dbPTM

G6PI_HUMAN - PTM Information in dbPTM

Basic Information of Protein

Overview of Protein Modification Sites with Functional and Structural Information
UniProt ID	G6PI_HUMAN
UniProt AC	P06744
Protein Name	Glucose-6-phosphate isomerase
Gene Name	GPI
Organism	Homo sapiens (Human).
Sequence Length	558
Subcellular Localization	Cytoplasm . Secreted .
Protein Description	Besides it's role as a glycolytic enzyme, mammalian GPI can function as a tumor-secreted cytokine and an angiogenic factor (AMF) that stimulates endothelial cell motility. GPI is also a neurotrophic factor (Neuroleukin) for spinal and sensory neurons..
Protein Sequence	MAALTRDPQFQKLQQWYREHRSELNLRRLFDANKDRFNHFSLTLNTNHGHILVDYSKNLVTEDVMRMLVDLAKSRGVEAARERMFNGEKINYTEGRAVLHVALRNRSNTPILVDGKDVMPEVNKVLDKMKSFCQRVRSGDWKGYTGKTITDVINIGIGGSDLGPLMVTEALKPYSSGGPRVWYVSNIDGTHIAKTLAQLNPESSLFIIASKTFTTQETITNAETAKEWFLQAAKDPSAVAKHFVALSTNTTKVKEFGIDPQNMFEFWDWVGGRYSLWSAIGLSIALHVGFDNFEQLLSGAHWMDQHFRTTPLEKNAPVLLALLGIWYINCFGCETHAMLPYDQYLHRFAAYFQQGDMESNGKYITKSGTRVDHQTGPIVWGEPGTNGQHAFYQLIHQGTKMIPCDFLIPVQTQHPIRKGLHHKILLANFLAQTEALMRGKSTEEARKELQAAGKSPEDLERLLPHKVFEGNRPTNSIVFTKLTPFMLGALVAMYEHKIFVQGIIWDINSFDQWGVELGKQLAKKIEPELDGSAQVTSHDASTNGLINFIKQQREARVQ

Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations	Modification	Substrate Peptides & Secondary Structure	ASA (%)	Reference
2	Acetylation	------MAALTRDPQ ------CCCCCCCHH	15.92	19413330
6	Phosphorylation	--MAALTRDPQFQKL --CCCCCCCHHHHHH	55.23	-
6 (in isoform 2)	Phosphorylation	-	55.23	-
12	2-Hydroxyisobutyrylation	TRDPQFQKLQQWYRE CCCHHHHHHHHHHHH	49.94	-
12	Acetylation	TRDPQFQKLQQWYRE CCCHHHHHHHHHHHH	49.94	19608861
12	Methylation	TRDPQFQKLQQWYRE CCCHHHHHHHHHHHH	49.94	19608861
12	Ubiquitination	TRDPQFQKLQQWYRE CCCHHHHHHHHHHHH	49.94	21890473
12 (in isoform 2)	Phosphorylation	-	49.94	24114839
13 (in isoform 2)	Phosphorylation	-	2.96	24114839
17	Phosphorylation	FQKLQQWYREHRSEL HHHHHHHHHHHHHHH	11.20	28064214
22	Phosphorylation	QWYREHRSELNLRRL HHHHHHHHHHHHHHH	48.63	26657352
34	Acetylation	RRLFDANKDRFNHFS HHHHHCCCCCCCEEE	52.59	23749302
34	Other	RRLFDANKDRFNHFS HHHHHCCCCCCCEEE	52.59	29775581
34	Ubiquitination	RRLFDANKDRFNHFS HHHHHCCCCCCCEEE	52.59	-
37 (in isoform 2)	Phosphorylation	-	13.78	22210691
41	Phosphorylation	KDRFNHFSLTLNTNH CCCCCEEEEEEECCC	16.94	21601212
44 (in isoform 2)	Phosphorylation	-	10.11	30622161
51	Ubiquitination	LNTNHGHILVDYSKN EECCCCEEEEECCCC	4.80	21890473
51	Acetylation	LNTNHGHILVDYSKN EECCCCEEEEECCCC	4.80	19608861
51	Ubiquitination	LNTNHGHILVDYSKN EECCCCEEEEECCCC	4.80	19608861
51 (in isoform 2)	Ubiquitination	-	4.80	-
55	Phosphorylation	HGHILVDYSKNLVTE CCEEEEECCCCCCHH	17.67	-
56	Phosphorylation	GHILVDYSKNLVTED CEEEEECCCCCCHHH	15.59	27642862
61	Phosphorylation	DYSKNLVTEDVMRML ECCCCCCHHHHHHHH	29.63	21712546
65	Sulfoxidation	NLVTEDVMRMLVDLA CCCHHHHHHHHHHHH	3.01	21406390
66	Methylation	LVTEDVMRMLVDLAK CCHHHHHHHHHHHHH	18.35	-
67	Sulfoxidation	VTEDVMRMLVDLAKS CHHHHHHHHHHHHHH	2.00	21406390
73	2-Hydroxyisobutyrylation	RMLVDLAKSRGVEAA HHHHHHHHHCCHHHH	48.24	-
73	Acetylation	RMLVDLAKSRGVEAA HHHHHHHHHCCHHHH	48.24	23236377
73	Ubiquitination	RMLVDLAKSRGVEAA HHHHHHHHHCCHHHH	48.24	21906983
74	Phosphorylation	MLVDLAKSRGVEAAR HHHHHHHHCCHHHHH	28.76	20068231
89	2-Hydroxyisobutyrylation	ERMFNGEKINYTEGR HHHHCCCCCCCCCCC	37.34	-
89	Acetylation	ERMFNGEKINYTEGR HHHHCCCCCCCCCCC	37.34	23954790
89	Ubiquitination	ERMFNGEKINYTEGR HHHHCCCCCCCCCCC	37.34	890473
92	Phosphorylation	FNGEKINYTEGRAVL HCCCCCCCCCCCEEE	15.05	28152594
93	Phosphorylation	NGEKINYTEGRAVLH CCCCCCCCCCCEEEE	27.72	28152594
106	Methylation	LHVALRNRSNTPILV EEEECCCCCCCCEEE	25.50	-
