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Glycogen phosphorylase, muscle form (EC 2.4.1.1) (Myophosphorylase)

 PYGM_RABIT              Reviewed;         843 AA.
P00489;
21-JUL-1986, integrated into UniProtKB/Swiss-Prot.
23-JAN-2007, sequence version 3.
20-DEC-2017, entry version 168.
RecName: Full=Glycogen phosphorylase, muscle form;
EC=2.4.1.1;
AltName: Full=Myophosphorylase;
Name=PYGM;
Oryctolagus cuniculus (Rabbit).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Glires; Lagomorpha; Leporidae;
Oryctolagus.
NCBI_TaxID=9986;
[1]
NUCLEOTIDE SEQUENCE [MRNA], AND ACETYLATION AT SER-2.
PubMed=3015680; DOI=10.1016/0014-5793(86)80829-8;
Nakano K., Hwang P.K., Fletterick R.J.;
"Complete cDNA sequence for rabbit muscle glycogen phosphorylase.";
FEBS Lett. 204:283-287(1986).
[2]
PROTEIN SEQUENCE OF 2-351.
PubMed=728424; DOI=10.1021/bi00619a012;
Koide A., Titani K., Ericsson L.H., Kumar S., Neurath H., Walsh K.A.;
"Sequence of the amino-terminal 349 residues of rabbit muscle glycogen
phosphorylase including the sites of covalent and allosteric
control.";
Biochemistry 17:5657-5672(1978).
[3]
PROTEIN SEQUENCE OF 352-429 AND 443-605.
PubMed=728425; DOI=10.1021/bi00619a013;
Hermann J., Titani K., Ericsson L.H., Wade R.D., Neurath H.,
Walsh K.A.;
"Amino acid sequence of two cyanogen bromide fragments of glycogen
phosphorylase.";
Biochemistry 17:5672-5679(1978).
[4]
PROTEIN SEQUENCE OF 352-843.
PubMed=728426; DOI=10.1021/bi00619a014;
Titani K., Koide A., Ericsson L.H., Kumar S., Hermann J., Wade R.D.,
Walsh K.A., Neurath H., Fischer E.H.;
"Sequence of the carboxyl-terminal 492 residues of rabbit muscle
glycogen phosphorylase including the pyridoxal 5'-phosphate binding
site.";
Biochemistry 17:5680-5693(1978).
[5]
PROTEIN SEQUENCE OF 71-81.
PubMed=670209;
Lee Y.M., Benisek W.F.;
"Inactivation of phosphorylase b by potassium ferrate. Identification
of a tyrosine residue involved in the binding of adenosine 5'-
monophosphate.";
J. Biol. Chem. 253:5460-5463(1978).
[6]
NUCLEOTIDE SEQUENCE [MRNA] OF 575-843.
PubMed=3840433; DOI=10.1111/j.1432-1033.1985.tb09193.x;
Hwang P.K., See Y.P., Vincentini A.M., Powers M.A., Fletterick R.J.,
Crerar M.M.;
"Comparative sequence analysis of rat, rabbit, and human muscle
glycogen phosphorylase cDNAs.";
Eur. J. Biochem. 152:267-274(1985).
[7]
X-RAY CRYSTALLOGRAPHY (2.5 ANGSTROMS) OF PHOSPHORYLASE A.
PubMed=728427;
Sprang S.R., Fletterick R.J.;
"Crystallographic analysis of phosphorylase alpha at 2.5-A resolution,
a comment on the chemical sequence.";
Biochemistry 17:5693-5694(1978).
[8]
X-RAY CRYSTALLOGRAPHY (2.8 ANGSTROMS) OF PHOSPHORYLASE A.
PubMed=2756432; DOI=10.1126/science.2756432;
Goldsmith E.J., Sprang S.R., Hamlin R., Xuong N.-H., Fletterick R.J.;
"Domain separation in the activation of glycogen phosphorylase a.";
Science 245:528-532(1989).
[9]
X-RAY CRYSTALLOGRAPHY (2.5 ANGSTROMS) OF PHOSPHORYLASE A WITH AMP.
PubMed=3616621; DOI=10.1126/science.3616621;
Sprang S.R., Goldsmith E.J., Fletterick R.J.;
"Structure of the nucleotide activation switch in glycogen
phosphorylase a.";
Science 237:1012-1019(1987).
[10]
X-RAY CRYSTALLOGRAPHY (3.0 ANGSTROMS) OF PHOSPHORYLASE B.
PubMed=728428;
Jenkins J.A., Johnson L.N., Wilson K.S.;
"Assignment of the amino acid sequence to the crystal structure of
glycogen phosphorylase b.";
Biochemistry 17:5694-5695(1978).
[11]
X-RAY CRYSTALLOGRAPHY (2.3 ANGSTROMS) OF PHOSPHORYLASE B.
PubMed=7500360; DOI=10.1006/jmbi.1995.0665;
Oikonomakos N.G., Zographos S.E., Johnson L.N., Papageorgiou A.C.,
Acharya K.R.;
"The binding of 2-deoxy-D-glucose 6-phosphate to glycogen
phosphorylase b: kinetic and crystallographic studies.";
J. Mol. Biol. 254:900-917(1995).
[12]
X-RAY CRYSTALLOGRAPHY (2.4 ANGSTROMS) OF PHOSPHORYLASE B.
