ARFG3_HUMAN - dbPTM
ARFG3_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID ARFG3_HUMAN
UniProt AC Q9NP61
Protein Name ADP-ribosylation factor GTPase-activating protein 3
Gene Name ARFGAP3
Organism Homo sapiens (Human).
Sequence Length 516
Subcellular Localization Cytoplasm . Golgi apparatus membrane
Peripheral membrane protein
Cytoplasmic side . Also found on peripheral punctate structures likely to be endoplasmic reticulum-Golgi intermediate compartment.
Protein Description GTPase-activating protein (GAP) for ADP ribosylation factor 1 (ARF1). Hydrolysis of ARF1-bound GTP may lead to dissociation of coatomer from Golgi-derived membranes to allow fusion with target membranes..
Protein Sequence MGDPSKQDILTIFKRLRSVPTNKVCFDCGAKNPSWASITYGVFLCIDCSGSHRSLGVHLSFIRSTELDSNWSWFQLRCMQVGGNASASSFFHQHGCSTNDTNAKYNSRAAQLYREKIKSLASQATRKHGTDLWLDSCVVPPLSPPPKEEDFFASHVSPEVSDTAWASAIAEPSSLTSRPVETTLENNEGGQEQGPSVEGLNVPTKATLEVSSIIKKKPNQAKKGLGAKKGSLGAQKLANTCFNEIEKQAQAADKMKEQEDLAKVVSKEESIVSSLRLAYKDLEIQMKKDEKMNISGKKNVDSDRLGMGFGNCRSVISHSVTSDMQTIEQESPIMAKPRKKYNDDSDDSYFTSSSSYFDEPVELRSSSFSSWDDSSDSYWKKETSKDTETVLKTTGYSDRPTARRKPDYEPVENTDEAQKKFGNVKAISSDMYFGRQSQADYETRARLERLSASSSISSADLFEEPRKQPAGNYSLSSVLPNAPDMAQFKQGVRSVAGKLSVFANGVVTSIQDRYGS
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
14UbiquitinationQDILTIFKRLRSVPT
HHHHHHHHHHHCCCC		46.8221890473
23AcetylationLRSVPTNKVCFDCGA
HHCCCCCCEEECCCC		42.7426051181
113PhosphorylationNSRAAQLYREKIKSL
HHHHHHHHHHHHHHH		12.49-
118UbiquitinationQLYREKIKSLASQAT
HHHHHHHHHHHHHHH		50.95-
143PhosphorylationSCVVPPLSPPPKEED
CEECCCCCCCCCHHH		40.9325159151
154PhosphorylationKEEDFFASHVSPEVS
CHHHCCHHCCCHHHC		21.1826074081
157PhosphorylationDFFASHVSPEVSDTA
HCCHHCCCHHHCCCH		15.2126074081
161PhosphorylationSHVSPEVSDTAWASA
HCCCHHHCCCHHHHH		27.8126074081
173PhosphorylationASAIAEPSSLTSRPV
HHHHCCCCCCCCCCC		29.5024275569
174PhosphorylationSAIAEPSSLTSRPVE
HHHCCCCCCCCCCCE		46.5124275569
179AcetylationPSSLTSRPVETTLEN
CCCCCCCCCEEEEEC		28.2319608861
183PhosphorylationTSRPVETTLENNEGG
CCCCCEEEEECCCCC		20.6924275569
184AcetylationSRPVETTLENNEGGQ
CCCCEEEEECCCCCC		9.6519608861
185AcetylationRPVETTLENNEGGQE
CCCEEEEECCCCCCC		56.7819608861
207PhosphorylationLNVPTKATLEVSSII
CCCCCCCEEEHHHHH		25.6320068231
211PhosphorylationTKATLEVSSIIKKKP
CCCEEEHHHHHHCCC		13.3725159151
212PhosphorylationKATLEVSSIIKKKPN
CCEEEHHHHHHCCCC		33.2425159151
223AcetylationKKPNQAKKGLGAKKG
CCCCCCCCCCCCCCC		63.4821466224
228AcetylationAKKGLGAKKGSLGAQ
CCCCCCCCCCCHHHH		56.7321466224
229AcetylationKKGLGAKKGSLGAQK
CCCCCCCCCCHHHHH		53.8821466224
231PhosphorylationGLGAKKGSLGAQKLA
CCCCCCCCHHHHHHH		32.2925072903
236AcetylationKGSLGAQKLANTCFN
CCCHHHHHHHHHHHH		49.3725953088
236UbiquitinationKGSLGAQKLANTCFN
CCCHHHHHHHHHHHH		49.37-
247UbiquitinationTCFNEIEKQAQAADK
HHHHHHHHHHHHHHH		57.50-
2632-HydroxyisobutyrylationKEQEDLAKVVSKEES
HHHHHHHHHHCHHHH		50.93-
263UbiquitinationKEQEDLAKVVSKEES
HHHHHHHHHHCHHHH		50.93-
266O-linked_GlycosylationEDLAKVVSKEESIVS
HHHHHHHCHHHHHHH		37.0228657654
270PhosphorylationKVVSKEESIVSSLRL
HHHCHHHHHHHHHHH		29.4025850435
273PhosphorylationSKEESIVSSLRLAYK
CHHHHHHHHHHHHHH		23.2225850435
