RLGPB_HUMAN - dbPTM
RLGPB_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID RLGPB_HUMAN
UniProt AC Q86X10
Protein Name Ral GTPase-activating protein subunit beta
Gene Name RALGAPB
Organism Homo sapiens (Human).
Sequence Length 1494
Subcellular Localization
Protein Description Non-catalytic subunit of the heterodimeric RalGAP1 and RalGAP2 complexes which act as GTPase activators for the Ras-like small GTPases RALA and RALB..
Protein Sequence MYSEWRSLHLVIQNDQGHTSVLHSYPESVGREVANAVVRPLGQVLGTPSVAGSENLLKTDKEVKWTMEVICYGLTLPLDGETVKYCVDVYTDWIMALVLPKDSIPLPVIKEPNQYVQTILKHLQNLFVPRQEQGSSQIRLCLQVLRAIQKLARESSLMARETWEVLLLFLLQINDILLAPPTVQGGIAENLAEKLIGVLFEVWLLACTRCFPTPPYWKTAKEMVANWRHHPAVVEQWSKVICALTSRLLRFTYGPSFPAFKVPDEDASLIPPEMDNECVAQTWFRFLHMLSNPVDLSNPAIISSTPKFQEQFLNVSGMPQELNQYPCLKHLPQIFFRAMRGISCLVDAFLGISRPRSDSAPPTPVNRLSMPQSAAVSTTPPHNRRHRAVTVNKATMKTSTVSTAHASKVQHQTSSTSPLSSPNQTSSEPRPLPAPRRPKVNSILNLFGSWLFDAAFVHCKLHNGINRDSSMTAITTQASMEFRRKGSQMSTDTMVSNPMFDASEFPDNYEAGRAEACGTLCRIFCSKKTGEEILPAYLSRFYMLLIQGLQINDYVCHPVLASVILNSPPLFCCDLKGIDVVVPYFISALETILPDRELSKFKSYVNPTELRRSSINILLSLLPLPHHFGTVKSEVVLEGKFSNDDSSSYDKPITFLSLKLRLVNILIGALQTETDPNNTQMILGAMLNIVQDSALLEAIGCQMEMGGGENNLKSHSRTNSGISSASGGSTEPTTPDSERPAQALLRDYALNTDSAAGLLIRSIHLVTQRLNSQWRQDMSISLAALELLSGLAKVKVMVDSGDRKRAISSVCTYIVYQCSRPAPLHSRDLHSMIVAAFQCLCVWLTEHPDMLDEKDCLKEVLEIVELGISGSKSKNNEQEVKYKGDKEPNPASMRVKDAAEATLTCIMQLLGAFPSPSGPASPCSLVNETTLIKYSRLPTINKHSFRYFVLDNSVILAMLEQPLGNEQNDFFPSVTVLVRGMSGRLAWAQQLCLLPRGAKANQKLFVPEPRPVPKNDVGFKYSVKHRPFPEEVDKIPFVKADLSIPDLHEIVTEELEERHEKLRSGMAQQIAYEIHLEQQSEEELQKRSFPDPVTDCKPPPPAQEFQTARLFLSHFGFLSLEALKEPANSRLPPHLIALDSTIPGFFDDIGYLDLLPCRPFDTVFIFYMKPGQKTNQEILKNVESSRTVQPHFLEFLLSLGWSVDVGRHPGWTGHVSTSWSINCCDDGEGSQQEVISSEDIGASIFNGQKKVLYYADALTEIAFVVPSPVESLTDSLESNISDQDSDSNMDLMPGILKQPSLTLELFPNHTDNLNSSQRLSPSSRMRKLPQGRPVPPLGPETRVSVVWVERYDDIENFPLSELMTEISTGVETTANSSTSLRSTTLEKEVPVIFIHPLNTGLFRIKIQGATGKFNMVIPLVDGMIVSRRALGFLVRQTVINICRRKRLESDSYSPPHVRRKQKITDIVNKYRNKQLEPEFYTSLFQEVGLKNCSS
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
47PhosphorylationPLGQVLGTPSVAGSE
CHHHHHCCCCCCCCC
14.2927251275
49PhosphorylationGQVLGTPSVAGSENL
HHHHCCCCCCCCCCC
25.1627251275
110UbiquitinationSIPLPVIKEPNQYVQ
CCCCCCCCCCHHHHH
68.31-
155PhosphorylationIQKLARESSLMARET
HHHHHHHCCCHHHHH
24.1827966365
221UbiquitinationPPYWKTAKEMVANWR
CCHHHHHHHHHHCCC
52.12-
221UbiquitinationPPYWKTAKEMVANWR
CCHHHHHHHHHHCCC
52.12-
316PhosphorylationQEQFLNVSGMPQELN
HHHHHCCCCCCHHHH
28.4421712546
343PhosphorylationFRAMRGISCLVDAFL
HHHHHHHHHHHHHHH
12.2924719451
357PhosphorylationLGISRPRSDSAPPTP
HCCCCCCCCCCCCCC
38.3030266825
359PhosphorylationISRPRSDSAPPTPVN
CCCCCCCCCCCCCCC
43.8730266825
