ARFG1_HUMAN - dbPTM
ARFG1_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID ARFG1_HUMAN
UniProt AC Q8N6T3
Protein Name ADP-ribosylation factor GTPase-activating protein 1
Gene Name ARFGAP1
Organism Homo sapiens (Human).
Sequence Length 406
Subcellular Localization Cytoplasm. Golgi apparatus. Associates with the Golgi complex..
Protein Description GTPase-activating protein (GAP) for the ADP ribosylation factor 1 (ARF1). Involved in membrane trafficking and /or vesicle transport. Promotes hydrolysis of the ARF1-bound GTP and thus, is required for the dissociation of coat proteins from Golgi-derived membranes and vesicles, a prerequisite for vesicle's fusion with target compartment. Probably regulates ARF1-mediated transport via its interaction with the KDELR proteins and TMED2. Overexpression induces the redistribution of the entire Golgi complex to the endoplasmic reticulum, as when ARF1 is deactivated. Its activity is stimulated by phosphoinosides and inhibited by phosphatidylcholine (By similarity)..
Protein Sequence MASPRTRKVLKEVRVQDENNVCFECGAFNPQWVSVTYGIWICLECSGRHRGLGVHLSFVRSVTMDKWKDIELEKMKAGGNAKFREFLESQEDYDPCWSLQEKYNSRAAALFRDKVVALAEGREWSLESSPAQNWTPPQPRTLPSMVHRVSGQPQSVTASSDKAFEDWLNDDLGSYQGAQGNRYVGFGNTPPPQKKEDDFLNNAMSSLYSGWSSFTTGASRFASAAKEGATKFGSQASQKASELGHSLNENVLKPAQEKVKEGKIFDDVSSGVSQLASKVQGVGSKGWRDVTTFFSGKAEGPLDSPSEGHSYQNSGLDHFQNSNIDQSFWETFGSAEPTKTRKSPSSDSWTCADTSTERRSSDSWEVWGSASTNRNSNSDGGEGGEGTKKAVPPAVPTDDGWDNQNW
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
3Phosphorylation-----MASPRTRKVL
-----CCCHHHHHHH		17.3926074081
6Phosphorylation--MASPRTRKVLKEV
--CCCHHHHHHHHHC		37.9226074081
49UbiquitinationCLECSGRHRGLGVHL
EHHCCCCCCCCCEEH		31.52-
57PhosphorylationRGLGVHLSFVRSVTM
CCCCEEHHEEEEECC		13.5524247654
63PhosphorylationLSFVRSVTMDKWKDI
HHEEEEECCCCCCCC		22.39-
68UbiquitinationSVTMDKWKDIELEKM
EECCCCCCCCCHHHH		55.35-
74AcetylationWKDIELEKMKAGGNA
CCCCCHHHHHCCCCH		59.3222424773
74UbiquitinationWKDIELEKMKAGGNA
CCCCCHHHHHCCCCH		59.32-
82UbiquitinationMKAGGNAKFREFLES
HHCCCCHHHHHHHHC		49.29-
93PhosphorylationFLESQEDYDPCWSLQ
HHHCCCCCCCCHHHH		22.4920044836
98PhosphorylationEDYDPCWSLQEKYNS
CCCCCCHHHHHHHHH		27.2220044836
102UbiquitinationPCWSLQEKYNSRAAA
CCHHHHHHHHHHHHH		36.45-
102 (in isoform 2)Ubiquitination-36.45-
103PhosphorylationCWSLQEKYNSRAAAL
CHHHHHHHHHHHHHH		20.02-
105PhosphorylationSLQEKYNSRAAALFR
HHHHHHHHHHHHHHH		21.87-
114UbiquitinationAAALFRDKVVALAEG
HHHHHHHHHHHHHCC		34.06-
118AcetylationFRDKVVALAEGREWS
HHHHHHHHHCCCCCC		2.77-
118UbiquitinationFRDKVVALAEGREWS
HHHHHHHHHCCCCCC		2.77-
118AcetylationFRDKVVALAEGREWS
HHHHHHHHHCCCCCC		2.7719608861
125PhosphorylationLAEGREWSLESSPAQ
HHCCCCCCCCCCCCC		19.9425159151
128PhosphorylationGREWSLESSPAQNWT
CCCCCCCCCCCCCCC		47.0930266825
129PhosphorylationREWSLESSPAQNWTP
CCCCCCCCCCCCCCC		18.1930266825
135PhosphorylationSSPAQNWTPPQPRTL
CCCCCCCCCCCCCCC		32.4222167270
