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Protein

Glycogen phosphorylase, brain form

Gene

PYGB

Organism
Homo sapiens (Human)
Status
Reviewed-Annotation score: 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

Enzyme regulationi

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.

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Binding sitei76AMPBy similarity1
Sitei109Involved in the association of subunitsBy similarity1
Sitei143Involved in the association of subunitsBy similarity1
Sitei156May be involved in allosteric controlBy similarity1

GO - Molecular functioni

  • glycogen phosphorylase activity Source: UniProtKB
  • pyridoxal phosphate binding Source: GO_Central

GO - Biological processi

  • glycogen catabolic process Source: UniProtKB
Complete GO annotation...

Keywords - Molecular functioni

Glycosyltransferase, Transferase

Keywords - Biological processi

Carbohydrate metabolism, Glycogen metabolism

Keywords - Ligandi

Pyridoxal phosphate

Enzyme and pathway databases

BioCyciMetaCyc:HS02178-MONOMER.
ZFISH:HS02178-MONOMER.
ReactomeiR-HSA-6798695. Neutrophil degranulation.
R-HSA-70221. Glycogen breakdown (glycogenolysis).

Protein family/group databases

CAZyiGT35. Glycosyltransferase Family 35.

Names & Taxonomyi

Protein namesi
Recommended name:
Glycogen phosphorylase, brain form (EC:2.4.1.1)
Gene namesi
Name:PYGB
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
Proteomesi
  • UP000005640 Componenti: Chromosome 20

Organism-specific databases

HGNCiHGNC:9723. PYGB.

Subcellular locationi

GO - Cellular componenti

  • cytoplasm Source: UniProtKB
  • extracellular exosome Source: UniProtKB
  • membrane Source: UniProtKB
Complete GO annotation...

Pathology & Biotechi

Organism-specific databases

DisGeNETi5834.
OpenTargetsiENSG00000100994.
PharmGKBiPA34066.

Chemistry databases

ChEMBLiCHEMBL3856.

Polymorphism and mutation databases

BioMutaiPYGB.
DMDMi20178317.

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Initiator methionineiRemovedCombined sources2 Publications
ChainiPRO_00001885352 – 843Glycogen phosphorylase, brain formAdd BLAST842

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei2N-acetylalanineCombined sources1 Publication1
Modified residuei15Phosphoserine; by PHK; in form phosphorylase ABy similarity1
Modified residuei197PhosphotyrosineBy similarity1
Modified residuei473PhosphotyrosineBy similarity1
Modified residuei681N6-(pyridoxal phosphate)lysineBy similarity1

Post-translational modificationi

Phosphorylation of Ser-15 converts phosphorylase B (unphosphorylated) to phosphorylase A.By similarity

Keywords - PTMi

Acetylation, Phosphoprotein

Proteomic databases

EPDiP11216.
MaxQBiP11216.
PaxDbiP11216.
PeptideAtlasiP11216.
PRIDEiP11216.

PTM databases

iPTMnetiP11216.
PhosphoSitePlusiP11216.
SwissPalmiP11216.

Expressioni

Gene expression databases

BgeeiENSG00000100994.
CleanExiHS_PYGB.
ExpressionAtlasiP11216. baseline and differential.
GenevisibleiP11216. HS.

Organism-specific databases

HPAiHPA031067.

Interactioni

Subunit structurei

Homodimer. Dimers associate into a tetramer to form the enzymatically active phosphorylase A.

Binary interactionsi

WithEntry#Exp.IntActNotes
PYGLP067375EBI-1047231,EBI-2511865
SIAH1Q8IUQ43EBI-1047231,EBI-747107

Protein-protein interaction databases

BioGridi111792. 50 interactors.
IntActiP11216. 7 interactors.
STRINGi9606.ENSP00000216962.

Chemistry databases

BindingDBiP11216.

