RGPA2_MOUSE - dbPTM
RGPA2_MOUSE - PTM Information in dbPTM
Basic Information of Protein
UniProt ID RGPA2_MOUSE
UniProt AC A3KGS3
Protein Name Ral GTPase-activating protein subunit alpha-2
Gene Name Ralgapa2
Organism Mus musculus (Mouse).
Sequence Length 1872
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 MFSRRSHGDVKKSTQKVLDPKKDVLTRLKHLRALLDNVDASDLKQFFETNYSQIYFIFYENFITLENSLKLKGNNKSQREELDSILFLFEKILQFLPERIFFRWHYQSIGSTLKKLLHTGNSIKIRCEGIRLFLLWLQALQTNCAEEQVLIFACLVPGFPAVLSSRGPCTLETLINPSPSIVDAKIYPEEITPLLPAISGEKIAEDQTCFFLQILLKYMVIQAASLEWKNKENQDTGFKFLFTLFRKYYLPHLFPSFTKLTNIYKPVLEIPHLRPKPVYVTVTRDNETIYSTKIPYMAARVVFIKWIVTFFLEKKYLTATQNTKNGVDVLPKIIQTVGGGAIQEKVPELDGAGSTEQDKSHSNSSTLSDRRLSNSSLCSIEEEHRTVYEMVQRILLSTRGYVNFVNEVFRQAFLLPSCEISVTRKVVQVYRKWILQNKPVFMEEPDKKDVAQEDADKLGLSETDSKEASSESSGHKRSSSWGRTYSFTSAMSRGCVTEEDNTNVKAGAQAMLQVFLTNAANVFLLEPCAEVPMLLREQVDASKAVLIIFRRMIMELTMNQKTWEQMLQILLRITEAVMQKPKDKHVKDLFAQSLAGLLFRTLIVAWIRANLCVYISRELWDDFLRVLSSLTEWEELITEWSNIMDSLTAVLARTVYGVEMTNLPLDKLSEQKEKKQRGKGCILEPQKGTAVGRSFSLSWRSHPDVTEPMRFRSATTSGAPGVEKARNTVRQKATEVEEFQQAESTAAADCDYLVVGQQQVPRSSSTSDITERLYSDSSQGQKVEHSQNLSSSEPKSVQESKGHVTHEHEGITMLVRRSSSPAELELKDDLQQAHGRCRQRQTSESTGSDTVVGYSNEAELPVSPWQACEEDPDLSTPTDAVADSDARHWLQLSPTDASNLTDSRECLADDCSIIAGGNLTGWHPDSAAVLWRRVLGILGDVNNIQSPKIHAKVFGYLYELWYKLAKIRDNLAISLDNQSSPSPPLLIPPLRMFASWLFKATTLPNEYKEGKLQAYKLICAMMTRRQDVLPNSDFLVHFYLVMHLGLTSEDQDVLNTIIKNCSPRFFSLGLPGFSMLVGDFITAAARVLSTDMLAAPRSEALTLLGSLVCFPNTYQEIPLLQSVPEVSDVVTGAEDVKHYLINILLKNATEEPNECARCIAICSLGVWICEELAQSASHPQVKDAINVIGVTLKFPNKIVAQVACDVLQLLVSYWEKLQMFETALPRKMAEILVATIAFLLPSAEYSSVETDKKFIVSLLLCLLDWCMALPVSALLHPVSTAVLEELHPSRAPLLDYIYRVLHCCVCGSSTYTQQSHYTLTLADLSSTDYDPFLPLANVRNSEPIQYHSSADLGNLLTVEEEKKRRSVELIPLTARMVMAHLVNHLGHYPLSGGPAVLHSLVSENHDNAHVEGTELSSEVFRSPNLQLFVFNDSTLISYLQTPAEGPAGGTSGGSLSDVRVIVRDISGKYSWDGKVLYGPLEGRLAPNGRNPSFQISGWHHHTCGPQKDLFNGEEGDDVLDKLLENIGHTSPECLLPSQLNLNEPSPTPCAMNWDQEKAIMEVILRQSAQEDEYVQRCNSDSSVTVTSQGQPSPVEPRGPFYFCRLLLDDLGMNSWDRRKNFHLLKKNSKLLRELKNLDSRQCRETHKIAVFYIAEGQEDKCSILANERGSQAYEDFVAGLGWEVDLSTHCGFMGGLQRNGSTGQTAPYYATSTVEVIFHVSTRMPSDSDDSLTKKLRHLGNDEVHIVWSEHSRDYRRGIIPTAFGDVSIIIYPMKNHMFFITITKKPEVPFFGPLFDGAIVSGKLLPSLICATCINASRAVKCLIPLYQSFYEERALYLEAIIQNHREVMTFEDFAAQVFSPSPSYSVSGTD
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
318PhosphorylationFLEKKYLTATQNTKN
HHHHHCCCCCCCCCC
25.27-
354PhosphorylationPELDGAGSTEQDKSH
CCCCCCCCCCCCCCC
28.3925293948
