UniProt Accession

 PYGB_HUMAN; P11216; Q96AK1; Q9NPX8 

Genbank Protein ID

 J03544; U47025; AL121772; BC017045; BC030795 

Genbank Nucleotide ID

 AAA59597.1; AAB60395.1; CAC00661.1; AAH17045.1; AAH30795.1 

Protein Name

 Glycogen phosphorylase, brain form 

Protein Synonyms/Alias

  

Gene Name

 PYGB 

Gene Synonyms/Alias

  

Created Date

 July 27, 2013 

Organism

 Homo sapiens (Human) 

NCBI Taxa ID

 9606 

Lysine Modification

Position	Peptide	Type	References
3	*****MAKPLTDSEK	acetylation	[1]
3	*****MAKPLTDSEK	ubiquitination	[2]
10	KPLTDSEKRKQISVR	ubiquitination	[2]
42	HLHFTLVKDRNVATP	ubiquitination	[3]
170	EFGIFNQKIVNGWQV	ubiquitination	[3]
192	RYGNPWEKARPEYML	ubiquitination	[2, 4]
235	DTPVPGYKNNTVNTM	ubiquitination	[3, 4]
248	TMRLWSAKAPNDFKL	ubiquitination	[2, 3, 4]
254	AKAPNDFKLQDFNVG	ubiquitination	[4, 5]
290	NDNFFEGKELRLKQE	ubiquitination	[2, 3]
316	IRRFKSSKFGCRDPV	acetylation	[6, 7]
359	RILVDVEKVDWDKAW	ubiquitination	[8]
364	VEKVDWDKAWEITKK	ubiquitination	[3, 8]
370	DKAWEITKKTCAYTN	ubiquitination	[8]
371	KAWEITKKTCAYTNH	ubiquitination	[2, 7, 9]
395	WPVSMFEKLLPRHLE	ubiquitination	[2, 4]
438	VIEEGDCKRINMAHL	ubiquitination	[2, 7]
465	RIHSEIVKQSVFKDF	ubiquitination	[3, 4]
470	IVKQSVFKDFYELEP	ubiquitination	[3, 4]
479	FYELEPEKFQNKTNG	ubiquitination	[3]
483	EPEKFQNKTNGITPR	ubiquitination	[3, 9]
520	LTDLSQLKKLLPLVS	ubiquitination	[2, 3, 4, 7, 10]
521	TDLSQLKKLLPLVSD	ubiquitination	[9]
642	PVVGDRLKVIFLENY	ubiquitination	[2]
656	YRVSLAEKVIPAADL	ubiquitination	[3, 4]
740	YDHLPELKQAVDQIS	ubiquitination	[3]