107	Phosphorylation	HVALRNRSNTPILVD EEECCCCCCCCEEEC	48.91	30266825
109	Phosphorylation	ALRNRSNTPILVDGK ECCCCCCCCEEECCC	16.98	19664994
112	Ubiquitination	NRSNTPILVDGKDVM CCCCCCEEECCCHHH	2.79	21890473
112 (in isoform 2)	Ubiquitination	-	2.79	-
116	Acetylation	TPILVDGKDVMPEVN CCEEECCCHHHHHHH	42.56	23954790
116	Ubiquitination	TPILVDGKDVMPEVN CCEEECCCHHHHHHH	42.56	21906983
119	Sulfoxidation	LVDGKDVMPEVNKVL EECCCHHHHHHHHHH	3.16	30846556
124	2-Hydroxyisobutyrylation	DVMPEVNKVLDKMKS HHHHHHHHHHHHHHH	49.72	-
124	Acetylation	DVMPEVNKVLDKMKS HHHHHHHHHHHHHHH	49.72	23954790
124	Ubiquitination	DVMPEVNKVLDKMKS HHHHHHHHHHHHHHH	49.72	21890473
130	Acetylation	NKVLDKMKSFCQRVR HHHHHHHHHHHHHHH	46.23	26051181
130	Ubiquitination	NKVLDKMKSFCQRVR HHHHHHHHHHHHHHH	46.23	-
131	Phosphorylation	KVLDKMKSFCQRVRS HHHHHHHHHHHHHHC	27.96	24719451
138	Phosphorylation	SFCQRVRSGDWKGYT HHHHHHHCCCCCCCC	37.94	24719451
142	2-Hydroxyisobutyrylation	RVRSGDWKGYTGKTI HHHCCCCCCCCCCCH	46.94	-
142	Acetylation	RVRSGDWKGYTGKTI HHHCCCCCCCCCCCH	46.94	19608861
142	Succinylation	RVRSGDWKGYTGKTI HHHCCCCCCCCCCCH	46.94	23954790
142	Ubiquitination	RVRSGDWKGYTGKTI HHHCCCCCCCCCCCH	46.94	19608861
146	Phosphorylation	GDWKGYTGKTITDVI CCCCCCCCCCHHCEE	19.34	27251275
147	Ubiquitination	DWKGYTGKTITDVIN CCCCCCCCCHHCEEE	29.02	-
148	Phosphorylation	WKGYTGKTITDVINI CCCCCCCCHHCEEEE	30.38	24719451
160	Phosphorylation	INIGIGGSDLGPLMV EEECCCCCCCHHHHH	25.17	24719451
163	Ubiquitination	GIGGSDLGPLMVTEA CCCCCCCHHHHHEEC	20.49	21890473
163 (in isoform 2)	Ubiquitination	-	20.49	-
168	Phosphorylation	DLGPLMVTEALKPYS CCHHHHHEECCCCCC	11.11	24719451
172	Ubiquitination	LMVTEALKPYSSGGP HHHEECCCCCCCCCC	49.29	-
174	Phosphorylation	VTEALKPYSSGGPRV HEECCCCCCCCCCCE	17.55	28857561
175	Phosphorylation	TEALKPYSSGGPRVW EECCCCCCCCCCCEE	30.91	28857561
176	Phosphorylation	EALKPYSSGGPRVWY ECCCCCCCCCCCEEE	41.76	28857561
183	Phosphorylation	SGGPRVWYVSNIDGT CCCCCEEEEEECCHH	7.37	28152594
185	Phosphorylation	GPRVWYVSNIDGTHI CCCEEEEEECCHHHH	16.63	28152594
194	Ubiquitination	IDGTHIAKTLAQLNP CCHHHHHHHHHHHCC	43.39	21906983
195	Phosphorylation	DGTHIAKTLAQLNPE CHHHHHHHHHHHCCC	20.50	21712546
203	Phosphorylation	LAQLNPESSLFIIAS HHHHCCCCCEEEEEE	33.33	21712546
204	Phosphorylation	AQLNPESSLFIIASK HHHCCCCCEEEEEEC	26.15	21712546
210	Phosphorylation	SSLFIIASKTFTTQE CCEEEEEECEEECCH	23.09	21712546
211	Acetylation	SLFIIASKTFTTQET CEEEEEECEEECCHH	38.34	132917
