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 | ||
* ASA = Accessible Surface Area
Locations | Modification | Substrate Peptides & Secondary Structure |
ASA (%) | Reference | Orthologous Protein Cluster |
---|---|---|---|---|---|
2 | Acetylation | ------MAEQEPTAE ------CCCCCCCHH | 27.46 | - | |
7 | Phosphorylation | -MAEQEPTAEQLAQI -CCCCCCCHHHHHHH | 41.91 | 23984901 | |
24 | Phosphorylation | ENEEDEHSVNYKPPA HCCCCCCCCCCCCCC | 15.26 | 27097102 | |
27 | Phosphorylation | EDEHSVNYKPPAQKS CCCCCCCCCCCCHHH | 23.79 | 23984901 | |
28 | Acetylation | DEHSVNYKPPAQKSI CCCCCCCCCCCHHHH | 39.04 | 22902405 | |
34 | Phosphorylation | YKPPAQKSIQEIQEL CCCCCHHHHHHHHHH | 19.88 | 20472934 | |
43 | Succinylation | QEIQELDKDDESLRK HHHHHHCCCCHHHHH | 78.63 | 26843850 | |
43 | Acetylation | QEIQELDKDDESLRK HHHHHHCCCCHHHHH | 78.63 | 22902405 | |
47 | Phosphorylation | ELDKDDESLRKYKEA HHCCCCHHHHHHHHH | 40.23 | 25532521 | |
50 | Methylation | KDDESLRKYKEALLG CCCHHHHHHHHHHHH | 67.00 | - | |
50 | "N6,N6-dimethyllysine" | KDDESLRKYKEALLG CCCHHHHHHHHHHHH | 67.00 | - | |
52 | "N6,N6-dimethyllysine" | DESLRKYKEALLGRV CHHHHHHHHHHHHCE | 39.28 | - | |
52 | Methylation | DESLRKYKEALLGRV CHHHHHHHHHHHHCE | 39.28 | - | |
52 | Acetylation | DESLRKYKEALLGRV CHHHHHHHHHHHHCE | 39.28 | 22902405 | |
62 | Phosphorylation | LLGRVAVSADPNVPN HHHCEECCCCCCCCC | 19.74 | 29779826 | |
99 | Acetylation | GDLESFKKQSFVLKE CCHHHHHHEEEEEEC | 49.52 | 22902405 | |
101 | Phosphorylation | LESFKKQSFVLKEGV HHHHHHEEEEEECCE | 26.63 | 19103160 | |
105 | Acetylation | KKQSFVLKEGVEYRI HHEEEEEECCEEEEE | 47.31 | 22902405 | |
111 | Methylation | LKEGVEYRIKISFRV EECCEEEEEEEEEEE | 15.37 | 166183 | |
111 | Dimethylation | LKEGVEYRIKISFRV EECCEEEEEEEEEEE | 15.37 | - | |
113 | Acetylation | EGVEYRIKISFRVNR CCEEEEEEEEEEECH | 24.25 | 22902405 | |
127 | Acetylation | REIVSGMKYIQHTYR HHHHCCCCHHHHHHC | 42.60 | 22902405 | |
133 | Phosphorylation | MKYIQHTYRKGVKID CCHHHHHHCCCCCCC | 14.27 | - | |
138 | Acetylation | HTYRKGVKIDKTDYM HHHCCCCCCCCCCCC | 54.58 | 22902405 | |
141 | Ubiquitination | RKGVKIDKTDYMVGS CCCCCCCCCCCCCCC | 46.93 | - | |
141 | Succinylation | RKGVKIDKTDYMVGS CCCCCCCCCCCCCCC | 46.93 | - | |
141 | Acetylation | RKGVKIDKTDYMVGS CCCCCCCCCCCCCCC | 46.93 | 22902405 | |
141 | Succinylation | RKGVKIDKTDYMVGS CCCCCCCCCCCCCCC | 46.93 | - | |
144 | Phosphorylation | VKIDKTDYMVGSYGP CCCCCCCCCCCCCCC | 10.03 | 22817900 | |
148 | Phosphorylation | KTDYMVGSYGPRAEE CCCCCCCCCCCCHHH | 18.59 | 22817900 | |
149 | Phosphorylation | TDYMVGSYGPRAEEY CCCCCCCCCCCHHHE | 25.81 | 25575281 | |
152 | Methylation | MVGSYGPRAEEYEFL CCCCCCCCHHHEEEE | 50.71 | 166189 | |
152 | Dimethylation | MVGSYGPRAEEYEFL CCCCCCCCHHHEEEE | 50.71 | - | |
160 | Phosphorylation | AEEYEFLTPMEEAPK HHHEEEECCHHHCCC | 26.38 | 23984901 | |
167 | Acetylation | TPMEEAPKGMLARGS CCHHHCCCCCCCCCC | 65.09 | 22902405 | |
174 | Phosphorylation | KGMLARGSYNIKSRF CCCCCCCCEECCCCC | 14.95 | 30181290 | |
178 | Acetylation | ARGSYNIKSRFTDDD CCCCEECCCCCCCCC | 31.76 | 25786129 | |
180 | Dimethylation | GSYNIKSRFTDDDKT CCEECCCCCCCCCCC | 33.22 | - | |
180 | Methylation | GSYNIKSRFTDDDKT CCEECCCCCCCCCCC | 33.22 | 166195 |
Modified Location | Modified Residue | Modification | Function | Reference | ||
---|---|---|---|---|---|---|
Oops, there are no descriptions of PTM sites of GDIR1_RAT !! |
* 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 !! |
Interacting Protein | Gene Name | Interaction Type | PPI Reference | Domain-Domain Interactions |
---|---|---|---|---|
Oops, there are no PPI records of GDIR1_RAT !! |
Kegg Drug | ||||||
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DrugBank | ||||||
There are no disease associations of PTM sites. |
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