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P06738

- PHSG_YEAST

UniProt

P06738 - PHSG_YEAST

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Protein

Glycogen phosphorylase

Gene
GPH1, YPR160W, P9584.1
Organism
Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Status
Reviewed - 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

Pyridoxal phosphate.

Enzyme regulationi

Activated by phosphorylation of Thr-31.

GO - Molecular functioni

  1. glycogen phosphorylase activity Source: SGD
  2. protein binding Source: IntAct
  3. pyridoxal phosphate binding Source: InterPro

GO - Biological processi

  1. 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:MONOMER-13684.
YEAST:YPR160W-MONOMER.

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
ProteomesiUP000002311: Chromosome XVI

Organism-specific databases

SGDiS000006364. GPH1.

Subcellular locationi

GO - Cellular componenti

  1. cytoplasm Source: SGD
Complete GO annotation...

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Initiator methioninei1 – 11Removed1 Publication
Chaini2 – 902901Glycogen phosphorylasePRO_0000188545Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei31 – 311Phosphothreonine6 Publications
Modified residuei333 – 3331Phosphoserine2 Publications
Modified residuei751 – 7511N6-(pyridoxal phosphate)lysine

Keywords - PTMi

Phosphoprotein

Proteomic databases

MaxQBiP06738.
PaxDbiP06738.
PeptideAtlasiP06738.

Expressioni

Gene expression databases

GenevestigatoriP06738.

Interactioni

Subunit structurei

Homodimer.1 Publication

Binary interactionsi

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

Protein-protein interaction databases

BioGridi36333. 91 interactions.
DIPiDIP-2648N.
IntActiP06738. 12 interactions.
MINTiMINT-426238.
STRINGi4932.YPR160W.

Structurei

Secondary structure

1
902
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi35 – 4410
Helixi47 – 559
Helixi64 – 7613
Helixi83 – 853
Helixi88 – 11730
Beta strandi121 – 1255
Helixi134 – 1407
Helixi158 – 16811
Helixi172 – 1765
Helixi188 – 20215
Beta strandi207 – 2126
Beta strandi220 – 2245
Beta strandi227 – 2315
Turni235 – 2384
Beta strandi244 – 25613
Beta strandi258 – 2603
Beta strandi273 – 2753
Beta strandi277 – 29014
Beta strandi297 – 30812
Helixi313 – 3175
Helixi321 – 3244
Helixi326 – 33611
Beta strandi337 – 3393
Helixi345 – 37228
Helixi377 – 3793
Helixi380 – 3834
Beta strandi384 – 3918
Turni392 – 3943
Helixi395 – 40612
Helixi412 – 42211
Beta strandi423 – 4275
Helixi432 – 4343
Beta strandi437 – 4393
Helixi440 – 4467
Helixi448 – 46821
Helixi474 – 4796
Beta strandi481 – 4833
Beta strandi486 – 4883
Beta strandi490 – 4923
Helixi493 – 5008
Beta strandi501 – 5088
Helixi509 – 5179
Turni518 – 5203
Helixi521 – 5277
Helixi529 – 5313
Beta strandi532 – 5343
Helixi541 – 5444
Turni545 – 5484
Helixi550 – 55910
Helixi566 – 5683
Helixi571 – 58212
Helixi585 – 60723
Turni608 – 6114
Helixi620 – 6223
Beta strandi624 – 6307
Helixi634 – 6363
Helixi638 – 65720
Helixi662 – 6687
Beta strandi672 – 6776
Helixi685 – 70117
Helixi705 – 7073
Beta strandi710 – 7167
Helixi721 – 7277
Helixi728 – 7303
Beta strandi732 – 7365
Helixi747 – 7537
Turni754 – 7563
Beta strandi758 – 7636
Helixi766 – 7749
Helixi776 – 7783
Beta strandi779 – 7835
Helixi786 – 79813
Helixi805 – 8139
Turni824 – 8274
Helixi828 – 8369
Turni838 – 8414
Helixi843 – 86321
Helixi865 – 87915
Helixi880 – 8823
Helixi884 – 89411

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1YGPX-ray2.80A/B24-902[»]
ProteinModelPortaliP06738.
SMRiP06738. Positions 27-901.

Miscellaneous databases

EvolutionaryTraceiP06738.

Family & Domainsi

Sequence similaritiesi

Phylogenomic databases

eggNOGiCOG0058.
GeneTreeiENSGT00390000016886.
HOGENOMiHOG000278444.
KOiK00688.
OMAiMDQISSG.
OrthoDBiEOG7FJH7X.

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: Complete.

