dbPTM

GFPT1_HUMAN - PTM Information in dbPTM

Basic Information of Protein

Overview of Protein Modification Sites with Functional and Structural Information
UniProt ID	GFPT1_HUMAN
UniProt AC	Q06210
Protein Name	Glutamine--fructose-6-phosphate aminotransferase [isomerizing] 1
Gene Name	GFPT1
Organism	Homo sapiens (Human).
Sequence Length	699
Subcellular Localization
Protein Description	Controls the flux of glucose into the hexosamine pathway. Most likely involved in regulating the availability of precursors for N- and O-linked glycosylation of proteins. Regulates the circadian expression of clock genes ARNTL/BMAL1 and CRY1..
Protein Sequence	MCGIFAYLNYHVPRTRREILETLIKGLQRLEYRGYDSAGVGFDGGNDKDWEANACKIQLIKKKGKVKALDEEVHKQQDMDLDIEFDVHLGIAHTRWATHGEPSPVNSHPQRSDKNNEFIVIHNGIITNYKDLKKFLESKGYDFESETDTETIAKLVKYMYDNRESQDTSFTTLVERVIQQLEGAFALVFKSVHFPGQAVGTRRGSPLLIGVRSEHKLSTDHIPILYRTARTQIGSKFTRWGSQGERGKDKKGSCNLSRVDSTTCLFPVEEKAVEYYFASDASAVIEHTNRVIFLEDDDVAAVVDGRLSIHRIKRTAGDHPGRAVQTLQMELQQIMKGNFSSFMQKEIFEQPESVVNTMRGRVNFDDYTVNLGGLKDHIKEIQRCRRLILIACGTSYHAGVATRQVLEELTELPVMVELASDFLDRNTPVFRDDVCFFLSQSGETADTLMGLRYCKERGALTVGITNTVGSSISRETDCGVHINAGPEIGVASTKAYTSQFVSLVMFALMMCDDRISMQERRKEIMLGLKRLPDLIKEVLSMDDEIQKLATELYHQKSVLIMGRGYHYATCLEGALKIKEITYMHSEGILAGELKHGPLALVDKLMPVIMIIMRDHTYAKCQNALQQVVARQGRPVVICDKEDTETIKNTKRTIKVPHSVDCLQGILSVIPLQLLAFHLAVLRGYDVDFPRNLAKSVTVE

Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations	Modification	Substrate Peptides & Secondary Structure	ASA (%)	Reference
2	S-palmitoylation	------MCGIFAYLN ------CCCHHHHHC	6.02	19801377
25	Acetylation	EILETLIKGLQRLEY HHHHHHHHHHHHHHH	57.59	25953088
25	Ubiquitination	EILETLIKGLQRLEY HHHHHHHHHHHHHHH	57.59	23000965
25 (in isoform 1)	Ubiquitination	-	57.59	21890473
25 (in isoform 2)	Ubiquitination	-	57.59	21890473
48	Neddylation	GFDGGNDKDWEANAC CCCCCCCHHHHHHHH	69.60	32015554
48	Ubiquitination	GFDGGNDKDWEANAC CCCCCCCHHHHHHHH	69.60	23000965
48 (in isoform 1)	Ubiquitination	-	69.60	21890473
48 (in isoform 2)	Ubiquitination	-	69.60	21890473
50	Ubiquitination	DGGNDKDWEANACKI CCCCCHHHHHHHHHE	16.61	21890473
56	Ubiquitination	DWEANACKIQLIKKK HHHHHHHHEEEHHHC	30.95	32015554
67	Acetylation	IKKKGKVKALDEEVH HHHCCCEEECCHHHH	46.87	27452117
73	Ubiquitination	VKALDEEVHKQQDMD EEECCHHHHHHHCCC	6.86	21890473
75	Ubiquitination	ALDEEVHKQQDMDLD ECCHHHHHHHCCCCC	55.63	33845483
98	Phosphorylation	IAHTRWATHGEPSPV EEECCCCCCCCCCCC	24.37	23186163
103	Phosphorylation	WATHGEPSPVNSHPQ CCCCCCCCCCCCCCC	36.86	25159151
107	Phosphorylation	GEPSPVNSHPQRSDK CCCCCCCCCCCCCCC	36.46	23186163
133	Ubiquitination	ITNYKDLKKFLESKG ECCHHHHHHHHHHCC	52.17	23503661
134	Ubiquitination	TNYKDLKKFLESKGY CCHHHHHHHHHHCCC	63.58	22817900
139	Ubiquitination	LKKFLESKGYDFESE HHHHHHHCCCCCCCC	52.71	21906983
139 (in isoform 1)	Ubiquitination	-	52.71	21890473
139 (in isoform 2)	Ubiquitination	-	52.71	21890473
141	Phosphorylation	KFLESKGYDFESETD HHHHHCCCCCCCCCC	22.61	20068231
145	Phosphorylation	SKGYDFESETDTETI HCCCCCCCCCCHHHH	45.87	20068231
147	Phosphorylation	GYDFESETDTETIAK CCCCCCCCCHHHHHH	58.46	20068231
149	Phosphorylation	DFESETDTETIAKLV CCCCCCCHHHHHHHH	42.31	20068231
151	Phosphorylation	ESETDTETIAKLVKY CCCCCHHHHHHHHHH	28.47	20068231
154	Ubiquitination	TDTETIAKLVKYMYD CCHHHHHHHHHHHHH	50.38	29967540
157	Ubiquitination	ETIAKLVKYMYDNRE HHHHHHHHHHHHCCC	34.43	-
158	Ubiquitination	TIAKLVKYMYDNRES HHHHHHHHHHHCCCC	8.07	23503661
159	Ubiquitination	IAKLVKYMYDNRESQ HHHHHHHHHHCCCCC	2.54	22817900
164	Ubiquitination	KYMYDNRESQDTSFT HHHHHCCCCCCCCHH	60.03	22817900
190	Ubiquitination	GAFALVFKSVHFPGQ HHHEEEEEECCCCCC	44.05	-
191	Phosphorylation	AFALVFKSVHFPGQA HHEEEEEECCCCCCC	14.90	23312004
201	Phosphorylation	FPGQAVGTRRGSPLL CCCCCCCCCCCCCEE	15.59	28857561
205	Phosphorylation	AVGTRRGSPLLIGVR CCCCCCCCCEEEEEE	15.57	30266825
213	Phosphorylation	PLLIGVRSEHKLSTD CEEEEEECCCCCCCC	41.46	28348404
216	Ubiquitination	IGVRSEHKLSTDHIP EEEECCCCCCCCCCC	39.83	33845483
218	Phosphorylation	VRSEHKLSTDHIPIL EECCCCCCCCCCCCH	36.27	23312004
219	Phosphorylation	RSEHKLSTDHIPILY ECCCCCCCCCCCCHH	41.87	28555341
