dbPTM

G6PI_YEAST - PTM Information in dbPTM

Basic Information of Protein

Overview of Protein Modification Sites with Functional and Structural Information
UniProt ID	G6PI_YEAST
UniProt AC	P12709
Protein Name	Glucose-6-phosphate isomerase
Gene Name	PGI1
Organism	Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast).
Sequence Length	554
Subcellular Localization	Cytoplasm.
Protein Description
Protein Sequence	MSNNSFTNFKLATELPAWSKLQKIYESQGKTLSVKQEFQKDAKRFEKLNKTFTNYDGSKILFDYSKNLVNDEIIAALIELAKEANVTGLRDAMFKGEHINSTEDRAVYHVALRNRANKPMYVDGVNVAPEVDSVLKHMKEFSEQVRSGEWKGYTGKKITDVVNIGIGGSDLGPVMVTEALKHYAGVLDVHFVSNIDGTHIAETLKVVDPETTLFLIASKTFTTAETITNANTAKNWFLSKTGNDPSHIAKHFAALSTNETEVAKFGIDTKNMFGFESWVGGRYSVWSAIGLSVALYIGYDNFEAFLKGAEAVDNHFTQTPLEDNIPLLGGLLSVWYNNFFGAQTHLVAPFDQYLHRFPAYLQQLSMESNGKSVTRGNVFTDYSTGSILFGEPATNAQHSFFQLVHQGTKLIPSDFILAAQSHNPIENKLHQKMLASNFFAQAEALMVGKDEEQVKAEGATGGLVPHKVFSGNRPTTSILAQKITPATLGALIAYYEHVTFTEGAIWNINSFDQWGVELGKVLAKVIGKELDNSSTISTHDASTNGLINQFKEWM

Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations	Modification	Substrate Peptides & Secondary Structure	ASA (%)	Reference
2	Acetylation	------MSNNSFTNF ------CCCCCCCCH	44.72	9298649
2	Phosphorylation	------MSNNSFTNF ------CCCCCCCCH	44.72	22369663
5	Phosphorylation	---MSNNSFTNFKLA ---CCCCCCCCHHHH	37.38	22369663
7	Phosphorylation	-MSNNSFTNFKLATE -CCCCCCCCHHHHCC	39.30	22369663
10	Acetylation	NNSFTNFKLATELPA CCCCCCHHHHCCCCH	39.00	24489116
10	Ubiquitination	NNSFTNFKLATELPA CCCCCCHHHHCCCCH	39.00	24961812
13	Phosphorylation	FTNFKLATELPAWSK CCCHHHHCCCCHHHH	48.79	28889911
19	Phosphorylation	ATELPAWSKLQKIYE HCCCCHHHHHHHHHH	26.12	22369663
20	Acetylation	TELPAWSKLQKIYES CCCCHHHHHHHHHHH	44.21	24489116
20	Ubiquitination	TELPAWSKLQKIYES CCCCHHHHHHHHHHH	44.21	22817900
23	2-Hydroxyisobutyrylation	PAWSKLQKIYESQGK CHHHHHHHHHHHCCC	58.66	-
23	Acetylation	PAWSKLQKIYESQGK CHHHHHHHHHHHCCC	58.66	24489116
23	Succinylation	PAWSKLQKIYESQGK CHHHHHHHHHHHCCC	58.66	23954790
23	Ubiquitination	PAWSKLQKIYESQGK CHHHHHHHHHHHCCC	58.66	23749301
27	Phosphorylation	KLQKIYESQGKTLSV HHHHHHHHCCCCCCH	27.54	28889911
30	2-Hydroxyisobutyrylation	KIYESQGKTLSVKQE HHHHHCCCCCCHHHH	38.36	-
30	Acetylation	KIYESQGKTLSVKQE HHHHHCCCCCCHHHH	38.36	24489116
30	Ubiquitination	KIYESQGKTLSVKQE HHHHHCCCCCCHHHH	38.36	23749301
31	Phosphorylation	IYESQGKTLSVKQEF HHHHCCCCCCHHHHH	30.96	22369663
33	Phosphorylation	ESQGKTLSVKQEFQK HHCCCCCCHHHHHHH	32.28	22369663
35	2-Hydroxyisobutyrylation	QGKTLSVKQEFQKDA CCCCCCHHHHHHHHH	40.51	-
35	Acetylation	QGKTLSVKQEFQKDA CCCCCCHHHHHHHHH	40.51	24489116
35	Succinylation	QGKTLSVKQEFQKDA CCCCCCHHHHHHHHH	40.51	23954790
35	Ubiquitination	QGKTLSVKQEFQKDA CCCCCCHHHHHHHHH	40.51	23749301
40	2-Hydroxyisobutyrylation	SVKQEFQKDAKRFEK CHHHHHHHHHHHHHH	66.04	-
40	Acetylation	SVKQEFQKDAKRFEK CHHHHHHHHHHHHHH	66.04	24489116
40	Succinylation	SVKQEFQKDAKRFEK CHHHHHHHHHHHHHH	66.04	23954790
40	Ubiquitination	SVKQEFQKDAKRFEK CHHHHHHHHHHHHHH	66.04	22817900
47	Acetylation	KDAKRFEKLNKTFTN HHHHHHHHHHCCCCC	55.43	25381059
47	Ubiquitination	KDAKRFEKLNKTFTN HHHHHHHHHHCCCCC	55.43	22817900
50	2-Hydroxyisobutyrylation	KRFEKLNKTFTNYDG HHHHHHHCCCCCCCC	56.29	-
50	Acetylation	KRFEKLNKTFTNYDG HHHHHHHCCCCCCCC	56.29	22865919
50	Succinylation	KRFEKLNKTFTNYDG HHHHHHHCCCCCCCC	56.29	23954790
50	Ubiquitination	KRFEKLNKTFTNYDG HHHHHHHCCCCCCCC	56.29	23749301
51	Phosphorylation	RFEKLNKTFTNYDGS HHHHHHCCCCCCCCC	34.32	22369663
53	Phosphorylation	EKLNKTFTNYDGSKI HHHHCCCCCCCCCEE	37.79	22369663
55	Phosphorylation	LNKTFTNYDGSKILF HHCCCCCCCCCEEEE	20.72	22369663
58	Phosphorylation	TFTNYDGSKILFDYS CCCCCCCCEEEEECC	17.39	22369663
59	Acetylation	FTNYDGSKILFDYSK CCCCCCCEEEEECCC	49.29	24489116
