RBGPR_HUMAN - dbPTM
RBGPR_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID RBGPR_HUMAN
UniProt AC Q9H2M9
Protein Name Rab3 GTPase-activating protein non-catalytic subunit
Gene Name RAB3GAP2
Organism Homo sapiens (Human).
Sequence Length 1393
Subcellular Localization Cytoplasm. In neurons, it is enriched in the synaptic soluble fraction.
Protein Description Regulatory 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. Rab3 GTPase-activating complex 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 MACSIVQFCYFQDLQAARDFLFPHLREEILSGALRRDPSKSTDWEDDGWGAWEENEPQEPEEEGNTCKTQKTSWLQDCVLSLSPTNDLMVIAREQKAVFLVPKWKYSDKGKEEMQFAVGWSGSLNVEEGECVTSALCIPLASQKRSSTGRPDWTCIVVGFTSGYVRFYTENGVLLLAQLLNEDPVLQLKCRTYEIPRHPGVTEQNEELSILYPAAIVTIDGFSLFQSLRACRNQVAKAAASGNENIQPPPLAYKKWGLQDIDTIIDHASVGIMTLSPFDQMKTASNIGGFNAAIKNSPPAMSQYITVGSNPFTGFFYALEGSTQPLLSHVALAVASKLTSALFNAASGWLGWKSKHEEEAVQKQKPKVEPATPLAVRFGLPDSRRHGESICLSPCNTLAAVTDDFGRVILLDVARGIAIRMWKGYRDAQIGWIQTVEDLHERVPEKADFSPFGNSQGPSRVAQFLVIYAPRRGILEVWSTQQGPRVGAFNVGKHCRLLYPGYKIMGLNNVTSQSWQPQTYQICLVDPVSGSVKTVNVPFHLALSDKKSERAKDMHLVKKLAALLKTKSPNLDLVETEIKELILDIKYPATKKQALESILASERLPFSCLRNITQTLMDTLKSQELESVDEGLLQFCANKLKLLQLYESVSQLNSLDFHLDTPFSDNDLALLLRLDEKELLKLQALLEKYKQENTRTNVRFSDDKDGVLPVKTFLEYLEYEKDVLNIKKISEEEYVALGSFFFWKCLHGESSTEDMCHTLESAGLSPQLLLSLLLSVWLSKEKDILDKPQSICCLHTMLSLLSKMKVAIDETWDSQSVSPWWQQMRTACIQSENNGAALLSAHVGHSVAAQISNNMTEKKFSQTVLGADSEALTDSWEALSLDTEYWKLLLKQLEDCLILQTLLHSKGNTQTSKVSSLQAEPLPRLSVKKLLEGGKGGIADSVAKWIFKQDFSPEVLKLANEERDAENPDEPKEGVNRSFLEVSEMEMDLGAIPDLLHLAYEQFPCSLELDVLHAHCCWEYVVQWNKDPEEARFFVRSIEHLKQIFNAHVQNGIALMMWNTFLVKRFSAATYLMDKVGKSPKDRLCRRDVGMSDTAMTSFLGSCLDLLQILMEADVSRDEIQVPVLDTEDAWLSVEGPISIVELALEQKHIHYPLVEHHSILCSILYAVMRFSLKTVKPLSLFDSKGKNAFFKDLTSIQLLPSGEMDPNFISVRQQFLLKVVSAAVQAQHSATKVKDPTEEATPTPFGKDQDWPALAVDLAHHLQVSEDVVRRHYVGELYNYGVDHLGEEAILQVHDKEVLASQLLVLTGQRLAHALLHTQTKEGMELLARLPPTLCTWLKAMDPQDLQNTEVPIATTAKLVNKVIELLPEKHGQYGLALHLIEAVEAISLPSL
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
31PhosphorylationHLREEILSGALRRDP
HHHHHHHHHHHCCCC
27.9021815630
39PhosphorylationGALRRDPSKSTDWED
HHHCCCCCCCCCCCC
43.4528450419
41PhosphorylationLRRDPSKSTDWEDDG
HCCCCCCCCCCCCCC
35.6228450419
42PhosphorylationRRDPSKSTDWEDDGW
CCCCCCCCCCCCCCC
49.2028450419
66PhosphorylationEPEEEGNTCKTQKTS
CCCCCCCCCCCCCCH
26.6623312004
68UbiquitinationEEEGNTCKTQKTSWL
CCCCCCCCCCCCHHH
52.5322817900
71UbiquitinationGNTCKTQKTSWLQDC
CCCCCCCCCHHHHHH
50.1621963094
83PhosphorylationQDCVLSLSPTNDLMV
HHHHHCCCCCCCEEE
