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Glycogen phosphorylase, brain form (EC 2.4.1.1)

 PYGB_HUMAN              Reviewed;         843 AA.
P11216; Q96AK1; Q9NPX8;
01-JUL-1989, integrated into UniProtKB/Swiss-Prot.
23-JAN-2007, sequence version 5.
11-DEC-2019, entry version 218.
RecName: Full=Glycogen phosphorylase, brain form {ECO:0000303|PubMed:3346228};
EC=2.4.1.1 {ECO:0000269|PubMed:27402852};
Name=PYGB {ECO:0000303|PubMed:3346228};
Homo sapiens (Human).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
Homo.
NCBI_TaxID=9606;
[1]
NUCLEOTIDE SEQUENCE [MRNA].
TISSUE=Brain;
PubMed=3346228;
Newgard C.B., Littman D.R., van Genderen C., Smith M., Fletterick R.J.;
"Human brain glycogen phosphorylase. Cloning, sequence analysis,
chromosomal mapping, tissue expression, and comparison with the human liver
and muscle isozymes.";
J. Biol. Chem. 263:3850-3857(1988).
[2]
NUCLEOTIDE SEQUENCE [MRNA].
TISSUE=Brain;
PubMed=2615594; DOI=10.1016/0169-328x(89)90052-1;
Gelinas R.P., Froman B.E., McElroy F., Tait R.C., Gorin F.A.;
"Human brain glycogen phosphorylase: characterization of fetal cDNA and
genomic sequences.";
Brain Res. Mol. Brain Res. 6:177-185(1989).
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
PubMed=11780052; DOI=10.1038/414865a;
Deloukas P., Matthews L.H., Ashurst J.L., Burton J., Gilbert J.G.R.,
Jones M., Stavrides G., Almeida J.P., Babbage A.K., Bagguley C.L.,
Bailey J., Barlow K.F., Bates K.N., Beard L.M., Beare D.M., Beasley O.P.,
Bird C.P., Blakey S.E., Bridgeman A.M., Brown A.J., Buck D., Burrill W.D.,
Butler A.P., Carder C., Carter N.P., Chapman J.C., Clamp M., Clark G.,
Clark L.N., Clark S.Y., Clee C.M., Clegg S., Cobley V.E., Collier R.E.,
Connor R.E., Corby N.R., Coulson A., Coville G.J., Deadman R., Dhami P.D.,
Dunn M., Ellington A.G., Frankland J.A., Fraser A., French L., Garner P.,
Grafham D.V., Griffiths C., Griffiths M.N.D., Gwilliam R., Hall R.E.,
Hammond S., Harley J.L., Heath P.D., Ho S., Holden J.L., Howden P.J.,
Huckle E., Hunt A.R., Hunt S.E., Jekosch K., Johnson C.M., Johnson D.,
Kay M.P., Kimberley A.M., King A., Knights A., Laird G.K., Lawlor S.,
Lehvaeslaiho M.H., Leversha M.A., Lloyd C., Lloyd D.M., Lovell J.D.,
Marsh V.L., Martin S.L., McConnachie L.J., McLay K., McMurray A.A.,
Milne S.A., Mistry D., Moore M.J.F., Mullikin J.C., Nickerson T.,
Oliver K., Parker A., Patel R., Pearce T.A.V., Peck A.I.,
Phillimore B.J.C.T., Prathalingam S.R., Plumb R.W., Ramsay H., Rice C.M.,
Ross M.T., Scott C.E., Sehra H.K., Shownkeen R., Sims S., Skuce C.D.,
Smith M.L., Soderlund C., Steward C.A., Sulston J.E., Swann R.M.,
Sycamore N., Taylor R., Tee L., Thomas D.W., Thorpe A., Tracey A.,
Tromans A.C., Vaudin M., Wall M., Wallis J.M., Whitehead S.L.,
Whittaker P., Willey D.L., Williams L., Williams S.A., Wilming L.,
Wray P.W., Hubbard T., Durbin R.M., Bentley D.R., Beck S., Rogers J.;
"The DNA sequence and comparative analysis of human chromosome 20.";
Nature 414:865-871(2001).
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
TISSUE=Lung, and Skin;
PubMed=15489334; DOI=10.1101/gr.2596504;
The MGC Project Team;
"The status, quality, and expansion of the NIH full-length cDNA project:
the Mammalian Gene Collection (MGC).";
Genome Res. 14:2121-2127(2004).
[5]
PROTEIN SEQUENCE OF 2-11.
TISSUE=Platelet;
PubMed=12665801; DOI=10.1038/nbt810;
Gevaert K., Goethals M., Martens L., Van Damme J., Staes A., Thomas G.R.,
Vandekerckhove J.;
"Exploring proteomes and analyzing protein processing by mass spectrometric
identification of sorted N-terminal peptides.";
Nat. Biotechnol. 21:566-569(2003).
[6]
PROTEIN SEQUENCE OF 2-11; 18-30; 51-61; 71-78; 193-206; 271-278; 353-359;
388-395; 400-425; 508-520; 522-533; 546-552; 558-569; 577-590; 623-640;
657-681; 731-754 AND 817-823, CLEAVAGE OF INITIATOR METHIONINE, ACETYLATION
AT ALA-2, AND IDENTIFICATION BY MASS SPECTROMETRY.
TISSUE=Colon adenocarcinoma;
Bienvenut W.V., Murray L., Brunton V.G., Frame M.C.;
Submitted (JUL-2007) to UniProtKB.
[7]
ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, CLEAVAGE OF INITIATOR
METHIONINE [LARGE SCALE ANALYSIS], AND IDENTIFICATION BY MASS SPECTROMETRY
[LARGE SCALE ANALYSIS].
