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UniProtKB/Swiss-Prot entry P06738


[Entry info] [Name and origin] [References] [Comments] [Cross-references] [Keywords] [Features] [Sequence] [Tools]

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Entry information
Entry name PHSG_YEAST
Primary accession number P06738
Secondary accession numbers None
Integrated into Swiss-Prot on January 1, 1988
Sequence was last modified on January 23, 2007 (Sequence version 3)
Annotations were last modified on    November 25, 2008 (Entry version 96)
Name and origin of the protein
Protein name Glycogen phosphorylase
Synonym EC 2.4.1.1
Gene name
Name: GPH1
OrderedLocusNames: YPR160W
ORFNames: P9584.1
From
Saccharomyces cerevisiae (Baker's yeast) [TaxID: 4932] 
Taxonomy Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes; Saccharomycetales; Saccharomycetaceae; Saccharomyces.
Protein existence 1: Evidence at protein level;
References
[1]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
DOI=10.1038/324080a0; PubMed=3537803 [NCBI, ExPASy, EBI, Israel, Japan]
Hwang P.K., Fletterick R.J.;
"Convergent and divergent evolution of regulatory sites in eukaryotic phosphorylases.";
Nature 324:80-84(1986).
[2]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
DOI=10.1002/yea.320101117; PubMed=7871892 [NCBI, ExPASy, EBI, Israel, Japan]
Roemer T.D., Fortin N., Bussey H.;
"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.";
Yeast 10:1527-1530(1994).
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=ATCC 204511 / S288c / AB972;
PubMed=9169875 [NCBI, ExPASy, EBI, Israel, Japan]
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., 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.;
"The nucleotide sequence of Saccharomyces cerevisiae chromosome XVI.";
Nature 387:103-105(1997).
[4]
PROTEIN SEQUENCE OF 2-10, AND PHOSPHORYLATION AT THR-31.
DOI=10.1016/0022-2836(92)90102-P; PubMed=1613787 [NCBI, ExPASy, EBI, Israel, Japan]
Rath V.L., Hwang P.K., Fletterick R.J.;
"Purification and crystallization of glycogen phosphorylase from Saccharomyces cerevisiae.";
J. Mol. Biol. 225:1027-1034(1992).
[5]
PROTEIN SEQUENCE OF 30-37 AND 737-754, PHOSPHORYLATION AT THR-31, AND PYRIDOXAL PHOSPHATE AT LYS-751.
DOI=10.1021/bi00680a031; PubMed=1092346 [NCBI, ExPASy, EBI, Israel, Japan]
Lerch K., Fischer E.H.;
"Amino acid sequence of two functional sites in yeast glycogen phosphorylase.";
Biochemistry 14:2009-2014(1975).
[6]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-31, AND MASS SPECTROMETRY.
DOI=10.1021/pr060559j; PubMed=17330950 [NCBI, ExPASy, EBI, Israel, Japan]
Li X., Gerber S.A., Rudner A.D., Beausoleil S.A., Haas W., Villen J., Elias J.E., Gygi S.P.;
"Large-scale phosphorylation analysis of alpha-factor-arrested Saccharomyces cerevisiae.";
J. Proteome Res. 6:1190-1197(2007).
[7]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-31, AND MASS SPECTROMETRY.
DOI=10.1073/pnas.0701622104; PubMed=17563356 [NCBI, ExPASy, EBI, Israel, Japan]
Smolka M.B., Albuquerque C.P., Chen S.H., Zhou H.;
"Proteome-wide identification of in vivo targets of DNA damage checkpoint kinases.";
Proc. Natl. Acad. Sci. U.S.A. 104:10364-10369(2007).
[8]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-18; SER-19; THR-31 AND SER-333, AND MASS SPECTROMETRY.
DOI=10.1074/mcp.M700468-MCP200; PubMed=18407956 [NCBI, ExPASy, EBI, Israel, Japan]
Albuquerque C.P., Smolka M.B., Payne S.H., Bafna V., Eng J., Zhou H.;
"A multidimensional chromatography technology for in-depth phosphoproteome analysis.";
Mol. Cell. Proteomics 7:1389-1396(2008).
[9]
X-RAY CRYSTALLOGRAPHY (2.8 ANGSTROMS) OF 14-901.
PubMed=8703213 [NCBI, ExPASy, EBI, Israel, Japan]
Lin K., Rath V.L., Dai S.C., Fletterick R.J., Hwang P.K.;
"A protein phosphorylation switch at the conserved allosteric site in GP.";
Science 273:1539-1542(1996).
[10]
SUBUNIT.
DOI=10.1016/0003-9861(83)90078-4; PubMed=6354094 [NCBI, ExPASy, EBI, Israel, Japan]
Becker J.U., Wingender-Drissen R., Schiltz E.;
"Purification and properties of phosphorylase from baker's yeast.";
Arch. Biochem. Biophys. 225:667-678(1983).
Comments
Copyright
Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms. Distributed under the Creative Commons Attribution-NoDerivs License.
Cross-references
Sequence databases
EMBL
X04604; CAA28273.1; ALT_INIT; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
L33835; AAB59313.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
U28371; AAB68057.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
PIR S61144; S61144.
3D structure databases
PDB
1YGP; X-ray; 2.80 A; A/B=24-902.[ExPASy / RCSB / EBI]
PDBsum 1YGP; -.
ModBase P06738.
Protein-protein interaction databases
DIP DIP:2648N; -.
IntAct P06738; -.
Enzyme and pathway databases
BioCyc MetaCyc:MON-13684; -.
Organism-specific databases
CYGD YPR160w; -.
SGD S000006364; GPH1.