141O-linked_GlycosylationWTPPQPRTLPSMVHR
CCCCCCCCCCCCCHH		50.1030059200
141PhosphorylationWTPPQPRTLPSMVHR
CCCCCCCCCCCCCHH		50.1025159151
144O-linked_GlycosylationPQPRTLPSMVHRVSG
CCCCCCCCCCHHCCC		36.2330059200
144PhosphorylationPQPRTLPSMVHRVSG
CCCCCCCCCCHHCCC		36.2323401153
150PhosphorylationPSMVHRVSGQPQSVT
CCCCHHCCCCCCEEE		31.5030266825
155PhosphorylationRVSGQPQSVTASSDK
HCCCCCCEEECCCCH		28.2830266825
157PhosphorylationSGQPQSVTASSDKAF
CCCCCEEECCCCHHH		26.5229255136
159PhosphorylationQPQSVTASSDKAFED
CCCEEECCCCHHHHH		29.6929255136
160PhosphorylationPQSVTASSDKAFEDW
CCEEECCCCHHHHHH		40.4429255136
162UbiquitinationSVTASSDKAFEDWLN
EEECCCCHHHHHHHH		57.85-
162 (in isoform 2)Ubiquitination-57.85-
165UbiquitinationASSDKAFEDWLNDDL
CCCCHHHHHHHHCCC		53.81-
172UbiquitinationEDWLNDDLGSYQGAQ
HHHHHCCCCCCCCCC		5.68-
174PhosphorylationWLNDDLGSYQGAQGN
HHHCCCCCCCCCCCC		22.9128796482
175PhosphorylationLNDDLGSYQGAQGNR
HHCCCCCCCCCCCCC		14.7928796482
178AcetylationDLGSYQGAQGNRYVG
CCCCCCCCCCCCCCC		9.8919608861
183PhosphorylationQGAQGNRYVGFGNTP
CCCCCCCCCCCCCCC		14.6628796482
189PhosphorylationRYVGFGNTPPPQKKE
CCCCCCCCCCCCCCH		37.2419664994
194UbiquitinationGNTPPPQKKEDDFLN
CCCCCCCCCHHHHHH		65.00-
203 (in isoform 5)Phosphorylation-9.7320068231
206PhosphorylationFLNNAMSSLYSGWSS
HHHHHHHHHHHCHHH		20.4528464451
208PhosphorylationNNAMSSLYSGWSSFT
HHHHHHHHHCHHHHH		13.69-
209PhosphorylationNAMSSLYSGWSSFTT
HHHHHHHHCHHHHHH		38.7925332170
212PhosphorylationSSLYSGWSSFTTGAS
HHHHHCHHHHHHHHH		21.0625332170
213PhosphorylationSLYSGWSSFTTGASR
HHHHCHHHHHHHHHH		21.8025627689
226AcetylationSRFASAAKEGATKFG
HHHHHHHHHHHHHHC		57.29156561
226UbiquitinationSRFASAAKEGATKFG
HHHHHHHHHHHHHHC		57.29-
230 (in isoform 5)Phosphorylation-37.4520873877
231SumoylationAAKEGATKFGSQASQ
HHHHHHHHHCHHHHH		47.39-
231AcetylationAAKEGATKFGSQASQ
HHHHHHHHHCHHHHH		47.3919608861
231SumoylationAAKEGATKFGSQASQ
HHHHHHHHHCHHHHH		47.3919608861
231UbiquitinationAAKEGATKFGSQASQ
HHHHHHHHHCHHHHH		47.3919608861
234PhosphorylationEGATKFGSQASQKAS
HHHHHHCHHHHHHHH		26.2126434776
237PhosphorylationTKFGSQASQKASELG
HHHCHHHHHHHHHHC		25.2829514088
239UbiquitinationFGSQASQKASELGHS
HCHHHHHHHHHHCCC		51.92-
241PhosphorylationSQASQKASELGHSLN
HHHHHHHHHHCCCCC		40.1523403867
246PhosphorylationKASELGHSLNENVLK
HHHHHCCCCCHHCCH		30.9630278072
253AcetylationSLNENVLKPAQEKVK
CCCHHCCHHHHHHHH		33.7423954790
253UbiquitinationSLNENVLKPAQEKVK
CCCHHCCHHHHHHHH		33.74-
256 (in isoform 2)Phosphorylation-60.6220068231
263AcetylationQEKVKEGKIFDDVSS
HHHHHCCCCCCCHHH		41.09130611
263UbiquitinationQEKVKEGKIFDDVSS
HHHHHCCCCCCCHHH		41.09-
269PhosphorylationGKIFDDVSSGVSQLA
CCCCCCHHHHHHHHH		28.5020068231
270PhosphorylationKIFDDVSSGVSQLAS
CCCCCHHHHHHHHHH		42.9621406692
273PhosphorylationDDVSSGVSQLASKVQ
CCHHHHHHHHHHHHC		24.0120873877
277PhosphorylationSGVSQLASKVQGVGS
HHHHHHHHHHCCCCC		41.7921406692
278UbiquitinationGVSQLASKVQGVGSK
HHHHHHHHHCCCCCC		32.7321906983
