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Protein

Glycogen [starch] synthase

Gene

gsy-1

Organism
Caenorhabditis elegans
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Transfers the glycosyl residue from UDP-Glc to the non-reducing end of alpha-1,4-glucan.1 Publication

Catalytic activityi

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

Kineticsi

  1. KM=3.9 mM for UDP-glucose (at 30 degrees Celsius)1 Publication
  1. Vmax=126 pmol/min/µg enzyme1 Publication

Pathwayi: glycogen biosynthesis

This protein is involved in the pathway glycogen biosynthesis, which is part of Glycan biosynthesis.1 Publication
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 sitei56UDP-glucoseBy similarity1

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Glycosyltransferase, Transferase

Keywords - Biological processi

Glycogen biosynthesis

Enzyme and pathway databases

ReactomeiR-CEL-3322077. Glycogen synthesis.
UniPathwayiUPA00164.

Protein family/group databases

CAZyiGT3. Glycosyltransferase Family 3.

Names & Taxonomyi

Protein namesi
Recommended name:
Glycogen [starch] synthase (EC:2.4.1.111 Publication)
Short name:
GS1 Publication
Gene namesi
Name:gsy-1Imported
ORF Names:Y46G5A.31Imported
OrganismiCaenorhabditis elegans
Taxonomic identifieri6239 [NCBI]
Taxonomic lineageiEukaryotaMetazoaEcdysozoaNematodaChromadoreaRhabditidaRhabditoideaRhabditidaePeloderinaeCaenorhabditis
Proteomesi
  • UP000001940 Componenti: Chromosome II

Organism-specific databases

WormBaseiY46G5A.31; CE24302; WBGene00001793; gsy-1.

Pathology & Biotechi

Disruption phenotypei

RNAi-mediated knockdown results in reduced survival.1 Publication

Mutagenesis

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Mutagenesisi151F → A: Partially inhibits the interaction with gyg-1. Loss of function. 1 Publication1
Mutagenesisi151F → R: Partially inhibits the interaction with gyg-1. Loss of function. 1 Publication1
Mutagenesisi157G → R: Partially inhibits the interaction with gyg-1. Loss of function. 1 Publication1
Mutagenesisi257Y → A: Complete inhibition of the interaction with gyg-1. Loss of function. 1 Publication1
Mutagenesisi261C → A: Slight reduction in the interaction with gyg-1. Partial loss of function in absence of glycogen branching enzyme. 1 Publication1
Mutagenesisi261C → R: Complete inhibition of the interaction with gyg-1. Loss of function. 1 Publication1

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00001947701 – 672Glycogen [starch] synthaseAdd BLAST672

Proteomic databases

EPDiQ9U2D9.
PaxDbiQ9U2D9.
PeptideAtlasiQ9U2D9.
PRIDEiQ9U2D9.

PTM databases

iPTMnetiQ9U2D9.

Expressioni

Gene expression databases

BgeeiWBGene00001793.

Interactioni

Subunit structurei

Forms a hetero-octamer with each protomer of the gsy-1 homotetramer bound to one molecule of gyg-1. The N-terminus is involved in interprotomer contacts with gyg-1. The interaction with gyg-1 is required for glycogen production but is not required for gsy-1 intrinsic activity.1 Publication

Protein-protein interaction databases

BioGridi40222. 10 interactors.
DIPiDIP-26557N.
IntActiQ9U2D9. 15 interactors.
MINTiMINT-1087535.
STRINGi6239.Y46G5A.31.