PubMed=19413330; DOI=10.1021/ac9004309;
Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J., Mohammed S.;
"Lys-N and trypsin cover complementary parts of the phosphoproteome in a
refined SCX-based approach.";
Anal. Chem. 81:4493-4501(2009).
[8]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=21269460; DOI=10.1186/1752-0509-5-17;
Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T.,
Bennett K.L., Superti-Furga G., Colinge J.;
"Initial characterization of the human central proteome.";
BMC Syst. Biol. 5:17-17(2011).
[9]
ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, CLEAVAGE OF INITIATOR
METHIONINE [LARGE SCALE ANALYSIS], AND IDENTIFICATION BY MASS SPECTROMETRY
[LARGE SCALE ANALYSIS].
PubMed=22814378; DOI=10.1073/pnas.1210303109;
Van Damme P., Lasa M., Polevoda B., Gazquez C., Elosegui-Artola A.,
Kim D.S., De Juan-Pardo E., Demeyer K., Hole K., Larrea E., Timmerman E.,
Prieto J., Arnesen T., Sherman F., Gevaert K., Aldabe R.;
"N-terminal acetylome analyses and functional insights of the N-terminal
acetyltransferase NatB.";
Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012).
[10]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Liver;
PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014;
Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., Wang L.,
Ye M., Zou H.;
"An enzyme assisted RP-RPLC approach for in-depth analysis of human liver
phosphoproteome.";
J. Proteomics 96:253-262(2014).
[11]
X-RAY CRYSTALLOGRAPHY (2.50 ANGSTROMS) OF 1-843 IN COMPLEX WITH AMP,
FUNCTION, CATALYTIC ACTIVITY, ACTIVITY REGULATION, SUBUNIT, AND
PHOSPHORYLATION.
PubMed=27402852; DOI=10.1074/jbc.m116.738898;
Mathieu C., de la Sierra-Gallay I.L., Duval R., Xu X., Cocaign A.,
Leger T., Woffendin G., Camadro J.M., Etchebest C., Haouz A., Dupret J.M.,
Rodrigues-Lima F.;
"Insights into Brain Glycogen Metabolism: THE STRUCTURE OF HUMAN BRAIN
GLYCOGEN PHOSPHORYLASE.";
J. Biol. Chem. 291:18072-18083(2016).
-!- FUNCTION: Glycogen phosphorylase that regulates glycogen mobilization
(PubMed:27402852). Phosphorylase is an important allosteric enzyme in
carbohydrate metabolism (PubMed:3346228). Enzymes from different
sources differ in their regulatory mechanisms and in their natural
substrates (PubMed:3346228). However, all known phosphorylases share
catalytic and structural properties (PubMed:3346228).
{ECO:0000269|PubMed:27402852, ECO:0000303|PubMed:3346228}.
-!- CATALYTIC ACTIVITY:
Reaction=[(1->4)-alpha-D-glucosyl](n) + phosphate = [(1->4)-alpha-D-
glucosyl](n-1) + alpha-D-glucose 1-phosphate; Xref=Rhea:RHEA:41732,
Rhea:RHEA-COMP:9584, Rhea:RHEA-COMP:9586, ChEBI:CHEBI:15444,
ChEBI:CHEBI:43474, ChEBI:CHEBI:58601; EC=2.4.1.1;
Evidence={ECO:0000269|PubMed:27402852};
-!- COFACTOR:
Name=pyridoxal 5'-phosphate; Xref=ChEBI:CHEBI:597326;
-!- ACTIVITY REGULATION: Activity of phosphorylase is controlled both by
allosteric means (through the non-covalent binding of metabolites) and
by covalent modification. Thus AMP allosterically activates, whereas
ATP, ADP, and glucose-6-phosphate allosterically inhibit, phosphorylase
B. Activated upon phosphorylation. {ECO:0000269|PubMed:27402852}.
-!- SUBUNIT: Homodimer. Dimers associate into a tetramer to form the
enzymatically active phosphorylase A. {ECO:0000269|PubMed:27402852}.
-!- INTERACTION:
P06737:PYGL; NbExp=8; IntAct=EBI-1047231, EBI-2511865;
Q8IUQ4:SIAH1; NbExp=3; IntAct=EBI-1047231, EBI-747107;
-!- PTM: Phosphorylated (PubMed:27402852). Phosphorylation of Ser-15
converts phosphorylase B (unphosphorylated) to phosphorylase A (By
similarity). {ECO:0000250|UniProtKB:P11217,
ECO:0000269|PubMed:27402852}.
-!- SIMILARITY: Belongs to the glycogen phosphorylase family.
{ECO:0000305}.
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EMBL; J03544; AAA59597.1; -; mRNA.
EMBL; U47025; AAB60395.1; -; mRNA.
EMBL; AL121772; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; BC017045; AAH17045.1; -; mRNA.
EMBL; BC030795; AAH30795.1; -; mRNA.
CCDS; CCDS13171.1; -.
PIR; A40138; A40138.
RefSeq; NP_002853.2; NM_002862.3.
PDB; 5IKO; X-ray; 2.50 A; A=1-843.
PDB; 5IKP; X-ray; 3.40 A; A=1-843.
PDBsum; 5IKO; -.
PDBsum; 5IKP; -.
SMR; P11216; -.
BioGrid; 111792; 54.
IntAct; P11216; 25.
MINT; P11216; -.
STRING; 9606.ENSP00000216962; -.
BindingDB; P11216; -.
ChEMBL; CHEMBL3856; -.
DrugBank; DB03496; Alvocidib.
DrugBank; DB00114; Pyridoxal phosphate.
CAZy; GT35; Glycosyltransferase Family 35.
iPTMnet; P11216; -.
PhosphoSitePlus; P11216; -.
SwissPalm; P11216; -.
BioMuta; PYGB; -.
DMDM; 20178317; -.
EPD; P11216; -.
jPOST; P11216; -.
