ARFG2_MOUSE - dbPTM
ARFG2_MOUSE - PTM Information in dbPTM
Basic Information of Protein
UniProt ID ARFG2_MOUSE
UniProt AC Q99K28
Protein Name ADP-ribosylation factor GTPase-activating protein 2
Gene Name Arfgap2
Organism Mus musculus (Mouse).
Sequence Length 520
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). May regulate coatomer-mediated protein transport from the Golgi complex to the endoplasmic reticulum. Hydrolysis of ARF1-bound GTP may lead to dissociation of coatomer from Golgi-derived membranes to allow fusion with target membranes (By similarity)..
Protein Sequence MAASPSKTEIQTIFKRLRAIPTNKACFDCGAKSPSWASITYGVFLCIDCSGVHRSLGVHLSFIRSTELDSNWSWLQLRCMQVGGNANATAFFRQHGCMANDANTKYTSRAAQMYREKIRQLGSAALTRHGTDLWIDSMNSAPSHSPEKKDSDFFTEHTQAPAWDTAATDPSGTQQPALPSESSSLAQPEQGPNTDLLGTSPQASLELKSSIIGKKKPAAAKKGLGAKKGLGAQKVSNQSFTEIERQAQVAEKLREQQAADAKKQAEESMVASMRLAYQELQIDRKKEEKKLQNLEGKKREQAERLGMGLVSRSSISHSVLSEMQMIEQETPLSAKSSRSQLDLFDDVGTFASGPPKYKDNPFSLGETFGSRWDSDAAWGMDRVEEKEPEVTISSIRPISERTASRREVETRSSGLESSEARQKFAGAKAISSDMFFGREVDSEYEARSRLQQLSGSSAISSSDLFGNMDGAHGGGTVSLGNVLPTADIAQFKQGVKSVAGKMAVLANGVMNSLQDRYGSY
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
2Acetylation------MAASPSKTE
------CCCCCCHHH		19.35-
4 (in isoform 2)Phosphorylation-21.8424719451
4Phosphorylation----MAASPSKTEIQ
----CCCCCCHHHHH		21.8426824392
6Phosphorylation--MAASPSKTEIQTI
--CCCCCCHHHHHHH		50.1126745281
8PhosphorylationMAASPSKTEIQTIFK
CCCCCCHHHHHHHHH		42.5329233185
12PhosphorylationPSKTEIQTIFKRLRA
CCHHHHHHHHHHHCC		33.7629233185
15SuccinylationTEIQTIFKRLRAIPT
HHHHHHHHHHCCCCC		46.8223954790
15AcetylationTEIQTIFKRLRAIPT
HHHHHHHHHHCCCCC		46.8222826441
24MalonylationLRAIPTNKACFDCGA
HCCCCCCCCCCCCCC		49.3526320211
131PhosphorylationAALTRHGTDLWIDSM
HHHHHHCCCCEEECC		23.0718846507
137PhosphorylationGTDLWIDSMNSAPSH
CCCCEEECCCCCCCC		15.6627742792
140PhosphorylationLWIDSMNSAPSHSPE
CEEECCCCCCCCCCC		32.6827087446
143PhosphorylationDSMNSAPSHSPEKKD
ECCCCCCCCCCCCCC		35.9926824392
145PhosphorylationMNSAPSHSPEKKDSD
CCCCCCCCCCCCCCC		38.8127087446
145 (in isoform 2)Phosphorylation-38.8124719451
171PhosphorylationDTAATDPSGTQQPAL
CCCCCCCCCCCCCCC		58.2323140645
173PhosphorylationAATDPSGTQQPALPS
CCCCCCCCCCCCCCC		28.5023140645
180PhosphorylationTQQPALPSESSSLAQ
CCCCCCCCCCCCCCC		51.4623140645
182PhosphorylationQPALPSESSSLAQPE
CCCCCCCCCCCCCCC		29.5723140645
183PhosphorylationPALPSESSSLAQPEQ
CCCCCCCCCCCCCCC		25.8923140645
184PhosphorylationALPSESSSLAQPEQG
CCCCCCCCCCCCCCC		36.6823140645
194PhosphorylationQPEQGPNTDLLGTSP
CCCCCCCCCCCCCCC		31.0223140645
199PhosphorylationPNTDLLGTSPQASLE
CCCCCCCCCCCHHHH		36.8823140645
199 (in isoform 2)Phosphorylation-36.88-
200PhosphorylationNTDLLGTSPQASLEL
CCCCCCCCCCHHHHH		17.1424453211
200 (in isoform 2)Phosphorylation-17.14-
204PhosphorylationLGTSPQASLELKSSI
CCCCCCHHHHHHHHH		19.68-
204 (in isoform 2)Phosphorylation-19.68-
207 (in isoform 2)Phosphorylation-8.71-
209PhosphorylationQASLELKSSIIGKKK
CHHHHHHHHHHCCCC		39.1229176673
210PhosphorylationASLELKSSIIGKKKP
HHHHHHHHHHCCCCH		19.3529176673
216 (in isoform 2)Phosphorylation-43.29-
223 (in isoform 2)Phosphorylation-28.7429514104
224 (in isoform 2)Phosphorylation-9.1728464351
236PhosphorylationGLGAQKVSNQSFTEI
CCCCCCCCCCCHHHH		35.8725521595
239PhosphorylationAQKVSNQSFTEIERQ
CCCCCCCCHHHHHHH		38.0827087446
241PhosphorylationKVSNQSFTEIERQAQ
CCCCCCHHHHHHHHH		41.1025521595
252SuccinylationRQAQVAEKLREQQAA
HHHHHHHHHHHHHHH		43.0123954790
253 (in isoform 2)Phosphorylation-5.6924719451
277PhosphorylationVASMRLAYQELQIDR
HHHHHHHHHHHHCCH		13.7029514104
290MalonylationDRKKEEKKLQNLEGK
CHHHHHHHHHHCCCH		59.5926320211
311PhosphorylationRLGMGLVSRSSISHS
HHCCCCCCHHHCCHH		31.3322324799
