RGPA2_HUMAN - dbPTM
RGPA2_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID RGPA2_HUMAN
UniProt AC Q2PPJ7
Protein Name Ral GTPase-activating protein subunit alpha-2
Gene Name RALGAPA2
Organism Homo sapiens (Human).
Sequence Length 1873
Subcellular Localization Cytoplasm .
Protein Description Catalytic subunit of the heterodimeric RalGAP2 complex which acts as a GTPase activator for the Ras-like small GTPases RALA and RALB..
Protein Sequence MFSRRSHGDVKKSTQKVLDPKKDVLTRLKHLRALLDNVDANDLKQFFETNYSQIYFIFYENFIALENSLKLKGNNKSQREELDSILFLFEKILQFLPERIFFRWHYQSIGSTLKKLLHTGNSIKIRCEGIRLFLLWLQALQTNCAEEQVLIFACLVPGFPAVMSSRGPCTLETLINPSPSVADVKIYPEEITPLLPAISGEKIAEDQTCFFLQILLKYMVIQAASLEWKNKENQDTGFKFLFTLFRKYYLPHLFPSFTKLTNIYKPVLDIPHLRPKPVYITTTRDNENIYSTKIPYMAARVVFIKWIVTFFLEKKYLTATQNTKNGVDVLPKIIQTVGGGAVQERAPELDGGGPTEQDKSHSNSSTLSDRRLSNSSLCSIEEEHRMVYEMVQRILLSTRGYVNFVNEVFHQAFLLPSCEIAVTRKVVQVYRKWILQDKPVFMEEPDRKDVAQEDAEKLGFSETDSKEASSESSGHKRSSSWGRTYSFTSAMSRGCVTEEENTNVKAGVQALLQVFLTNSANIFLLEPCAEVPVLLKEQVDACKAVLIIFRRMIMELTMNKKTWEQMLQILLRITEAVMQKPKDKQIKDLFAQSLAGLLFRTLMVAWIRANLCVYISRELWDDFLGVLSSLTEWEELINEWANIMDSLTAVLARTVYGVEMTNLPLDKLSEQKEKKQRGKGCVLDPQKGTTVGRSFSLSWRSHPDVTEPMRFRSATTSGAPGVEKARNIVRQKATEVEECQQSENAPAAGSGHLTVGQQQQVLRSSSTSDIPEPLCSDSSQGQKAENTQNSSSSEPQPIQENKGHVKREHEGITILVRRSSSPAELDLKDDLQQTQGKCRERQKSESTNSDTTLGCTNEAELSMGPWQTCEEDPELNTPTDVVADADARHWLQLSPTDASNLTDSSECLTDDCSIIAGGSLTGWHPDSAAVLWRRVLGILGDVNNIQSPKIHARVFCYLYELWYKLAKIRDNLAISLDNQSSPSPPVLIPPLRMFASWLFKAATLPNEYKEGKLQAYRLICAMMTRRQDVLPNSDFLVHFYLVMHLGLTSEDQDILNTIIRHCPPRFFSLGFPGFSMLVGDFITAAARVLSTDILTAPRSEAVTVLGSLVCFPNTYQEIPLLQSVPEVNEAITGTEDVKHYLINILLKNATEEPNEYARCIAVCSLGVWICEELAQCTSHPQVKEAINVIGVTLKFPNKIVAQVACDVLQLLVSYWEKLQMFETSLPRKMAEILVATVAFLLPSAEYSSVETDKKFIVSLLLCLLDWCMALPVSVLLHPVSTAVLEEQHSARAPLLDYIYRVLHCCVCGSSTYTQQSHYILTLADLSSTDYDPFLPLANVKSSEPVQYHSSAELGNLLTVEEEKKRRSLELIPLTARMVMAHLVNHLGHYPLSGGPAILHSLVSENHDNAHVEGSELSFEVFRSPNLQLFVFNDSTLISYLQTPTEGPVGGSPVGSLSDVRVIVRDISGKYSWDGKVLYGPLEGCLAPNGRNPSFLISSWHRDTFGPQKDSSQVEEGDDVLDKLLENIGHTSPECLLPSQLNLNEPSLTPCGMNYDQEKEIIEVILRQNAQEDEYIQSHNFDSAMKVTSQGQPSPVEPRGPFYFCRLLLDDLGMNSWDRRKNFHLLKKNSKLLRELKNLDSRQCRETHKIAVFYIAEGQEDKCSILSNERGSQAYEDFVAGLGWEVDLSTHCGFMGGLQRNGSTGQTAPYYATSTVEVIFHVSTRMPSDSDDSLTKKLRHLGNDEVHIVWSEHSRDYRRGIIPTAFGDVSIIIYPMKNHMFFIAITKKPEVPFFGPLFDGAIVSGKLLPSLVCATCINASRAVKCLIPLYQSFYEERALYLEAIIQNHREVMTFEDFAAQVFSPSPSYSLSGTD