MassIVE; P11216; -.
MaxQB; P11216; -.
PaxDb; P11216; -.
PeptideAtlas; P11216; -.
PRIDE; P11216; -.
ProteomicsDB; 52720; -.
DNASU; 5834; -.
Ensembl; ENST00000216962; ENSP00000216962; ENSG00000100994.
GeneID; 5834; -.
KEGG; hsa:5834; -.
UCSC; uc002wup.4; human.
CTD; 5834; -.
DisGeNET; 5834; -.
EuPathDB; HostDB:ENSG00000100994.11; -.
GeneCards; PYGB; -.
HGNC; HGNC:9723; PYGB.
HPA; HPA031067; -.
MIM; 138550; gene.
neXtProt; NX_P11216; -.
OpenTargets; ENSG00000100994; -.
PharmGKB; PA34066; -.
eggNOG; KOG2099; Eukaryota.
eggNOG; COG0058; LUCA.
GeneTree; ENSGT00950000183148; -.
InParanoid; P11216; -.
KO; K00688; -.
OMA; TEAWIRN; -.
OrthoDB; 240595at2759; -.
PhylomeDB; P11216; -.
TreeFam; TF300309; -.
BioCyc; MetaCyc:HS02178-MONOMER; -.
Reactome; R-HSA-6798695; Neutrophil degranulation.
Reactome; R-HSA-70221; Glycogen breakdown (glycogenolysis).
ChiTaRS; PYGB; human.
GenomeRNAi; 5834; -.
Pharos; P11216; Tbio.
PRO; PR:P11216; -.
Proteomes; UP000005640; Chromosome 20.
RNAct; P11216; protein.
Bgee; ENSG00000100994; Expressed in 205 organ(s), highest expression level in lower esophagus muscularis layer.
ExpressionAtlas; P11216; baseline and differential.
Genevisible; P11216; HS.
GO; GO:0035578; C:azurophil granule lumen; TAS:Reactome.
GO; GO:0005737; C:cytoplasm; IDA:UniProtKB.
GO; GO:0070062; C:extracellular exosome; HDA:UniProtKB.
GO; GO:0005576; C:extracellular region; TAS:Reactome.
GO; GO:0016020; C:membrane; HDA:UniProtKB.
GO; GO:0008184; F:glycogen phosphorylase activity; IBA:GO_Central.
GO; GO:0102250; F:linear malto-oligosaccharide phosphorylase activity; IEA:UniProtKB-EC.
GO; GO:0030170; F:pyridoxal phosphate binding; IBA:GO_Central.
GO; GO:0102499; F:SHG alpha-glucan phosphorylase activity; IEA:UniProtKB-EC.
GO; GO:0005980; P:glycogen catabolic process; IBA:GO_Central.
GO; GO:0043312; P:neutrophil degranulation; TAS:Reactome.
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;
Direct protein sequencing; Glycogen metabolism; Glycosyltransferase;
Phosphoprotein; Polymorphism; Pyridoxal phosphate; Reference proteome;
Transferase.
INIT_MET 1
/note="Removed"
/evidence="ECO:0000244|PubMed:19413330,
ECO:0000244|PubMed:22814378, ECO:0000269|PubMed:12665801,
ECO:0000269|Ref.6"
CHAIN 2..843
/note="Glycogen phosphorylase, brain form"
/id="PRO_0000188535"
REGION 677..678
/note="Pyridoxal 5'-phosphate"
/evidence="ECO:0000269|PubMed:27402852"
BINDING 43
/note="AMP; shared with dimeric partner"
/evidence="ECO:0000269|PubMed:27402852"
BINDING 197
/note="AMP"
/evidence="ECO:0000269|PubMed:27402852"
BINDING 310
/note="AMP"
/evidence="ECO:0000269|PubMed:27402852"
BINDING 569
/note="Pyridoxal 5'-phosphate"
/evidence="ECO:0000269|PubMed:27402852"
SITE 76
/note="Participates in a stacking interaction with the
adenine ring of AMP"
/evidence="ECO:0000269|PubMed:27402852"
SITE 109
/note="Involved in the association of subunits"
/evidence="ECO:0000250"
SITE 143
/note="Involved in the association of subunits"
/evidence="ECO:0000250"
SITE 156
/note="May be involved in allosteric control"
/evidence="ECO:0000250"
MOD_RES 2
/note="N-acetylalanine"
/evidence="ECO:0000244|PubMed:19413330,
ECO:0000244|PubMed:22814378, ECO:0000269|Ref.6"
MOD_RES 15
/note="Phosphoserine; by PHK; in form phosphorylase A"
/evidence="ECO:0000250|UniProtKB:P53534"
MOD_RES 197
/note="Phosphotyrosine"
/evidence="ECO:0000250|UniProtKB:Q8CI94"
MOD_RES 473
/note="Phosphotyrosine"
/evidence="ECO:0000250|UniProtKB:Q8CI94"
MOD_RES 681
/note="N6-(pyridoxal phosphate)lysine"
/evidence="ECO:0000269|PubMed:27402852"
VARIANT 303
/note="A -> S (in dbSNP:rs2228976)"
/id="VAR_034428"
VARIANT 502
/note="D -> N (in dbSNP:rs2227891)"
/id="VAR_020212"
CONFLICT 2..3
/note="AK -> GE (in Ref. 1 and 2)"
/evidence="ECO:0000305"
CONFLICT 248
/note="K -> R (in Ref. 1; AAA59597)"
/evidence="ECO:0000305"
CONFLICT 302
/note="A -> G (in Ref. 1; AAA59597)"
/evidence="ECO:0000305"
CONFLICT 835..843
/note="IPPPNIPRD -> LQHLPHPEWESGGATCWAPPELCTHLAMY (in Ref.
