P06738 (PHSG_YEAST) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Glycogen phosphorylase
EC=2.4.1.1

Gene names

Name:	GPH1
Ordered Locus Names:	YPR160W
ORF Names:	P9584.1

Organism

Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast) [Reference proteome]

Taxonomic identifier

559292 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Opisthokonta › Fungi › Dikarya › Ascomycota › saccharomyceta › Saccharomycotina › Saccharomycetes › Saccharomycetales › Saccharomycetaceae › Saccharomyces › Saccharomyces cerevisiae

Protein attributes

Sequence length	902 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Evidence 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.11
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.

Ontologies

Keywords
Biological process	Carbohydrate metabolism Glycogen metabolism
Ligand	Pyridoxal phosphate
Molecular function	Glycosyltransferase Transferase
PTM	Phosphoprotein
Technical term	3D-structure Complete proteome Direct protein sequencing Reference proteome
Gene Ontology (GO)
Biological_process	glycogen catabolic process Inferred from mutant phenotype PubMed 2657401. Source: SGD
Cellular_component	cytoplasm Inferred from direct assay PubMed 14562095. Source: SGD
Molecular_function	glycogen phosphorylase activity Inferred from mutant phenotype PubMed 2657401. Source: SGD pyridoxal phosphate binding Inferred from electronic annotation. Source: InterPro
Complete GO annotation...

Binary interactions

With	Entry	#Exp.	IntAct	Notes
PRP40	P33203	2	EBI-13389,EBI-701
RSP5	P39940	2	EBI-13389,EBI-16219

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Initiator methionine

1

1

Removed Ref.5

Chain

2 – 902

901

Glycogen phosphorylase

PRO_0000188545

Amino acid modifications

Modified residue

18

1

Phosphothreonine Ref.9

Modified residue

19

1

Phosphoserine Ref.9

Modified residue

31

1

Phosphothreonine Ref.5 Ref.6 Ref.7 Ref.8 Ref.9

Modified residue

333

1

Phosphoserine Ref.9

Modified residue

751

1

N6-(pyridoxal phosphate)lysine

Experimental info

Sequence conflict

167 – 168

2

DL → EG in CAA28273. Ref.1

Sequence conflict

167 – 168

2

DL → EG in AAB59313. Ref.2

Sequence conflict

326

1

A → P in CAA28273. Ref.1

Sequence conflict

326

1

A → P in AAB59313. Ref.2

Sequence conflict

440 – 441

2

VG → RR in CAA28273. Ref.1

Sequence conflict

440 – 441

2

VG → RR in AAB59313. Ref.2

Sequence conflict

508

1

A → V in CAA28273. Ref.1

Sequence conflict

508

1

A → V in AAB59313. Ref.2

Sequence conflict

524

1

V → I in CAA28273. Ref.1

Sequence conflict

524

1

V → I in AAB59313. Ref.2

Sequence conflict

578

1

G → E in CAA28273. Ref.1

Sequence conflict

578

1

G → E in AAB59313. Ref.2

Sequence conflict

876

1

V → L in CAA28273. Ref.1

Sequence conflict

876

1

V → L in AAB59313. Ref.2

Secondary structure

1

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902

Helix Strand Turn

Details...

