dbPTM

GDIR2_HUMAN - PTM Information in dbPTM

Basic Information of Protein

Overview of Protein Modification Sites with Functional and Structural Information
UniProt ID	GDIR2_HUMAN
UniProt AC	P52566
Protein Name	Rho GDP-dissociation inhibitor 2
Gene Name	ARHGDIB
Organism	Homo sapiens (Human).
Sequence Length	201
Subcellular Localization	Cytoplasm, cytosol .
Protein Description	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. [PubMed: 8356058]
Protein Sequence	MTEKAPEPHVEEDDDDELDSKLNYKPPPQKSLKELQEMDKDDESLIKYKKTLLGDGPVVTDPKAPNVVVTRLTLVCESAPGPITMDLTGDLEALKKETIVLKEGSEYRVKIHFKVNRDIVSGLKYVQHTYRTGVKVDKATFMVGSYGPRPEEYEFLTPVEEAPKGMLARGTYHNKSFFTDDDKQDHLSWEWNLSIKKEWTE

Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations	Modification	Substrate Peptides & Secondary Structure	ASA (%)	Reference
2	Acetylation	------MTEKAPEPH ------CCCCCCCCC	46.31	-
2	Phosphorylation	------MTEKAPEPH ------CCCCCCCCC	46.31	26074081
4	Acetylation	----MTEKAPEPHVE ----CCCCCCCCCCC	61.14	25953088
4	Ubiquitination	----MTEKAPEPHVE ----CCCCCCCCCCC	61.14	-
20	Phosphorylation	DDDDELDSKLNYKPP CCCCCCHHHCCCCCC	52.22	28787133
21	Acetylation	DDDELDSKLNYKPPP CCCCCHHHCCCCCCC	40.18	19608861
21	Ubiquitination	DDDELDSKLNYKPPP CCCCCHHHCCCCCCC	40.18	19608861
24	Nitration	ELDSKLNYKPPPQKS CCHHHCCCCCCCCHH	35.00	-
24	Phosphorylation	ELDSKLNYKPPPQKS CCHHHCCCCCCCCHH	35.00	19321744
25	Acetylation	LDSKLNYKPPPQKSL CHHHCCCCCCCCHHH	50.39	19608861
25	Ubiquitination	LDSKLNYKPPPQKSL CHHHCCCCCCCCHHH	50.39	19608861
30	Acetylation	NYKPPPQKSLKELQE CCCCCCCHHHHHHHH	64.63	23749302
30	Ubiquitination	NYKPPPQKSLKELQE CCCCCCCHHHHHHHH	64.63	19608861
31	Phosphorylation	YKPPPQKSLKELQEM CCCCCCHHHHHHHHC	39.15	29978859
33	Ubiquitination	PPPQKSLKELQEMDK CCCCHHHHHHHHCCC	64.57	-
33	Acetylation	PPPQKSLKELQEMDK CCCCHHHHHHHHCCC	64.57	23749302
38	Sulfoxidation	SLKELQEMDKDDESL HHHHHHHCCCCCHHH	5.11	28465586
40	Ubiquitination	KELQEMDKDDESLIK HHHHHCCCCCHHHHH	66.81	19608861
40	Acetylation	KELQEMDKDDESLIK HHHHHCCCCCHHHHH	66.81	19608861
44	Phosphorylation	EMDKDDESLIKYKKT HCCCCCHHHHHHHHH	42.25	28348404
47	Ubiquitination	KDDESLIKYKKTLLG CCCHHHHHHHHHHHC	57.20	19608861
47	Acetylation	KDDESLIKYKKTLLG CCCHHHHHHHHHHHC	57.20	19608861
48	Phosphorylation	DDESLIKYKKTLLGD CCHHHHHHHHHHHCC	15.66	29978859
49	Ubiquitination	DESLIKYKKTLLGDG CHHHHHHHHHHHCCC	33.99	-
50	Ubiquitination	ESLIKYKKTLLGDGP HHHHHHHHHHHCCCC	41.12	21890473
50	Ubiquitination	ESLIKYKKTLLGDGP HHHHHHHHHHHCCCC	41.12	21890473
51	Phosphorylation	SLIKYKKTLLGDGPV HHHHHHHHHHCCCCC	24.06	23911959
60	Phosphorylation	LGDGPVVTDPKAPNV HCCCCCCCCCCCCCE	46.98	23911959
63	Acetylation	GPVVTDPKAPNVVVT CCCCCCCCCCCEEEE	78.33	23749302
63	Ubiquitination	GPVVTDPKAPNVVVT CCCCCCCCCCCEEEE	78.33	-
70	O-linked_Glycosylation	KAPNVVVTRLTLVCE CCCCEEEEEEEEEEE	14.35	30379171
73	Phosphorylation	NVVVTRLTLVCESAP CEEEEEEEEEEECCC	17.54	28122231
73	O-linked_Glycosylation	NVVVTRLTLVCESAP CEEEEEEEEEEECCC	17.54	30379171
76	S-nitrosylation	VTRLTLVCESAPGPI EEEEEEEEECCCCCE	3.73	25040305
78	Phosphorylation	RLTLVCESAPGPITM EEEEEEECCCCCEEE	34.34	28122231
95	Ubiquitination	TGDLEALKKETIVLK CCCHHHHHHCEEEEE	56.46	-
95	Acetylation	TGDLEALKKETIVLK CCCHHHHHHCEEEEE	56.46	26822725
96	Ubiquitination	GDLEALKKETIVLKE CCHHHHHHCEEEEEC	62.02	-
102	Ubiquitination	KKETIVLKEGSEYRV HHCEEEEECCCEEEE	49.49	19608861
102	Acetylation	KKETIVLKEGSEYRV HHCEEEEECCCEEEE	49.49	19608861
110	Ubiquitination	EGSEYRVKIHFKVNR CCCEEEEEEEEEECC	22.82	-
114	Ubiquitination	YRVKIHFKVNRDIVS EEEEEEEEECCHHHH	25.16	-
114	Acetylation	YRVKIHFKVNRDIVS EEEEEEEEECCHHHH	25.16	25953088
124	Ubiquitination	RDIVSGLKYVQHTYR CHHHHHCEEEEEECC	47.07	21890473
124	Ubiquitination	RDIVSGLKYVQHTYR CHHHHHCEEEEEECC	47.07	21906983
124	Acetylation	RDIVSGLKYVQHTYR CHHHHHCEEEEEECC	47.07	19608861
125	Phosphorylation	DIVSGLKYVQHTYRT HHHHHCEEEEEECCC	15.47	23882029
129	Phosphorylation	GLKYVQHTYRTGVKV HCEEEEEECCCCCEE	9.52	28176486
130	Phosphorylation	LKYVQHTYRTGVKVD CEEEEEECCCCCEEC	12.21	28176486
132	Phosphorylation	YVQHTYRTGVKVDKA EEEEECCCCCEECEE	35.59	27080861
135	Acetylation	HTYRTGVKVDKATFM EECCCCCEECEEEEE	46.17	23749302
135	Ubiquitination	HTYRTGVKVDKATFM EECCCCCEECEEEEE	46.17	-
138	Acetylation	RTGVKVDKATFMVGS CCCCEECEEEEEEEC	52.92	23749302
138	Ubiquitination	RTGVKVDKATFMVGS CCCCEECEEEEEEEC	52.92	-
140	Phosphorylation	GVKVDKATFMVGSYG CCEECEEEEEEECCC	20.29	28464451
145	Phosphorylation	KATFMVGSYGPRPEE EEEEEEECCCCCHHH	18.59	22617229
146	Phosphorylation	ATFMVGSYGPRPEEY EEEEEECCCCCHHHC	25.81	22115753
153	Phosphorylation	YGPRPEEYEFLTPVE CCCCHHHCEEEEEHH	15.43	19321744
157	Phosphorylation	PEEYEFLTPVEEAPK HHHCEEEEEHHHCCC	30.52	30108239
164	Ubiquitination	TPVEEAPKGMLARGT EEHHHCCCCCCCCCC	65.09	21890473
175	Ubiquitination	ARGTYHNKSFFTDDD CCCCCCCCCCCCCCC	35.01	19608861
175	Acetylation	ARGTYHNKSFFTDDD CCCCCCCCCCCCCCC	35.01	19608861
179	Phosphorylation	YHNKSFFTDDDKQDH CCCCCCCCCCCCCCC	36.19	-
194	Phosphorylation	LSWEWNLSIKKEWTE CEEEEEEEEEECCCC	29.20	27251275
196	Acetylation	WEWNLSIKKEWTE-- EEEEEEEEECCCC--	41.06	25953088
197	Acetylation	EWNLSIKKEWTE--- EEEEEEEECCCC---	57.73	11921139

