G6PI_RAT - PTM Information in dbPTM

Basic Information of Protein

• UniProt ID: G6PI_RAT
• UniProt AC: Q6P6V0
• Protein Name: Glucose-6-phosphate isomerase {ECO:0000250|UniProtKB:P06745}
• Gene Name: Gpi {ECO:0000312|RGD:2727}
• Organism: Rattus norvegicus (Rat).
• Sequence Length: 558
• Subcellular Localization: Secreted. Cytoplasm .
• 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 (By similarity)..
• Protein Sequence: MAALTRNPEFQKLLEWHRANSANLKLRELFEADPERFNHFSLNLNTNHGHILLDYSKNLVNKEVLHMLVDLAKSRGVEAARDNMFSGLKINSTEDRAVLHVALRNRSNRSIMMDGKDVMPEVNKVLDKMKSFCQRVRSGDWKGYTGKAITDIINIGIGGSDLGPLMVTEALKPYSKGGPRVWFVSNIDGTHIAKTLANLNPESSLFIIASKTFTTQETITNAETAKEWFLQAAKDPSAVAKHFVALSTNTDKVKEFGIDPKNMFEFWDWVGGRYSLWSAIGLSIALHVGFDHFEQLLSGAHWMDQHFMKTPLDKNAPVLLALLGIWYINFYGCETHAMLPYDQYMHRFAAYFQQGDMESNGKYITKSGARVDYQTGPIVWGEPGTNGQHAFYQLIHQGTKMIPCDFLIPVQTQHPIRNGLHHKILLANFLAQTEALMKGKSPEEARKELQAAGKSPEELEKLLPHKVFEGNRPTNSIVFTKLTPFILGALIAMYEHKIFVQGIIWDINSFDQWGVELGKQLAKKIEPELDGSSAVTSHDSSTNGLIGFIKLQRDTKID

Overview of Protein Modification Sites with Functional and Structural Information

Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations	Modification	Substrate Peptides & Secondary Structure	ASA (%)	Reference
2	Acetylation	------MAALTRNPE ------CCCCCCCHH	15.92	-
12	Acetylation	TRNPEFQKLLEWHRA CCCHHHHHHHHHHHH	61.43	22902405
25	Acetylation	RANSANLKLRELFEA HHCCCCCHHHHHHHH	45.35	22902405
62	Acetylation	YSKNLVNKEVLHMLV CCCHHCCHHHHHHHH	41.54	22902405
62	Ubiquitination	YSKNLVNKEVLHMLV CCCHHCCHHHHHHHH	41.54	-
73	Acetylation	HMLVDLAKSRGVEAA HHHHHHHHHCCHHHH	48.24	22902405
86	Phosphorylation	AARDNMFSGLKINST HHHHCCCCCCEECCC	32.23	22673903
89	Acetylation	DNMFSGLKINSTEDR HCCCCCCEECCCCCH	43.28	22902405
107	Phosphorylation	HVALRNRSNRSIMMD HHHHHCCCCCCEEEC	39.89	-
116	Acetylation	RSIMMDGKDVMPEVN CCEEECCCCCHHHHH	42.77	22902405
124	Acetylation	DVMPEVNKVLDKMKS CCHHHHHHHHHHHHH	49.72	22902405
128	Acetylation	EVNKVLDKMKSFCQR HHHHHHHHHHHHHHH	44.03	22902405
142	Acetylation	RVRSGDWKGYTGKAI HHHCCCCCCCCCCHH	46.94	25786129
147	Acetylation	DWKGYTGKAITDIIN CCCCCCCCHHHCEEE	28.90	26302492
185	Phosphorylation	GPRVWFVSNIDGTHI CCCEEEEECCCCCHH	20.70	-
203	Phosphorylation	LANLNPESSLFIIAS HHHCCCCCCEEEEEE	33.33	22673903
204	Phosphorylation	ANLNPESSLFIIASK HHCCCCCCEEEEEEC	26.15	22673903
212	Phosphorylation	LFIIASKTFTTQETI EEEEEECEECCCHHC	24.58	29779826
214	Phosphorylation	IIASKTFTTQETITN EEEECEECCCHHCCC	32.57	22673903
215	Phosphorylation	IASKTFTTQETITNA EEECEECCCHHCCCH	21.88	28432305
218	Phosphorylation	KTFTTQETITNAETA CEECCCHHCCCHHHH	24.23	28432305
220	Phosphorylation	FTTQETITNAETAKE ECCCHHCCCHHHHHH	35.48	28432305
224	Phosphorylation	ETITNAETAKEWFLQ HHCCCHHHHHHHHHH	40.39	28432305
226	Ubiquitination	ITNAETAKEWFLQAA CCCHHHHHHHHHHHC	64.00	-
226	Acetylation	ITNAETAKEWFLQAA CCCHHHHHHHHHHHC	64.00	22902405
234	Ubiquitination	EWFLQAAKDPSAVAK HHHHHHCCCHHHHHH	73.51	-
234	Acetylation	EWFLQAAKDPSAVAK HHHHHHCCCHHHHHH	73.51	22902405
237	Phosphorylation	LQAAKDPSAVAKHFV HHHCCCHHHHHHHEE	45.57	29779826
241	Acetylation	KDPSAVAKHFVALST CCHHHHHHHEEEEEC	30.86	22902405
247	Phosphorylation	AKHFVALSTNTDKVK HHHEEEEECCCHHHH	15.18	22673903
248	Phosphorylation	KHFVALSTNTDKVKE HHEEEEECCCHHHHH	42.88	22673903
250	Phosphorylation	FVALSTNTDKVKEFG EEEEECCCHHHHHCC	36.97	22673903
252	Acetylation	ALSTNTDKVKEFGID EEECCCHHHHHCCCC	53.84	22902405
254	Acetylation	STNTDKVKEFGIDPK ECCCHHHHHCCCCHH	53.73	22902405
362	Acetylation	GDMESNGKYITKSGA CCCCCCCCEEECCCC	37.42	22902405
438	Acetylation	AQTEALMKGKSPEEA HHHHHHHCCCCHHHH	65.13	22902405
438	Ubiquitination	AQTEALMKGKSPEEA HHHHHHHCCCCHHHH	65.13	-
441	Phosphorylation	EALMKGKSPEEARKE HHHHCCCCHHHHHHH	46.33	25403869
447	Ubiquitination	KSPEEARKELQAAGK CCHHHHHHHHHHCCC	70.58	-
454	Succinylation	KELQAAGKSPEELEK HHHHHCCCCHHHHHH	59.10	-
454	Malonylation	KELQAAGKSPEELEK HHHHHCCCCHHHHHH	59.10	-
454	N6-malonyllysine	KELQAAGKSPEELEK HHHHHCCCCHHHHHH	59.10	-
454	Acetylation	KELQAAGKSPEELEK HHHHHCCCCHHHHHH	59.10	22902405
455	Phosphorylation	ELQAAGKSPEELEKL HHHHCCCCHHHHHHH	36.30	25403869
461	Acetylation	KSPEELEKLLPHKVF CCHHHHHHHCCCCCC	68.87	22902405
466	Acetylation	LEKLLPHKVFEGNRP HHHHCCCCCCCCCCC	46.83	22902405
466	Ubiquitination	LEKLLPHKVFEGNRP HHHHCCCCCCCCCCC	46.83	-
524	Acetylation	LGKQLAKKIEPELDG HHHHHHHHCCCCCCC	46.85	22902405
532	Phosphorylation	IEPELDGSSAVTSHD CCCCCCCCCCCCCCC	18.13	22673903
533	Phosphorylation	EPELDGSSAVTSHDS CCCCCCCCCCCCCCC	32.08	22673903
536	Phosphorylation	LDGSSAVTSHDSSTN CCCCCCCCCCCCCCC	21.76	22673903
537	Phosphorylation	DGSSAVTSHDSSTNG CCCCCCCCCCCCCCC	20.78	22673903
540	Phosphorylation	SAVTSHDSSTNGLIG CCCCCCCCCCCCEEE	33.37	25575281
541	Phosphorylation	AVTSHDSSTNGLIGF CCCCCCCCCCCEEEE	31.76	25575281
542	Phosphorylation	VTSHDSSTNGLIGFI CCCCCCCCCCEEEEE	36.94	25575281
550	Acetylation	NGLIGFIKLQRDTKI CCEEEEEEEECCCCC	35.98	22902405

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	CK2	-	Uniprot

Functions of PTM Sites

Modified Location	Modified Residue	Modification	Function	Reference
185	S	Phosphorylation	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.

Oops, there are no SNP-PTM records of G6PI_RAT !!

Protein-Protein Interaction

Oops, there are no PPI records of G6PI_RAT !!

Drug and Disease Associations

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