PubMed=8976550; DOI=10.1002/pro.5560051204;
Oikonomakos N.G., Zographos S.E., Tsitsanou K.E., Johnson L.N.,
Acharya K.R.;
"Activator anion binding site in pyridoxal phosphorylase b: the
binding of phosphite, phosphate, and fluorophosphate in the crystal.";
Protein Sci. 5:2416-2428(1996).
[13]
X-RAY CRYSTALLOGRAPHY (1.99 ANGSTROMS) OF PHOSPHORYLASE B.
PubMed=9568898; DOI=10.1002/pro.5560070409;
Gregoriou M., Noble M.E.M., Watson K.A., Garman E.F., Krulle T.M.,
de la Fuente C., Fleet G.W., Oikonomakos N.G., Johnson L.N.;
"The structure of a glycogen phosphorylase glucopyranose
spirohydantoin complex at 1.8-A resolution and 100 K: the role of the
water structure and its contribution to binding.";
Protein Sci. 7:915-927(1998).
-!- 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.
-!- CATALYTIC ACTIVITY: ((1->4)-alpha-D-glucosyl)(n) + phosphate =
((1->4)-alpha-D-glucosyl)(n-1) + alpha-D-glucose 1-phosphate.
-!- COFACTOR:
Name=pyridoxal 5'-phosphate; Xref=ChEBI:CHEBI:597326;
-!- 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.
-!- SUBUNIT: Homodimer. Dimers associate into a tetramer to form the
enzymatically active phosphorylase A.
-!- PTM: Phosphorylation of Ser-15 converts phosphorylase B
(unphosphorylated) to phosphorylase A.
-!- SIMILARITY: Belongs to the glycogen phosphorylase family.
{ECO:0000305}.
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EMBL; D00040; BAA00027.1; -; mRNA.
EMBL; X04265; CAA27816.1; -; mRNA.
EMBL; X03030; CAA26833.1; -; mRNA.
PIR; A24302; PHRBG.
RefSeq; NP_001075653.1; NM_001082184.1.
UniGene; Ocu.2087; -.
PDB; 1A8I; X-ray; 1.78 A; A=2-843.
PDB; 1ABB; X-ray; 2.80 A; A/B/C/D=11-838.
PDB; 1AXR; X-ray; 2.30 A; A=2-843.
PDB; 1B4D; X-ray; 2.00 A; A=2-843.
PDB; 1BX3; X-ray; 2.30 A; A=2-843.
PDB; 1C50; X-ray; 2.30 A; A=14-843.
PDB; 1C8K; X-ray; 1.76 A; A=2-843.
PDB; 1C8L; X-ray; 2.30 A; A=2-843.
PDB; 1E1Y; X-ray; 2.23 A; A=2-843.
PDB; 1FS4; X-ray; 2.38 A; A=2-843.
PDB; 1FTQ; X-ray; 2.35 A; A=2-843.
PDB; 1FTW; X-ray; 2.36 A; A=2-843.
PDB; 1FTY; X-ray; 2.38 A; A=2-843.
PDB; 1FU4; X-ray; 2.36 A; A=2-843.
PDB; 1FU7; X-ray; 2.36 A; A=2-843.
PDB; 1FU8; X-ray; 2.35 A; A=2-843.
PDB; 1GFZ; X-ray; 2.30 A; A=2-843.
PDB; 1GG8; X-ray; 2.31 A; A=2-843.
PDB; 1GGN; X-ray; 2.36 A; A=2-843.
PDB; 1GPA; X-ray; 2.90 A; A/B/C/D=2-843.
PDB; 1GPB; X-ray; 1.90 A; A=2-843.
PDB; 1GPY; X-ray; 2.40 A; A=2-843.
PDB; 1H5U; X-ray; 1.76 A; A=2-843.
PDB; 1HLF; X-ray; 2.26 A; A=2-843.
PDB; 1K06; X-ray; 1.80 A; A=2-843.
PDB; 1K08; X-ray; 2.26 A; A=2-843.
PDB; 1KTI; X-ray; 1.97 A; A=2-843.
PDB; 1LWN; X-ray; 2.00 A; A=2-843.
PDB; 1LWO; X-ray; 2.00 A; A=2-843.
PDB; 1NOI; X-ray; 2.50 A; A/B/C/D=2-843.
PDB; 1NOJ; X-ray; 2.40 A; A=2-843.
PDB; 1NOK; X-ray; 2.40 A; A=2-843.
PDB; 1P29; X-ray; 2.20 A; A=2-843.
PDB; 1P2B; X-ray; 2.20 A; A=2-843.
PDB; 1P2D; X-ray; 1.94 A; A=2-843.
PDB; 1P2G; X-ray; 2.30 A; A=2-843.
PDB; 1P4G; X-ray; 2.10 A; A=2-843.
PDB; 1P4H; X-ray; 2.06 A; A=2-843.
PDB; 1P4J; X-ray; 2.00 A; A=2-843.
PDB; 1PYG; X-ray; 2.87 A; A/B/C/D=2-843.
PDB; 1UZU; X-ray; 2.30 A; A=2-843.
PDB; 1WUT; X-ray; 2.26 A; A=2-843.
PDB; 1WUY; X-ray; 2.26 A; A=2-843.
PDB; 1WV0; X-ray; 2.26 A; A=2-843.
PDB; 1WV1; X-ray; 2.26 A; A=2-843.
PDB; 1WW2; X-ray; 1.90 A; A=2-843.
