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P06737

- PYGL_HUMAN

UniProt

P06737 - PYGL_HUMAN

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Protein

Glycogen phosphorylase, liver form

Gene

PYGL

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli

Functioni

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 activityi

((1->4)-alpha-D-glucosyl)(n) + phosphate = ((1->4)-alpha-D-glucosyl)(n-1) + alpha-D-glucose 1-phosphate.

Cofactori

Pyridoxal phosphate.

Enzyme regulationi

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.

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei76 – 761AMPBy similarity
Sitei109 – 1091Involved in the association of subunitsBy similarity
Sitei143 – 1431Involved in the association of subunitsBy similarity
Sitei156 – 1561May be involved in allosteric controlBy similarity

GO - Molecular functioni

  1. AMP binding Source: UniProtKB
  2. ATP binding Source: UniProtKB
  3. bile acid binding Source: UniProtKB
  4. drug binding Source: UniProtKB
  5. glucose binding Source: UniProtKB
  6. glycogen phosphorylase activity Source: UniProtKB
  7. protein homodimerization activity Source: UniProtKB
  8. purine nucleobase binding Source: UniProtKB
  9. pyridoxal phosphate binding Source: InterPro
  10. vitamin binding Source: UniProtKB

GO - Biological processi

  1. 5-phosphoribose 1-diphosphate biosynthetic process Source: Ensembl
  2. carbohydrate metabolic process Source: Reactome
  3. glucose homeostasis Source: UniProtKB
  4. glucose metabolic process Source: Reactome
  5. glycogen catabolic process Source: Reactome
  6. glycogen metabolic process Source: UniProtKB
  7. necroptotic process Source: Ensembl
  8. small molecule metabolic process Source: Reactome
Complete GO annotation...

Keywords - Molecular functioni

Glycosyltransferase, Transferase

Keywords - Biological processi

Carbohydrate metabolism, Glycogen metabolism

Keywords - Ligandi

Nucleotide-binding, Pyridoxal phosphate

Enzyme and pathway databases

BioCyciMetaCyc:HS02099-MONOMER.
ReactomeiREACT_1008. Glycogen breakdown (glycogenolysis).

Protein family/group databases

CAZyiGT35. Glycosyltransferase Family 35.

Names & Taxonomyi

Protein namesi
Recommended name:
Glycogen phosphorylase, liver form (EC:2.4.1.1)
Gene namesi
Name:PYGL
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640: Chromosome 14

Organism-specific databases

HGNCiHGNC:9725. PYGL.

Subcellular locationi

GO - Cellular componenti

  1. cytoplasm Source: HPA
  2. cytosol Source: Reactome
  3. extracellular vesicular exosome Source: UniProtKB
  4. plasma membrane Source: HPA
Complete GO annotation...

Pathology & Biotechi

Involvement in diseasei

Glycogen storage disease 6 (GSD6) [MIM:232700]: A metabolic disorder characterized by mild to moderate hypoglycemia, mild ketosis, growth retardation, and prominent hepatomegaly. Heart and skeletal muscle are not affected.1 Publication
Note: The disease is caused by mutations affecting the gene represented in this entry.
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti339 – 3391N → S in GSD6. 1 Publication
VAR_007908
Natural varianti377 – 3771N → K in GSD6. 1 Publication
VAR_007909

Keywords - Diseasei

Disease mutation, Glycogen storage disease

Organism-specific databases

MIMi232700. phenotype.
Orphaneti369. Glycogen storage disease due to liver glycogen phosphorylase deficiency.
PharmGKBiPA34068.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Initiator methioninei1 – 11Removed1 Publication
Chaini2 – 847846Glycogen phosphorylase, liver formPRO_0000188524Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei2 – 21N-acetylalanine1 Publication
Modified residuei15 – 151Phosphoserine; by PHK; in form phosphorylase A1 Publication
Modified residuei364 – 3641N6-succinyllysineBy similarity
Modified residuei681 – 6811N6-(pyridoxal phosphate)lysineBy similarity

Post-translational modificationi

Phosphorylation of Ser-15 converts phosphorylase B (unphosphorylated) to phosphorylase A.1 Publication

Keywords - PTMi

Acetylation, Phosphoprotein

Proteomic databases

MaxQBiP06737.
PaxDbiP06737.
PeptideAtlasiP06737.
PRIDEiP06737.

