dbPTM

PYGB_HUMAN - PTM Information in dbPTM

Basic Information of Protein

Overview of Protein Modification Sites with Functional and Structural Information
UniProt ID	PYGB_HUMAN
UniProt AC	P11216
Protein Name	Glycogen phosphorylase, brain form {ECO:0000303\|PubMed:3346228}
Gene Name	PYGB {ECO:0000303\|PubMed:3346228}
Organism	Homo sapiens (Human).
Sequence Length	843
Subcellular Localization
Protein Description	Glycogen phosphorylase that regulates glycogen mobilization. [PubMed: 27402852 Phosphorylase is an important allosteric enzyme in carbohydrate metabolism]
Protein Sequence	MAKPLTDSEKRKQISVRGLAGLGDVAEVRKSFNRHLHFTLVKDRNVATPRDYFFALAHTVRDHLVGRWIRTQQHYYERDPKRIYYLSLEFYMGRTLQNTMVNLGLQNACDEAIYQLGLDLEELEEIEEDAGLGNGGLGRLAACFLDSMATLGLAAYGYGIRYEFGIFNQKIVNGWQVEEADDWLRYGNPWEKARPEYMLPVHFYGRVEHTPDGVKWLDTQVVLAMPYDTPVPGYKNNTVNTMRLWSAKAPNDFKLQDFNVGDYIEAVLDRNLAENISRVLYPNDNFFEGKELRLKQEYFVVAATLQDIIRRFKSSKFGCRDPVRTCFETFPDKVAIQLNDTHPALSIPELMRILVDVEKVDWDKAWEITKKTCAYTNHTVLPEALERWPVSMFEKLLPRHLEIIYAINQRHLDHVAALFPGDVDRLRRMSVIEEGDCKRINMAHLCVIGSHAVNGVARIHSEIVKQSVFKDFYELEPEKFQNKTNGITPRRWLLLCNPGLADTIVEKIGEEFLTDLSQLKKLLPLVSDEVFIRDVAKVKQENKLKFSAFLEKEYKVKINPSSMFDVHVKRIHEYKRQLLNCLHVVTLYNRIKRDPAKAFVPRTVMIGGKAAPGYHMAKLIIKLVTSIGDVVNHDPVVGDRLKVIFLENYRVSLAEKVIPAADLSQQISTAGTEASGTGNMKFMLNGALTIGTMDGANVEMAEEAGAENLFIFGLRVEDVEALDRKGYNAREYYDHLPELKQAVDQISSGFFSPKEPDCFKDIVNMLMHHDRFKVFADYEAYMQCQAQVDQLYRNPKEWTKKVIRNIACSGKFSSDRTITEYAREIWGVEPSDLQIPPPNIPRD

Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations	Modification	Substrate Peptides & Secondary Structure	ASA (%)	Reference
2	Acetylation	------MAKPLTDSE ------CCCCCCCHH	23.36	22814378
3	Acetylation	-----MAKPLTDSEK -----CCCCCCCHHH	38.98	23236377
3	Malonylation	-----MAKPLTDSEK -----CCCCCCCHHH	38.98	26320211
3	Ubiquitination	-----MAKPLTDSEK -----CCCCCCCHHH	38.98	24816145
6	Phosphorylation	--MAKPLTDSEKRKQ --CCCCCCCHHHHHH	46.11	29255136
8	Phosphorylation	MAKPLTDSEKRKQIS CCCCCCCHHHHHHEE	39.52	29255136
10	Ubiquitination	KPLTDSEKRKQISVR CCCCCHHHHHHEEHH	69.70	-
10	Acetylation	KPLTDSEKRKQISVR CCCCCHHHHHHEEHH	69.70	30584359
12	Ubiquitination	LTDSEKRKQISVRGL CCCHHHHHHEEHHHC	64.15	27667366
15	Phosphorylation	SEKRKQISVRGLAGL HHHHHHEEHHHCCCC	11.85	30278072
31	Phosphorylation	DVAEVRKSFNRHLHF CHHHHHHHHHCCEEE	19.72	28464451
39	Phosphorylation	FNRHLHFTLVKDRNV HHCCEEEEEECCCCC	21.64	-
42	Ubiquitination	HLHFTLVKDRNVATP CEEEEEECCCCCCCH	54.83	21906983
48	Phosphorylation	VKDRNVATPRDYFFA ECCCCCCCHHHHHHH	17.99	26437602
52	Phosphorylation	NVATPRDYFFALAHT CCCCHHHHHHHHHHH	11.24	-
75	Phosphorylation	WIRTQQHYYERDPKR HHHHCCCHHHCCCCC	11.59	25884760
76	Phosphorylation	IRTQQHYYERDPKRI HHHCCCHHHCCCCCE	11.45	25884760
84	Phosphorylation	ERDPKRIYYLSLEFY HCCCCCEEEEEEEEH	11.46	24043423
85	Phosphorylation	RDPKRIYYLSLEFYM CCCCCEEEEEEEEHH	6.35	24043423
87	Phosphorylation	PKRIYYLSLEFYMGR CCCEEEEEEEEHHCC	15.10	24043423
91	Phosphorylation	YYLSLEFYMGRTLQN EEEEEEEHHCCCHHH	6.84	24043423
162	Phosphorylation	AYGYGIRYEFGIFNQ HHHCCCEEEEEEECC	17.43	20068231
170	Ubiquitination	EFGIFNQKIVNGWQV EEEEECCEEECCEEE	50.12	-
186	Phosphorylation	EADDWLRYGNPWEKA ECCCHHHCCCHHHHC	21.05	25690035
192	Ubiquitination	RYGNPWEKARPEYML HCCCHHHHCCCCCEE	45.91	23503661
197	Phosphorylation	WEKARPEYMLPVHFY HHHCCCCCEEEEEEE	13.46	27155012
198	Sulfoxidation	EKARPEYMLPVHFYG HHCCCCCEEEEEEEE	3.04	30846556
204	Phosphorylation	YMLPVHFYGRVEHTP CEEEEEEEECCEECC	6.80	27259358
210	Phosphorylation	FYGRVEHTPDGVKWL EEECCEECCCCCEEE	15.01	-
227	Phosphorylation	QVVLAMPYDTPVPGY EEEEEECCCCCCCCC	21.26	-
229	Phosphorylation	VLAMPYDTPVPGYKN EEEECCCCCCCCCCC	21.97	-
235	Ubiquitination	DTPVPGYKNNTVNTM CCCCCCCCCCCCCCE	50.03	21906983
241	Phosphorylation	YKNNTVNTMRLWSAK CCCCCCCCEEEEECC	10.18	-
248	Ubiquitination	TMRLWSAKAPNDFKL CEEEEECCCCCCCCC	59.88	21906983
254	Ubiquitination	AKAPNDFKLQDFNVG CCCCCCCCCCCCCHH	48.37	21987572
263	Phosphorylation	QDFNVGDYIEAVLDR CCCCHHHHHHHHHCC	8.50	22817900
277	Phosphorylation	RNLAENISRVLYPND CCHHHHHHCCCCCCC	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	23749302
359	Ubiquitination	RILVDVEKVDWDKAW HHHHCHHHCCHHHHH	45.39	22817900
364	Acetylation	VEKVDWDKAWEITKK HHHCCHHHHHHHHHH	51.66	25953088
364	Ubiquitination	VEKVDWDKAWEITKK HHHCCHHHHHHHHHH	51.66	21906983
370	Ubiquitination	DKAWEITKKTCAYTN HHHHHHHHHHHCCCC	52.31	33845483
371	Ubiquitination	KAWEITKKTCAYTNH HHHHHHHHHHCCCCC	39.94	21906983