1; AAA59597)"
/evidence="ECO:0000305"
HELIX 23..38
/evidence="ECO:0000244|PDB:5IKO"
TURN 44..46
/evidence="ECO:0000244|PDB:5IKO"
HELIX 49..78
/evidence="ECO:0000244|PDB:5IKO"
STRAND 82..86
/evidence="ECO:0000244|PDB:5IKO"
HELIX 96..102
/evidence="ECO:0000244|PDB:5IKO"
HELIX 106..115
/evidence="ECO:0000244|PDB:5IKO"
HELIX 120..126
/evidence="ECO:0000244|PDB:5IKO"
STRAND 130..132
/evidence="ECO:0000244|PDB:5IKP"
HELIX 136..150
/evidence="ECO:0000244|PDB:5IKO"
STRAND 155..160
/evidence="ECO:0000244|PDB:5IKO"
STRAND 168..172
/evidence="ECO:0000244|PDB:5IKO"
STRAND 175..179
/evidence="ECO:0000244|PDB:5IKO"
TURN 183..186
/evidence="ECO:0000244|PDB:5IKO"
HELIX 195..197
/evidence="ECO:0000244|PDB:5IKO"
STRAND 199..210
/evidence="ECO:0000244|PDB:5IKO"
STRAND 213..232
/evidence="ECO:0000244|PDB:5IKO"
STRAND 234..237
/evidence="ECO:0000244|PDB:5IKP"
STRAND 239..248
/evidence="ECO:0000244|PDB:5IKO"
HELIX 260..274
/evidence="ECO:0000244|PDB:5IKO"
HELIX 275..277
/evidence="ECO:0000244|PDB:5IKO"
STRAND 279..281
/evidence="ECO:0000244|PDB:5IKO"
HELIX 290..313
/evidence="ECO:0000244|PDB:5IKO"
HELIX 326..329
/evidence="ECO:0000244|PDB:5IKO"
HELIX 330..333
/evidence="ECO:0000244|PDB:5IKO"
STRAND 334..341
/evidence="ECO:0000244|PDB:5IKO"
HELIX 342..345
/evidence="ECO:0000244|PDB:5IKO"
HELIX 346..356
/evidence="ECO:0000244|PDB:5IKO"
HELIX 362..372
/evidence="ECO:0000244|PDB:5IKO"
STRAND 373..376
/evidence="ECO:0000244|PDB:5IKO"
HELIX 382..384
/evidence="ECO:0000244|PDB:5IKO"
STRAND 387..389
/evidence="ECO:0000244|PDB:5IKO"
HELIX 390..396
/evidence="ECO:0000244|PDB:5IKO"
HELIX 398..418
/evidence="ECO:0000244|PDB:5IKO"
HELIX 423..429
/evidence="ECO:0000244|PDB:5IKO"
STRAND 431..433
/evidence="ECO:0000244|PDB:5IKO"
STRAND 435..437
/evidence="ECO:0000244|PDB:5IKO"
STRAND 439..441
/evidence="ECO:0000244|PDB:5IKO"
HELIX 442..448
/evidence="ECO:0000244|PDB:5IKO"
STRAND 453..457
/evidence="ECO:0000244|PDB:5IKO"
HELIX 458..466
/evidence="ECO:0000244|PDB:5IKO"
TURN 467..469
/evidence="ECO:0000244|PDB:5IKO"
HELIX 470..475
/evidence="ECO:0000244|PDB:5IKO"
HELIX 477..479
/evidence="ECO:0000244|PDB:5IKO"
STRAND 480..482
/evidence="ECO:0000244|PDB:5IKO"
HELIX 490..495
/evidence="ECO:0000244|PDB:5IKO"
HELIX 498..508
/evidence="ECO:0000244|PDB:5IKO"
HELIX 511..513
/evidence="ECO:0000244|PDB:5IKO"
HELIX 516..526
/evidence="ECO:0000244|PDB:5IKO"
HELIX 529..554
/evidence="ECO:0000244|PDB:5IKO"
STRAND 562..569
/evidence="ECO:0000244|PDB:5IKO"
TURN 573..576
/evidence="ECO:0000244|PDB:5IKO"
HELIX 577..593
/evidence="ECO:0000244|PDB:5IKO"
STRAND 602..607
/evidence="ECO:0000244|PDB:5IKO"
HELIX 615..632
/evidence="ECO:0000244|PDB:5IKO"
TURN 635..637
/evidence="ECO:0000244|PDB:5IKO"
HELIX 638..640
/evidence="ECO:0000244|PDB:5IKO"
STRAND 641..648
/evidence="ECO:0000244|PDB:5IKO"
HELIX 651..657
/evidence="ECO:0000244|PDB:5IKO"
HELIX 658..660
/evidence="ECO:0000244|PDB:5IKP"
STRAND 662..666
/evidence="ECO:0000244|PDB:5IKO"
TURN 670..672
/evidence="ECO:0000244|PDB:5IKP"
HELIX 678..684
/evidence="ECO:0000244|PDB:5IKO"
STRAND 688..691
/evidence="ECO:0000244|PDB:5IKO"
HELIX 696..704
/evidence="ECO:0000244|PDB:5IKO"
HELIX 706..708
/evidence="ECO:0000244|PDB:5IKO"
STRAND 709..711
/evidence="ECO:0000244|PDB:5IKO"
HELIX 716..725
/evidence="ECO:0000244|PDB:5IKO"
HELIX 730..734
/evidence="ECO:0000244|PDB:5IKO"
HELIX 737..748
/evidence="ECO:0000244|PDB:5IKO"
TURN 749..751
/evidence="ECO:0000244|PDB:5IKO"
STRAND 753..755
/evidence="ECO:0000244|PDB:5IKP"
TURN 756..759
/evidence="ECO:0000244|PDB:5IKO"
HELIX 760..768
/evidence="ECO:0000244|PDB:5IKO"
HELIX 774..792
/evidence="ECO:0000244|PDB:5IKO"
HELIX 795..807
/evidence="ECO:0000244|PDB:5IKO"
HELIX 810..812
