GDIA_MOUSE - dbPTM
GDIA_MOUSE - PTM Information in dbPTM
Basic Information of Protein
UniProt ID GDIA_MOUSE
UniProt AC P50396
Protein Name Rab GDP dissociation inhibitor alpha
Gene Name Gdi1
Organism Mus musculus (Mouse).
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 MDEEYDVIVLGTGLTECILSGIMSVNGKKVLHMDRNPYYGGESSSITPLEELYKRFQILEGPPESMGRGRDWNVDLIPKFLMANGQLVKMLLYTEVTRYLDFKVVEGSFVYKGGKIYKVPSTETEALASNLMGMFEKRRFRKFLVFVANFDENDPKTFEGVDPQNTSMRDVYRKFDLGQDVIDFTGHALALYRTDDYLDQPCLETINRIKLYSESLARYGKSPYLYPLYGLGELPQGFARLSAIYGGTYMLNKPVDDIIMENGKVVGVKSEGEVARCKQLICDPSYIPDRVQKAGQVIRIICILSHPIKNTNDANSCQIIIPQNQVNRKSDIYVCMISYAHNVAAQGKYIAIASTTVETAEPEKEVEPALELLEPIDQKFVAISDLYEPIDDGSESQVFCSCSYDATTHFETTCNDIKDIYKRMAGSAFDFENMKRKQNDVFGEADQ
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-
38PhosphorylationLHMDRNPYYGGESSS
EECCCCCCCCCCCCC		20.4922817900
39PhosphorylationHMDRNPYYGGESSSI
ECCCCCCCCCCCCCC		21.6630635358
43PhosphorylationNPYYGGESSSITPLE
CCCCCCCCCCCCCHH		32.4322817900
44PhosphorylationPYYGGESSSITPLEE
CCCCCCCCCCCCHHH		22.8122817900
45PhosphorylationYYGGESSSITPLEEL
CCCCCCCCCCCHHHH		39.5022817900
47PhosphorylationGGESSSITPLEELYK
CCCCCCCCCHHHHHH		24.6230635358
53PhosphorylationITPLEELYKRFQILE
CCCHHHHHHHHCHHC		11.9130635358
54UbiquitinationTPLEELYKRFQILEG
CCHHHHHHHHCHHCC		60.4022790023
79UbiquitinationWNVDLIPKFLMANGQ
CCCCHHHHHHHHCCC		44.10-
93PhosphorylationQLVKMLLYTEVTRYL
CEEEHHHHHHHHHHC		9.2620415495
94PhosphorylationLVKMLLYTEVTRYLD
EEEHHHHHHHHHHCC		24.7720415495
97PhosphorylationMLLYTEVTRYLDFKV
HHHHHHHHHHCCEEE		13.8320415495
112SuccinylationVEGSFVYKGGKIYKV
EEEEEEEECCEEEEC		56.7523954790
112AcetylationVEGSFVYKGGKIYKV
EEEEEEEECCEEEEC		56.7522826441
117PhosphorylationVYKGGKIYKVPSTET
EEECCEEEECCCHHH		14.9322817900
121PhosphorylationGKIYKVPSTETEALA
CEEEECCCHHHHHHH		41.6929899451
122PhosphorylationKIYKVPSTETEALAS
EEEECCCHHHHHHHH		40.6429899451
124PhosphorylationYKVPSTETEALASNL
EECCCHHHHHHHHHH		27.0129899451
137AcetylationNLMGMFEKRRFRKFL
HHHHHHHHHHHHEEE		37.2922826441
157PhosphorylationFDENDPKTFEGVDPQ
CCCCCCCCCCCCCCC		32.1022817900
166PhosphorylationEGVDPQNTSMRDVYR
CCCCCCCCCHHHHHH		20.7422817900
167PhosphorylationGVDPQNTSMRDVYRK
CCCCCCCCHHHHHHH		21.2622817900
172PhosphorylationNTSMRDVYRKFDLGQ
CCCHHHHHHHCCCCC		16.6322817900
202S-nitrosylationDDYLDQPCLETINRI
CCCCCCHHHHHHHHH		4.4522588120
202S-nitrosocysteineDDYLDQPCLETINRI
CCCCCCHHHHHHHHH		4.45-
210UbiquitinationLETINRIKLYSESLA
HHHHHHHHHHHHHHH		37.83-
210AcetylationLETINRIKLYSESLA
HHHHHHHHHHHHHHH		37.8322826441
221UbiquitinationESLARYGKSPYLYPL
HHHHHHCCCCCEECC		39.0527667366
229PhosphorylationSPYLYPLYGLGELPQ
CCCEECCCCCCCCCC		13.0522817900
242PhosphorylationPQGFARLSAIYGGTY
CCHHHHHHHHHCCCE		13.68-
245PhosphorylationFARLSAIYGGTYMLN
HHHHHHHHCCCEECC		14.82-
269UbiquitinationNGKVVGVKSEGEVAR
CCEEEEECCCCCHHH		36.5422790023
269AcetylationNGKVVGVKSEGEVAR
CCEEEEECCCCCHHH		36.5422826441
278UbiquitinationEGEVARCKQLICDPS
CCCHHHEEEEEECHH		42.4522790023
282S-nitrosocysteineARCKQLICDPSYIPD
HHEEEEEECHHHCCH		9.52-
282S-nitrosylationARCKQLICDPSYIPD
HHEEEEEECHHHCCH		9.5222588120
309AcetylationCILSHPIKNTNDANS
EEECCCCCCCCCCCC		63.2722826441
317S-nitrosylationNTNDANSCQIIIPQN
CCCCCCCCEEEEEHH		3.1922588120
317S-palmitoylationNTNDANSCQIIIPQN
CCCCCCCCEEEEEHH		3.1928526873
317GlutathionylationNTNDANSCQIIIPQN
CCCCCCCCEEEEEHH		3.1924333276
317S-nitrosocysteineNTNDANSCQIIIPQN
CCCCCCCCEEEEEHH		3.19-
329AcetylationPQNQVNRKSDIYVCM
EHHHCCCCCCEEEEE		47.4822826441
339PhosphorylationIYVCMISYAHNVAAQ
EEEEEEECCCHHHHC		10.8522817900
427PhosphorylationIYKRMAGSAFDFENM
HHHHHCCCCCCHHHH		19.0725521595
435AcetylationAFDFENMKRKQNDVF
CCCHHHHHHHHCCCC		68.947618889
435UbiquitinationAFDFENMKRKQNDVF
CCCHHHHHHHHCCCC		68.9422790023
437UbiquitinationDFENMKRKQNDVFGE
CHHHHHHHHCCCCCC		48.1922790023
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

Oops, there are no upstream regulatory protein records of GDIA_MOUSE !!
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of GDIA_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 GDIA_MOUSE !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions

Oops, there are no PPI records of GDIA_MOUSE !!
Drug and Disease Associations
Kegg Drug
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of GDIA_MOUSE

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Related Literatures of Post-Translational Modification
Phosphorylation
ReferencePubMed
"Large-scale identification and evolution indexing of tyrosinephosphorylation sites from murine brain.";
Ballif B.A., Carey G.R., Sunyaev S.R., Gygi S.P.;
J. Proteome Res. 7:311-318(2008).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-339, AND MASSSPECTROMETRY.

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