278 (in isoform 1)Ubiquitination-32.7321906983
283 (in isoform 2)Phosphorylation-30.3920873877
284PhosphorylationSKVQGVGSKGWRDVT
HHHCCCCCCCCEEEE		26.1128857561
285UbiquitinationKVQGVGSKGWRDVTT
HHCCCCCCCCEEEEH		57.47-
291PhosphorylationSKGWRDVTTFFSGKA
CCCCEEEEHHCCCCC		23.3628857561
295PhosphorylationRDVTTFFSGKAEGPL
EEEEHHCCCCCCCCC		34.8821815630
297SumoylationVTTFFSGKAEGPLDS
EEHHCCCCCCCCCCC		41.91-
304PhosphorylationKAEGPLDSPSEGHSY
CCCCCCCCCCCCCCC		37.7025106551
306PhosphorylationEGPLDSPSEGHSYQN
CCCCCCCCCCCCCCC		61.2325106551
310PhosphorylationDSPSEGHSYQNSGLD
CCCCCCCCCCCCCCH		38.9918669648
311PhosphorylationSPSEGHSYQNSGLDH
CCCCCCCCCCCCCHH		13.1618669648
314PhosphorylationEGHSYQNSGLDHFQN
CCCCCCCCCCHHHCC		25.8028464451
322PhosphorylationGLDHFQNSNIDQSFW
CCHHHCCCCCCHHHH		25.1229496963
327PhosphorylationQNSNIDQSFWETFGS
CCCCCCHHHHHHHCC		28.6928464451
331PhosphorylationIDQSFWETFGSAEPT
CCHHHHHHHCCCCCC		24.7226074081
334PhosphorylationSFWETFGSAEPTKTR
HHHHHHCCCCCCCCC		25.8520068231
338PhosphorylationTFGSAEPTKTRKSPS
HHCCCCCCCCCCCCC		36.2326074081
339UbiquitinationFGSAEPTKTRKSPSS
HCCCCCCCCCCCCCC		57.98-
340PhosphorylationGSAEPTKTRKSPSSD
CCCCCCCCCCCCCCC		45.8923403867
342UbiquitinationAEPTKTRKSPSSDSW
CCCCCCCCCCCCCCC		72.46-
343PhosphorylationEPTKTRKSPSSDSWT
CCCCCCCCCCCCCCE		27.0719664994
345PhosphorylationTKTRKSPSSDSWTCA
CCCCCCCCCCCCEEC		54.6022167270
346PhosphorylationKTRKSPSSDSWTCAD
CCCCCCCCCCCEECC		38.7630266825
348PhosphorylationRKSPSSDSWTCADTS
CCCCCCCCCEECCCC		26.6630266825
350PhosphorylationSPSSDSWTCADTSTE
CCCCCCCEECCCCCC		11.1922167270
351PhosphorylationPSSDSWTCADTSTER
CCCCCCEECCCCCCC		2.3427251275
353PhosphorylationSDSWTCADTSTERRS
CCCCEECCCCCCCCC		43.2527251275
354PhosphorylationDSWTCADTSTERRSS
CCCEECCCCCCCCCC		21.0125159151
355PhosphorylationSWTCADTSTERRSSD
CCEECCCCCCCCCCC		28.9023927012
356PhosphorylationWTCADTSTERRSSDS
CEECCCCCCCCCCCC		35.2923403867
360PhosphorylationDTSTERRSSDSWEVW
CCCCCCCCCCCEEEE		44.7223401153
361PhosphorylationTSTERRSSDSWEVWG
CCCCCCCCCCEEEEE		33.5823927012
363PhosphorylationTERRSSDSWEVWGSA
CCCCCCCCEEEEEEC		27.3830266825
368PhosphorylationSDSWEVWGSASTNRN
CCCEEEEEECCCCCC		20.6427251275
369PhosphorylationDSWEVWGSASTNRNS
CCEEEEEECCCCCCC		11.8823927012
371PhosphorylationWEVWGSASTNRNSNS
EEEEEECCCCCCCCC		28.1023927012
372PhosphorylationEVWGSASTNRNSNSD
EEEEECCCCCCCCCC		37.6023663014
376PhosphorylationSASTNRNSNSDGGEG
ECCCCCCCCCCCCCC		34.1825849741
378PhosphorylationSTNRNSNSDGGEGGE
CCCCCCCCCCCCCCC		37.1426657352
384PhosphorylationNSDGGEGGEGTKKAV
CCCCCCCCCCCCCCC		26.3427251275
387PhosphorylationGGEGGEGTKKAVPPA
CCCCCCCCCCCCCCC		25.6824300666
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
-KUbiquitinationE3 ubiquitin ligaseTRIP12Q14669
PMID:22028794
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of ARFG1_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 ARFG1_HUMAN !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