PTM databases

PhosphoSiteiP06737.

Expressioni

Gene expression databases

BgeeiP06737.
CleanExiHS_PYGL.
ExpressionAtlasiP06737. baseline and differential.
GenevestigatoriP06737.

Organism-specific databases

HPAiHPA000962.
HPA004119.

Interactioni

Subunit structurei

Homodimer. Dimers associate into a tetramer to form the enzymatically active phosphorylase A. Interacts with PPP1R3B By similarity.By similarity

Protein-protein interaction databases

BioGridi111794. 30 interactions.
IntActiP06737. 8 interactions.
MINTiMINT-1208599.
STRINGi9606.ENSP00000216392.

Structurei

Secondary structure

1
847
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Turni8 – 103
Helixi11 – 133
Beta strandi14 – 174
Helixi19 – 3820
Helixi44 – 463
Helixi49 – 6214
Helixi65 – 7814
Beta strandi82 – 865
Beta strandi90 – 934
Helixi96 – 1027
Helixi106 – 11510
Helixi120 – 1256
Beta strandi130 – 1356
Helixi136 – 15015
Beta strandi155 – 1606
Beta strandi168 – 1725
Beta strandi175 – 1795
Turni183 – 1864
Helixi195 – 1973
Beta strandi199 – 2046
Beta strandi206 – 2105
Beta strandi213 – 2186
Beta strandi220 – 23213
Beta strandi234 – 2374
Beta strandi239 – 24810
Helixi255 – 2606
Helixi263 – 2686
Helixi270 – 2745
Helixi275 – 2773
Helixi291 – 31424
Beta strandi315 – 3173
Beta strandi322 – 3254
Helixi327 – 3293
Helixi330 – 3334
Beta strandi334 – 3418
Turni342 – 3454
Helixi346 – 35611
Helixi362 – 37211
Beta strandi373 – 3764
Helixi382 – 3843
Beta strandi387 – 3893
Helixi390 – 3967
Helixi398 – 41821
Beta strandi419 – 4213
Helixi423 – 4297
Beta strandi431 – 4333
Beta strandi435 – 4373
Beta strandi439 – 4413
Helixi442 – 4487
Beta strandi451 – 4577
Helixi458 – 4669
Turni467 – 4693
Helixi470 – 4756
Helixi477 – 4793
Beta strandi480 – 4823
Helixi490 – 4956
Helixi498 – 50811
Helixi511 – 5133
Helixi516 – 52510
Helixi529 – 55325
Beta strandi554 – 5563
Beta strandi562 – 5698
Turni573 – 5764
Helixi577 – 59317
Beta strandi595 – 5973
Beta strandi602 – 6076
Helixi615 – 63319
Turni635 – 6373
Helixi638 – 6403
Beta strandi641 – 6466
Helixi651 – 6577
Helixi658 – 6603
Beta strandi662 – 6665
Turni670 – 6723
Helixi678 – 6847
Beta strandi688 – 6914
Helixi697 – 7048
Helixi706 – 7083
Beta strandi709 – 7113
Helixi716 – 72510
Helixi729 – 7357
Helixi737 – 74812
Turni749 – 7513
Turni756 – 7594
Helixi760 – 7689
Helixi774 – 79219
Helixi795 – 80612
Helixi810 – 8123
Helixi814 – 82411