59	Ubiquitination	FTNYDGSKILFDYSK CCCCCCCEEEEECCC	49.29	23749301
87	Phosphorylation	LAKEANVTGLRDAMF HHHHCCCCCHHHHHH	30.24	11283598
95	2-Hydroxyisobutyrylation	GLRDAMFKGEHINST CHHHHHHCCCCCCCC	50.75	-
95	Acetylation	GLRDAMFKGEHINST CHHHHHHCCCCCCCC	50.75	24489116
95	Succinylation	GLRDAMFKGEHINST CHHHHHHCCCCCCCC	50.75	23954790
101	Phosphorylation	FKGEHINSTEDRAVY HCCCCCCCCHHHHHH	32.35	22369663
102	Phosphorylation	KGEHINSTEDRAVYH CCCCCCCCHHHHHHH	37.10	22369663
108	Phosphorylation	STEDRAVYHVALRNR CCHHHHHHHHHHHCC	6.92	21082442
118	Acetylation	ALRNRANKPMYVDGV HHHCCCCCCCEECCE	30.12	24489116
118	Ubiquitination	ALRNRANKPMYVDGV HHHCCCCCCCEECCE	30.12	17644757
121	Phosphorylation	NRANKPMYVDGVNVA CCCCCCCEECCEECC	12.15	24909858
136	Acetylation	PEVDSVLKHMKEFSE HHHHHHHHHHHHHHH	39.23	24489116
136	Ubiquitination	PEVDSVLKHMKEFSE HHHHHHHHHHHHHHH	39.23	17644757
139	2-Hydroxyisobutyrylation	DSVLKHMKEFSEQVR HHHHHHHHHHHHHHH	56.16	-
139	Acetylation	DSVLKHMKEFSEQVR HHHHHHHHHHHHHHH	56.16	24489116
147	Phosphorylation	EFSEQVRSGEWKGYT HHHHHHHCCCCCCCC	42.06	21440633
151	2-Hydroxyisobutyrylation	QVRSGEWKGYTGKKI HHHCCCCCCCCCCEE	37.42	-
151	Acetylation	QVRSGEWKGYTGKKI HHHCCCCCCCCCCEE	37.42	22865919
151	Succinylation	QVRSGEWKGYTGKKI HHHCCCCCCCCCCEE	37.42	23954790
169	Phosphorylation	VNIGIGGSDLGPVMV EEEECCCCCCCHHHH	25.17	21440633
193	Phosphorylation	VLDVHFVSNIDGTHI CEEEEEEECCCCCCH	27.42	17287358
198	Phosphorylation	FVSNIDGTHIAETLK EEECCCCCCHHEEEE	13.32	17287358
218	Phosphorylation	TTLFLIASKTFTTAE CEEEEEEECEECCCH	25.82	21440633
220	Phosphorylation	LFLIASKTFTTAETI EEEEEECEECCCHHH	24.58	22369663
222	Phosphorylation	LIASKTFTTAETITN EEEECEECCCHHHCC	30.26	22369663
223	Phosphorylation	IASKTFTTAETITNA EEECEECCCHHHCCC	20.50	25752575
226	Phosphorylation	KTFTTAETITNANTA CEECCCHHHCCCHHH	30.55	28889911
234	Acetylation	ITNANTAKNWFLSKT HCCCHHHHHCHHCCC	53.31	24489116
234	Succinylation	ITNANTAKNWFLSKT HCCCHHHHHCHHCCC	53.31	23954790
234	Ubiquitination	ITNANTAKNWFLSKT HCCCHHHHHCHHCCC	53.31	23749301
239	Phosphorylation	TAKNWFLSKTGNDPS HHHHCHHCCCCCCHH	20.78	21440633
240	2-Hydroxyisobutyrylation	AKNWFLSKTGNDPSH HHHCHHCCCCCCHHH	63.70	-
240	Acetylation	AKNWFLSKTGNDPSH HHHCHHCCCCCCHHH	63.70	24489116
241	Phosphorylation	KNWFLSKTGNDPSHI HHCHHCCCCCCHHHH	37.53	23749301
246	Phosphorylation	SKTGNDPSHIAKHFA CCCCCCHHHHHHHHH	30.32	23749301
250	2-Hydroxyisobutyrylation	NDPSHIAKHFAALST CCHHHHHHHHHHCCC	38.36	-
250	Acetylation	NDPSHIAKHFAALST CCHHHHHHHHHHCCC	38.36	24489116
250	Ubiquitination	NDPSHIAKHFAALST CCHHHHHHHHHHCCC	38.36	17644757
256	Phosphorylation	AKHFAALSTNETEVA HHHHHHCCCCCHHHH	25.18	21440633
264	2-Hydroxyisobutyrylation	TNETEVAKFGIDTKN CCCHHHHHCCCCCCC	49.66	-
264	Ubiquitination	TNETEVAKFGIDTKN CCCHHHHHCCCCCCC	49.66	17644757
