Basic Information | Overview of PTM Sites | Experimental PTM Sites | Protein-Protein Interactions | Drug and Disease Associations | Related Literatures
Basic Information
Protein Name :  Rho GDP-dissociation inhibitor 1  

UniProtKB / Swiss-Prot ID :  GDIR1_HUMAN

Gene Name (Synonyms) : 
ARHGDIA, GDIA1  

Species :  Homo sapiens (Human). 

Subcellular Localization :  Cytoplasm. 

Protein Function :  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 (By similarity). 

Protein Sequence MAEQEPTAEQLAQIAAENEEDEHSVNYKPPAQKSIQEIQELDKDDESLRKYKEALLGRVAVSADPNVPNV...
Predicted Secondary Structure  -
Protein Variant -
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Overview of Protein Modification Sites with Functional and Structural Information
Accessible Surface Area (ASA)
Pred. Secondary
Real Secondary
Disorder Prediction
Protein Domain
&
Experimental PTM Sites
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Experimental Post-Translational Modification Sites Download
Locations
Modification
Substrate Sites
&
Secondary Structure
Accessible Surface Area (%)
Resource
Reference
Structural Characterization
Orthologous
Protein Cluster
2N-acetylalanine.---MAEQEP
---
27.46UniProtKB
Link-
24PhosphoserineEDEHSVNYK
15.26HPRD
Link
24PhosphoserineEDEHSVNYK
15.26Phosphositeplus
Link
27PhosphotyrosineHSVNYKPPA
23.79Phosphositeplus
Link
34PhosphoserinePAQKSIQEI
19.88HPRD
Link
34PhosphoserinePAQKSIQEI
19.88Phosphositeplus
Link
96PhosphoserineGDLESFKKQ
50.06Phosphositeplus
Link
99Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)ESFKKQSFV
49.52Phosphositeplus
Link
101PhosphoserineFKKQSFVLK
26.63Phosphositeplus
Link
101Phosphoserine (PAK1)FKKQSFVLK
26.63PhosphoELM
Link
105N6-acetyllysineSFVLKEGVE
47.31HPRD
Link
105N6-acetyllysineSFVLKEGVE
47.31Phosphositeplus
Link
105N6-acetyllysine.SFVLKEGVE
47.31UniProtKB
Link
127Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)VSGMKYIQH
42.60Phosphositeplus
Link
127N6-acetyllysineVSGMKYIQH
42.60HPRD
Link
127N6-acetyllysineVSGMKYIQH
42.60Phosphositeplus
Link
127N6-acetyllysine.VSGMKYIQH
42.60UniProtKB
Link
133PhosphotyrosineIQHTYRKGV
14.27Phosphositeplus
Link
141Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)VKIDKTDYM
46.93Phosphositeplus
Link
141N6-acetyllysineVKIDKTDYM
46.93HPRD
Link
141N6-acetyllysineVKIDKTDYM
46.93Phosphositeplus
Link
141N6-acetyllysineVKIDKTDYM
46.93SysPTM
Link
141N6-acetyllysine.VKIDKTDYM
46.93UniProtKB
Link
156PhosphotyrosineRAEEYEFLT
11.95Phosphositeplus
Link
167Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)EEAPKGMLA
65.09Phosphositeplus
Link
174PhosphoserineLARGSYSIK
15.34Phosphositeplus
Link
174Phosphoserine (PAK1)LARGSYSIK
15.34PhosphoELM
Link
178N6-acetyllysineSYSIKSRFT
29.64HPRD
Link
178N6-acetyllysineSYSIKSRFT
29.64Phosphositeplus
Link
178N6-acetyllysine.SYSIKSRFT
29.64UniProtKB
Link
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Protein-Protein Interactions
      Interacting Protein      
Interaction type
Source ID
      Resource      
      Pubmed ID      
Domain-Domain Interactions
PLAK_HUMANphysical interactionMINT-63856MINT16169070
RADI_HUMANphysical interactionMINT-18848MINT9681826
RADI_HUMANphysical interactionMINT-18849MINT9681826
SET_HUMANphysical interactionMINT-4298468MINT17245428
NED4L_HUMANphysical interactionMINT-63860MINT16169070
SH3G3_HUMANphysical interactionMINT-63861MINT16169070
Q9HAA9_HUMANphysical interactionMINT-63862MINT16169070
Q6FI97_HUMANphysical interactionEBI-733861
intact16169070
CDN1B_HUMANphysical interactionEBI-733864
intact16169070
NED4L_HUMANphysical interactionEBI-733867
intact16169070
Q6IBE6_HUMANphysical interactionEBI-736295
intact16169070
PLAK_HUMANphysical interactionEBI-731215
intact16169070
FEN1_HUMANphysical interactionEBI-729528
intact16169070
RHOA_HUMANdirect interaction
physical interaction
EBI-1028216
EBI-1061466
intact10489445
17353931
CDC42_HUMANphysical interactionEBI-1061260
intact17353931
RHOC_HUMANphysical interactionEBI-1061332
intact17353931
EI2BA_HUMANphysical interaction
physical interaction
EBI-1061419
EBI-1075768
intact17353931
17353931
ROAA_HUMANphysical interactionEBI-1083034
intact17353931
FUS_HUMANphysical interactionEBI-1075895
intact17353931
EWS_HUMANphysical interactionEBI-1076238
intact17353931
ROA3_HUMANphysical interactionEBI-1085940
intact17353931
IF2B1_HUMANphysical interactionEBI-1084000
intact17353931
GDIR1_HUMANphysical interactionEBI-1085674
intact17353931
CDC42_HUMANin vitroHPRD:03565HPRD10676816
RHOA_HUMANin vivoHPRD:03565HPRD11149925
RADI_HUMANin vitro
in vivo
HPRD:03565HPRD9287351
9681826
RAC2_HUMANin vitroHPRD:03565HPRD11513578
VAV_HUMANin vitroHPRD:03565HPRD10664460
GDIR1_HUMANin vitroHPRD:03565HPRD11320308
9195882
SIA4C_HUMANyeast 2-hybridHPRD:03565HPRD16169070
PLAK_HUMANyeast 2-hybridHPRD:03565HPRD16169070
CDN1B_HUMANyeast 2-hybridHPRD:03565HPRD16169070
SH3G3_HUMANyeast 2-hybridHPRD:03565HPRD16169070
NED4L_HUMANyeast 2-hybridHPRD:03565HPRD16169070
RHOQ_HUMANENSP00000269321STRING
CDN1A_HUMANENSP00000269321STRING
RAC2_HUMANENSP00000269321STRING
RHBT2_HUMANENSP00000269321STRING
RHOF_HUMANENSP00000269321STRING
RHOB_HUMANENSP00000269321STRING
RAC3_HUMANENSP00000269321STRING
RHOD_HUMANENSP00000269321STRING
CDC42_HUMANENSP00000269321STRING
RHOJ_HUMANENSP00000269321STRING
MIRO2_HUMANENSP00000269321STRING
RHOG_HUMANENSP00000269321STRING
RADI_HUMANENSP00000269321STRING
RHOC_HUMANENSP00000269321STRING
RHBT1_HUMANENSP00000269321STRING
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Disease Reference
Kegg disease
OMIM disease
615244Nephrotic syndrome 8 (NPHS8)
Drug Reference
There are no disease associations of PTM sites.
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Related Literatures of Post-Translational Modification
Acetylation
ReferencePubMed
"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.
"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.
"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.
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Basic Information | Overview of PTM Sites | Experimental PTM Sites | Protein-Protein Interactions | Drug and Disease Associations | Related Literatures