RPGP1_HUMAN - dbPTM
RPGP1_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID RPGP1_HUMAN
UniProt AC P47736
Protein Name Rap1 GTPase-activating protein 1
Gene Name RAP1GAP
Organism Homo sapiens (Human).
Sequence Length 663
Subcellular Localization Golgi apparatus membrane
Peripheral membrane protein.
Protein Description GTPase activator for the nuclear Ras-related regulatory protein RAP-1A (KREV-1), converting it to the putatively inactive GDP-bound state..
Protein Sequence MIEKMQGSRMDEQRCSFPPPLKTEEDYIPYPSVHEVLGREGPFPLILLPQFGGYWIEGTNHEITSIPETEPLQSPTTKVKLECNPTARIYRKHFLGKEHFNYYSLDAALGHLVFSLKYDVIGDQEHLRLLLRTKCRTYHDVIPISCLTEFPNVVQMAKLVCEDVNVDRFYPVLYPKASRLIVTFDEHVISNNFKFGVIYQKLGQTSEEELFSTNEESPAFVEFLEFLGQKVKLQDFKGFRGGLDVTHGQTGTESVYCNFRNKEIMFHVSTKLPYTEGDAQQLQRKRHIGNDIVAVVFQDENTPFVPDMIASNFLHAYVVVQAEGGGPDGPLYKVSVTARDDVPFFGPPLPDPAVFRKGPEFQEFLLTKLINAEYACYKAEKFAKLEERTRAALLETLYEELHIHSQSMMGLGGDEDKMENGSGGGGFFESFKRVIRSRSQSMDAMGLSNKKPNTVSTSHSGSFAPNNPDLAKAAGISLIVPGKSPTRKKSGPFGSRRSSAIGIENIQEVQEKRESPPAGQKTPDSGHVSQEPKSENSSTQSSPEMPTTKNRAETAAQRAEALKDFSRSSSSASSFASVVEETEGVDGEDTGLESVSSSGTPHKRDSFIYSTWLEDSVSTTSGGSSPGPSRSPHPDAGKLGDPACPEIKIQLEASEQHMPQLGC
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
7 (in isoform 4)Phosphorylation-17.4521815630
8PhosphorylationMIEKMQGSRMDEQRC
CCCCCCCCCCCCCCC		13.9320068231
9 (in isoform 4)Phosphorylation-43.3125849741
16PhosphorylationRMDEQRCSFPPPLKT
CCCCCCCCCCCCCCC		42.8728555341
17 (in isoform 3)Phosphorylation-13.9126657352
23 (in isoform 3)Phosphorylation-52.9026657352
27PhosphorylationPLKTEEDYIPYPSVH
CCCCCCCCCCCCCHH		13.69-
27 (in isoform 3)Phosphorylation-13.6923090842
50 (in isoform 4)Phosphorylation-49.9723663014
51 (in isoform 4)Phosphorylation-8.4923663014
52 (in isoform 4)Phosphorylation-24.0423663014
54 (in isoform 4)Phosphorylation-12.0023663014
56 (in isoform 4)Phosphorylation-2.3523663014
60 (in isoform 4)Phosphorylation-41.4723663014
69PhosphorylationEITSIPETEPLQSPT
EEEECCCCCCCCCCC		37.2326074081
74PhosphorylationPETEPLQSPTTKVKL
CCCCCCCCCCCEEEE		31.7125159151
76PhosphorylationTEPLQSPTTKVKLEC
CCCCCCCCCEEEEEE		44.4926074081
77PhosphorylationEPLQSPTTKVKLECN
CCCCCCCCEEEEEEC		36.9126074081
138 (in isoform 4)Phosphorylation-4.0827251275
232UbiquitinationEFLGQKVKLQDFKGF
HHHCCCEECCCCCCC		47.68-
237UbiquitinationKVKLQDFKGFRGGLD
CEECCCCCCCCCCEE		66.48-
250PhosphorylationLDVTHGQTGTESVYC
EEECCCCCCCEEEEE		51.1428270605
252PhosphorylationVTHGQTGTESVYCNF
ECCCCCCCEEEEEEC		28.6028270605
254PhosphorylationHGQTGTESVYCNFRN
CCCCCCEEEEEECCC		20.4428857561
262AcetylationVYCNFRNKEIMFHVS
EEEECCCCEEEEEEE		44.3423749302
268 (in isoform 3)Ubiquitination-5.48-
326AcetylationVVQAEGGGPDGPLYK
