dbPTM

PMG1_YEAST - PTM Information in dbPTM

Basic Information of Protein

Overview of Protein Modification Sites with Functional and Structural Information
UniProt ID	PMG1_YEAST
UniProt AC	P00950
Protein Name	Phosphoglycerate mutase 1
Gene Name	GPM1
Organism	Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast).
Sequence Length	247
Subcellular Localization	Cytoplasm . Mitochondrion outer membrane Peripheral membrane protein Cytoplasmic side . Mitochondrion intermembrane space .
Protein Description	Interconversion of 3- and 2-phosphoglycerate with 2,3-bisphosphoglycerate as the primer of the reaction. Can also Catalyzes the reaction of EC 5.4.2.4 (synthase), but with a reduced activity..
Protein Sequence	MPKLVLVRHGQSEWNEKNLFTGWVDVKLSAKGQQEAARAGELLKEKKVYPDVLYTSKLSRAIQTANIALEKADRLWIPVNRSWRLNERHYGDLQGKDKAETLKKFGEEKFNTYRRSFDVPPPPIDASSPFSQKGDERYKYVDPNVLPETESLALVIDRLLPYWQDVIAKDLLSGKTVMIAAHGNSLRGLVKHLEGISDADIAKLNIPTGIPLVFELDENLKPSKPSYYLDPEAAAAGAAAVANQGKK

Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations	Modification	Substrate Peptides & Secondary Structure	ASA (%)	Reference
3	2-Hydroxyisobutyrylation	-----MPKLVLVRHG -----CCCEEEEECC	50.34	-
12	Phosphorylation	VLVRHGQSEWNEKNL EEEECCCCCCCCCCC	49.53	19823750
17	Ubiquitination	GQSEWNEKNLFTGWV CCCCCCCCCCCCEEE	56.59	23749301
17	Acetylation	GQSEWNEKNLFTGWV CCCCCCCCCCCCEEE	56.59	24489116
21	Phosphorylation	WNEKNLFTGWVDVKL CCCCCCCCEEEEEEE	33.04	22369663
27	Ubiquitination	FTGWVDVKLSAKGQQ CCEEEEEEECHHHHH	32.06	23749301
31	Acetylation	VDVKLSAKGQQEAAR EEEEECHHHHHHHHH	54.60	25381059
31	Ubiquitination	VDVKLSAKGQQEAAR EEEEECHHHHHHHHH	54.60	23749301
31	2-Hydroxyisobutyrylation	VDVKLSAKGQQEAAR EEEEECHHHHHHHHH	54.60	-
31	Succinylation	VDVKLSAKGQQEAAR EEEEECHHHHHHHHH	54.60	23954790
44	Succinylation	ARAGELLKEKKVYPD HHHHHHHHHCCCCCC	78.93	23954790
44	Acetylation	ARAGELLKEKKVYPD HHHHHHHHHCCCCCC	78.93	24489116
44	2-Hydroxyisobutyrylation	ARAGELLKEKKVYPD HHHHHHHHHCCCCCC	78.93	-
44	Ubiquitination	ARAGELLKEKKVYPD HHHHHHHHHCCCCCC	78.93	23749301
46	Ubiquitination	AGELLKEKKVYPDVL HHHHHHHCCCCCCHH	46.05	22817900
47	Ubiquitination	GELLKEKKVYPDVLY HHHHHHCCCCCCHHH	48.36	23749301
47	Succinylation	GELLKEKKVYPDVLY HHHHHHCCCCCCHHH	48.36	23954790
47	Acetylation	GELLKEKKVYPDVLY HHHHHHCCCCCCHHH	48.36	24489116
47	2-Hydroxyisobutyrylation	GELLKEKKVYPDVLY HHHHHHCCCCCCHHH	48.36	-
49	Phosphorylation	LLKEKKVYPDVLYTS HHHHCCCCCCHHHHH	11.55	21440633
54	Phosphorylation	KVYPDVLYTSKLSRA CCCCCHHHHHHHHHH	14.60	28889911
55	Phosphorylation	VYPDVLYTSKLSRAI CCCCHHHHHHHHHHH	18.41	21440633
56	Phosphorylation	YPDVLYTSKLSRAIQ CCCHHHHHHHHHHHH	20.31	28152593
57	Succinylation	PDVLYTSKLSRAIQT CCHHHHHHHHHHHHH	42.56	23954790
57	Acetylation	PDVLYTSKLSRAIQT CCHHHHHHHHHHHHH	42.56	24489116
57	Ubiquitination	PDVLYTSKLSRAIQT CCHHHHHHHHHHHHH	42.56	23749301
57	2-Hydroxyisobutyrylation	PDVLYTSKLSRAIQT CCHHHHHHHHHHHHH	42.56	-
59	Phosphorylation	VLYTSKLSRAIQTAN HHHHHHHHHHHHHHH	24.33	21440633
64	Phosphorylation	KLSRAIQTANIALEK HHHHHHHHHHHHHHH	18.63	28152593
71	2-Hydroxyisobutyrylation	TANIALEKADRLWIP HHHHHHHHCCEEEEE	57.34	-
71	Succinylation	TANIALEKADRLWIP HHHHHHHHCCEEEEE	57.34	23954790
71	Acetylation	TANIALEKADRLWIP HHHHHHHHCCEEEEE	57.34	24489116
71	Ubiquitination	TANIALEKADRLWIP HHHHHHHHCCEEEEE	57.34	23749301
90	Phosphorylation	WRLNERHYGDLQGKD CCCCHHCCCCCCCCC	20.68	28889911
96	Succinylation	HYGDLQGKDKAETLK CCCCCCCCCHHHHHH	42.99	23954790
96	Acetylation	HYGDLQGKDKAETLK CCCCCCCCCHHHHHH	42.99	24489116
96	2-Hydroxyisobutyrylation	HYGDLQGKDKAETLK CCCCCCCCCHHHHHH	42.99	-
96	Ubiquitination	HYGDLQGKDKAETLK CCCCCCCCCHHHHHH	42.99	22817900
98	Acetylation	GDLQGKDKAETLKKF CCCCCCCHHHHHHHH	52.16	24489116
98	Ubiquitination	GDLQGKDKAETLKKF CCCCCCCHHHHHHHH	52.16	22817900
103	Acetylation	KDKAETLKKFGEEKF CCHHHHHHHHCHHHH	54.17	24489116
103	Succinylation	KDKAETLKKFGEEKF CCHHHHHHHHCHHHH	54.17	23954790
103	2-Hydroxyisobutyrylation	KDKAETLKKFGEEKF CCHHHHHHHHCHHHH	54.17	-
103	Ubiquitination	KDKAETLKKFGEEKF CCHHHHHHHHCHHHH	54.17	22817900
104	Succinylation	DKAETLKKFGEEKFN CHHHHHHHHCHHHHH	62.81	23954790
104	Ubiquitination	DKAETLKKFGEEKFN CHHHHHHHHCHHHHH	62.81	22817900
104	2-Hydroxyisobutyrylation	DKAETLKKFGEEKFN CHHHHHHHHCHHHHH	62.81	-
104	Acetylation	DKAETLKKFGEEKFN CHHHHHHHHCHHHHH	62.81	24489116
109	2-Hydroxyisobutyrylation	LKKFGEEKFNTYRRS HHHHCHHHHHHCCCC	39.34	-
109	Ubiquitination	LKKFGEEKFNTYRRS HHHHCHHHHHHCCCC	39.34	23749301
109	Succinylation	LKKFGEEKFNTYRRS HHHHCHHHHHHCCCC	39.34	23954790
109	Acetylation	LKKFGEEKFNTYRRS HHHHCHHHHHHCCCC	39.34	24489116
112	Phosphorylation	FGEEKFNTYRRSFDV HCHHHHHHCCCCCCC	22.87	25521595
113	Phosphorylation	GEEKFNTYRRSFDVP CHHHHHHCCCCCCCC	12.72	25521595
116	Phosphorylation	KFNTYRRSFDVPPPP HHHHCCCCCCCCCCC	19.46	22369663
127	Phosphorylation	PPPPIDASSPFSQKG CCCCCCCCCCCCCCC	34.49	22369663
128	Phosphorylation	PPPIDASSPFSQKGD CCCCCCCCCCCCCCC	31.52	22369663
131	Phosphorylation	IDASSPFSQKGDERY CCCCCCCCCCCCCCC	34.07	22369663
133	Acetylation	ASSPFSQKGDERYKY CCCCCCCCCCCCCCC	68.10	24489116
133	Succinylation	ASSPFSQKGDERYKY CCCCCCCCCCCCCCC	68.10	23954790
133	Ubiquitination	ASSPFSQKGDERYKY CCCCCCCCCCCCCCC	68.10	23749301
138	Phosphorylation	SQKGDERYKYVDPNV CCCCCCCCCCCCCCC	12.48	22369663
139	Acetylation	QKGDERYKYVDPNVL CCCCCCCCCCCCCCC	45.05	24489116
139	Succinylation	QKGDERYKYVDPNVL CCCCCCCCCCCCCCC	45.05	23954790
139	Ubiquitination	QKGDERYKYVDPNVL CCCCCCCCCCCCCCC	45.05	23749301
140	Phosphorylation	KGDERYKYVDPNVLP CCCCCCCCCCCCCCC	10.93	21440633
169	Ubiquitination	YWQDVIAKDLLSGKT HHHHHHHHHHHCCCE	37.47	23749301
169	2-Hydroxyisobutyrylation	YWQDVIAKDLLSGKT HHHHHHHHHHHCCCE	37.47	-
169	Succinylation	YWQDVIAKDLLSGKT HHHHHHHHHHHCCCE	37.47	23954790
169	Acetylation	YWQDVIAKDLLSGKT HHHHHHHHHHHCCCE	37.47	24489116
173	Phosphorylation	VIAKDLLSGKTVMIA HHHHHHHCCCEEEEE	45.61	21440633
175	Ubiquitination	AKDLLSGKTVMIAAH HHHHHCCCEEEEEEC	34.27	23749301
175	2-Hydroxyisobutyrylation	AKDLLSGKTVMIAAH HHHHHCCCEEEEEEC	34.27	-
175	Acetylation	AKDLLSGKTVMIAAH HHHHHCCCEEEEEEC	34.27	24489116
176	Phosphorylation	KDLLSGKTVMIAAHG HHHHCCCEEEEEECC	20.87	20377248
185	Phosphorylation	MIAAHGNSLRGLVKH EEEECCCHHHHHHHH	24.84	17287358
191	2-Hydroxyisobutyrylation	NSLRGLVKHLEGISD CHHHHHHHHHCCCCH	47.73	-
191	Succinylation	NSLRGLVKHLEGISD CHHHHHHHHHCCCCH	47.73	23954790
191	Acetylation	NSLRGLVKHLEGISD CHHHHHHHHHCCCCH	47.73	24489116
191	Ubiquitination	NSLRGLVKHLEGISD CHHHHHHHHHCCCCH	47.73	23749301
197	Phosphorylation	VKHLEGISDADIAKL HHHHCCCCHHHHHHC	37.29	22369663
203	Ubiquitination	ISDADIAKLNIPTGI CCHHHHHHCCCCCCC	42.26	15699485
221	Acetylation	FELDENLKPSKPSYY EEECCCCCCCCCCCC	59.85	22865919
223	Phosphorylation	LDENLKPSKPSYYLD ECCCCCCCCCCCCCC	56.46	21440633
224	Ubiquitination	DENLKPSKPSYYLDP CCCCCCCCCCCCCCH	46.65	24961812
246	Acetylation	AAVANQGKK------ HHHHHCCCC------	45.61	24489116