Reference

 [1] Proteomic investigations of lysine acetylation identify diverse substrates of mitochondrial deacetylase sirt3.
 Sol EM, Wagner SA, Weinert BT, Kumar A, Kim HS, Deng CX, Choudhary C.
 PLoS One. 2012;7(12):e50545. [PMID: 23236377]
 [2] Refined preparation and use of anti-diglycine remnant (K-ε-GG) antibody enables routine quantification of 10,000s of ubiquitination sites in single proteomics experiments.
 Udeshi ND, Svinkina T, Mertins P, Kuhn E, Mani DR, Qiao JW, Carr SA.
 Mol Cell Proteomics. 2013 Mar;12(3):825-31. [PMID: 23266961]
 [3] Systematic and quantitative assessment of the ubiquitin-modified proteome.
 Kim W, Bennett EJ, Huttlin EL, Guo A, Li J, Possemato A, Sowa ME, Rad R, Rush J, Comb MJ, Harper JW, Gygi SP.
 Mol Cell. 2011 Oct 21;44(2):325-40. [PMID: 21906983]
 [4] Landscape of the PARKIN-dependent ubiquitylome in response to mitochondrial depolarization.
 Sarraf SA, Raman M, Guarani-Pereira V, Sowa ME, Huttlin EL, Gygi SP, Harper JW.
 Nature. 2013 Apr 18;496(7445):372-6. [PMID: 23503661]
 [5] Ubiquitin ligase substrate identification through quantitative proteomics at both the protein and peptide levels.
 Lee KA, Hammerle LP, Andrews PS, Stokes MP, Mustelin T, Silva JC, Black RA, Doedens JR.
 J Biol Chem. 2011 Dec 2;286(48):41530-8. [PMID: 21987572]
 [6] Lysine acetylation targets protein complexes and co-regulates major cellular functions.
 Choudhary C, Kumar C, Gnad F, Nielsen ML, Rehman M, Walther TC, Olsen JV, Mann M.
 Science. 2009 Aug 14;325(5942):834-40. [PMID: 19608861]
 [7] Integrated proteomic analysis of post-translational modifications by serial enrichment.
 Mertins P, Qiao JW, Patel J, Udeshi ND, Clauser KR, Mani DR, Burgess MW, Gillette MA, Jaffe JD, Carr SA.
 Nat Methods. 2013 Jul;10(7):634-7. [PMID: 23749302]
 [8] Proteomic analyses reveal divergent ubiquitylation site patterns in murine tissues.
 Wagner SA, Beli P, Weinert BT, Schölz C, Kelstrup CD, Young C, Nielsen ML, Olsen JV, Brakebusch C, Choudhary C.
 Mol Cell Proteomics. 2012 Dec;11(12):1578-85. [PMID: 22790023]
 [9] A proteome-wide, quantitative survey of in vivo ubiquitylation sites reveals widespread regulatory roles.
 Wagner SA, Beli P, Weinert BT, Nielsen ML, Cox J, Mann M, Choudhary C.
 Mol Cell Proteomics. 2011 Oct;10(10):M111.013284. [PMID: 21890473]
 [10] Methods for quantification of in vivo changes in protein ubiquitination following proteasome and deubiquitinase inhibition.
 Udeshi ND, Mani DR, Eisenhaure T, Mertins P, Jaffe JD, Clauser KR, Hacohen N, Carr SA.
 Mol Cell Proteomics. 2012 May;11(5):148-59. [PMID: 22505724] 

Functional 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. 

Sequence Annotation

 BINDING 76 76 AMP (By similarity).
 MOD_RES 2 2 N-acetylalanine.
 MOD_RES 15 15 Phosphoserine; by PHK; in form
 MOD_RES 197 197 Phosphotyrosine (By similarity).
 MOD_RES 473 473 Phosphotyrosine (By similarity).
 MOD_RES 681 681 N6-(pyridoxal phosphate)lysine (By  

Keyword

 Acetylation; Allosteric enzyme; Carbohydrate metabolism; Complete proteome; Direct protein sequencing; Glycogen metabolism; Glycosyltransferase; Phosphoprotein; Polymorphism; Pyridoxal phosphate; Reference proteome; Transferase. 

Sequence Source

 UniProt (SWISSPROT/TrEMBL); GenBank; EMBL 

Protein Length

 843 AA 

Protein Sequence

Gene Ontology

 GO:0005737; C:cytoplasm; IDA:UniProtKB.
 GO:0008184; F:glycogen phosphorylase activity; NAS:UniProtKB.
 GO:0030170; F:pyridoxal phosphate binding; IEA:InterPro.
 GO:0006006; P:glucose metabolic process; TAS:Reactome.
 GO:0005980; P:glycogen catabolic process; NAS:UniProtKB.
 GO:0044281; P:small molecule metabolic process; TAS:Reactome. 

Interpro

 IPR011833; Glycg_phsphrylas.
 IPR000811; Glyco_trans_35. 

Pfam

 PF00343; Phosphorylase 

SMART

  

PROSITE

 PS00102; PHOSPHORYLASE 

PRINTS