355PhosphorylationELDGAGSTEQDKSHS
CCCCCCCCCCCCCCC
36.4325293948
360PhosphorylationGSTEQDKSHSNSSTL
CCCCCCCCCCCCCCH
40.2025293948
362PhosphorylationTEQDKSHSNSSTLSD
CCCCCCCCCCCCHHH
45.5627681418
364PhosphorylationQDKSHSNSSTLSDRR
CCCCCCCCCCHHHHH
27.9325293948
365PhosphorylationDKSHSNSSTLSDRRL
CCCCCCCCCHHHHHC
37.3027681418
366PhosphorylationKSHSNSSTLSDRRLS
CCCCCCCCHHHHHCC
30.0627681418
368PhosphorylationHSNSSTLSDRRLSNS
CCCCCCHHHHHCCCC
29.2027681418
373PhosphorylationTLSDRRLSNSSLCSI
CHHHHHCCCCCCCCH
32.6225521595
375PhosphorylationSDRRLSNSSLCSIEE
HHHHCCCCCCCCHHH
22.7027087446
376PhosphorylationDRRLSNSSLCSIEEE
HHHCCCCCCCCHHHH
37.3325521595
379PhosphorylationLSNSSLCSIEEEHRT
CCCCCCCCHHHHHHH
38.0225521595
478PhosphorylationESSGHKRSSSWGRTY
CCCCCCCCCCCCCCE
33.2630387612
480PhosphorylationSGHKRSSSWGRTYSF
CCCCCCCCCCCCEEC
34.4923737553
484PhosphorylationRSSSWGRTYSFTSAM
CCCCCCCCEECCCCH
21.4126745281
485PhosphorylationSSSWGRTYSFTSAMS
CCCCCCCEECCCCHH
10.6323140645
486PhosphorylationSSWGRTYSFTSAMSR
CCCCCCEECCCCHHC
22.8025521595
488PhosphorylationWGRTYSFTSAMSRGC
CCCCEECCCCHHCCC
15.0526745281
489PhosphorylationGRTYSFTSAMSRGCV
CCCEECCCCHHCCCC
21.6926745281
492PhosphorylationYSFTSAMSRGCVTEE
EECCCCHHCCCCCCC
25.8228066266
580AcetylationITEAVMQKPKDKHVK
HHHHHHCCCCCHHHH
35.6266694561
582AcetylationEAVMQKPKDKHVKDL
HHHHCCCCCHHHHHH
83.1366694567
694PhosphorylationKGTAVGRSFSLSWRS
CCCCCCCCEEEEECC
17.1726745281
696PhosphorylationTAVGRSFSLSWRSHP
CCCCCCEEEEECCCC
23.8122942356
698PhosphorylationVGRSFSLSWRSHPDV
CCCCEEEEECCCCCC
21.1728066266
701PhosphorylationSFSLSWRSHPDVTEP
CEEEEECCCCCCCCC
32.8723684622
713PhosphorylationTEPMRFRSATTSGAP
CCCCEECCCCCCCCC
27.5329550500
715PhosphorylationPMRFRSATTSGAPGV
CCEECCCCCCCCCCH
23.8126824392
716PhosphorylationMRFRSATTSGAPGVE
CEECCCCCCCCCCHH
25.5323737553
763PhosphorylationGQQQVPRSSSTSDIT
CCCCCCCCCCCCHHH
23.6728609623
764PhosphorylationQQQVPRSSSTSDITE
CCCCCCCCCCCHHHH
38.6328609623
765PhosphorylationQQVPRSSSTSDITER
CCCCCCCCCCHHHHH
32.9325521595
766PhosphorylationQVPRSSSTSDITERL
CCCCCCCCCHHHHHH
32.1628609623
767PhosphorylationVPRSSSTSDITERLY
CCCCCCCCHHHHHHH
29.0328609623
770PhosphorylationSSSTSDITERLYSDS
CCCCCHHHHHHHCCC
21.7518846507
792PhosphorylationHSQNLSSSEPKSVQE
CCCCCCCCCCCCHHH
55.32-
818PhosphorylationITMLVRRSSSPAELE
EEEEEECCCCCCCEE
25.3025521595
819PhosphorylationTMLVRRSSSPAELEL
EEEEECCCCCCCEEC
38.2325521595
820PhosphorylationMLVRRSSSPAELELK