PDB; 1WW3; X-ray; 1.80 A; A=2-843.
PDB; 1XC7; X-ray; 1.83 A; A=2-843.
PDB; 1XKX; X-ray; 1.93 A; A=2-843.
PDB; 1XL0; X-ray; 1.92 A; A=2-843.
PDB; 1XL1; X-ray; 2.10 A; A=2-843.
PDB; 1Z62; X-ray; 1.90 A; A=2-843.
PDB; 1Z6P; X-ray; 2.40 A; A=2-843.
PDB; 1Z6Q; X-ray; 2.03 A; A=2-843.
PDB; 2AMV; X-ray; 2.30 A; A=2-843.
PDB; 2F3P; X-ray; 1.94 A; A=2-843.
PDB; 2F3Q; X-ray; 1.96 A; A=2-843.
PDB; 2F3S; X-ray; 1.96 A; A=2-843.
PDB; 2F3U; X-ray; 1.93 A; A=2-843.
PDB; 2FET; X-ray; 2.03 A; A=2-843.
PDB; 2FF5; X-ray; 2.03 A; A=2-843.
PDB; 2FFR; X-ray; 2.03 A; A=13-837.
PDB; 2G9Q; X-ray; 2.50 A; A=2-843.
PDB; 2G9R; X-ray; 2.07 A; A=2-843.
PDB; 2G9U; X-ray; 2.15 A; A=2-843.
PDB; 2G9V; X-ray; 2.15 A; A=2-843.
PDB; 2GJ4; X-ray; 1.60 A; A=13-836.
PDB; 2GM9; X-ray; 2.30 A; A=13-837.
PDB; 2GPA; X-ray; 2.00 A; A=2-843.
PDB; 2GPB; X-ray; 2.30 A; A=2-843.
PDB; 2GPN; X-ray; 1.99 A; A=2-843.
PDB; 2IEG; X-ray; 1.90 A; A/B=2-843.
PDB; 2IEI; X-ray; 1.91 A; A/B=2-843.
PDB; 2OFF; X-ray; 2.20 A; A=2-843.
PDB; 2PRI; X-ray; 2.30 A; A=2-843.
PDB; 2PRJ; X-ray; 2.30 A; A=2-843.
PDB; 2PYD; X-ray; 1.93 A; A=1-843.
PDB; 2PYI; X-ray; 1.88 A; A=1-843.
PDB; 2QLM; X-ray; 2.10 A; A=2-843.
PDB; 2QLN; X-ray; 2.15 A; A=2-843.
PDB; 2QN1; X-ray; 2.40 A; A=2-843.
PDB; 2QN2; X-ray; 2.70 A; A=2-843.
PDB; 2QN3; X-ray; 1.96 A; A=2-843.
PDB; 2QN7; X-ray; 1.83 A; A=2-843.
PDB; 2QN8; X-ray; 1.90 A; A=2-843.
PDB; 2QN9; X-ray; 2.00 A; A=2-843.
PDB; 2QNB; X-ray; 1.80 A; A=2-843.
PDB; 2QRG; X-ray; 1.85 A; A=2-843.
PDB; 2QRH; X-ray; 1.83 A; A=2-843.
PDB; 2QRM; X-ray; 1.90 A; A=2-843.
PDB; 2QRP; X-ray; 1.86 A; A=2-843.
PDB; 2QRQ; X-ray; 1.80 A; A=2-843.
PDB; 2SKC; X-ray; 2.40 A; A=2-843.
PDB; 2SKD; X-ray; 2.40 A; A=2-843.
PDB; 2SKE; X-ray; 2.46 A; A=2-843.
PDB; 3AMV; X-ray; 2.10 A; A=2-843.
PDB; 3BCR; X-ray; 2.14 A; A=2-843.
PDB; 3BCS; X-ray; 2.00 A; A=2-843.
PDB; 3BCU; X-ray; 2.03 A; A=2-843.
PDB; 3BD6; X-ray; 2.00 A; A=2-843.
PDB; 3BD7; X-ray; 1.90 A; A=2-843.
PDB; 3BD8; X-ray; 2.10 A; A=2-843.
PDB; 3BDA; X-ray; 2.00 A; A=2-843.
PDB; 3CUT; X-ray; 2.30 A; A=2-843.
PDB; 3CUU; X-ray; 2.30 A; A=2-843.
PDB; 3CUV; X-ray; 1.93 A; A=2-843.
PDB; 3CUW; X-ray; 2.00 A; A=2-843.
PDB; 3E3L; X-ray; 2.59 A; A/B/C/D=2-843.
PDB; 3E3N; X-ray; 2.70 A; A/B/C/D/E/F/G/H=2-843.
PDB; 3E3O; X-ray; 2.60 A; A/B/C/D=2-843.
PDB; 3EBO; X-ray; 1.90 A; A=2-843.
PDB; 3EBP; X-ray; 2.00 A; A=2-843.
PDB; 3G2H; X-ray; 2.03 A; A=2-843.
PDB; 3G2I; X-ray; 2.00 A; A=2-843.
PDB; 3G2J; X-ray; 2.14 A; A=2-843.
PDB; 3G2K; X-ray; 2.00 A; A=2-843.
PDB; 3G2L; X-ray; 2.30 A; A=2-843.
PDB; 3G2N; X-ray; 2.10 A; A=2-843.
PDB; 3GPB; X-ray; 2.30 A; A=2-843.
PDB; 3L79; X-ray; 1.86 A; A=1-843.