211	Ubiquitination	SLFIIASKTFTTQET CEEEEEECEEECCHH	38.34	-
212	Phosphorylation	LFIIASKTFTTQETI EEEEEECEEECCHHC	24.58	28857561
214	Phosphorylation	IIASKTFTTQETITN EEEECEEECCHHCCC	32.57	26657352
215	Phosphorylation	IASKTFTTQETITNA EEECEEECCHHCCCH	21.88	26657352
218	Phosphorylation	KTFTTQETITNAETA CEEECCHHCCCHHHH	24.23	26657352
220	Phosphorylation	FTTQETITNAETAKE EECCHHCCCHHHHHH	35.48	22673903
221	Phosphorylation	TTQETITNAETAKEW ECCHHCCCHHHHHHH	31.74	27251275
224	Phosphorylation	ETITNAETAKEWFLQ HHCCCHHHHHHHHHH	40.39	22673903
226	Acetylation	ITNAETAKEWFLQAA CCCHHHHHHHHHHHC	64.00	26822725
226	Phosphorylation	ITNAETAKEWFLQAA CCCHHHHHHHHHHHC	64.00	27251275
226	Ubiquitination	ITNAETAKEWFLQAA CCCHHHHHHHHHHHC	64.00	21890473
234	2-Hydroxyisobutyrylation	EWFLQAAKDPSAVAK HHHHHHCCCHHHHHH	73.51	-
234	Acetylation	EWFLQAAKDPSAVAK HHHHHHCCCHHHHHH	73.51	23954790
234	Succinylation	EWFLQAAKDPSAVAK HHHHHHCCCHHHHHH	73.51	23954790
234	Ubiquitination	EWFLQAAKDPSAVAK HHHHHHCCCHHHHHH	73.51	-
237	Ubiquitination	LQAAKDPSAVAKHFV HHHCCCHHHHHHHEE	45.57	21890473
237	Phosphorylation	LQAAKDPSAVAKHFV HHHCCCHHHHHHHEE	45.57	28450419
237 (in isoform 2)	Ubiquitination	-	45.57	-
241	2-Hydroxyisobutyrylation	KDPSAVAKHFVALST CCHHHHHHHEEEEEC	30.86	-
241	Acetylation	KDPSAVAKHFVALST CCHHHHHHHEEEEEC	30.86	27178108
241	Ubiquitination	KDPSAVAKHFVALST CCHHHHHHHEEEEEC	30.86	21906983
245	Ubiquitination	AVAKHFVALSTNTTK HHHHHEEEEECCCCC	8.54	21890473
245 (in isoform 2)	Ubiquitination	-	8.54	-
247	Phosphorylation	AKHFVALSTNTTKVK HHHEEEEECCCCCHH	15.18	20860994
248	Phosphorylation	KHFVALSTNTTKVKE HHEEEEECCCCCHHH	37.12	19764811
250	Phosphorylation	FVALSTNTTKVKEFG EEEEECCCCCHHHCC	28.25	25159151
251	Phosphorylation	VALSTNTTKVKEFGI EEEECCCCCHHHCCC	35.59	25159151
252	Ubiquitination	ALSTNTTKVKEFGID EEECCCCCHHHCCCC	49.63	21890473
252	2-Hydroxyisobutyrylation	ALSTNTTKVKEFGID EEECCCCCHHHCCCC	49.63	-
252	Acetylation	ALSTNTTKVKEFGID EEECCCCCHHHCCCC	49.63	25953088
252	Malonylation	ALSTNTTKVKEFGID EEECCCCCHHHCCCC	49.63	26320211
252	Ubiquitination	ALSTNTTKVKEFGID EEECCCCCHHHCCCC	49.63	-
252 (in isoform 2)	Ubiquitination	-	49.63	-
261	Phosphorylation	KEFGIDPQNMFEFWD HHCCCCHHHHHHHHH	50.72	27251275
309	Phosphorylation	WMDQHFRTTPLEKNA HHCHHCCCCCHHHCH	31.64	26437602
359	Phosphorylation	FQQGDMESNGKYITK HHHCCCCCCCEEEEC	44.22	21712546
362	Acetylation	GDMESNGKYITKSGT CCCCCCCEEEECCCC	37.42	26051181
