Home

RhoGDI alpha (human)

Overview RhoGDI alpha 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. Monomer. Forms a heterodimer with RAC1. Interacts with FER. Belongs to the Rho GDI family. Note: This description may include information from UniProtKB. Protein type: Apoptosis; Cell development/differentiation; G protein regulator, misc.; Cell adhesion; Motility/polarity/chemotaxis Cellular Component: cytoskeleton; immunological synapse; cytosol Molecular Function: protein binding; Rho GDP-dissociation inhibitor activity; GTPase activator activity Biological Process: regulation of small GTPase mediated signal transduction; regulation of protein localization; nerve growth factor receptor signaling pathway; small GTPase mediated signal transduction; positive regulation of axonogenesis; negative regulation of axonogenesis; negative regulation of cell adhesion; cell motility; regulation of axonogenesis; Rho protein signal transduction; negative regulation of apoptosis Reference #:  P52565 (UniProtKB) Alt. Names/Synonyms: ARHGDIA; GDIA1; GDIR1; MGC117248; Rho GDI 1; Rho GDP dissociation inhibitor (GDI) alpha; Rho GDP-dissociation inhibitor 1; Rho-GDI alpha; RHOGDI; RHOGDI-1 Gene Symbols: ARHGDIA Molecular weight: 23,207 Da Basal Isoelectric point: 5.03  Predict pI for various phosphorylation states Protein-Specific Antibodies or siRNAs from Cell Signaling Technology®

Select Structure to View Below RhoGDI alpha 1CC0 - E/F=1-204 (human) 1FSO - A=67-204 (human) 1FST - A/B=24-204 (human) 1FT0 - A/B=67-204 (human) 1FT3 - A/B=67-204 (human) 1HH4 - D/E=1-204 (human) 1KMT - A/B=67-204 (human) 1QVY - A/B/C/D=67-204 (human) 1RHO - A/B/C=59-203 (human) 2BXW - A/B=67-204 (human) 2JHS - A=67-202 (human) 2JHT - A/B/C/D=67-202 (human) 2JHU - A/B=67-202 (human) 2JHV - A/B/C/D/E/F=67-202 (human) 2JHW - A/B=67-202 (human) 2JHX - A/B=67-202 (human) 2JHY - A=67-202 (human) 2JHZ - A/B=67-202 (human) 2JI0 - A=67-202 (human)

STRING  |  Scansite  |  Phospho.ELM  |  NetworKIN  |  Pfam  |  RCSB PDB 1CC0 1FSO 1FST 1FT0 1FT3 1HH4 1KMT 1QVY 1RHO 2BXW 2JHS 2JHT 2JHU 2JHV 2JHW 2JHX 2JHY 2JHZ 2JI0  |  Phospho3D  |  DISEASE  |  Source  |  UCSD-Nature  |  GeneCards  |  UniProtKB  |  Entrez-Gene  |  Ensembl Gene

	Sites Implicated In
cell adhesion, altered: S34‑p cytoskeletal reorganization: K141‑a transcription, altered: S96‑p, S174‑p activation: S96‑p, S174‑p intracellular localization: Y156‑p molecular association, regulation: S34‑p, S101‑p, Y156‑p, S174‑p

	Modification Sites and Domains	Show Modification Legend
Click here to view phosphorylation modifications only

	Modification Sites in Parent Protein, Orthologs, and Isoforms	Show Modification Legend

SS  SS: The number of records in which this modification site was determined using site-specific methods. SS methods include amino acid sequencing, site-directed mutagenesis, modification site-specific antibodies, specific MS strategies, etc.	MS  MS: The number of records in which this modification site was assigned using ONLY proteomic discovery-mode mass spectrometry.			human ► Hide Isoforms
0	1		T7	_MAEQEPTAEQLAQI
0	5		S24-p	ENEEDEHsVNykPPA
1	49		Y27-p	EDEHsVNykPPAQKs
0	1		K28-a	DEHsVNykPPAQKsI
3	9		S34-p	ykPPAQKsIQEIQEL
0	1		K43-a	QEIQELDkDDEsLRK
0	2		S47-p	ELDkDDEsLRKykEA
0	1		K50	kDDEsLRKykEALLG
0	2		Y51-p	DDEsLRKykEALLGR
0	1		K52	DEsLRKyKEALLGRV
0	4		K52-u	DEsLRKykEALLGRV
2	0		S96-p	DLTGDLEsFKkQsFV
0	21		K98	TGDLEsFKkQsFVLk
0	7		K99	GDLEsFKKQsFVLkE
0	3		K99-u	GDLEsFKkQsFVLkE
3	3		S101-p	LEsFKkQsFVLkEGV
0	1		K105-a	KkQsFVLkEGVEYRI
0	1		R111	LkEGVEYRIKISFRV
0	1		K127-a	REIVSGMkYIQHtyR
0	2		K127-u	REIVSGMkYIQHtyR
0	4		T132-p	GMkYIQHtyRKGVKI
0	209		Y133-p	MkYIQHtyRKGVKID
0	1		K138	HtyRKGVKIDkTDyM
0	5		K141-a	RKGVKIDkTDyMVGS
0	25		K141-u	RKGVKIDkTDyMVGS
0	2		Y144-p	VKIDkTDyMVGSYGP
0	1		S148	kTDyMVGSYGPRAEE
0	1		R152	MVGSYGPRAEEyEFL
2	20		Y156-p	YGPRAEEyEFLTPVE
0	6		K167-u	TPVEEAPkGMLARGs
3	0		S174-p	kGMLARGsYSIkSRF
0	4		K178-a	ARGsYSIkSRFTDDD
0	1		R180	GsYSIkSRFTDDDKT
0	1		-	gap