PDB; 3L7A; X-ray; 1.90 A; A=1-843.
PDB; 3L7B; X-ray; 2.00 A; A=1-843.
PDB; 3L7C; X-ray; 1.93 A; A=1-843.
PDB; 3L7D; X-ray; 2.00 A; A=1-843.
PDB; 3MQF; X-ray; 1.95 A; A=2-843.
PDB; 3MRT; X-ray; 1.98 A; A=2-843.
PDB; 3MRV; X-ray; 1.94 A; A=2-843.
PDB; 3MRX; X-ray; 1.95 A; A=2-843.
PDB; 3MS2; X-ray; 2.10 A; A=2-843.
PDB; 3MS4; X-ray; 2.07 A; A=2-843.
PDB; 3MS7; X-ray; 1.95 A; A=2-843.
PDB; 3MSC; X-ray; 1.95 A; A=2-843.
PDB; 3MT7; X-ray; 2.00 A; A=2-843.
PDB; 3MT8; X-ray; 2.00 A; A=2-843.
PDB; 3MT9; X-ray; 2.05 A; A=2-843.
PDB; 3MTA; X-ray; 2.23 A; A=2-843.
PDB; 3MTB; X-ray; 1.95 A; A=2-843.
PDB; 3MTD; X-ray; 2.10 A; A=2-843.
PDB; 3NC4; X-ray; 2.07 A; A=3-843.
PDB; 3NP7; X-ray; 2.05 A; A=2-843.
PDB; 3NP9; X-ray; 2.00 A; A=2-843.
PDB; 3NPA; X-ray; 1.97 A; A=2-843.
PDB; 3S0J; X-ray; 2.00 A; A=2-843.
PDB; 3SYM; X-ray; 2.40 A; A=2-843.
PDB; 3SYR; X-ray; 2.40 A; A=2-843.
PDB; 3T3D; X-ray; 2.50 A; A=2-843.
PDB; 3T3E; X-ray; 2.15 A; A=2-843.
PDB; 3T3G; X-ray; 2.40 A; A=2-843.
PDB; 3T3H; X-ray; 2.60 A; A=2-843.
PDB; 3T3I; X-ray; 2.65 A; A=2-843.
PDB; 3ZCP; X-ray; 1.83 A; A=1-843.
PDB; 3ZCQ; X-ray; 2.15 A; A=1-843.
PDB; 3ZCR; X-ray; 2.07 A; A=1-843.
PDB; 3ZCS; X-ray; 2.03 A; A=1-843.
PDB; 3ZCT; X-ray; 2.00 A; A=1-843.
PDB; 3ZCU; X-ray; 2.05 A; A=1-843.
PDB; 3ZCV; X-ray; 1.83 A; A=1-843.
PDB; 4CTM; X-ray; 1.95 A; A=1-843.
PDB; 4CTN; X-ray; 2.10 A; A=1-843.
PDB; 4CTO; X-ray; 1.90 A; A=1-843.
PDB; 4EJ2; X-ray; 2.65 A; A=13-837.
PDB; 4EKE; X-ray; 2.60 A; A=13-837.
PDB; 4EKY; X-ray; 2.45 A; A=13-837.
PDB; 4EL0; X-ray; 2.40 A; A=13-837.
PDB; 4EL5; X-ray; 2.00 A; A=13-837.
PDB; 4GPB; X-ray; 2.30 A; A=2-843.
PDB; 4MHO; X-ray; 2.00 A; A=13-837.
PDB; 4MHS; X-ray; 2.00 A; A=13-837.
PDB; 4MI3; X-ray; 2.15 A; A=13-837.
PDB; 4MI6; X-ray; 1.90 A; A=13-837.
PDB; 4MI9; X-ray; 1.85 A; A=13-837.
PDB; 4MIC; X-ray; 2.45 A; A=13-837.
PDB; 4MRA; X-ray; 2.34 A; A=13-837.
PDB; 4YI3; X-ray; 1.80 A; A=1-843.
PDB; 4YI5; X-ray; 1.80 A; A=1-843.
PDB; 4YUA; X-ray; 2.00 A; A=13-837.
PDB; 4Z5X; X-ray; 2.10 A; A=1-843.
PDB; 5GPB; X-ray; 2.30 A; A=2-843.
PDB; 5JTT; X-ray; 1.85 A; A=1-843.
PDB; 5JTU; X-ray; 1.85 A; A=1-843.
PDB; 5LRC; X-ray; 2.00 A; A=2-843.
PDB; 5LRD; X-ray; 1.80 A; A=1-843.
PDB; 5LRE; X-ray; 1.80 A; A=2-843.
PDB; 5LRF; X-ray; 1.75 A; A=2-843.
PDB; 5MCB; X-ray; 1.95 A; A=13-837.
PDB; 5O50; X-ray; 1.90 A; A=2-843.
PDB; 5O52; X-ray; 1.90 A; A=1-843.
PDB; 5O54; X-ray; 2.45 A; A=1-843.
PDB; 5O56; X-ray; 2.45 A; A=1-843.
PDB; 6GPB; X-ray; 2.86 A; A=2-843.
PDB; 7GPB; X-ray; 2.90 A; A/B/C/D=2-843.
PDB; 8GPB; X-ray; 2.20 A; A=2-843.
PDB; 9GPB; X-ray; 2.90 A; A/B/C/D=2-843.
PDBsum; 1A8I; -.
