dbPTM

PGM1_HUMAN - PTM Information in dbPTM

Basic Information of Protein

Overview of Protein Modification Sites with Functional and Structural Information
UniProt ID	PGM1_HUMAN
UniProt AC	P36871
Protein Name	Phosphoglucomutase-1
Gene Name	PGM1
Organism	Homo sapiens (Human).
Sequence Length	562
Subcellular Localization	Isoform 1: Cytoplasm.
Protein Description	This enzyme participates in both the breakdown and synthesis of glucose..
Protein Sequence	MVKIVTVKTQAYQDQKPGTSGLRKRVKVFQSSANYAENFIQSIISTVEPAQRQEATLVVGGDGRFYMKEAIQLIARIAAANGIGRLVIGQNGILSTPAVSCIIRKIKAIGGIILTASHNPGGPNGDFGIKFNISNGGPAPEAITDKIFQISKTIEEYAVCPDLKVDLGVLGKQQFDLENKFKPFTVEIVDSVEAYATMLRSIFDFSALKELLSGPNRLKIRIDAMHGVVGPYVKKILCEELGAPANSAVNCVPLEDFGGHHPDPNLTYAADLVETMKSGEHDFGAAFDGDGDRNMILGKHGFFVNPSDSVAVIAANIFSIPYFQQTGVRGFARSMPTSGALDRVASATKIALYETPTGWKFFGNLMDASKLSLCGEESFGTGSDHIREKDGLWAVLAWLSILATRKQSVEDILKDHWQKYGRNFFTRYDYEEVEAEGANKMMKDLEALMFDRSFVGKQFSANDKVYTVEKADNFEYSDPVDGSISRNQGLRLIFTDGSRIVFRLSGTGSAGATIRLYIDSYEKDVAKINQDPQVMLAPLISIALKVSQLQERTGRTAPTVIT

Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations	Modification	Substrate Peptides & Secondary Structure	ASA (%)	Reference
1	Acetylation	-------MVKIVTVK -------CCEEEEEE	6.63	22814378
1 (in isoform 2)	Acetylation	-	6.63	21406692
2 (in isoform 2)	Phosphorylation	-	6.11	21406692
3	2-Hydroxyisobutyrylation	-----MVKIVTVKTQ -----CCEEEEEECC	30.11	-
3	Acetylation	-----MVKIVTVKTQ -----CCEEEEEECC	30.11	27452117
8	Acetylation	MVKIVTVKTQAYQDQ CCEEEEEECCCCCCC	26.08	25953088
8	Ubiquitination	MVKIVTVKTQAYQDQ CCEEEEEECCCCCCC	26.08	-
9	Phosphorylation	VKIVTVKTQAYQDQK CEEEEEECCCCCCCC	17.69	21406692
9 (in isoform 2)	Phosphorylation	-	17.69	21406692
11 (in isoform 2)	Phosphorylation	-	14.80	21406692
12	Phosphorylation	VTVKTQAYQDQKPGT EEEECCCCCCCCCCC	11.64	21406692
12 (in isoform 2)	Phosphorylation	-	11.64	21406692
16	Acetylation	TQAYQDQKPGTSGLR CCCCCCCCCCCCHHH	54.42	19608861
16	Malonylation	TQAYQDQKPGTSGLR CCCCCCCCCCCCHHH	54.42	26320211
16	Ubiquitination	TQAYQDQKPGTSGLR CCCCCCCCCCCCHHH	54.42	19608861
19	Phosphorylation	YQDQKPGTSGLRKRV CCCCCCCCCHHHHHH	28.31	28348404
20	Phosphorylation	QDQKPGTSGLRKRVK CCCCCCCCHHHHHHH	41.57	28555341
24 (in isoform 2)	Phosphorylation	-	67.59	21406692
27 (in isoform 2)	Phosphorylation	-	41.17	21406692
30 (in isoform 2)	Phosphorylation	-	39.19	21406692
37 (in isoform 2)	Phosphorylation	-	42.17	21406692
38 (in isoform 2)	Phosphorylation	-	31.02	21406692
42	Phosphorylation	YAENFIQSIISTVEP HHHHHHHHHHHCCCH	19.64	22673903
45	Phosphorylation	NFIQSIISTVEPAQR HHHHHHHHCCCHHHC	25.40	22673903
46	Phosphorylation	FIQSIISTVEPAQRQ HHHHHHHCCCHHHCC	20.62	22673903
56	Phosphorylation	PAQRQEATLVVGGDG HHHCCEEEEEECCCC	21.23	26437602
66	Phosphorylation	VGGDGRFYMKEAIQL ECCCCCCCHHHHHHH	13.10	-
115	Phosphorylation	AIGGIILTASHNPGG HCCEEEEEEECCCCC	18.73	29255136
117	Phosphorylation	GGIILTASHNPGGPN CEEEEEEECCCCCCC	20.68	29255136
133 (in isoform 2)	Phosphorylation	-	3.68	21406692
134	Phosphorylation	FGIKFNISNGGPAPE CEEEEEECCCCCCCH	30.44	19764811
135 (in isoform 2)	Phosphorylation	-	56.49	24719451
146	Ubiquitination	APEAITDKIFQISKT CCHHHHHHHHHHCCC	36.45	21890473
146	2-Hydroxyisobutyrylation	APEAITDKIFQISKT CCHHHHHHHHHHCCC	36.45	-
146	Acetylation	APEAITDKIFQISKT CCHHHHHHHHHHCCC	36.45	25953088
146	Ubiquitination	APEAITDKIFQISKT CCHHHHHHHHHHCCC	36.45	21890473
146 (in isoform 1)	Ubiquitination	-	36.45	21890473
152	Acetylation	DKIFQISKTIEEYAV HHHHHHCCCHHHHCC	55.97	27452117
164	2-Hydroxyisobutyrylation	YAVCPDLKVDLGVLG HCCCCCCEEEEECCC	40.87	-
164	Acetylation	YAVCPDLKVDLGVLG HCCCCCCEEEEECCC	40.87	26051181
164	Ubiquitination	YAVCPDLKVDLGVLG HCCCCCCEEEEECCC	40.87	-
164 (in isoform 2)	Ubiquitination	-	40.87	21890473
164	Ubiquitination	YAVCPDLKVDLGVLG HCCCCCCEEEEECCC	40.87	21890473
172	2-Hydroxyisobutyrylation	VDLGVLGKQQFDLEN EEEECCCCCCCCCCC	36.44	-
172	Ubiquitination	VDLGVLGKQQFDLEN EEEECCCCCCCCCCC	36.44	-
185	Phosphorylation	ENKFKPFTVEIVDSV CCCCCCEEEEEHHHH	26.25	22673903
191	Phosphorylation	FTVEIVDSVEAYATM EEEEEHHHHHHHHHH	15.80	22673903
195	Phosphorylation	IVDSVEAYATMLRSI EHHHHHHHHHHHHHH	6.79	19835603
197	Phosphorylation	DSVEAYATMLRSIFD HHHHHHHHHHHHHCC	12.22	19835603
201	Phosphorylation	AYATMLRSIFDFSAL HHHHHHHHHCCHHHH	24.52	28857561
206	Phosphorylation	LRSIFDFSALKELLS HHHHCCHHHHHHHHH	34.24	24972180
213	Phosphorylation	SALKELLSGPNRLKI HHHHHHHHCCCCEEE	65.90	26437602
219	Acetylation	LSGPNRLKIRIDAMH HHCCCCEEEEEEHHC	27.05	20167786
224 (in isoform 2)	Phosphorylation	-	6.90	27251275
232	Phosphorylation	MHGVVGPYVKKILCE HCCCHHHHHHHHHHH	20.97	23403867
234	2-Hydroxyisobutyrylation	GVVGPYVKKILCEEL CCHHHHHHHHHHHHH	28.40	-
234	Acetylation	GVVGPYVKKILCEEL CCHHHHHHHHHHHHH	28.40	19608861
247	Phosphorylation	ELGAPANSAVNCVPL HHCCCCCCCCCEEEH	35.38	-
293	Methylation	AFDGDGDRNMILGKH ECCCCCCCCEEEEEC	39.90	115487269
295	Sulfoxidation	DGDGDRNMILGKHGF CCCCCCCEEEEECEE	2.52	30846556
334	Phosphorylation	GVRGFARSMPTSGAL CCCHHHHCCCCCCHH	26.19	20068231
338	Phosphorylation	FARSMPTSGALDRVA HHHCCCCCCHHHHHH	19.05	-
