Q9ET01 (PYGL_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Glycogen phosphorylase, liver form
EC=2.4.1.1

Gene names

Name:

Pygl

Organism

Mus musculus (Mouse) [Reference proteome]

Taxonomic identifier

10090 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Opisthokonta › Metazoa › Eumetazoa › Bilateria › Deuterostomia › Chordata › Craniata › Vertebrata › Gnathostomata › Teleostomi › Euteleostomi › Sarcopterygii › Tetrapoda › Amniota › Mammalia › Theria › Eutheria › Euarchontoglires › Glires › Rodentia › Sciurognathi › Muroidea › Muridae › Murinae › Mus › Mus

Protein attributes

Sequence length	850 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Evidence at protein level

General annotation (Comments)

Function	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 By similarity.
Catalytic activity	(1,4-alpha-D-glucosyl)(n) + phosphate = (1,4-alpha-D-glucosyl)(n-1) + alpha-D-glucose 1-phosphate.
Cofactor	Pyridoxal phosphate By similarity.
Enzyme regulation	Activity of phosphorylase is controlled both by allosteric means (through the noncovalent binding of metabolites) and by covalent modification. Thus AMP allosterically activates, whereas ATP, ADP, and glucose-6-phosphate allosterically inhibit, phosphorylase B By similarity.
Subunit structure	Homodimer. Dimers associate into a tetramer to form the enzymatically active phosphorylase A. Interacts with PPP1R3B By similarity.
Post-translational modification	Phosphorylation of Ser-15 converts phosphorylase B (unphosphorylated) to phosphorylase A By similarity.
Sequence similarities	Belongs to the glycogen phosphorylase family.

Ontologies

Keywords
Biological process	Carbohydrate metabolism Glycogen metabolism
Ligand	Nucleotide-binding Pyridoxal phosphate
Molecular function	Glycosyltransferase Transferase
PTM	Acetylation Phosphoprotein
Technical term	Allosteric enzyme Complete proteome Direct protein sequencing Reference proteome
Gene Ontology (GO)
Biological_process	5-phosphoribose 1-diphosphate biosynthetic process Inferred from electronic annotation. Source: Compara glucose homeostasis Inferred from electronic annotation. Source: Compara glycogen catabolic process Inferred from electronic annotation. Source: Compara glycogen metabolic process Inferred from direct assay PubMed 11960689. Source: MGI
Cellular_component	cytoplasm Inferred from electronic annotation. Source: Compara plasma membrane Inferred from electronic annotation. Source: Compara
Molecular_function	AMP binding Inferred from electronic annotation. Source: Compara ATP binding Inferred from electronic annotation. Source: Compara bile acid binding Inferred from electronic annotation. Source: Compara carbohydrate binding Inferred from electronic annotation. Source: Compara drug binding Inferred from electronic annotation. Source: Compara glycogen phosphorylase activity Inferred from direct assay PubMed 11960689. Source: MGI purine nucleobase binding Inferred from electronic annotation. Source: Compara pyridoxal phosphate binding Inferred from electronic annotation. Source: InterPro vitamin binding Inferred from electronic annotation. Source: Compara
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Initiator methionine	1	1	Removed Ref.3
	Chain	2 – 850	849	Glycogen phosphorylase, liver form		PRO_0000188525
Sites
	Binding site	76	1	AMP By similarity
	Site	109	1	Involved in the association of subunits By similarity
	Site	143	1	Involved in the association of subunits By similarity
	Site	156	1	May be involved in allosteric control By similarity
Amino acid modifications
	Modified residue	2	1	N-acetylalanine Ref.3
	Modified residue	15	1	Phosphoserine; by PHK; in form phosphorylase A By similarity
	Modified residue	527	1	Phosphoserine Ref.4
	Modified residue	681	1	N6-(pyridoxal phosphate)lysine By similarity
Experimental info
	Sequence conflict	198	1	M → V in AAG00588. Ref.1