Structurei

Secondary structure

1672
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Beta strandi7 – 9Combined sources3
Helixi13 – 21Combined sources9
Helixi27 – 29Combined sources3
Helixi37 – 42Combined sources6
Beta strandi44 – 50Combined sources7
Turni51 – 54Combined sources4
Beta strandi57 – 59Combined sources3
Helixi60 – 75Combined sources16
Helixi76 – 78Combined sources3
Beta strandi79 – 84Combined sources6
Helixi89 – 92Combined sources4
Beta strandi94 – 96Combined sources3
Helixi102 – 111Combined sources10
Helixi112 – 114Combined sources3
Beta strandi118 – 123Combined sources6
Beta strandi130 – 134Combined sources5
Helixi136 – 142Combined sources7
Helixi143 – 153Combined sources11
Helixi163 – 184Combined sources22
Beta strandi192 – 199Combined sources8
Turni200 – 202Combined sources3
Helixi203 – 211Combined sources9
Beta strandi215 – 224Combined sources10
Helixi226 – 233Combined sources8
Helixi247 – 253Combined sources7
Helixi257 – 269Combined sources13
Beta strandi270 – 277Combined sources8
Helixi278 – 287Combined sources10
Beta strandi293 – 295Combined sources3
Helixi302 – 304Combined sources3
Turni308 – 310Combined sources3
Helixi311 – 329Combined sources19
Turni330 – 332Combined sources3
Helixi338 – 340Combined sources3
Beta strandi341 – 350Combined sources10
Turni352 – 356Combined sources5
Helixi357 – 373Combined sources17
Turni377 – 381Combined sources5
Beta strandi383 – 389Combined sources7
Beta strandi394 – 397Combined sources4
Helixi399 – 430Combined sources32
Turni431 – 433Combined sources3
Helixi438 – 440Combined sources3
Helixi444 – 455Combined sources12
Beta strandi465 – 471Combined sources7
Helixi476 – 483Combined sources8
Beta strandi493 – 498Combined sources6
Helixi514 – 520Combined sources7
Beta strandi522 – 525Combined sources4
Beta strandi529 – 533Combined sources5
Helixi535 – 542Combined sources8
Beta strandi547 – 550Combined sources4
Helixi554 – 562Combined sources9
Helixi566 – 569Combined sources4
Beta strandi571 – 574Combined sources4
Beta strandi577 – 579Combined sources3
Helixi581 – 596Combined sources16
Helixi600 – 613Combined sources14
Helixi614 – 617Combined sources4
Helixi619 – 622Combined sources4
Helixi624 – 637Combined sources14
Helixi641 – 647Combined sources7
Turni649 – 651Combined sources3

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
4QLBX-ray2.60A/B/C/D1-672[»]
ProteinModelPortaliQ9U2D9.
SMRiQ9U2D9.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Belongs to the glycosyltransferase 3 family.Curated

Phylogenomic databases

eggNOGiKOG3742. Eukaryota.
COG0438. LUCA.
GeneTreeiENSGT00390000018612.
HOGENOMiHOG000160890.
InParanoidiQ9U2D9.
KOiK00693.
OMAiFYGHMDF.
OrthoDBiEOG091G0304.
PhylomeDBiQ9U2D9.

Family and domain databases

InterProiIPR008631. Glycogen_synth.
[Graphical view]
PANTHERiPTHR10176. PTHR10176. 1 hit.
PfamiPF05693. Glycogen_syn. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Q9U2D9-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MPDHARMPRN LSSNKIAKTI AGEDLDEEEV LEMDAGQSAR EEGRFVFECA
60 70 80 90 100
WEVANKVGGI YTVLRSKAQI STEELGDQYC MFGPMKDGKW RLEVDPIEPE
110 120 130 140 150
NRTIRAAMKR FQADGFRCMY GRWLIEGYPK VILFDLGSGA VKMNEWKHEL
160 170 180 190 200
FEQCKIGIPH EDIESNDAVI LGFMVALFLK HFRESVTSYT PLVVAHFHEW
210 220 230 240 250
QAGVGLLMTR LWKLDIATVY TTHATLLGRH LCAGGADLYN NLDSFDLDAE
260 270 280 290 300
AGKRKIYHQY CLERAACQTA HIFTTVSEIT GLEAEHFLCR KPDVLTPNGL
310 320 330 340 350
NVVKFAALHE FQNLHAQNKE KINQFIRGHF HGHLDFDLDK TLYFFTAGRY
360 370 380 390 400
EFSNKGGDMF IESLARLNHY LKTTSDPRHM GVTVVAFLIY PAPANSFNVE
410 420 430 440 450
SLKGQAVTKQ LKEAVDRIKE KVGQRIFDIC LQGHLPEPEE LMSPADNILL
460 470 480 490 500
KRCIMSLHNS SLPPICTHNM IRADDPVLES LRRTSLFNKP EDRVKVVFHP
510 520 530 540 550
EFLSSVSPLI GLDYEDFVRG CHLGVFPSYY EPWGYTPAEC TVMGIPSVST
560 570 580 590 600
NLSGFGCFMQ EHVEDHEQKG IYVIDRRHKA AEESVQELAQ VMYDFCGQSR
610 620 630 640 650
RQRIILRNSN EGLSALLDWQ NLGVFYRDCR RLALERLHPD VDKIMRDNEG
660 670
KVPSAATSRR PSIHSSDGED DE
Length:672
Mass (Da):76,459
Last modified:May 1, 2000 - v1
Checksum:i3B3C3E9044CAC8A0
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AL110485 Genomic DNA. Translation: CAB60373.1.
RefSeqiNP_496736.1. NM_064335.5.
UniGeneiCel.7404.