235	Phosphorylation	TARTQIGSKFTRWGS HHCHHCCCCHHCCCC	26.65	9836513
235 (in isoform 2)	Phosphorylation	-	26.65	10806197
239 (in isoform 2)	Phosphorylation	-	38.60	25849741
242	Phosphorylation	SKFTRWGSQGERGKD CCHHCCCCCCCCCCC	28.22	26437602
243	Phosphorylation	KFTRWGSQGERGKDK CHHCCCCCCCCCCCC	54.55	32142685
243 (in isoform 2)	Phosphorylation	-	54.55	25849741
245	Phosphorylation	TRWGSQGERGKDKKG HCCCCCCCCCCCCCC	51.10	32142685
251	Ubiquitination	GERGKDKKGSCNLSR CCCCCCCCCCCCCCC	67.21	29967540
253	Phosphorylation	RGKDKKGSCNLSRVD CCCCCCCCCCCCCCC	14.54	23927012
257	Phosphorylation	KKGSCNLSRVDSTTC CCCCCCCCCCCCCCE	19.10	23401153
261	Phosphorylation	CNLSRVDSTTCLFPV CCCCCCCCCCEEEEE	23.82	20201521
262	Phosphorylation	NLSRVDSTTCLFPVE CCCCCCCCCEEEEEC	19.64	29255136
263	Phosphorylation	LSRVDSTTCLFPVEE CCCCCCCCEEEEECH	15.91	22167270
275	Phosphorylation	VEEKAVEYYFASDAS ECHHHHHEEECCCHH	9.40	26074081
276	Phosphorylation	EEKAVEYYFASDASA CHHHHHEEECCCHHH	4.52	26074081
315	Phosphorylation	SIHRIKRTAGDHPGR EEEEEECCCCCCCCH	29.95	24114839
327	Ubiquitination	PGRAVQTLQMELQQI CCHHHHHHHHHHHHH	2.26	22817900
327 (in isoform 2)	Ubiquitination	-	2.26	21890473
329	Sulfoxidation	RAVQTLQMELQQIMK HHHHHHHHHHHHHHC	6.62	30846556
335	Sulfoxidation	QMELQQIMKGNFSSF HHHHHHHHCCCHHHH	3.85	30846556
343	Sulfoxidation	KGNFSSFMQKEIFEQ CCCHHHHHHHHHHHC	6.34	30846556
345	Ubiquitination	NFSSFMQKEIFEQPE CHHHHHHHHHHHCCH	40.78	22817900
345 (in isoform 1)	Ubiquitination	-	40.78	21890473
352	Ubiquitination	KEIFEQPESVVNTMR HHHHHCCHHHHHHCC	56.72	22817900
357	Ubiquitination	QPESVVNTMRGRVNF CCHHHHHHCCCCCCC	9.17	22817900
357 (in isoform 2)	Ubiquitination	-	9.17	21890473
358	Sulfoxidation	PESVVNTMRGRVNFD CHHHHHHCCCCCCCC	3.45	21406390
361	Ubiquitination	VVNTMRGRVNFDDYT HHHHCCCCCCCCHHE	15.16	22817900
367	Phosphorylation	GRVNFDDYTVNLGGL CCCCCCHHEEECCCH	17.90	-
368	Phosphorylation	RVNFDDYTVNLGGLK CCCCCHHEEECCCHH	15.20	-
370	Ubiquitination	NFDDYTVNLGGLKDH CCCHHEEECCCHHHH	25.76	22817900
375	2-Hydroxyisobutyrylation	TVNLGGLKDHIKEIQ EEECCCHHHHHHHHH	51.00	-
375	Ubiquitination	TVNLGGLKDHIKEIQ EEECCCHHHHHHHHH	51.00	22817900
375 (in isoform 1)	Ubiquitination	-	51.00	21890473
379	2-Hydroxyisobutyrylation	GGLKDHIKEIQRCRR CCHHHHHHHHHHHHH	45.40	-
379	Acetylation	GGLKDHIKEIQRCRR CCHHHHHHHHHHHHH	45.40	27452117
379	Ubiquitination	GGLKDHIKEIQRCRR CCHHHHHHHHHHHHH	45.40	22817900
382	Ubiquitination	KDHIKEIQRCRRLIL HHHHHHHHHHHHHHH	39.24	22817900
386	Ubiquitination	KEIQRCRRLILIACG HHHHHHHHHHHHHHC	29.70	22817900
394	Phosphorylation	LILIACGTSYHAGVA HHHHHHCCCHHHCHH	26.46	20068231
395	Phosphorylation	ILIACGTSYHAGVAT HHHHHCCCHHHCHHH	10.54	20068231
396	Phosphorylation	LIACGTSYHAGVATR HHHHCCCHHHCHHHH	8.77	20068231
400	Ubiquitination	GTSYHAGVATRQVLE CCCHHHCHHHHHHHH	5.22	22817900