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1EM6X-ray2.20A/B1-847[»]
1EXVX-ray2.40A/B1-847[»]
1FA9X-ray2.40A2-847[»]
1FC0X-ray2.40A/B2-847[»]
1L5QX-ray2.25A/B1-847[»]
1L5RX-ray2.10A/B1-847[»]
1L5SX-ray2.10A/B1-847[»]
1L7XX-ray2.30A/B1-847[»]
1XOIX-ray2.10A/B2-847[»]
2ATIX-ray1.90A/B2-847[»]
2QLLX-ray2.56A1-847[»]
2ZB2X-ray2.45A/B1-847[»]
3CEHX-ray2.80A/B24-832[»]
3CEJX-ray3.30A/B24-832[»]
3CEMX-ray2.47A/B24-832[»]
3DD1X-ray2.57A/B2-847[»]
3DDSX-ray1.80A/B2-847[»]
3DDWX-ray1.90A/B2-847[»]
ProteinModelPortaliP06737.
SMRiP06737. Positions 6-839.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP06737.

Family & Domainsi

Sequence similaritiesi

Belongs to the glycogen phosphorylase family.Curated

Phylogenomic databases

eggNOGiCOG0058.
GeneTreeiENSGT00390000016886.
HOVERGENiHBG006848.
InParanoidiP06737.
KOiK00688.
OMAiDLVNMLF.
PhylomeDBiP06737.
TreeFamiTF300309.

Family and domain databases

InterProiIPR011833. Glycg_phsphrylas.
IPR000811. Glyco_trans_35.
[Graphical view]
PANTHERiPTHR11468. PTHR11468. 1 hit.
PfamiPF00343. Phosphorylase. 1 hit.
[Graphical view]
PIRSFiPIRSF000460. Pprylas_GlgP. 1 hit.
TIGRFAMsiTIGR02093. P_ylase. 1 hit.
PROSITEiPS00102. PHOSPHORYLASE. 1 hit.
[Graphical view]

Sequences (2)i

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

This entry describes 2 isoformsi produced by alternative splicing. Align

Isoform 1 (identifier: P06737-1) [UniParc]FASTAAdd to Basket

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

« Hide

        10         20         30         40         50
MAKPLTDQEK RRQISIRGIV GVENVAELKK SFNRHLHFTL VKDRNVATTR
60 70 80 90 100
DYYFALAHTV RDHLVGRWIR TQQHYYDKCP KRVYYLSLEF YMGRTLQNTM
110 120 130 140 150
INLGLQNACD EAIYQLGLDI EELEEIEEDA GLGNGGLGRL AACFLDSMAT
160 170 180 190 200
LGLAAYGYGI RYEYGIFNQK IRDGWQVEEA DDWLRYGNPW EKSRPEFMLP
210 220 230 240 250
VHFYGKVEHT NTGTKWIDTQ VVLALPYDTP VPGYMNNTVN TMRLWSARAP
260 270 280 290 300
NDFNLRDFNV GDYIQAVLDR NLAENISRVL YPNDNFFEGK ELRLKQEYFV
310 320 330 340 350
VAATLQDIIR RFKASKFGST RGAGTVFDAF PDQVAIQLND THPALAIPEL
360 370 380 390 400
MRIFVDIEKL PWSKAWELTQ KTFAYTNHTV LPEALERWPV DLVEKLLPRH
410 420 430 440 450
LEIIYEINQK HLDRIVALFP KDVDRLRRMS LIEEEGSKRI NMAHLCIVGS
460 470 480 490 500
HAVNGVAKIH SDIVKTKVFK DFSELEPDKF QNKTNGITPR RWLLLCNPGL
510 520 530 540 550
AELIAEKIGE DYVKDLSQLT KLHSFLGDDV FLRELAKVKQ ENKLKFSQFL
560 570 580 590 600
ETEYKVKINP SSMFDVQVKR IHEYKRQLLN CLHVITMYNR IKKDPKKLFV
610 620 630 640 650
PRTVIIGGKA APGYHMAKMI IKLITSVADV VNNDPMVGSK LKVIFLENYR
660 670 680 690 700
VSLAEKVIPA TDLSEQISTA GTEASGTGNM KFMLNGALTI GTMDGANVEM
710 720 730 740 750
AEEAGEENLF IFGMRIDDVA ALDKKGYEAK EYYEALPELK LVIDQIDNGF
760 770 780 790 800
FSPKQPDLFK DIINMLFYHD RFKVFADYEA YVKCQDKVSQ LYMNPKAWNT
810 820 830 840
MVLKNIAASG KFSSDRTIKE YAQNIWNVEP SDLKISLSNE SNKVNGN
Length:847
Mass (Da):97,149
Last modified:January 23, 2007 - v4
Checksum:i74017E8125FB5735
GO
Isoform 2 (identifier: P06737-2) [UniParc]FASTAAdd to Basket