362	Ubiquitination	GDMESNGKYITKSGT CCCCCCCEEEECCCC	37.42	21906983
365	Phosphorylation	ESNGKYITKSGTRVD CCCCEEEECCCCEEC	18.96	24719451
366	2-Hydroxyisobutyrylation	SNGKYITKSGTRVDH CCCEEEECCCCEECC	37.01	-
366	Acetylation	SNGKYITKSGTRVDH CCCEEEECCCCEECC	37.01	25953088
366	Ubiquitination	SNGKYITKSGTRVDH CCCEEEECCCCEECC	37.01	21906983
367	Phosphorylation	NGKYITKSGTRVDHQ CCEEEECCCCEECCC	36.43	26437602
400	Acetylation	QLIHQGTKMIPCDFL HHHHCCCCEECCCEE	41.47	26051181
401	Sulfoxidation	LIHQGTKMIPCDFLI HHHCCCCEECCCEEE	4.08	30846556
404	S-nitrosylation	QGTKMIPCDFLIPVQ CCCCEECCCEEEECC	3.90	22178444
412	Phosphorylation	DFLIPVQTQHPIRKG CEEEECCCCCCCCCC	29.13	-
423	Ubiquitination	IRKGLHHKILLANFL CCCCHHHHHHHHHHH	25.05	-
437	Sulfoxidation	LAQTEALMRGKSTEE HHHHHHHHCCCCHHH	7.37	30846556
438	Methylation	AQTEALMRGKSTEEA HHHHHHHCCCCHHHH	50.68	-
440	Ubiquitination	TEALMRGKSTEEARK HHHHHCCCCHHHHHH	43.79	-
441	Phosphorylation	EALMRGKSTEEARKE HHHHCCCCHHHHHHH	43.82	26437602
442	Phosphorylation	ALMRGKSTEEARKEL HHHCCCCHHHHHHHH	41.13	26437602
447	2-Hydroxyisobutyrylation	KSTEEARKELQAAGK CCHHHHHHHHHHCCC	70.58	-
447	Ubiquitination	KSTEEARKELQAAGK CCHHHHHHHHHHCCC	70.58	-
454	N6-malonyllysine	KELQAAGKSPEDLER HHHHHCCCCHHHHHH	59.10	-
454	Acetylation	KELQAAGKSPEDLER HHHHHCCCCHHHHHH	59.10	23954790
454	Malonylation	KELQAAGKSPEDLER HHHHHCCCCHHHHHH	59.10	21908771
454	Succinylation	KELQAAGKSPEDLER HHHHHCCCCHHHHHH	59.10	-
454	Ubiquitination	KELQAAGKSPEDLER HHHHHCCCCHHHHHH	59.10	-
455	Phosphorylation	ELQAAGKSPEDLERL HHHHCCCCHHHHHHH	32.38	29255136
466	Acetylation	LERLLPHKVFEGNRP HHHHCCCCHHCCCCC	46.83	25953088
466	Phosphorylation	LERLLPHKVFEGNRP HHHHCCCCHHCCCCC	46.83	27251275
466	Sumoylation	LERLLPHKVFEGNRP HHHHCCCCHHCCCCC	46.83	-
466	Ubiquitination	LERLLPHKVFEGNRP HHHHCCCCHHCCCCC	46.83	21906983
476	Phosphorylation	EGNRPTNSIVFTKLT CCCCCCCCEEEEECC	23.70	28857561
477	Ubiquitination	GNRPTNSIVFTKLTP CCCCCCCEEEEECCH	2.99	21890473
477 (in isoform 2)	Ubiquitination	-	2.99	-
524	Acetylation	LGKQLAKKIEPELDG HHHHHHHHCCCCCCC	46.85	26051181
524	Ubiquitination	LGKQLAKKIEPELDG HHHHHHHHCCCCCCC	46.85	-
532	Phosphorylation	IEPELDGSAQVTSHD CCCCCCCCCEEECCC	18.39	28857561
536	Phosphorylation	LDGSAQVTSHDASTN CCCCCEEECCCCCCC	14.31	22673903
537	Phosphorylation	DGSAQVTSHDASTNG CCCCEEECCCCCCCH	22.10	22673903
543	Phosphorylation	TSHDASTNGLINFIK ECCCCCCCHHHHHHH	40.55	27251275
550	Acetylation	NGLINFIKQQREARV CHHHHHHHHHHHHHC	35.92	26051181