26.71-
96UbiquitinationMVIAREQKAVFLVPK
EEEEECCEEEEEEEC
41.59-
103UbiquitinationKAVFLVPKWKYSDKG
EEEEEEECCCCCCCC
49.16-
227PhosphorylationDGFSLFQSLRACRNQ
CCHHHHHHHHHHHHH
16.7024719451
254UbiquitinationQPPPLAYKKWGLQDI
CCCCCCCCCCCCCCH
36.1229967540
255UbiquitinationPPPLAYKKWGLQDID
CCCCCCCCCCCCCHH
33.54-
274PhosphorylationHASVGIMTLSPFDQM
HCCEEEEEECHHHHC
23.3622210691
363UbiquitinationHEEEAVQKQKPKVEP
HHHHHHHHHCCCCCC
54.4030230243
372PhosphorylationKPKVEPATPLAVRFG
CCCCCCCCCCCHHCC
29.5628674419
423UbiquitinationGIAIRMWKGYRDAQI
HHHHHCCCCCHHHCC
36.40-
446UbiquitinationLHERVPEKADFSPFG
HHHHCCCCCCCCCCC
47.3827667366
446 (in isoform 1)Ubiquitination-47.3821890473
450PhosphorylationVPEKADFSPFGNSQG
CCCCCCCCCCCCCCC
21.6223401153
455PhosphorylationDFSPFGNSQGPSRVA
CCCCCCCCCCHHHHH
36.5725850435
459PhosphorylationFGNSQGPSRVAQFLV
CCCCCCHHHHHHEEE
46.3326552605
493UbiquitinationVGAFNVGKHCRLLYP
CEEEECCCCEEEECC
34.94-
544PhosphorylationVPFHLALSDKKSERA
CCEEEECCCCCCHHH
41.6025159151
546UbiquitinationFHLALSDKKSERAKD
EEEECCCCCCHHHHH
55.6229967540
547UbiquitinationHLALSDKKSERAKDM
EEECCCCCCHHHHHH
63.64-
559UbiquitinationKDMHLVKKLAALLKT
HHHHHHHHHHHHHHC
35.56-
565UbiquitinationKKLAALLKTKSPNLD
HHHHHHHHCCCCCCC
55.5529967540
566PhosphorylationKLAALLKTKSPNLDL
HHHHHHHCCCCCCCC
36.4028348404
567AcetylationLAALLKTKSPNLDLV
HHHHHHCCCCCCCCC
63.437661925
567UbiquitinationLAALLKTKSPNLDLV
HHHHHHCCCCCCCCC
63.4333845483
568PhosphorylationAALLKTKSPNLDLVE
HHHHHCCCCCCCCCH
25.0128348404
592UbiquitinationIKYPATKKQALESIL
CCCCCCHHHHHHHHH
36.1330230243
601PhosphorylationALESILASERLPFSC
HHHHHHHHCCCCHHH
21.5824719451
607PhosphorylationASERLPFSCLRNITQ
HHCCCCHHHHHHHHH
15.4220068231
639UbiquitinationLLQFCANKLKLLQLY
HHHHHHHHHHHHHHH
28.5929967540
641UbiquitinationQFCANKLKLLQLYES
HHHHHHHHHHHHHHH
49.08-
677UbiquitinationLLLRLDEKELLKLQA
HHHHCCHHHHHHHHH
54.0229967540
681UbiquitinationLDEKELLKLQALLEK
CCHHHHHHHHHHHHH
51.7029967540
688UbiquitinationKLQALLEKYKQENTR
HHHHHHHHHHHHCCC
58.6929967540
704UbiquitinationNVRFSDDKDGVLPVK
CCCCCCCCCCEEEHH
62.4630230243
711UbiquitinationKDGVLPVKTFLEYLE
CCCEEEHHHHHHHHH
31.4529967540
721UbiquitinationLEYLEYEKDVLNIKK
HHHHHHHHCCCCCCC
52.8429967540
727UbiquitinationEKDVLNIKKISEEEY
HHCCCCCCCCCHHHH
42.8729967540
799PhosphorylationCCLHTMLSLLSKMKV
HHHHHHHHHHHHCCH
19.2224719451
811PhosphorylationMKVAIDETWDSQSVS
CCHHHCCCCCCCCCC
30.7227732954
814PhosphorylationAIDETWDSQSVSPWW
HHCCCCCCCCCCHHH
18.8627732954
816PhosphorylationDETWDSQSVSPWWQQ
CCCCCCCCCCHHHHH