The sequence of this isoform differs from the canonical sequence as follows:
     82-115: Missing.

Note: No experimental confirmation available.

Show »
Length:813
Mass (Da):93,134
Checksum:i40B7DB0528A64AAA
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti2 – 32AK → GE in AAA52577. (PubMed:2877458)Curated
Sequence conflicti2 – 32AK → GE in AAC18079. (PubMed:9536091)Curated
Sequence conflicti83 – 831V → E in AAA52577. (PubMed:2877458)Curated
Sequence conflicti323 – 3231A → Q in AAA52577. (PubMed:2877458)Curated
Sequence conflicti344 – 3452AL → RI in AAA52577. (PubMed:2877458)Curated
Sequence conflicti369 – 3691T → N in AAA52577. (PubMed:2877458)Curated
Sequence conflicti369 – 3691T → N in AAC18079. (PubMed:9536091)Curated
Sequence conflicti570 – 5701R → S in AAC17450. 1 PublicationCurated
Sequence conflicti683 – 6831Missing in AAH09895. (PubMed:15489334)Curated
Sequence conflicti715 – 7151R → G in BAG62279. (PubMed:14702039)Curated

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti222 – 2221V → I.1 Publication
Corresponds to variant rs946616 [ dbSNP | Ensembl ].
VAR_007907
Natural varianti231 – 2311V → E.
Corresponds to variant rs1042195 [ dbSNP | Ensembl ].
VAR_013095
Natural varianti339 – 3391N → S in GSD6. 1 Publication
VAR_007908
Natural varianti377 – 3771N → K in GSD6. 1 Publication
VAR_007909
Natural varianti425 – 4251R → P.1 Publication
Corresponds to variant rs2228499 [ dbSNP | Ensembl ].
VAR_034425
Natural varianti698 – 6981V → G.
Corresponds to variant rs35831273 [ dbSNP | Ensembl ].
VAR_034426
Natural varianti715 – 7151R → S.
Corresponds to variant rs1042210 [ dbSNP | Ensembl ].
VAR_013096
Natural varianti806 – 8061I → L.
Corresponds to variant rs34313873 [ dbSNP | Ensembl ].
VAR_034427
Natural varianti845 – 8451N → S.1 Publication
Corresponds to variant rs78558135 [ dbSNP | Ensembl ].
VAR_069054

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei82 – 11534Missing in isoform 2. 1 PublicationVSP_045339Add
BLAST

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
M14636 mRNA. Translation: AAA52577.1.
AF066858 mRNA. Translation: AAC17450.1.
AF046798
, AF046787, AF046788, AF046789, AF046790, AF046791, AF046792, AF046793, AF046794, AF046795, AF046796, AF046797 Genomic DNA. Translation: AAC18079.1.
AF046785 mRNA. Translation: AAC23504.1.
Y15233 mRNA. Translation: CAA75517.1.
AK300580 mRNA. Translation: BAG62279.1.
AL358334 Genomic DNA. No translation available.
CH471078 Genomic DNA. Translation: EAW65685.1.
BC009895 mRNA. Translation: AAH09895.3.
BC082229 mRNA. Translation: AAH82229.2.
BC095850 mRNA. Translation: AAH95850.2.
BC110791 mRNA. Translation: AAI10792.2.
M36807 mRNA. Translation: AAA35906.1.
CCDSiCCDS32080.1. [P06737-1]
CCDS53894.1. [P06737-2]
PIRiA25518.
RefSeqiNP_001157412.1. NM_001163940.1. [P06737-2]
NP_002854.3. NM_002863.4. [P06737-1]
UniGeneiHs.282417.

