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Reviewed, UniProtKB/Swiss-Prot P06738 (PHSG_YEAST)

Last modified June 16, 2009. Version 102. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | Third-party data | Customize display text xml rdf/xml gff fasta
Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Binary interactions · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents

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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 (Baker's yeast) [Complete proteome]
Taxonomic identifier4932 [NCBI]
Taxonomic lineageEukaryota › Fungi › Dikarya › Ascomycota › Saccharomycotina › Saccharomycetes › Saccharomycetales › Saccharomycetaceae › Saccharomyces

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Protein attributes

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

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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.10

Sequence similarities

Belongs to the glycogen phosphorylase family.

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Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Initiator methionine11Removed Ref.4
Chain2 – 902901Glycogen phosphorylase
PRO_0000188545

Amino acid modifications

Modified residue181Phosphothreonine Ref.8
Modified residue191Phosphoserine Ref.8
Modified residue311Phosphothreonine Ref.4 Ref.8 Ref.5 Ref.6 Ref.7
Modified residue3331Phosphoserine Ref.8
Modified residue7511N6-(pyridoxal phosphate)lysine

Experimental info

Sequence conflict167 – 1682EG → DL in AAB68057. Ref.3
Sequence conflict3261P → A in AAB68057. Ref.3
Sequence conflict440 – 4412RR → VG in AAB68057. Ref.3
Sequence conflict5081V → A in AAB68057. Ref.3
Sequence conflict5241I → V in AAB68057. Ref.3
Sequence conflict5781E → G in AAB68057. Ref.3
Sequence conflict8761L → V in AAB68057. Ref.3

Secondary structure

1 ........................................................................................................................................... 902
Helix Strand Turn

Details...

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Sequences

Sequence LengthMass (Da)Tools
P06738-1 [UniParc].

Last modified January 23, 2007. Version 3.
Checksum: 049C5A6F4E4A4826

FASTA902103,544
        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 IKGALDEGGF 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 YKNSVPQQQR AESITAVLYP NDNFAQGKEL RLKQQYFWCA 

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

       430        440        450        460        470        480 
KTFAYTNHTV MQEALEKWPR RLFGHLLPRH LEIIYDINWF FLQDVAKKFP KDVDLLSRIS 

       490        500        510        520        530        540 
IIEENSPERQ IRMAFLAIVG SHKVNGVVEL HSELIKTTIF KDFIKFYGPS KFVNVTNGIT 

       550        560        570        580        590        600 
PRRWLKQANP SLAKLISETL NDPTEEYLLD MAKLTQLEKY 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 KSVLSLANVG FFSSDRCIEE YSDTIWNVEP 


VT

« Hide

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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: 3537803] [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: 7871892] [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: 9169875] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: ATCC 204511 / S288c / AB972.
[4]"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: 1613787] [Abstract]
Cited for: PROTEIN SEQUENCE OF 2-10, PHOSPHORYLATION AT THR-31.
[5]"Amino acid sequence of two functional sites in yeast glycogen phosphorylase."
Lerch K., Fischer E.H.
Biochemistry 14:2009-2014(1975) [PubMed: 1092346] [Abstract]
Cited for: PROTEIN SEQUENCE OF 30-37 AND 737-754, PHOSPHORYLATION AT THR-31, PYRIDOXAL PHOSPHATE AT LYS-751.
[6]"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: 17330950] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-31, MASS SPECTROMETRY.
[7]"Proteome-wide identification of in vivo targets of DNA damage checkpoint kinases."
Smolka M.B., Albuquerque C.P., Chen S.H., Zhou H.
Proc. Natl. Acad. Sci. U.S.A. 104:10364-10369(2007) [PubMed: 17563356] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-31, MASS SPECTROMETRY.
[8]"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: 18407956] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-18; SER-19; THR-31 AND SER-333, MASS SPECTROMETRY.
[9]"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: 8703213] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.8 ANGSTROMS) OF 14-901.
[10]"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: 6354094] [Abstract]
Cited for: SUBUNIT.
+Additional computationally mapped references.

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Cross-references

Sequence databases

X04604 Genomic DNA. Translation: CAA28273.1. Different initiation.
L33835 Genomic DNA. Translation: AAB59313.1.
U28371 Genomic DNA. Translation: AAB68057.1.
PIRS61144.

3D structure databases

EntryMethodResolution (Å)ChainPositionsPDBsum
1YGPX-ray2.80A/B24-902[»]
ModBaseSearch...

Protein-protein interaction databases

DIPDIP:2648N.
IntActP06738. 21 interactions.

Protein family/group databases

CAZyGT35. Glycosyltransferase Family 35.

Proteomic databases

PeptideAtlasP06738.
PRIDEP06738.

Genome annotation databases

EnsemblYPR160W. Saccharomyces cerevisiae. [Contig view]
GenomeReviewsGene locus YPR160W in contig U00094_GR.
KEGGsce:YPR160W.

Organism-specific databases

CYGDYPR160w.
SGDS000006364. GPH1.
Yeast-GFPSearch...

Phylogenomic databases

HOGENOMP06738.

Enzyme and pathway databases

BioCycMetaCyc:MON-13684.
BRENDA2.4.1.1. 250.

Gene expression databases

GermOnlineYPR160W. Saccharomyces cerevisiae.

Family and domain databases

InterProIPR011833. Glycg_phsphrylas.
IPR000811. Glyco_trans_35.
[Graphical view]
PANTHERPTHR11468. Glyco_trans_35. 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...

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Entry information

Entry namePHSG_YEAST
AccessionPrimary (citable) accession number: P06738
Entry history
Integrated into UniProtKB/Swiss-Prot: January 1, 1988
Last sequence update: January 23, 2007
Last modified: June 16, 2009
This is version 102 of the entry and version 3 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation projectFPAP (Fungal Proteome Annotation Project)

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Relevant documents

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

SIMILARITY comments

Index of protein domains and families

Yeast

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

Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Binary interactions · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents