dbPTM

GDIR1_HUMAN - PTM Information in dbPTM

Basic Information of Protein

Overview of Protein Modification Sites with Functional and Structural Information
UniProt ID	GDIR1_HUMAN
UniProt AC	P52565
Protein Name	Rho GDP-dissociation inhibitor 1
Gene Name	ARHGDIA
Organism	Homo sapiens (Human).
Sequence Length	204
Subcellular Localization	Cytoplasm .
Protein Description	Controls Rho proteins homeostasis. Regulates the GDP/GTP exchange reaction of the Rho proteins by inhibiting the dissociation of GDP from them, and the subsequent binding of GTP to them. Retains Rho proteins such as CDC42, RAC1 and RHOA in an inactive cytosolic pool, regulating their stability and protecting them from degradation. Actively involved in the recycling and distribution of activated Rho GTPases in the cell, mediates extraction from membranes of both inactive and activated molecules due its exceptionally high affinity for prenylated forms. Through the modulation of Rho proteins, may play a role in cell motility regulation. In glioma cells, inhibits cell migration and invasion by mediating the signals of SEMA5A and PLXNB3 that lead to inactivation of RAC1..
Protein Sequence	MAEQEPTAEQLAQIAAENEEDEHSVNYKPPAQKSIQEIQELDKDDESLRKYKEALLGRVAVSADPNVPNVVVTGLTLVCSSAPGPLELDLTGDLESFKKQSFVLKEGVEYRIKISFRVNREIVSGMKYIQHTYRKGVKIDKTDYMVGSYGPRAEEYEFLTPVEEAPKGMLARGSYSIKSRFTDDDKTDHLSWEWNLTIKKDWKD

Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations	Modification	Substrate Peptides & Secondary Structure	ASA (%)	Reference
2	Acetylation	------MAEQEPTAE ------CCCCCCCHH	27.46	20068231
7	Phosphorylation	-MAEQEPTAEQLAQI -CCCCCCCHHHHHHH	41.91	23401153
24	Phosphorylation	ENEEDEHSVNYKPPA HCCCCCCCCCCCCCC	15.26	23401153
27	Phosphorylation	EDEHSVNYKPPAQKS CCCCCCCCCCCCHHH	23.79	23401153
28	Ubiquitination	DEHSVNYKPPAQKSI CCCCCCCCCCCHHHH	39.04	-
28	Acetylation	DEHSVNYKPPAQKSI CCCCCCCCCCCHHHH	39.04	23236377
34	Phosphorylation	YKPPAQKSIQEIQEL CCCCCHHHHHHHHHH	19.88	29255136
43	Succinylation	QEIQELDKDDESLRK HHHHHHCCCCHHHHH	78.63	23954790
43	Ubiquitination	QEIQELDKDDESLRK HHHHHHCCCCHHHHH	78.63	-
43	Malonylation	QEIQELDKDDESLRK HHHHHHCCCCHHHHH	78.63	26320211
43	2-Hydroxyisobutyrylation	QEIQELDKDDESLRK HHHHHHCCCCHHHHH	78.63	-
43	Acetylation	QEIQELDKDDESLRK HHHHHHCCCCHHHHH	78.63	23954790
47	Phosphorylation	ELDKDDESLRKYKEA HHCCCCHHHHHHHHH	40.23	23401153
50	Methylation	KDDESLRKYKEALLG CCCHHHHHHHHHHHH	67.00	17506542
50	Ubiquitination	KDDESLRKYKEALLG CCCHHHHHHHHHHHH	67.00	-
51	Phosphorylation	DDESLRKYKEALLGR CCHHHHHHHHHHHHC	13.97	23312004
52	Methylation	DESLRKYKEALLGRV CHHHHHHHHHHHHCE	39.28	17506542
52	Ubiquitination	DESLRKYKEALLGRV CHHHHHHHHHHHHCE	39.28	-
52	2-Hydroxyisobutyrylation	DESLRKYKEALLGRV CHHHHHHHHHHHHCE	39.28	-
52	Acetylation	DESLRKYKEALLGRV CHHHHHHHHHHHHCE	39.28	27452117
96	Phosphorylation	DLTGDLESFKKQSFV ECCCCHHHHHHEEEE	50.06	22817900
99	Ubiquitination	GDLESFKKQSFVLKE CCHHHHHHEEEEEEC	49.52	21890473
99	Ubiquitination	GDLESFKKQSFVLKE CCHHHHHHEEEEEEC	49.52	21890473
99	Ubiquitination	GDLESFKKQSFVLKE CCHHHHHHEEEEEEC	49.52	21890473
99	Ubiquitination	GDLESFKKQSFVLKE CCHHHHHHEEEEEEC	49.52	21890473
99	Ubiquitination	GDLESFKKQSFVLKE CCHHHHHHEEEEEEC	49.52	21890473
99	Malonylation	GDLESFKKQSFVLKE CCHHHHHHEEEEEEC	49.52	26320211
101	Phosphorylation	LESFKKQSFVLKEGV HHHHHHEEEEEECCE	26.63	23911959
105	Succinylation	KKQSFVLKEGVEYRI HHEEEEEECCEEEEE	47.31	23954790
105	Ubiquitination	KKQSFVLKEGVEYRI HHEEEEEECCEEEEE	47.31	19608861
105	Acetylation	KKQSFVLKEGVEYRI HHEEEEEECCEEEEE	47.31	19608861
115	Phosphorylation	VEYRIKISFRVNREI EEEEEEEEEEECHHH	11.29	23312004
126	Sulfoxidation	NREIVSGMKYIQHTY CHHHHCCCCHHHHHH	2.01	30846556
127	Ubiquitination	REIVSGMKYIQHTYR HHHHCCCCHHHHHHC	42.60	21890473
127	Ubiquitination	REIVSGMKYIQHTYR HHHHCCCCHHHHHHC	42.60	21890473
127	Ubiquitination	REIVSGMKYIQHTYR HHHHCCCCHHHHHHC	42.60	21890473
127	Ubiquitination	REIVSGMKYIQHTYR HHHHCCCCHHHHHHC	42.60	21890473
127	Malonylation	REIVSGMKYIQHTYR HHHHCCCCHHHHHHC	42.60	26320211
127	Acetylation	REIVSGMKYIQHTYR HHHHCCCCHHHHHHC	42.60	19608861
