Reviewed, UniProtKB/Swiss-Prot P27472 (GYS2_YEAST)

Names and origin

Protein names

Recommended name:
    Glycogen [starch] synthase isoform 2
    EC=2.4.1.11

Gene names

Name:	GSY2
Ordered Locus Names:	YLR258W
ORF Names:	L8479.8

Organism

Saccharomyces cerevisiae (Baker's yeast) [Complete proteome]

Taxonomic identifier

4932 [NCBI]

Taxonomic lineage

Eukaryota › Fungi › Dikarya › Ascomycota › Saccharomycotina › Saccharomycetes › Saccharomycetales › Saccharomycetaceae › Saccharomyces

Protein attributes

Sequence length	705 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	Transfers the glycosyl residue from UDP-Glc to the non-reducing end of alpha-1,4-glucan. Is believed to regulate the synthesis of glycogen.
Catalytic activity	UDP-glucose ((1->4)-alpha-D-glucosyl)(n) = UDP + ((1->4)-alpha-D-glucosyl)(n+1).
Enzyme regulation	Allosteric activation by glucose-6-phosphate, and phosphorylation by a cAMP-dependent kinase.
Pathway	Glycan biosynthesis; glycogen biosynthesis.
Subunit structure	Interacts with PCL10. Ref.4
Post-translational modification	Phosphorylated by the cyclin-CDK PCL10-PHO85. Phosphorylation causes inactivation of enzyme. Ref.3 Ref.5 Ref.7 Ref.8 Ref.9
Miscellaneous	Present with 14600 molecules/cell in log phase SD medium. Ref.6
Sequence similarities	Belongs to the glycosyltransferase 3 family.

Ontologies

Keywords
Biological process	Glycogen biosynthesis
Molecular function	Glycosyltransferase Transferase
PTM	Phosphoprotein
Technical term	Allosteric enzyme Complete proteome
Gene Ontology (GO)
Biological process	glycogen biosynthetic process Ref.1 Inferred from genetic interaction. Source: SGD
Cellular component	cytoplasm Inferred from direct assay. Source: SGD
Molecular function	glycogen (starch) synthase activity Ref.1 Inferred from genetic interaction. Source: SGD identical protein binding Inferred from physical interaction. Source: IntAct
Complete GO annotation...

Binary interactions

With	Entry	#Exp.	IntAct	Notes
itself		2	EBI-8036,EBI-8036
ADE17	P38009	1	EBI-8036,EBI-14223
ARO8	P53090	1	EBI-8036,EBI-2042933
GDB1	Q06625	1	EBI-8036,EBI-37861
GLG1	P36143	1	EBI-8036,EBI-2064417
GLG2	P47011	1	EBI-8036,EBI-7646
GLN1	P32288	1	EBI-8036,EBI-7665
GSY1	P23337	1	EBI-8036,EBI-8031
IPP1	P00817	1	EBI-8036,EBI-9338
MBF1	O14467	1	EBI-8036,EBI-2043025
PIG2	P40187	1	EBI-8036,EBI-13419
RNR2	P09938	1	EBI-8036,EBI-15240
RSP5	P39940	1	EBI-8036,EBI-16219

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Initiator methionine	1	1	Removed By similarity
	Chain	2 – 705	704	Glycogen [starch] synthase isoform 2		PRO_0000194774
Sites
	Binding site	20	1	UDP-glucose By similarity
Amino acid modifications
	Modified residue	159	1	Phosphoserine Potential
	Modified residue	363	1	Phosphoserine Potential
	Modified residue	467	1	Phosphoserine Ref.8 Ref.9
	Modified residue	651	1	Phosphoserine Ref.5 Ref.7 Ref.8 Ref.9
	Modified residue	655	1	Phosphoserine; by PHO85 Ref.3 Ref.5 Ref.7 Ref.8 Ref.9
	Modified residue	661	1	Phosphoserine; by PKA Potential
	Modified residue	663	1	Phosphoserine; by PKA Potential
	Modified residue	668	1	Phosphothreonine; by PHO85 Ref.3
Experimental info
	Sequence conflict	535	1	A → S in AAA88716. Ref.1

Sequences

	Sequence		Length	Mass (Da)
	P27472-1 [UniParc]. Last modified January 23, 2007. Version 3. Checksum: 4670D8328CEDB0D2	FASTA	705	80,079
	10 20 30 40 50 60 MSRDLQNHLL FETATEVANR VGGIYSVLKS KAPITVAQYK DHYHLIGPLN KATYQNEVDI 70 80 90 100 110 120 LDWKKPEAFS DEMRPVQHAL QTMESRGVHF VYGRWLIEGA PKVILFDLDS VRGYSNEWKG 130 140 150 160 170 180 DLWSLVGIPS PENDFETNDA ILLGYTVAWF LGEVAHLDSQ HAIVAHFHEW LAGVALPLCR 190 200 210 220 230 240 KRRIDVVTIF TTHATLLGRY LCASGSFDFY NCLESVDVDH EAGRFGIYHR YCIERAAAHS 250 260 270 280 290 300 ADVFTTVSQI TAFEAEHLLK RKPDGILPNG LNVIKFQAFH EFQNLHALKK EKINDFVRGH 310 320 330 340 350 360 FHGCFDFDLD NTLYFFIAGR YEYKNKGADM FIEALARLNY RLKVSGSKKT VVAFIVMPAK 370 380 390 400 410 420 NNSFTVEALK GQAEVRALEN TVHEVTTSIG KRIFDHAIRY PHNGLTTELP TDLGELLKSS 430 440 450 460 470 480 DKVMLKRRIL ALRRPEGQLP PIVTHNMVDD ANDLILNKIR QVQLFNSPSD RVKMIFHPEF 490 500 510 520 530 540 LNANNPILGL DYDEFVRGCH LGVFPSYYEP WGYTPAECTV MGVPSITTNV SGFGAYMEDL 550 560 570 580 590 600 IETNQAKDYG IYIVDRRFKA PDESVEQLVD YMEEFVKKTR RQRINQRNRT ERLSDLLDWK 610 620 630 640 650 660 RMGLEYVKAR QLALRRGYPD QFRELVGEEL NDSNMDALAG GKKLKVARPL SVPGSPRDLR 670 680 690 700 SNSTVYMTPG DLGTLQEVNN ADDYFSLGVN PAADDDDDGP YADDS

