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Protein

Glycogen [starch] synthase isoform 2

Gene

GSY2

Organism
Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Status
Reviewed-Annotation score: -Experimental evidence at protein leveli

Functioni

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.

Miscellaneous

Present with 14600 molecules/cell in log phase SD medium.1 Publication

Catalytic activityi

UDP-alpha-D-glucose + ((1->4)-alpha-D-glucosyl)(n) = UDP + ((1->4)-alpha-D-glucosyl)(n+1).

Enzyme regulationi

Allosteric activation by glucose-6-phosphate, and phosphorylation by a cAMP-dependent kinase.

Pathwayi: glycogen biosynthesis

This protein is involved in the pathway glycogen biosynthesis, which is part of Glycan biosynthesis.
View all proteins of this organism that are known to be involved in the pathway glycogen biosynthesis and in Glycan biosynthesis.

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Binding sitei20UDP-glucoseBy similarity1

GO - Molecular functioni

  • glycogen (starch) synthase activity Source: SGD
  • identical protein binding Source: IntAct

GO - Biological processi

  • glycogen biosynthetic process Source: SGD

Keywordsi

Molecular functionAllosteric enzyme, Glycosyltransferase, Transferase
Biological processGlycogen biosynthesis

Enzyme and pathway databases

BioCyciYEAST:YLR258W-MONOMER
UniPathwayiUPA00164

Protein family/group databases

CAZyiGT3 Glycosyltransferase Family 3

Names & Taxonomyi

Protein namesi
Recommended name:
Glycogen [starch] synthase isoform 2 (EC:2.4.1.11)
Gene namesi
Name:GSY2
Ordered Locus Names:YLR258W
ORF Names:L8479.8
OrganismiSaccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Taxonomic identifieri559292 [NCBI]
Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaSaccharomycotinaSaccharomycetesSaccharomycetalesSaccharomycetaceaeSaccharomyces
Proteomesi
  • UP000002311 Componenti: Chromosome XII

Organism-specific databases

EuPathDBiFungiDB:YLR258W
SGDiS000004248 GSY2

Subcellular locationi

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00001947741 – 705Glycogen [starch] synthase isoform 2Add BLAST705

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei159PhosphoserineSequence analysis1
Modified residuei363PhosphoserineSequence analysis1
Modified residuei467PhosphoserineCombined sources1
Modified residuei651PhosphoserineCombined sources1
Modified residuei655Phosphoserine; by PHO85Combined sources1 Publication1
Modified residuei661Phosphoserine; by PKASequence analysis1
Modified residuei663Phosphoserine; by PKASequence analysis1
Modified residuei668Phosphothreonine; by PHO851 Publication1

Post-translational modificationi

Phosphorylated by the cyclin-CDK PCL10-PHO85. Phosphorylation causes inactivation of enzyme.1 Publication

Keywords - PTMi

Phosphoprotein

Proteomic databases

MaxQBiP27472
PaxDbiP27472
PRIDEiP27472
TopDownProteomicsiP27472

PTM databases

iPTMnetiP27472

Interactioni

Subunit structurei

Interacts with PCL10.1 Publication

Binary interactionsi

Show more details

GO - Molecular functioni

  • identical protein binding Source: IntAct

Protein-protein interaction databases

BioGridi31526, 99 interactors
DIPiDIP-1255N
IntActiP27472, 34 interactors
MINTiP27472
STRINGi4932.YLR258W