Genome annotation databases

EnsemblMetazoaiY46G5A.31; Y46G5A.31; WBGene00001793.
GeneIDi174924.
KEGGicel:CELE_Y46G5A.31.
UCSCiY46G5A.31. c. elegans.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AL110485 Genomic DNA. Translation: CAB60373.1.
RefSeqiNP_496736.1. NM_064335.5.
UniGeneiCel.7404.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
4QLBX-ray2.60A/B/C/D1-672[»]
ProteinModelPortaliQ9U2D9.
SMRiQ9U2D9.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi40222. 10 interactors.
DIPiDIP-26557N.
IntActiQ9U2D9. 15 interactors.
MINTiMINT-1087535.
STRINGi6239.Y46G5A.31.

Protein family/group databases

CAZyiGT3. Glycosyltransferase Family 3.

PTM databases

iPTMnetiQ9U2D9.

Proteomic databases

EPDiQ9U2D9.
PaxDbiQ9U2D9.
PeptideAtlasiQ9U2D9.
PRIDEiQ9U2D9.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblMetazoaiY46G5A.31; Y46G5A.31; WBGene00001793.
GeneIDi174924.
KEGGicel:CELE_Y46G5A.31.
UCSCiY46G5A.31. c. elegans.

Organism-specific databases

CTDi174924.
WormBaseiY46G5A.31; CE24302; WBGene00001793; gsy-1.

Phylogenomic databases

eggNOGiKOG3742. Eukaryota.
COG0438. LUCA.
GeneTreeiENSGT00390000018612.
HOGENOMiHOG000160890.
InParanoidiQ9U2D9.
KOiK00693.
OMAiFYGHMDF.
OrthoDBiEOG091G0304.
PhylomeDBiQ9U2D9.

Enzyme and pathway databases

UniPathwayiUPA00164.
ReactomeiR-CEL-3322077. Glycogen synthesis.

Miscellaneous databases

PROiQ9U2D9.

Gene expression databases

BgeeiWBGene00001793.

Family and domain databases

InterProiIPR008631. Glycogen_synth.
[Graphical view]
PANTHERiPTHR10176. PTHR10176. 1 hit.
PfamiPF05693. Glycogen_syn. 1 hit.
[Graphical view]
ProtoNetiSearch...

Entry informationi

Entry nameiGYS_CAEEL
AccessioniPrimary (citable) accession number: Q9U2D9
Entry historyi
Integrated into UniProtKB/Swiss-Prot: January 11, 2001
Last sequence update: May 1, 2000
Last modified: November 2, 2016
This is version 111 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programCaenorhabditis annotation project

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

Documents

  1. Caenorhabditis elegans
    Caenorhabditis elegans: entries, gene names and cross-references to WormBase
  2. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  3. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  4. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.