363PhosphorylationRSDSAPPTPVNRLSM
CCCCCCCCCCCCCCC
38.5230266825
369PhosphorylationPTPVNRLSMPQSAAV
CCCCCCCCCCCCCCC
25.7723403867
373PhosphorylationNRLSMPQSAAVSTTP
CCCCCCCCCCCCCCC
16.6022617229
377PhosphorylationMPQSAAVSTTPPHNR
CCCCCCCCCCCCCCC
23.1023401153
378PhosphorylationPQSAAVSTTPPHNRR
CCCCCCCCCCCCCCC
36.4030266825
379PhosphorylationQSAAVSTTPPHNRRH
CCCCCCCCCCCCCCC
27.5830266825
390PhosphorylationNRRHRAVTVNKATMK
CCCCCEEEEEHHHCC
19.8520068231
393AcetylationHRAVTVNKATMKTST
CCEEEEEHHHCCCCC
40.6825953088
393MethylationHRAVTVNKATMKTST
CCEEEEEHHHCCCCC
40.68115976143
395PhosphorylationAVTVNKATMKTSTVS
EEEEEHHHCCCCCCC
22.3230576142
397MethylationTVNKATMKTSTVSTA
EEEHHHCCCCCCCHH
34.66115976149
398PhosphorylationVNKATMKTSTVSTAH
EEHHHCCCCCCCHHC
20.8620068231
399PhosphorylationNKATMKTSTVSTAHA
EHHHCCCCCCCHHCH
22.6920068231
400PhosphorylationKATMKTSTVSTAHAS
HHHCCCCCCCHHCHH
24.5720068231
402PhosphorylationTMKTSTVSTAHASKV
HCCCCCCCHHCHHHC
21.6928348404
403PhosphorylationMKTSTVSTAHASKVQ
CCCCCCCHHCHHHCC
20.3728348404
407PhosphorylationTVSTAHASKVQHQTS
CCCHHCHHHCCCCCC
24.4030576142
413PhosphorylationASKVQHQTSSTSPLS
HHHCCCCCCCCCCCC
23.6323898821
414PhosphorylationSKVQHQTSSTSPLSS
HHCCCCCCCCCCCCC
25.6723911959
415PhosphorylationKVQHQTSSTSPLSSP
HCCCCCCCCCCCCCC
35.9725159151
416PhosphorylationVQHQTSSTSPLSSPN
CCCCCCCCCCCCCCC
33.8425159151
417PhosphorylationQHQTSSTSPLSSPNQ
CCCCCCCCCCCCCCC
26.2825159151
420PhosphorylationTSSTSPLSSPNQTSS
CCCCCCCCCCCCCCC
47.3225159151
421PhosphorylationSSTSPLSSPNQTSSE
CCCCCCCCCCCCCCC
35.2425159151
425PhosphorylationPLSSPNQTSSEPRPL
CCCCCCCCCCCCCCC
40.6423663014
426PhosphorylationLSSPNQTSSEPRPLP
CCCCCCCCCCCCCCC
23.9623663014
427PhosphorylationSSPNQTSSEPRPLPA
CCCCCCCCCCCCCCC
55.8223663014
469PhosphorylationHNGINRDSSMTAITT
CCCCCCCCCCCEEHH
20.8328857561
470PhosphorylationNGINRDSSMTAITTQ
CCCCCCCCCCEEHHH
25.1728857561
472PhosphorylationINRDSSMTAITTQAS
CCCCCCCCEEHHHHC
19.4926471730
475PhosphorylationDSSMTAITTQASMEF
CCCCCEEHHHHCHHH
15.4727690223
476O-linked_GlycosylationSSMTAITTQASMEFR
CCCCEEHHHHCHHHH
18.9428657654
476PhosphorylationSSMTAITTQASMEFR
CCCCEEHHHHCHHHH
18.9424719451
479PhosphorylationTAITTQASMEFRRKG
CEEHHHHCHHHHHCC
14.7227690223
487PhosphorylationMEFRRKGSQMSTDTM
HHHHHCCCCCCCCCC
26.2428857561
490PhosphorylationRRKGSQMSTDTMVSN
HHCCCCCCCCCCCCC
18.5928857561
491PhosphorylationRKGSQMSTDTMVSNP
HCCCCCCCCCCCCCC
30.1028857561
493PhosphorylationGSQMSTDTMVSNPMF
CCCCCCCCCCCCCCC
21.4028857561
496PhosphorylationMSTDTMVSNPMFDAS
CCCCCCCCCCCCCHH
25.1330576142
503PhosphorylationSNPMFDASEFPDNYE
CCCCCCHHHCCCCHH
41.4330576142
519PhosphorylationGRAEACGTLCRIFCS
HHHHHHHHHHHHHHC
23.67-