28.6327732954
818PhosphorylationTWDSQSVSPWWQQMR
CCCCCCCCHHHHHHH
21.7627251275
852PhosphorylationHSVAAQISNNMTEKK
HHHHHHHCCCCCCCC
15.2924719451
861PhosphorylationNMTEKKFSQTVLGAD
CCCCCCCHHHHHCCC
33.5528270605
863PhosphorylationTEKKFSQTVLGADSE
CCCCCHHHHHCCCHH
19.2527732954
869PhosphorylationQTVLGADSEALTDSW
HHHHCCCHHHHHCHH
25.0027732954
873PhosphorylationGADSEALTDSWEALS
CCCHHHHHCHHHHHH
34.7328450419
875PhosphorylationDSEALTDSWEALSLD
CHHHHHCHHHHHHCC
22.9129507054
880PhosphorylationTDSWEALSLDTEYWK
HCHHHHHHCCHHHHH
31.1127732954
883PhosphorylationWEALSLDTEYWKLLL
HHHHHCCHHHHHHHH
35.9528270605
885PhosphorylationALSLDTEYWKLLLKQ
HHHCCHHHHHHHHHH
15.2228270605
901PhosphorylationEDCLILQTLLHSKGN
HHHHHHHHHHHCCCC
28.0422817900
906UbiquitinationLQTLLHSKGNTQTSK
HHHHHHCCCCCCCCC
45.4929967540
909PhosphorylationLLHSKGNTQTSKVSS
HHHCCCCCCCCCCHH
41.7226074081
911PhosphorylationHSKGNTQTSKVSSLQ
HCCCCCCCCCCHHCC
28.6026074081
912PhosphorylationSKGNTQTSKVSSLQA
CCCCCCCCCCHHCCC
22.6526074081
913UbiquitinationKGNTQTSKVSSLQAE
CCCCCCCCCHHCCCC
49.9121890473
913UbiquitinationKGNTQTSKVSSLQAE
CCCCCCCCCHHCCCC
49.9127667366
913 (in isoform 1)Ubiquitination-49.9121890473
915PhosphorylationNTQTSKVSSLQAEPL
CCCCCCCHHCCCCCC
29.1229632367
916PhosphorylationTQTSKVSSLQAEPLP
CCCCCCHHCCCCCCC
27.7329632367
926PhosphorylationAEPLPRLSVKKLLEG
CCCCCCCCHHHHHHC
32.9226074081
929UbiquitinationLPRLSVKKLLEGGKG
CCCCCHHHHHHCCCC
57.0329967540
935AcetylationKKLLEGGKGGIADSV
HHHHHCCCCCHHHHH
65.8926051181
935UbiquitinationKKLLEGGKGGIADSV
HHHHHCCCCCHHHHH
65.8932015554
941PhosphorylationGKGGIADSVAKWIFK
CCCCHHHHHHHHHHC
18.2328102081
944UbiquitinationGIADSVAKWIFKQDF
CHHHHHHHHHHCCCC
38.37-
948UbiquitinationSVAKWIFKQDFSPEV
HHHHHHHCCCCCHHH
39.5632015554
952PhosphorylationWIFKQDFSPEVLKLA
HHHCCCCCHHHHHHH
28.5721815630
957UbiquitinationDFSPEVLKLANEERD
CCCHHHHHHHHHCHH
51.2132015554
963MethylationLKLANEERDAENPDE
HHHHHHCHHCCCCCC
42.11115489921
972UbiquitinationAENPDEPKEGVNRSF
CCCCCCCCCCCCHHH
66.1224816145
978PhosphorylationPKEGVNRSFLEVSEM
CCCCCCHHHHHHHHH
29.04-
1092PhosphorylationCRRDVGMSDTAMTSF
CCCCCCCCHHHHHHH
26.3624043423
1094PhosphorylationRDVGMSDTAMTSFLG
CCCCCCHHHHHHHHH
15.8324043423
1097PhosphorylationGMSDTAMTSFLGSCL
CCCHHHHHHHHHHHH
17.5424043423
1098PhosphorylationMSDTAMTSFLGSCLD
CCHHHHHHHHHHHHH
12.8524043423
1102PhosphorylationAMTSFLGSCLDLLQI
HHHHHHHHHHHHHHH
17.4124043423
1116PhosphorylationILMEADVSRDEIQVP
HHHHCCCCCCCCCCC
34.2624043423
1152PhosphorylationLEQKHIHYPLVEHHS