Sequences

	Sequence		Length	Mass (Da)
	Q9ET01 [UniParc]. Last modified July 27, 2011. Version 4. Checksum: C4BFF6A9AA4E181E	FASTA	850	97,463
	10 20 30 40 50 60 MAKPLTDQEK RRQISIRGIV GVENVAELKK GFNRHLHFTL VKDRNVATPR DYYFALAHTV 70 80 90 100 110 120 RDHLVGRWIR TQQHYYDKCP KRVYYLSLEF YMGRTLQNTM INLGLQNACD EAIYQLGLDM 130 140 150 160 170 180 EELEEIEEDA GLGNGGLGRL AACFLDSMAT LGLAAYGYGI RYEYGIFNQK IREGWQVEEA 190 200 210 220 230 240 DDWLRHGNPW EKARPEFMLP VHFYGRVEHT QTGTKWVDTQ VVLALPYDTP VPGYMNNTVN 250 260 270 280 290 300 TMRLWSARAP NDFNLQDFNV GDYIQAVLDR NLAENISRVL YPNDNFFEGK ELRLKQEYFV 310 320 330 340 350 360 VAATLQDVIR RFKASKFGSK DGMGTVFDAF PDQVAIQLND THPALAIPEL MRIFVDIEKL 370 380 390 400 410 420 PWAKAWEITK KTFAYTNHTV LPEALERWPV ELVEKLLPRH LEIIYEINQK HLDRIVALFP 430 440 450 460 470 480 KDISRMRRMS LIEEEGGKRI NMAHLCIVGC HAVNGVAKIH SDIVKTQVFK DFSELEPDKF 490 500 510 520 530 540 QNKTNGITPR RWLLLCNPGL ADLIAEKIGE DYVKDLSQLT KLHSFVSDDI FLREIAKVKQ 550 560 570 580 590 600 ENKLKFSQFL EKEYKVKINP SSMFDVHVKR IHEYKRQLLN CLHVITMYNR IKKDPKKFFV 610 620 630 640 650 660 PRTVIIGGKA APGYHMAKMI IKLITSVAEV VNNDPMVGSK LKVIFLENYR VSLAEKVIPA 670 680 690 700 710 720 TDLSEQISTA GTEASGTGNM KFMLNGALTI GTMDGANVEM AEEAGEENLF IFGMRVDDVA 730 740 750 760 770 780 ALDKKGYEAK EYYEALPELK LVIDQIDNGF FSPNQPDLFK DIINMLFYHD RFKVFADYEA 790 800 810 820 830 840 YVKCQEKVSQ LYMNQKAWNT MVLKNIAASG KFSSDRTIKE YAKDIWNMEP SDLKISLSNE 850 SSNGVSANGK

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Expression and regulation of glycogen phosphorylase in 3T3-L1 adipocytes." McInerney M.M., Hurt C.B., Laipis P.J., Frost S.C. Submitted (JUL-2000) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [MRNA]. Strain: BTBR T+ tf/J. Tissue: Liver.
[2]	"The transcriptional landscape of the mammalian genome." Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J. , Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y. Science 309:1559-1563(2005) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. Strain: C57BL/6J. Tissue: Adipose tissue and Placenta.
[3]	Kanor S., Bienvenut W.V. Submitted (OCT-2005) to UniProtKB Cited for: PROTEIN SEQUENCE OF 2-10; 162-170; 173-185; 279-290; 353-359; 388-395; 492-507 AND 643-650, CLEAVAGE OF INITIATOR METHIONINE, ACETYLATION AT ALA-2, MASS SPECTROMETRY. Strain: C57BL/6. Tissue: Liver.
[4]	"Large-scale phosphorylation analysis of mouse liver." Villen J., Beausoleil S.A., Gerber S.A., Gygi S.P. Proc. Natl. Acad. Sci. U.S.A. 104:1488-1493(2007) [PubMed] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-527, MASS SPECTROMETRY. Tissue: Liver.
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBL GenBank DDBJ	AF288783 mRNA. Translation: AAG00588.1. AK140321 mRNA. Translation: BAE24332.1. AK145989 mRNA. Translation: BAE26811.1.
IPI	IPI00319525.
RefSeq	NP_573461.2. NM_133198.2.
UniGene	Mm.256926. Mm.447796.
3D structure databases
ProteinModelPortal	Q9ET01.
SMR	Q9ET01. Positions 6-839.
ModBase	Search...
Protein-protein interaction databases
IntAct	Q9ET01. 2 interactions.
Protein family/group databases
CAZy	GT35. Glycosyltransferase Family 35.
PTM databases
PhosphoSite	Q9ET01.
Proteomic databases
PaxDb	Q9ET01.
PRIDE	Q9ET01.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
Ensembl	ENSMUST00000071250; ENSMUSP00000071231; ENSMUSG00000021069.
GeneID	110095.
KEGG	mmu:110095.
Organism-specific databases
CTD	5836.
MGI	MGI:97829. Pygl.
Phylogenomic databases
eggNOG	COG0058.
GeneTree	ENSGT00390000016886.
HOGENOM	HOG000278444.
HOVERGEN	HBG006848.
InParanoid	Q3UKJ0.
KO	K00688.
OMA	IVDVKLF.
OrthoDB	EOG4S1T6F.
Gene expression databases
ArrayExpress	Q9ET01.
Bgee	Q9ET01.
CleanEx	MM_PYGL.
Genevestigator	Q9ET01.
GermOnline	ENSMUSG00000021069. Mus musculus.
Family and domain databases
InterPro	IPR011833. Glycg_phsphrylas. IPR000811. Glyco_trans_35. [Graphical view]
PANTHER	PTHR11468. PTHR11468. 1 hit.
Pfam	PF00343. Phosphorylase. 1 hit. [Graphical view]
PIRSF	PIRSF000460. Pprylas_GlgP. 1 hit.
TIGRFAMs	TIGR02093. P_ylase. 1 hit.
PROSITE	PS00102. PHOSPHORYLASE. 1 hit. [Graphical view]
ProtoNet	Search...
Other
BindingDB	Q9ET01.
ChEMBL	CHEMBL3008.
NextBio	363317.
SOURCE	Search...

Entry information

Entry name

PYGL_MOUSE

Accession

Primary (citable) accession number: Q9ET01
Secondary accession number(s): Q3UKJ0

Entry history

Integrated into UniProtKB/Swiss-Prot:	April 16, 2002
Last sequence update:	July 27, 2011
Last modified:	April 3, 2013
This is version 108 of the entry and version 4 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program