EEEECCCCCCCCEEE		28.1619608861
357UbiquitinationPDPAVFRKGPEFQEF
CCHHHHCCCHHHHHH		68.31-
374PhosphorylationTKLINAEYACYKAEK
HHHHCHHHHHHHHHH		10.2825147952
378AcetylationNAEYACYKAEKFAKL
CHHHHHHHHHHHHHH		50.3719608861
378UbiquitinationNAEYACYKAEKFAKL
CHHHHHHHHHHHHHH		50.37-
384AcetylationYKAEKFAKLEERTRA
HHHHHHHHHHHHHHH		60.6119608861
387 (in isoform 3)Ubiquitination-70.55-
437PhosphorylationSFKRVIRSRSQSMDA
HHHHHHHHHCCCCCC		25.7628857561
439PhosphorylationKRVIRSRSQSMDAMG
HHHHHHHCCCCCCCC		28.0529255136
441PhosphorylationVIRSRSQSMDAMGLS
HHHHHCCCCCCCCCC		21.6329255136
442AcetylationIRSRSQSMDAMGLSN
HHHHCCCCCCCCCCC		2.7119608861
448AcetylationSMDAMGLSNKKPNTV
CCCCCCCCCCCCCCC		40.6519608861
448PhosphorylationSMDAMGLSNKKPNTV
CCCCCCCCCCCCCCC		40.6521815630
454PhosphorylationLSNKKPNTVSTSHSG
CCCCCCCCCCCCCCC		25.1020873877
456PhosphorylationNKKPNTVSTSHSGSF
CCCCCCCCCCCCCCC		23.3520873877
457PhosphorylationKKPNTVSTSHSGSFA
CCCCCCCCCCCCCCC		26.5620873877
458PhosphorylationKPNTVSTSHSGSFAP
CCCCCCCCCCCCCCC		14.2420873877
460PhosphorylationNTVSTSHSGSFAPNN
CCCCCCCCCCCCCCC		35.5825849741
462PhosphorylationVSTSHSGSFAPNNPD
CCCCCCCCCCCCCHH		22.6520873877
477PhosphorylationLAKAAGISLIVPGKS
HHHHHCCEEECCCCC		15.8928176443
484PhosphorylationSLIVPGKSPTRKKSG
EEECCCCCCCCCCCC		37.1029255136
486PhosphorylationIVPGKSPTRKKSGPF
ECCCCCCCCCCCCCC		63.3130266825
490PhosphorylationKSPTRKKSGPFGSRR
CCCCCCCCCCCCCCC		55.5230576142
493 (in isoform 2)Phosphorylation-18.5224076635
495PhosphorylationKKSGPFGSRRSSAIG
CCCCCCCCCCHHCCC		25.5421815630
498PhosphorylationGPFGSRRSSAIGIEN
CCCCCCCHHCCCCCC		24.0229255136
499 (in isoform 2)Phosphorylation-23.30-
499PhosphorylationPFGSRRSSAIGIENI
CCCCCCHHCCCCCCH		23.3029255136
503 (in isoform 2)Phosphorylation-2.75-
505 (in isoform 4)Phosphorylation-39.0424719451
510 (in isoform 2)Phosphorylation-50.1424719451
515PhosphorylationEVQEKRESPPAGQKT
HHHHHHCCCCCCCCC		39.9726055452
518 (in isoform 4)Phosphorylation-36.1124719451
520 (in isoform 4)Phosphorylation-48.8624719451
522PhosphorylationSPPAGQKTPDSGHVS
CCCCCCCCCCCCCCC		25.1729255136
524 (in isoform 4)Phosphorylation-72.9127251275
525PhosphorylationAGQKTPDSGHVSQEP
CCCCCCCCCCCCCCC		31.8123663014
529PhosphorylationTPDSGHVSQEPKSEN
CCCCCCCCCCCCCCC		24.1323663014
534PhosphorylationHVSQEPKSENSSTQS
CCCCCCCCCCCCCCC		53.3723090842
537PhosphorylationQEPKSENSSTQSSPE
CCCCCCCCCCCCCCC		30.6128450419
538PhosphorylationEPKSENSSTQSSPEM
CCCCCCCCCCCCCCC		41.8923663014
539PhosphorylationPKSENSSTQSSPEMP
CCCCCCCCCCCCCCC		32.0823663014
541PhosphorylationSENSSTQSSPEMPTT
CCCCCCCCCCCCCCC		48.2025159151
542PhosphorylationENSSTQSSPEMPTTK
CCCCCCCCCCCCCCH		18.3025159151