274PhosphorylationKEESIVSSLRLAYKD
HHHHHHHHHHHHHHH		13.4525850435
279PhosphorylationVSSLRLAYKDLEIQM
HHHHHHHHHHHHHHC		15.0429978859
280AcetylationSSLRLAYKDLEIQMK
HHHHHHHHHHHHHCC		50.6725953088
295PhosphorylationKDEKMNISGKKNVDS
CCCCCCCCCCCCCCH		39.2924719451
314PhosphorylationMGFGNCRSVISHSVT
CCCCHHHHHHHCCCC		26.4623403867
317PhosphorylationGNCRSVISHSVTSDM
CHHHHHHHCCCCCCC		13.9323403867
319PhosphorylationCRSVISHSVTSDMQT
HHHHHHCCCCCCCCC		21.9423403867
321PhosphorylationSVISHSVTSDMQTIE
HHHHCCCCCCCCCCC		23.2523403867
322PhosphorylationVISHSVTSDMQTIEQ
HHHCCCCCCCCCCCC		29.0023403867
326PhosphorylationSVTSDMQTIEQESPI
CCCCCCCCCCCCCCC		21.6123403867
331PhosphorylationMQTIEQESPIMAKPR
CCCCCCCCCCCCCCC		21.3023401153
336UbiquitinationQESPIMAKPRKKYND
CCCCCCCCCCCCCCC		28.16-
341PhosphorylationMAKPRKKYNDDSDDS
CCCCCCCCCCCCCCC		27.1930576142
345PhosphorylationRKKYNDDSDDSYFTS
CCCCCCCCCCCCCCC		46.2924719451
348PhosphorylationYNDDSDDSYFTSSSS
CCCCCCCCCCCCCCC		27.4329978859
349PhosphorylationNDDSDDSYFTSSSSY
CCCCCCCCCCCCCCC		20.1928464451
351PhosphorylationDSDDSYFTSSSSYFD
CCCCCCCCCCCCCCC		21.3329978859
352PhosphorylationSDDSYFTSSSSYFDE
CCCCCCCCCCCCCCC		20.5129978859
353PhosphorylationDDSYFTSSSSYFDEP
CCCCCCCCCCCCCCC		21.9029978859
354PhosphorylationDSYFTSSSSYFDEPV
CCCCCCCCCCCCCCE		28.9128464451
355PhosphorylationSYFTSSSSYFDEPVE
CCCCCCCCCCCCCEE		31.5929978859
356PhosphorylationYFTSSSSYFDEPVEL
CCCCCCCCCCCCEEE		19.5929978859
365PhosphorylationDEPVELRSSSFSSWD
CCCEEECCCCCCCCC		42.8522617229
366PhosphorylationEPVELRSSSFSSWDD
CCEEECCCCCCCCCC		29.0328102081
367PhosphorylationPVELRSSSFSSWDDS
CEEECCCCCCCCCCC		30.3225159151
369PhosphorylationELRSSSFSSWDDSSD
EECCCCCCCCCCCCC		32.2525159151
370PhosphorylationLRSSSFSSWDDSSDS
ECCCCCCCCCCCCCC		32.3025159151
374PhosphorylationSFSSWDDSSDSYWKK
CCCCCCCCCCCCCEE		33.3125159151
375PhosphorylationFSSWDDSSDSYWKKE
CCCCCCCCCCCCEEC		37.2523403867
377PhosphorylationSWDDSSDSYWKKETS
CCCCCCCCCCEECCC		34.5428796482
378PhosphorylationWDDSSDSYWKKETSK
CCCCCCCCCEECCCC		26.6628796482
380UbiquitinationDSSDSYWKKETSKDT
CCCCCCCEECCCCCC		32.28-
381UbiquitinationSSDSYWKKETSKDTE
CCCCCCEECCCCCCC		52.67-
392UbiquitinationKDTETVLKTTGYSDR
CCCCHHHHHCCCCCC		39.4421890473
394PhosphorylationTETVLKTTGYSDRPT
CCHHHHHCCCCCCCC		32.3227251275
396PhosphorylationTVLKTTGYSDRPTAR
HHHHHCCCCCCCCCC		12.81-
397PhosphorylationVLKTTGYSDRPTARR
HHHHCCCCCCCCCCC		28.6127251275
401PhosphorylationTGYSDRPTARRKPDY
CCCCCCCCCCCCCCC		33.4230576142
405UbiquitinationDRPTARRKPDYEPVE
CCCCCCCCCCCCCCC		36.37-
408PhosphorylationTARRKPDYEPVENTD
CCCCCCCCCCCCCCH		30.5721945579
414PhosphorylationDYEPVENTDEAQKKF
CCCCCCCCHHHHHHH		23.01-
425UbiquitinationQKKFGNVKAISSDMY
HHHHCCEEEEECCCC		43.96-
428PhosphorylationFGNVKAISSDMYFGR
HCCEEEEECCCCCCC		25.7422617229
429PhosphorylationGNVKAISSDMYFGRQ
CCEEEEECCCCCCCH		21.9322617229
431SulfoxidationVKAISSDMYFGRQSQ
EEEEECCCCCCCHHH		3.0130846556
432PhosphorylationKAISSDMYFGRQSQA
EEEECCCCCCCHHHC		14.1028796482
437PhosphorylationDMYFGRQSQADYETR
CCCCCCHHHCCHHHH		26.4428857561
441PhosphorylationGRQSQADYETRARLE
CCHHHCCHHHHHHHH		23.4028796482
443PhosphorylationQSQADYETRARLERL
HHHCCHHHHHHHHHH		24.3326552605