PDBsum; 1ABB; -.
PDBsum; 1AXR; -.
PDBsum; 1B4D; -.
PDBsum; 1BX3; -.
PDBsum; 1C50; -.
PDBsum; 1C8K; -.
PDBsum; 1C8L; -.
PDBsum; 1E1Y; -.
PDBsum; 1FS4; -.
PDBsum; 1FTQ; -.
PDBsum; 1FTW; -.
PDBsum; 1FTY; -.
PDBsum; 1FU4; -.
PDBsum; 1FU7; -.
PDBsum; 1FU8; -.
PDBsum; 1GFZ; -.
PDBsum; 1GG8; -.
PDBsum; 1GGN; -.
PDBsum; 1GPA; -.
PDBsum; 1GPB; -.
PDBsum; 1GPY; -.
PDBsum; 1H5U; -.
PDBsum; 1HLF; -.
PDBsum; 1K06; -.
PDBsum; 1K08; -.
PDBsum; 1KTI; -.
PDBsum; 1LWN; -.
PDBsum; 1LWO; -.
PDBsum; 1NOI; -.
PDBsum; 1NOJ; -.
PDBsum; 1NOK; -.
PDBsum; 1P29; -.
PDBsum; 1P2B; -.
PDBsum; 1P2D; -.
PDBsum; 1P2G; -.
PDBsum; 1P4G; -.
PDBsum; 1P4H; -.
PDBsum; 1P4J; -.
PDBsum; 1PYG; -.
PDBsum; 1UZU; -.
PDBsum; 1WUT; -.
PDBsum; 1WUY; -.
PDBsum; 1WV0; -.
PDBsum; 1WV1; -.
PDBsum; 1WW2; -.
PDBsum; 1WW3; -.
PDBsum; 1XC7; -.
PDBsum; 1XKX; -.
PDBsum; 1XL0; -.
PDBsum; 1XL1; -.
PDBsum; 1Z62; -.
PDBsum; 1Z6P; -.
PDBsum; 1Z6Q; -.
PDBsum; 2AMV; -.
PDBsum; 2F3P; -.
PDBsum; 2F3Q; -.
PDBsum; 2F3S; -.
PDBsum; 2F3U; -.
PDBsum; 2FET; -.
PDBsum; 2FF5; -.
PDBsum; 2FFR; -.
PDBsum; 2G9Q; -.
PDBsum; 2G9R; -.
PDBsum; 2G9U; -.
PDBsum; 2G9V; -.
PDBsum; 2GJ4; -.
PDBsum; 2GM9; -.
PDBsum; 2GPA; -.
PDBsum; 2GPB; -.
PDBsum; 2GPN; -.
PDBsum; 2IEG; -.
PDBsum; 2IEI; -.
PDBsum; 2OFF; -.
PDBsum; 2PRI; -.
PDBsum; 2PRJ; -.
PDBsum; 2PYD; -.
PDBsum; 2PYI; -.
PDBsum; 2QLM; -.
PDBsum; 2QLN; -.
PDBsum; 2QN1; -.
PDBsum; 2QN2; -.
PDBsum; 2QN3; -.
PDBsum; 2QN7; -.
PDBsum; 2QN8; -.
PDBsum; 2QN9; -.
PDBsum; 2QNB; -.
PDBsum; 2QRG; -.
PDBsum; 2QRH; -.
PDBsum; 2QRM; -.
PDBsum; 2QRP; -.
PDBsum; 2QRQ; -.
PDBsum; 2SKC; -.
PDBsum; 2SKD; -.
PDBsum; 2SKE; -.
PDBsum; 3AMV; -.
PDBsum; 3BCR; -.
PDBsum; 3BCS; -.
PDBsum; 3BCU; -.
PDBsum; 3BD6; -.
PDBsum; 3BD7; -.
PDBsum; 3BD8; -.
PDBsum; 3BDA; -.
PDBsum; 3CUT; -.
PDBsum; 3CUU; -.
PDBsum; 3CUV; -.
PDBsum; 3CUW; -.
PDBsum; 3E3L; -.
PDBsum; 3E3N; -.
PDBsum; 3E3O; -.
PDBsum; 3EBO; -.
PDBsum; 3EBP; -.
PDBsum; 3G2H; -.
PDBsum; 3G2I; -.
PDBsum; 3G2J; -.
PDBsum; 3G2K; -.
PDBsum; 3G2L; -.
PDBsum; 3G2N; -.
PDBsum; 3GPB; -.
PDBsum; 3L79; -.
PDBsum; 3L7A; -.
PDBsum; 3L7B; -.
PDBsum; 3L7C; -.
PDBsum; 3L7D; -.
PDBsum; 3MQF; -.
PDBsum; 3MRT; -.
PDBsum; 3MRV; -.
PDBsum; 3MRX; -.
PDBsum; 3MS2; -.
PDBsum; 3MS4; -.
PDBsum; 3MS7; -.
PDBsum; 3MSC; -.
PDBsum; 3MT7; -.
PDBsum; 3MT8; -.
PDBsum; 3MT9; -.
PDBsum; 3MTA; -.
PDBsum; 3MTB; -.
PDBsum; 3MTD; -.
PDBsum; 3NC4; -.
PDBsum; 3NP7; -.
PDBsum; 3NP9; -.
PDBsum; 3NPA; -.
PDBsum; 3S0J; -.
PDBsum; 3SYM; -.
