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P06738 (PHSG_YEAST) Reviewed, UniProtKB/Swiss-Prot

Last modified March 19, 2014. Version 143. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (4) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Interactions·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Glycogen phosphorylase

EC=2.4.1.1
Gene names
Name:GPH1
Ordered Locus Names:YPR160W
ORF Names:P9584.1
OrganismSaccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast) [Reference proteome]
Taxonomic identifier559292 [NCBI]
Taxonomic lineageEukaryotaFungiDikaryaAscomycotaSaccharomycotinaSaccharomycetesSaccharomycetalesSaccharomycetaceaeSaccharomyces

Protein attributes

Sequence length902 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

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 activity

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

Cofactor

Pyridoxal phosphate.

Enzyme regulation

Activated by phosphorylation of Thr-31.

Subunit structure

Homodimer. Ref.13

Sequence similarities

Belongs to the glycogen phosphorylase family.

Sequence caution

The sequence CAA28273.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally extended.

Binary interactions

With

Entry

#Exp.

IntAct

Notes

PRP40P332032EBI-13389,EBI-701
RSP5P399402EBI-13389,EBI-16219

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Initiator methionine11Removed Ref.5
Chain2 – 902901Glycogen phosphorylase
PRO_0000188545

Amino acid modifications

Modified residue311Phosphothreonine Ref.5 Ref.6 Ref.7 Ref.8 Ref.9 Ref.10
Modified residue3331Phosphoserine Ref.9 Ref.10
Modified residue7511N6-(pyridoxal phosphate)lysine

Experimental info

Sequence conflict167 – 1682DL → EG in CAA28273. Ref.1
Sequence conflict167 – 1682DL → EG in AAB59313. Ref.2
Sequence conflict3261A → P in CAA28273. Ref.1
Sequence conflict3261A → P in AAB59313. Ref.2
Sequence conflict440 – 4412VG → RR in CAA28273. Ref.1
Sequence conflict440 – 4412VG → RR in AAB59313. Ref.2
Sequence conflict5081A → V in CAA28273. Ref.1
Sequence conflict5081A → V in AAB59313. Ref.2
Sequence conflict5241V → I in CAA28273. Ref.1
Sequence conflict5241V → I in AAB59313. Ref.2
Sequence conflict5781G → E in CAA28273. Ref.1
Sequence conflict5781G → E in AAB59313. Ref.2
Sequence conflict8761V → L in CAA28273. Ref.1
Sequence conflict8761V → L in AAB59313. Ref.2

Secondary structure

............................................................................................................................................. 902
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
P06738 [UniParc].

Last modified October 5, 2010. Version 4.
Checksum: F5B6098D69ABAE43

FASTA902103,275
        10         20         30         40         50         60 
MPPASTSTTN DMITEEPTSP HQIPRLTRRL TGFLPQEIKS IDTMIPLKSR ALWNKHQVKK 

        70         80         90        100        110        120 
FNKAEDFQDR FIDHVETTLA RSLYNCDDMA AYEAASMSIR DNLVIDWNKT QQKFTTRDPK 

       130        140        150        160        170        180 
RVYYLSLEFL MGRALDNALI NMKIEDPEDP AASKGKPREM IKGALDDLGF KLEDVLDQEP 

       190        200        210        220        230        240 
DAGLGNGGLG RLAACFVDSM ATEGIPAWGY GLRYEYGIFA QKIIDGYQVE TPDYWLNSGN 

       250        260        270        280        290        300 
PWEIERNEVQ IPVTFYGYVD RPEGGKTTLS ASQWIGGERV LAVAYDFPVP GFKTSNVNNL 

       310        320        330        340        350        360 
RLWQARPTTE FDFAKFNNGD YKNSVAQQQR AESITAVLYP NDNFAQGKEL RLKQQYFWCA 

       370        380        390        400        410        420 
ASLHDILRRF KKSKRPWTEF PDQVAIQLND THPTLAIVEL QRVLVDLEKL DWHEAWDIVT 

       430        440        450        460        470        480 
KTFAYTNHTV MQEALEKWPV GLFGHLLPRH LEIIYDINWF FLQDVAKKFP KDVDLLSRIS 

       490        500        510        520        530        540 
IIEENSPERQ IRMAFLAIVG SHKVNGVAEL HSELIKTTIF KDFVKFYGPS KFVNVTNGIT 