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
185	S	Phosphorylation	Kinase	CSNK2A1	P68400	GPS
185	S	Phosphorylation	Kinase	CK2-FAMILY	-	GPS
185	S	Phosphorylation	Kinase	CK2	-	Uniprot
185	S	Phosphorylation	Kinase	CK2_GROUP	-	PhosphoELM

Functions of PTM Sites

Modified Location	Modified Residue	Modification	Function	Reference
185	S	Phosphorylation		11004567
Phosphorylation at Ser-185 by CK2 has been shown to decrease enzymatic activity and may contribute to secretion by a non-classical secretory pathway.

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 G6PI_HUMAN !!

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference
PAR14_HUMAN	PARP14	physical	17875708
TPIS_HUMAN	TPI1	physical	22939629
PDC6I_HUMAN	PDCD6IP	physical	22939629
AMFR_HUMAN	AMFR	physical	24810856
AL4A1_HUMAN	ALDH4A1	physical	26344197
ANXA7_HUMAN	ANXA7	physical	26344197
DCXR_HUMAN	DCXR	physical	26344197
FUMH_HUMAN	FH	physical	26344197
PEF1_HUMAN	PEF1	physical	26344197
TPIS_HUMAN	TPI1	physical	26344197
TRAP1_HUMAN	TRAP1	physical	27173435
PLST_HUMAN	PLS3	physical	27173435
IF2P_HUMAN	EIF5B	physical	27173435
HPRT_HUMAN	HPRT1	physical	27173435
PDIA3_HUMAN	PDIA3	physical	27173435

Drug and Disease Associations

Kegg Disease
There are no disease associations of PTM sites.
OMIM Disease
613470	Hemolytic anemia, non-spherocytic, due to glucose phosphate isomerase deficiency (HA-GPID)
Kegg Drug
There are no disease associations of PTM sites.
DrugBank
There are no disease associations of PTM sites.

Regulatory Network of G6PI_HUMAN

Related Literatures of Post-Translational Modification

Acetylation
Reference	PubMed
"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: ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, AND MASS SPECTROMETRY.	19413330 [Abstract]
"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-12 AND LYS-142, AND MASSSPECTROMETRY.	19608861 [Abstract]
Malonylation
Reference	PubMed
"The first identification of lysine malonylation substrates and itsregulatory enzyme."; Peng C., Lu Z., Xie Z., Cheng Z., Chen Y., Tan M., Luo H., Zhang Y.,He W., Yang K., Zwaans B.M., Tishkoff D., Ho L., Lombard D., He T.C.,Dai J., Verdin E., Ye Y., Zhao Y.; Mol. Cell. Proteomics 10:M111.012658.01-M111.012658.12(2011). Cited for: MALONYLATION AT LYS-454.	21908771 [Abstract]
N6-malonyllysine
Reference	PubMed
"The first identification of lysine malonylation substrates and itsregulatory enzyme."; Peng C., Lu Z., Xie Z., Cheng Z., Chen Y., Tan M., Luo H., Zhang Y.,He W., Yang K., Zwaans B.M., Tishkoff D., Ho L., Lombard D., He T.C.,Dai J., Verdin E., Ye Y., Zhao Y.; Mol. Cell. Proteomics 10:M111.012658.01-M111.012658.12(2011). Cited for: MALONYLATION AT LYS-454.	21908771 [Abstract]
Phosphorylation
Reference	PubMed
"Differential regulation of phosphoglucose isomerase/autocrinemotility factor activities by protein kinase CK2 phosphorylation."; Yanagawa T., Funasaka T., Tsutsumi S., Raz T., Tanaka N., Raz A.; J. Biol. Chem. 280:10419-10426(2005). Cited for: PHOSPHORYLATION AT SER-185, AND MUTAGENESIS OF SER-185.	15637053 [Abstract]
"Phosphohexose isomerase/autocrine motilityfactor/neuroleukin/maturation factor is a multifunctionalphosphoprotein."; Haga A., Niinaka Y., Raz A.; Biochim. Biophys. Acta 1480:235-244(2000). Cited for: FUNCTION, AND PHOSPHORYLATION AT SER-185.	11004567 [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-109, AND MASSSPECTROMETRY.	19690332 [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 THR-109, AND MASSSPECTROMETRY.	18669648 [Abstract]

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