Genome annotation databases

EnsembliENST00000216392; ENSP00000216392; ENSG00000100504. [P06737-1]
ENST00000544180; ENSP00000443787; ENSG00000100504. [P06737-2]
GeneIDi5836.
KEGGihsa:5836.
UCSCiuc001wyu.3. human. [P06737-1]

Polymorphism databases

DMDMi6648082.

Keywords - Coding sequence diversityi

Alternative splicing, Polymorphism

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
M14636 mRNA. Translation: AAA52577.1 .
AF066858 mRNA. Translation: AAC17450.1 .
AF046798
, AF046787 , AF046788 , AF046789 , AF046790 , AF046791 , AF046792 , AF046793 , AF046794 , AF046795 , AF046796 , AF046797 Genomic DNA. Translation: AAC18079.1 .
AF046785 mRNA. Translation: AAC23504.1 .
Y15233 mRNA. Translation: CAA75517.1 .
AK300580 mRNA. Translation: BAG62279.1 .
AL358334 Genomic DNA. No translation available.
CH471078 Genomic DNA. Translation: EAW65685.1 .
BC009895 mRNA. Translation: AAH09895.3 .
BC082229 mRNA. Translation: AAH82229.2 .
BC095850 mRNA. Translation: AAH95850.2 .
BC110791 mRNA. Translation: AAI10792.2 .
M36807 mRNA. Translation: AAA35906.1 .
CCDSi CCDS32080.1. [P06737-1 ]
CCDS53894.1. [P06737-2 ]
PIRi A25518.
RefSeqi NP_001157412.1. NM_001163940.1. [P06737-2 ]
NP_002854.3. NM_002863.4. [P06737-1 ]
UniGenei Hs.282417.

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
1EM6 X-ray 2.20 A/B 1-847 [» ]
1EXV X-ray 2.40 A/B 1-847 [» ]
1FA9 X-ray 2.40 A 2-847 [» ]
1FC0 X-ray 2.40 A/B 2-847 [» ]
1L5Q X-ray 2.25 A/B 1-847 [» ]
1L5R X-ray 2.10 A/B 1-847 [» ]
1L5S X-ray 2.10 A/B 1-847 [» ]
1L7X X-ray 2.30 A/B 1-847 [» ]
1XOI X-ray 2.10 A/B 2-847 [» ]
2ATI X-ray 1.90 A/B 2-847 [» ]
2QLL X-ray 2.56 A 1-847 [» ]
2ZB2 X-ray 2.45 A/B 1-847 [» ]
3CEH X-ray 2.80 A/B 24-832 [» ]
3CEJ X-ray 3.30 A/B 24-832 [» ]
3CEM X-ray 2.47 A/B 24-832 [» ]
3DD1 X-ray 2.57 A/B 2-847 [» ]
3DDS X-ray 1.80 A/B 2-847 [» ]
3DDW X-ray 1.90 A/B 2-847 [» ]
ProteinModelPortali P06737.
SMRi P06737. Positions 6-839.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 111794. 30 interactions.
IntActi P06737. 8 interactions.
MINTi MINT-1208599.
STRINGi 9606.ENSP00000216392.

Chemistry

BindingDBi P06737.
ChEMBLi CHEMBL2568.
DrugBanki DB00131. Adenosine monophosphate.

Protein family/group databases

CAZyi GT35. Glycosyltransferase Family 35.

PTM databases

PhosphoSitei P06737.

Polymorphism databases

DMDMi 6648082.

Proteomic databases

MaxQBi P06737.
PaxDbi P06737.
PeptideAtlasi P06737.
PRIDEi P06737.

