GDIB_RAT - dbPTM
GDIB_RAT - PTM Information in dbPTM
Basic Information of Protein
UniProt ID GDIB_RAT
UniProt AC P50399
Protein Name Rab GDP dissociation inhibitor beta
Gene Name Gdi2
Organism Rattus norvegicus (Rat).
Sequence Length 445
Subcellular Localization Cytoplasm. Membrane
Peripheral membrane protein.
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..
Protein Sequence MNEEYDVIVLGTGLTECILSGIMSVNGKKVLHMDQNPYYGGESASITPLEDLYKRFKLPGQPPASMGRGRDWNVDLIPKFLMANGQLVKMLLFTEVTRYMDFKVIEGSFVYKGGKIYKVPSTEAEALASSLMGLFEKRRFRKFLVYVANFDEKDPRTFEGVDPKKTSMRDVYKKFDLGQDVIDFTGHSLALYRTDDYLDQPCCETINRIKLYSESLARYGKSPYLYPLYGLGELPQGFARLSAIYGGTYMLNKPIEEIIVQNGKVVGVKSEGEIARCKQLICDPSYVKDRVEKVGQVIRVICILSHPIKNTNDANSCQIIIPQNQVNRKSDIYVCMISFAHNVAAQGKYIAIVSTTVETKEPEKEIRPALELLEPIEQKFVSISDLFVPKDLGTDSQIFISRAYDATTHFETTCDDIKDIYKRMTGSEFDFEEMKRKKNDIYGED
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-------MNEEYDVI
-------CCCCCCEE
14.90-
57SuccinylationEDLYKRFKLPGQPPA
HHHHHHCCCCCCCCC
58.78-
57SuccinylationEDLYKRFKLPGQPPA
HHHHHHCCCCCCCCC
58.78-
99PhosphorylationLFTEVTRYMDFKVIE
HHHCHHHHCCEEEEE
7.53-
112AcetylationIEGSFVYKGGKIYKV
EEEEEEEECCEEEEC
56.7522902405
129PhosphorylationTEAEALASSLMGLFE
HHHHHHHHHHHHHHH
25.5122673903
130PhosphorylationEAEALASSLMGLFEK
HHHHHHHHHHHHHHH
19.4422673903
142AcetylationFEKRRFRKFLVYVAN
HHHHCHHHEEEEEEC
40.1022902405
153AcetylationYVANFDEKDPRTFEG
EEECCCCCCCCCCCC
74.9126302492
164AcetylationTFEGVDPKKTSMRDV
CCCCCCCCCCCHHHH
65.3122902405
165AcetylationFEGVDPKKTSMRDVY
CCCCCCCCCCHHHHH
51.7426302492
174AcetylationSMRDVYKKFDLGQDV
CHHHHHHHCCCCCCC
26.8222902405
213PhosphorylationINRIKLYSESLARYG
HHHHHHHHHHHHHHC
31.01-
221AcetylationESLARYGKSPYLYPL
HHHHHHCCCCCEECC
39.0566734115
221UbiquitinationESLARYGKSPYLYPL
HHHHHHCCCCCEECC
39.05-
224PhosphorylationARYGKSPYLYPLYGL
HHHCCCCCEECCCCC
26.42-
226PhosphorylationYGKSPYLYPLYGLGE
HCCCCCEECCCCCCC
5.83-
229PhosphorylationSPYLYPLYGLGELPQ
CCCEECCCCCCCCCC
13.05-
269AcetylationNGKVVGVKSEGEIAR
CCEEEEECCHHHHHH
36.5422902405
360UbiquitinationVSTTVETKEPEKEIR
EEEEECCCCCHHHHH
58.74-
382PhosphorylationPIEQKFVSISDLFVP
HHHHHCCCHHHCCCC
21.36-
418SuccinylationETTCDDIKDIYKRMT
ECHHHHHHHHHHHHH
45.1026843850
425PhosphorylationKDIYKRMTGSEFDFE
HHHHHHHHCCCCCHH
41.4025575281
427PhosphorylationIYKRMTGSEFDFEEM
HHHHHHCCCCCHHHH
26.3928432305

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 GDIB_RAT !!

Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of GDIB_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 GDIB_RAT !!

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

Oops, there are no PPI records of GDIB_RAT !!

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

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Related Literatures of Post-Translational Modification

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