Structurei

Secondary structure

1843
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Helixi23 – 38Combined sources16
Turni44 – 46Combined sources3
Helixi49 – 78Combined sources30
Beta strandi82 – 86Combined sources5
Helixi96 – 102Combined sources7
Helixi106 – 115Combined sources10
Helixi120 – 126Combined sources7
Beta strandi130 – 132Combined sources3
Helixi136 – 150Combined sources15
Beta strandi155 – 160Combined sources6
Beta strandi168 – 172Combined sources5
Beta strandi175 – 179Combined sources5
Turni183 – 186Combined sources4
Helixi195 – 197Combined sources3
Beta strandi199 – 210Combined sources12
Beta strandi213 – 232Combined sources20
Beta strandi234 – 237Combined sources4
Beta strandi239 – 248Combined sources10
Helixi260 – 274Combined sources15
Helixi275 – 277Combined sources3
Beta strandi279 – 281Combined sources3
Helixi290 – 313Combined sources24
Helixi326 – 329Combined sources4
Helixi330 – 333Combined sources4
Beta strandi334 – 341Combined sources8
Helixi342 – 345Combined sources4
Helixi346 – 356Combined sources11
Helixi362 – 372Combined sources11
Beta strandi373 – 376Combined sources4
Helixi382 – 384Combined sources3
Beta strandi387 – 389Combined sources3
Helixi390 – 396Combined sources7
Helixi398 – 418Combined sources21
Helixi423 – 429Combined sources7
Beta strandi431 – 433Combined sources3
Beta strandi435 – 437Combined sources3
Beta strandi439 – 441Combined sources3
Helixi442 – 448Combined sources7
Beta strandi453 – 457Combined sources5
Helixi458 – 466Combined sources9
Turni467 – 469Combined sources3
Helixi470 – 475Combined sources6
Helixi477 – 479Combined sources3
Beta strandi480 – 482Combined sources3
Helixi490 – 495Combined sources6
Helixi498 – 508Combined sources11
Helixi511 – 513Combined sources3
Helixi516 – 526Combined sources11
Helixi529 – 554Combined sources26
Beta strandi562 – 569Combined sources8
Turni573 – 576Combined sources4
Helixi577 – 593Combined sources17
Beta strandi602 – 607Combined sources6
Helixi615 – 632Combined sources18
Turni635 – 637Combined sources3
Helixi638 – 640Combined sources3
Beta strandi641 – 648Combined sources8
Helixi651 – 657Combined sources7
Helixi658 – 660Combined sources3
Beta strandi662 – 666Combined sources5
Turni670 – 672Combined sources3
Helixi678 – 684Combined sources7
Beta strandi688 – 691Combined sources4
Helixi696 – 704Combined sources9
Helixi706 – 708Combined sources3
Beta strandi709 – 711Combined sources3
Helixi716 – 725Combined sources10
Helixi730 – 734Combined sources5
Helixi737 – 748Combined sources12
Turni749 – 751Combined sources3
Beta strandi753 – 755Combined sources3
Turni756 – 759Combined sources4
Helixi760 – 768Combined sources9
Helixi774 – 792Combined sources19
Helixi795 – 807Combined sources13
Helixi810 – 812Combined sources3
Helixi814 – 824Combined sources11

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
5IKOX-ray2.50A1-843[»]
5IKPX-ray3.40A1-843[»]
ProteinModelPortaliP11216.
SMRiP11216.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Belongs to the glycogen phosphorylase family.Curated

Phylogenomic databases

eggNOGiKOG2099. Eukaryota.
COG0058. LUCA.
GeneTreeiENSGT00390000016886.
HOVERGENiHBG006848.
InParanoidiP11216.
KOiK00688.
OMAiATYEYYN.
OrthoDBiEOG091G03RB.
PhylomeDBiP11216.
TreeFamiTF300309.

Family and domain databases

CDDicd04300. GT1_Glycogen_Phosphorylase. 1 hit.
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]

Sequencei

Sequence statusi: Complete.

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

P11216-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MAKPLTDSEK RKQISVRGLA GLGDVAEVRK SFNRHLHFTL VKDRNVATPR
60 70 80 90 100
DYFFALAHTV RDHLVGRWIR TQQHYYERDP KRIYYLSLEF YMGRTLQNTM
110 120 130 140 150
VNLGLQNACD EAIYQLGLDL EELEEIEEDA GLGNGGLGRL AACFLDSMAT
160 170 180 190 200
LGLAAYGYGI RYEFGIFNQK IVNGWQVEEA DDWLRYGNPW EKARPEYMLP
210 220 230 240 250
VHFYGRVEHT PDGVKWLDTQ VVLAMPYDTP VPGYKNNTVN TMRLWSAKAP
260 270 280 290 300
NDFKLQDFNV GDYIEAVLDR NLAENISRVL YPNDNFFEGK ELRLKQEYFV
310 320 330 340 350
VAATLQDIIR RFKSSKFGCR DPVRTCFETF PDKVAIQLND THPALSIPEL
360 370 380 390 400
MRILVDVEKV DWDKAWEITK KTCAYTNHTV LPEALERWPV SMFEKLLPRH
410 420 430 440 450
LEIIYAINQR HLDHVAALFP GDVDRLRRMS VIEEGDCKRI NMAHLCVIGS
460 470 480 490 500
HAVNGVARIH SEIVKQSVFK DFYELEPEKF QNKTNGITPR RWLLLCNPGL
510 520 530 540 550
ADTIVEKIGE EFLTDLSQLK KLLPLVSDEV FIRDVAKVKQ ENKLKFSAFL
560 570 580 590 600
EKEYKVKINP SSMFDVHVKR IHEYKRQLLN CLHVVTLYNR IKRDPAKAFV
610 620 630 640 650
PRTVMIGGKA APGYHMAKLI IKLVTSIGDV VNHDPVVGDR LKVIFLENYR
660 670 680 690 700
VSLAEKVIPA ADLSQQISTA GTEASGTGNM KFMLNGALTI GTMDGANVEM
710 720 730 740 750
AEEAGAENLF IFGLRVEDVE ALDRKGYNAR EYYDHLPELK QAVDQISSGF
760 770 780 790 800
FSPKEPDCFK DIVNMLMHHD RFKVFADYEA YMQCQAQVDQ LYRNPKEWTK
810 820 830 840
KVIRNIACSG KFSSDRTITE YAREIWGVEP SDLQIPPPNI PRD
Length:843
Mass (Da):96,696
Last modified:January 23, 2007 - v5
Checksum:i810BFAD3002CACB0
GO