/evidence="ECO:0000244|PDB:5IKO"
HELIX 814..824
/evidence="ECO:0000244|PDB:5IKO"
SEQUENCE 843 AA; 96696 MW; 810BFAD3002CACB0 CRC64;
MAKPLTDSEK RKQISVRGLA GLGDVAEVRK SFNRHLHFTL VKDRNVATPR DYFFALAHTV
RDHLVGRWIR TQQHYYERDP KRIYYLSLEF YMGRTLQNTM VNLGLQNACD EAIYQLGLDL
EELEEIEEDA GLGNGGLGRL AACFLDSMAT LGLAAYGYGI RYEFGIFNQK IVNGWQVEEA
DDWLRYGNPW EKARPEYMLP VHFYGRVEHT PDGVKWLDTQ VVLAMPYDTP VPGYKNNTVN
TMRLWSAKAP NDFKLQDFNV GDYIEAVLDR NLAENISRVL YPNDNFFEGK ELRLKQEYFV
VAATLQDIIR RFKSSKFGCR DPVRTCFETF PDKVAIQLND THPALSIPEL MRILVDVEKV
DWDKAWEITK KTCAYTNHTV LPEALERWPV SMFEKLLPRH LEIIYAINQR HLDHVAALFP
GDVDRLRRMS VIEEGDCKRI NMAHLCVIGS HAVNGVARIH SEIVKQSVFK DFYELEPEKF
QNKTNGITPR RWLLLCNPGL ADTIVEKIGE EFLTDLSQLK KLLPLVSDEV FIRDVAKVKQ
ENKLKFSAFL EKEYKVKINP SSMFDVHVKR IHEYKRQLLN CLHVVTLYNR IKRDPAKAFV
PRTVMIGGKA APGYHMAKLI IKLVTSIGDV VNHDPVVGDR LKVIFLENYR VSLAEKVIPA
ADLSQQISTA GTEASGTGNM KFMLNGALTI GTMDGANVEM AEEAGAENLF IFGLRVEDVE
ALDRKGYNAR EYYDHLPELK QAVDQISSGF FSPKEPDCFK DIVNMLMHHD RFKVFADYEA
YMQCQAQVDQ LYRNPKEWTK KVIRNIACSG KFSSDRTITE YAREIWGVEP SDLQIPPPNI
PRD


Related products :

Catalog number Product name Quantity
LF-PA40977 anti-Glycogen Phosphorylase, Brain Form, Rabbit polyclonal to Glycogen Phosphorylase, Brain Form, Isotype IgG, Host Rabbit 50 ug
LF-PA40976 anti-Glycogen Phosphorylase, Brain Form, Rabbit polyclonal to Glycogen Phosphorylase, Brain Form, Isotype IgG, Host Rabbit 50 ug
AP06856PU-N Glycogen Phosphorylase, Brain Form (PYGB) (brain) 50 µg
8G67X Glycogen phosphorylase brain form 0.5 mg
GTX20885 Glycogen phosphorylase brain form 100 µg
8G67 Glycogen phosphorylase brain form 0.1 mg
4GP31-8G7 Glycogen phosphorylase brain form 1 mg
4GP31-6G5 Glycogen phosphorylase brain form 1 mg
GTX22075 Glycogen phosphorylase brain form 250 µg
GTX20886 Glycogen phosphorylase brain form 100 µg
NB120-882 Glycogen phosphorylase brain form 0.2 mg
4GP31-7B9 Glycogen phosphorylase brain form 1 mg
GTX20887 Glycogen phosphorylase brain form 100 µg
NB120-885 Glycogen phosphorylase brain form 0.2 mg
GTX104291 Glycogen phosphorylase brain form 100 µl
8G67XC Glycogen phosphorylase brain form 1 mg
GTX20881 Glycogen phosphorylase brain form 100 µg
GTX20880 Glycogen phosphorylase brain form 100 µg
GTX20882 Glycogen phosphorylase brain form 100 µg
AP06887PU-N Glycogen phosphorylase brain form 50 µg
GTX22069 Glycogen phosphorylase brain form 100 µg
GTX20883 Glycogen phosphorylase brain form 100 µg
ARP48587_P050 Glycogen phosphorylase brain form 50 µg
ARP48586_P050 Glycogen phosphorylase brain form 50 µg
GTX20877 Glycogen phosphorylase brain form 100 µg
Pathways :
WP1073: Glycogen Metabolism
WP1403: AMPK signaling
WP2148: Brain derived neurotrophic factor
WP436: Glycogen Metabolism
WP576: Glycogen Metabolism
WP1388: Glycogen Metabolism
WP2042: PKA-HCG-Glycogen Syntase
WP317: Glycogen Metabolism
WP500: Glycogen Metabolism
WP955: Glycogen Metabolism
WP1189: Glycogen Metabolism
WP160: Glycogen Metabolism
WP2249: Metastatic brain tumor
WP478: Glycogen Catabolism
WP835: Glycogen Metabolism

Related Genes :
[ppnP OR1_03385] Pyrimidine/purine nucleoside phosphorylase (EC 2.4.2.1) (EC 2.4.2.2) (Adenosine phosphorylase) (Cytidine phosphorylase) (Guanosine phosphorylase) (EC 2.4.2.15) (Inosine phosphorylase) (Thymidine phosphorylase) (EC 2.4.2.4) (Uridine phosphorylase) (EC 2.4.2.3) (Xanthosine phosphorylase)
[AGL GDE] Glycogen debranching enzyme (Glycogen debrancher) [Includes: 4-alpha-glucanotransferase (EC 2.4.1.25) (Oligo-1,4-1,4-glucantransferase); Amylo-alpha-1,6-glucosidase (Amylo-1,6-glucosidase) (EC 3.2.1.33) (Dextrin 6-alpha-D-glucosidase)]