PDBsum; 3SYR; -.
PDBsum; 3T3D; -.
PDBsum; 3T3E; -.
PDBsum; 3T3G; -.
PDBsum; 3T3H; -.
PDBsum; 3T3I; -.
PDBsum; 3ZCP; -.
PDBsum; 3ZCQ; -.
PDBsum; 3ZCR; -.
PDBsum; 3ZCS; -.
PDBsum; 3ZCT; -.
PDBsum; 3ZCU; -.
PDBsum; 3ZCV; -.
PDBsum; 4CTM; -.
PDBsum; 4CTN; -.
PDBsum; 4CTO; -.
PDBsum; 4EJ2; -.
PDBsum; 4EKE; -.
PDBsum; 4EKY; -.
PDBsum; 4EL0; -.
PDBsum; 4EL5; -.
PDBsum; 4GPB; -.
PDBsum; 4MHO; -.
PDBsum; 4MHS; -.
PDBsum; 4MI3; -.
PDBsum; 4MI6; -.
PDBsum; 4MI9; -.
PDBsum; 4MIC; -.
PDBsum; 4MRA; -.
PDBsum; 4YI3; -.
PDBsum; 4YI5; -.
PDBsum; 4YUA; -.
PDBsum; 4Z5X; -.
PDBsum; 5GPB; -.
PDBsum; 5JTT; -.
PDBsum; 5JTU; -.
PDBsum; 5LRC; -.
PDBsum; 5LRD; -.
PDBsum; 5LRE; -.
PDBsum; 5LRF; -.
PDBsum; 5MCB; -.
PDBsum; 5O50; -.
PDBsum; 5O52; -.
PDBsum; 5O54; -.
PDBsum; 5O56; -.
PDBsum; 6GPB; -.
PDBsum; 7GPB; -.
PDBsum; 8GPB; -.
PDBsum; 9GPB; -.
ProteinModelPortal; P00489; -.
SMR; P00489; -.
DIP; DIP-38240N; -.
ELM; P00489; -.
IntAct; P00489; 5.
MINT; MINT-6368963; -.
STRING; 9986.ENSOCUP00000001880; -.
BindingDB; P00489; -.
ChEMBL; CHEMBL4696; -.
CAZy; GT35; Glycosyltransferase Family 35.
iPTMnet; P00489; -.
PRIDE; P00489; -.
GeneID; 100008972; -.
KEGG; ocu:100008972; -.
CTD; 5837; -.
eggNOG; KOG2099; Eukaryota.
eggNOG; COG0058; LUCA.
HOGENOM; HOG000278444; -.
HOVERGEN; HBG006848; -.
InParanoid; P00489; -.
KO; K00688; -.
BRENDA; 2.4.1.1; 1749.
SABIO-RK; P00489; -.
EvolutionaryTrace; P00489; -.
PRO; PR:P00489; -.
Proteomes; UP000001811; Unplaced.
GO; GO:0098723; C:skeletal muscle myofibril; IDA:CAFA.
GO; GO:0008184; F:glycogen phosphorylase activity; IEA:InterPro.
GO; GO:0102250; F:linear malto-oligosaccharide phosphorylase activity; IEA:UniProtKB-EC.
GO; GO:0000166; F:nucleotide binding; IEA:UniProtKB-KW.
GO; GO:0030170; F:pyridoxal phosphate binding; IEA:InterPro.
GO; GO:0102499; F:SHG alpha-glucan phosphorylase activity; IEA:UniProtKB-EC.
GO; GO:0005977; P:glycogen metabolic process; IEA:UniProtKB-KW.
CDD; cd04300; GT1_Glycogen_Phosphorylase; 1.
InterPro; IPR011833; Glycg_phsphrylas.
InterPro; IPR000811; Glyco_trans_35.
InterPro; IPR035090; Pyridoxal_P_attach_site.
PANTHER; PTHR11468; PTHR11468; 1.
Pfam; PF00343; Phosphorylase; 1.
PIRSF; PIRSF000460; Pprylas_GlgP; 1.
TIGRFAMs; TIGR02093; P_ylase; 1.
PROSITE; PS00102; PHOSPHORYLASE; 1.
1: Evidence at protein level;
3D-structure; Acetylation; Allosteric enzyme; Carbohydrate metabolism;
Complete proteome; Direct protein sequencing; Glycogen metabolism;
Glycosyltransferase; Nucleotide-binding; Phosphoprotein;
Pyridoxal phosphate; Reference proteome; Transferase.
INIT_MET 1 1 Removed. {ECO:0000269|PubMed:728424}.
CHAIN 2 843 Glycogen phosphorylase, muscle form.
/FTId=PRO_0000188532.
BINDING 76 76 AMP.
SITE 109 109 Involved in the association of subunits.
SITE 143 143 Involved in the association of subunits.
SITE 156 156 Can be labeled by an AMP analog; may be
involved in allosteric regulation.
MOD_RES 2 2 N-acetylserine.
{ECO:0000269|PubMed:3015680}.
MOD_RES 15 15 Phosphoserine; by PHK; in form
phosphorylase A.
{ECO:0000250|UniProtKB:P11217}.
MOD_RES 204 204 Phosphotyrosine.
{ECO:0000250|UniProtKB:P09812}.
MOD_RES 227 227 Phosphotyrosine.
{ECO:0000250|UniProtKB:P09812}.
MOD_RES 364 364 N6-succinyllysine.