402	Phosphorylation	SYHAGVATRQVLEEL CHHHCHHHHHHHHHH	21.16	20068231
404	Ubiquitination	HAGVATRQVLEELTE HHCHHHHHHHHHHHC	39.53	22817900
410	Phosphorylation	RQVLEELTELPVMVE HHHHHHHHCCCHHHH	38.46	20639409
420	Phosphorylation	PVMVELASDFLDRNT CHHHHHHHHHHCCCC	41.33	20639409
467	Phosphorylation	LTVGITNTVGSSISR EEEEEECCCCCCCCC	20.00	19664995
470	Phosphorylation	GITNTVGSSISRETD EEECCCCCCCCCCCC	21.84	-
473	Phosphorylation	NTVGSSISRETDCGV CCCCCCCCCCCCCEE	26.47	-
511	Ubiquitination	VMFALMMCDDRISMQ HHHHHHHCCCCCCHH	2.83	24816145
518	Ubiquitination	CDDRISMQERRKEIM CCCCCCHHHHHHHHH	33.96	29967540
529	2-Hydroxyisobutyrylation	KEIMLGLKRLPDLIK HHHHHHHHCHHHHHH	50.52	-
529	Succinylation	KEIMLGLKRLPDLIK HHHHHHHHCHHHHHH	50.52	23954790
529	Ubiquitination	KEIMLGLKRLPDLIK HHHHHHHHCHHHHHH	50.52	32015554
536	Ubiquitination	KRLPDLIKEVLSMDD HCHHHHHHHHCCCCH	49.41	24816145
541	Sulfoxidation	LIKEVLSMDDEIQKL HHHHHCCCCHHHHHH	7.05	21406390
547	Acetylation	SMDDEIQKLATELYH CCCHHHHHHHHHHHH	45.83	23954790
547	Ubiquitination	SMDDEIQKLATELYH CCCHHHHHHHHHHHH	45.83	32015554
553	Phosphorylation	QKLATELYHQKSVLI HHHHHHHHHCCEEEE	8.93	28152594
554	Ubiquitination	KLATELYHQKSVLIM HHHHHHHHCCEEEEE	41.01	24816145
556	Acetylation	ATELYHQKSVLIMGR HHHHHHCCEEEEECC	29.26	25953088
557	Phosphorylation	TELYHQKSVLIMGRG HHHHHCCEEEEECCC	18.65	-
578	2-Hydroxyisobutyrylation	LEGALKIKEITYMHS HHHCHHEEEEEEECC	41.29	-
619	2-Hydroxyisobutyrylation	MRDHTYAKCQNALQQ HCCCHHHHHHHHHHH	26.41	-
622	Ubiquitination	HTYAKCQNALQQVVA CHHHHHHHHHHHHHH	52.68	24816145
629	Ubiquitination	NALQQVVARQGRPVV HHHHHHHHHCCCCEE	10.14	24816145
640	2-Hydroxyisobutyrylation	RPVVICDKEDTETIK CCEEEECCCCCHHHH	53.75	-
640	Acetylation	RPVVICDKEDTETIK CCEEEECCCCCHHHH	53.75	25953088
640	Ubiquitination	RPVVICDKEDTETIK CCEEEECCCCCHHHH	53.75	24816145
647	Ubiquitination	KEDTETIKNTKRTIK CCCCHHHHCCCCEEC	67.02	24816145
650	Acetylation	TETIKNTKRTIKVPH CHHHHCCCCEECCCC	57.87	7674023
654	Ubiquitination	KNTKRTIKVPHSVDC HCCCCEECCCCCHHH	49.45	24816145
665	Ubiquitination	SVDCLQGILSVIPLQ CHHHHHHHHHHHHHH	1.35	24816145
672	Ubiquitination	ILSVIPLQLLAFHLA HHHHHHHHHHHHHHH	29.13	24816145
676	Ubiquitination	IPLQLLAFHLAVLRG HHHHHHHHHHHHHCC	4.97	24816145
676 (in isoform 2)	Ubiquitination	-	4.97	21890473
694	Acetylation	DFPRNLAKSVTVE-- CCCCCHHCCCCCC--	48.93	-
694	Ubiquitination	DFPRNLAKSVTVE-- CCCCCHHCCCCCC--	48.93	24816145
694 (in isoform 1)	Ubiquitination	-	48.93	21890473
695	Phosphorylation	FPRNLAKSVTVE--- CCCCHHCCCCCC---	19.88	23911959
697	Phosphorylation	RNLAKSVTVE----- CCHHCCCCCC-----	26.47	27134283
701	Ubiquitination	KSVTVE--------- CCCCCC---------		24816145
719	Ubiquitination	--------------------------- ---------------------------		24816145

