RB3GP_MOUSE - dbPTM
RB3GP_MOUSE - PTM Information in dbPTM
Basic Information of Protein
UniProt ID RB3GP_MOUSE
UniProt AC Q80UJ7
Protein Name Rab3 GTPase-activating protein catalytic subunit
Gene Name Rab3gap1
Organism Mus musculus (Mouse).
Sequence Length 981
Subcellular Localization Cytoplasm. In neurons, it is enriched in the synaptic soluble fraction..
Protein Description Probable catalytic subunit of a GTPase activating protein that has specificity for Rab3 subfamily (RAB3A, RAB3B, RAB3C and RAB3D). Rab3 proteins are involved in regulated exocytosis of neurotransmitters and hormones. Specifically converts active Rab3-GTP to the inactive form Rab3-GDP. Required for normal eye and brain development. May participate in neurodevelopmental processes such as proliferation, migration and differentiation before synapse formation, and non-synaptic vesicular release of neurotransmitters (By similarity)..
Protein Sequence MAADSEPESEVFEITDFTTASEWERFISKVEEVLNDWKLIGPSLGKPLEKGIFTSGTWEERSDEISFADFRFSVTHHYLVQESPDKERKDEELEDAIPQSMQDLLCMNNDFPPRAHCLVRWYGLREFVVIAPAAHSDAVLSESKCNLLLSSISIALGNTGCQVPLFVQIHHKWRRMYMGECQGPGVRTDFEMVHLRKVPSQYTHLSGLLDIFKSKIGCPLTPLPPVSIAIRLTYVLQDWQQYFWPQQPPDIDALVGGEVGGLEFGKLPFGACEDPISELHLATTWPHLTEGIIVDNDVYSDLDPVQAPHWSVRVRKADNPQCLLGDFVTEFLKICRRKESTDEILGRSTFEEEGREVADITHALSKLTEPAPVPIHKLSVSNMVHTAKKKIRKHRGEESPLNSDVLNTILLFLFPDAVSEKPLDGTTSIDNSIPAPEAGDYTLYNQFKSAPSDSLTYKLALCLCMINFYHGGLKGVAHLWQEFVLEMRFRWENNFLIPGLASGSPDLRCCLLHQKLQMLNCCIERKKARDEGKKTSLSDSTTSAYPGDAGKTGGQLGLDHLRDTEKEKGEVGKSWDSWSDSEEEFFECLSDTEDLKGNGQESGKKGGPKEMANLKPEGRLHQHGKLTLLHNGEPLYIPVTQEPAPMTEDLLEEQSEVLAKLGTSAEGAHLRARMQSACLLSDMESFKAANPGCFLEDFVRWYSPRDYIEEEVTDEKGNVVLKGELSARMKIPSNMWVEAWETAKPVPARRQRRLFDDTREAEKVLHYLAMQKPADLARHLLPCVIHAAVLKVKEEESLENIPSVKKIIKQIIAHSSKVLHFPNPEDKKLEEIILQITTVEAIIARARSLKAKFGTEKCEHEEEKEGLERFVSCLLEQPEVSVTGAGRGHAGRIIHKLFVNAQRAAAVALPEEELKKSGCPEERRQTLVSDFPPPAGRELILRATVPRPAPYSKALPQRMYSVLTKEDFRLAGAFSSDTSFF
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
5Phosphorylation---MAADSEPESEVF
---CCCCCCCHHHEE
50.7727180971
9PhosphorylationAADSEPESEVFEITD
CCCCCCHHHEEEECC
50.1821743459
15PhosphorylationESEVFEITDFTTASE
HHHEEEECCCCCHHH
20.1925293948
18PhosphorylationVFEITDFTTASEWER
EEEECCCCCHHHHHH
25.0220415495
19PhosphorylationFEITDFTTASEWERF
EEECCCCCHHHHHHH
28.3420415495
21PhosphorylationITDFTTASEWERFIS
ECCCCCHHHHHHHHH
40.9420415495
28PhosphorylationSEWERFISKVEEVLN
HHHHHHHHHHHHHHC
28.1225619855
38UbiquitinationEEVLNDWKLIGPSLG
HHHHCCCCCCCCCCC
32.84-
43PhosphorylationDWKLIGPSLGKPLEK
CCCCCCCCCCCCCCC
44.5325619855
83PhosphorylationHHYLVQESPDKERKD
EEEECCCCCCHHHCH
22.7025521595
181S-nitrosocysteineRRMYMGECQGPGVRT
HHHHCCCCCCCCCCC
4.73-
181S-nitrosylationRRMYMGECQGPGVRT
HHHHCCCCCCCCCCC
4.7321278135
322S-nitrosocysteineRKADNPQCLLGDFVT
ECCCCCCCCHHHHHH