{ECO:0000250|UniProtKB:Q9ET01}.
MOD_RES 430 430 Phosphoserine.
{ECO:0000250|UniProtKB:Q9WUB3}.
MOD_RES 473 473 Phosphotyrosine.
{ECO:0000250|UniProtKB:Q9WUB3}.
MOD_RES 514 514 Phosphoserine.
{ECO:0000250|UniProtKB:P09812}.
MOD_RES 524 524 Phosphoserine.
{ECO:0000250|UniProtKB:Q9ET01}.
MOD_RES 681 681 N6-(pyridoxal phosphate)lysine.
MOD_RES 747 747 Phosphoserine.
{ECO:0000250|UniProtKB:P09812}.
MOD_RES 748 748 Phosphoserine.
{ECO:0000250|UniProtKB:P09812}.
CONFLICT 31 33 NFN -> DFD (in Ref. 2; AA sequence).
{ECO:0000305}.
CONFLICT 43 43 D -> N (in Ref. 2; AA sequence).
{ECO:0000305}.
CONFLICT 56 58 LAH -> HAL (in Ref. 2; AA sequence).
{ECO:0000305}.
CONFLICT 89 89 E -> Q (in Ref. 2; AA sequence).
{ECO:0000305}.
CONFLICT 113 113 T -> D (in Ref. 2; AA sequence).
{ECO:0000305}.
CONFLICT 309 309 Missing (in Ref. 2; AA sequence).
{ECO:0000305}.
CONFLICT 578 579 LL -> FF (in Ref. 6; CAA26833).
{ECO:0000305}.
CONFLICT 610 610 A -> P (in Ref. 1; BAA00027/CAA27816).
{ECO:0000305}.
CONFLICT 713 713 G -> C (in Ref. 6; CAA26833).
{ECO:0000305}.
HELIX 9 13 {ECO:0000244|PDB:1A8I}.
HELIX 15 17 {ECO:0000244|PDB:2GJ4}.
HELIX 22 38 {ECO:0000244|PDB:2GJ4}.
TURN 44 46 {ECO:0000244|PDB:2GJ4}.
HELIX 49 62 {ECO:0000244|PDB:2GJ4}.
HELIX 65 78 {ECO:0000244|PDB:2GJ4}.
STRAND 82 86 {ECO:0000244|PDB:2GJ4}.
STRAND 90 93 {ECO:0000244|PDB:2GJ4}.
HELIX 96 102 {ECO:0000244|PDB:2GJ4}.
HELIX 106 115 {ECO:0000244|PDB:2GJ4}.
HELIX 120 124 {ECO:0000244|PDB:2GJ4}.
STRAND 130 132 {ECO:0000244|PDB:2GJ4}.
HELIX 136 150 {ECO:0000244|PDB:2GJ4}.
STRAND 155 160 {ECO:0000244|PDB:2GJ4}.
STRAND 168 172 {ECO:0000244|PDB:2GJ4}.
STRAND 175 179 {ECO:0000244|PDB:2GJ4}.
TURN 183 186 {ECO:0000244|PDB:2GJ4}.
HELIX 195 197 {ECO:0000244|PDB:2GJ4}.
STRAND 199 204 {ECO:0000244|PDB:2GJ4}.
STRAND 206 209 {ECO:0000244|PDB:2GJ4}.
STRAND 211 218 {ECO:0000244|PDB:2GJ4}.
STRAND 220 232 {ECO:0000244|PDB:2GJ4}.
STRAND 234 237 {ECO:0000244|PDB:2GJ4}.
STRAND 239 248 {ECO:0000244|PDB:2GJ4}.
TURN 251 254 {ECO:0000244|PDB:5LRF}.
TURN 256 258 {ECO:0000244|PDB:1GPA}.
STRAND 259 261 {ECO:0000244|PDB:1C8K}.
HELIX 263 268 {ECO:0000244|PDB:2GJ4}.
HELIX 270 274 {ECO:0000244|PDB:2GJ4}.
HELIX 275 277 {ECO:0000244|PDB:2GJ4}.
STRAND 284 286 {ECO:0000244|PDB:2QRQ}.
HELIX 291 313 {ECO:0000244|PDB:2GJ4}.
TURN 315 319 {ECO:0000244|PDB:1C8K}.
STRAND 322 325 {ECO:0000244|PDB:1GPB}.
HELIX 327 329 {ECO:0000244|PDB:2GJ4}.
HELIX 330 333 {ECO:0000244|PDB:2GJ4}.
STRAND 334 341 {ECO:0000244|PDB:2GJ4}.
TURN 342 345 {ECO:0000244|PDB:2GJ4}.
HELIX 346 356 {ECO:0000244|PDB:2GJ4}.
HELIX 362 372 {ECO:0000244|PDB:2GJ4}.
STRAND 373 376 {ECO:0000244|PDB:2GJ4}.
HELIX 382 384 {ECO:0000244|PDB:2GJ4}.
STRAND 387 389 {ECO:0000244|PDB:2GJ4}.
HELIX 390 396 {ECO:0000244|PDB:2GJ4}.
HELIX 398 418 {ECO:0000244|PDB:2GJ4}.
STRAND 419 421 {ECO:0000244|PDB:3E3L}.
HELIX 423 429 {ECO:0000244|PDB:2GJ4}.
STRAND 431 433 {ECO:0000244|PDB:2GJ4}.
STRAND 435 437 {ECO:0000244|PDB:2GJ4}.
