dbPTM

ARFG2_HUMAN - PTM Information in dbPTM

Basic Information of Protein

Overview of Protein Modification Sites with Functional and Structural Information
UniProt ID	ARFG2_HUMAN
UniProt AC	Q8N6H7
Protein Name	ADP-ribosylation factor GTPase-activating protein 2
Gene Name	ARFGAP2
Organism	Homo sapiens (Human).
Sequence Length	521
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). Implicated in coatomer-mediated protein transport between the Golgi complex and the endoplasmic reticulum. Hydrolysis of ARF1-bound GTP may lead to dissociation of coatomer from Golgi-derived membranes to allow fusion with target membranes..
Protein Sequence	MAAEPNKTEIQTLFKRLRAVPTNKACFDCGAKNPSWASITYGVFLCIDCSGVHRSLGVHLSFIRSTELDSNWNWFQLRCMQVGGNANATAFFRQHGCTANDANTKYNSRAAQMYREKIRQLGSAALARHGTDLWIDNMSSAVPNHSPEKKDSDFFTEHTQPPAWDAPATEPSGTQQPAPSTESSGLAQPEHGPNTDLLGTSPKASLELKSSIIGKKKPAAAKKGLGAKKGLGAQKVSSQSFSEIERQAQVAEKLREQQAADAKKQAEESMVASMRLAYQELQIDRKKEEKKLQNLEGKKREQAERLGMGLVSRSSVSHSVLSEMQVIEQETPVSAKSSRSQLDLFDDVGTFASGPPKYKDNPFSLGESFGSRWDTDAAWGMDRVEEKEPEVTISSIRPISERATNRREVESRSSGLESSEARQKFAGAKAISSDMFFGREVDAEYEARSRLQQLSGSSAISSSDLFGDMDGAHGAGSVSLGNVLPTADIAQFKQGVKSVAGKMAVLANGVMNSLQDRYGSY

Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations	Modification	Substrate Peptides & Secondary Structure	ASA (%)	Reference
2	Acetylation	------MAAEPNKTE ------CCCCCCHHH	22.11	22814378
7	Ubiquitination	-MAAEPNKTEIQTLF -CCCCCCHHHHHHHH	59.24	-
8	Phosphorylation	MAAEPNKTEIQTLFK CCCCCCHHHHHHHHH	44.98	20068231
15	Ubiquitination	TEIQTLFKRLRAVPT HHHHHHHHHHCCCCC	54.35	-
24	Malonylation	LRAVPTNKACFDCGA HCCCCCCCCHHHCCC	49.35	26320211
24	Ubiquitination	LRAVPTNKACFDCGA HCCCCCCCCHHHCCC	49.35	-
88 (in isoform 2)	Phosphorylation	-	9.63	28348404
93 (in isoform 2)	Phosphorylation	-	22.57	28348404
94 (in isoform 2)	Phosphorylation	-	31.97	28348404
102	Ubiquitination	HGCTANDANTKYNSR CCCCCHHHCHHHHHH	25.96	-
105	Ubiquitination	TANDANTKYNSRAAQ CCHHHCHHHHHHHHH	42.09	-
123	Phosphorylation	EKIRQLGSAALARHG HHHHHHHHHHHHHHC	20.97	-
131	Phosphorylation	AALARHGTDLWIDNM HHHHHHCCCEEEECC	23.07	23927012
139	Phosphorylation	DLWIDNMSSAVPNHS CEEEECCCCCCCCCC	22.77	22167270
140	Phosphorylation	LWIDNMSSAVPNHSP EEEECCCCCCCCCCC	23.63	22167270
146	Phosphorylation	SSAVPNHSPEKKDSD CCCCCCCCCCCCCCC	41.20	22167270
152	Phosphorylation	HSPEKKDSDFFTEHT CCCCCCCCCCCCCCC	45.24	26074081
156	Phosphorylation	KKDSDFFTEHTQPPA CCCCCCCCCCCCCCC	27.18	21406692
159	Phosphorylation	SDFFTEHTQPPAWDA CCCCCCCCCCCCCCC	36.22	21406692
169	Phosphorylation	PAWDAPATEPSGTQQ CCCCCCCCCCCCCCC	47.58	21406692
172	Phosphorylation	DAPATEPSGTQQPAP CCCCCCCCCCCCCCC	48.52	21406692
174	Phosphorylation	PATEPSGTQQPAPST CCCCCCCCCCCCCCC	28.50	21406692
180	Phosphorylation	GTQQPAPSTESSGLA CCCCCCCCCCCCCCC	47.08	18669648
181	Phosphorylation	TQQPAPSTESSGLAQ CCCCCCCCCCCCCCC	38.54	21406692
183	Phosphorylation	QPAPSTESSGLAQPE CCCCCCCCCCCCCCC	29.78	26074081
184	Phosphorylation	PAPSTESSGLAQPEH CCCCCCCCCCCCCCC	31.43	26074081
191	Acetylation	SGLAQPEHGPNTDLL CCCCCCCCCCCCCCC	64.79	-
195	Phosphorylation	QPEHGPNTDLLGTSP CCCCCCCCCCCCCCC	31.02	30576142
200	Phosphorylation	PNTDLLGTSPKASLE CCCCCCCCCCCHHHH	41.65	26074081
201	Phosphorylation	NTDLLGTSPKASLEL CCCCCCCCCCHHHHH	23.70	28348404
205	Phosphorylation	LGTSPKASLELKSSI CCCCCCHHHHHHHHH	28.62	23403867
209	Ubiquitination	PKASLELKSSIIGKK CCHHHHHHHHHCCCC	32.55	-
210	Phosphorylation	KASLELKSSIIGKKK CHHHHHHHHHCCCCC	39.12	23403867
211	Phosphorylation	ASLELKSSIIGKKKP HHHHHHHHHCCCCCH	19.35	23403867
215	Acetylation	LKSSIIGKKKPAAAK HHHHHCCCCCHHHHH	47.41	25953088
215	Ubiquitination	LKSSIIGKKKPAAAK HHHHHCCCCCHHHHH	47.41	-
222	Acetylation	KKKPAAAKKGLGAKK CCCHHHHHHCCCCCC	42.52	7975635
223	Acetylation	KKPAAAKKGLGAKKG CCHHHHHHCCCCCCC	55.42	7975645
228	Acetylation	AKKGLGAKKGLGAQK HHHCCCCCCCCCCCC	45.64	7975655
229	Ubiquitination	KKGLGAKKGLGAQKV HHCCCCCCCCCCCCC	59.85	-
235	Ubiquitination	KKGLGAQKVSSQSFS CCCCCCCCCCCCCHH	43.48	-
237	Phosphorylation	GLGAQKVSSQSFSEI CCCCCCCCCCCHHHH	29.69	23401153
238	Phosphorylation	LGAQKVSSQSFSEIE CCCCCCCCCCHHHHH	32.60	25072903
240	Phosphorylation	AQKVSSQSFSEIERQ CCCCCCCCHHHHHHH	32.46	29255136
242	Phosphorylation	KVSSQSFSEIERQAQ CCCCCCHHHHHHHHH	42.80	29255136
250	Ubiquitination	EIERQAQVAEKLREQ HHHHHHHHHHHHHHH	9.23	-
252	Ubiquitination	ERQAQVAEKLREQQA HHHHHHHHHHHHHHH	54.49	-
253	Acetylation	RQAQVAEKLREQQAA HHHHHHHHHHHHHHH	43.01	25953088
253	Ubiquitination	RQAQVAEKLREQQAA HHHHHHHHHHHHHHH	43.01	-
269	Phosphorylation	AKKQAEESMVASMRL HHHHHHHHHHHHHHH	15.29	28555341
270	Sulfoxidation	KKQAEESMVASMRLA HHHHHHHHHHHHHHH	3.10	21406390
273	Phosphorylation	AEESMVASMRLAYQE HHHHHHHHHHHHHHH	7.94	28857561
278	Phosphorylation	VASMRLAYQELQIDR HHHHHHHHHHHHCCH	13.70	21945579
290	Ubiquitination	IDRKKEEKKLQNLEG CCHHHHHHHHHHCCC	60.93	21890473
291	Ubiquitination	DRKKEEKKLQNLEGK CHHHHHHHHHHCCCH	59.59	-
298	Acetylation	KLQNLEGKKREQAER HHHHCCCHHHHHHHH	39.00	23749302
298	Ubiquitination	KLQNLEGKKREQAER HHHHCCCHHHHHHHH	39.00	-
308	Sulfoxidation	EQAERLGMGLVSRSS HHHHHHCCCCCCHHH	4.43	21406390
312	Phosphorylation	RLGMGLVSRSSVSHS HHCCCCCCHHHCCHH	31.33	23186163
314	Phosphorylation	GMGLVSRSSVSHSVL CCCCCCHHHCCHHHH	27.82	23401153
315	Phosphorylation	MGLVSRSSVSHSVLS CCCCCHHHCCHHHHH	26.91	21712546
317	Phosphorylation	LVSRSSVSHSVLSEM CCCHHHCCHHHHHHC	16.40	21712546