       550        560        570        580        590        600 
PRRWLKQANP SLAKLISETL NDPTEEYLLD MAKLTQLGKY VEDKEFLKKW NQVKLNNKIR 

       610        620        630        640        650        660 
LVDLIKKEND GVDIINREYL DDTLFDMQVK RIHEYKRQQL NVFGIIYRYL AMKNMLKNGA 

       670        680        690        700        710        720 
SIEEVAKKYP RKVSIFGGKS APGYYMAKLI IKLINCVADI VNNDESIEHL LKVVFVADYN 

       730        740        750        760        770        780 
VSKAEIIIPA SDLSEHISTA GTEASGTSNM KFVMNGGLII GTVDGANVEI TREIGEDNVF 

       790        800        810        820        830        840 
LFGNLSENVE ELRYNHQYHP QDLPSSLDSV LSYIESGQFS PENPNEFKPL VDSIKYHGDY 

       850        860        870        880        890        900 
YLVSDDFESY LATHELVDQE FHNQRSEWLK KSVLSVANVG FFSSDRCIEE YSDTIWNVEP 


VT 

« Hide

References

« Hide 'large scale' references
[1]"Convergent and divergent evolution of regulatory sites in eukaryotic phosphorylases."
Hwang P.K., Fletterick R.J.
Nature 324:80-84(1986) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[2]"DNA sequence analysis of a 10.4 kbp region on the right arm of yeast chromosome XVI positions GPH1 and SGV1 adjacent to KRE6, and identifies two novel tRNA genes."
Roemer T.D., Fortin N., Bussey H.
Yeast 10:1527-1530(1994) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[3]"The nucleotide sequence of Saccharomyces cerevisiae chromosome XVI."
Bussey H., Storms R.K., Ahmed A., Albermann K., Allen E., Ansorge W., Araujo R., Aparicio A., Barrell B.G., Badcock K., Benes V., Botstein D., Bowman S., Brueckner M., Carpenter J., Cherry J.M., Chung E., Churcher C.M. expand/collapse author list , Coster F., Davis K., Davis R.W., Dietrich F.S., Delius H., DiPaolo T., Dubois E., Duesterhoeft A., Duncan M., Floeth M., Fortin N., Friesen J.D., Fritz C., Goffeau A., Hall J., Hebling U., Heumann K., Hilbert H., Hillier L.W., Hunicke-Smith S., Hyman R.W., Johnston M., Kalman S., Kleine K., Komp C., Kurdi O., Lashkari D., Lew H., Lin A., Lin D., Louis E.J., Marathe R., Messenguy F., Mewes H.-W., Mirtipati S., Moestl D., Mueller-Auer S., Namath A., Nentwich U., Oefner P., Pearson D., Petel F.X., Pohl T.M., Purnelle B., Rajandream M.A., Rechmann S., Rieger M., Riles L., Roberts D., Schaefer M., Scharfe M., Scherens B., Schramm S., Schroeder M., Sdicu A.-M., Tettelin H., Urrestarazu L.A., Ushinsky S., Vierendeels F., Vissers S., Voss H., Walsh S.V., Wambutt R., Wang Y., Wedler E., Wedler H., Winnett E., Zhong W.-W., Zollner A., Vo D.H., Hani J.
Nature 387:103-105(1997) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: ATCC 204508 / S288c.
[4]Saccharomyces Genome Database
Submitted (DEC-2009) to the EMBL/GenBank/DDBJ databases
Cited for: GENOME REANNOTATION.
Strain: ATCC 204508 / S288c.
[5]"Purification and crystallization of glycogen phosphorylase from Saccharomyces cerevisiae."
Rath V.L., Hwang P.K., Fletterick R.J.
J. Mol. Biol. 225:1027-1034(1992) [PubMed] [Europe PMC] [Abstract]
Cited for: PROTEIN SEQUENCE OF 2-10, PHOSPHORYLATION AT THR-31.
[6]"Amino acid sequence of two functional sites in yeast glycogen phosphorylase."
Lerch K., Fischer E.H.
Biochemistry 14:2009-2014(1975) [PubMed] [Europe PMC] [Abstract]
Cited for: PROTEIN SEQUENCE OF 30-37 AND 737-754, PHOSPHORYLATION AT THR-31, PYRIDOXAL PHOSPHATE AT LYS-751.
[7]"Quantitative phosphoproteomics applied to the yeast pheromone signaling pathway."
Gruhler A., Olsen J.V., Mohammed S., Mortensen P., Faergeman N.J., Mann M., Jensen O.N.
Mol. Cell. Proteomics 4:310-327(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-31, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Strain: YAL6B.
[8]"Large-scale phosphorylation analysis of alpha-factor-arrested Saccharomyces cerevisiae."
Li X., Gerber S.A., Rudner A.D., Beausoleil S.A., Haas W., Villen J., Elias J.E., Gygi S.P.
J. Proteome Res. 6:1190-1197(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-31, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Strain: ADR376.
[9]"A multidimensional chromatography technology for in-depth phosphoproteome analysis."
Albuquerque C.P., Smolka M.B., Payne S.H., Bafna V., Eng J., Zhou H.
Mol. Cell. Proteomics 7:1389-1396(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-31 AND SER-333, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[10]"Global analysis of Cdk1 substrate phosphorylation sites provides insights into evolution."
Holt L.J., Tuch B.B., Villen J., Johnson A.D., Gygi S.P., Morgan D.O.
Science 325:1682-1686(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-31 AND SER-333, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[11]"N-terminal acetylome analyses and functional insights of the N-terminal acetyltransferase NatB."
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.
Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[12]"A protein phosphorylation switch at the conserved allosteric site in GP."
Lin K., Rath V.L., Dai S.C., Fletterick R.J., Hwang P.K.
Science 273:1539-1542(1996) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.8 ANGSTROMS) OF 14-901.
[13]"Purification and properties of phosphorylase from baker's yeast."
Becker J.U., Wingender-Drissen R., Schiltz E.
Arch. Biochem. Biophys. 225:667-678(1983) [PubMed] [Europe PMC] [Abstract]
Cited for: SUBUNIT.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
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.
PIRS61144.
RefSeqNP_015486.1. NM_001184257.1.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
1YGPX-ray2.80A/B24-902[»]
ProteinModelPortalP06738.
SMRP06738. Positions 27-901.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid36333. 91 interactions.
DIPDIP-2648N.
IntActP06738. 12 interactions.
MINTMINT-426238.
STRING4932.YPR160W.

