dbPTM

PYGB_MOUSE - PTM Information in dbPTM

Basic Information of Protein

Overview of Protein Modification Sites with Functional and Structural Information
UniProt ID	PYGB_MOUSE
UniProt AC	Q8CI94
Protein Name	Glycogen phosphorylase, brain form
Gene Name	Pygb
Organism	Mus musculus (Mouse).
Sequence Length	843
Subcellular Localization
Protein Description	Glycogen phosphorylase that regulates glycogen mobilization. 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	MAKPLTDSERQKQISVRGIAGLGDVAEVRKSFNRHLHFTLVKDRNVATPRDYFFALAHTVRDHLVGRWIRTQQHYYERDPKRIYYLSLEFYMGRTLQNTMVNLGLQTACDEATYQLGLDLEELEEIEEDAGLGNGGLGRLAACFLDSMATLGLAAYGYGIRYEFGIFNQKIVNGWQVEEADDWLRYGNPWEKARPEYMLPVHFYGRVEHTPDGVLWLDTQVVLAMPYDTPVPGYKNNTVNTMRLWSAKAPNDFKLKDFNVGDYIEAVLDRNLAENISRVLYPNDNFFEGKELRLKQEYFVVAATLQDIIRRFKSSRFGCRDPVRTCFETFPDKVAIQLNDTHPALSIPELMRILVDVEKVDWDKAWEITKKTCAYTNHTVLPEALERWPVSMFEKLLPRHLEIIYAINQRHLDHVAALFPGDVDRLRRMSVIEEGDCKRINMAHLCVIGSHAVNGVARIHSEIVKQSVFKDFYELEPEKFQNKTNGITPRRWLLLCNPGLAEIIVERIGEGFLTDLSQLKKLLSLVDDEAFIRDVAKVKQENKLKFSAQLEKEYKVKINPASMFDVHVKRIHEYKRQLLNCLHIITLYNRIKKDPAKAFVPRTVMIGGKAAPGYHMAKMIIKLVTSIGDVVNHDPVVGDRLRVIFLENYRVSLAEKVIPAADLSQQISTAGTEASGTGNMKFMLNGALTIGTMDGANVEMAEEAGEENLFIFGMRVEDVEALDQKGYNAREFYERLPELRQAVDQISSGFFSPKDPDCFKDVVNMLMYHDRFKVFADYEAYIQCQAQVDRLYRNSKEWTKKVIRNIACSGKFSSDRTITEYAREIWGVEPSDLQIPPPNLPKD

Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations	Modification	Substrate Peptides & Secondary Structure	ASA (%)	Reference
2	Acetylation	------MAKPLTDSE ------CCCCCCHHH	23.36	-
8	Phosphorylation	MAKPLTDSERQKQIS CCCCCCHHHHHHHHH	29.46	-
15	Phosphorylation	SERQKQISVRGIAGL HHHHHHHHHHCCCCC	11.85	23684622
31	Phosphorylation	DVAEVRKSFNRHLHF CHHHHHHHHHCCEEE	19.72	21454597
42	Ubiquitination	HLHFTLVKDRNVATP CEEEEEECCCCCCCH	54.83	-
143	S-nitrosocysteine	GLGRLAACFLDSMAT HHHHHHHHHHHHHHH	2.64	-
143	S-nitrosylation	GLGRLAACFLDSMAT HHHHHHHHHHHHHHH	2.64	21278135
156	Phosphorylation	ATLGLAAYGYGIRYE HHHHHHHHHCCCEEE	12.79	-
186	Phosphorylation	EADDWLRYGNPWEKA ECCCHHHCCCHHHHC	21.05	28542873
197	Phosphorylation	WEKARPEYMLPVHFY HHHCCCCCEEEEEEE	13.46	22817900
204	Phosphorylation	YMLPVHFYGRVEHTP CEEEEEEEECCEECC	6.80	22817900
219	Phosphorylation	DGVLWLDTQVVLAMP CCEEEEEEEEEEECC	22.54	-
229	Phosphorylation	VLAMPYDTPVPGYKN EEECCCCCCCCCCCC	21.97	-
234	Phosphorylation	YDTPVPGYKNNTVNT CCCCCCCCCCCCCCC	12.41	-
277	Phosphorylation	RNLAENISRVLYPND CHHHHHHHCCCCCCC	28.11	20531401
290	Malonylation	NDNFFEGKELRLKQE CCCCCCCCCCCCCCE	46.51	26320211
290	Acetylation	NDNFFEGKELRLKQE CCCCCCCCCCCCCCE	46.51	38026401
290	Ubiquitination	NDNFFEGKELRLKQE CCCCCCCCCCCCCCE	46.51	27667366
359	Ubiquitination	RILVDVEKVDWDKAW HHHHCHHHCCHHHHH	45.39	-
364	Acetylation	VEKVDWDKAWEITKK HHHCCHHHHHHHHHH	51.66	23954790
364	Ubiquitination	VEKVDWDKAWEITKK HHHCCHHHHHHHHHH	51.66	-
370	Malonylation	DKAWEITKKTCAYTN HHHHHHHHHHHCCCC	52.31	26320211
370	Ubiquitination	DKAWEITKKTCAYTN HHHHHHHHHHHCCCC	52.31	27667366
373	S-nitrosylation	WEITKKTCAYTNHTV HHHHHHHHCCCCCCC	3.61	21278135
373	S-nitrosocysteine	WEITKKTCAYTNHTV HHHHHHHHCCCCCCC	3.61	-
405	Phosphorylation	PRHLEIIYAINQRHL HHHHHHHHHHHHHCH	13.69	22817900
430	Phosphorylation	VDRLRRMSVIEEGDC HHHHHHCCEECCCCC	20.38	-
437	S-nitrosocysteine	SVIEEGDCKRINMAH CEECCCCCCEEEECE	4.73	-
437	S-nitrosylation	SVIEEGDCKRINMAH CEECCCCCCEEEECE	4.73	19101475
446	S-nitrosocysteine	RINMAHLCVIGSHAV EEEECEEEEECHHHH	1.18	-
446	S-palmitoylation	RINMAHLCVIGSHAV EEEECEEEEECHHHH	1.18	28680068
446	S-nitrosylation	RINMAHLCVIGSHAV EEEECEEEEECHHHH	1.18	21278135
473	Phosphorylation	QSVFKDFYELEPEKF HHHCCCHHHCCHHHH	29.73	25521595
483	Ubiquitination	EPEKFQNKTNGITPR CHHHHCCCCCCCCHH	32.36	27667366
514	Phosphorylation	RIGEGFLTDLSQLKK HHCCCCCCCHHHHHH	32.41	25338131
517	Phosphorylation	EGFLTDLSQLKKLLS CCCCCCHHHHHHHHH	35.96	25338131
521	Ubiquitination	TDLSQLKKLLSLVDD CCHHHHHHHHHHCCH	64.35	-
524	Phosphorylation	SQLKKLLSLVDDEAF HHHHHHHHHCCHHHH	36.46	27180971
555	Malonylation	AQLEKEYKVKINPAS EECCHHHCCCCCHHH	37.84	26073543
562	Phosphorylation	KVKINPASMFDVHVK CCCCCHHHHCEEEHH	22.65	23140645
574	Phosphorylation	HVKRIHEYKRQLLNC EHHHHHHHHHHHHHH	9.41	29899451
575	Acetylation	VKRIHEYKRQLLNCL HHHHHHHHHHHHHHH	30.59	15618471
597	Malonylation	RIKKDPAKAFVPRTV HHCCCHHHHCCCCEE	47.98	26320211
614	Phosphorylation	GGKAAPGYHMAKMII CCEECCCHHHHHHHH	6.33	28464351
618	Ubiquitination	APGYHMAKMIIKLVT CCCHHHHHHHHHHHH	24.05	-
681	N6-(pyridoxal phosphate)lysine	ASGTGNMKFMLNGAL CCCCCCCEEEECCEE	31.46	-
681	Other	ASGTGNMKFMLNGAL CCCCCCCEEEECCEE	31.46	-
725	Ubiquitination	DVEALDQKGYNAREF HHHHHHHCCCCHHHH	64.13	27667366
758	S-nitrosocysteine	FSPKDPDCFKDVVNM CCCCCCCHHHHHHHH	5.78	-
758	S-nitrosylation	FSPKDPDCFKDVVNM CCCCCCCHHHHHHHH	5.78	21278135
808	S-nitrosocysteine	KVIRNIACSGKFSSD HHHHHHHCCCCCCCC	4.95	-
808	S-nitrosylation	KVIRNIACSGKFSSD HHHHHHHCCCCCCCC	4.95	21278135
811	Acetylation	RNIACSGKFSSDRTI HHHHCCCCCCCCCCH	26.27	22826441

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	-	Uniprot

Functions of PTM Sites

Modified Location	Modified Residue	Modification	Function	Reference
15	S	Phosphorylation		-
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 PYGB_MOUSE !!

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference	Domain-Domain Interactions
Oops, there are no PPI records of PYGB_MOUSE !!

Drug and Disease Associations

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

Regulatory Network of PYGB_MOUSE

Related Literatures of Post-Translational Modification

Phosphorylation
Reference	PubMed
"Large-scale identification and evolution indexing of tyrosinephosphorylation sites from murine brain."; Ballif B.A., Carey G.R., Sunyaev S.R., Gygi S.P.; J. Proteome Res. 7:311-318(2008). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-197 AND TYR-473, ANDMASS SPECTROMETRY.	18034455 [Abstract]

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