547PhosphorylationQSSPEMPTTKNRAET
CCCCCCCCCHHHHHH		49.4423090842
548 (in isoform 4)Phosphorylation-22.0524719451
548PhosphorylationSSPEMPTTKNRAETA
CCCCCCCCHHHHHHH		22.0523090842
554 (in isoform 4)Phosphorylation-26.7224719451
559 (in isoform 4)Phosphorylation-8.3724719451
562 (in isoform 4)Phosphorylation-4.0424719451
563 (in isoform 4)Phosphorylation-64.8724719451
579 (in isoform 4)Phosphorylation-5.2224719451
605 (in isoform 4)Phosphorylation-53.3424719451
606 (in isoform 4)Phosphorylation-19.9924719451
606PhosphorylationGTPHKRDSFIYSTWL
CCCCCCCCCEEEEEC		19.9928857561
609PhosphorylationHKRDSFIYSTWLEDS
CCCCCCEEEEECCCC		9.6828857561
610PhosphorylationKRDSFIYSTWLEDSV
CCCCCEEEEECCCCC		14.3228857561
611PhosphorylationRDSFIYSTWLEDSVS
CCCCEEEEECCCCCC		19.6628857561
624PhosphorylationVSTTSGGSSPGPSRS
CCCCCCCCCCCCCCC		36.5628348404
625PhosphorylationSTTSGGSSPGPSRSP
CCCCCCCCCCCCCCC		36.8327251275
631PhosphorylationSSPGPSRSPHPDAGK
CCCCCCCCCCCCCCC		31.7230576142
688 (in isoform 4)Phosphorylation-27251275
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
484SPhosphorylationKinaseCDK1P06493
PSP
490SPhosphorylationKinasePRKACAP17612
GPS
490SPhosphorylationKinasePKA-FAMILY-GPS
490SPhosphorylationKinasePKA_GROUP-PhosphoELM
499SPhosphorylationKinasePRKACAP17612
GPS
499SPhosphorylationKinasePKA-FAMILY-GPS
499SPhosphorylationKinasePKA_GROUP-PhosphoELM
525SPhosphorylationKinaseGSK3BP49841
PhosphoELM
525SPhosphorylationKinasePLK1P53350
PSP
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of RPGP1_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 RPGP1_HUMAN !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
AFAD_HUMANMLLT4physical
12590145
MEX3B_HUMANMEX3Bphysical
16169070
PROF2_HUMANPFN2physical
16169070
RAP1A_HUMANRAP1Aphysical
12842888
CNR1_HUMANCNR1physical
15657046
FBW1A_HUMANBTRCphysical
25329897
FBW1B_HUMANFBXW11physical
25329897
PLK1_HUMANPLK1physical
25329897
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 RPGP1_HUMAN

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Related Literatures of Post-Translational Modification
Acetylation
ReferencePubMed
"Lysine acetylation targets protein complexes and co-regulates majorcellular functions.";
Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T.,Olsen J.V., Mann M.;
Science 325:834-840(2009).
Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-262 AND LYS-384, AND MASSSPECTROMETRY.
Phosphorylation
ReferencePubMed
"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 SER-441, AND MASSSPECTROMETRY.
"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-484 AND SER-499, ANDMASS SPECTROMETRY.

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