Yeast-GFP YPR160W.
Gene expression databases
GermOnline YPR160W; Saccharomyces cerevisiae.
Ontologies
GO
GO:0005737; Cellular component: cytoplasm (inferred from direct assay from SGD).
GO:0008184; Molecular function: glycogen phosphorylase activity (inferred from mutant phenotype from SGD).
GO:0005515; Molecular function: protein binding (inferred from physical interaction from IntAct).
GO:0030170; Molecular function: pyridoxal phosphate binding (inferred from electronic annotation from InterPro).
GO:0005980; Biological process: glycogen catabolic process (inferred from mutant phenotype from SGD).
QuickGo view.
Family and domain databases
InterPro IPR011833; Glycg_phsphrylas.
IPR000811; Glyco_trans_35.
Graphical view of domain structure.
PANTHER PTHR11468; Glyco_trans_35; 1.
Pfam PF00343; Phosphorylase; 1.
Pfam graphical view of domain structure.
PIRSF PIRSF000460; Pprylas_GlgP; 1.
TIGRFAMs TIGR02093; P_ylase; 1.
PROSITE PS00102; PHOSPHORYLASE; 1.
ProtoNet P06738.
Proteomic databases
PeptideAtlas P06738; -.
Genome annotation databases
Ensembl YPR160W; Saccharomyces cerevisiae. [Contig view]
GenomeReviews U00094_GR; YPR160W.
Phylogenomic databases
HOGENOM P06738; -.
Other
LinkHub P06738; -.
UniRef View cluster of proteins with at least 50% / 90% / 100% identity.
Keywords
3D-structure; Carbohydrate metabolism; Complete proteome; Direct protein sequencing; Glycogen metabolism; Glycosyltransferase; Phosphoprotein; Pyridoxal phosphate; Transferase.
Features
SEVIEWER logo Feature table viewer
KeyFrom   To Length Description FTId
INIT_MET   1     1        Removed. 
CHAIN   2   902  901     Glycogen phosphorylase. PRO_0000188545
BINDING   751   751        Pyridoxal phosphate (covalent). 
MOD_RES   18    18        Phosphothreonine. 
MOD_RES   19    19        Phosphoserine. 
MOD_RES   31    31        Phosphothreonine. 
MOD_RES   333   333        Phosphoserine. 
CONFLICT   167   168        EG -> DL (in Ref. 3; AAB68057). 
CONFLICT   326   326        P -> A (in Ref. 3; AAB68057). 
CONFLICT   440   441        RR -> VG (in Ref. 3; AAB68057). 
CONFLICT   508   508        V -> A (in Ref. 3; AAB68057). 
CONFLICT   524   524        I -> V (in Ref. 3; AAB68057). 
CONFLICT   578   578        E -> G (in Ref. 3; AAB68057). 
CONFLICT   876   876        L -> V (in Ref. 3; AAB68057). 
HELIX   64    76  13      
HELIX   83    85  3      
HELIX   88   117  30      
STRAND   121   125  5      
HELIX   134   140  7      
HELIX   159   162  4      
HELIX   165   168  4      
HELIX   172   176  5      
HELIX   188   202  15      
STRAND   207   212  6      
STRAND   220   224  5      
STRAND   227   231  5      
TURN   235   238  4      
STRAND   244   256  13      
STRAND   258   260  3      
STRAND   273   275  3      
STRAND   277   290  14      
STRAND   297   308  12      
HELIX   313   317  5      
HELIX   321   324  4      
HELIX   326   336  11      
STRAND   337   339  3      
HELIX   345   372  28      
HELIX   377   379  3      
HELIX   380   383  4      
STRAND   384   391  8      
TURN   392   394  3      
HELIX   395   406  12      
HELIX   412   422  11      
STRAND   423   427  5      
HELIX   432   434  3      
STRAND   437   439  3      
HELIX   440   446  7      
HELIX   448   468  21      
HELIX   474   479  6      
STRAND   481   483  3      
STRAND   486   488  3      
STRAND   490   492  3      
HELIX   493   500  8      
STRAND   501   508  8      
HELIX   509   517  9      
TURN   518   520  3      
HELIX   521   527  7      
HELIX   529   531  3      
STRAND   532   534  3      
HELIX   541   544  4      
TURN   545   548  4      
HELIX   550   559  10      
HELIX   566   568  3      
HELIX   571   582  12      
HELIX   585   607  23      
TURN   608   611  4      
HELIX   620   622  3      
STRAND   624   630  7      
HELIX   634   636  3      
HELIX   638   657  20      
HELIX   662   668  7      
STRAND   672   677  6      
HELIX   685   701  17      
HELIX   705   707  3      
STRAND   710   716  7      
HELIX   721   727  7      
HELIX   728   730  3      
STRAND   732   736  5      
HELIX   747   753  7      
TURN   754   756  3      
STRAND   758   763  6      
HELIX   766   774  9      
HELIX   776   778  3      
STRAND   779   783  5      
HELIX   786   798  13      
HELIX   805   813  9      
TURN   824   827  4      
HELIX   828   836  9      
TURN   838   841  4      
HELIX   843   863  21      
HELIX   865   879  15      
HELIX   880   882  3      
HELIX   884   894  11      
Sequence information
Length: 902 AA [This is the length of the unprocessed precursor] Molecular weight: 103544 Da [This is the MW of the unprocessed precursor] CRC64: 049C5A6F4E4A4826 [This is a checksum on the sequence]
        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 

P06738 in FASTA format

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