270	Ubiquitination	AKFGIDTKNMFGFES HHCCCCCCCCCCCCC	42.54	15699485
368	Phosphorylation	LQQLSMESNGKSVTR HHHHCHHCCCCCCCC	42.09	23749301
371	Ubiquitination	LSMESNGKSVTRGNV HCHHCCCCCCCCCCC	46.10	23749301
372	Phosphorylation	SMESNGKSVTRGNVF CHHCCCCCCCCCCCE	30.07	23749301
374	Phosphorylation	ESNGKSVTRGNVFTD HCCCCCCCCCCCEEC	39.69	21440633
380	Phosphorylation	VTRGNVFTDYSTGSI CCCCCCEECCCCCEE	29.73	22369663
382	Phosphorylation	RGNVFTDYSTGSILF CCCCEECCCCCEEEE	12.69	22369663
383	Phosphorylation	GNVFTDYSTGSILFG CCCEECCCCCEEEEC	29.15	22369663
384	Phosphorylation	NVFTDYSTGSILFGE CCEECCCCCEEEECC	28.81	22369663
386	Phosphorylation	FTDYSTGSILFGEPA EECCCCCEEEECCCC	19.06	22369663
394	Phosphorylation	ILFGEPATNAQHSFF EEECCCCCCCCCCHH	41.63	22369663
399	Phosphorylation	PATNAQHSFFQLVHQ CCCCCCCCHHHHHHC	18.71	22369663
408	Phosphorylation	FQLVHQGTKLIPSDF HHHHHCCCCEECHHH	18.99	22369663
409	Ubiquitination	QLVHQGTKLIPSDFI HHHHCCCCEECHHHH	51.77	17644757
428	Acetylation	SHNPIENKLHQKMLA CCCHHHHHHHHHHHH	34.26	24489116
428	Ubiquitination	SHNPIENKLHQKMLA CCCHHHHHHHHHHHH	34.26	24961812
432	Ubiquitination	IENKLHQKMLASNFF HHHHHHHHHHHHCHH	25.74	24961812
455	Acetylation	GKDEEQVKAEGATGG CCCHHHHHHCCCCCC	40.18	24489116
460	Phosphorylation	QVKAEGATGGLVPHK HHHHCCCCCCCCCCC	42.51	22369663
467	Acetylation	TGGLVPHKVFSGNRP CCCCCCCCCCCCCCC	38.62	24489116
467	Ubiquitination	TGGLVPHKVFSGNRP CCCCCCCCCCCCCCC	38.62	23749301
470	Phosphorylation	LVPHKVFSGNRPTTS CCCCCCCCCCCCCCH	37.84	22369663
475	Phosphorylation	VFSGNRPTTSILAQK CCCCCCCCCHHHHHH	29.91	22369663
476	Phosphorylation	FSGNRPTTSILAQKI CCCCCCCCHHHHHHC	19.22	22369663
477	Phosphorylation	SGNRPTTSILAQKIT CCCCCCCHHHHHHCC	20.34	22369663
482	Ubiquitination	TTSILAQKITPATLG CCHHHHHHCCHHHHH	42.83	17644757
520	Ubiquitination	QWGVELGKVLAKVIG HHHHHHHHHHHHHHC	46.85	22817900
524	Acetylation	ELGKVLAKVIGKELD HHHHHHHHHHCCCCC	30.17	22865919
524	Ubiquitination	ELGKVLAKVIGKELD HHHHHHHHHHCCCCC	30.17	23749301
528	2-Hydroxyisobutyrylation	VLAKVIGKELDNSST HHHHHHCCCCCCCCC	43.94	-
528	Acetylation	VLAKVIGKELDNSST HHHHHHCCCCCCCCC	43.94	24489116
528	Succinylation	VLAKVIGKELDNSST HHHHHHCCCCCCCCC	43.94	23954790
528	Ubiquitination	VLAKVIGKELDNSST HHHHHHCCCCCCCCC	43.94	23749301
533	Phosphorylation	IGKELDNSSTISTHD HCCCCCCCCCEECCH	28.64	22369663
534	Phosphorylation	GKELDNSSTISTHDA CCCCCCCCCEECCHH	35.69	22369663
535	Phosphorylation	KELDNSSTISTHDAS CCCCCCCCEECCHHH	20.83	22369663
537	Phosphorylation	LDNSSTISTHDASTN CCCCCCEECCHHHHC	21.56	22369663
538	Phosphorylation	DNSSTISTHDASTNG CCCCCEECCHHHHCC	21.66	22369663
542	Phosphorylation	TISTHDASTNGLINQ CEECCHHHHCCHHHH	28.58	22369663
543	Phosphorylation	ISTHDASTNGLINQF EECCHHHHCCHHHHH	34.72	22369663

