dbPTM

RPGP2_HUMAN - PTM Information in dbPTM

Basic Information of Protein

Overview of Protein Modification Sites with Functional and Structural Information
UniProt ID	RPGP2_HUMAN
UniProt AC	Q684P5
Protein Name	Rap1 GTPase-activating protein 2
Gene Name	RAP1GAP2
Organism	Homo sapiens (Human).
Sequence Length	730
Subcellular Localization	Cytoplasm . Cytoplasm, perinuclear region .
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	MFGRKRSVSFGGFGWIDKTMLASLKVKKQELANSSDATLPDRPLSPPLTAPPTMKSSEFFEMLEKMQGIKLEEQKPGPQKNKDDYIPYPSIDEVVEKGGPYPQVILPQFGGYWIEDPENVGTPTSLGSSICEEEEEDNLSPNTFGYKLECKGEARAYRRHFLGKDHLNFYCTGSSLGNLILSVKCEEAEGIEYLRVILRSKLKTVHERIPLAGLSKLPSVPQIAKAFCDDAVGLRFNPVLYPKASQMIVSYDEHEVNNTFKFGVIYQKARQTLEEELFGNNEESPAFKEFLDLLGDTITLQDFKGFRGGLDVTHGQTGVESVYTTFRDREIMFHVSTKLPFTDGDAQQLQRKRHIGNDIVAIIFQEENTPFVPDMIASNFLHAYIVVQVETPGTETPSYKVSVTAREDVPTFGPPLPSPPVFQKGPEFREFLLTKLTNAENACCKSDKFAKLEDRTRAALLDNLHDELHAHTQAMLGLGPEEDKFENGGHGGFLESFKRAIRVRSHSMETMVGGQKKSHSGGIPGSLSGGISHNSMEVTKTTFSPPVVAATVKNQSRSPIKRRSGLFPRLHTGSEGQGDSRARCDSTSSTPKTPDGGHSSQEIKSETSSNPSSPEICPNKEKPFMKLKENGRAISRSSSSTSSVSSTAGEGEAMEEGDSGGSQPSTTSPFKQEVFVYSPSPSSESPSLGAAATPIIMSRSPTDAKSRNSPRSNLKFRFDKLSHASSGAGH

Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations	Modification	Substrate Peptides & Secondary Structure	ASA (%)	Reference
7	Phosphorylation	-MFGRKRSVSFGGFG -CCCCCCCCCCCCCC	25.75	22617229
9	Phosphorylation	FGRKRSVSFGGFGWI CCCCCCCCCCCCCCC	21.30	23401153
23	Phosphorylation	IDKTMLASLKVKKQE CCHHHHHHCCCCHHH	25.43	28060719
34	Phosphorylation	KKQELANSSDATLPD CHHHHCCCCCCCCCC	24.80	28450419
35	Phosphorylation	KQELANSSDATLPDR HHHHCCCCCCCCCCC	30.95	28450419
38	Phosphorylation	LANSSDATLPDRPLS HCCCCCCCCCCCCCC	43.76	26657352
45	Phosphorylation	TLPDRPLSPPLTAPP CCCCCCCCCCCCCCC	27.44	23401153
49	Phosphorylation	RPLSPPLTAPPTMKS CCCCCCCCCCCCCCH	42.78	22115753
53	Phosphorylation	PPLTAPPTMKSSEFF CCCCCCCCCCHHHHH	35.85	28450419
56	Phosphorylation	TAPPTMKSSEFFEML CCCCCCCHHHHHHHH	25.03	26074081
57	Phosphorylation	APPTMKSSEFFEMLE CCCCCCHHHHHHHHH	32.67	26074081
70 (in isoform 2)	Phosphorylation	-	57.58	-
85	Phosphorylation	PQKNKDDYIPYPSID CCCCCCCCCCCCCHH	17.58	27642862
182	Phosphorylation	SLGNLILSVKCEEAE CCCCEEEEEECCCCC	16.73	24719451
201 (in isoform 2)	Ubiquitination	-	47.79	-
216	Ubiquitination	IPLAGLSKLPSVPQI CCCCCHHCCCCHHHH	70.25	-
241	Phosphorylation	LRFNPVLYPKASQMI CCCCCCCCCCHHHEE	11.70	26074081
268	Ubiquitination	KFGVIYQKARQTLEE EEEHHHHHHHHHHHH	28.68	-
304	Ubiquitination	TITLQDFKGFRGGLD EEEHHHCCCCCCCCC	66.48	-
405 (in isoform 3)	Ubiquitination	-	15.65	21906983
409 (in isoform 2)	Ubiquitination	-	4.05	21906983
418	Phosphorylation	TFGPPLPSPPVFQKG CCCCCCCCCCHHHCC	49.90	27050516
424 (in isoform 1)	Ubiquitination	-	66.04	21906983
424	Ubiquitination	PSPPVFQKGPEFREF CCCCHHHCCHHHHHH	66.04	2190698
435	Ubiquitination	FREFLLTKLTNAENA HHHHHHHHHHCHHHH	53.97	-
451	Ubiquitination	CKSDKFAKLEDRTRA CCCCHHHCHHHHHHH	56.39	-
496	Phosphorylation	GHGGFLESFKRAIRV CCCCHHHHHHHHHHH	37.91	-
505	Phosphorylation	KRAIRVRSHSMETMV HHHHHHHCCCCCEEE	19.63	23401153
507	Phosphorylation	AIRVRSHSMETMVGG HHHHHCCCCCEEECC	21.40	23401153
510	Phosphorylation	VRSHSMETMVGGQKK HHCCCCCEEECCEEC	14.44	28450419
518	Phosphorylation	MVGGQKKSHSGGIPG EECCEECCCCCCCCC	29.89	28555341
520	Phosphorylation	GGQKKSHSGGIPGSL CCEECCCCCCCCCCC	45.89	26552605
526	Phosphorylation	HSGGIPGSLSGGISH CCCCCCCCCCCCCCC	17.63	26552605
528	Phosphorylation	GGIPGSLSGGISHNS CCCCCCCCCCCCCCC	36.35	26552605
532	Phosphorylation	GSLSGGISHNSMEVT CCCCCCCCCCCEEEE	21.64	26552605
535	Phosphorylation	SGGISHNSMEVTKTT CCCCCCCCEEEEECC	15.76	26552605
539	Phosphorylation	SHNSMEVTKTTFSPP CCCCEEEEECCCCCC	14.90	26552605
541	Phosphorylation	NSMEVTKTTFSPPVV CCEEEEECCCCCCEE	24.57	28450419
542	Phosphorylation	SMEVTKTTFSPPVVA CEEEEECCCCCCEEE	24.54	28450419
544	Phosphorylation	EVTKTTFSPPVVAAT EEEECCCCCCEEEEE	26.63	25159151
556	Phosphorylation	AATVKNQSRSPIKRR EEEECCCCCCCCCCC	44.08	29514088
558	Phosphorylation	TVKNQSRSPIKRRSG EECCCCCCCCCCCCC	35.90	26055452
564	Phosphorylation	RSPIKRRSGLFPRLH CCCCCCCCCCCCCCC	43.83	22499768
572	Phosphorylation	GLFPRLHTGSEGQGD CCCCCCCCCCCCCCC	47.17	28102081
574	Phosphorylation	FPRLHTGSEGQGDSR CCCCCCCCCCCCCCC	39.44	28102081
580	Phosphorylation	GSEGQGDSRARCDST CCCCCCCCCCCCCCC	34.36	30576142
586	Phosphorylation	DSRARCDSTSSTPKT CCCCCCCCCCCCCCC	33.54	25884760
587	Phosphorylation	SRARCDSTSSTPKTP CCCCCCCCCCCCCCC	17.28	30576142
588	Phosphorylation	RARCDSTSSTPKTPD CCCCCCCCCCCCCCC	35.85	28060719
589	Phosphorylation	ARCDSTSSTPKTPDG CCCCCCCCCCCCCCC	49.14	30576142
590	Phosphorylation	RCDSTSSTPKTPDGG CCCCCCCCCCCCCCC	28.68	28060719
593	Phosphorylation	STSSTPKTPDGGHSS CCCCCCCCCCCCCCC	28.02	23401153
599	Phosphorylation	KTPDGGHSSQEIKSE CCCCCCCCCHHHCCC	36.67	23403867
600	Phosphorylation	TPDGGHSSQEIKSET CCCCCCCCHHHCCCC	26.59	23403867
605	Phosphorylation	HSSQEIKSETSSNPS CCCHHHCCCCCCCCC	52.33	22617229
607	Phosphorylation	SQEIKSETSSNPSSP CHHHCCCCCCCCCCC	44.54	22115753
608	Phosphorylation	QEIKSETSSNPSSPE HHHCCCCCCCCCCCC	24.86	23401153
609	Phosphorylation	EIKSETSSNPSSPEI HHCCCCCCCCCCCCC	61.24	23401153
612	Phosphorylation	SETSSNPSSPEICPN CCCCCCCCCCCCCCC	63.88	25159151
613	Phosphorylation	ETSSNPSSPEICPNK CCCCCCCCCCCCCCC	28.01	23401153
620	Acetylation	SPEICPNKEKPFMKL CCCCCCCCCCCCEEE	52.86	19826871
637	Phosphorylation	NGRAISRSSSSTSSV CCEEECCCCCCCCCC	27.99	28270605
638	Phosphorylation	GRAISRSSSSTSSVS CEEECCCCCCCCCCC	27.48	26657352
639	Phosphorylation	RAISRSSSSTSSVSS EEECCCCCCCCCCCC	38.59	28270605
640	Phosphorylation	AISRSSSSTSSVSST EECCCCCCCCCCCCC	33.97	28270605
641	Phosphorylation	ISRSSSSTSSVSSTA ECCCCCCCCCCCCCC	27.28	28270605
642	Phosphorylation	SRSSSSTSSVSSTAG CCCCCCCCCCCCCCC	30.59	28270605
643	Phosphorylation	RSSSSTSSVSSTAGE CCCCCCCCCCCCCCC	26.55	28270605
645	Phosphorylation	SSSTSSVSSTAGEGE CCCCCCCCCCCCCCC	24.74	28270605
646	Phosphorylation	SSTSSVSSTAGEGEA CCCCCCCCCCCCCCC	21.81	28270605
647	Phosphorylation	STSSVSSTAGEGEAM CCCCCCCCCCCCCCC	31.04	28270605
662	Phosphorylation	EEGDSGGSQPSTTSP CCCCCCCCCCCCCCC	42.30	-
665	Phosphorylation	DSGGSQPSTTSPFKQ CCCCCCCCCCCCCCE	36.36	26074081
666	Phosphorylation	SGGSQPSTTSPFKQE CCCCCCCCCCCCCEE	37.67	26074081
667	Phosphorylation	GGSQPSTTSPFKQEV CCCCCCCCCCCCEEE	38.45	26074081
668	Phosphorylation	GSQPSTTSPFKQEVF CCCCCCCCCCCEEEE	28.55	26074081
677	Phosphorylation	FKQEVFVYSPSPSSE CCEEEEEECCCCCCC	11.91	26074081
678	Phosphorylation	KQEVFVYSPSPSSES CEEEEEECCCCCCCC	17.38	26074081
680	Phosphorylation	EVFVYSPSPSSESPS EEEEECCCCCCCCCC	31.32	26074081
682	Phosphorylation	FVYSPSPSSESPSLG EEECCCCCCCCCCCC	51.59	26074081
683	Phosphorylation	VYSPSPSSESPSLGA EECCCCCCCCCCCCC	45.54	26074081
685	Phosphorylation	SPSPSSESPSLGAAA CCCCCCCCCCCCCCC	23.03	26074081
687	Phosphorylation	SPSSESPSLGAAATP CCCCCCCCCCCCCCC	49.03	28270605
693	Phosphorylation	PSLGAAATPIIMSRS CCCCCCCCCEEECCC	15.42	28270605
698	Phosphorylation	AATPIIMSRSPTDAK CCCCEEECCCCCCHH	21.14	28270605
700	Phosphorylation	TPIIMSRSPTDAKSR CCEEECCCCCCHHHC	25.50	28270605
702	Phosphorylation	IIMSRSPTDAKSRNS EEECCCCCCHHHCCC	50.24	28270605
706	Phosphorylation	RSPTDAKSRNSPRSN CCCCCHHHCCCCCCC	38.11	30576142