[] Genome polyprotein [Cleaved into: P3; Protein 3AB; P2; P1; Capsid protein VP0 (VP4-VP2); Capsid protein VP4 (P1A) (Virion protein 4); Capsid protein VP2 (P1B) (Virion protein 2); Capsid protein VP3 (P1C) (Virion protein 3); Capsid protein VP1 (P1D) (Virion protein 1); Protease 2A (P2A) (EC 3.4.22.29) (Picornain 2A) (Protein 2A); Protein 2B (P2B); Protein 2C (P2C) (EC 3.6.1.15); Protein 3A (P3A); Viral protein genome-linked (VPg) (Protein 3B) (P3B); Protein 3CD (EC 3.4.22.28); Protease 3C (P3C) (EC 3.4.22.28); RNA-directed RNA polymerase (RdRp) (EC 2.7.7.48) (3D polymerase) (3Dpol) (Protein 3D) (3D)]
[hchA A8C65_13880 A9R57_25255 AKG99_20940 AMK83_16550 B7C53_22525 B9M99_11580 B9T59_01945 BJJ90_15205 BMT49_12710 BON66_15955 BON86_06490 BON95_14610 BUE81_10670 BvCms12BK_01457 BvCms28BK_04168 BvCmsHHP001_02632 BvCmsKKP061_00566 BvCmsKSP015_01352 BvCmsKSP045_04450 BvCmsKSP058_03204 BvCmsKSP067_02879 BvCmsKSP083_03900 BvCmsNSP006_03750 BvCmsNSP007_03329 BvCmsNSP047_03567 BvCmsSINP011_04162 BW690_17225 BZL69_29425 C2U48_24800 C5715_19445 C5N07_21380 C6669_19295 C7B06_02290 C7B07_03930 C9025_17620 C9077_19550 C9078_12950 C9083_21590 C9212_13125 C9Y80_10480 C9Y95_17520 C9Z12_18550 CDC27_10055 CDL37_00765 CI694_25210 CIJ94_05515 COD46_23180 CQP61_17160 CRD98_26150 D2188_01360 D6W60_25270 D9D20_21030 D9D43_06110 D9H68_20750 D9H70_25730 D9I87_15275 DEN89_24995 DEO04_05510 DL800_09215 DNQ41_14245 DQE83_22775 DTL43_21780 DTM25_06080 DU321_04440 DXT73_20690 E2134_24005 E2135_17195 E2855_02503 E2863_02392 E5P22_21380 E5S46_06650 EB575_25290 EC95NR1_00961 ED648_25045 ELT20_21515 ELV08_24970 EPS97_16570 EPT01_11070 EQ825_23250 ERS085379_01273 ERS085386_05041 ExPECSC038_01920 EXX71_02385 EXX78_21815 EYD11_09165 FNJ83_13175 FQ915_04255 FQR64_09390 FWK02_18105 HmCmsJML079_02678 HMPREF3040_01583 HW43_13705 NCTC10082_04431 NCTC10418_03071 NCTC10767_03558 NCTC11022_01867 NCTC11126_04427 NCTC11181_05650 NCTC12950_02263 NCTC8985_00529 NCTC9111_05933 NCTC9703_00277 PGD_01271 PU06_24500 SAMEA3472043_00447 SAMEA3472055_03589 SAMEA3472056_01268 SAMEA3472070_00654 SAMEA3472080_04213 SAMEA3472090_03376 SAMEA3472110_00060 SAMEA3472112_00448 SAMEA3752372_00752 UN91_23615 WQ89_10695] Protein/nucleic acid deglycase HchA (EC 3.1.2.-) (EC 3.5.1.-) (EC 3.5.1.124) (Maillard deglycase)
[ppnP AYO08_19345 C5609_17210 CBL13_02384 CBP06_27875 E4195_25045 EQ845_08700] Pyrimidine/purine nucleoside phosphorylase (EC 2.4.2.1) (EC 2.4.2.2) (Adenosine phosphorylase) (Cytidine phosphorylase) (Guanosine phosphorylase) (EC 2.4.2.15) (Inosine phosphorylase) (Thymidine phosphorylase) (EC 2.4.2.4) (Uridine phosphorylase) (EC 2.4.2.3) (Xanthosine phosphorylase)
[Gsk3b] Glycogen synthase kinase-3 beta (GSK-3 beta) (EC 2.7.11.26) (Serine/threonine-protein kinase GSK3B) (EC 2.7.11.1)
[ppnP OR214_03073] Pyrimidine/purine nucleoside phosphorylase (EC 2.4.2.1) (EC 2.4.2.2) (Adenosine phosphorylase) (Cytidine phosphorylase) (Guanosine phosphorylase) (EC 2.4.2.15) (Inosine phosphorylase) (Thymidine phosphorylase) (EC 2.4.2.4) (Uridine phosphorylase) (EC 2.4.2.3) (Xanthosine phosphorylase)
[ppnP OR16_09104] Pyrimidine/purine nucleoside phosphorylase (EC 2.4.2.1) (EC 2.4.2.2) (Adenosine phosphorylase) (Cytidine phosphorylase) (Guanosine phosphorylase) (EC 2.4.2.15) (Inosine phosphorylase) (Thymidine phosphorylase) (EC 2.4.2.4) (Uridine phosphorylase) (EC 2.4.2.3) (Xanthosine phosphorylase)
[GDB1 YPR184W] Glycogen debranching enzyme (Glycogen debrancher) [Includes: 4-alpha-glucanotransferase (EC 2.4.1.25) (Oligo-1,4-1,4-glucantransferase); Amylo-alpha-1,6-glucosidase (Amylo-1,6-glucosidase) (EC 3.2.1.33) (Dextrin 6-alpha-D-glucosidase)]