Structurei

Secondary structure

1705
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Beta strandi4 – 14Combined sources11
Turni15 – 18Combined sources4
Helixi23 – 39Combined sources17
Helixi40 – 42Combined sources3
Beta strandi43 – 48Combined sources6
Turni51 – 53Combined sources3
Helixi54 – 57Combined sources4
Beta strandi58 – 60Combined sources3
Beta strandi63 – 65Combined sources3
Helixi66 – 68Combined sources3
Helixi71 – 73Combined sources3
Helixi74 – 84Combined sources11
Turni85 – 87Combined sources3
Beta strandi90 – 97Combined sources8
Beta strandi102 – 106Combined sources5
Helixi109 – 114Combined sources6
Helixi115 – 126Combined sources12
Helixi135 – 157Combined sources23
Beta strandi160 – 169Combined sources10
Helixi170 – 172Combined sources3
Helixi175 – 181Combined sources7
Beta strandi187 – 194Combined sources8
Helixi196 – 201Combined sources6
Beta strandi203 – 205Combined sources3
Helixi209 – 212Combined sources4
Helixi213 – 215Combined sources3
Helixi218 – 224Combined sources7
Helixi228 – 240Combined sources13
Beta strandi241 – 248Combined sources8
Helixi249 – 258Combined sources10
Beta strandi259 – 261Combined sources3
Beta strandi264 – 266Combined sources3
Helixi273 – 276Combined sources4
Helixi281 – 300Combined sources20
Turni301 – 303Combined sources3
Helixi309 – 311Combined sources3
Beta strandi312 – 320Combined sources9
Turni323 – 327Combined sources5
Helixi328 – 344Combined sources17
Beta strandi350 – 356Combined sources7
Beta strandi361 – 364Combined sources4
Helixi366 – 399Combined sources34
Turni400 – 404Combined sources5
Beta strandi407 – 409Combined sources3
Helixi413 – 416Combined sources4
Helixi419 – 432Combined sources14
Beta strandi442 – 447Combined sources6
Helixi450 – 452Combined sources3
Helixi454 – 462Combined sources9
Beta strandi471 – 476Combined sources6
Beta strandi486 – 488Combined sources3
Helixi492 – 498Combined sources7
Beta strandi500 – 503Combined sources4
Beta strandi507 – 511Combined sources5
Helixi513 – 520Combined sources8
Beta strandi525 – 528Combined sources4
Helixi532 – 538Combined sources7
Helixi543 – 548Combined sources6
Beta strandi551 – 554Combined sources4
Beta strandi557 – 559Combined sources3
Helixi561 – 576Combined sources16
Helixi580 – 592Combined sources13
Helixi593 – 597Combined sources5
Helixi599 – 617Combined sources19
Helixi619 – 624Combined sources6
Beta strandi626 – 628Combined sources3
Helixi635 – 638Combined sources4

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
3NAZX-ray3.00A/B/C/D1-705[»]
3NB0X-ray2.41A/B/C/D1-705[»]
3NCHX-ray2.88A/B/C/D1-705[»]
3O3CX-ray3.51A/B/C/D1-705[»]
3RSZX-ray3.01A/B/C/D1-705[»]
3RT1X-ray2.80A/B/C/D1-705[»]
4KQ2X-ray2.95A/B/C/D1-705[»]
4KQMX-ray2.77A/B/C/D1-705[»]
5SUKX-ray2.88A/B/C/D1-705[»]
5SULX-ray3.30A/B1-705[»]
5UW0X-ray2.73A/B/C/D1-700[»]
5UW1X-ray3.26A/B/C/D1-700[»]
5UW4X-ray2.98A/B/C/D1-700[»]
5UX7X-ray2.69A/B/C/D1-700[»]
ProteinModelPortaliP27472
SMRiP27472
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP27472

Family & Domainsi

Sequence similaritiesi

Belongs to the glycosyltransferase 3 family.Curated

Phylogenomic databases

HOGENOMiHOG000160890
InParanoidiP27472
KOiK00693
OMAiTADEWGD
OrthoDBiEOG092C0XGC

Family and domain databases

CDDicd03793 GT1_Glycogen_synthase_GSY2_lik, 1 hit
InterProiView protein in InterPro
IPR008631 Glycogen_synth
PANTHERiPTHR10176 PTHR10176, 1 hit
PfamiView protein in Pfam
PF05693 Glycogen_syn, 1 hit

Sequencei

Sequence statusi: Complete.

P27472-1 [UniParc]FASTAAdd to basket

« Hide

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

YADDS
Length:705
Mass (Da):80,079
Last modified:January 23, 2007 - v3
Checksum:i4670D8328CEDB0D2
GO

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sequence conflicti248S → P AA sequence (PubMed:2114092).Curated1
Sequence conflicti535A → S in AAA88716 (PubMed:1908457).Curated1
Sequence conflicti622F → FF AA sequence (PubMed:2114092).Curated1

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M65206 Genomic DNA Translation: AAA88716.1
U17244 Genomic DNA Translation: AAB67378.1
BK006945 Genomic DNA Translation: DAA09571.1
PIRiS51396
RefSeqiNP_013359.1, NM_001182145.1

Genome annotation databases

EnsemblFungiiYLR258W; YLR258W; YLR258W
GeneIDi850962
KEGGisce:YLR258W

Similar proteinsi

Entry informationi

Entry nameiGYS2_YEAST
AccessioniPrimary (citable) accession number: P27472
Secondary accession number(s): D6VYQ5
Entry historyiIntegrated into UniProtKB/Swiss-Prot: August 1, 1992
Last sequence update: January 23, 2007
Last modified: April 25, 2018
This is version 168 of the entry and version 3 of the sequence. See 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
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Main funding by: National Institutes of Health