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Protein Page:
RhoGDI alpha (human)
p Phosphorylation
ac Acetylation
me Methylation
m1 Mono-methylation
m2 Di-methylation
m3 Tri-methylation
ub Ubiquitination
sm Sumoylation
ne Neddylation
gl O-GlcNAc
ga O-GalNAc
pa Palmitoylation
ad Adenylylation
sn S-Nitrosylation
ca Caspase cleavage
sc Succinylation

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; G protein regulator, misc.; Cell adhesion; Cell development/differentiation; Motility/polarity/chemotaxis
Cellular Component: cytoskeleton; immunological synapse; cytosol
Molecular Function: protein binding; Rho GDP-dissociation inhibitor activity; GTPase activator activity
Biological Process: nerve growth factor receptor signaling pathway; negative regulation of cell adhesion; regulation of axonogenesis; Rho protein signal transduction; regulation of small GTPase mediated signal transduction; regulation of protein localization; regulation of catalytic activity; small GTPase mediated signal transduction; positive regulation of axonogenesis; negative regulation of axonogenesis; cell motility; positive regulation of GTPase activity; 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® Total Proteins
Select Structure to View Below

RhoGDI alpha

Protein Structure Not Found.


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Sites Implicated In
cell adhesion, altered: S34‑p
cytoskeletal reorganization: K141‑ac
transcription, altered: S96‑p, S174‑p
activity, induced: 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
 

Show Multiple Sequence Alignment


 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 6 S24-p ENEEDEHsVNykPPA
1 48 Y27-p EDEHsVNykPPAQKs
0 2 K28-ac DEHsVNykPPAQKsI
4 11 S34-p ykPPAQKsIQEIQEL
0 2 K43-ac QEIQELDkDDEsLRK
0 1 K43-sc QEIQELDkDDEsLRK
0 3 S47-p ELDkDDEsLRKykEA
0 1 K50 kDDEsLRKykEALLG
0 2 Y51-p DDEsLRKykEALLGR
0 1 K52 DEsLRKyKEALLGRV
0 4 K52-ub DEsLRKykEALLGRV
3 0 S96-p DLTGDLEsFKkQsFV
0 21 K98 TGDLEsFKkQsFVLk
0 7 K99 GDLEsFKKQsFVLkE
0 3 K99-ub GDLEsFKkQsFVLkE
4 5 S101-p LEsFKkQsFVLkEGV
0 1 K105-ac KkQsFVLkEGVEYRI
0 1 K105-sc KkQsFVLkEGVEYRI
0 1 R111 LkEGVEYRIKISFRV
0 2 K127-ac REIVSGMkYIQHtyR
0 2 K127-ub REIVSGMkYIQHtyR
0 4 T132-p GMkYIQHtyRKGVkI
0 212 Y133-p MkYIQHtyRKGVkID
1 0 K138-sm HtyRKGVkIDkTDYM
0 1 K138 HtyRKGVKIDkTDYM
0 6 K141-ac RKGVkIDkTDYMVGS
0 25 K141-ub RKGVkIDkTDYMVGS
0 1 Y144 VkIDkTDYMVGSYGP
0 1 S148 kTDYMVGSYGPRAEE
0 1 R152 MVGSYGPRAEEyEFL
2 19 Y156-p YGPRAEEyEFLTPVE
0 1 K167-ac TPVEEAPkGMLARGs
0 6 K167-ub TPVEEAPkGMLARGs
4 0 S174-p kGMLARGsYSIkSRF
0 4 K178-ac ARGsYSIkSRFTDDD
0 1 K178-sc ARGsYSIkSRFTDDD
0 1 R180 GsYSIkSRFTDDDKT
0 1 - gap
  RhoGDI alpha iso3  
T7 _MAEQEPTAEQLAQI
S24 ENEEDEHSVNYKPPA
Y27 EDEHSVNYKPPAQKS
K28 DEHSVNYKPPAQKSI
S34 YKPPAQKSIQEIQEL
K43 QEIQELDKDDESLRK
K43 QEIQELDKDDESLRK
S47 ELDKDDESLRKYKEA
K50 KDDESLRKYKEALLG
Y51 DDESLRKYKEALLGR
K52 DESLRKYKEALLGRV
K52 DESLRKYKEALLGRV
S96 DLTGDLESFKKQSFV
K98 TGDLESFKKQSFVLK
K99 GDLESFKKQSFVLKE
K99 GDLESFKKQSFVLKE
S101 LESFKKQSFVLKEGV
K105 KKQSFVLKEGVEYRI
K105 KKQSFVLKEGVEYRI
R111 LKEGVEYRIKISFRV
K127 REIVSGMKYIQHTYR
K127 REIVSGMKYIQHTYR
T132 GMKYIQHTYRKGVKI
Y133 MKYIQHTYRKGVKID
K138 HTYRKGVKIDKTDYM
K138 HTYRKGVKIDKTDYM
K141 RKGVKIDKTDYMVGS
K141 RKGVKIDKTDYMVGS
Y144 VKIDKTDYMVGSYGP
S148 KTDYMVGSYGPRAEE
R152 MVGSYGPRAEEYEFL
Y156 YGPRAEEYEFLTPVE
K167 TPVEEAPKGSISPsH
K167 TPVEEAPKGSISPsH
- gap
- gap
D209 RGGAGVWDARPRGGR
- gap
S173-p PKGSISPsHPRPGFR
  mouse