STRAND 439 441 {ECO:0000244|PDB:2GJ4}.
HELIX 442 448 {ECO:0000244|PDB:2GJ4}.
STRAND 453 457 {ECO:0000244|PDB:2GJ4}.
HELIX 458 466 {ECO:0000244|PDB:2GJ4}.
TURN 467 469 {ECO:0000244|PDB:2GJ4}.
HELIX 470 475 {ECO:0000244|PDB:2GJ4}.
HELIX 477 479 {ECO:0000244|PDB:2GJ4}.
STRAND 480 482 {ECO:0000244|PDB:2GJ4}.
HELIX 490 495 {ECO:0000244|PDB:2GJ4}.
HELIX 498 508 {ECO:0000244|PDB:2GJ4}.
HELIX 511 514 {ECO:0000244|PDB:2GJ4}.
HELIX 516 525 {ECO:0000244|PDB:2GJ4}.
HELIX 529 554 {ECO:0000244|PDB:2GJ4}.
STRAND 562 569 {ECO:0000244|PDB:2GJ4}.
TURN 573 576 {ECO:0000244|PDB:2GJ4}.
HELIX 577 593 {ECO:0000244|PDB:2GJ4}.
STRAND 602 607 {ECO:0000244|PDB:2GJ4}.
HELIX 615 631 {ECO:0000244|PDB:2GJ4}.
TURN 635 637 {ECO:0000244|PDB:2GJ4}.
HELIX 638 640 {ECO:0000244|PDB:2GJ4}.
STRAND 641 646 {ECO:0000244|PDB:2GJ4}.
HELIX 651 657 {ECO:0000244|PDB:2GJ4}.
HELIX 658 660 {ECO:0000244|PDB:2GJ4}.
STRAND 662 666 {ECO:0000244|PDB:2GJ4}.
TURN 670 672 {ECO:0000244|PDB:2QNB}.
STRAND 673 675 {ECO:0000244|PDB:1Z6P}.
HELIX 678 684 {ECO:0000244|PDB:2GJ4}.
STRAND 688 691 {ECO:0000244|PDB:2GJ4}.
HELIX 697 704 {ECO:0000244|PDB:2GJ4}.
HELIX 706 708 {ECO:0000244|PDB:2GJ4}.
STRAND 709 711 {ECO:0000244|PDB:2GJ4}.
HELIX 716 725 {ECO:0000244|PDB:2GJ4}.
HELIX 729 735 {ECO:0000244|PDB:2GJ4}.
HELIX 737 748 {ECO:0000244|PDB:2GJ4}.
TURN 749 751 {ECO:0000244|PDB:2GJ4}.
STRAND 753 755 {ECO:0000244|PDB:1C8K}.
TURN 756 759 {ECO:0000244|PDB:2GJ4}.
HELIX 760 768 {ECO:0000244|PDB:2GJ4}.
HELIX 775 777 {ECO:0000244|PDB:2GJ4}.
HELIX 778 792 {ECO:0000244|PDB:2GJ4}.
HELIX 795 806 {ECO:0000244|PDB:2GJ4}.
HELIX 810 812 {ECO:0000244|PDB:2GJ4}.
HELIX 814 824 {ECO:0000244|PDB:2GJ4}.
SEQUENCE 843 AA; 97289 MW; 9884F06FDD3AE9D3 CRC64;
MSRPLSDQEK RKQISVRGLA GVENVTELKK NFNRHLHFTL VKDRNVATPR DYYFALAHTV
RDHLVGRWIR TQQHYYEKDP KRIYYLSLEF YMGRTLQNTM VNLALENACD EATYQLGLDM
EELEEIEEDA GLGNGGLGRL AACFLDSMAT LGLAAYGYGI RYEFGIFNQK ICGGWQMEEA
DDWLRYGNPW EKARPEFTLP VHFYGRVEHT SQGAKWVDTQ VVLAMPYDTP VPGYRNNVVN
TMRLWSAKAP NDFNLKDFNV GGYIQAVLDR NLAENISRVL YPNDNFFEGK ELRLKQEYFV
VAATLQDIIR RFKSSKFGCR DPVRTNFDAF PDKVAIQLND THPSLAIPEL MRVLVDLERL
DWDKAWEVTV KTCAYTNHTV LPEALERWPV HLLETLLPRH LQIIYEINQR FLNRVAAAFP
GDVDRLRRMS LVEEGAVKRI NMAHLCIAGS HAVNGVARIH SEILKKTIFK DFYELEPHKF
QNKTNGITPR RWLVLCNPGL AEIIAERIGE EYISDLDQLR KLLSYVDDEA FIRDVAKVKQ
ENKLKFAAYL EREYKVHINP NSLFDVQVKR IHEYKRQLLN CLHVITLYNR IKKEPNKFVV
PRTVMIGGKA APGYHMAKMI IKLITAIGDV VNHDPVVGDR LRVIFLENYR VSLAEKVIPA
ADLSEQISTA GTEASGTGNM KFMLNGALTI GTMDGANVEM AEEAGEENFF IFGMRVEDVD
RLDQRGYNAQ EYYDRIPELR QIIEQLSSGF FSPKQPDLFK DIVNMLMHHD RFKVFADYEE
YVKCQERVSA LYKNPREWTR MVIRNIATSG KFSSDRTIAQ YAREIWGVEP SRQRLPAPDE
KIP


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