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
24	Y	Phosphorylation	Kinase	SYK	P43405	PSP
24	Y	Phosphorylation	Kinase	SRC	P12931	PSP
31	S	Phosphorylation	Kinase	PRKCA	P17252	GPS
130	Y	Phosphorylation	Kinase	ABL	P00519	PSP
153	Y	Phosphorylation	Kinase	SRC	P12931	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 GDIR2_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 GDIR2_HUMAN !!

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference
VAV_HUMAN	VAV1	physical	10664460
A4_HUMAN	APP	physical	21832049
RHOC_HUMAN	RHOC	physical	26344197
SUMO4_HUMAN	SUMO4	physical	26344197
WSB1_HUMAN	WSB1	physical	26424695
FBXL5_HUMAN	FBXL5	physical	27383304

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 GDIR2_HUMAN

Related Literatures of Post-Translational Modification

Acetylation
Reference	PubMed
"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-21; LYS-25; LYS-40; LYS-47;LYS-102; LYS-124 AND LYS-175, AND MASS SPECTROMETRY.	19608861 [Abstract]
Phosphorylation
Reference	PubMed
"Quantitative phosphoproteomic analysis of T cell receptor signalingreveals system-wide modulation of protein-protein interactions."; Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K.,Rodionov V., Han D.K.; Sci. Signal. 2:RA46-RA46(2009). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-145, AND MASSSPECTROMETRY.	19690332 [Abstract]
"Immunoaffinity profiling of tyrosine phosphorylation in cancercells."; Rush J., Moritz A., Lee K.A., Guo A., Goss V.L., Spek E.J., Zhang H.,Zha X.-M., Polakiewicz R.D., Comb M.J.; Nat. Biotechnol. 23:94-101(2005). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-24, AND MASSSPECTROMETRY.	15592455 [Abstract]