[hchA A9819_11910 ACN81_03425 AML35_08765 AW059_23935 BANRA_00208 BANRA_00433 BANRA_02614 BHF46_18455 BMT91_24760 BON76_21885 BvCmsC61A_00149 BvCmsKSNP120_04693 BvCmsKSP026_03873 BvCmsKSP076_04891 C7B08_25495 CR538_10415 D2F89_25795 D3Y67_22910 D9G42_11130 D9I97_22010 D9J11_25195 DP258_02540 E3B71_05970 EC3234A_36c00010 EC382_21100 ECTO6_01955 EHH55_07135 EPS71_23885 FORC82_1921 FV293_07100 NCTC8500_02249 NCTC9117_02637 NCTC9969_02156 SAMEA3472108_01151 SAMEA3484427_04795 SAMEA3484429_02051 SAMEA3752557_05476 SAMEA3752559_04333] Protein/nucleic acid deglycase HchA (EC 3.1.2.-) (EC 3.5.1.-) (EC 3.5.1.124) (Maillard deglycase)
[] Genome polyprotein [Cleaved into: Capsid protein C (Capsid protein) (Core protein); Protein prM (Precursor membrane protein); Peptide pr (Peptide precursor); Small envelope protein M (Matrix protein); Envelope protein E; Non-structural protein 1 (NS1); Non-structural protein 2A (NS2A); Serine protease subunit NS2B (Flavivirin protease NS2B regulatory subunit) (Non-structural protein 2B); Serine protease NS3 (EC 3.4.21.91) (EC 3.6.1.15) (EC 3.6.4.13) (Flavivirin protease NS3 catalytic subunit) (Non-structural protein 3); Non-structural protein 4A (NS4A); Peptide 2k; Non-structural protein 4B (NS4B); RNA-directed RNA polymerase NS5 (EC 2.1.1.56) (EC 2.1.1.57) (EC 2.7.7.48) (Non-structural protein 5)]
[Phkg1 Phkg] Phosphorylase b kinase gamma catalytic chain, skeletal muscle/heart isoform (EC 2.7.11.19) (Phosphorylase kinase subunit gamma-1) (Serine/threonine-protein kinase PHKG1) (EC 2.7.11.1) (EC 2.7.11.26)
[Dll1] Delta-like protein 1 (Drosophila Delta homolog 1) (Delta1) [Cleaved into: Dll1-soluble form (Dll1-EC) (Shed form); Dll1-derived cell-associated form (Dll1-TMIC) (Membrane-associated fragment); Dll1-intracellular form (Dll1-IC)]
[EPM2A] Laforin (EC 3.1.3.-) (EC 3.1.3.16) (EC 3.1.3.48) (Glucan phosphatase) (Glycogen phosphatase) (Lafora PTPase) (LAFPTPase)
[] Genome polyprotein [Cleaved into: Core protein p21 (Capsid protein C) (p21); Core protein p19; Envelope glycoprotein E1 (gp32) (gp35); Envelope glycoprotein E2 (NS1) (gp68) (gp70); p7; Protease NS2-3 (p23) (EC 3.4.22.-); Serine protease NS3 (EC 3.4.21.98) (EC 3.6.1.15) (EC 3.6.4.13) (Hepacivirin) (NS3P) (p70); Non-structural protein 4A (NS4A) (p8); Non-structural protein 4B (NS4B) (p27); Non-structural protein 5A (NS5A) (p56); RNA-directed RNA polymerase (EC 2.7.7.48) (NS5B) (p68)]
[TPS1 BYP1 CIF1 FDP1 GGS1 GLC6 TSS1 YBR126C YBR0922] Alpha,alpha-trehalose-phosphate synthase [UDP-forming] 56 kDa subunit (EC 2.4.1.15) (General glucose sensor subunit 1) (Glycogen metabolism control protein GLC6) (Trehalose synthase complex catalytic subunit TPS1) (Trehalose-6-phosphate synthase) (UDP-glucose-glucosephosphate glucosyltransferase)
[] Genome polyprotein [Cleaved into: P1; Capsid protein VP0 (VP4-VP2); Capsid protein VP4 (P1A) (Virion protein 4); Capsid protein VP2 (P1B) (Virion protein 2); Capsid protein VP3 (P1C) (Virion protein 3); Capsid protein VP1 (P1D) (Virion protein 1); P2; Protease 2A (P2A) (EC 3.4.22.29) (Picornain 2A) (Protein 2A); Protein 2B (P2B); Protein 2C (P2C) (EC 3.6.1.15); P3; Protein 3AB; Protein 3A (P3A); Viral protein genome-linked (VPg) (Protein 3B) (P3B); Protein 3CD (EC 3.4.22.28); Protease 3C (P3C) (EC 3.4.22.28); RNA-directed RNA polymerase (RdRp) (EC 2.7.7.48) (3D polymerase) (3Dpol) (Protein 3D) (3D)]
[Cpt1c] Carnitine O-palmitoyltransferase 1, brain isoform (CPT1-B) (EC 2.3.1.21) (CPT IC) (Carnitine O-palmitoyltransferase I, brain isoform) (CPTI-B) (Carnitine palmitoyltransferase 1C)
[PHS1 At3g29320 MUO10.17] Alpha-glucan phosphorylase 1 (AtPHS1) (EC 2.4.1.1) (Alpha-glucan phosphorylase, L isozyme) (Starch phosphorylase L)