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
7	S	Phosphorylation	Kinase	PKACA	P17612	PSP
7	S	Phosphorylation	Kinase	PKG1	Q13976	PSP

Functions of PTM Sites

Modified Location	Modified Residue	Modification	Function	Reference
7	S	Phosphorylation		15632203
In vitro phosphorylated by cGMP-dependent protein kinase 1 (cGKI) at Ser-7; the phosphorylation probably does not regulate GAP activity.

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 RPGP2_HUMAN !!

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference	Domain-Domain Interactions
Oops, there are no PPI records of RPGP2_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 RPGP2_HUMAN

Related Literatures of Post-Translational Modification

Phosphorylation
Reference	PubMed
"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-45; THR-49 AND SER-544,AND MASS SPECTROMETRY.	19690332 [Abstract]
"Lys-N and trypsin cover complementary parts of the phosphoproteome ina refined SCX-based approach."; Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J.,Mohammed S.; Anal. Chem. 81:4493-4501(2009). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-609 AND SER-613, ANDMASS SPECTROMETRY.	19413330 [Abstract]
"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-45 AND THR-49, AND MASSSPECTROMETRY.	18669648 [Abstract]
"A probability-based approach for high-throughput proteinphosphorylation analysis and site localization."; Beausoleil S.A., Villen J., Gerber S.A., Rush J., Gygi S.P.; Nat. Biotechnol. 24:1285-1292(2006). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-544, AND MASSSPECTROMETRY.	16964243 [Abstract]
"Rap1GAP2 is a new GTPase-activating protein of Rap1 expressed inhuman platelets."; Schultess J., Danielewski O., Smolenski A.P.; Blood 105:3185-3192(2005). Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1 AND 2), FUNCTION,PHOSPHORYLATION AT SER-7, SUBCELLULAR LOCATION, TISSUE SPECIFICITY,AND MUTAGENESIS OF SER-7 AND ASN-357.	15632203 [Abstract]

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