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sequence conflicti2 – 3AK → GE (PubMed:3346228).Curated2
Sequence conflicti2 – 3AK → GE (PubMed:2615594).Curated2
Sequence conflicti248K → R in AAA59597 (PubMed:3346228).Curated1
Sequence conflicti302A → G in AAA59597 (PubMed:3346228).Curated1
Sequence conflicti835 – 843IPPPNIPRD → LQHLPHPEWESGGATCWAPP ELCTHLAMY in AAA59597 (PubMed:3346228).Curated9

Natural variant

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Natural variantiVAR_034428303A → S.Corresponds to variant rs2228976dbSNPEnsembl.1
Natural variantiVAR_020212502D → N.Corresponds to variant rs2227891dbSNPEnsembl.1

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
J03544 mRNA. Translation: AAA59597.1.
U47025 mRNA. Translation: AAB60395.1.
AL121772 Genomic DNA. Translation: CAC00661.1.
BC017045 mRNA. Translation: AAH17045.1.
BC030795 mRNA. Translation: AAH30795.1.
CCDSiCCDS13171.1.
PIRiA40138.
RefSeqiNP_002853.2. NM_002862.3.
UniGeneiHs.368157.

Genome annotation databases

EnsembliENST00000216962; ENSP00000216962; ENSG00000100994.
GeneIDi5834.
KEGGihsa:5834.
UCSCiuc002wup.4. human.

Keywords - Coding sequence diversityi

Polymorphism

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
J03544 mRNA. Translation: AAA59597.1.
U47025 mRNA. Translation: AAB60395.1.
AL121772 Genomic DNA. Translation: CAC00661.1.
BC017045 mRNA. Translation: AAH17045.1.
BC030795 mRNA. Translation: AAH30795.1.
CCDSiCCDS13171.1.
PIRiA40138.
RefSeqiNP_002853.2. NM_002862.3.
UniGeneiHs.368157.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
5IKOX-ray2.50A1-843[»]
5IKPX-ray3.40A1-843[»]
ProteinModelPortaliP11216.
SMRiP11216.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi111792. 50 interactors.
IntActiP11216. 7 interactors.
STRINGi9606.ENSP00000216962.

Chemistry databases

BindingDBiP11216.
ChEMBLiCHEMBL3856.

Protein family/group databases

CAZyiGT35. Glycosyltransferase Family 35.

PTM databases

iPTMnetiP11216.
PhosphoSitePlusiP11216.
SwissPalmiP11216.

Polymorphism and mutation databases

BioMutaiPYGB.
DMDMi20178317.

Proteomic databases

EPDiP11216.
MaxQBiP11216.
PaxDbiP11216.
PeptideAtlasiP11216.
PRIDEiP11216.

Protocols and materials databases

DNASUi5834.
Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000216962; ENSP00000216962; ENSG00000100994.
GeneIDi5834.
KEGGihsa:5834.
UCSCiuc002wup.4. human.

Organism-specific databases

CTDi5834.
DisGeNETi5834.
GeneCardsiPYGB.
HGNCiHGNC:9723. PYGB.
HPAiHPA031067.
MIMi138550. gene.
neXtProtiNX_P11216.
OpenTargetsiENSG00000100994.
PharmGKBiPA34066.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiKOG2099. Eukaryota.
COG0058. LUCA.
GeneTreeiENSGT00390000016886.
HOVERGENiHBG006848.
InParanoidiP11216.
KOiK00688.
OMAiATYEYYN.
OrthoDBiEOG091G03RB.
PhylomeDBiP11216.
TreeFamiTF300309.

Enzyme and pathway databases

BioCyciMetaCyc:HS02178-MONOMER.
ZFISH:HS02178-MONOMER.
ReactomeiR-HSA-6798695. Neutrophil degranulation.
R-HSA-70221. Glycogen breakdown (glycogenolysis).

Miscellaneous databases

ChiTaRSiPYGB. human.
GenomeRNAii5834.
PROiP11216.
SOURCEiSearch...

Gene expression databases

BgeeiENSG00000100994.
CleanExiHS_PYGB.
ExpressionAtlasiP11216. baseline and differential.
GenevisibleiP11216. HS.

Family and domain databases

CDDicd04300. GT1_Glycogen_Phosphorylase. 1 hit.
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]
ProtoNetiSearch...

Entry informationi

Entry nameiPYGB_HUMAN
AccessioniPrimary (citable) accession number: P11216
Secondary accession number(s): Q96AK1, Q9NPX8
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 1, 1989
Last sequence update: January 23, 2007
Last modified: November 30, 2016
This is version 192 of the entry and version 5 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, Direct protein sequencing, Reference proteome

Documents

  1. Human chromosome 20
    Human chromosome 20: 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

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.