RB3GP_HUMAN - dbPTM
RB3GP_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID RB3GP_HUMAN
UniProt AC Q15042
Protein Name Rab3 GTPase-activating protein catalytic subunit
Gene Name RAB3GAP1
Organism Homo sapiens (Human).
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..
Protein Sequence MAADSEPESEVFEITDFTTASEWERFISKVEEVLNDWKLIGNSLGKPLEKGIFTSGTWEEKSDEISFADFKFSVTHHYLVQESTDKEGKDELLEDVVPQSMQDLLGMNNDFPPRAHCLVRWYGLREFVVIAPAAHSDAVLSESKCNLLLSSVSIALGNTGCQVPLFVQIHHKWRRMYVGECQGPGVRTDFEMVHLRKVPNQYTHLSGLLDIFKSKIGCPLTPLPPVSIAIRFTYVLQDWQQYFWPQQPPDIDALVGGEVGGLEFGKLPFGACEDPISELHLATTWPHLTEGIIVDNDVYSDLDPIQAPHWSVRVRKAENPQCLLGDFVTEFFKICRRKESTDEILGRSAFEEEGKETADITHALSKLTEPASVPIHKLSVSNMVHTAKKKIRKHRGVEESPLNNDVLNTILLFLFPDAVSEKPLDGTTSTDNNNPPSESEDYNLYNQFKSAPSDSLTYKLALCLCMINFYHGGLKGVAHLWQEFVLEMRFRWENNFLIPGLASGPPDLRCCLLHQKLQMLNCCIERKKARDEGKKTSASDVTNIYPGDAGKAGDQLVPDNLKETDKEKGEVGKSWDSWSDSEEEFFECLSDTEELKGNGQESGKKGGPKEMANLRPEGRLYQHGKLTLLHNGEPLYIPVTQEPAPMTEDLLEEQSEVLAKLGTSAEGAHLRARMQSACLLSDMESFKAANPGCSLEDFVRWYSPRDYIEEEVIDEKGNVVLKGELSARMKIPSNMWVEAWETAKPIPARRQRRLFDDTREAEKVLHYLAIQKPADLARHLLPCVIHAAVLKVKEEESLENISSVKKIIKQIISHSSKVLHFPNPEDKKLEEIIHQITNVEALIARARSLKAKFGTEKCEQEEEKEDLERFVSCLLEQPEVLVTGAGRGHAGRIIHKLFVNAQRAAAMTPPEEELKRMGSPEERRQNSVSDFPPPAGREFILRTTVPRPAPYSKALPQRMYSVLTKEDFRLAGAFSSDTSFF
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		50.7722496350
9PhosphorylationAADSEPESEVFEITD
CCCCCCHHHEEEECC		50.1822496350
15PhosphorylationESEVFEITDFTTASE
HHHEEEECCCCCHHH		20.1927732954
18PhosphorylationVFEITDFTTASEWER
EEEECCCCCHHHHHH		25.0227732954
29UbiquitinationEWERFISKVEEVLND
HHHHHHHHHHHHHHC		49.18-
29UbiquitinationEWERFISKVEEVLND
HHHHHHHHHHHHHHC		49.18-
38UbiquitinationEEVLNDWKLIGNSLG
HHHHHCCHHHCCCCC		32.8421890473
38UbiquitinationEEVLNDWKLIGNSLG
HHHHHCCHHHCCCCC		32.8421890473
46UbiquitinationLIGNSLGKPLEKGIF
HHCCCCCCCCCCCCC		52.2821890473
46UbiquitinationLIGNSLGKPLEKGIF
HHCCCCCCCCCCCCC		52.2821906983
46 (in isoform 1)Ubiquitination-52.2821890473
50UbiquitinationSLGKPLEKGIFTSGT
CCCCCCCCCCCCCCC		66.0621890473
50UbiquitinationSLGKPLEKGIFTSGT
CCCCCCCCCCCCCCC		66.0621890473
50 (in isoform 1)Ubiquitination-66.0621890473
66PhosphorylationEEKSDEISFADFKFS
CCCCCCCEECCEEEE		16.6023312004
83PhosphorylationHHYLVQESTDKEGKD
EEEEEECCCCCCCCH		25.47-
153UbiquitinationNLLLSSVSIALGNTG
HHHHHHHHHHCCCCC		12.23-