Protein family/group databases

CAZyGT35. Glycosyltransferase Family 35.

Proteomic databases

PaxDbP06738.
PeptideAtlasP06738.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblFungiYPR160W; YPR160W; YPR160W.
GeneID856289.
KEGGsce:YPR160W.

Organism-specific databases

SGDS000006364. GPH1.

Phylogenomic databases

eggNOGCOG0058.
GeneTreeENSGT00390000016886.
HOGENOMHOG000278444.
KOK00688.
OMAYFALAHA.
OrthoDBEOG7FJH7X.

Enzyme and pathway databases

BioCycMetaCyc:MONOMER-13684.
YEAST:YPR160W-MONOMER.

Gene expression databases

GenevestigatorP06738.

Family and domain databases

InterProIPR011833. Glycg_phsphrylas.
IPR000811. Glyco_trans_35.
[Graphical view]
PANTHERPTHR11468. PTHR11468. 1 hit.
PfamPF00343. Phosphorylase. 1 hit.
[Graphical view]
PIRSFPIRSF000460. Pprylas_GlgP. 1 hit.
TIGRFAMsTIGR02093. P_ylase. 1 hit.
PROSITEPS00102. PHOSPHORYLASE. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

EvolutionaryTraceP06738.
NextBio981626.

Entry information

Entry namePHSG_YEAST
AccessionPrimary (citable) accession number: P06738
Secondary accession number(s): D6W4G1
Entry history
Integrated into UniProtKB/Swiss-Prot: January 1, 1988
Last sequence update: October 5, 2010
Last modified: March 19, 2014
This is version 143 of the entry and version 4 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programFungal Protein Annotation Program

Relevant documents

Yeast chromosome XVI

Yeast (Saccharomyces cerevisiae) chromosome XVI: entries and gene names

Yeast

Yeast (Saccharomyces cerevisiae): entries, gene names and cross-references to SGD

SIMILARITY comments

Index of protein domains and families

PDB cross-references

Index of Protein Data Bank (PDB) cross-references