Protocols and materials databases

DNASUi 5836.
Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENST00000216392 ; ENSP00000216392 ; ENSG00000100504 . [P06737-1 ]
ENST00000544180 ; ENSP00000443787 ; ENSG00000100504 . [P06737-2 ]
GeneIDi 5836.
KEGGi hsa:5836.
UCSCi uc001wyu.3. human. [P06737-1 ]

Organism-specific databases

CTDi 5836.
GeneCardsi GC14M051324.
HGNCi HGNC:9725. PYGL.
HPAi HPA000962.
HPA004119.
MIMi 232700. phenotype.
613741. gene.
neXtProti NX_P06737.
Orphaneti 369. Glycogen storage disease due to liver glycogen phosphorylase deficiency.
PharmGKBi PA34068.
GenAtlasi Search...

Phylogenomic databases

eggNOGi COG0058.
GeneTreei ENSGT00390000016886.
HOVERGENi HBG006848.
InParanoidi P06737.
KOi K00688.
OMAi DLVNMLF.
PhylomeDBi P06737.
TreeFami TF300309.

Enzyme and pathway databases

BioCyci MetaCyc:HS02099-MONOMER.
Reactomei REACT_1008. Glycogen breakdown (glycogenolysis).

Miscellaneous databases

ChiTaRSi PYGL. human.
EvolutionaryTracei P06737.
GenomeRNAii 5836.
NextBioi 22742.
PROi P06737.
SOURCEi Search...

Gene expression databases

Bgeei P06737.
CleanExi HS_PYGL.
ExpressionAtlasi P06737. baseline and differential.
Genevestigatori P06737.