171UbiquitinationPLFVQIHHKWRRMYV
CEEEEEECCCCCEEC		32.76-
188PhosphorylationCQGPGVRTDFEMVHL
CCCCCCCCCEEEEEE		42.51-
197UbiquitinationFEMVHLRKVPNQYTH
EEEEEEECCCCHHCC		69.29-
197UbiquitinationFEMVHLRKVPNQYTH
EEEEEEECCCCHHCC		69.29-
215UbiquitinationLLDIFKSKIGCPLTP
HHHHHHHCCCCCCCC		43.65-
215UbiquitinationLLDIFKSKIGCPLTP
HHHHHHHCCCCCCCC		43.65-
272UbiquitinationGKLPFGACEDPISEL
CCCCCCCCCCCCHHH		6.62-
294UbiquitinationHLTEGIIVDNDVYSD
CCCCCEEECCCCCCC		5.48-
311UbiquitinationPIQAPHWSVRVRKAE
CCCCCCCEEEEECCC		9.30-
316UbiquitinationHWSVRVRKAENPQCL
CCEEEEECCCCCCCC		58.14-
316UbiquitinationHWSVRVRKAENPQCL
CCEEEEECCCCCCCC		58.14-
322UbiquitinationRKAENPQCLLGDFVT
ECCCCCCCCCHHHHH		3.41-
322GlutathionylationRKAENPQCLLGDFVT
ECCCCCCCCCHHHHH		3.4122555962
333UbiquitinationDFVTEFFKICRRKES
HHHHHHHHHHCCCCC		46.33-
338UbiquitinationFFKICRRKESTDEIL
HHHHHCCCCCHHHHH		36.34-
338UbiquitinationFFKICRRKESTDEIL
HHHHHCCCCCHHHHH		36.3421906983
338 (in isoform 1)Ubiquitination-36.3421890473
340PhosphorylationKICRRKESTDEILGR
HHHCCCCCHHHHHCC		44.1625850435
341PhosphorylationICRRKESTDEILGRS
HHCCCCCHHHHHCCH		38.4525850435
345UbiquitinationKESTDEILGRSAFEE
CCCHHHHHCCHHHHH		4.36-
348PhosphorylationTDEILGRSAFEEEGK
HHHHHCCHHHHHCCH		35.2030108239
355UbiquitinationSAFEEEGKETADITH
HHHHHCCHHHHHHHH		55.99-
355UbiquitinationSAFEEEGKETADITH
HHHHHCCHHHHHHHH		55.99-
357PhosphorylationFEEEGKETADITHAL
HHHCCHHHHHHHHHH		32.8728555341
365PhosphorylationADITHALSKLTEPAS
HHHHHHHHHCCCCCC		26.8027251275
366UbiquitinationDITHALSKLTEPASV
HHHHHHHHCCCCCCC		61.35-
366UbiquitinationDITHALSKLTEPASV
HHHHHHHHCCCCCCC		61.35-
368PhosphorylationTHALSKLTEPASVPI
HHHHHHCCCCCCCCH		43.5923898821
372PhosphorylationSKLTEPASVPIHKLS
HHCCCCCCCCHHHCC		38.8623898821
377UbiquitinationPASVPIHKLSVSNMV
CCCCCHHHCCHHHHH		43.08-
377UbiquitinationPASVPIHKLSVSNMV
CCCCCHHHCCHHHHH		43.08-
379PhosphorylationSVPIHKLSVSNMVHT
CCCHHHCCHHHHHHH		28.4426657352
381PhosphorylationPIHKLSVSNMVHTAK
CHHHCCHHHHHHHHH		18.8123312004
386PhosphorylationSVSNMVHTAKKKIRK
CHHHHHHHHHHHHHH		28.8525159151
388UbiquitinationSNMVHTAKKKIRKHR
HHHHHHHHHHHHHHC		56.61-
389UbiquitinationNMVHTAKKKIRKHRG
HHHHHHHHHHHHHCC		51.47-
400PhosphorylationKHRGVEESPLNNDVL
HHCCCCCCCCCHHHH		22.6025159151
449UbiquitinationYNLYNQFKSAPSDSL
CCHHHHHHCCCCCCH		35.62-
450PhosphorylationNLYNQFKSAPSDSLT
