dbPTM

PYGM_HUMAN - PTM Information in dbPTM

Basic Information of Protein

Overview of Protein Modification Sites with Functional and Structural Information
UniProt ID	PYGM_HUMAN
UniProt AC	P11217
Protein Name	Glycogen phosphorylase, muscle form
Gene Name	PYGM
Organism	Homo sapiens (Human).
Sequence Length	842
Subcellular Localization
Protein Description	Phosphorylase is an important allosteric enzyme in carbohydrate metabolism. Enzymes from different sources differ in their regulatory mechanisms and in their natural substrates. However, all known phosphorylases share catalytic and structural properties..
Protein Sequence	MSRPLSDQEKRKQISVRGLAGVENVTELKKNFNRHLHFTLVKDRNVATPRDYYFALAHTVRDHLVGRWIRTQQHYYEKDPKRIYYLSLEFYMGRTLQNTMVNLALENACDEATYQLGLDMEELEEIEEDAGLGNGGLGRLAACFLDSMATLGLAAYGYGIRYEFGIFNQKISGGWQMEEADDWLRYGNPWEKARPEFTLPVHFYGHVEHTSQGAKWVDTQVVLAMPYDTPVPGYRNNVVNTMRLWSAKAPNDFNLKDFNVGGYIQAVLDRNLAENISRVLYPNDNFFEGKELRLKQEYFVVAATLQDIIRRFKSSKFGCRDPVRTNFDAFPDKVAIQLNDTHPSLAIPELMRILVDLERMDWDKAWDVTVRTCAYTNHTVLPEALERWPVHLLETLLPRHLQIIYEINQRFLNRVAAAFPGDVDRLRRMSLVEEGAVKRINMAHLCIAGSHAVNGVARIHSEILKKTIFKDFYELEPHKFQNKTNGITPRRWLVLCNPGLAEVIAERIGEDFISDLDQLRKLLSFVDDEAFIRDVAKVKQENKLKFAAYLEREYKVHINPNSLFDIQVKRIHEYKRQLLNCLHVITLYNRIKREPNKFFVPRTVMIGGKAAPGYHMAKMIIRLVTAIGDVVNHDPAVGDRLRVIFLENYRVSLAEKVIPAADLSEQISTAGTEASGTGNMKFMLNGALTIGTMDGANVEMAEEAGEENFFIFGMRVEDVDKLDQRGYNAQEYYDRIPELRQVIEQLSSGFFSPKQPDLFKDIVNMLMHHDRFKVFADYEDYIKCQEKVSALYKNPREWTRMVIRNIATSGKFSSDRTIAQYAREIWGVEPSRQRLPAPDEAI

Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations	Modification	Substrate Peptides & Secondary Structure	ASA (%)	Reference
2	Phosphorylation	------MSRPLSDQE ------CCCCCCHHH	42.48	22673903
2	Acetylation	------MSRPLSDQE ------CCCCCCHHH	42.48	-
6	Phosphorylation	--MSRPLSDQEKRKQ --CCCCCCHHHHHHH	39.67	30001349
11	Dimethylation	PLSDQEKRKQISVRG CCCHHHHHHHCCHHH	35.05	-
11	Methylation	PLSDQEKRKQISVRG CCCHHHHHHHCCHHH	35.05	115372769
15	Phosphorylation	QEKRKQISVRGLAGV HHHHHHCCHHHHCCC	11.85	30278072
26	Phosphorylation	LAGVENVTELKKNFN HCCCCCHHHHHHHHC	47.37	26437602
39	Phosphorylation	FNRHLHFTLVKDRNV HCCCEEEEEECCCCC	21.64	-
42	Ubiquitination	HLHFTLVKDRNVATP CEEEEEECCCCCCCC	54.83	21906983
48	Phosphorylation	VKDRNVATPRDYYFA ECCCCCCCCHHHHHH	17.99	26437602
52	Phosphorylation	NVATPRDYYFALAHT CCCCCHHHHHHHHHH	11.19	28152594
53	Phosphorylation	VATPRDYYFALAHTV CCCCHHHHHHHHHHH	6.15	28152594
71	Phosphorylation	LVGRWIRTQQHYYEK HHHHHHHHCCHHHHC	24.36	26437602
76	Phosphorylation	IRTQQHYYEKDPKRI HHHCCHHHHCCCCCE	17.87	26437602
84	Phosphorylation	EKDPKRIYYLSLEFY HCCCCCEEEEEEEEH	11.46	24043423
85	Phosphorylation	KDPKRIYYLSLEFYM CCCCCEEEEEEEEHH	6.35	24043423
87	Phosphorylation	PKRIYYLSLEFYMGR CCCEEEEEEEEHHCC	15.10	24043423
91	Phosphorylation	YYLSLEFYMGRTLQN EEEEEEEHHCCHHHH	6.84	24043423
95	Phosphorylation	LEFYMGRTLQNTMVN EEEHHCCHHHHHHHH	27.28	27542207
99	Phosphorylation	MGRTLQNTMVNLALE HCCHHHHHHHHHHHH	14.99	27542207
113	Phosphorylation	ENACDEATYQLGLDM HCCCCHHHHHCCCCH	15.11	27542207
114	Phosphorylation	NACDEATYQLGLDME CCCCHHHHHCCCCHH	14.59	27542207
160	Ubiquitination	LAAYGYGIRYEFGIF HHHHCCCEEEEEEEE	2.97	22817900
162	Nitration	AYGYGIRYEFGIFNQ HHCCCEEEEEEEECC	17.43	-
162	Phosphorylation	AYGYGIRYEFGIFNQ HHCCCEEEEEEEECC	17.43	20068231
186	Phosphorylation	EADDWLRYGNPWEKA CCCCHHHCCCHHHHC	21.05	25690035
198	Phosphorylation	EKARPEFTLPVHFYG HHCCCCCEECEEEEE	28.61	26437602
202	Ubiquitination	PEFTLPVHFYGHVEH CCCEECEEEEEECEE	14.31	23000965
204	Phosphorylation	FTLPVHFYGHVEHTS CEECEEEEEECEECC	7.46	26437602
207	Ubiquitination	PVHFYGHVEHTSQGA CEEEEEECEECCCCC	5.11	23000965
210	Phosphorylation	FYGHVEHTSQGAKWV EEEECEECCCCCEEE	14.83	26437602
219	Phosphorylation	QGAKWVDTQVVLAMP CCCEEEEEEEEEECC	17.40	23607784
227	Phosphorylation	QVVLAMPYDTPVPGY EEEEECCCCCCCCCC	21.26	23607784
229	Phosphorylation	VLAMPYDTPVPGYRN EEECCCCCCCCCCCC	21.97	23607784
234	Phosphorylation	YDTPVPGYRNNVVNT CCCCCCCCCCCCHHH	12.23	23607784
241	Phosphorylation	YRNNVVNTMRLWSAK CCCCCHHHHHHHCCC	7.64	26437602
248	Ubiquitination	TMRLWSAKAPNDFNL HHHHHCCCCCCCCCC	59.88	22817900
277	Phosphorylation	RNLAENISRVLYPND HHHHHHHHCCCCCCC	28.11	26437602
281	Phosphorylation	ENISRVLYPNDNFFE HHHHCCCCCCCCCCC	9.35	28152594
290	Ubiquitination	NDNFFEGKELRLKQE CCCCCCCCCCCCCCE	46.51	23000965
295	Ubiquitination	EGKELRLKQEYFVVA CCCCCCCCCEEHHHE	34.35	23000965
298	Phosphorylation	ELRLKQEYFVVAATL CCCCCCEEHHHEHHH	10.12	21406692
304	Phosphorylation	EYFVVAATLQDIIRR EEHHHEHHHHHHHHH	18.40	21406692
316	Acetylation	IRRFKSSKFGCRDPV HHHHHHCCCCCCCCC	53.52	22636571
325	Phosphorylation	GCRDPVRTNFDAFPD CCCCCCCCCCCCCCC	40.23	26437602
364	Succinylation	LERMDWDKAWDVTVR HHHCCHHHHHCEEEE	47.31	-
372	Phosphorylation	AWDVTVRTCAYTNHT HHCEEEEECCCCCCC	9.35	-
395	Ubiquitination	WPVHLLETLLPRHLQ CCHHHHHHHCHHHHH	33.30	21890473
395	Phosphorylation	WPVHLLETLLPRHLQ CCHHHHHHHCHHHHH	33.30	22673903
430	Phosphorylation	VDRLRRMSLVEEGAV HHHHHHHHHHHHCCC	27.70	22777824
450	Phosphorylation	AHLCIAGSHAVNGVA HHHHHHCHHHHCCHH	10.15	-
461	Phosphorylation	NGVARIHSEILKKTI CCHHHHCHHHHHHHH	24.78	26437602
467	Phosphorylation	HSEILKKTIFKDFYE CHHHHHHHHCCCHHH	30.02	-
473	Phosphorylation	KTIFKDFYELEPHKF HHHCCCHHHCCCHHC	29.73	19764811
483	Ubiquitination	EPHKFQNKTNGITPR CCHHCCCCCCCCCCC	32.36	21890473
484	Phosphorylation	PHKFQNKTNGITPRR CHHCCCCCCCCCCCC	46.34	26437602
514	Phosphorylation	RIGEDFISDLDQLRK HHCCCHHCCHHHHHH	31.92	19764811
524	Phosphorylation	DQLRKLLSFVDDEAF HHHHHHHHHCCHHHH	33.39	22673903
537	Acetylation	AFIRDVAKVKQENKL HHHHHHHHHHHHCCH	50.22	20167786
568	Ubiquitination	NSLFDIQVKRIHEYK CCCHHEEHHHHHHHH	4.61	22817900
574	Phosphorylation	QVKRIHEYKRQLLNC EHHHHHHHHHHHHHH	9.41	26437602
603	Phosphorylation	NKFFVPRTVMIGGKA CCCCCCCEEEECCEE	14.35	-
609	Acetylation	RTVMIGGKAAPGYHM CEEEECCEECCCHHH	35.84	30591717
614	Phosphorylation	GGKAAPGYHMAKMII CCEECCCHHHHHHHH	6.33	28348404
618	Acetylation	APGYHMAKMIIRLVT CCCHHHHHHHHHHHH	24.05	30591723
625	Phosphorylation	KMIIRLVTAIGDVVN HHHHHHHHHHHHHHC	19.70	-
656	Ubiquitination	YRVSLAEKVIPAADL CCHHHHHHHCCHHHH	39.60	22817900
666	Ubiquitination	PAADLSEQISTAGTE CHHHHHHHHHCCCCC	31.40	22817900
681	Other	ASGTGNMKFMLNGAL CCCCCCCEEEECCEE	31.46	-
681	N6-(pyridoxal phosphate)lysine	ASGTGNMKFMLNGAL CCCCCCCEEEECCEE	31.46	-
732	Phosphorylation	RGYNAQEYYDRIPEL CCCCHHHHHHHHHHH	9.89	19764811
733	Phosphorylation	GYNAQEYYDRIPELR CCCHHHHHHHHHHHH	9.67	19764811
747	Phosphorylation	RQVIEQLSSGFFSPK HHHHHHHHCCCCCCC	28.27	26437602
748	Phosphorylation	QVIEQLSSGFFSPKQ HHHHHHHCCCCCCCC	48.49	26437602
752	Phosphorylation	QLSSGFFSPKQPDLF HHHCCCCCCCCCCHH	29.00	24719451
754	Ubiquitination	SSGFFSPKQPDLFKD HCCCCCCCCCCHHHH	73.58	22817900
789	Phosphorylation	IKCQEKVSALYKNPR HHHHHHHHHHHCCHH	24.51	26437602
792	Phosphorylation	QEKVSALYKNPREWT HHHHHHHHCCHHHHH	14.40	-
809	Phosphorylation	VIRNIATSGKFSSDR HHHHHHHCCCCCCCH	30.85	26437602
831	Phosphorylation	EIWGVEPSRQRLPAP HHHCCCCCCCCCCCC	27.78	26437602