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

P06738-1 [UniParc]FASTAAdd to Basket

« Hide

MPPASTSTTN DMITEEPTSP HQIPRLTRRL TGFLPQEIKS IDTMIPLKSR    50
ALWNKHQVKK FNKAEDFQDR FIDHVETTLA RSLYNCDDMA AYEAASMSIR 100
DNLVIDWNKT QQKFTTRDPK RVYYLSLEFL MGRALDNALI NMKIEDPEDP 150
AASKGKPREM IKGALDDLGF KLEDVLDQEP DAGLGNGGLG RLAACFVDSM 200
ATEGIPAWGY GLRYEYGIFA QKIIDGYQVE TPDYWLNSGN PWEIERNEVQ 250
IPVTFYGYVD RPEGGKTTLS ASQWIGGERV LAVAYDFPVP GFKTSNVNNL 300
RLWQARPTTE FDFAKFNNGD YKNSVAQQQR AESITAVLYP NDNFAQGKEL 350
RLKQQYFWCA ASLHDILRRF KKSKRPWTEF PDQVAIQLND THPTLAIVEL 400
QRVLVDLEKL DWHEAWDIVT KTFAYTNHTV MQEALEKWPV GLFGHLLPRH 450
LEIIYDINWF FLQDVAKKFP KDVDLLSRIS IIEENSPERQ IRMAFLAIVG 500
SHKVNGVAEL HSELIKTTIF KDFVKFYGPS KFVNVTNGIT PRRWLKQANP 550
SLAKLISETL NDPTEEYLLD MAKLTQLGKY VEDKEFLKKW NQVKLNNKIR 600
LVDLIKKEND GVDIINREYL DDTLFDMQVK RIHEYKRQQL NVFGIIYRYL 650
AMKNMLKNGA SIEEVAKKYP RKVSIFGGKS APGYYMAKLI IKLINCVADI 700
VNNDESIEHL LKVVFVADYN VSKAEIIIPA SDLSEHISTA GTEASGTSNM 750
KFVMNGGLII GTVDGANVEI TREIGEDNVF LFGNLSENVE ELRYNHQYHP 800
QDLPSSLDSV LSYIESGQFS PENPNEFKPL VDSIKYHGDY YLVSDDFESY 850
LATHELVDQE FHNQRSEWLK KSVLSVANVG FFSSDRCIEE YSDTIWNVEP 900
VT 902
Length:902
Mass (Da):103,275
Last modified:October 5, 2010 - v4
Checksum:iF5B6098D69ABAE43
GO

Sequence cautioni

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

Sequence conflict

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti167 – 1682DL → EG in CAA28273. 1 Publication
Sequence conflicti167 – 1682DL → EG in AAB59313. 1 Publication
Sequence conflicti326 – 3261A → P in CAA28273. 1 Publication
Sequence conflicti326 – 3261A → P in AAB59313. 1 Publication
Sequence conflicti440 – 4412VG → RR in CAA28273. 1 Publication
Sequence conflicti440 – 4412VG → RR in AAB59313. 1 Publication
Sequence conflicti508 – 5081A → V in CAA28273. 1 Publication
Sequence conflicti508 – 5081A → V in AAB59313. 1 Publication
Sequence conflicti524 – 5241V → I in CAA28273. 1 Publication
Sequence conflicti524 – 5241V → I in AAB59313. 1 Publication
Sequence conflicti578 – 5781G → E in CAA28273. 1 Publication
Sequence conflicti578 – 5781G → E in AAB59313. 1 Publication
Sequence conflicti876 – 8761V → L in CAA28273. 1 Publication
Sequence conflicti876 – 8761V → L in AAB59313. 1 Publication

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
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:
EMBL
GenBank
DDBJ
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 .
PIRi S61144.
RefSeqi NP_015486.1. NM_001184257.1.

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
1YGP X-ray 2.80 A/B 24-902 [» ]
ProteinModelPortali P06738.
SMRi P06738. Positions 27-901.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 36333. 91 interactions.
DIPi DIP-2648N.
IntActi P06738. 12 interactions.
MINTi MINT-426238.
STRINGi 4932.YPR160W.

Protein family/group databases

CAZyi GT35. Glycosyltransferase Family 35.

Proteomic databases

MaxQBi P06738.
PaxDbi P06738.
PeptideAtlasi P06738.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

EnsemblFungii YPR160W ; YPR160W ; YPR160W .
GeneIDi 856289.
KEGGi sce:YPR160W.

Organism-specific databases

SGDi S000006364. GPH1.

Phylogenomic databases

eggNOGi COG0058.
GeneTreei ENSGT00390000016886.
HOGENOMi HOG000278444.
KOi K00688.
OMAi MDQISSG.
OrthoDBi EOG7FJH7X.

Enzyme and pathway databases

BioCyci MetaCyc:MONOMER-13684.
YEAST:YPR160W-MONOMER.

Miscellaneous databases

EvolutionaryTracei P06738.
NextBioi 981626.

Gene expression databases

Genevestigatori P06738.

Family and domain databases

InterProi IPR011833. Glycg_phsphrylas.
IPR000811. Glyco_trans_35.
[Graphical view ]
PANTHERi PTHR11468. PTHR11468. 1 hit.
Pfami PF00343. Phosphorylase. 1 hit.
[Graphical view ]
PIRSFi PIRSF000460. Pprylas_GlgP. 1 hit.
TIGRFAMsi TIGR02093. P_ylase. 1 hit.
PROSITEi PS00102. PHOSPHORYLASE. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  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.
    , 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. 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. 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.

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: June 11, 2014
This is version 145 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

External Data

Dasty 3

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