Family and domain databases

InterProi IPR011833. Glycg_phsphrylas.
IPR000811. Glyco_trans_35.
[Graphical view ]
PANTHERi PTHR11468. PTHR11468. 1 hit.
Pfami PF00343. Phosphorylase. 1 hit.
[Graphical view ]
PIRSFi PIRSF000460. Pprylas_GlgP. 1 hit.
TIGRFAMsi TIGR02093. P_ylase. 1 hit.
PROSITEi PS00102. PHOSPHORYLASE. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  1. "Sequence analysis of the cDNA encoding human liver glycogen phosphorylase reveals tissue-specific codon usage."
    Newgard C.B., Nakano K., Hwang P.K., Fletterick R.J.
    Proc. Natl. Acad. Sci. U.S.A. 83:8132-8136(1986) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), VARIANT PRO-425.
    Tissue: Liver.
  2. Carty M.D., Clancy Y.C., Soeller W.C.
    Submitted (MAY-1998) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
    Tissue: Liver.
  3. "Identification of a mutation in liver glycogen phosphorylase in glycogen storage disease type VI."
    Chang S., Rosenberg M.J., Morton H., Francomano C.A., Biesecker L.G.
    Hum. Mol. Genet. 7:865-870(1998) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
  4. "Mutations in the liver glycogen phosphorylase gene 'PYGL' underlying glycogenosis type VI."
    Burwinkel B., Bakker H.D., Herschkovitz E., Moses S.W., Shin Y.S., Kilimann M.W.
    Am. J. Hum. Genet. 62:785-791(1998) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), VARIANTS GSD6 SER-339 AND LYS-377, VARIANT ILE-222.
    Tissue: Blood.
  5. "Complete sequencing and characterization of 21,243 full-length human cDNAs."
    Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.
    , Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.
    Nat. Genet. 36:40-45(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2), VARIANT SER-845.
  6. "The DNA sequence and analysis of human chromosome 14."
    Heilig R., Eckenberg R., Petit J.-L., Fonknechten N., Da Silva C., Cattolico L., Levy M., Barbe V., De Berardinis V., Ureta-Vidal A., Pelletier E., Vico V., Anthouard V., Rowen L., Madan A., Qin S., Sun H., Du H.
    , Pepin K., Artiguenave F., Robert C., Cruaud C., Bruels T., Jaillon O., Friedlander L., Samson G., Brottier P., Cure S., Segurens B., Aniere F., Samain S., Crespeau H., Abbasi N., Aiach N., Boscus D., Dickhoff R., Dors M., Dubois I., Friedman C., Gouyvenoux M., James R., Madan A., Mairey-Estrada B., Mangenot S., Martins N., Menard M., Oztas S., Ratcliffe A., Shaffer T., Trask B., Vacherie B., Bellemere C., Belser C., Besnard-Gonnet M., Bartol-Mavel D., Boutard M., Briez-Silla S., Combette S., Dufosse-Laurent V., Ferron C., Lechaplais C., Louesse C., Muselet D., Magdelenat G., Pateau E., Petit E., Sirvain-Trukniewicz P., Trybou A., Vega-Czarny N., Bataille E., Bluet E., Bordelais I., Dubois M., Dumont C., Guerin T., Haffray S., Hammadi R., Muanga J., Pellouin V., Robert D., Wunderle E., Gauguet G., Roy A., Sainte-Marthe L., Verdier J., Verdier-Discala C., Hillier L.W., Fulton L., McPherson J., Matsuda F., Wilson R., Scarpelli C., Gyapay G., Wincker P., Saurin W., Quetier F., Waterston R., Hood L., Weissenbach J.
    Nature 421:601-607(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  7. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  8. "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
    The MGC Project Team
    Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
    Tissue: Placenta, Skin and Uterus.
  9. "McArdle's & Hers' diseases: glycogen phosphorylase transcriptional expression in human tissues."
    Gorin F.A., Mullinax R.L., Ignacio P.C., Neve R.L., Kurnit D.M.
    J. Neurogenet. 4:293-308(1987) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 482-847 (ISOFORM 1).
    Tissue: Fetal brain.
  10. "Lys-N and trypsin cover complementary parts of the phosphoproteome in a refined SCX-based approach."
    Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J., Mohammed S.
    Anal. Chem. 81:4493-4501(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS], CLEAVAGE OF INITIATOR METHIONINE [LARGE SCALE ANALYSIS].
  11. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  12. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  13. Cited for: X-RAY CRYSTALLOGRAPHY (2.2 ANGSTROMS).
  14. "Activation of human liver glycogen phosphorylase by alteration of the secondary structure and packing of the catalytic core."
    Rath V.L., Ammirati M., LeMotte P.K., Fennell K.F., Mansour M.N., Danley D.E., Hynes T.R., Schulte G.K., Wasilko D.J., Pandit J.
    Mol. Cell 6:139-148(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.4 ANGSTROMS), PHOSPHORYLATION AT SER-15.
  15. "Structure-activity analysis of the purine binding site of human liver glycogen phosphorylase."
    Ekstrom J.L., Pauly T.A., Carty M.D., Soeller W.C., Culp J., Danley D.E., Hoover D.J., Treadway J.L., Gibbs E.M., Fletterick R.J., Day Y.S., Myszka D.G., Rath V.L.
    Chem. Biol. 9:915-924(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.25 ANGSTROMS).

Entry informationi

Entry nameiPYGL_HUMAN
AccessioniPrimary (citable) accession number: P06737
Secondary accession number(s): A6NDQ4
, B4DUB7, F5H816, O60567, O60752, O60913, Q501V9, Q641R5, Q96G82
Entry historyi
Integrated into UniProtKB/Swiss-Prot: January 1, 1988
Last sequence update: January 23, 2007
Last modified: October 29, 2014
This is version 179 of the entry and version 4 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

Miscellaneousi

Keywords - Technical termi

3D-structure, Allosteric enzyme, Complete proteome, Reference proteome

Documents

  1. Human chromosome 14
    Human chromosome 14: entries, gene names and cross-references to MIM
  2. Human entries with polymorphisms or disease mutations
    List of human entries with polymorphisms or disease mutations
  3. Human polymorphisms and disease mutations
    Index of human polymorphisms and disease mutations
  4. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  5. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  6. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3