dbPTM

AGFG1_HUMAN - PTM Information in dbPTM

Basic Information of Protein

Overview of Protein Modification Sites with Functional and Structural Information
UniProt ID	AGFG1_HUMAN
UniProt AC	P52594
Protein Name	Arf-GAP domain and FG repeat-containing protein 1
Gene Name	AGFG1
Organism	Homo sapiens (Human).
Sequence Length	562
Subcellular Localization	Nucleus . Cytoplasmic vesicle .
Protein Description	Required for vesicle docking or fusion during acrosome biogenesis (By similarity). May play a role in RNA trafficking or localization. In case of infection by HIV-1, acts as a cofactor for viral Rev and promotes movement of Rev-responsive element-containing RNAs from the nuclear periphery to the cytoplasm. This step is essential for HIV-1 replication..
Protein Sequence	MAASAKRKQEEKHLKMLRDMTGLPHNRKCFDCDQRGPTYVNMTVGSFVCTSCSGSLRGLNPPHRVKSISMTTFTQQEIEFLQKHGNEVCKQIWLGLFDDRSSAIPDFRDPQKVKEFLQEKYEKKRWYVPPEQAKVVASVHASISGSSASSTSSTPEVKPLKSLLGDSAPTLHLNKGTPSQSPVVGRSQGQQQEKKQFDLLSDLGSDIFAAPAPQSTATANFANFAHFNSHAAQNSANADFANFDAFGQSSGSSNFGGFPTASHSPFQPQTTGGSAASVNANFAHFDNFPKSSSADFGTFNTSQSHQTASAVSKVSTNKAGLQTADKYAALANLDNIFSAGQGGDQGSGFGTTGKAPVGSVVSVPSQSSASSDKYAALAELDSVFSSAATSSNAYTSTSNASSNVFGTVPVVASAQTQPASSSVPAPFGATPSTNPFVAAAGPSVASSTNPFQTNARGATAATFGTASMSMPTGFGTPAPYSLPTSFSGSFQQPAFPAQAAFPQQTAFSQQPNGAGFAAFGQTKPVVTPFGQVAAAGVSSNPFMTGAPTGQFPTGSSSTNPFL

Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations	Modification	Substrate Peptides & Secondary Structure	ASA (%)	Reference
18	Dimethylation	EKHLKMLRDMTGLPH HHHHHHHHHHHCCCC	28.31	-
18	Methylation	EKHLKMLRDMTGLPH HHHHHHHHHHHCCCC	28.31	115372799
21	Phosphorylation	LKMLRDMTGLPHNRK HHHHHHHHCCCCCCC	39.60	28857561
38	Phosphorylation	DCDQRGPTYVNMTVG CCCCCCCCEEEEECC	42.81	22210691
39	Phosphorylation	CDQRGPTYVNMTVGS CCCCCCCEEEEECCE	7.92	22210691
67	Phosphorylation	NPPHRVKSISMTTFT CCCCCCCEEEEEECH	19.62	28857561
69	Phosphorylation	PHRVKSISMTTFTQQ CCCCCEEEEEECHHH	19.71	28857561
71	Phosphorylation	RVKSISMTTFTQQEI CCCEEEEEECHHHHH	16.39	28857561
72	Phosphorylation	VKSISMTTFTQQEIE CCEEEEEECHHHHHH	18.95	28857561
74	Phosphorylation	SISMTTFTQQEIEFL EEEEEECHHHHHHHH	27.53	28787133
83	Ubiquitination	QEIEFLQKHGNEVCK HHHHHHHHHCHHHHH	56.48	-
114	Ubiquitination	FRDPQKVKEFLQEKY CCCHHHHHHHHHHHH	50.19	-
120	Acetylation	VKEFLQEKYEKKRWY HHHHHHHHHHHHCCC	45.83	30591935
120	Ubiquitination	VKEFLQEKYEKKRWY HHHHHHHHHHHHCCC	45.83	-
123	Acetylation	FLQEKYEKKRWYVPP HHHHHHHHHCCCCCH	44.54	30591941
124	Acetylation	LQEKYEKKRWYVPPE HHHHHHHHCCCCCHH	35.90	30591947
138	O-linked_Glycosylation	EQAKVVASVHASISG HHCCEEEEEEEEECC	11.65	30059200
138	Phosphorylation	EQAKVVASVHASISG HHCCEEEEEEEEECC	11.65	27080861
142	O-linked_Glycosylation	VVASVHASISGSSAS EEEEEEEEECCCCCC	11.47	30059200
142	Phosphorylation	VVASVHASISGSSAS EEEEEEEEECCCCCC	11.47	25159151
144	O-linked_Glycosylation	ASVHASISGSSASST EEEEEEECCCCCCCC	30.08	30059200
144	Phosphorylation	ASVHASISGSSASST EEEEEEECCCCCCCC	30.08	25159151
146	Phosphorylation	VHASISGSSASSTSS EEEEECCCCCCCCCC	18.88	18669648
147	O-linked_Glycosylation	HASISGSSASSTSST EEEECCCCCCCCCCC	35.38	30059200
147	Phosphorylation	HASISGSSASSTSST EEEECCCCCCCCCCC	35.38	20068231
149	O-linked_Glycosylation	SISGSSASSTSSTPE EECCCCCCCCCCCCC	35.78	30059200
149	Phosphorylation	SISGSSASSTSSTPE EECCCCCCCCCCCCC	35.78	20068231
150	Phosphorylation	ISGSSASSTSSTPEV ECCCCCCCCCCCCCC	31.83	20068231
151	O-linked_Glycosylation	SGSSASSTSSTPEVK CCCCCCCCCCCCCCC	24.97	30059200
151	Phosphorylation	SGSSASSTSSTPEVK CCCCCCCCCCCCCCC	24.97	25159151
152	Phosphorylation	GSSASSTSSTPEVKP CCCCCCCCCCCCCCC	33.88	20068231
153	Phosphorylation	SSASSTSSTPEVKPL CCCCCCCCCCCCCCH	48.33	20068231
154	O-linked_Glycosylation	SASSTSSTPEVKPLK CCCCCCCCCCCCCHH	24.20	30059200
154	Phosphorylation	SASSTSSTPEVKPLK CCCCCCCCCCCCCHH	24.20	18669648
158	Acetylation	TSSTPEVKPLKSLLG CCCCCCCCCHHHHHC	42.86	26051181
161	Methylation	TPEVKPLKSLLGDSA CCCCCCHHHHHCCCC	47.81	115976713
162	O-linked_Glycosylation	PEVKPLKSLLGDSAP CCCCCHHHHHCCCCC	36.19	30059200
162	Phosphorylation	PEVKPLKSLLGDSAP CCCCCHHHHHCCCCC	36.19	30266825
167	Phosphorylation	LKSLLGDSAPTLHLN HHHHHCCCCCEEECC	34.06	25159151
170	O-linked_Glycosylation	LLGDSAPTLHLNKGT HHCCCCCEEECCCCC	26.90	OGP
170	Phosphorylation	LLGDSAPTLHLNKGT HHCCCCCEEECCCCC	26.90	23927012
175	Acetylation	APTLHLNKGTPSQSP CCEEECCCCCCCCCC	71.21	23236377
175	Ubiquitination	APTLHLNKGTPSQSP CCEEECCCCCCCCCC	71.21	-
177	Phosphorylation	TLHLNKGTPSQSPVV EEECCCCCCCCCCCC	22.75	29255136
179	Phosphorylation	HLNKGTPSQSPVVGR ECCCCCCCCCCCCCC	43.03	22167270
181	Phosphorylation	NKGTPSQSPVVGRSQ CCCCCCCCCCCCCCC	24.81	19664994
187	Phosphorylation	QSPVVGRSQGQQQEK CCCCCCCCCCCHHHH	32.50	26074081
194	Acetylation	SQGQQQEKKQFDLLS CCCCHHHHHHHHHHH	47.76	18584449
278 (in isoform 2)	Ubiquitination	-	7.22	21906983
291	O-linked_Glycosylation	HFDNFPKSSSADFGT CCCCCCCCCCCCCCC	29.75	30059200
291	Phosphorylation	HFDNFPKSSSADFGT CCCCCCCCCCCCCCC	29.75	23401153
292	O-linked_Glycosylation	FDNFPKSSSADFGTF CCCCCCCCCCCCCCC	35.35	30059200
292	Phosphorylation	FDNFPKSSSADFGTF CCCCCCCCCCCCCCC	35.35	30278072
293	O-linked_Glycosylation	DNFPKSSSADFGTFN CCCCCCCCCCCCCCC	38.66	30059200
293	Phosphorylation	DNFPKSSSADFGTFN CCCCCCCCCCCCCCC	38.66	30278072
298	O-linked_Glycosylation	SSSADFGTFNTSQSH CCCCCCCCCCCCCCC	17.44	30059200
298	Phosphorylation	SSSADFGTFNTSQSH CCCCCCCCCCCCCCC	17.44	23898821
301	O-linked_Glycosylation	ADFGTFNTSQSHQTA CCCCCCCCCCCCHHH	24.77	30059200
301	Phosphorylation	ADFGTFNTSQSHQTA CCCCCCCCCCCCHHH	24.77	23401153
