PGM2L_HUMAN - PTM Information in dbPTM

Basic Information of Protein

• UniProt ID: PGM2L_HUMAN
• UniProt AC: Q6PCE3
• Protein Name: Glucose 1,6-bisphosphate synthase
• Gene Name: PGM2L1
• Organism: Homo sapiens (Human).
• Sequence Length: 622
• Protein Description: Glucose 1,6-bisphosphate synthase using 1,3-bisphosphoglycerate as a phosphate donor and a series of 1-phosphate sugars as acceptors, including glucose 1-phosphate, mannose 1-phosphate, ribose 1-phosphate and deoxyribose 1-phosphate. 5 or 6-phosphosugars are bad substrates, with the exception of glucose 6-phosphate. Also synthesizes ribose 1,5-bisphosphate. Has only low phosphopentomutase and phosphoglucomutase activities..
• Protein Sequence: MAENTEGDLNSNLLHAPYHTGDPQLDTAIGQWLRWDKNPKTKEQIENLLRNGMNKELRDRLCCRMTFGTAGLRSAMGAGFCYINDLTVIQSTQGMYKYLERCFSDFKQRGFVVGYDTRGQVTSSCSSQRLAKLTAAVLLAKDVPVYLFSRYVPTPFVPYAVQKLKAVAGVMITASHNRKEDNGYKVYWETGAQITSPHDKEILKCIEECVEPWNGSWNDNLVDTSPLKRDPLQDICRRYMEDLKKICFYRELNSKTTLKFVHTSFHGVGHDYVQLAFKVFGFKPPIPVPEQKDPDPDFSTVKCPNPEEGESVLELSLRLAEKENARVVLATDPDADRLAAAELQENGCWKVFTGNELAALFGWWMFDCWKKNKSRNADVKNVYMLATTVSSKILKAIALKEGFHFEETLPGFKWIGSRIIDLLENGKEVLFAFEESIGFLCGTSVLDKDGVSAAVVVAEMASYLETMNITLKQQLVKVYEKYGYHISKTSYFLCYEPPTIKSIFERLRNFDSPKEYPKFCGTFAILHVRDVTTGYDSSQPNKKSVLPVSKNSQMITFTFQNGCVATLRTSGTEPKIKYYAEMCASPDQSDTALLEEELKKLIDALIENFLQPSKNGLIWRSV

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
42	Ubiquitination	WDKNPKTKEQIENLL CCCCCCHHHHHHHHH	54.47	29967540
69	Phosphorylation	CCRMTFGTAGLRSAM HHHCCCCCHHHHHHH	17.23	28060719
134	Phosphorylation	SQRLAKLTAAVLLAK HHHHHHHHHHHHHHC	16.32	21406692
146	Phosphorylation	LAKDVPVYLFSRYVP HHCCCCCEEEECCCC	8.92	-
159	Phosphorylation	VPTPFVPYAVQKLKA CCCCCHHHHHHHHHH	17.69	22817900
173	Phosphorylation	AVAGVMITASHNRKE HHEEEEEEECCCCCC	12.19	29255136
175	Phosphorylation	AGVMITASHNRKEDN EEEEEEECCCCCCCC	16.79	29255136
200	Acetylation	QITSPHDKEILKCIE CCCCCCHHHHHHHHH	43.55	25953088
225	Phosphorylation	NDNLVDTSPLKRDPL CCCCCCCCCCCCCHH	24.62	24719451
249	Phosphorylation	DLKKICFYRELNSKT HHHHHHHHHHCCCCC	9.96	28152594
254	Phosphorylation	CFYRELNSKTTLKFV HHHHHCCCCCEEEEE	43.96	28152594
311	Phosphorylation	PNPEEGESVLELSLR CCHHHCCCHHHHHHH	42.74	-
316	Phosphorylation	GESVLELSLRLAEKE CCCHHHHHHHHHHHH	11.32	24719451
374	Phosphorylation	DCWKKNKSRNADVKN HHHHHCHHCCCCCCH	39.91	29759185
383	Phosphorylation	NADVKNVYMLATTVS CCCCCHHHHHHHHHH	8.87	29759185
387	Phosphorylation	KNVYMLATTVSSKIL CHHHHHHHHHHHHHH	24.62	29978859
388	Phosphorylation	NVYMLATTVSSKILK HHHHHHHHHHHHHHH	16.88	29978859
390	Phosphorylation	YMLATTVSSKILKAI HHHHHHHHHHHHHHH	24.66	29978859
391	Phosphorylation	MLATTVSSKILKAIA HHHHHHHHHHHHHHH	21.27	29759185
395	Ubiquitination	TVSSKILKAIALKEG HHHHHHHHHHHHHCC	41.02	33845483
501	Methylation	CYEPPTIKSIFERLR ECCCCCHHHHHHHHH	39.72	23644510
532	Phosphorylation	ILHVRDVTTGYDSSQ EEEEEECCCCCCCCC	20.84	-
533	Phosphorylation	LHVRDVTTGYDSSQP EEEEECCCCCCCCCC	33.33	-
544	Phosphorylation	SSQPNKKSVLPVSKN CCCCCCCCCEEECCC	30.42	29888752
549	Phosphorylation	KKSVLPVSKNSQMIT CCCCEEECCCCEEEE	24.95	29888752
578	Phosphorylation	GTEPKIKYYAEMCAS CCCCCHHHHHHHHCC	16.04	21406692
579	Phosphorylation	TEPKIKYYAEMCASP CCCCHHHHHHHHCCC	7.35	21406692
585	Phosphorylation	YYAEMCASPDQSDTA HHHHHHCCCCHHHHH	24.87	21406692
589	Phosphorylation	MCASPDQSDTALLEE HHCCCCHHHHHHHHH	44.29	21406692
591	Phosphorylation	ASPDQSDTALLEEEL CCCCHHHHHHHHHHH	25.18	21406692

Upstream regulatory proteins (kinases for phosphorylation sites, E3 ubiquitin ligases of ubiquitination sites, ...)

Oops, there are no upstream regulatory protein records of PGM2L_HUMAN !!

Functions of PTM Sites

Oops, there are no descriptions of PTM sites of PGM2L_HUMAN !!

Disease-associated PTM Sites based on SAP

* Distance = the distance between SAP position and PTM sites.

Oops, there are no SNP-PTM records of PGM2L_HUMAN !!

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference
PIPNB_HUMAN	PITPNB	physical	26344197

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.

Related Literatures of Post-Translational Modification

Phosphorylation

"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-175, AND MASSSPECTROMETRY.
PubMed: 19413330

"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-175, AND MASSSPECTROMETRY.
PubMed: 18669648

"Combining protein-based IMAC, peptide-based IMAC, and MudPIT forefficient phosphoproteomic analysis.";
Cantin G.T., Yi W., Lu B., Park S.K., Xu T., Lee J.-D.,Yates J.R. III;
J. Proteome Res. 7:1346-1351(2008).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-175, AND MASSSPECTROMETRY.
PubMed: 18220336

"Automated phosphoproteome analysis for cultured cancer cells by two-dimensional nanoLC-MS using a calcined titania/C18 biphasic column.";
Imami K., Sugiyama N., Kyono Y., Tomita M., Ishihama Y.;
Anal. Sci. 24:161-166(2008).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-175, AND MASSSPECTROMETRY.
PubMed: 18187866

"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-175, AND MASSSPECTROMETRY.
PubMed: 17081983