CHHHHHHCCCCCCHH		46.85-
475SumoylationNFYHGGLKGVAHLWQ
HHHHCCHHHHHHHHH		55.39-
527AcetylationLNCCIERKKARDEGK
HHHHHHHHHHHHCCC		37.697677719
534AcetylationKKARDEGKKTSASDV
HHHHHCCCCCCHHHC		51.327677729
535UbiquitinationKARDEGKKTSASDVT
HHHHCCCCCCHHHCC		59.58-
536PhosphorylationARDEGKKTSASDVTN
HHHCCCCCCHHHCCC		32.7723401153
537PhosphorylationRDEGKKTSASDVTNI
HHCCCCCCHHHCCCC		34.3525159151
539PhosphorylationEGKKTSASDVTNIYP
CCCCCCHHHCCCCCC		32.1723927012
542PhosphorylationKTSASDVTNIYPGDA
CCCHHHCCCCCCCCC		22.3823927012
545PhosphorylationASDVTNIYPGDAGKA
HHHCCCCCCCCCCCC		11.8423403867
562UbiquitinationQLVPDNLKETDKEKG
CCCCCCCCCCCHHCC		65.90-
574PhosphorylationEKGEVGKSWDSWSDS
HCCCCCCCCCCCCCC		30.1325137130
577PhosphorylationEVGKSWDSWSDSEEE
CCCCCCCCCCCCHHH		23.4025137130
579PhosphorylationGKSWDSWSDSEEEFF
CCCCCCCCCCHHHHH		34.9025137130
581PhosphorylationSWDSWSDSEEEFFEC
CCCCCCCCHHHHHHH		41.2025137130
590PhosphorylationEEFFECLSDTEELKG
HHHHHHHCCHHHHCC		54.8928102081
592PhosphorylationFFECLSDTEELKGNG
HHHHHCCHHHHCCCC		28.1626074081
663PhosphorylationEVLAKLGTSAEGAHL
HHHHHHCCCCHHHHH		34.8929255136
664PhosphorylationVLAKLGTSAEGAHLR
HHHHHCCCCHHHHHH		23.6429255136
676PhosphorylationHLRARMQSACLLSDM
HHHHHHHHHHHHCCH		16.1725850435
678GlutathionylationRARMQSACLLSDMES
HHHHHHHHHHCCHHH		4.8122555962
728UbiquitinationLKGELSARMKIPSNM
EEEEEECCCCCCCCC		24.45-
772UbiquitinationLHYLAIQKPADLARH
HHHHHHCCHHHHHHH		35.74-
772UbiquitinationLHYLAIQKPADLARH
HHHHHHCCHHHHHHH		35.74-
8052-HydroxyisobutyrylationLENISSVKKIIKQII
HCCHHHHHHHHHHHH		39.96-
805UbiquitinationLENISSVKKIIKQII
HCCHHHHHHHHHHHH		39.96-
809MalonylationSSVKKIIKQIISHSS
HHHHHHHHHHHHCCC		38.6326320211
809UbiquitinationSSVKKIIKQIISHSS
HHHHHHHHHHHHCCC		38.63-
813UbiquitinationKIIKQIISHSSKVLH
HHHHHHHHCCCCCCC		20.95-
817UbiquitinationQIISHSSKVLHFPNP
HHHHCCCCCCCCCCH		52.40-
852UbiquitinationRARSLKAKFGTEKCE
HHHHHHHHHCCHHCC		42.62-
857UbiquitinationKAKFGTEKCEQEEEK
HHHHCCHHCCHHHHH		42.80-
857UbiquitinationKAKFGTEKCEQEEEK
HHHHCCHHCCHHHHH		42.80-
871UbiquitinationKEDLERFVSCLLEQP
HHHHHHHHHHHHHCC		5.04-
873GlutathionylationDLERFVSCLLEQPEV
HHHHHHHHHHHCCCE		4.1722555962
887MethylationVLVTGAGRGHAGRII
EEEECCCCCHHHHHH		32.9454558467
892MethylationAGRGHAGRIIHKLFV
CCCCHHHHHHHHHHH		26.0254558475
896UbiquitinationHAGRIIHKLFVNAQR