EEEECCCCCCCEECH
29.4025521595
893PhosphorylationARHWLQLSPTDASNL
CCHHHCCCCCCHHHC
16.8829472430
895PhosphorylationHWLQLSPTDASNLTD
HHHCCCCCCHHHCCC
40.6023984901
898PhosphorylationQLSPTDASNLTDSRE
CCCCCCHHHCCCCCH
34.8723984901
901PhosphorylationPTDASNLTDSRECLA
CCCHHHCCCCCHHHC
35.8623737553
903PhosphorylationDASNLTDSRECLADD
CHHHCCCCCHHHCCC
25.4123737553
974PhosphorylationIRDNLAISLDNQSSP
HHHCEEEECCCCCCC
24.8625293948
979PhosphorylationAISLDNQSSPSPPLL
EEECCCCCCCCCCCC
50.9325293948
980PhosphorylationISLDNQSSPSPPLLI
EECCCCCCCCCCCCC
21.4525293948
982PhosphorylationLDNQSSPSPPLLIPP
CCCCCCCCCCCCCHH
40.8925293948
1346PhosphorylationRNSEPIQYHSSADLG
CCCCCCEECCCCCCC
12.3723984901
1348PhosphorylationSEPIQYHSSADLGNL
CCCCEECCCCCCCCC
23.4519060867
1349PhosphorylationEPIQYHSSADLGNLL
CCCEECCCCCCCCCC
16.7023984901
1357PhosphorylationADLGNLLTVEEEKKR
CCCCCCCCHHHHHHH
29.1021082442
1366PhosphorylationEEEKKRRSVELIPLT
HHHHHHCCCCHHHHH
24.7924759943
1592PhosphorylationVTSQGQPSPVEPRGP
EEECCCCCCCCCCCC
33.4230635358
1721PhosphorylationVEVIFHVSTRMPSDS
EEEEEEEECCCCCCC
11.17-
1722PhosphorylationEVIFHVSTRMPSDSD
EEEEEEECCCCCCCC
29.87-

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
696SPhosphorylationKinasePKBP31750
Uniprot
715TPhosphorylationKinasePKBP31750
Uniprot

Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of RGPA2_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 RGPA2_MOUSE !!

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

Oops, there are no PPI records of RGPA2_MOUSE !!

Drug and Disease Associations
Kegg Drug
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of RGPA2_MOUSE

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Related Literatures of Post-Translational Modification
Phosphorylation
ReferencePubMed
"Solid tumor proteome and phosphoproteome analysis by high resolutionmass spectrometry.";
Zanivan S., Gnad F., Wickstroem S.A., Geiger T., Macek B., Cox J.,Faessler R., Mann M.;
J. Proteome Res. 7:5314-5326(2008).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-819 AND SER-820, ANDMASS SPECTROMETRY.
"Large-scale phosphorylation analysis of mouse liver.";
Villen J., Beausoleil S.A., Gerber S.A., Gygi S.P.;
Proc. Natl. Acad. Sci. U.S.A. 104:1488-1493(2007).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-373; SER-376; SER-379;SER-819 AND SER-820, AND MASS SPECTROMETRY.

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