319	Phosphorylation	SRSSVSHSVLSEMQV CHHHCCHHHHHHCEE	19.76	21712546
322	Ubiquitination	SVSHSVLSEMQVIEQ HCCHHHHHHCEEEEE	28.94	21890473
322	Phosphorylation	SVSHSVLSEMQVIEQ HCCHHHHHHCEEEEE	28.94	21712546
331	Phosphorylation	MQVIEQETPVSAKSS CEEEEECCCCCCCCC	28.78	28450419
334	Phosphorylation	IEQETPVSAKSSRSQ EEECCCCCCCCCHHH	31.05	25159151
336	Acetylation	QETPVSAKSSRSQLD ECCCCCCCCCHHHHH	41.27	25953088
336	Ubiquitination	QETPVSAKSSRSQLD ECCCCCCCCCHHHHH	41.27	-
337	Phosphorylation	ETPVSAKSSRSQLDL CCCCCCCCCHHHHHC	30.60	23401153
338	Phosphorylation	TPVSAKSSRSQLDLF CCCCCCCCHHHHHCC	34.93	25159151
340	Phosphorylation	VSAKSSRSQLDLFDD CCCCCCHHHHHCCCC	36.72	25159151
350	Phosphorylation	DLFDDVGTFASGPPK HCCCCCCCCCCCCCC	18.84	23403867
353	Phosphorylation	DDVGTFASGPPKYKD CCCCCCCCCCCCCCC	47.87	23186163
357	Ubiquitination	TFASGPPKYKDNPFS CCCCCCCCCCCCCCC	68.98	-
358	Phosphorylation	FASGPPKYKDNPFSL CCCCCCCCCCCCCCC	29.37	24702127
359	Ubiquitination	ASGPPKYKDNPFSLG CCCCCCCCCCCCCCC	58.09	-
364	Phosphorylation	KYKDNPFSLGESFGS CCCCCCCCCCCCCCC	36.40	23927012
368	Phosphorylation	NPFSLGESFGSRWDT CCCCCCCCCCCCCCC	32.86	22167270
371	Phosphorylation	SLGESFGSRWDTDAA CCCCCCCCCCCCCCC	28.34	22167270
387	Ubiquitination	GMDRVEEKEPEVTIS CCCCCCCCCCCEEEE	66.13	-
392	Phosphorylation	EEKEPEVTISSIRPI CCCCCCEEEEECCCC	17.30	23312004
394	Phosphorylation	KEPEVTISSIRPISE CCCCEEEEECCCCCH	15.45	24719451
395	Phosphorylation	EPEVTISSIRPISER CCCEEEEECCCCCHH	20.83	25954137
400	Phosphorylation	ISSIRPISERATNRR EEECCCCCHHHCCHH	24.58	25159151
404	Phosphorylation	RPISERATNRREVES CCCCHHHCCHHHHHH	35.16	24719451
413	Phosphorylation	RREVESRSSGLESSE HHHHHHHHCCCCCHH	37.73	29507054
414	Phosphorylation	REVESRSSGLESSEA HHHHHHHCCCCCHHH	46.41	25159151
418	Phosphorylation	SRSSGLESSEARQKF HHHCCCCCHHHHHHH	38.22	25159151
419	Phosphorylation	RSSGLESSEARQKFA HHCCCCCHHHHHHHC	26.37	21815630
429	Acetylation	RQKFAGAKAISSDMF HHHHCCCCHHCCCCC	45.39	25953088
429	Ubiquitination	RQKFAGAKAISSDMF HHHHCCCCHHCCCCC	45.39	21890473
432	Phosphorylation	FAGAKAISSDMFFGR HCCCCHHCCCCCCCC	25.74	29255136
433	Phosphorylation	AGAKAISSDMFFGRE CCCCHHCCCCCCCCC	27.29	30266825
435	Sulfoxidation	AKAISSDMFFGREVD CCHHCCCCCCCCCCC	3.03	21406390
445	Phosphorylation	GREVDAEYEARSRLQ CCCCCHHHHHHHHHH	19.33	20007894
458	Phosphorylation	LQQLSGSSAISSSDL HHHHHCCCCCCHHHC	32.90	28348404
461	Phosphorylation	LSGSSAISSSDLFGD HHCCCCCCHHHCCCC	24.41	28348404
462	Phosphorylation	SGSSAISSSDLFGDM HCCCCCCHHHCCCCC	23.04	28348404
463	Phosphorylation	GSSAISSSDLFGDMD CCCCCCHHHCCCCCC	31.38	28348404
477	Phosphorylation	DGAHGAGSVSLGNVL CCCCCCCCCCCCCCC	14.17	28348404
479	Phosphorylation	AHGAGSVSLGNVLPT CCCCCCCCCCCCCCC	32.05	28348404
498	Phosphorylation	QFKQGVKSVAGKMAV HHHHHHHHHHHHHHH	18.13	22817900
513	Phosphorylation	LANGVMNSLQDRYGS HHHHHHHHHHHHHCC	14.87	14702039
520	Phosphorylation	SLQDRYGSY------ HHHHHHCCC------	20.80	22199227

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_HUMAN !!

Functions of PTM Sites

Modified Location	Modified Residue	Modification	Function	Reference
Oops, there are no descriptions of PTM sites of ARFG2_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 ARFG2_HUMAN !!

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference	Domain-Domain Interactions
MTND_HUMAN	ADI1	physical	26344197
ARFG1_HUMAN	ARFGAP1	physical	26344197

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 ARFG2_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-146; SER-368 ANDSER-432, 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-432, AND MASSSPECTROMETRY.	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-146; SER-368 ANDSER-432, AND MASS SPECTROMETRY.	18669648 [Abstract]
"Kinase-selective enrichment enables quantitative phosphoproteomics ofthe kinome across the cell cycle."; Daub H., Olsen J.V., Bairlein M., Gnad F., Oppermann F.S., Korner R.,Greff Z., Keri G., Stemmann O., Mann M.; Mol. Cell 31:438-448(2008). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-146 AND SER-368, ANDMASS SPECTROMETRY.	18691976 [Abstract]
"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-146 AND SER-498, ANDMASS SPECTROMETRY.	17081983 [Abstract]