UniProt ID | GDIR1_MOUSE | |
---|---|---|
UniProt AC | Q99PT1 | |
Protein Name | Rho GDP-dissociation inhibitor 1 | |
Gene Name | Arhgdia | |
Organism | Mus musculus (Mouse). | |
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 | 25619855 | |
24 | Phosphorylation | ENEEDEHSVNYKPPA HCCCCCCCCCCCCCC | 15.26 | 26824392 | |
27 | Phosphorylation | EDEHSVNYKPPAQKS CCCCCCCCCCCCHHH | 23.79 | 25619855 | |
28 | Acetylation | DEHSVNYKPPAQKSI CCCCCCCCCCCHHHH | 39.04 | 23236377 | |
34 | Phosphorylation | YKPPAQKSIQEIQEL CCCCCHHHHHHHHHH | 19.88 | 25521595 | |
43 | Acetylation | QEIQELDKDDESLRK HHHHHHCCCCHHHHH | 78.63 | 23806337 | |
43 | Ubiquitination | QEIQELDKDDESLRK HHHHHHCCCCHHHHH | 78.63 | 22790023 | |
47 | Phosphorylation | ELDKDDESLRKYKEA HHCCCCHHHHHHHHH | 40.23 | 26824392 | |
51 | Phosphorylation | DDESLRKYKEALLGR CCHHHHHHHHHHHHC | 13.97 | 29514104 | |
52 | Acetylation | DESLRKYKEALLGRV CHHHHHHHHHHHHCE | 39.28 | 23806337 | |
52 | Succinylation | DESLRKYKEALLGRV CHHHHHHHHHHHHCE | 39.28 | 23806337 | |
52 | Malonylation | DESLRKYKEALLGRV CHHHHHHHHHHHHCE | 39.28 | 26320211 | |
62 | Phosphorylation | LLGRVAVSADPNVPN HHHCEECCCCCCCCC | 19.74 | 27180971 | |
79 | Glutathionylation | VTRLTLVCSTAPGPL EEEEEEEEECCCCCE | 3.17 | 24333276 | |
96 | Phosphorylation | DLTGDLESFKKQSFV ECCCCHHHHHHEEEE | 50.06 | 19581409 | |
98 | Acetylation | TGDLESFKKQSFVLK CCCHHHHHHEEEEEE | 60.21 | 156627 | |
99 | Malonylation | GDLESFKKQSFVLKE CCHHHHHHEEEEEEC | 49.52 | 26320211 | |
99 | Acetylation | GDLESFKKQSFVLKE CCHHHHHHEEEEEEC | 49.52 | 22826441 | |
99 | Ubiquitination | GDLESFKKQSFVLKE CCHHHHHHEEEEEEC | 49.52 | 27667366 | |
101 | Phosphorylation | LESFKKQSFVLKEGV HHHHHHEEEEEECCE | 26.63 | 26824392 | |
105 | Acetylation | KKQSFVLKEGVEYRI HHEEEEEECCEEEEE | 47.31 | 22826441 | |
105 | Succinylation | KKQSFVLKEGVEYRI HHEEEEEECCEEEEE | 47.31 | 23954790 | |
127 | Malonylation | REIVSGMKYIQHTYR HHHHCCCCHHHHHHC | 42.60 | 26320211 | |
127 | Ubiquitination | REIVSGMKYIQHTYR HHHHCCCCHHHHHHC | 42.60 | - | |
127 | Acetylation | REIVSGMKYIQHTYR HHHHCCCCHHHHHHC | 42.60 | 23236377 | |
132 | Phosphorylation | GMKYIQHTYRKGVKI CCCHHHHHHCCCCCC | 14.51 | 29472430 | |
133 | Phosphorylation | MKYIQHTYRKGVKID CCHHHHHHCCCCCCC | 14.27 | 29472430 | |
138 | Malonylation | HTYRKGVKIDKTDYM HHHCCCCCCCCCCCC | 54.58 | 26320211 | |
138 | Ubiquitination | HTYRKGVKIDKTDYM HHHCCCCCCCCCCCC | 54.58 | - | |
141 | Ubiquitination | RKGVKIDKTDYMVGS CCCCCCCCCCCCCCC | 46.93 | 27667366 | |
141 | Succinylation | RKGVKIDKTDYMVGS CCCCCCCCCCCCCCC | 46.93 | 23806337 | |
141 | Succinylation | RKGVKIDKTDYMVGS CCCCCCCCCCCCCCC | 46.93 | - | |
141 | Acetylation | RKGVKIDKTDYMVGS CCCCCCCCCCCCCCC | 46.93 | 23806337 | |
141 | Malonylation | RKGVKIDKTDYMVGS CCCCCCCCCCCCCCC | 46.93 | 26320211 | |
148 | Phosphorylation | KTDYMVGSYGPRAEE CCCCCCCCCCCCHHH | 18.59 | 24899341 | |
149 | Phosphorylation | TDYMVGSYGPRAEEY CCCCCCCCCCCHHHE | 25.81 | 29472430 | |
160 | Phosphorylation | AEEYEFLTPMEEAPK HHHEEEECCHHHCCC | 26.38 | - | |
167 | Acetylation | TPMEEAPKGMLARGS CCHHHCCCCCCCCCC | 65.09 | 23236377 | |
167 | Ubiquitination | TPMEEAPKGMLARGS CCHHHCCCCCCCCCC | 65.09 | 22790023 | |
174 | Phosphorylation | KGMLARGSYNIKSRF CCCCCCCCEECCCCC | 14.95 | 24719451 | |
178 | Succinylation | ARGSYNIKSRFTDDD CCCCEECCCCCCCCC | 31.76 | 23954790 | |
178 | Ubiquitination | ARGSYNIKSRFTDDD CCCCEECCCCCCCCC | 31.76 | 27667366 | |
178 | Malonylation | ARGSYNIKSRFTDDD CCCCEECCCCCCCCC | 31.76 | 26320211 | |
178 | Acetylation | ARGSYNIKSRFTDDD CCCCEECCCCCCCCC | 31.76 | 23806337 | |
179 | Phosphorylation | RGSYNIKSRFTDDDK CCCEECCCCCCCCCC | 28.91 | 28059163 |
Modified Location | Modified Residue | Modification | Type of Upstream Proteins | Gene Name of Upstream Proteins | UniProt AC of Upstream Proteins | Sources |
---|---|---|---|---|---|---|
96 | S | Phosphorylation | Kinase | PRKCA | P17252 | GPS |
Modified Location | Modified Residue | Modification | Function | Reference | ||
---|---|---|---|---|---|---|
Oops, there are no descriptions of PTM sites of GDIR1_MOUSE !! |
* 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_MOUSE !! |
Interacting Protein | Gene Name | Interaction Type | PPI Reference | Domain-Domain Interactions |
---|---|---|---|---|
Oops, there are no PPI records of GDIR1_MOUSE !! |
Kegg Drug | ||||||
---|---|---|---|---|---|---|
DrugBank | ||||||
There are no disease associations of PTM sites. |
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