GDIB_MOUSE - dbPTM
GDIB_MOUSE - PTM Information in dbPTM
Basic Information of Protein
UniProt ID GDIB_MOUSE
UniProt AC Q61598
Protein Name Rab GDP dissociation inhibitor beta
Gene Name Gdi2
Organism Mus musculus (Mouse).
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-
29UbiquitinationIMSVNGKKVLHMDQN
HHCCCCEEEEECCCC
51.97-
38PhosphorylationLHMDQNPYYGGESAS
EECCCCCCCCCCCCC
23.4522817900
39PhosphorylationHMDQNPYYGGESASI
ECCCCCCCCCCCCCC
21.6622817900
54AcetylationTPLEDLYKRFKLPGQ
CCHHHHHHHCCCCCC
59.67132935
54UbiquitinationTPLEDLYKRFKLPGQ
CCHHHHHHHCCCCCC
59.67-
57UbiquitinationEDLYKRFKLPGQPPA
HHHHHHCCCCCCCCC
58.78-
57AcetylationEDLYKRFKLPGQPPA
HHHHHHCCCCCCCCC
58.7823806337
57SuccinylationEDLYKRFKLPGQPPA
HHHHHHCCCCCCCCC
58.78-
57SuccinylationEDLYKRFKLPGQPPA
HHHHHHCCCCCCCCC
58.7823806337
65PhosphorylationLPGQPPASMGRGRDW
CCCCCCCCCCCCCCC
27.7828066266
68MethylationQPPASMGRGRDWNVD
CCCCCCCCCCCCCCC
28.47-
79UbiquitinationWNVDLIPKFLMANGQ
CCCCHHHHHHHHCCC
44.10-
112UbiquitinationIEGSFVYKGGKIYKV
EEEEEEEECCEEEEC
56.75-
112AcetylationIEGSFVYKGGKIYKV
EEEEEEEECCEEEEC
56.7523236377
112SuccinylationIEGSFVYKGGKIYKV
EEEEEEEECCEEEEC
56.7523954790
117PhosphorylationVYKGGKIYKVPSTEA
EEECCEEEECCCHHH
14.93-
129PhosphorylationTEAEALASSLMGLFE
HHHHHHHHHHHHHHH
25.5129472430
130PhosphorylationEAEALASSLMGLFEK
HHHHHHHHHHHHHHH
19.4426745281
137AcetylationSLMGLFEKRRFRKFL
HHHHHHHHHCHHHEE
41.3523954790
142UbiquitinationFEKRRFRKFLVYVAN
HHHHCHHHEEEEEEC
40.10-
153UbiquitinationYVANFDEKDPRTFEG
EEECCCCCCCCCCCC
74.91-
164SuccinylationTFEGVDPKKTSMRDV
CCCCCCCCCCCHHHH
65.3123954790
164UbiquitinationTFEGVDPKKTSMRDV
CCCCCCCCCCCHHHH
65.31-
164MalonylationTFEGVDPKKTSMRDV
CCCCCCCCCCCHHHH
65.3126320211
164AcetylationTFEGVDPKKTSMRDV
CCCCCCCCCCCHHHH
65.3123806337
174AcetylationSMRDVYKKFDLGQDV
CHHHHHHHCCCCCCC
26.8222826441
174UbiquitinationSMRDVYKKFDLGQDV
CHHHHHHHCCCCCCC
26.82-
210UbiquitinationCETINRIKLYSESLA
HHHHHHHHHHHHHHH
37.83-
221UbiquitinationESLARYGKSPYLYPL
HHHHHHCCCCCEECC
39.05-
229PhosphorylationSPYLYPLYGLGELPQ
CCCEECCCCCCCCCC
13.0518563927
242PhosphorylationPQGFARLSAIYGGTY
CCHHHHHHHHHCCCE
13.6825367039
245PhosphorylationFARLSAIYGGTYMLN
HHHHHHHHCCCEECC
14.8225367039
248PhosphorylationLSAIYGGTYMLNKPI
HHHHHCCCEECCCCH
11.0325367039
249PhosphorylationSAIYGGTYMLNKPIE
HHHHCCCEECCCCHH
11.6825367039