343	Methylation	PTSGALDRVASATKI CCCCHHHHHHHCCEE	27.10	115487279
346	Phosphorylation	GALDRVASATKIALY CHHHHHHHCCEEEEE	33.35	28258704
348	Phosphorylation	LDRVASATKIALYET HHHHHHCCEEEEEEC	22.08	26074081
349	Ubiquitination	DRVASATKIALYETP HHHHHCCEEEEEECC	26.21	21890473
349	Acetylation	DRVASATKIALYETP HHHHHCCEEEEEECC	26.21	27452117
349	Ubiquitination	DRVASATKIALYETP HHHHHCCEEEEEECC	26.21	21890473
349 (in isoform 1)	Ubiquitination	-	26.21	21890473
353	Phosphorylation	SATKIALYETPTGWK HCCEEEEEECCCCCH	14.56	21945579
355	Phosphorylation	TKIALYETPTGWKFF CEEEEEECCCCCHHH	16.76	21945579
357	Phosphorylation	IALYETPTGWKFFGN EEEEECCCCCHHHHH	64.19	21945579
364 (in isoform 2)	Phosphorylation	-	27.34	27251275
367 (in isoform 2)	Ubiquitination	-	51.35	21890473
367	Ubiquitination	KFFGNLMDASKLSLC HHHHHHHCHHHHEEC	51.35	21890473
369	Phosphorylation	FGNLMDASKLSLCGE HHHHHCHHHHEECCC	29.84	20068231
371 (in isoform 2)	Phosphorylation	-	4.35	27642862
372	Phosphorylation	LMDASKLSLCGEESF HHCHHHHEECCCCCC	25.91	24275569
378	Phosphorylation	LSLCGEESFGTGSDH HEECCCCCCCCCCHH	25.36	28857561
381	Phosphorylation	CGEESFGTGSDHIRE CCCCCCCCCCHHHHH	31.34	24275569
406	2-Hydroxyisobutyrylation	LSILATRKQSVEDIL HHHHHHCCCCHHHHH	42.44	-
408	Phosphorylation	ILATRKQSVEDILKD HHHHCCCCHHHHHHH	30.43	26657352
419	Ubiquitination	ILKDHWQKYGRNFFT HHHHHHHHHCCCCCC	44.47	21890473
419	Acetylation	ILKDHWQKYGRNFFT HHHHHHHHHCCCCCC	44.47	19608861
419	Succinylation	ILKDHWQKYGRNFFT HHHHHHHHHCCCCCC	44.47	-
419	Succinylation	ILKDHWQKYGRNFFT HHHHHHHHHCCCCCC	44.47	19608861
419	Ubiquitination	ILKDHWQKYGRNFFT HHHHHHHHHCCCCCC	44.47	19608861
419 (in isoform 1)	Ubiquitination	-	44.47	21890473
426 (in isoform 2)	Phosphorylation	-	24.96	27251275
430	Phosphorylation	NFFTRYDYEEVEAEG CCCCCCCHHHHHHHH	12.68	-
437 (in isoform 2)	Ubiquitination	-	41.31	21890473
437	Ubiquitination	YEEVEAEGANKMMKD HHHHHHHHHHHHHHH	41.31	21890473
443	Acetylation	EGANKMMKDLEALMF HHHHHHHHHHHHHHC	56.51	27452117
449	Sulfoxidation	MKDLEALMFDRSFVG HHHHHHHHCCHHHCC	4.18	30846556
452	Methylation	LEALMFDRSFVGKQF HHHHHCCHHHCCCEE	22.26	115487249
457	2-Hydroxyisobutyrylation	FDRSFVGKQFSANDK CCHHHCCCEECCCCE	42.75	-
457	Acetylation	FDRSFVGKQFSANDK CCHHHCCCEECCCCE	42.75	27452117
457	Malonylation	FDRSFVGKQFSANDK CCHHHCCCEECCCCE	42.75	26320211
457	Succinylation	FDRSFVGKQFSANDK CCHHHCCCEECCCCE	42.75	23954790
457	Ubiquitination	FDRSFVGKQFSANDK CCHHHCCCEECCCCE	42.75	-
460	Phosphorylation	SFVGKQFSANDKVYT HHCCCEECCCCEEEE	24.54	26437602
464	Acetylation	KQFSANDKVYTVEKA CEECCCCEEEEEEEC	36.63	27452117
467	Phosphorylation	SANDKVYTVEKADNF CCCCEEEEEEECCCC	25.77	15378030
470	Ubiquitination	DKVYTVEKADNFEYS CEEEEEEECCCCCCC	57.62	2190698
470 (in isoform 1)	Ubiquitination	-	57.62	21890473
476	Phosphorylation	EKADNFEYSDPVDGS EECCCCCCCCCCCCC	17.78	-
477	Phosphorylation	KADNFEYSDPVDGSI ECCCCCCCCCCCCCC	28.39	26437602
483	Phosphorylation	YSDPVDGSISRNQGL CCCCCCCCCCCCCCE	16.96	21712546
485	Phosphorylation	DPVDGSISRNQGLRL CCCCCCCCCCCCEEE	27.20	26437602
488 (in isoform 2)	Ubiquitination	-	51.71	21890473
491	Methylation	ISRNQGLRLIFTDGS CCCCCCEEEEEECCC	32.34	115487259
495	Phosphorylation	QGLRLIFTDGSRIVF CCEEEEEECCCEEEE	32.24	23532336
498	Phosphorylation	RLIFTDGSRIVFRLS EEEEECCCEEEEEEE	22.95	23532336
505	O-linked_Glycosylation	SRIVFRLSGTGSAGA CEEEEEEECCCCCCC	30.01	30379171
505	Phosphorylation	SRIVFRLSGTGSAGA CEEEEEEECCCCCCC	30.01	25072903
507	Phosphorylation	IVFRLSGTGSAGATI EEEEEECCCCCCCEE	25.29	25072903
509	Phosphorylation	FRLSGTGSAGATIRL EEEECCCCCCCEEEE	24.30	28258704
513	Phosphorylation	GTGSAGATIRLYIDS CCCCCCCEEEEEEEC	13.00	21406692
520	Phosphorylation	TIRLYIDSYEKDVAK EEEEEEECHHHHHHH	26.15	-
521	Phosphorylation	IRLYIDSYEKDVAKI EEEEEECHHHHHHHH	24.21	26437602
523	2-Hydroxyisobutyrylation	LYIDSYEKDVAKINQ EEEECHHHHHHHHCC	49.63	-
523	Acetylation	LYIDSYEKDVAKINQ EEEECHHHHHHHHCC	49.63	23236377
523 (in isoform 2)	Phosphorylation	-	49.63	27251275
527 (in isoform 2)	Phosphorylation	-	41.88	27251275
541	Phosphorylation	VMLAPLISIALKVSQ HHHHHHHHHHHHHHH	14.97	22673903

