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Protein

Glycogen phosphorylase

Gene

GPH1

Organism
Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
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

Activated by phosphorylation of Thr-31.

GO - Molecular functioni

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

GO - Biological processi

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

Keywords - Molecular functioni

Glycosyltransferase, Transferase

Keywords - Biological processi

Carbohydrate metabolism, Glycogen metabolism

Keywords - Ligandi

Pyridoxal phosphate

Enzyme and pathway databases

BioCyciMetaCyc:YPR160W-MONOMER.
YEAST:YPR160W-MONOMER.
ReactomeiR-SCE-6798695. Neutrophil degranulation.
R-SCE-70221. Glycogen breakdown (glycogenolysis).

Protein family/group databases

CAZyiGT35. Glycosyltransferase Family 35.

Names & Taxonomyi

Protein namesi
Recommended name:
Glycogen phosphorylase (EC:2.4.1.1)
Gene namesi
Name:GPH1
Ordered Locus Names:YPR160W
ORF Names:P9584.1
OrganismiSaccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Taxonomic identifieri559292 [NCBI]
Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaSaccharomycotinaSaccharomycetesSaccharomycetalesSaccharomycetaceaeSaccharomyces
Proteomesi
  • UP000002311 Componenti: Chromosome XVI

Organism-specific databases

EuPathDBiFungiDB:YPR160W.
SGDiS000006364. GPH1.

Subcellular locationi

GO - Cellular componenti

  • cytoplasm Source: SGD
Complete GO annotation...

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Initiator methionineiRemoved1 Publication
ChainiPRO_00001885452 – 902Glycogen phosphorylaseAdd BLAST901

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei31PhosphothreonineCombined sources2 Publications1
Modified residuei333PhosphoserineCombined sources1
Modified residuei751N6-(pyridoxal phosphate)lysine1

Keywords - PTMi

Phosphoprotein

Proteomic databases

MaxQBiP06738.
PRIDEiP06738.

PTM databases

iPTMnetiP06738.

Interactioni

Subunit structurei

Homodimer.1 Publication

Binary interactionsi

WithEntry#Exp.IntActNotes
PRP40P332032EBI-13389,EBI-701
RSP5P399402EBI-13389,EBI-16219

Protein-protein interaction databases

BioGridi36333. 98 interactors.
DIPiDIP-2648N.
IntActiP06738. 12 interactors.
MINTiMINT-426238.

Structurei

Secondary structure

1902
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Helixi35 – 44Combined sources10
Helixi47 – 55Combined sources9
Helixi64 – 76Combined sources13
Helixi83 – 85Combined sources3
Helixi88 – 117Combined sources30
Beta strandi121 – 125Combined sources5
Helixi134 – 140Combined sources7
Helixi158 – 168Combined sources11
Helixi172 – 176Combined sources5
Helixi188 – 202Combined sources15
Beta strandi207 – 212Combined sources6
Beta strandi220 – 224Combined sources5
Beta strandi227 – 231Combined sources5
Turni235 – 238Combined sources4
Beta strandi244 – 256Combined sources13
Beta strandi258 – 260Combined sources3
Beta strandi273 – 275Combined sources3
Beta strandi277 – 290Combined sources14
Beta strandi297 – 308Combined sources12
Helixi313 – 317Combined sources5
Helixi321 – 324Combined sources4
Helixi326 – 336Combined sources11
Beta strandi337 – 339Combined sources3
Helixi345 – 372Combined sources28
Helixi377 – 379Combined sources3
Helixi380 – 383Combined sources4
Beta strandi384 – 391Combined sources8
Turni392 – 394Combined sources3
Helixi395 – 406Combined sources12
Helixi412 – 422Combined sources11
Beta strandi423 – 427Combined sources5
Helixi432 – 434Combined sources3
Beta strandi437 – 439Combined sources3
Helixi440 – 446Combined sources7
Helixi448 – 468Combined sources21
Helixi474 – 479Combined sources6
Beta strandi481 – 483Combined sources3
Beta strandi486 – 488Combined sources3
Beta strandi490 – 492Combined sources3
Helixi493 – 500Combined sources8
Beta strandi501 – 508Combined sources8
Helixi509 – 517Combined sources9
Turni518 – 520Combined sources3
Helixi521 – 527Combined sources7
Helixi529 – 531Combined sources3
Beta strandi532 – 534Combined sources3
Helixi541 – 544Combined sources4
Turni545 – 548Combined sources4
Helixi550 – 559Combined sources10
Helixi566 – 568Combined sources3
Helixi571 – 582Combined sources12
Helixi585 – 607Combined sources23
Turni608 – 611Combined sources4
Helixi620 – 622Combined sources3
Beta strandi624 – 630Combined sources7
Helixi634 – 636Combined sources3
Helixi638 – 657Combined sources20
Helixi662 – 668Combined sources7
Beta strandi672 – 677Combined sources6
Helixi685 – 701Combined sources17
Helixi705 – 707Combined sources3
Beta strandi710 – 716Combined sources7
Helixi721 – 727Combined sources7
Helixi728 – 730Combined sources3
Beta strandi732 – 736Combined sources5
Helixi747 – 753Combined sources7
Turni754 – 756Combined sources3
Beta strandi758 – 763Combined sources6
Helixi766 – 774Combined sources9
Helixi776 – 778Combined sources3
Beta strandi779 – 783Combined sources5
Helixi786 – 798Combined sources13
Helixi805 – 813Combined sources9
Turni824 – 827Combined sources4
Helixi828 – 836Combined sources9
Turni838 – 841Combined sources4
Helixi843 – 863Combined sources21
Helixi865 – 879Combined sources15
Helixi880 – 882Combined sources3
Helixi884 – 894Combined sources11

