GDIA_RAT - dbPTM
GDIA_RAT - PTM Information in dbPTM
Basic Information of Protein
UniProt ID GDIA_RAT
UniProt AC P50398
Protein Name Rab GDP dissociation inhibitor alpha
Gene Name Gdi1
Organism Rattus norvegicus (Rat).
Sequence Length 447
Subcellular Localization Cytoplasm. Golgi apparatus, trans-Golgi network.
Protein Description Regulates the GDP/GTP exchange reaction of most Rab proteins by inhibiting the dissociation of GDP from them, and the subsequent binding of GTP to them. Promotes the dissociation of GDP-bound Rab proteins from the membrane and inhibits their activation. Promotes the dissociation of RAB1A, RAB3A, RAB5A and RAB10 from membranes..
Protein Sequence MDEEYDVIVLGTGLTECILSGIMSVNGKKVLHMDRNPYYGGESSSITPLEELYKRFQLLEGPPESMGRGRDWNVDLIPKFLMANGQLVKMLLYTEVTRYLDFKVVEGSFVYKGGKIYKVPSTETEALASNLMGMFEKRRFRKFLVFVANFDENDPKTFEGVDPQTTSMRDVYRKFDLGQDVIDFTGHALALYRTDDYLDQPCLETINRIKLYSESLARYGKSPYLYPLYGLGELPQGFARLSAIYGGTYMLNKPVDDIIMENGKVVGVKSEGEVARCKQLICDPSYIPDRVRKAGQVIRIICILSHPIKNTNDANSCQIIIPQNQVNRKSDIYVCMISYAHNVAAQGKYIAIASTTVETAEPEKEVEPALELLEPIDQKFVAISDLYEPIDDGSESQVFCSCSYDATTHFETTCNDIKDIYKRMAGSAFDFENMKRKQNDVFGEADQ
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
1Acetylation-------MDEEYDVI
-------CCCCCEEE
15.33-
54UbiquitinationTPLEELYKRFQLLEG
CCHHHHHHHHHHHHC
60.40-
54AcetylationTPLEELYKRFQLLEG
CCHHHHHHHHHHHHC
60.4022902405
93PhosphorylationQLVKMLLYTEVTRYL
CEEEHHHHHHHHHHC
9.26-
112AcetylationVEGSFVYKGGKIYKV
EEEEEEEECCEEEEC
56.7522902405
157PhosphorylationFDENDPKTFEGVDPQ
CCCCCCCCCCCCCCC
32.1027115346
174AcetylationSMRDVYRKFDLGQDV
CHHHHHHHCCCCCCE
26.0822902405
208DimethylationPCLETINRIKLYSES
HHHHHHHHHHHHHHH
24.46-
208MethylationPCLETINRIKLYSES
HHHHHHHHHHHHHHH
24.46-
210"N6,N6-dimethyllysine"LETINRIKLYSESLA
HHHHHHHHHHHHHHH
37.83-
210MethylationLETINRIKLYSESLA
HHHHHHHHHHHHHHH
37.8312692561
213PhosphorylationINRIKLYSESLARYG
HHHHHHHHHHHHHHC
31.0120051515
221UbiquitinationESLARYGKSPYLYPL
HHHHHHCCCCCEECC
39.05-
221AcetylationESLARYGKSPYLYPL
HHHHHHCCCCCEECC
39.0522902405
224PhosphorylationARYGKSPYLYPLYGL
HHHCCCCCEECCCCC
26.42-
226PhosphorylationYGKSPYLYPLYGLGE
HCCCCCEECCCCCCC
5.83-
229PhosphorylationSPYLYPLYGLGELPQ
CCCEECCCCCCCCCC
13.05-
253AcetylationGGTYMLNKPVDDIIM
CCCEECCCCHHEEEE
42.3222902405
264MethylationDIIMENGKVVGVKSE
EEEEECCEEEEECCC
45.3812692561
269AcetylationNGKVVGVKSEGEVAR
CCEEEEECCCCCHHH
36.5422902405
269MethylationNGKVVGVKSEGEVAR
CCEEEEECCCCCHHH
36.5412692561
317S-nitrosylationNTNDANSCQIIIPQN
CCCCCCCCEEEEEHH
3.1922178444
317S-nitrosocysteineNTNDANSCQIIIPQN
CCCCCCCCEEEEEHH
3.19-
339PhosphorylationIYVCMISYAHNVAAQ
EEEEEEECCCHHHHC
10.85-
427PhosphorylationIYKRMAGSAFDFENM
HHHHHCCCCCCHHHH
19.0728432305
435AcetylationAFDFENMKRKQNDVF
CCCHHHHHHHHCCCC
68.9422902405
435UbiquitinationAFDFENMKRKQNDVF
CCCHHHHHHHHCCCC
68.94-
437UbiquitinationDFENMKRKQNDVFGE
CHHHHHHHHCCCCCC
48.19-

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
213SPhosphorylationKinaseSGK1O00141
PSP

Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of GDIA_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 GDIA_RAT !!

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

Oops, there are no PPI records of GDIA_RAT !!

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

loading...

Related Literatures of Post-Translational Modification

TOP