313PhosphorylationGMGLVSRSSISHSVL
CCCCCCHHHCCHHHH		25.2326239621
314PhosphorylationMGLVSRSSISHSVLS
CCCCCHHHCCHHHHH		27.3126239621
316PhosphorylationLVSRSSISHSVLSEM
CCCHHHCCHHHHHHH		16.2025177544
318PhosphorylationSRSSISHSVLSEMQM
CHHHCCHHHHHHHHH		20.2626239621
321PhosphorylationSISHSVLSEMQMIEQ
HCCHHHHHHHHHHHH		28.9428833060
330 (in isoform 2)Phosphorylation-29.2624719451
330PhosphorylationMQMIEQETPLSAKSS
HHHHHHCCCCCCCCC		29.2623984901
333PhosphorylationIEQETPLSAKSSRSQ
HHHCCCCCCCCCHHH		34.5528833060
336PhosphorylationETPLSAKSSRSQLDL
CCCCCCCCCHHHCCC		30.6027087446
337PhosphorylationTPLSAKSSRSQLDLF
CCCCCCCCHHHCCCC		34.9326239621
339PhosphorylationLSAKSSRSQLDLFDD
CCCCCCHHHCCCCCC		36.7225521595
349PhosphorylationDLFDDVGTFASGPPK
CCCCCCCCCCCCCCC		18.8423984901
356UbiquitinationTFASGPPKYKDNPFS
CCCCCCCCCCCCCCC		68.9822790023
356 (in isoform 2)Ubiquitination-68.9822790023
357PhosphorylationFASGPPKYKDNPFSL
CCCCCCCCCCCCCCC		29.3720139300
358 (in isoform 2)Ubiquitination-58.0922790023
358UbiquitinationASGPPKYKDNPFSLG
CCCCCCCCCCCCCCC		58.0922790023
363PhosphorylationKYKDNPFSLGETFGS
CCCCCCCCCCCCCCC		36.4020139300
367PhosphorylationNPFSLGETFGSRWDS
CCCCCCCCCCCCCCC		31.3429472430
370PhosphorylationSLGETFGSRWDSDAA
CCCCCCCCCCCCCCC		26.4620139300
370 (in isoform 2)Ubiquitination-26.46-
372 (in isoform 2)Ubiquitination-15.91-
393PhosphorylationKEPEVTISSIRPISE
CCCCEEEEEECCCCH		15.4525367039
394PhosphorylationEPEVTISSIRPISER
CCCEEEEEECCCCHH		20.8325367039
410PhosphorylationASRREVETRSSGLES
CCCHHHHHHHCCCCC		40.8127841257
412PhosphorylationRREVETRSSGLESSE
CHHHHHHHCCCCCHH		35.8629899451
413PhosphorylationREVETRSSGLESSEA
HHHHHHHCCCCCHHH		44.0727841257
427 (in isoform 2)Phosphorylation-8.4824719451
428 (in isoform 2)Ubiquitination-45.3922790023
428UbiquitinationRQKFAGAKAISSDMF
HHHHCCCCHHCCCCC		45.3922790023
431PhosphorylationFAGAKAISSDMFFGR
HCCCCHHCCCCCCCC		25.7425521595
432PhosphorylationAGAKAISSDMFFGRE
CCCCHHCCCCCCCCC		27.2924925903
442 (in isoform 2)Ubiquitination-47.45-
442PhosphorylationFFGREVDSEYEARSR
CCCCCCCCHHHHHHH		47.4529899451
444PhosphorylationGREVDSEYEARSRLQ
CCCCCCHHHHHHHHH		20.8815592455
445 (in isoform 2)Phosphorylation-33.2924719451
448PhosphorylationDSEYEARSRLQQLSG
CCHHHHHHHHHHHHC		44.3723984901
454PhosphorylationRSRLQQLSGSSAISS
HHHHHHHHCCCCCCH		32.0823984901
456PhosphorylationRLQQLSGSSAISSSD
HHHHHHCCCCCCHHH		17.1423984901
457PhosphorylationLQQLSGSSAISSSDL
HHHHHCCCCCCHHHH		32.9023984901
460PhosphorylationLSGSSAISSSDLFGN
HHCCCCCCHHHHCCC		24.4123984901
461PhosphorylationSGSSAISSSDLFGNM
HCCCCCCHHHHCCCC		23.0423984901
462PhosphorylationGSSAISSSDLFGNMD
CCCCCCHHHHCCCCC		31.3823984901
476PhosphorylationDGAHGGGTVSLGNVL
CCCCCCCCEECCCCC		15.3623984901
478PhosphorylationAHGGGTVSLGNVLPT
CCCCCCEECCCCCCC		30.3223984901
485PhosphorylationSLGNVLPTADIAQFK
ECCCCCCCCCHHHHH		32.5723984901
497PhosphorylationQFKQGVKSVAGKMAV
HHHHHHHHHHHHHHH		18.1322817900
512PhosphorylationLANGVMNSLQDRYGS
HHHHHHHHHHHHHCC		14.87-
519PhosphorylationSLQDRYGSY------
HHHHHHCCC------		20.8026745281
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 ARFG2_MOUSE !!
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of ARFG2_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 ARFG2_MOUSE !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions

Oops, there are no PPI records of ARFG2_MOUSE !!
Drug and Disease Associations
Kegg Drug
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of ARFG2_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-145, AND MASSSPECTROMETRY.
"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-336, AND MASSSPECTROMETRY.

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