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1YGPX-ray2.80A/B24-902[»]
ProteinModelPortaliP06738.
SMRiP06738.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP06738.

Family & Domainsi

Sequence similaritiesi

Belongs to the glycogen phosphorylase family.Curated

Phylogenomic databases

GeneTreeiENSGT00390000016886.
HOGENOMiHOG000278444.
InParanoidiP06738.
KOiK00688.
OMAiRMMRRWI.
OrthoDBiEOG092C0DIQ.

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.

P06738-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MPPASTSTTN DMITEEPTSP HQIPRLTRRL TGFLPQEIKS IDTMIPLKSR
60 70 80 90 100
ALWNKHQVKK FNKAEDFQDR FIDHVETTLA RSLYNCDDMA AYEAASMSIR
110 120 130 140 150
DNLVIDWNKT QQKFTTRDPK RVYYLSLEFL MGRALDNALI NMKIEDPEDP
160 170 180 190 200
AASKGKPREM IKGALDDLGF KLEDVLDQEP DAGLGNGGLG RLAACFVDSM
210 220 230 240 250
ATEGIPAWGY GLRYEYGIFA QKIIDGYQVE TPDYWLNSGN PWEIERNEVQ
260 270 280 290 300
IPVTFYGYVD RPEGGKTTLS ASQWIGGERV LAVAYDFPVP GFKTSNVNNL
310 320 330 340 350
RLWQARPTTE FDFAKFNNGD YKNSVAQQQR AESITAVLYP NDNFAQGKEL
360 370 380 390 400
RLKQQYFWCA ASLHDILRRF KKSKRPWTEF PDQVAIQLND THPTLAIVEL
410 420 430 440 450
QRVLVDLEKL DWHEAWDIVT KTFAYTNHTV MQEALEKWPV GLFGHLLPRH
460 470 480 490 500
LEIIYDINWF FLQDVAKKFP KDVDLLSRIS IIEENSPERQ IRMAFLAIVG
510 520 530 540 550
SHKVNGVAEL HSELIKTTIF KDFVKFYGPS KFVNVTNGIT PRRWLKQANP
560 570 580 590 600
SLAKLISETL NDPTEEYLLD MAKLTQLGKY VEDKEFLKKW NQVKLNNKIR
610 620 630 640 650
LVDLIKKEND GVDIINREYL DDTLFDMQVK RIHEYKRQQL NVFGIIYRYL
660 670 680 690 700
AMKNMLKNGA SIEEVAKKYP RKVSIFGGKS APGYYMAKLI IKLINCVADI
710 720 730 740 750
VNNDESIEHL LKVVFVADYN VSKAEIIIPA SDLSEHISTA GTEASGTSNM
760 770 780 790 800
KFVMNGGLII GTVDGANVEI TREIGEDNVF LFGNLSENVE ELRYNHQYHP
810 820 830 840 850
QDLPSSLDSV LSYIESGQFS PENPNEFKPL VDSIKYHGDY YLVSDDFESY
860 870 880 890 900
LATHELVDQE FHNQRSEWLK KSVLSVANVG FFSSDRCIEE YSDTIWNVEP