269UbiquitinationNGKVVGVKSEGEIAR
CCEEEEECCHHHHHH
36.54-
269SuccinylationNGKVVGVKSEGEIAR
CCEEEEECCHHHHHH
36.5423806337
269AcetylationNGKVVGVKSEGEIAR
CCEEEEECCHHHHHH
36.5423806337
269MalonylationNGKVVGVKSEGEIAR
CCEEEEECCHHHHHH
36.5426320211
278UbiquitinationEGEIARCKQLICDPS
HHHHHHHEEEECCHH
42.45-
288AcetylationICDPSYVKDRVEKVG
ECCHHHHHHHHHHHH
31.4222826441
293AcetylationYVKDRVEKVGQVIRV
HHHHHHHHHHHHHHH
49.1322826441
293UbiquitinationYVKDRVEKVGQVIRV
HHHHHHHHHHHHHHH
49.13-
309AcetylationCILSHPIKNTNDANS
HHHCCCCCCCCCCCC
63.27-
309MalonylationCILSHPIKNTNDANS
HHHCCCCCCCCCCCC
63.2726320211
317S-nitrosocysteineNTNDANSCQIIIPQN
CCCCCCCCEEEEEHH
3.19-
317S-nitrosylationNTNDANSCQIIIPQN
CCCCCCCCEEEEEHH
3.1921278135
329AcetylationPQNQVNRKSDIYVCM
EHHHCCCCCCEEEEE
47.48-
333PhosphorylationVNRKSDIYVCMISFA
CCCCCCEEEEEHHCC
7.8125367039
360UbiquitinationVSTTVETKEPEKEIR
EEEEECCCCCHHHHH
58.74-
382PhosphorylationPIEQKFVSISDLFVP
HHHHHCCCHHHCCCC
21.3626643407
384PhosphorylationEQKFVSISDLFVPKD
HHHCCCHHHCCCCCC
22.2823984901
390UbiquitinationISDLFVPKDLGTDSQ
HHHCCCCCCCCCCCE
61.35-
414S-nitrosocysteineTTHFETTCDDIKDIY
CCCEECHHHHHHHHH
6.05-
414S-nitrosylationTTHFETTCDDIKDIY
CCCEECHHHHHHHHH
6.0520925432
414GlutathionylationTTHFETTCDDIKDIY
CCCEECHHHHHHHHH
6.0524333276
418AcetylationETTCDDIKDIYKRMT
ECHHHHHHHHHHHHH
45.1022826441
418UbiquitinationETTCDDIKDIYKRMT
ECHHHHHHHHHHHHH
45.10-
422AcetylationDDIKDIYKRMTGSEF
HHHHHHHHHHHCCCC
35.7123806337
425PhosphorylationKDIYKRMTGSEFDFE
HHHHHHHHCCCCCHH
41.4020139300
427PhosphorylationIYKRMTGSEFDFEEM
HHHHHHCCCCCHHHH
26.3922817900
435AcetylationEFDFEEMKRKKNDIY
CCCHHHHHHHHCCCC
65.43155633
435UbiquitinationEFDFEEMKRKKNDIY
CCCHHHHHHHHCCCC
65.43-
442PhosphorylationKRKKNDIYGED----
HHHHCCCCCCC----
19.8225367039

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_MOUSE !!

Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

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

Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
RAB6A_HUMANRAB6Aphysical
7782346
RAB4A_HUMANRAB4Aphysical
7782346
RAB2A_HUMANRAB2Aphysical
7782346
RAB1A_HUMANRAB1Aphysical
7782346

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

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Related Literatures of Post-Translational Modification

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