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Two glycogen synthase isoforms in Saccharomyces cerevisiae are coded by distinct genes that are differentially controlled." Farkast I., Hardy T.A., Roach P.J., Goebl M.G. J. Biol. Chem. 266:15602-15607(1991) [PubMed: 1908457] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[2]	"The nucleotide sequence of Saccharomyces cerevisiae chromosome XII." Johnston M., Hillier L.W., Riles L., Albermann K., Andre B., Ansorge W., Benes V., Brueckner M., Delius H., Dubois E., Duesterhoeft A., Entian K.-D., Floeth M., Goffeau A., Hebling U., Heumann K., Heuss-Neitzel D., Hilbert H. , Hilger F., Kleine K., Koetter P., Louis E.J., Messenguy F., Mewes H.-W., Miosga T., Moestl D., Mueller-Auer S., Nentwich U., Obermaier B., Piravandi E., Pohl T.M., Portetelle D., Purnelle B., Rechmann S., Rieger M., Rinke M., Rose M., Scharfe M., Scherens B., Scholler P., Schwager C., Schwarz S., Underwood A.P., Urrestarazu L.A., Vandenbol M., Verhasselt P., Vierendeels F., Voet M., Volckaert G., Voss H., Wambutt R., Wedler E., Wedler H., Zimmermann F.K., Zollner A., Hani J., Hoheisel J.D. Nature 387:87-90(1997) [PubMed: 9169871] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: ATCC 204511 / S288c / AB972.
[3]	"Cyclin partners determine Pho85 protein kinase substrate specificity in vitro and in vivo: control of glycogen biosynthesis by Pcl8 and Pcl10." Huang D., Moffat J., Wilson W.A., Moore L., Cheng C., Roach P.J., Andrews B.J. Mol. Cell. Biol. 18:3289-3299(1998) [PubMed: 9584169] [Abstract] Cited for: PHOSPHORYLATION AT SER-655 AND THR-668.
[4]	"Substrate targeting of the yeast cyclin-dependent kinase Pho85p by the cyclin Pcl10p." Wilson W.A., Mahrenholz A.M., Roach P.J. Mol. Cell. Biol. 19:7020-7030(1999) [PubMed: 10490639] [Abstract] Cited for: INTERACTION WITH PCL10.
[5]	"Phosphoproteome analysis by mass spectrometry and its application to Saccharomyces cerevisiae." Ficarro S.B., McCleland M.L., Stukenberg P.T., Burke D.J., Ross M.M., Shabanowitz J., Hunt D.F., White F.M. Nat. Biotechnol. 20:301-305(2002) [PubMed: 11875433] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-651 AND SER-655, MASS SPECTROMETRY.
[6]	"Global analysis of protein expression in yeast." Ghaemmaghami S., Huh W.-K., Bower K., Howson R.W., Belle A., Dephoure N., O'Shea E.K., Weissman J.S. Nature 425:737-741(2003) [PubMed: 14562106] [Abstract] Cited for: LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS].
[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: 17330950] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-651 AND SER-655, MASS SPECTROMETRY.
[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: 17563356] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-467; SER-651 AND SER-655, 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: 18407956] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-467; SER-651 AND SER-655, MASS SPECTROMETRY.
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBLGenBankDDBJ	M65206 Genomic DNA. Translation: AAA88716.1. U17244 Genomic DNA. Translation: AAB67378.1.
PIR	S51396.
RefSeq	NP_013359.1.
3D structure databases
ModBase	Search...
Protein-protein interaction databases
DIP	DIP:1255N.
IntAct	P27472. 26 interactions.
Protein family/group databases
CAZy	GT3. Glycosyltransferase Family 3.
Proteomic databases
PeptideAtlas	P27472.
PRIDE	P27472.
Genome annotation databases
Ensembl	YLR258W. Saccharomyces cerevisiae. [Contig view]
GeneID	850962.
GenomeReviews	Gene locus YLR258W in contig Y13138_GR.
KEGG	sce:YLR258W.
NMPDR	fig|4932.3.peg.4373.
Organism-specific databases
CYGD	YLR258w.
SGD	S000004248. GSY2.
Yeast-GFP	Search...
Phylogenomic databases
HOGENOM	P27472.
OMA	P27472. VFECAWE.
Enzyme and pathway databases
BRENDA	2.4.1.11. 250.
Gene expression databases
ArrayExpress	P27472.
GermOnline	YLR258W. Saccharomyces cerevisiae.
Family and domain databases
InterPro	IPR008631. Glycogen_synth. [Graphical view]
PANTHER	PTHR10176. Glycogen_synth. 1 hit.
Pfam	PF05693. Glycogen_syn. 1 hit. [Graphical view]
ProtoNet	Search...
Other Resources
NextBio	967445.

Entry information

Entry name

GYS2_YEAST

Accession

Primary (citable) accession number: P27472

Entry history

Integrated into UniProtKB/Swiss-Prot:	August 1, 1992
Last sequence update:	January 23, 2007
Last modified:	June 16, 2009
This is version 85 of the entry and version 3 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

FPAP (Fungal Proteome Annotation Project)