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
173PhosphorylationRGPCTLETLINPSPS
CCCEEEEHHCCCCCC
35.7322210691
180PhosphorylationTLINPSPSVADVKIY
HHCCCCCCCCCCEEC
33.9822210691
256PhosphorylationYLPHLFPSFTKLTNI
CHHHHCCCCHHHCCC
37.9124719451
290PhosphorylationTRDNENIYSTKIPYM
CCCCCCCCCCCCHHH
23.1318083107
296PhosphorylationIYSTKIPYMAARVVF
CCCCCCHHHHHHHHH
11.6718083107
316PhosphorylationTFFLEKKYLTATQNT
HHHHHHHCCCCCCCC
21.98-
336PhosphorylationVLPKIIQTVGGGAVQ
HHHHHHHHHCCCCHH
15.6522210691
355PhosphorylationELDGGGPTEQDKSHS
CCCCCCCCCCCCCCC
49.9423312004
360PhosphorylationGPTEQDKSHSNSSTL
CCCCCCCCCCCCCCH
40.2023312004
362PhosphorylationTEQDKSHSNSSTLSD
CCCCCCCCCCCCHHH
45.5623312004
364PhosphorylationQDKSHSNSSTLSDRR
CCCCCCCCCCHHHHH
27.9323312004
365PhosphorylationDKSHSNSSTLSDRRL
CCCCCCCCCHHHHHC
37.3023312004
366PhosphorylationKSHSNSSTLSDRRLS
CCCCCCCCHHHHHCC
30.0624719451
368PhosphorylationHSNSSTLSDRRLSNS
CCCCCCHHHHHCCCC
29.2023312004
373PhosphorylationTLSDRRLSNSSLCSI
CHHHHHCCCCCCCCH
32.6223401153
375PhosphorylationSDRRLSNSSLCSIEE
HHHHCCCCCCCCHHH
22.7023401153
376PhosphorylationDRRLSNSSLCSIEEE
HHHCCCCCCCCHHHH
37.3330266825
379PhosphorylationLSNSSLCSIEEEHRM
CCCCCCCCHHHHHHH
38.0230266825
388PhosphorylationEEEHRMVYEMVQRIL
HHHHHHHHHHHHHHH
6.75-
425UbiquitinationCEIAVTRKVVQVYRK
CCEEEEHHHHHHHHH
37.07-
461PhosphorylationDAEKLGFSETDSKEA
HHHHHCCCCCCCCCC
37.4823312004
463PhosphorylationEKLGFSETDSKEASS
HHHCCCCCCCCCCCC
44.3623312004
465PhosphorylationLGFSETDSKEASSES
HCCCCCCCCCCCCCC
39.5523312004
469PhosphorylationETDSKEASSESSGHK
CCCCCCCCCCCCCCC
35.4123312004
473PhosphorylationKEASSESSGHKRSSS
CCCCCCCCCCCCCCC
40.6523312004
478PhosphorylationESSGHKRSSSWGRTY
CCCCCCCCCCCCCCE
33.2627251275
479PhosphorylationSSGHKRSSSWGRTYS
CCCCCCCCCCCCCEE
33.8627251275
480PhosphorylationSGHKRSSSWGRTYSF
CCCCCCCCCCCCEEH
34.4916490346
484PhosphorylationRSSSWGRTYSFTSAM
CCCCCCCCEEHHHHH
21.4123403867
485PhosphorylationSSSWGRTYSFTSAMS
CCCCCCCEEHHHHHH
10.6323403867
486PhosphorylationSSWGRTYSFTSAMSR
CCCCCCEEHHHHHHC
22.8023401153
488PhosphorylationWGRTYSFTSAMSRGC
CCCCEEHHHHHHCCC
15.0523927012
489PhosphorylationGRTYSFTSAMSRGCV
CCCEEHHHHHHCCCC
21.6923403867
492PhosphorylationYSFTSAMSRGCVTEE
EEHHHHHHCCCCCCC
25.8223403867
497PhosphorylationAMSRGCVTEEENTNV
HHHCCCCCCCCCCCH
41.5828985074