Helix

35 – 44

10

Helix

47 – 55

9

Helix

64 – 76

13

Helix

83 – 85

3

Helix

88 – 117

30

Beta strand

121 – 125

5

Helix

134 – 140

7

Helix

158 – 168

11

Helix

172 – 176

5

Helix

188 – 202

15

Beta strand

207 – 212

6

Beta strand

220 – 224

5

Beta strand

227 – 231

5

Turn

235 – 238

4

Beta strand

244 – 256

13

Beta strand

258 – 260

3

Beta strand

273 – 275

3

Beta strand

277 – 290

14

Beta strand

297 – 308

12

Helix

313 – 317

5

Helix

321 – 324

4

Helix

326 – 336

11

Beta strand

337 – 339

3

Helix

345 – 372

28

Helix

377 – 379

3

Helix

380 – 383

4

Beta strand

384 – 391

8

Turn

392 – 394

3

Helix

395 – 406

12

Helix

412 – 422

11

Beta strand

423 – 427

5

Helix

432 – 434

3

Beta strand

437 – 439

3

Helix

440 – 446

7

Helix

448 – 468

21

Helix

474 – 479

6

Beta strand

481 – 483

3

Beta strand

486 – 488

3

Beta strand

490 – 492

3

Helix

493 – 500

8

Beta strand

501 – 508

8

Helix

509 – 517

9

Turn

518 – 520

3

Helix

521 – 527

7

Helix

529 – 531

3

Beta 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

Beta strand

624 – 630

7

Helix

634 – 636

3

Helix

638 – 657

20

Helix

662 – 668

7

Beta strand

672 – 677

6

Helix

685 – 701

17

Helix

705 – 707

3

Beta strand

710 – 716

7

Helix

721 – 727

7

Helix

728 – 730

3

Beta strand

732 – 736

5

Helix

747 – 753

7

Turn

754 – 756

3

Beta strand

758 – 763

6

Helix

766 – 774

9

Helix

776 – 778

3

Beta 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

Sequences

	Sequence		Length	Mass (Da)
	P06738 [UniParc]. Last modified October 5, 2010. Version 4. Checksum: F5B6098D69ABAE43	FASTA	902	103,275
	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

References

	« Hide 'large scale' referencesShow '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. , 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 204511 / S288c / AB972.
[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]	"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, MASS SPECTROMETRY. Strain: ADR376.
[8]	"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] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-31, MASS SPECTROMETRY.
[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-18; SER-19; THR-31 AND SER-333, MASS SPECTROMETRY.
[10]	"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.
[11]	"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.

PIR

S61144.

RefSeq

NP_015486.1. NM_001184257.1.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
1YGP	X-ray	2.80	A/B	24-902	[»]

ProteinModelPortal

P06738.

SMR

P06738. Positions 27-901.

ModBase

Search...

Protein-protein interaction databases

DIP

DIP-2648N.

IntAct

P06738. 23 interactions.

MINT

MINT-426238.

STRING

4932.YPR160W.

Protein family/group databases

CAZy

GT35. Glycosyltransferase Family 35.

Proteomic databases

PaxDb

P06738.

PeptideAtlas

P06738.

Protocols and materials databases

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

EnsemblFungi

YPR160W; YPR160W; YPR160W.

GeneID

856289.

KEGG

sce:YPR160W.

Organism-specific databases

SGD

S000006364. GPH1.

Phylogenomic databases

eggNOG

COG0058.

GeneTree

ENSGT00390000016886.

HOGENOM

HOG000278444.

KO

K00688.

OMA

IVDVKLF.

OrthoDB

EOG42RHGD.

Enzyme and pathway databases

BioCyc

MetaCyc:MONOMER-13684.

Gene expression databases

Genevestigator

P06738.

GermOnline

YPR160W. Saccharomyces cerevisiae.

Family and domain databases

InterPro

IPR011833. Glycg_phsphrylas.
IPR000811. Glyco_trans_35.
[Graphical view]

PANTHER

PTHR11468. PTHR11468. 1 hit.

Pfam

PF00343. Phosphorylase. 1 hit.
[Graphical view]

PIRSF

PIRSF000460. Pprylas_GlgP. 1 hit.

TIGRFAMs

TIGR02093. P_ylase. 1 hit.

PROSITE

PS00102. PHOSPHORYLASE. 1 hit.
[Graphical view]

ProtoNet

Search...

Other

EvolutionaryTrace

P06738.

NextBio

981626.

Entry information

Entry name

PHSG_YEAST

Accession

Primary (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:	April 3, 2013
This is version 136 of the entry and version 4 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Fungal Protein Annotation Program