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
467	T	Phosphorylation	Kinase	PAK1	Q13153	Uniprot

Functions of PTM Sites

Modified Location	Modified Residue	Modification	Function	Reference
467	T	Phosphorylation		15378030
Phosphorylation at Thr-467 by PAK1 significantly enhances enzymatic activity.

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 PGM1_HUMAN !!

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference
S10A1_HUMAN	S100A1	physical	8894274
S100B_HUMAN	S100B	physical	8894274
A4_HUMAN	APP	physical	21832049
TALDO_HUMAN	TALDO1	physical	22939629
PGM2_HUMAN	PGM2	physical	22939629
PUR9_HUMAN	ATIC	physical	26344197
CATA_HUMAN	CAT	physical	26344197
ENOA_HUMAN	ENO1	physical	26344197
EXOC2_HUMAN	EXOC2	physical	26344197
GALK2_HUMAN	GALK2	physical	26344197
G6PI_HUMAN	GPI	physical	26344197
GRHPR_HUMAN	GRHPR	physical	26344197
LKHA4_HUMAN	LTA4H	physical	26344197
PGM2_HUMAN	PGM2	physical	26344197
AGM1_HUMAN	PGM3	physical	26344197
PRDX6_HUMAN	PRDX6	physical	26344197
SCPDL_HUMAN	SCCPDH	physical	26344197
TALDO_HUMAN	TALDO1	physical	26344197
TPIS_HUMAN	TPI1	physical	26344197

Drug and Disease Associations

Kegg Disease
There are no disease associations of PTM sites.
OMIM Disease
614921	Congenital disorder of glycosylation 1T (CDG1T)
Kegg Drug
There are no disease associations of PTM sites.
DrugBank
There are no disease associations of PTM sites.

Regulatory Network of PGM1_HUMAN

Related Literatures of Post-Translational Modification

Acetylation
Reference	PubMed
"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-16 AND LYS-419, AND MASSSPECTROMETRY.	19608861 [Abstract]
Phosphorylation
Reference	PubMed
"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 SER-117, 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-115 AND SER-117, ANDMASS SPECTROMETRY.	18669648 [Abstract]
"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-117, AND MASSSPECTROMETRY.	18187866 [Abstract]
"Improved titanium dioxide enrichment of phosphopeptides from HeLacells and high confident phosphopeptide identification by cross-validation of MS/MS and MS/MS/MS spectra."; Yu L.-R., Zhu Z., Chan K.C., Issaq H.J., Dimitrov D.S., Veenstra T.D.; J. Proteome Res. 6:4150-4162(2007). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-115 AND SER-117, ANDMASS SPECTROMETRY.	17924679 [Abstract]
"An extensive survey of tyrosine phosphorylation revealing new sitesin human mammary epithelial cells."; Heibeck T.H., Ding S.-J., Opresko L.K., Zhao R., Schepmoes A.A.,Yang F., Tolmachev A.V., Monroe M.E., Camp D.G. II, Smith R.D.,Wiley H.S., Qian W.-J.; J. Proteome Res. 8:3852-3861(2009). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-353, AND MASSSPECTROMETRY.	19534553 [Abstract]

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