526PhosphorylationTLCRIFCSKKTGEEI
HHHHHHHCCCCCCCH
26.83-
537PhosphorylationGEEILPAYLSRFYML
CCCHHHHHHHHHHHH
11.8522817900
608PhosphorylationFKSYVNPTELRRSSI
HHHCCCHHHHHHHHH
42.3124719451
642PhosphorylationVVLEGKFSNDDSSSY
EEEEECCCCCCCCCC
42.7228857561
646PhosphorylationGKFSNDDSSSYDKPI
ECCCCCCCCCCCCCC
24.8523403867
647PhosphorylationKFSNDDSSSYDKPIT
CCCCCCCCCCCCCCC
39.6523403867
648PhosphorylationFSNDDSSSYDKPITF
CCCCCCCCCCCCCCH
41.1023403867
649PhosphorylationSNDDSSSYDKPITFL
CCCCCCCCCCCCCHH
29.9023312004
651UbiquitinationDDSSSYDKPITFLSL
CCCCCCCCCCCHHHH
30.04-
654PhosphorylationSSYDKPITFLSLKLR
CCCCCCCCHHHHHHH
27.3523312004
657PhosphorylationDKPITFLSLKLRLVN
CCCCCHHHHHHHHHH
21.1923312004
714PhosphorylationGGENNLKSHSRTNSG
CCCCCCCCCCCCCCC
29.8423909892
716PhosphorylationENNLKSHSRTNSGIS
CCCCCCCCCCCCCCC
48.1430576142
718PhosphorylationNLKSHSRTNSGISSA
CCCCCCCCCCCCCCC
36.4329255136
720PhosphorylationKSHSRTNSGISSASG
CCCCCCCCCCCCCCC
36.5723401153
723PhosphorylationSRTNSGISSASGGST
CCCCCCCCCCCCCCC
24.3129255136
724PhosphorylationRTNSGISSASGGSTE
CCCCCCCCCCCCCCC
25.2429255136
726PhosphorylationNSGISSASGGSTEPT
CCCCCCCCCCCCCCC
45.7129255136
729PhosphorylationISSASGGSTEPTTPD
CCCCCCCCCCCCCCC
32.8730278072
730PhosphorylationSSASGGSTEPTTPDS
CCCCCCCCCCCCCCC
49.6230278072
733PhosphorylationSGGSTEPTTPDSERP
CCCCCCCCCCCCCCH
44.7423401153
734PhosphorylationGGSTEPTTPDSERPA
CCCCCCCCCCCCCHH
35.5030278072
737PhosphorylationTEPTTPDSERPAQAL
CCCCCCCCCCHHHHH
36.3923927012
748PhosphorylationAQALLRDYALNTDSA
HHHHHHHHCCCCCCH
13.4227642862
762PhosphorylationAAGLLIRSIHLVTQR
HHHHHHHHHHHHHHH
13.8428188228
767PhosphorylationIRSIHLVTQRLNSQW
HHHHHHHHHHHHHHH
17.8427251275
779PhosphorylationSQWRQDMSISLAALE
HHHHHHHHHHHHHHH
19.8120068231
781PhosphorylationWRQDMSISLAALELL
HHHHHHHHHHHHHHH
12.4920068231
789PhosphorylationLAALELLSGLAKVKV
HHHHHHHHCCCCEEE
44.3720068231
892PhosphorylationDKEPNPASMRVKDAA
CCCCCCCHHHHHHHH
14.3727134283
921PhosphorylationPSPSGPASPCSLVNE
CCCCCCCCCCCCCCC
29.5825627689
924PhosphorylationSGPASPCSLVNETTL
CCCCCCCCCCCCCEE
38.44-
958 (in isoform 2)Ubiquitination-3.6621906983
999UbiquitinationCLLPRGAKANQKLFV
HCCCCCCCCCCCEEC
51.17-
1003AcetylationRGAKANQKLFVPEPR
CCCCCCCCEECCCCC
43.6418586741
1003UbiquitinationRGAKANQKLFVPEPR
CCCCCCCCEECCCCC
43.64-
1014UbiquitinationPEPRPVPKNDVGFKY
CCCCCCCCCCCCCEE
67.04-
1020UbiquitinationPKNDVGFKYSVKHRP
CCCCCCCEEEECCCC
30.59-
1021PhosphorylationKNDVGFKYSVKHRPF
CCCCCCEEEECCCCC
19.2128152594
1022PhosphorylationNDVGFKYSVKHRPFP
CCCCCEEEECCCCCC
25.8628152594
1024UbiquitinationVGFKYSVKHRPFPEE
CCCEEEECCCCCCHH
28.14-
1167PhosphorylationFDTVFIFYMKPGQKT
CCEEEEEEECCCCCC
10.22-
1176UbiquitinationKPGQKTNQEILKNVE
