GDIR1_RAT - dbPTM
GDIR1_RAT - PTM Information in dbPTM
Basic Information of Protein
UniProt ID GDIR1_RAT
UniProt AC Q5XI73
Protein Name Rho GDP-dissociation inhibitor 1 {ECO:0000250|UniProtKB:P19803}
Gene Name Arhgdia {ECO:0000312|RGD:1359547}
Organism Rattus norvegicus (Rat).
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 MAEQEPTAEQLAQIAAENEEDEHSVNYKPPAQKSIQEIQELDKDDESLRKYKEALLGRVAVSADPNVPNVIVTRLTLVCSTAPGPLELDLTGDLESFKKQSFVLKEGVEYRIKISFRVNREIVSGMKYIQHTYRKGVKIDKTDYMVGSYGPRAEEYEFLTPMEEAPKGMLARGSYNIKSRFTDDDKTDHLSWEWNLTIKKEWKD
Overview of Protein Modification Sites with Functional and Structural Information
Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations Modification Substrate Peptides
&
Secondary Structure
ASA (%) Reference Orthologous
Protein Cluster
2Acetylation------MAEQEPTAE
------CCCCCCCHH
27.46-
7Phosphorylation-MAEQEPTAEQLAQI
-CCCCCCCHHHHHHH
41.9123984901
24PhosphorylationENEEDEHSVNYKPPA
HCCCCCCCCCCCCCC
15.2627097102
27PhosphorylationEDEHSVNYKPPAQKS
CCCCCCCCCCCCHHH
23.7923984901
28AcetylationDEHSVNYKPPAQKSI
CCCCCCCCCCCHHHH
39.0422902405
34PhosphorylationYKPPAQKSIQEIQEL
CCCCCHHHHHHHHHH
19.8820472934
43SuccinylationQEIQELDKDDESLRK
HHHHHHCCCCHHHHH
78.6326843850
43AcetylationQEIQELDKDDESLRK
HHHHHHCCCCHHHHH
78.6322902405
47PhosphorylationELDKDDESLRKYKEA
HHCCCCHHHHHHHHH
40.2325532521
50MethylationKDDESLRKYKEALLG
CCCHHHHHHHHHHHH
67.00-
50"N6,N6-dimethyllysine"KDDESLRKYKEALLG
CCCHHHHHHHHHHHH
67.00-
52"N6,N6-dimethyllysine"DESLRKYKEALLGRV
CHHHHHHHHHHHHCE
39.28-
52MethylationDESLRKYKEALLGRV
CHHHHHHHHHHHHCE
39.28-
52AcetylationDESLRKYKEALLGRV
CHHHHHHHHHHHHCE
39.2822902405
62PhosphorylationLLGRVAVSADPNVPN
HHHCEECCCCCCCCC
19.7429779826
99AcetylationGDLESFKKQSFVLKE
CCHHHHHHEEEEEEC
49.5222902405
101PhosphorylationLESFKKQSFVLKEGV
HHHHHHEEEEEECCE
26.6319103160
105AcetylationKKQSFVLKEGVEYRI
HHEEEEEECCEEEEE
47.3122902405
111MethylationLKEGVEYRIKISFRV
EECCEEEEEEEEEEE
15.37166183
111DimethylationLKEGVEYRIKISFRV
EECCEEEEEEEEEEE
15.37-
113AcetylationEGVEYRIKISFRVNR
CCEEEEEEEEEEECH
24.2522902405
127AcetylationREIVSGMKYIQHTYR
HHHHCCCCHHHHHHC
42.6022902405
133PhosphorylationMKYIQHTYRKGVKID
CCHHHHHHCCCCCCC
14.27-
138AcetylationHTYRKGVKIDKTDYM
HHHCCCCCCCCCCCC
54.5822902405
141UbiquitinationRKGVKIDKTDYMVGS
CCCCCCCCCCCCCCC
46.93-
141SuccinylationRKGVKIDKTDYMVGS
CCCCCCCCCCCCCCC
46.93-
141AcetylationRKGVKIDKTDYMVGS
CCCCCCCCCCCCCCC
46.9322902405
141SuccinylationRKGVKIDKTDYMVGS
CCCCCCCCCCCCCCC
46.93-
144PhosphorylationVKIDKTDYMVGSYGP
CCCCCCCCCCCCCCC
10.0322817900
148PhosphorylationKTDYMVGSYGPRAEE
CCCCCCCCCCCCHHH
18.5922817900
149PhosphorylationTDYMVGSYGPRAEEY
CCCCCCCCCCCHHHE
25.8125575281
152MethylationMVGSYGPRAEEYEFL
CCCCCCCCHHHEEEE
50.71166189
152DimethylationMVGSYGPRAEEYEFL
CCCCCCCCHHHEEEE
50.71-
160PhosphorylationAEEYEFLTPMEEAPK
HHHEEEECCHHHCCC
26.3823984901
167AcetylationTPMEEAPKGMLARGS
CCHHHCCCCCCCCCC
65.0922902405
174PhosphorylationKGMLARGSYNIKSRF
CCCCCCCCEECCCCC
14.9530181290
178AcetylationARGSYNIKSRFTDDD
CCCCEECCCCCCCCC
31.7625786129
180DimethylationGSYNIKSRFTDDDKT
CCEECCCCCCCCCCC
33.22-
180MethylationGSYNIKSRFTDDDKT
CCEECCCCCCCCCCC
33.22166195

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
34SPhosphorylationKinasePAK2Q13177
PSP
101SPhosphorylationKinasePAK2Q13177
PSP

Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of GDIR1_RAT !!

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_RAT !!

Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions

Oops, there are no PPI records of GDIR1_RAT !!

Drug and Disease Associations
Kegg Drug
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of GDIR1_RAT

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Related Literatures of Post-Translational Modification

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