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
205	S	Phosphorylation	Kinase	PRKACA	P17612	GPS
205	S	Phosphorylation	Kinase	PRKACA	P17612	GPS
205	S	Phosphorylation	Kinase	PKA-FAMILY	-	GPS
205	S	Phosphorylation	Kinase	PKA_GROUP	-	PhosphoELM
235	S	Phosphorylation	Kinase	PRKACA	P17612	GPS
235	S	Phosphorylation	Kinase	PRKACA	P17612	GPS
235	S	Phosphorylation	Kinase	PKA-FAMILY	-	GPS
235	S	Phosphorylation	Kinase	PKA_GROUP	-	PhosphoELM
243	S	Phosphorylation	Kinase	PRKAA1	Q13131	GPS
261	S	Phosphorylation	Kinase	PRKAA1	Q13131	GPS
261	S	Phosphorylation	Kinase	CAMK2A	Q9UQM7	PSP
261	S	Phosphorylation	Kinase	CAMK2-FAMILY	-	GPS
261	S	Phosphorylation	Kinase	PKA-FAMILY	-	GPS

Functions of PTM Sites

Modified Location	Modified Residue	Modification	Function	Reference
Oops, there are no descriptions of PTM sites of GFPT1_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 GFPT1_HUMAN !!

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference
MK08_HUMAN	MAPK8	physical	21988832
SYCC_HUMAN	CARS	physical	22863883
IMA7_HUMAN	KPNA6	physical	22863883
NCBP1_HUMAN	NCBP1	physical	22863883
ANM3_HUMAN	PRMT3	physical	22863883
SF01_HUMAN	SF1	physical	22863883
XPO7_HUMAN	XPO7	physical	22863883
ASNS_HUMAN	ASNS	physical	26344197
CRK_HUMAN	CRK	physical	26344197
GARS_HUMAN	GARS	physical	26344197
SETD3_HUMAN	SETD3	physical	26344197

Drug and Disease Associations

Kegg Disease
There are no disease associations of PTM sites.
OMIM Disease
610542	Myasthenic syndrome, congenital, 12 (CMS12)
Kegg Drug
There are no disease associations of PTM sites.
DrugBank
There are no disease associations of PTM sites.

Regulatory Network of GFPT1_HUMAN

Related Literatures of Post-Translational Modification

Phosphorylation
Reference	PubMed
"Large-scale proteomics analysis of the human kinome."; Oppermann F.S., Gnad F., Olsen J.V., Hornberger R., Greff Z., Keri G.,Mann M., Daub H.; Mol. Cell. Proteomics 8:1751-1764(2009). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-261, AND MASSSPECTROMETRY.	19369195 [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 SER-261, AND MASSSPECTROMETRY.	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-261, AND MASSSPECTROMETRY.	19413330 [Abstract]
"Large-scale phosphoproteome analysis of human liver tissue byenrichment and fractionation of phosphopeptides with strong anionexchange chromatography."; Han G., Ye M., Zhou H., Jiang X., Feng S., Jiang X., Tian R., Wan D.,Zou H., Gu J.; Proteomics 8:1346-1361(2008). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-261, AND MASSSPECTROMETRY.	18318008 [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-261, AND MASSSPECTROMETRY.	18669648 [Abstract]
"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 SER-261, AND MASSSPECTROMETRY.	16964243 [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-261, AND MASSSPECTROMETRY.	17081983 [Abstract]