127	Ubiquitination	REIVSGMKYIQHTYR HHHHCCCCHHHHHHC	42.60	21890473
128	Phosphorylation	EIVSGMKYIQHTYRK HHHCCCCHHHHHHCC	9.27	26437602
132	Phosphorylation	GMKYIQHTYRKGVKI CCCHHHHHHCCCCCC	14.51	28152594
133	Phosphorylation	MKYIQHTYRKGVKID CCHHHHHHCCCCCCC	14.27	24927040
138	Sumoylation	HTYRKGVKIDKTDYM HHHCCCCCCCCCCCC	54.58	-
138	Malonylation	HTYRKGVKIDKTDYM HHHCCCCCCCCCCCC	54.58	26320211
138	Sumoylation	HTYRKGVKIDKTDYM HHHCCCCCCCCCCCC	54.58	25114211
138	Acetylation	HTYRKGVKIDKTDYM HHHCCCCCCCCCCCC	54.58	25953088
141	Sumoylation	RKGVKIDKTDYMVGS CCCCCCCCCCCCEEC	46.93	19608861
141	Succinylation	RKGVKIDKTDYMVGS CCCCCCCCCCCCEEC	46.93	-
141	Succinylation	RKGVKIDKTDYMVGS CCCCCCCCCCCCEEC	46.93	-
141	Ubiquitination	RKGVKIDKTDYMVGS CCCCCCCCCCCCEEC	46.93	21890473
141	Ubiquitination	RKGVKIDKTDYMVGS CCCCCCCCCCCCEEC	46.93	21890473
141	Ubiquitination	RKGVKIDKTDYMVGS CCCCCCCCCCCCEEC	46.93	20639865
141	2-Hydroxyisobutyrylation	RKGVKIDKTDYMVGS CCCCCCCCCCCCEEC	46.93	-
141	Malonylation	RKGVKIDKTDYMVGS CCCCCCCCCCCCEEC	46.93	26320211
141	Acetylation	RKGVKIDKTDYMVGS CCCCCCCCCCCCEEC	46.93	16916647
144	Phosphorylation	VKIDKTDYMVGSYGP CCCCCCCCCEECCCC	10.03	22817900
145	Sulfoxidation	KIDKTDYMVGSYGPR CCCCCCCCEECCCCC	2.83	30846556
148	Phosphorylation	KTDYMVGSYGPRAEE CCCCCEECCCCCHHH	18.59	21815630
149	Phosphorylation	TDYMVGSYGPRAEEY CCCCEECCCCCHHHE	25.81	27732954
150	Acetylation	DYMVGSYGPRAEEYE CCCEECCCCCHHHEE	13.60	19608861
156	Phosphorylation	YGPRAEEYEFLTPVE CCCCHHHEEEEECHH	11.95	28796482
160	Phosphorylation	AEEYEFLTPVEEAPK HHHEEEEECHHHCCC	30.52	28450419
167	Ubiquitination	TPVEEAPKGMLARGS ECHHHCCCCCCCCCC	65.09	21906983
167	Ubiquitination	TPVEEAPKGMLARGS ECHHHCCCCCCCCCC	65.09	21890473
167	Acetylation	TPVEEAPKGMLARGS ECHHHCCCCCCCCCC	65.09	23954790
167	Ubiquitination	TPVEEAPKGMLARGS ECHHHCCCCCCCCCC	65.09	21890473
172	Ubiquitination	APKGMLARGSYSIKS CCCCCCCCCCEEEEE	30.54	19608861
172	Acetylation	APKGMLARGSYSIKS CCCCCCCCCCEEEEE	30.54	19608861
174	Phosphorylation	KGMLARGSYSIKSRF CCCCCCCCEEEEECC	15.34	25159151
175	Phosphorylation	GMLARGSYSIKSRFT CCCCCCCEEEEECCC	19.76	26699800
176	Phosphorylation	MLARGSYSIKSRFTD CCCCCCEEEEECCCC	25.82	26699800
178	Succinylation	ARGSYSIKSRFTDDD CCCCEEEEECCCCCC	29.64	23954790
178	Ubiquitination	ARGSYSIKSRFTDDD CCCCEEEEECCCCCC	29.64	19608861
178	Malonylation	ARGSYSIKSRFTDDD CCCCEEEEECCCCCC	29.64	26320211
178	Acetylation	ARGSYSIKSRFTDDD CCCCEEEEECCCCCC	29.64	19608861
186	Ubiquitination	SRFTDDDKTDHLSWE ECCCCCCCCCCEEEE	63.95	19608861
186	Acetylation	SRFTDDDKTDHLSWE ECCCCCCCCCCEEEE	63.95	19608861
197	Phosphorylation	LSWEWNLTIKKDWKD EEEEEEEEEECCCCC	27.77	26091039
223	Acetylation	-------------------------- --------------------------		19608861