[aro-1 aro-2 aro-4 aro-5 aro-9 B14H13.20 NCU016321] Pentafunctional AROM polypeptide [Includes: 3-dehydroquinate synthase (DHQS) (EC 4.2.3.4); 3-phosphoshikimate 1-carboxyvinyltransferase (EC 2.5.1.19) (5-enolpyruvylshikimate-3-phosphate synthase) (EPSP synthase) (EPSPS); Shikimate kinase (SK) (EC 2.7.1.71); 3-dehydroquinate dehydratase (3-dehydroquinase) (EC 4.2.1.10); Shikimate dehydrogenase (EC 1.1.1.25)]
[PF0853] Probable 6-oxopurine nucleoside phosphorylase (EC 2.4.2.1) (Purine nucleoside phosphorylase) (PNP) (PfPNP)
[ACE DCP DCP1] Angiotensin-converting enzyme (ACE) (EC 3.2.1.-) (EC 3.4.15.1) (Dipeptidyl carboxypeptidase I) (Kininase II) (CD antigen CD143) [Cleaved into: Angiotensin-converting enzyme, soluble form]
[Galnt2] Polypeptide N-acetylgalactosaminyltransferase 2 (EC 2.4.1.41) (Polypeptide GalNAc transferase 2) (GalNAc-T2) (pp-GaNTase 2) (Protein-UDP acetylgalactosaminyltransferase 2) (UDP-GalNAc:polypeptide N-acetylgalactosaminyltransferase 2) [Cleaved into: Polypeptide N-acetylgalactosaminyltransferase 2 soluble form]
[GSK3B] Glycogen synthase kinase-3 beta (GSK-3 beta) (EC 2.7.11.26) (Serine/threonine-protein kinase GSK3B) (EC 2.7.11.1)
[hchA A8M42_01610 AM465_15370 AWF59_019055 AZZ83_004235 B9N33_26475 BFD68_20845 C7B02_06890 CCZ14_26645 CCZ17_22700 CRT43_11430 CT143_08220 CUB99_23505 D3C88_02905 D9D33_15385 D9E49_19020 D9I20_10460 D9J46_03345 DNR41_00375 DS966_16070 DU333_03260 DW236_02290 ECTO124_02024 EGT48_04930 ELT23_21030 ELT33_08025 ELT34_19745 ELU82_24705 ELU96_05025 ELV13_26065 ELV32_25680 ELX83_25640 EPS76_06485 EPS91_17475 EPS94_00505 ERS085406_02591 EWK56_00075 ExPECSC007_02422 ExPECSC065_02714 FNJ67_10775 FV295_16190 HmCmsJML122_02218 NCTC10766_03778 NCTC7928_05955 NCTC8450_02317 NCTC9007_02951 NCTC9075_02834 SY51_11150 U12A_02105 U14A_02105] Protein/nucleic acid deglycase HchA (EC 3.1.2.-) (EC 3.5.1.-) (EC 3.5.1.124) (Maillard deglycase)
[Atk TK] Tachykinins (AmTRP) (Tachykinin-related peptide) [Cleaved into: APTGHQEMQ-amide (AmTRP1) (Tachykinin-related peptide 1) (TRP1); ALMGFQGVR-amide (AmTRP2) (Tachykinin-related peptide 2) (TRP2); Brain peptide NSIINDVKNELFPEDIN; APMGFQGMR-amide 1 (AmTRP3) (Tachykinin-related peptide 3-1) (TRP3-1); Brain peptide ASFDDEYY; APMGFQGMR-amide 2 (AmTRP3) (Tachykinin-related peptide 3-2) (TRP3-2); Brain peptide SLEEILDEIK; Brain peptide SLEEILDEI; Brain peptide EILDEI; TTRFQDSRSKDVYLIDYPEDY-amide (AmTAP1) (Tachykinin-associated peptide 1); Brain peptide VLSMDGYQNILDKKDELLGEWE; Brain peptide APMGFYGT; APMGFYGTR-amide (AmTRP4) (Tachykinin-related peptide 4) (TRP4); Brain peptide IILDALEELD; Brain peptide ILDALEELD; Brain peptide GVMDFQIGLQ; ARMGFHGMR-amide (AmTRP5) (Tachykinin-related peptide 5) (TRP5); SPFRYLGAR-amide (AmTRP6) (Tachykinin-related peptide 6) (TRP6); NPRWEFRGKFVGVR-amide (AmTRP7) (Tachykinin-related peptide 7) (TRP7)]
[Mmel1 Nep2 Nl1 Sep] Membrane metallo-endopeptidase-like 1 (EC 3.4.24.11) (NEP2(m)) (Neprilysin II) (NEPII) (Neprilysin-2) (NEP2) (NL2) (Neprilysin-like 1) (NL-1) (Neprilysin-like peptidase) (NEPLP) (Soluble secreted endopeptidase) [Cleaved into: Membrane metallo-endopeptidase-like 1, soluble form (Neprilysin-2 secreted) (NEP2(s))]
[Ace Dcp1] Angiotensin-converting enzyme (ACE) (EC 3.2.1.-) (EC 3.4.15.1) (Dipeptidyl carboxypeptidase I) (Kininase II) (CD antigen CD143) [Cleaved into: Angiotensin-converting enzyme, soluble form]
[MMEL1 MELL1 MMEL2 NEP2] Membrane metallo-endopeptidase-like 1 (EC 3.4.24.11) (Membrane metallo-endopeptidase-like 2) (NEP2(m)) (Neprilysin II) (NEPII) (Neprilysin-2) (NEP2) (NL2) [Cleaved into: Membrane metallo-endopeptidase-like 1, soluble form (Neprilysin-2 secreted) (NEP2(s))]
[Gsk3b] Glycogen synthase kinase-3 beta (GSK-3 beta) (EC 2.7.11.26) (Factor A) (FA) (Serine/threonine-protein kinase GSK3B) (EC 2.7.11.1)

Bibliography :