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P06738

- PHSG_YEAST

UniProt

P06738 - PHSG_YEAST

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Protein

Glycogen phosphorylase

Gene

GPH1

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

Enzyme regulationi

Activated by phosphorylation of Thr-31.

GO - Molecular functioni

  1. glycogen phosphorylase activity Source: SGD
  2. 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.
ReactomeiREACT_244738. 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
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. 93 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 – 4410Combined sources
Helixi47 – 559Combined sources
Helixi64 – 7613Combined sources
Helixi83 – 853Combined sources
Helixi88 – 11730Combined sources
Beta strandi121 – 1255Combined sources
Helixi134 – 1407Combined sources
Helixi158 – 16811Combined sources
Helixi172 – 1765Combined sources
Helixi188 – 20215Combined sources
Beta strandi207 – 2126Combined sources
Beta strandi220 – 2245Combined sources
Beta strandi227 – 2315Combined sources
Turni235 – 2384Combined sources
Beta strandi244 – 25613Combined sources
Beta strandi258 – 2603Combined sources
Beta strandi273 – 2753Combined sources
Beta strandi277 – 29014Combined sources
Beta strandi297 – 30812Combined sources
Helixi313 – 3175Combined sources
Helixi321 – 3244Combined sources
Helixi326 – 33611Combined sources
Beta strandi337 – 3393Combined sources
Helixi345 – 37228Combined sources
Helixi377 – 3793Combined sources
Helixi380 – 3834Combined sources
Beta strandi384 – 3918Combined sources
Turni392 – 3943Combined sources
Helixi395 – 40612Combined sources
Helixi412 – 42211Combined sources
Beta strandi423 – 4275Combined sources
Helixi432 – 4343Combined sources
Beta strandi437 – 4393Combined sources
Helixi440 – 4467Combined sources
Helixi448 – 46821Combined sources
Helixi474 – 4796Combined sources
Beta strandi481 – 4833Combined sources
Beta strandi486 – 4883Combined sources
Beta strandi490 – 4923Combined sources
Helixi493 – 5008Combined sources
Beta strandi501 – 5088Combined sources
Helixi509 – 5179Combined sources
Turni518 – 5203Combined sources
Helixi521 – 5277Combined sources
Helixi529 – 5313Combined sources
Beta strandi532 – 5343Combined sources
Helixi541 – 5444Combined sources
Turni545 – 5484Combined sources
Helixi550 – 55910Combined sources
Helixi566 – 5683Combined sources
Helixi571 – 58212Combined sources
Helixi585 – 60723Combined sources
Turni608 – 6114Combined sources
Helixi620 – 6223Combined sources
Beta strandi624 – 6307Combined sources
Helixi634 – 6363Combined sources
Helixi638 – 65720Combined sources
Helixi662 – 6687Combined sources
Beta strandi672 – 6776Combined sources
Helixi685 – 70117Combined sources
Helixi705 – 7073Combined sources
Beta strandi710 – 7167Combined sources
Helixi721 – 7277Combined sources
Helixi728 – 7303Combined sources
Beta strandi732 – 7365Combined sources
Helixi747 – 7537Combined sources
Turni754 – 7563Combined sources
Beta strandi758 – 7636Combined sources
Helixi766 – 7749Combined sources
Helixi776 – 7783Combined sources
Beta strandi779 – 7835Combined sources
Helixi786 – 79813Combined sources
Helixi805 – 8139Combined sources
Turni824 – 8274Combined sources
Helixi828 – 8369Combined sources
Turni838 – 8414Combined sources
Helixi843 – 86321Combined sources
Helixi865 – 87915Combined sources
Helixi880 – 8823Combined sources
Helixi884 – 89411Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1YGPX-ray2.80A/B24-902[»]
ProteinModelPortaliP06738.
SMRiP06738. Positions 27-901.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP06738.

Family & Domainsi

Sequence similaritiesi

Belongs to the glycogen phosphorylase family.Curated

Phylogenomic databases

eggNOGiCOG0058.
GeneTreeiENSGT00390000016886.
HOGENOMiHOG000278444.
InParanoidiP06738.
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

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

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti167 – 1682DL → EG in CAA28273. (PubMed:3537803)Curated
Sequence conflicti167 – 1682DL → EG in AAB59313. (PubMed:7871892)Curated
Sequence conflicti326 – 3261A → P in CAA28273. (PubMed:3537803)Curated
Sequence conflicti326 – 3261A → P in AAB59313. (PubMed:7871892)Curated
Sequence conflicti440 – 4412VG → RR in CAA28273. (PubMed:3537803)Curated
Sequence conflicti440 – 4412VG → RR in AAB59313. (PubMed:7871892)Curated
Sequence conflicti508 – 5081A → V in CAA28273. (PubMed:3537803)Curated
Sequence conflicti508 – 5081A → V in AAB59313. (PubMed:7871892)Curated
Sequence conflicti524 – 5241V → I in CAA28273. (PubMed:3537803)Curated
Sequence conflicti524 – 5241V → I in AAB59313. (PubMed:7871892)Curated
Sequence conflicti578 – 5781G → E in CAA28273. (PubMed:3537803)Curated
Sequence conflicti578 – 5781G → E in AAB59313. (PubMed:7871892)Curated
Sequence conflicti876 – 8761V → L in CAA28273. (PubMed:3537803)Curated
Sequence conflicti876 – 8761V → L in AAB59313. (PubMed:7871892)Curated

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 .
PIRi S61144.
RefSeqi NP_015486.1. NM_001184257.1.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
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. 93 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.
InParanoidi P06738.
KOi K00688.
OMAi MDQISSG.
OrthoDBi EOG7FJH7X.

Enzyme and pathway databases

BioCyci MetaCyc:MONOMER-13684.
YEAST:YPR160W-MONOMER.
Reactomei REACT_244738. Glycogen breakdown (glycogenolysis).

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: November 26, 2014
This is version 148 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