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
27	Y	Phosphorylation	Kinase	SRC	P12931	PSP
34	S	Phosphorylation	Kinase	PRKCA	P17252	GPS
96	S	Phosphorylation	Kinase	PRKCA	P17252	GPS
101	S	Phosphorylation	Kinase	PAK1	Q13153	PSP
156	Y	Phosphorylation	Kinase	SRC	P12931	PSP
174	S	Phosphorylation	Kinase	BRSK2	Q8IWQ3	PSP
174	S	Phosphorylation	Kinase	PRKACA	P17612	GPS
174	S	Phosphorylation	Kinase	PAK1	Q13153	PSP
-	K	Ubiquitination	E3 ubiquitin ligase	RNF128	Q8TEB7	PMID:17114425

Functions of PTM Sites

Modified Location	Modified Residue	Modification	Function	Reference
Oops, there are no descriptions of PTM sites of GDIR1_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 GDIR1_HUMAN !!

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference
RHOA_HUMAN	RHOA	physical	17353931
RAC1_HUMAN	RAC1	physical	17353931
RHOC_HUMAN	RHOC	physical	17353931
CDC42_HUMAN	CDC42	physical	17353931
EI2BA_HUMAN	EIF2B1	physical	17353931
DHX9_HUMAN	DHX9	physical	17353931
IF2B1_HUMAN	IGF2BP1	physical	17353931
ROAA_HUMAN	HNRNPAB	physical	17353931
EWS_HUMAN	EWSR1	physical	17353931
ROA3_HUMAN	HNRNPA3	physical	17353931
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
RHOA_HUMAN	RHOA	physical	15659383
TNR1A_HUMAN	TNFRSF1A	physical	15659383
ACL6A_HUMAN	ACTL6A	physical	16169070
CDN1B_HUMAN	CDKN1B	physical	16169070
NED4L_HUMAN	NEDD4L	physical	16169070
SH3G3_HUMAN	SH3GL3	physical	16169070
PLAK_HUMAN	JUP	physical	16169070
FEN1_HUMAN	FEN1	physical	16169070
RADI_HUMAN	RDX	physical	9287351
GDIR1_HUMAN	ARHGDIA	physical	11513578
RAC1_HUMAN	RAC1	physical	10673424
CDC42_HUMAN	CDC42	physical	9490022
RHOA_HUMAN	RHOA	physical	9490022
RAC1_HUMAN	RAC1	physical	9490022
RAC2_HUMAN	RAC2	physical	9490022
RAC1_HUMAN	RAC1	physical	11368848
RAC2_HUMAN	RAC2	physical	11368848
RHOH_HUMAN	RHOH	physical	11368848
RHOG_HUMAN	RHOG	physical	11368848
RHOA_HUMAN	RHOA	physical	11368848
XIAP_HUMAN	XIAP	physical	22532870
PSD10_HUMAN	PSMD10	physical	20628200
RHOA_HUMAN	RHOA	physical	20628200
PIR_HUMAN	PIR	physical	22939629
CDC42_HUMAN	CDC42	physical	24276241
ALDOA_HUMAN	ALDOA	physical	26344197
FA98B_HUMAN	FAM98B	physical	26344197
GDIA_HUMAN	GDI1	physical	26344197
HINT1_HUMAN	HINT1	physical	26344197
PEPL1_HUMAN	NPEPL1	physical	26344197
PDIA3_HUMAN	PDIA3	physical	26344197
PFKAM_HUMAN	PFKM	physical	26344197
PFKAP_HUMAN	PFKP	physical	26344197
RHOC_HUMAN	RHOC	physical	26344197
SUMO3_HUMAN	SUMO3	physical	26344197
SUMO4_HUMAN	SUMO4	physical	26344197
RHOA_HUMAN	RHOA	physical	14749388
STOM_HUMAN	STOM	physical	27173435
PRC2B_HUMAN	PRRC2B	physical	27173435
FBXW7_HUMAN	FBXW7	physical	28772241

Drug and Disease Associations

Kegg Disease
There are no disease associations of PTM sites.
OMIM Disease
615244	Nephrotic syndrome 8 (NPHS8)
Kegg Drug
There are no disease associations of PTM sites.
DrugBank
There are no disease associations of PTM sites.

Regulatory Network of GDIR1_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 ALA-2, 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-105; LYS-127; LYS-141 ANDLYS-178, AND MASS SPECTROMETRY.	19608861 [Abstract]
"Substrate and functional diversity of lysine acetylation revealed bya proteomics survey."; Kim S.C., Sprung R., Chen Y., Xu Y., Ball H., Pei J., Cheng T.,Kho Y., Xiao H., Xiao L., Grishin N.V., White M., Yang X.-J., Zhao Y.; Mol. Cell 23:607-618(2006). Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-141, AND MASS SPECTROMETRY.	16916647 [Abstract]