 
T7-p _MAEQEPtAEQLAQI
S24-p ENEEDEHsVNYKPPA
Y27 EDEHsVNYKPPAQKs
K28 DEHsVNYKPPAQKsI
S34-p YKPPAQKsIQEIQEL
K43-ac QEIQELDkDDEsLRK
K43 QEIQELDKDDEsLRK
S47-p ELDkDDEsLRKYKEA
K50 kDDEsLRKYKEALLG
Y51 DDEsLRKYKEALLGR
K52 DEsLRKYKEALLGRV
K52 DEsLRKYKEALLGRV
S96-p DLTGDLEsFkkQsFV
K98-ac TGDLEsFkkQsFVLk
K99-ac GDLEsFkkQsFVLkE
K99 GDLEsFkKQsFVLkE
S101-p LEsFkkQsFVLkEGV
K105 kkQsFVLKEGVEYRI
K105-sc kkQsFVLkEGVEYRI
R111 LkEGVEYRIKISFRV
K127-ac REIVSGMkYIQHtyR
K127-ub REIVSGMkYIQHtyR
T132-p GMkYIQHtyRKGVkI
Y133-p MkYIQHtyRKGVkID
K138 HtyRKGVKIDkTDYM
K138-ub HtyRKGVkIDkTDYM
K141-ac RKGVkIDkTDYMVGS
K141-ub RKGVkIDkTDYMVGS
Y144 VkIDkTDYMVGSYGP
S148 kTDYMVGSYGPRAEE
R152 MVGSYGPRAEEYEFL
Y156 YGPRAEEYEFLTPME
K167-ac TPMEEAPkGMLARGS
K167-ub TPMEEAPkGMLARGS
S174 kGMLARGSYNIkSRF
K178 ARGSYNIKSRFTDDD
K178-sc ARGSYNIkSRFTDDD
R180 GSYNIkSRFTDDDKT
- gap
  rat

 
T7 _MAEQEPTAEQLAQI
S24 ENEEDEHSVNYKPPA
Y27 EDEHSVNYKPPAQKs
K28 DEHSVNYKPPAQKsI
S34-p YKPPAQKsIQEIQEL
K43 QEIQELDKDDESLRk
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
K105 KKQsFVLKEGVEYrI
R111-m2 LKEGVEYrIKISFRV
K127 REIVSGMKYIQHTyR
K127 REIVSGMKYIQHTyR
T132 GMKYIQHTyRKGVKI
Y133-p MKYIQHTyRKGVKID
K138 HTyRKGVKIDkTDyM
K138 HTyRKGVKIDkTDyM
K141 RKGVKIDKTDyMVGs
K141-ub RKGVKIDkTDyMVGs
Y144-p VKIDkTDyMVGsYGP
S148-p kTDyMVGsYGPrAEE
R152-m2 MVGsYGPrAEEYEFL
Y156 YGPrAEEYEFLTPME
K167 TPMEEAPKGMLARGS
K167 TPMEEAPKGMLARGS
S174 KGMLARGSYNIKSrF
K178 ARGSYNIKSrFTDDD
K178 ARGSYNIKSrFTDDD
R180-m2 GSYNIKSrFTDDDKT
- gap
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