GDIR1_MOUSE - dbPTM
GDIR1_MOUSE - PTM Information in dbPTM
Basic Information of Protein
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
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
41.9125619855
24PhosphorylationENEEDEHSVNYKPPA
HCCCCCCCCCCCCCC
15.2626824392
27PhosphorylationEDEHSVNYKPPAQKS
CCCCCCCCCCCCHHH
23.7925619855
28AcetylationDEHSVNYKPPAQKSI
CCCCCCCCCCCHHHH
39.0423236377
34PhosphorylationYKPPAQKSIQEIQEL
CCCCCHHHHHHHHHH
19.8825521595
43AcetylationQEIQELDKDDESLRK
HHHHHHCCCCHHHHH
78.6323806337
43UbiquitinationQEIQELDKDDESLRK
HHHHHHCCCCHHHHH
78.6322790023
47PhosphorylationELDKDDESLRKYKEA
HHCCCCHHHHHHHHH
40.2326824392
51PhosphorylationDDESLRKYKEALLGR
CCHHHHHHHHHHHHC
13.9729514104
52AcetylationDESLRKYKEALLGRV
CHHHHHHHHHHHHCE
39.2823806337
52SuccinylationDESLRKYKEALLGRV
CHHHHHHHHHHHHCE
39.2823806337
52MalonylationDESLRKYKEALLGRV
CHHHHHHHHHHHHCE
39.2826320211
62PhosphorylationLLGRVAVSADPNVPN
HHHCEECCCCCCCCC
19.7427180971
79GlutathionylationVTRLTLVCSTAPGPL
EEEEEEEEECCCCCE
3.1724333276
96PhosphorylationDLTGDLESFKKQSFV
ECCCCHHHHHHEEEE
50.0619581409
98AcetylationTGDLESFKKQSFVLK
CCCHHHHHHEEEEEE
60.21156627
99MalonylationGDLESFKKQSFVLKE
CCHHHHHHEEEEEEC
49.5226320211
99AcetylationGDLESFKKQSFVLKE
CCHHHHHHEEEEEEC
49.5222826441
99UbiquitinationGDLESFKKQSFVLKE
CCHHHHHHEEEEEEC
49.5227667366
101PhosphorylationLESFKKQSFVLKEGV
HHHHHHEEEEEECCE
26.6326824392
105AcetylationKKQSFVLKEGVEYRI
HHEEEEEECCEEEEE
47.3122826441
105SuccinylationKKQSFVLKEGVEYRI
HHEEEEEECCEEEEE
47.3123954790
127MalonylationREIVSGMKYIQHTYR
HHHHCCCCHHHHHHC
42.6026320211
127UbiquitinationREIVSGMKYIQHTYR
HHHHCCCCHHHHHHC
42.60-
127AcetylationREIVSGMKYIQHTYR
HHHHCCCCHHHHHHC
42.6023236377
132PhosphorylationGMKYIQHTYRKGVKI
CCCHHHHHHCCCCCC
14.5129472430
133PhosphorylationMKYIQHTYRKGVKID
CCHHHHHHCCCCCCC
14.2729472430
138MalonylationHTYRKGVKIDKTDYM
HHHCCCCCCCCCCCC
54.5826320211
138UbiquitinationHTYRKGVKIDKTDYM
HHHCCCCCCCCCCCC
54.58-
141UbiquitinationRKGVKIDKTDYMVGS
CCCCCCCCCCCCCCC
46.9327667366
141SuccinylationRKGVKIDKTDYMVGS
CCCCCCCCCCCCCCC
46.9323806337
141SuccinylationRKGVKIDKTDYMVGS
CCCCCCCCCCCCCCC
46.93-
141AcetylationRKGVKIDKTDYMVGS
CCCCCCCCCCCCCCC
46.9323806337
141MalonylationRKGVKIDKTDYMVGS
CCCCCCCCCCCCCCC
46.9326320211
148PhosphorylationKTDYMVGSYGPRAEE
CCCCCCCCCCCCHHH
18.5924899341
149PhosphorylationTDYMVGSYGPRAEEY
CCCCCCCCCCCHHHE
25.8129472430
160PhosphorylationAEEYEFLTPMEEAPK
HHHEEEECCHHHCCC
26.38-
167AcetylationTPMEEAPKGMLARGS
CCHHHCCCCCCCCCC
65.0923236377
167UbiquitinationTPMEEAPKGMLARGS
CCHHHCCCCCCCCCC
65.0922790023
174PhosphorylationKGMLARGSYNIKSRF
CCCCCCCCEECCCCC
14.9524719451
178SuccinylationARGSYNIKSRFTDDD
CCCCEECCCCCCCCC
31.7623954790
178UbiquitinationARGSYNIKSRFTDDD
CCCCEECCCCCCCCC
31.7627667366
178MalonylationARGSYNIKSRFTDDD
CCCCEECCCCCCCCC
31.7626320211
178AcetylationARGSYNIKSRFTDDD
CCCCEECCCCCCCCC
31.7623806337
179PhosphorylationRGSYNIKSRFTDDDK
CCCEECCCCCCCCCC
28.9128059163

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
96SPhosphorylationKinasePRKCAP17252
GPS

Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of GDIR1_MOUSE !!

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_MOUSE !!

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

Oops, there are no PPI records of GDIR1_MOUSE !!

Drug and Disease Associations
Kegg Drug
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of GDIR1_MOUSE

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Related Literatures of Post-Translational Modification

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