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Protein

Glycogen phosphorylase, brain form

Gene

Pygb

Organism
Rattus norvegicus (Rat)
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 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

  • carbohydrate binding Source: RGD
  • drug binding Source: RGD
  • glycogen phosphorylase activity Source: RGD
  • protein homodimerization activity Source: RGD
  • pyridoxal phosphate binding Source: GO_Central

GO - Biological processi

  • glycogen catabolic process Source: RGD
  • glycogen metabolic process Source: RGD
Complete GO annotation...

Keywords - Molecular functioni

Glycosyltransferase, Transferase

Keywords - Biological processi

Carbohydrate metabolism, Glycogen metabolism

Keywords - Ligandi

Pyridoxal phosphate

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
OrganismiRattus norvegicus (Rat)
Taxonomic identifieri10116 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeRattus
Proteomesi
  • UP000002494 Componenti: Unplaced

Organism-specific databases

RGDi3460. Pygb.

Subcellular locationi

GO - Cellular componenti

  • axon Source: RGD
  • cytoplasm Source: GO_Central
Complete GO annotation...

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Initiator methionineiRemovedBy similarity
Chaini2 – ›838›837Glycogen phosphorylase, brain formPRO_0000188538Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei2 – 21N-acetylalanineBy similarity
Modified residuei15 – 151PhosphoserineCombined sources
Modified residuei197 – 1971PhosphotyrosineBy similarity
Modified residuei473 – 4731PhosphotyrosineBy similarity
Modified residuei524 – 5241PhosphoserineCombined sources
Modified residuei681 – 6811N6-(pyridoxal phosphate)lysineBy similarity

Post-translational modificationi

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

Keywords - PTMi

Acetylation, Phosphoprotein

Proteomic databases

PaxDbiP53534.
PeptideAtlasiP53534.
PRIDEiP53534.

2D gel databases

World-2DPAGE0004:P53534.

PTM databases

iPTMnetiP53534.

Interactioni

Subunit structurei

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

GO - Molecular functioni

  • protein homodimerization activity Source: RGD

Protein-protein interaction databases

BioGridi247767. 2 interactions.
IntActiP53534. 2 interactions.
STRINGi10116.ENSRNOP00000010158.

Structurei

3D structure databases

ProteinModelPortaliP53534.
SMRiP53534. Positions 14-838.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Belongs to the glycogen phosphorylase family.Curated

Phylogenomic databases

eggNOGiKOG2099. Eukaryota.
COG0058. LUCA.
HOGENOMiHOG000278444.
HOVERGENiHBG006848.
InParanoidiP53534.
KOiK00688.

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]

Sequencei

Sequence statusi: Fragment.

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

P53534-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MAKPLTDSER QKQISVRGIA GLGDVAEVRK SFNRHLHFTL VKDRNVATPR
60 70 80 90 100
DYFFALAHTV RDHLVGRWIR TQQHYYERDP KRIYYLSLEF YMGRTLQNTM
110 120 130 140 150
VNLGLQTACD EATYQLGLDL EELEEIEEDA GLGNGGLGRL AACFLDSMAT
160 170 180 190 200
LGLAAYGYGI RYEFGIFNQK IVNGWQVEEA DDWLRYGNPW EKARPEYMLP
210 220 230 240 250
VHFYGRVEHT PNGVLWLDTQ VVLAMPYDTP VPGYKNNTVN TMRLWSAKAP
260 270 280 290 300
NDFKLKDFNV 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
AEIIVERIGE GFLTDLSQLK KLLSLVDDEA FIRDVAKVKQ ENKLKFSAQL
560 570 580 590 600
EKEYKVKINP CSMFDVHVKR IHEYKRQLLN CLHIITLYNR IKKDPTKTFV
610 620 630 640 650
PRTVMIGGKA APGYHMAKMI IKLVTSIGDV VNHDPVVGDR LRVIFLENYR
660 670 680 690 700
VSLAEKVIPA ADLSQQISTA GTEASGTGNM KFMLNGALTI GTMDGANVEM
710 720 730 740 750
AEEAGEENLF IFGMRVEDVE ALDQKGYNAQ EFYERLPELR QAVDQISSGF
760 770 780 790 800
FSPKDPDCFK DVVNMLMYHD RFKVFADYEA YIQCQAQVDH LYRNPKDWTK
810 820 830
KVIRNIACSG KFSSDRTITE YAREIWGVEP SDLQIPPP
Length:838
Mass (Da):96,174
Last modified:January 23, 2007 - v3
Checksum:i281C4BBE1EE08240
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti589 – 5891N → K in AAA40815 (PubMed:3209063).Curated
Non-terminal residuei838 – 8381

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
L10668 mRNA. Translation: AAA41252.1.
M27726 mRNA. Translation: AAA40815.1.
PIRiS37300.
RefSeqiNP_037320.1. NM_013188.1.
UniGeneiRn.1518.

Genome annotation databases

GeneIDi25739.
KEGGirno:25739.
UCSCiRGD:3460. rat.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
L10668 mRNA. Translation: AAA41252.1.
M27726 mRNA. Translation: AAA40815.1.
PIRiS37300.
RefSeqiNP_037320.1. NM_013188.1.
UniGeneiRn.1518.

3D structure databases

ProteinModelPortaliP53534.
SMRiP53534. Positions 14-838.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi247767. 2 interactions.
IntActiP53534. 2 interactions.
STRINGi10116.ENSRNOP00000010158.

Protein family/group databases

CAZyiGT35. Glycosyltransferase Family 35.

PTM databases

iPTMnetiP53534.

2D gel databases

World-2DPAGE0004:P53534.

Proteomic databases

PaxDbiP53534.
PeptideAtlasiP53534.
PRIDEiP53534.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

GeneIDi25739.
KEGGirno:25739.
UCSCiRGD:3460. rat.

Organism-specific databases

CTDi5834.
RGDi3460. Pygb.

Phylogenomic databases

eggNOGiKOG2099. Eukaryota.
COG0058. LUCA.
HOGENOMiHOG000278444.
HOVERGENiHBG006848.
InParanoidiP53534.
KOiK00688.

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]
ProtoNetiSearch...

Entry informationi

Entry nameiPYGB_RAT
AccessioniPrimary (citable) accession number: P53534
Entry historyi
Integrated into UniProtKB/Swiss-Prot: October 1, 1996
Last sequence update: January 23, 2007
Last modified: September 7, 2016
This is version 121 of the entry and version 3 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Allosteric enzyme, Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. 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.