	physical	25416956
RIPR2_HUMAN	FAM65B	physical	25416956
IKZF3_HUMAN	IKZF3	physical	25416956
NNRE_HUMAN	APOA1BP	physical	26344197
GDIR1_HUMAN	ARHGDIA	physical	26344197
GDIR2_HUMAN	ARHGDIB	physical	26344197
GDIR3_HUMAN	ARHGDIG	physical	26344197
GORS2_HUMAN	GORASP2	physical	26344197
PA1B2_HUMAN	PAFAH1B2	physical	26344197
PRRC1_HUMAN	PRRC1	physical	26344197
RPE_HUMAN	RPE	physical	26344197
GLYM_HUMAN	SHMT2	physical	26344197
CMC1_HUMAN	SLC25A12	physical	26344197
TRIO_HUMAN	TRIO	physical	26344197
CNKR1_HUMAN	CNKSR1	physical	14749388
RHG01_HUMAN	ARHGAP1	physical	14749388
RHPN1_HUMAN	RHPN1	physical	14749388
RIPR2_HUMAN	FAM65B	physical	21516116
NVL_HUMAN	NVL	physical	26496610
UB2V2_HUMAN	UBE2V2	physical	26496610
FUBP3_HUMAN	FUBP3	physical	26496610
BAZ1A_HUMAN	BAZ1A	physical	26496610
STK39_HUMAN	STK39	physical	26496610
SYNP2_HUMAN	SYNPO2	physical	26496610
DAAM1_HUMAN	DAAM1	physical	25241761
RASF1_HUMAN	RASSF1	physical	26825171
RTKN_HUMAN	RTKN	physical	26825171
S10A4_HUMAN	S100A4	physical	26825171
AGAP2_HUMAN	AGAP2	physical	22453919
AGAP1_HUMAN	AGAP1	physical	22453919
ARHGB_HUMAN	ARHGEF11	physical	28514442
ARHG2_HUMAN	ARHGEF2	physical	28514442
ARHG1_HUMAN	ARHGEF1	physical	28514442
ARHGC_HUMAN	ARHGEF12	physical	28514442
GDS1_HUMAN	RAP1GDS1	physical	28514442
PKN3_HUMAN	PKN3	physical	28514442
PKN2_HUMAN	PKN2	physical	28514442
RAP2C_HUMAN	RAP2C	physical	28514442
BGAL_HUMAN	GLB1	physical	28514442
PPGB_HUMAN	CTSA	physical	28514442
DAAM1_HUMAN	DAAM1	physical	28514442
PTEN_HUMAN	PTEN	physical	22720799
GDIR1_HUMAN	ARHGDIA	physical	26719334

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 RHOA_HUMAN

Related Literatures of Post-Translational Modification

Phosphorylation
Reference	PubMed
"cGMP-dependent protein kinase phosphorylates and inactivates RhoA."; Sawada N., Itoh H., Yamashita J., Doi K., Inoue M., Masatsugu K.,Fukunaga Y., Sakaguchi S., Sone M., Yamahara K., Yurugi T., Nakao K.; Biochem. Biophys. Res. Commun. 280:798-805(2001). Cited for: PHOSPHORYLATION AT SER-188 BY PRKG1.	11162591 [Abstract]
"An extensive survey of tyrosine phosphorylation revealing new sitesin human mammary epithelial cells."; Heibeck T.H., Ding S.-J., Opresko L.K., Zhao R., Schepmoes A.A.,Yang F., Tolmachev A.V., Monroe M.E., Camp D.G. II, Smith R.D.,Wiley H.S., Qian W.-J.; J. Proteome Res. 8:3852-3861(2009). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-156, AND MASSSPECTROMETRY.	19534553 [Abstract]

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