CCCCCCCHHHHHHHH
44.32-
1176 (in isoform 3)Ubiquitination-44.3221906983
1176 (in isoform 4)Ubiquitination-44.3221906983
1180UbiquitinationKTNQEILKNVESSRT
CCCHHHHHHHHHCCC
65.692190698
1180 (in isoform 1)Ubiquitination-65.6921906983
1278PhosphorylationSLTDSLESNISDQDS
HHHHHHHHCCCCCCC
44.7724275569
1281PhosphorylationDSLESNISDQDSDSN
HHHHHCCCCCCCCCC
33.2124275569
1285PhosphorylationSNISDQDSDSNMDLM
HCCCCCCCCCCCCCC
36.9910574462
1300PhosphorylationPGILKQPSLTLELFP
CHHHCCCCEEEEECC
31.3430266825
1302PhosphorylationILKQPSLTLELFPNH
HHCCCCEEEEECCCC
23.6426657352
1310PhosphorylationLELFPNHTDNLNSSQ
EEECCCCCCCCCHHC
32.9725159151
1315PhosphorylationNHTDNLNSSQRLSPS
CCCCCCCHHCCCCCC
30.8923401153
1316PhosphorylationHTDNLNSSQRLSPSS
CCCCCCHHCCCCCCH
20.4626657352
1320PhosphorylationLNSSQRLSPSSRMRK
CCHHCCCCCCHHHCC
25.5625159151
1322PhosphorylationSSQRLSPSSRMRKLP
HHCCCCCCHHHCCCC
27.4820068231
1323PhosphorylationSQRLSPSSRMRKLPQ
HCCCCCCHHHCCCCC
33.2220068231
1351PhosphorylationSVVWVERYDDIENFP
EEEEEEECCCCCCCC
12.40-
1405AcetylationNTGLFRIKIQGATGK
CCCEEEEEEECCCCC
25.4012431619
1410PhosphorylationRIKIQGATGKFNMVI
EEEEECCCCCEEEEE
47.96-
1412AcetylationKIQGATGKFNMVIPL
EEECCCCCEEEEEEC
29.2512431631
1449PhosphorylationCRRKRLESDSYSPPH
HHHHCCCCCCCCCHH
36.1323403867
1451PhosphorylationRKRLESDSYSPPHVR
HHCCCCCCCCCHHHC
36.4723403867
1452PhosphorylationKRLESDSYSPPHVRR
HCCCCCCCCCHHHCC
30.1323403867
1453PhosphorylationRLESDSYSPPHVRRK
CCCCCCCCCHHHCCH
35.5923403867
1466UbiquitinationRKQKITDIVNKYRNK
CHHHHHHHHHHHHCC
2.48-
1469UbiquitinationKITDIVNKYRNKQLE
HHHHHHHHHHCCCCC
34.39-

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 RLGPB_HUMAN !!

Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of RLGPB_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 RLGPB_HUMAN !!

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

Oops, there are no PPI records of RLGPB_HUMAN !!

Drug and Disease Associations
Kegg Disease
There are no disease associations of PTM sites.
OMIM Disease
There are no disease associations of PTM sites.
Kegg Drug
There are no disease associations of PTM sites.
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of RLGPB_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-417 AND SER-421, ANDMASS SPECTROMETRY.
"Quantitative phosphoproteomic analysis of T cell receptor signalingreveals system-wide modulation of protein-protein interactions.";
Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K.,Rodionov V., Han D.K.;
Sci. Signal. 2:RA46-RA46(2009).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-734, AND MASSSPECTROMETRY.

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