	RhoGDI alpha iso3
T7	_MAEQEPTAEQLAQI
S24	ENEEDEHSVNYKPPA
Y27	EDEHSVNYKPPAQKS
K28	DEHSVNYKPPAQKSI
S34	YKPPAQKSIQEIQEL
K43	QEIQELDKDDESLRK
S47	ELDKDDESLRKYKEA
K50	KDDESLRKYKEALLG
Y51	DDESLRKYKEALLGR
K52	DESLRKYKEALLGRV
K52	DESLRKYKEALLGRV
S96	DLTGDLESFKKQSFV
K98	TGDLESFKKQSFVLK
K99	GDLESFKKQSFVLKE
K99	GDLESFKKQSFVLKE
S101	LESFKKQSFVLKEGV
K105	KKQSFVLKEGVEYRI
R111	LKEGVEYRIKISFRV
K127	REIVSGMKYIQHTYR
K127	REIVSGMKYIQHTYR
T132	GMKYIQHTYRKGVKI
Y133	MKYIQHTYRKGVKID
K138	HTYRKGVKIDKTDYM
K141	RKGVKIDKTDYMVGS
K141	RKGVKIDKTDYMVGS
Y144	VKIDKTDYMVGSYGP
S148	KTDYMVGSYGPRAEE
R152	MVGSYGPRAEEYEFL
Y156	YGPRAEEYEFLTPVE
K167	TPVEEAPKGSISPsH
-	gap
-	gap
-	gap
S173-p	PKGSISPsHPRPGFR

	mouse
T7-p	_MAEQEPtAEQLAQI
S24-p	ENEEDEHsVNYKPPA
Y27	EDEHsVNYKPPAQKs
K28	DEHsVNYKPPAQKsI
S34-p	YKPPAQKsIQEIQEL
K43	QEIQELDKDDEsLRK
S47-p	ELDKDDEsLRKYKEA
K50	KDDEsLRKYKEALLG
Y51	DDEsLRKYKEALLGR
K52	DEsLRKYKEALLGRV
K52	DEsLRKYKEALLGRV
S96-p	DLTGDLEsFkkQsFV
K98-a	TGDLEsFkkQsFVLK
K99-a	GDLEsFkkQsFVLKE
K99	GDLEsFkKQsFVLKE
S101-p	LEsFkkQsFVLKEGV
K105	kkQsFVLKEGVEYRI
R111	LKEGVEYRIKISFRV
K127	REIVSGMKYIQHtyR
K127-u	REIVSGMkYIQHtyR
T132-p	GMkYIQHtyRKGVkI
Y133-p	MkYIQHtyRKGVkID
K138-u	HtyRKGVkIDkTDYM
K141-a	RKGVkIDkTDYMVGS
K141-u	RKGVkIDkTDYMVGS
Y144	VkIDkTDYMVGSYGP
S148	kTDYMVGSYGPRAEE
R152	MVGSYGPRAEEYEFL
Y156	YGPRAEEYEFLTPME
K167-u	TPMEEAPkGMLARGS
S174	kGMLARGSYNIKSRF
K178	ARGSYNIKSRFTDDD
R180	GSYNIKSRFTDDDKT
-	gap

	rat
T7	_MAEQEPTAEQLAQI
S24	ENEEDEHSVNYKPPA
Y27	EDEHSVNYKPPAQKs
K28	DEHSVNYKPPAQKsI
S34-p	YKPPAQKsIQEIQEL
K43	QEIQELDKDDESLRk
S47	ELDKDDESLRkYkEA
K50-m2	KDDESLRkYkEALLG
Y51	DDESLRkYkEALLGR
K52-m2	DESLRkYkEALLGRV
K52	DESLRkYKEALLGRV
S96	DLTGDLESFKKQsFV
K98	TGDLESFKKQsFVLK
K99	GDLESFKKQsFVLKE
K99	GDLESFKKQsFVLKE
S101-p	LESFKKQsFVLKEGV
K105	KKQsFVLKEGVEYrI
R111-m2	LKEGVEYrIKISFRV
K127	REIVSGMKYIQHTyR
K127	REIVSGMKYIQHTyR
T132	GMKYIQHTyRKGVKI
Y133-p	MKYIQHTyRKGVKID
K138	HTyRKGVKIDkTDyM
K141	RKGVKIDKTDyMVGs
K141-u	RKGVKIDkTDyMVGs
Y144-p	VKIDkTDyMVGsYGP
S148-p	kTDyMVGsYGPrAEE
R152-m2	MVGsYGPrAEEYEFL
Y156	YGPrAEEYEFLTPME
K167	TPMEEAPKGMLARGS
S174	KGMLARGSYNIKSrF
K178	ARGSYNIKSrFTDDD
R180-m2	GSYNIKSrFTDDDKT
-	gap

Home  |  Curator Login With enhanced literature mining using Linguamatics I2E Produced by 3rd Millennium  |  Design by Digizyme ©2003-2013 Cell Signaling Technology, Inc.