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
-	K	Ubiquitination	E3 ubiquitin ligase	RSP5	P39940	PMID:22199232

Functions of PTM Sites

Modified Location	Modified Residue	Modification	Function	Reference
Oops, there are no descriptions of PTM sites of G6PI_YEAST !!

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_YEAST !!

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference
DHE2_YEAST	GDH2	genetic	7901008
NHP6B_YEAST	NHP6B	genetic	20093466
TPS2_YEAST	TPS2	genetic	20093466
MUP1_YEAST	MUP1	genetic	20093466
PPT2_YEAST	PPT2	genetic	21623372
TPS2_YEAST	TPS2	genetic	21623372
ARO1_YEAST	ARO1	genetic	21623372
THRC_YEAST	THR4	genetic	21623372
ADH3_YEAST	ADH3	genetic	21623372
ATP5E_YEAST	ATP15	genetic	21623372
CYS3_YEAST	CYS3	genetic	21623372
HSP72_YEAST	SSA2	physical	22940862
RL7A_YEAST	RPL7A	physical	22940862
G6PI_YEAST	PGI1	physical	22940862
DED1_YEAST	DED1	physical	22940862
SSB1_YEAST	SSB1	physical	22940862
ABF2_YEAST	ABF2	physical	22940862
HSP7F_YEAST	SSE1	physical	22940862
HSP71_YEAST	SSA1	physical	22940862
RS3_YEAST	RPS3	physical	22940862
ARP3_YEAST	ARP3	genetic	27708008
DED1_YEAST	DED1	genetic	27708008
MAK16_YEAST	MAK16	genetic	27708008
RPB1_YEAST	RPO21	genetic	27708008
RRP1_YEAST	RRP1	genetic	27708008
MOB2_YEAST	MOB2	genetic	27708008
TAD3_YEAST	TAD3	genetic	27708008
UTP15_YEAST	UTP15	genetic	27708008
PRP24_YEAST	PRP24	genetic	27708008
NOG2_YEAST	NOG2	genetic	27708008
CET1_YEAST	CET1	genetic	27708008
ASA1_YEAST	ASA1	genetic	27708008
ORC4_YEAST	ORC4	genetic	27708008
BUD31_YEAST	BUD31	genetic	27708008
RL13A_YEAST	RPL13A	genetic	27708008
TPS2_YEAST	TPS2	genetic	27708008
VPS41_YEAST	VPS41	genetic	27708008
DHAS_YEAST	HOM2	genetic	27708008
SEM1_YEAST	SEM1	genetic	27708008
RV167_YEAST	RVS167	genetic	27708008
CEM1_YEAST	CEM1	genetic	27708008
CUL3_YEAST	CUL3	genetic	27708008
SKN1_YEAST	SKN1	genetic	27708008
OPI1_YEAST	OPI1	genetic	27708008
HTD2_YEAST	HTD2	genetic	27708008
ATG32_YEAST	ATG32	genetic	27708008
LPLA_YEAST	AIM22	genetic	27708008
YJE9_YEAST	YJL049W	genetic	27708008
NCA3_YEAST	NCA3	genetic	27708008
FABG_YEAST	OAR1	genetic	27708008
ELF1_YEAST	ELF1	genetic	27708008
MEH1_YEAST	MEH1	genetic	27708008
UBI4P_YEAST	UBI4	genetic	27708008
ENT2_YEAST	ENT2	genetic	27708008
LIPB_YEAST	LIP2	genetic	27708008
YPT7_YEAST	YPT7	genetic	27708008
ATG3_YEAST	ATG3	genetic	27708008
MSB4_YEAST	MSB4	genetic	27708008
MSN1_YEAST	MSN1	genetic	27708008
LIPA_YEAST	LIP5	genetic	27708008
PMT3_YEAST	PMT3	genetic	27708008
CHL1_YEAST	CHL1	genetic	27708008
SQSTM_HUMAN	SQSTM1	physical	27107014

Drug and Disease Associations

Kegg Drug
DrugBank
There are no disease associations of PTM sites.

Regulatory Network of G6PI_YEAST

Related Literatures of Post-Translational Modification

Acetylation
Reference	PubMed
"Proteome studies of Saccharomyces cerevisiae: identification andcharacterization of abundant proteins."; Garrels J.I., McLaughlin C.S., Warner J.R., Futcher B., Latter G.I.,Kobayashi R., Schwender B., Volpe T., Anderson D.S.,Mesquita-Fuentes R., Payne W.E.; Electrophoresis 18:1347-1360(1997). Cited for: ACETYLATION AT SER-2.	9298649 [Abstract]
Phosphorylation
Reference	PubMed
"A multidimensional chromatography technology for in-depthphosphoproteome analysis."; Albuquerque C.P., Smolka M.B., Payne S.H., Bafna V., Eng J., Zhou H.; Mol. Cell. Proteomics 7:1389-1396(2008). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-51; THR-53; THR-102;THR-223; SER-470; SER-534; SER-537 AND THR-538, AND MASS SPECTROMETRY.	18407956 [Abstract]
"Proteome-wide identification of in vivo targets of DNA damagecheckpoint kinases."; Smolka M.B., Albuquerque C.P., Chen S.H., Zhou H.; Proc. Natl. Acad. Sci. U.S.A. 104:10364-10369(2007). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-534 AND SER-537, ANDMASS SPECTROMETRY.	17563356 [Abstract]
"Analysis of phosphorylation sites on proteins from Saccharomycescerevisiae by electron transfer dissociation (ETD) massspectrometry."; Chi A., Huttenhower C., Geer L.Y., Coon J.J., Syka J.E.P., Bai D.L.,Shabanowitz J., Burke D.J., Troyanskaya O.G., Hunt D.F.; Proc. Natl. Acad. Sci. U.S.A. 104:2193-2198(2007). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-193 AND THR-198, ANDMASS SPECTROMETRY.	17287358 [Abstract]
"Quantitative phosphoproteomics applied to the yeast pheromonesignaling pathway."; Gruhler A., Olsen J.V., Mohammed S., Mortensen P., Faergeman N.J.,Mann M., Jensen O.N.; Mol. Cell. Proteomics 4:310-327(2005). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-33, AND MASSSPECTROMETRY.	15665377 [Abstract]