HHCCCCCCCHHHHHH
9.5422817900
1166PhosphorylationSILCSILYAVMRFSL
HHHHHHHHHHHHHCC
8.7622817900
1175PhosphorylationVMRFSLKTVKPLSLF
HHHHCCCCCCCHHHC
38.77-
1177MalonylationRFSLKTVKPLSLFDS
HHCCCCCCCHHHCCC
45.5332601280
1180PhosphorylationLKTVKPLSLFDSKGK
CCCCCCHHHCCCCCC
35.2023312004
1184PhosphorylationKPLSLFDSKGKNAFF
CCHHHCCCCCCCCCC
35.6523312004
1185UbiquitinationPLSLFDSKGKNAFFK
CHHHCCCCCCCCCCC
75.6229967540
1219UbiquitinationVRQQFLLKVVSAAVQ
HHHHHHHHHHHHHHH
42.6230230243
1233UbiquitinationQAQHSATKVKDPTEE
HHHHHCCCCCCCCCC
47.1832015554
1235UbiquitinationQHSATKVKDPTEEAT
HHHCCCCCCCCCCCC
60.5929967540
1238PhosphorylationATKVKDPTEEATPTP
CCCCCCCCCCCCCCC
57.5023312004
1242PhosphorylationKDPTEEATPTPFGKD
CCCCCCCCCCCCCCC
30.8625159151
1244PhosphorylationPTEEATPTPFGKDQD
CCCCCCCCCCCCCCC
27.2223312004
1322UbiquitinationALLHTQTKEGMELLA
HHHHCCCHHHHHHHH
42.3121963094
1359UbiquitinationVPIATTAKLVNKVIE
CCHHHHHHHHHHHHH
51.3723000965
1363UbiquitinationTTAKLVNKVIELLPE
HHHHHHHHHHHHCHH
36.7921890473
1363UbiquitinationTTAKLVNKVIELLPE
HHHHHHHHHHHHCHH
36.7923000965
1363 (in isoform 1)Ubiquitination-36.7921890473

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 RBGPR_HUMAN !!

Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of RBGPR_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 RBGPR_HUMAN !!

Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
RBM26_HUMANRBM26physical
22939629
UTP20_HUMANUTP20physical
22939629
RB3GP_HUMANRAB3GAP1physical
26344197

Drug and Disease Associations
Kegg Disease
There are no disease associations of PTM sites.
OMIM Disease
212720Martsolf syndrome (MARTS)
614225Warburg micro syndrome 2 (WARBM2)
Kegg Drug
There are no disease associations of PTM sites.
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of RBGPR_HUMAN

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Related Literatures of Post-Translational Modification
Phosphorylation
ReferencePubMed
"A quantitative atlas of mitotic phosphorylation.";
Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,Elledge S.J., Gygi S.P.;
Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-450, AND MASSSPECTROMETRY.
"Phosphoproteome of resting human platelets.";
Zahedi R.P., Lewandrowski U., Wiesner J., Wortelkamp S., Moebius J.,Schuetz C., Walter U., Gambaryan S., Sickmann A.;
J. Proteome Res. 7:526-534(2008).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-901, AND MASSSPECTROMETRY.

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