VT
Length:902
Mass (Da):103,275
Last modified:October 5, 2010 - v4
Checksum:iF5B6098D69ABAE43
GO

Sequence cautioni

The sequence CAA28273 differs from that shown. Reason: Erroneous initiation. Translation N-terminally extended.Curated

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sequence conflicti167 – 168DL → EG in CAA28273 (PubMed:3537803).Curated2
Sequence conflicti167 – 168DL → EG in AAB59313 (PubMed:7871892).Curated2
Sequence conflicti326A → P in CAA28273 (PubMed:3537803).Curated1
Sequence conflicti326A → P in AAB59313 (PubMed:7871892).Curated1
Sequence conflicti440 – 441VG → RR in CAA28273 (PubMed:3537803).Curated2
Sequence conflicti440 – 441VG → RR in AAB59313 (PubMed:7871892).Curated2
Sequence conflicti508A → V in CAA28273 (PubMed:3537803).Curated1
Sequence conflicti508A → V in AAB59313 (PubMed:7871892).Curated1
Sequence conflicti524V → I in CAA28273 (PubMed:3537803).Curated1
Sequence conflicti524V → I in AAB59313 (PubMed:7871892).Curated1
Sequence conflicti578G → E in CAA28273 (PubMed:3537803).Curated1
Sequence conflicti578G → E in AAB59313 (PubMed:7871892).Curated1
Sequence conflicti876V → L in CAA28273 (PubMed:3537803).Curated1
Sequence conflicti876V → L in AAB59313 (PubMed:7871892).Curated1

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X04604 Genomic DNA. Translation: CAA28273.1. Different initiation.
L33835 Genomic DNA. Translation: AAB59313.1.
U28371 Genomic DNA. Translation: AAB68057.1.
BK006949 Genomic DNA. Translation: DAA11577.1.
PIRiS61144.
RefSeqiNP_015486.1. NM_001184257.1.

Genome annotation databases

EnsemblFungiiYPR160W; YPR160W; YPR160W.
GeneIDi856289.
KEGGisce:YPR160W.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X04604 Genomic DNA. Translation: CAA28273.1. Different initiation.
L33835 Genomic DNA. Translation: AAB59313.1.
U28371 Genomic DNA. Translation: AAB68057.1.
BK006949 Genomic DNA. Translation: DAA11577.1.
PIRiS61144.
RefSeqiNP_015486.1. NM_001184257.1.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1YGPX-ray2.80A/B24-902[»]
ProteinModelPortaliP06738.
SMRiP06738.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi36333. 98 interactors.
DIPiDIP-2648N.
IntActiP06738. 12 interactors.
MINTiMINT-426238.

Protein family/group databases

CAZyiGT35. Glycosyltransferase Family 35.

PTM databases

iPTMnetiP06738.

Proteomic databases

MaxQBiP06738.
PRIDEiP06738.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblFungiiYPR160W; YPR160W; YPR160W.
GeneIDi856289.
KEGGisce:YPR160W.

Organism-specific databases

EuPathDBiFungiDB:YPR160W.
SGDiS000006364. GPH1.

Phylogenomic databases

GeneTreeiENSGT00390000016886.
HOGENOMiHOG000278444.
InParanoidiP06738.
KOiK00688.
OMAiRMMRRWI.
OrthoDBiEOG092C0DIQ.

Enzyme and pathway databases

BioCyciMetaCyc:YPR160W-MONOMER.
YEAST:YPR160W-MONOMER.
ReactomeiR-SCE-6798695. Neutrophil degranulation.
R-SCE-70221. Glycogen breakdown (glycogenolysis).

Miscellaneous databases

EvolutionaryTraceiP06738.
PROiP06738.

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 nameiPHSG_YEAST
AccessioniPrimary (citable) accession number: P06738
Secondary accession number(s): D6W4G1
Entry historyi
Integrated into UniProtKB/Swiss-Prot: January 1, 1988
Last sequence update: October 5, 2010
Last modified: November 30, 2016
This is version 166 of the entry and version 4 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programFungal Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  2. SIMILARITY comments
    Index of protein domains and families
  3. Yeast
    Yeast (Saccharomyces cerevisiae): entries, gene names and cross-references to SGD
  4. Yeast chromosome XVI
    Yeast (Saccharomyces cerevisiae) chromosome XVI: entries and gene names

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.