372	Phosphorylation	AWEITKKTCAYTNHT HHHHHHHHHCCCCCC	12.15	-
395	Ubiquitination	WPVSMFEKLLPRHLE CCHHHHHHHHHHHHH	44.02	23503661
405	Phosphorylation	PRHLEIIYAINQRHL HHHHHHHHHHHHHCH	13.69	28152594
430	Phosphorylation	VDRLRRMSVIEEGDC HHHHHHCCEECCCCC	20.38	29507054
438	Acetylation	VIEEGDCKRINMAHL EECCCCCCEEEECEE	62.14	25953088
438	Ubiquitination	VIEEGDCKRINMAHL EECCCCCCEEEECEE	62.14	-
465	Ubiquitination	RIHSEIVKQSVFKDF HHCHHHHHHHHCCCH	42.38	21906983
470	Ubiquitination	IVKQSVFKDFYELEP HHHHHHCCCHHHCCH	44.78	21906983
473	Phosphorylation	QSVFKDFYELEPEKF HHHCCCHHHCCHHHH	29.73	19534553
479	Ubiquitination	FYELEPEKFQNKTNG HHHCCHHHHCCCCCC	64.07	29967540
483	Ubiquitination	EPEKFQNKTNGITPR CHHHHCCCCCCCCHH	32.36	21906983
484	Phosphorylation	PEKFQNKTNGITPRR HHHHCCCCCCCCHHH	46.34	26437602
517	Phosphorylation	EEFLTDLSQLKKLLP HHHHHCHHHHHHHHH	35.96	24719451
520	Ubiquitination	LTDLSQLKKLLPLVS HHCHHHHHHHHHHCC	33.47	23000965
521	Ubiquitination	TDLSQLKKLLPLVSD HCHHHHHHHHHHCCC	64.94	23000965
527	Phosphorylation	KKLLPLVSDEVFIRD HHHHHHCCCCHHHHH	35.42	24076635
545	Ubiquitination	VKQENKLKFSAFLEK HCHHCCCCEEEHHCE	38.59	29967540
552	Ubiquitination	KFSAFLEKEYKVKIN CEEEHHCEECCCCCC	69.37	29967540
554	Phosphorylation	SAFLEKEYKVKINPS EEHHCEECCCCCCHH	31.95	-
557	Ubiquitination	LEKEYKVKINPSSMF HCEECCCCCCHHHHC	32.39	29967540
561	Phosphorylation	YKVKINPSSMFDVHV CCCCCCHHHHCEEEH	29.91	20068231
562	Phosphorylation	KVKINPSSMFDVHVK CCCCCHHHHCEEEHH	25.40	20068231
574	Phosphorylation	HVKRIHEYKRQLLNC EHHHHHHHHHHHHHH	9.41	26437602
597	Ubiquitination	RIKRDPAKAFVPRTV HHCCCHHHHCCCCEE	47.98	24816145
603	Phosphorylation	AKAFVPRTVMIGGKA HHHCCCCEEEECCEE	14.35	22210691
609	Ubiquitination	RTVMIGGKAAPGYHM CEEEECCEECCCHHH	35.84	-
614	Phosphorylation	GGKAAPGYHMAKLII CCEECCCHHHHHHHH	6.33	28348404
616	Sulfoxidation	KAAPGYHMAKLIIKL EECCCHHHHHHHHHH	2.37	30846556
642	Ubiquitination	PVVGDRLKVIFLENY CCCCCCEEEEEEECC	33.89	33845483
656	Ubiquitination	YRVSLAEKVIPAADL CCHHHHHHHCCHHHH	39.60	21906983
681	N6-(pyridoxal phosphate)lysine	ASGTGNMKFMLNGAL CCCCCCCEEEECCEE	31.46	-
681	Other	ASGTGNMKFMLNGAL CCCCCCCEEEECCEE	31.46	27402852
727	Phosphorylation	EALDRKGYNAREYYD HHHHHCCCCHHHHHH	14.53	-
732	Phosphorylation	KGYNAREYYDHLPEL CCCCHHHHHHHHHHH	14.51	-
733	Phosphorylation	GYNAREYYDHLPELK CCCHHHHHHHHHHHH	7.67	-
740	Ubiquitination	YDHLPELKQAVDQIS HHHHHHHHHHHHHHH	34.25	22817900
752	Phosphorylation	QISSGFFSPKEPDCF HHHCCCCCCCCCCHH	32.57	24719451
754	Ubiquitination	SSGFFSPKEPDCFKD HCCCCCCCCCCHHHH	79.34	29967540
796	Malonylation	DQLYRNPKEWTKKVI HHHHHCHHHHHHHHH	70.23	26320211
796	Acetylation	DQLYRNPKEWTKKVI HHHHHCHHHHHHHHH	70.23	18530339
796	Ubiquitination	DQLYRNPKEWTKKVI HHHHHCHHHHHHHHH	70.23	27667366
799	Phosphorylation	YRNPKEWTKKVIRNI HHCHHHHHHHHHHHH	23.29	29083192
809	Phosphorylation	VIRNIACSGKFSSDR HHHHHHCCCCCCCCC	35.68	29457462
811	Ubiquitination	RNIACSGKFSSDRTI HHHHCCCCCCCCCCH	26.27	33845483
811	Acetylation	RNIACSGKFSSDRTI HHHHCCCCCCCCCCH	26.27	25953088

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	PHKA1	P46020	PSP
15	S	Phosphorylation	Kinase	LMTK2	Q8IWU2	GPS
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		27402852
Phosphorylation of Ser-15 converts phosphorylase B (unphosphorylated) to phosphorylase A (By similarity).

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 PYGB_HUMAN !!

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference
FUMH_HUMAN	FH	physical	22863883
LIMD1_HUMAN	LIMD1	physical	22863883
UBA6_HUMAN	UBA6	physical	22863883
XPP1_HUMAN	XPNPEP1	physical	22863883
PYGB_HUMAN	PYGB	physical	25416956
PYGL_HUMAN	PYGL	physical	25416956
SIAH1_HUMAN	SIAH1	physical	25416956
ACLY_HUMAN	ACLY	physical	26344197
NNRE_HUMAN	APOA1BP	physical	26344197
GLGB_HUMAN	GBE1	physical	26344197
PFKAL_HUMAN	PFKL	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.

Regulatory Network of PYGB_HUMAN

Related Literatures of Post-Translational Modification

Acetylation
Reference	PubMed
"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: ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, AND MASS SPECTROMETRY.	19413330 [Abstract]
Phosphorylation
Reference	PubMed
"Large-scale proteomics analysis of the human kinome."; Oppermann F.S., Gnad F., Olsen J.V., Hornberger R., Greff Z., Keri G.,Mann M., Daub H.; Mol. Cell. Proteomics 8:1751-1764(2009). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-15, AND MASSSPECTROMETRY.	19369195 [Abstract]
"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-15, AND MASSSPECTROMETRY.	17081983 [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-197 AND TYR-473, ANDMASS SPECTROMETRY.	19534553 [Abstract]
"Global survey of phosphotyrosine signaling identifies oncogenickinases in lung cancer."; Rikova K., Guo A., Zeng Q., Possemato A., Yu J., Haack H., Nardone J.,Lee K., Reeves C., Li Y., Hu Y., Tan Z., Stokes M., Sullivan L.,Mitchell J., Wetzel R., Macneill J., Ren J.M., Yuan J.,Bakalarski C.E., Villen J., Kornhauser J.M., Smith B., Li D., Zhou X.,Gygi S.P., Gu T.-L., Polakiewicz R.D., Rush J., Comb M.J.; Cell 131:1190-1203(2007). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-76 AND TYR-197, AND MASSSPECTROMETRY.	18083107 [Abstract]

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