ERD21_HUMANKDELR1physical
11703931
LRRK2_HUMANLRRK2physical
22423108
LRRK2_HUMANLRRK2physical
22363216
A4_HUMANAPPphysical
21832049
RAB23_HUMANRAB23physical
21988832
KAPCB_HUMANPRKACBphysical
21988832
RL11_HUMANRPL11physical
21988832
RFC3_HUMANRFC3physical
21988832
REEP5_HUMANREEP5physical
21988832
MED27_HUMANMED27physical
21988832
CSN5_HUMANCOPS5physical
21988832
RAIN_HUMANRASIP1physical
21988832
ASB10_HUMANASB10physical
21988832
HXK1_HUMANHK1physical
22863883
KRA32_HUMANKRTAP3-2physical
25416956
KRA92_HUMANKRTAP9-2physical
25416956
KR109_HUMANKRTAP10-9physical
25416956
TCEA1_HUMANTCEA1physical
26344197
SHIP2_HUMANINPPL1physical
28514442
SCC4_HUMANMAU2physical
28514442
AP2A1_HUMANAP2A1physical
28514442
DIP2B_HUMANDIP2Bphysical
28514442
NIPBL_HUMANNIPBLphysical
28514442
AP2M1_HUMANAP2M1physical
28514442
AURKA_HUMANAURKAphysical
28514442
AP1B1_HUMANAP1B1physical
28514442
FNTB_HUMANFNTBphysical
28514442
AP2A2_HUMANAP2A2physical
28514442
JIP4_HUMANSPAG9physical
28514442
POTEF_HUMANPOTEFphysical
28514442
AP2S1_HUMANAP2S1physical
28514442
AP2B1_HUMANAP2B1physical
28514442
FNTA_HUMANFNTAphysical
28514442
TGFA1_HUMANTGFBRAP1physical
28514442
UFSP2_HUMANUFSP2physical
28514442
SEC63_HUMANSEC63physical
28514442
STX5_HUMANSTX5physical
28514442
RIC8A_HUMANRIC8Aphysical
28514442
DPYL1_HUMANCRMP1physical
28514442
CARM1_HUMANCARM1physical
28514442
ARF1_HUMANARF1physical
16332543
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 ARFG1_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-231, AND MASS SPECTROMETRY.
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 THR-135 AND SER-304, ANDMASS SPECTROMETRY.
"Global proteomic profiling of phosphopeptides using electron transferdissociation tandem mass spectrometry.";
Molina H., Horn D.M., Tang N., Mathivanan S., Pandey A.;
Proc. Natl. Acad. Sci. U.S.A. 104:2199-2204(2007).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-246, AND MASSSPECTROMETRY.
"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 THR-189, AND MASSSPECTROMETRY.
"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 THR-189, AND MASSSPECTROMETRY.
"Combining protein-based IMAC, peptide-based IMAC, and MudPIT forefficient phosphoproteomic analysis.";
Cantin G.T., Yi W., Lu B., Park S.K., Xu T., Lee J.-D.,Yates J.R. III;
J. Proteome Res. 7:1346-1351(2008).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-135, AND MASSSPECTROMETRY.
"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 THR-189, AND MASSSPECTROMETRY.
"Large-scale characterization of HeLa cell nuclear phosphoproteins.";
Beausoleil S.A., Jedrychowski M., Schwartz D., Elias J.E., Villen J.,Li J., Cohn M.A., Cantley L.C., Gygi S.P.;
Proc. Natl. Acad. Sci. U.S.A. 101:12130-12135(2004).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-135, AND MASSSPECTROMETRY.

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