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
Oops, there are no upstream regulatory protein records of PMG1_YEAST !!

Functions of PTM Sites

Modified Location	Modified Residue	Modification	Function	Reference
Oops, there are no descriptions of PTM sites of PMG1_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 PMG1_YEAST !!

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference
CFAH_HUMAN	CFH	physical	17959597
PMG1_YEAST	GPM1	physical	9512715
PMG2_YEAST	GPM2	genetic	16941010
PMG3_YEAST	GPM3	genetic	16941010
UBI4P_YEAST	UBI4	physical	20694217

Drug and Disease Associations

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

Regulatory Network of PMG1_YEAST

Related Literatures of Post-Translational Modification

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 SER-116; SER-127; SER-128;SER-131 AND SER-197, 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-116; SER-127; SER-128AND SER-197, AND MASS 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-12; SER-116; SER-128 ANDSER-185, AND MASS SPECTROMETRY.	17287358 [Abstract]
"Large-scale phosphorylation analysis of alpha-factor-arrestedSaccharomyces cerevisiae."; Li X., Gerber S.A., Rudner A.D., Beausoleil S.A., Haas W., Villen J.,Elias J.E., Gygi S.P.; J. Proteome Res. 6:1190-1197(2007). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-116, AND MASSSPECTROMETRY.	17330950 [Abstract]