674UbiquitinationKLSEQKEKKQRGKGC
HHHHHHHHHHCCCCC
62.33-
675UbiquitinationLSEQKEKKQRGKGCV
HHHHHHHHHCCCCCE
46.44-
679UbiquitinationKEKKQRGKGCVLDPQ
HHHHHCCCCCEECCC
51.86-
679MethylationKEKKQRGKGCVLDPQ
HHHHHCCCCCEECCC
51.8680503683
689PhosphorylationVLDPQKGTTVGRSFS
EECCCCCCCCCCCEE
25.9129514088
690PhosphorylationLDPQKGTTVGRSFSL
ECCCCCCCCCCCEEE
29.6329514088
694PhosphorylationKGTTVGRSFSLSWRS
CCCCCCCCEEEEECC
17.1730266825
696PhosphorylationTTVGRSFSLSWRSHP
CCCCCCEEEEECCCC
23.8123401153
698PhosphorylationVGRSFSLSWRSHPDV
CCCCEEEEECCCCCC
21.1730266825
701PhosphorylationSFSLSWRSHPDVTEP
CEEEEECCCCCCCCC
32.8728348404
713PhosphorylationTEPMRFRSATTSGAP
CCCCCCCCCCCCCCC
27.5325884760
715PhosphorylationPMRFRSATTSGAPGV
CCCCCCCCCCCCCCH
23.8129255136
716PhosphorylationMRFRSATTSGAPGVE
CCCCCCCCCCCCCHH
25.5329255136
717PhosphorylationRFRSATTSGAPGVEK
CCCCCCCCCCCCHHH
28.7123403867
764PhosphorylationQQQQVLRSSSTSDIP
HHHHHHHCCCCCCCC
25.2023403867
765PhosphorylationQQQVLRSSSTSDIPE
HHHHHHCCCCCCCCC
31.0726657352
766PhosphorylationQQVLRSSSTSDIPEP
HHHHHCCCCCCCCCC
32.9323401153
767PhosphorylationQVLRSSSTSDIPEPL
HHHHCCCCCCCCCCC
32.1625159151
768PhosphorylationVLRSSSTSDIPEPLC
HHHCCCCCCCCCCCC
35.1823403867
776PhosphorylationDIPEPLCSDSSQGQK
CCCCCCCCCCCCCCC
48.4823403867
778PhosphorylationPEPLCSDSSQGQKAE
CCCCCCCCCCCCCCC
14.3123403867
779PhosphorylationEPLCSDSSQGQKAEN
CCCCCCCCCCCCCCC
43.2323403867
813PhosphorylationKREHEGITILVRRSS
CCHHCCEEEEEECCC
21.08-
819PhosphorylationITILVRRSSSPAELD
EEEEEECCCCCCCCC
25.3023401153
820PhosphorylationTILVRRSSSPAELDL
EEEEECCCCCCCCCC
38.2325159151
821PhosphorylationILVRRSSSPAELDLK
EEEECCCCCCCCCCH
29.4023927012
834PhosphorylationLKDDLQQTQGKCRER
CHHHHHHHHHHHHHH
26.7424702127
844PhosphorylationKCRERQKSESTNSDT
HHHHHHHHCCCCCCC
28.5720736484
846PhosphorylationRERQKSESTNSDTTL
HHHHHHCCCCCCCCC
39.7220736484
847PhosphorylationERQKSESTNSDTTLG
HHHHHCCCCCCCCCC
34.3920736484
849PhosphorylationQKSESTNSDTTLGCT
HHHCCCCCCCCCCCC
36.1020736484
902PhosphorylationPTDASNLTDSSECLT
CCCHHHCCCCHHHCC
37.7827251275
904PhosphorylationDASNLTDSSECLTDD
CHHHCCCCHHHCCCC
23.8527251275
905PhosphorylationASNLTDSSECLTDDC
HHHCCCCHHHCCCCC
34.8327251275
980PhosphorylationAISLDNQSSPSPPVL
EEECCCCCCCCCCCC
50.9326657352
981PhosphorylationISLDNQSSPSPPVLI
EECCCCCCCCCCCCC
21.4526657352
1091PhosphorylationAAARVLSTDILTAPR