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
15	S	Phosphorylation	Kinase	PHK-FAMILY	-	GPS
15	S	Phosphorylation	Kinase	PHK	-	Uniprot
15	S	Phosphorylation	Kinase	PHK_GROUP	-	PhosphoELM

Functions of PTM Sites

Modified Location	Modified Residue	Modification	Function	Reference
15	S	Phosphorylation		1150650
Phosphorylation of Ser-15 converts phosphorylase B (unphosphorylated) to phosphorylase A.

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 PYGM_HUMAN !!

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference	Domain-Domain Interactions
NTAQ1_HUMAN	WDYHV1	physical	25416956
GLGB_HUMAN	GBE1	physical	26344197

Drug and Disease Associations

Kegg Disease
There are no disease associations of PTM sites.
OMIM Disease
232600	Glycogen storage disease 5 (GSD5)
Kegg Drug
There are no disease associations of PTM sites.
DrugBank
There are no disease associations of PTM sites.

Regulatory Network of PYGM_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-316, AND MASS SPECTROMETRY.	19608861 [Abstract]
Phosphorylation
Reference	PubMed
"Global phosphoproteome of HT-29 human colon adenocarcinoma cells."; Kim J.-E., Tannenbaum S.R., White F.M.; J. Proteome Res. 4:1339-1346(2005). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-15, AND MASSSPECTROMETRY.	16083285 [Abstract]
"Regulation of glycogen phosphorylase. Role of the peptide regionsurrounding the phosphoserine residue in determining enzymeproperties."; Carty T.J., Tu J., Graves D.J.; J. Biol. Chem. 250:4980-4985(1975). Cited for: PHOSPHORYLATION AT SER-15.	1150650 [Abstract]

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