451PhosphorylationRARLERLSASSSISS
HHHHHHHHHCCCCCH		32.1225159151
453PhosphorylationRLERLSASSSISSAD
HHHHHHHCCCCCHHH		22.6525159151
454PhosphorylationLERLSASSSISSADL
HHHHHHCCCCCHHHH		31.2625693802
455PhosphorylationERLSASSSISSADLF
HHHHHCCCCCHHHHC		24.8022617229
457PhosphorylationLSASSSISSADLFEE
HHHCCCCCHHHHCCC		22.7825693802
458PhosphorylationSASSSISSADLFEEP
HHCCCCCHHHHCCCC		24.9225693802
467UbiquitinationDLFEEPRKQPAGNYS
HHCCCCCCCCCCCCC		71.93-
473PhosphorylationRKQPAGNYSLSSVLP
CCCCCCCCCHHHCCC		15.2928796482
474PhosphorylationKQPAGNYSLSSVLPN
CCCCCCCCHHHCCCC		26.2728796482
476PhosphorylationPAGNYSLSSVLPNAP
CCCCCCHHHCCCCCC		16.6828796482
477PhosphorylationAGNYSLSSVLPNAPD
CCCCCHHHCCCCCCC		32.7328796482
489UbiquitinationAPDMAQFKQGVRSVA
CCCHHHHHHHHHHHH		33.78-
498AcetylationGVRSVAGKLSVFANG
HHHHHHHHHHHHHCC		28.0525953088
500PhosphorylationRSVAGKLSVFANGVV
HHHHHHHHHHHCCEE		20.7620393185
508PhosphorylationVFANGVVTSIQDRYG
HHHCCEEEEHHHHCC		20.0827251275
509O-linked_GlycosylationFANGVVTSIQDRYGS
HHCCEEEEHHHHCCC		13.4728657654
509PhosphorylationFANGVVTSIQDRYGS
HHCCEEEEHHHHCCC		13.4727251275
513MethylationVVTSIQDRYGS----
EEEEHHHHCCC----		22.72-
516PhosphorylationSIQDRYGS-------
EHHHHCCC-------		28.2822199227
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 ARFG3_HUMAN !!
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of ARFG3_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 ARFG3_HUMAN !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
A4_HUMANAPPphysical
21832049
CD14_HUMANCD14physical
21988832
IL8_HUMANCXCL8physical
21988832
SHPK_HUMANSHPKphysical
26186194
MTND_HUMANADI1physical
26344197
ARFG1_HUMANARFGAP1physical
26344197
PLEC_HUMANPLECphysical
27173435
VIP2_HUMANPPIP5K2physical
27173435
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 ARFG3_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-223; LYS-228 AND LYS-229,AND MASS SPECTROMETRY.
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-370 AND SER-453, ANDMASS SPECTROMETRY.
"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-428, 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-331 AND SER-453, ANDMASS SPECTROMETRY.
"Automated phosphoproteome analysis for cultured cancer cells by two-dimensional nanoLC-MS using a calcined titania/C18 biphasic column.";
Imami K., Sugiyama N., Kyono Y., Tomita M., Ishihama Y.;
Anal. Sci. 24:161-166(2008).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-270, AND MASSSPECTROMETRY.
"Improved titanium dioxide enrichment of phosphopeptides from HeLacells and high confident phosphopeptide identification by cross-validation of MS/MS and MS/MS/MS spectra.";
Yu L.-R., Zhu Z., Chan K.C., Issaq H.J., Dimitrov D.S., Veenstra T.D.;
J. Proteome Res. 6:4150-4162(2007).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-331, AND MASSSPECTROMETRY.
"Global, in vivo, and site-specific phosphorylation dynamics insignaling networks.";
Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P.,Mann M.;
Cell 127:635-648(2006).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-143, AND MASSSPECTROMETRY.

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