HHHHHHHHHHHCHHH		32.9621890473
896UbiquitinationHAGRIIHKLFVNAQR
HHHHHHHHHHHCHHH		32.9621890473
896 (in isoform 1)Ubiquitination-32.9621890473
908PhosphorylationAQRAAAMTPPEEELK
HHHHHHCCCCHHHHH		30.8525159151
909UbiquitinationQRAAAMTPPEEELKR
HHHHHCCCCHHHHHH		22.63-
915UbiquitinationTPPEEELKRMGSPEE
CCCHHHHHHCCCHHH		43.55-
915 (in isoform 3)Phosphorylation-43.5524076635
919PhosphorylationEELKRMGSPEERRQN
HHHHHCCCHHHHHHC		21.5729255136
921UbiquitinationLKRMGSPEERRQNSV
HHHCCCHHHHHHCCC		66.87-
922UbiquitinationKRMGSPEERRQNSVS
HHCCCHHHHHHCCCC		57.45-
927PhosphorylationPEERRQNSVSDFPPP
HHHHHHCCCCCCCCC		18.0524670416
929PhosphorylationERRQNSVSDFPPPAG
HHHHCCCCCCCCCCC		33.1023312004
953UbiquitinationPRPAPYSKALPQRMY
CCCCCCCCCCCHHHH		48.3621890473
953UbiquitinationPRPAPYSKALPQRMY
CCCCCCCCCCCHHHH		48.362189047
953 (in isoform 1)Ubiquitination-48.3621890473
965UbiquitinationRMYSVLTKEDFRLAG
HHHHHHCHHHHHHHC		51.64-
972UbiquitinationKEDFRLAGAFSSDTS
HHHHHHHCCCCCCCC		31.57-
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_HUMAN !!
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of RB3GP_HUMAN !!
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_HUMAN !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
RPH3L_HUMANRPH3ALphysical
14593078
WDR7_HUMANWDR7physical
12786944
DMXL2_HUMANDMXL2physical
12786944
RB22A_HUMANRAB22Aphysical
16923123
RB39A_HUMANRAB39Aphysical
16923123
RB39B_HUMANRAB39Bphysical
16923123
RBGPR_HUMANRAB3GAP2physical
22863883
SEN34_HUMANTSEN34physical
22863883
RBGPR_HUMANRAB3GAP2physical
24885147
VAPB_HUMANVAPBphysical
24885147
Drug and Disease Associations
Kegg Disease
There are no disease associations of PTM sites.
OMIM Disease
600118Warburg micro syndrome 1 (WARBM1)
Kegg Drug
There are no disease associations of PTM sites.
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of RB3GP_HUMAN

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Related Literatures of Post-Translational Modification
Phosphorylation
ReferencePubMed
"Global, in vivo, and site-specific phosphorylation dynamics insignaling networks.";
Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P.,Mann M.;
Cell 127:635-648(2006).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-579; SER-581 ANDSER-590, AND MASS SPECTROMETRY.

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