3.41-
322S-nitrosylationRKADNPQCLLGDFVT
ECCCCCCCCHHHHHH
3.4122178444
340PhosphorylationKICRRKESTDEILGR
HHHCCCCCCCHHHCC
44.1629899451
379PhosphorylationPVPIHKLSVSNMVHT
CCCCHHCCHHHHHHH
28.4425266776
381PhosphorylationPIHKLSVSNMVHTAK
CCHHCCHHHHHHHHH
18.8124719451
535PhosphorylationARDEGKKTSLSDSTT
HHHCCCCCCCCCCCC
38.0825521595
536PhosphorylationRDEGKKTSLSDSTTS
HHCCCCCCCCCCCCC
34.4525521595
538PhosphorylationEGKKTSLSDSTTSAY
CCCCCCCCCCCCCCC
29.3127087446
540PhosphorylationKKTSLSDSTTSAYPG
CCCCCCCCCCCCCCC
30.1525619855
541PhosphorylationKTSLSDSTTSAYPGD
CCCCCCCCCCCCCCC
29.7525619855
542PhosphorylationTSLSDSTTSAYPGDA
CCCCCCCCCCCCCCC
18.4725619855
543PhosphorylationSLSDSTTSAYPGDAG
CCCCCCCCCCCCCCC
26.3725619855
545PhosphorylationSDSTTSAYPGDAGKT
CCCCCCCCCCCCCCC
13.9125619855
574PhosphorylationEKGEVGKSWDSWSDS
HCCCCCCCCCCCCCC
30.1322817900
577PhosphorylationEVGKSWDSWSDSEEE
CCCCCCCCCCCCHHH
23.4029550500
579PhosphorylationGKSWDSWSDSEEEFF
CCCCCCCCCCHHHHH
34.9022817900
581PhosphorylationSWDSWSDSEEEFFEC
CCCCCCCCHHHHHHH
41.2022817900
590PhosphorylationEEFFECLSDTEDLKG
HHHHHHHHCCCCCCC
54.8929550500
592PhosphorylationFFECLSDTEDLKGNG
HHHHHHCCCCCCCCC
28.2029550500
663PhosphorylationEVLAKLGTSAEGAHL
HHHHHHCCCCHHHHH
34.8930635358
664PhosphorylationVLAKLGTSAEGAHLR
HHHHHCCCCHHHHHH
23.6430635358
673MethylationEGAHLRARMQSACLL
HHHHHHHHHHHHHHH
19.7616189003
678S-palmitoylationRARMQSACLLSDMES
HHHHHHHHHHCCHHH
4.8128680068
700MethylationCFLEDFVRWYSPRDY
CCHHHHHHHCCHHHH
26.9716189013
793AcetylationHAAVLKVKEEESLEN
HHHHHHHCCHHHHCC
58.7923954790
858S-nitrosylationAKFGTEKCEHEEEKE
HHHCCCCCCCHHHHH
5.4121278135
858S-nitrosocysteineAKFGTEKCEHEEEKE
HHHCCCCCCCHHHHH
5.41-
872PhosphorylationEGLERFVSCLLEQPE
HHHHHHHHHHHHCCC
9.0629899451
873GlutathionylationGLERFVSCLLEQPEV
HHHHHHHHHHHCCCE
4.1724333276
881PhosphorylationLLEQPEVSVTGAGRG
HHHCCCEEECCCCCC
16.5829899451
883PhosphorylationEQPEVSVTGAGRGHA
HCCCEEECCCCCCHH
17.5129899451
944PhosphorylationRELILRATVPRPAPY
CEEEEEEECCCCCCC
25.3024719451
960PhosphorylationKALPQRMYSVLTKED
CCCCHHHHHHHCHHH
9.60-

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 RB3GP_MOUSE !!

Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of RB3GP_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 RB3GP_MOUSE !!

Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
RBG10_HUMANRABGAP1Lphysical
26496610
RBG1L_HUMANRABGAP1Lphysical
26496610
SRRT_HUMANSRRTphysical
26496610
CCD94_HUMANCCDC94physical
26496610
DEFM_HUMANPDFphysical
26496610
ZC3HE_HUMANZC3H14physical
26496610

Drug and Disease Associations
Kegg Drug
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of RB3GP_MOUSE

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Related Literatures of Post-Translational Modification

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