302	O-linked_Glycosylation	DFGTFNTSQSHQTAS CCCCCCCCCCCHHHH	30.69	30059200
302	Phosphorylation	DFGTFNTSQSHQTAS CCCCCCCCCCCHHHH	30.69	25159151
304	O-linked_Glycosylation	GTFNTSQSHQTASAV CCCCCCCCCHHHHHH	19.82	30059200
304	Phosphorylation	GTFNTSQSHQTASAV CCCCCCCCCHHHHHH	19.82	21712546
307	Phosphorylation	NTSQSHQTASAVSKV CCCCCCHHHHHHHHH	19.70	29978859
309	Phosphorylation	SQSHQTASAVSKVST CCCCHHHHHHHHHHC	32.37	26074081
312	O-linked_Glycosylation	HQTASAVSKVSTNKA CHHHHHHHHHHCCHH	27.36	30059200
312	Phosphorylation	HQTASAVSKVSTNKA CHHHHHHHHHHCCHH	27.36	26074081
313	Acetylation	QTASAVSKVSTNKAG HHHHHHHHHHCCHHH	33.34	26051181
313	Ubiquitination	QTASAVSKVSTNKAG HHHHHHHHHHCCHHH	33.34	-
315	Phosphorylation	ASAVSKVSTNKAGLQ HHHHHHHHCCHHHCC	29.96	24719451
316	Phosphorylation	SAVSKVSTNKAGLQT HHHHHHHCCHHHCCH	43.66	27251275
318	Ubiquitination	VSKVSTNKAGLQTAD HHHHHCCHHHCCHHH	43.87	2190698
318 (in isoform 1)	Ubiquitination	-	43.87	21906983
318 (in isoform 3)	Ubiquitination	-	43.87	21906983
323	Phosphorylation	TNKAGLQTADKYAAL CCHHHCCHHHHHHHH	41.70	26356563
326	Acetylation	AGLQTADKYAALANL HHCCHHHHHHHHHCC	34.03	26051181
326	Phosphorylation	AGLQTADKYAALANL HHCCHHHHHHHHHCC	34.03	24719451
327	Phosphorylation	GLQTADKYAALANLD HCCHHHHHHHHHCCC	9.54	25159151
328	Phosphorylation	LQTADKYAALANLDN CCHHHHHHHHHCCCC	11.18	27251275
351	O-linked_Glycosylation	DQGSGFGTTGKAPVG CCCCCCCCCCCCCCC	30.07	30059200
351	Phosphorylation	DQGSGFGTTGKAPVG CCCCCCCCCCCCCCC	30.07	27642862
359	O-linked_Glycosylation	TGKAPVGSVVSVPSQ CCCCCCCCEEECCCC	21.41	30059200
359	Phosphorylation	TGKAPVGSVVSVPSQ CCCCCCCCEEECCCC	21.41	30206219
362	O-linked_Glycosylation	APVGSVVSVPSQSSA CCCCCEEECCCCCCC	26.59	30059200
362	Phosphorylation	APVGSVVSVPSQSSA CCCCCEEECCCCCCC	26.59	29255136
365	O-linked_Glycosylation	GSVVSVPSQSSASSD CCEEECCCCCCCCCC	40.31	30059200
365	Phosphorylation	GSVVSVPSQSSASSD CCEEECCCCCCCCCC	40.31	29255136
367	O-linked_Glycosylation	VVSVPSQSSASSDKY EEECCCCCCCCCCHH	32.01	30059200
367	Phosphorylation	VVSVPSQSSASSDKY EEECCCCCCCCCCHH	32.01	30108239
368	O-linked_Glycosylation	VSVPSQSSASSDKYA EECCCCCCCCCCHHH	25.24	30059200
368	Phosphorylation	VSVPSQSSASSDKYA EECCCCCCCCCCHHH	25.24	25159151
370	O-linked_Glycosylation	VPSQSSASSDKYAAL CCCCCCCCCCHHHHH	40.80	30059200
370	Phosphorylation	VPSQSSASSDKYAAL CCCCCCCCCCHHHHH	40.80	25159151
371	O-linked_Glycosylation	PSQSSASSDKYAALA CCCCCCCCCHHHHHH	37.53	30059200
371	Phosphorylation	PSQSSASSDKYAALA CCCCCCCCCHHHHHH	37.53	30206219
385	O-linked_Glycosylation	AELDSVFSSAATSSN HHHHHHHHHHCCCCC	19.53	30059200
386	Phosphorylation	ELDSVFSSAATSSNA HHHHHHHHHCCCCCC	15.51	24719451
389	O-linked_Glycosylation	SVFSSAATSSNAYTS HHHHHHCCCCCCCCC	32.19	30059200
389	Phosphorylation	SVFSSAATSSNAYTS HHHHHHCCCCCCCCC	32.19	27251275
391	O-linked_Glycosylation	FSSAATSSNAYTSTS HHHHCCCCCCCCCCC	22.56	30059200
392	Phosphorylation	SSAATSSNAYTSTSN HHHCCCCCCCCCCCC	36.41	27251275
395	O-linked_Glycosylation	ATSSNAYTSTSNASS CCCCCCCCCCCCCCC	24.10	30059200
396	O-linked_Glycosylation	TSSNAYTSTSNASSN CCCCCCCCCCCCCCC	19.70	30059200
398	O-linked_Glycosylation	SNAYTSTSNASSNVF CCCCCCCCCCCCCCC	30.11	30059200
401	O-linked_Glycosylation	YTSTSNASSNVFGTV CCCCCCCCCCCCCCC	27.05	30059200
402	O-linked_Glycosylation	TSTSNASSNVFGTVP CCCCCCCCCCCCCCE	34.30	30059200
407	O-linked_Glycosylation	ASSNVFGTVPVVASA CCCCCCCCCEEEEEC	15.35	30059200
421	O-linked_Glycosylation	AQTQPASSSVPAPFG CCCCCCCCCCCCCCC	37.14	30059200
446	O-linked_Glycosylation	AAGPSVASSTNPFQT CCCCCCCCCCCCCCC	35.22	30059200
448	O-linked_Glycosylation	GPSVASSTNPFQTNA CCCCCCCCCCCCCCC	44.40	30059200
456	Methylation	NPFQTNARGATAATF CCCCCCCCCCCEEEC	37.03	115385871
480	Phosphorylation	GFGTPAPYSLPTSFS CCCCCCCCCCCCCCC	25.58	-
481	O-linked_Glycosylation	FGTPAPYSLPTSFSG CCCCCCCCCCCCCCC	27.15	30059200
489	O-linked_Glycosylation	LPTSFSGSFQQPAFP CCCCCCCCCCCCCCC	20.77	30059200
544	Phosphorylation	VSSNPFMTGAPTGQF CCCCCCCCCCCCCCC	30.48	-
556	Phosphorylation	GQFPTGSSSTNPFL- CCCCCCCCCCCCCC-	42.39	-
557	Phosphorylation	QFPTGSSSTNPFL-- CCCCCCCCCCCCC--	33.62	-
558	Phosphorylation	FPTGSSSTNPFL--- CCCCCCCCCCCC---	49.19	-