HHHHHHCCCCCCCCH
23.9327732954
1095PhosphorylationVLSTDILTAPRSEAV
HHCCCCCCCCHHHHH
34.6427732954
1223PhosphorylationEKLQMFETSLPRKMA
HHHHHHHHCCCHHHH
25.0529449344
1224PhosphorylationKLQMFETSLPRKMAE
HHHHHHHCCCHHHHH
29.2222210691
1313PhosphorylationVCGSSTYTQQSHYIL
HCCCCCCCCCCCEEE
21.8830576142
1330PhosphorylationADLSSTDYDPFLPLA
HHCCCCCCCCCCCCC
26.1330576142
1347PhosphorylationKSSEPVQYHSSAELG
CCCCCCCCCCCCHHC
12.1427642862
1349PhosphorylationSEPVQYHSSAELGNL
CCCCCCCCCCHHCCC
26.7226356563
1350PhosphorylationEPVQYHSSAELGNLL
CCCCCCCCCHHCCCC
16.6726356563
1457PhosphorylationGSPVGSLSDVRVIVR
CCCCCCHHHEEEEEE
35.4424719451
1467PhosphorylationRVIVRDISGKYSWDG
EEEEEECCCCCCCCC
33.2626657352
1470PhosphorylationVRDISGKYSWDGKVL
EEECCCCCCCCCCEE
20.6526657352
1493PhosphorylationAPNGRNPSFLISSWH
CCCCCCCCCEEEEEC
35.9128348404
1508UbiquitinationRDTFGPQKDSSQVEE
CCCCCCCCCHHHCCC
63.8129967540
1574PhosphorylationQNAQEDEYIQSHNFD
CCCCCCHHHHHCCCC
19.3127642862
1587PhosphorylationFDSAMKVTSQGQPSP
CCCCEEECCCCCCCC
15.1525907765
1588PhosphorylationDSAMKVTSQGQPSPV
CCCEEECCCCCCCCC
34.9928450419
1593PhosphorylationVTSQGQPSPVEPRGP
ECCCCCCCCCCCCCC
33.4210574462
1640PhosphorylationRELKNLDSRQCRETH
HHHCCCCHHHHHHHH
27.67-
1646PhosphorylationDSRQCRETHKIAVFY
CHHHHHHHHCEEEEE
14.76-
1736UbiquitinationSDDSLTKKLRHLGND
CCCHHHHHHHHCCCC
45.58-
1839PhosphorylationFYEERALYLEAIIQN
HHHHHHHHHHHHHHH
11.0823401153

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
486SPhosphorylationKinaseAKT1P31749
PSP
696SPhosphorylationKinasePKBP31749
Uniprot
715TPhosphorylationKinaseAKT1P31749
PSP

Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of RGPA2_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 RGPA2_HUMAN !!

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

Oops, there are no PPI records of RGPA2_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 RGPA2_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-820 AND SER-821, ANDMASS SPECTROMETRY.
"Adipocytes contain a novel complex similar to the tuberous sclerosiscomplex.";
Gridley S., Chavez J.A., Lane W.S., Lienhard G.E.;
Cell. Signal. 18:1626-1632(2006).
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), INTERACTION WITH RALGAPB,SUBCELLULAR LOCATION, AND PHOSPHORYLATION AT SER-486; SER-696 ANDTHR-715.

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