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 AGFG1_HUMAN !!

Functions of PTM Sites

Modified Location	Modified Residue	Modification	Function	Reference
Oops, there are no descriptions of PTM sites of AGFG1_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 AGFG1_HUMAN !!

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference
EPS15_HUMAN	EPS15	physical	10613896
A4_HUMAN	APP	physical	21832049
SUCB1_HUMAN	SUCLA2	physical	22939629
GPN1_HUMAN	GPN1	physical	22863883
HPBP1_HUMAN	HSPBP1	physical	22863883
IPO11_HUMAN	IPO11	physical	22863883
OGT1_HUMAN	OGT	physical	22863883
PPME1_HUMAN	PPME1	physical	22863883
SHLB1_HUMAN	SH3GLB1	physical	22863883
SURF2_HUMAN	SURF2	physical	22863883
TPRKB_HUMAN	TPRKB	physical	22863883
ZPR1_HUMAN	ZPR1	physical	22863883
DPOE2_HUMAN	POLE2	physical	25416956
NYAP2_HUMAN	NYAP2	physical	25416956

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 AGFG1_HUMAN

Related Literatures of Post-Translational Modification

Phosphorylation
Reference	PubMed
"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-177 AND SER-181, ANDMASS SPECTROMETRY.	18669648 [Abstract]
"Phosphoproteome of resting human platelets."; Zahedi R.P., Lewandrowski U., Wiesner J., Wortelkamp S., Moebius J.,Schuetz C., Walter U., Gambaryan S., Sickmann A.; J. Proteome Res. 7:526-534(2008). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-177 AND SER-181, ANDMASS SPECTROMETRY.	18088087 [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 THR-177 AND SER-181, ANDMASS SPECTROMETRY.	17081983 [Abstract]
"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-177, AND MASSSPECTROMETRY.	19690332 [Abstract]