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Protein

Glycogenin-1

Gene

GYG1

Organism
Oryctolagus cuniculus (Rabbit)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Self-glucosylates, via an inter-subunit mechanism, to form an oligosaccharide primer that serves as substrate for glycogen synthase.

Catalytic activityi

UDP-alpha-D-glucose + glycogenin = UDP + alpha-D-glucosylglycogenin.

Cofactori

Mn2+1 PublicationNote: Divalent metal ions. Required for self-glucosylation. Manganese is the most effective.1 Publication

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
Active sitei861 Publication1
Metal bindingi102Manganese1 Publication1
Metal bindingi104Manganese1 Publication1
Sitei160Important for catalytic activity1 Publication1
Sitei163Important for catalytic activity1 Publication1
Metal bindingi212Manganese1 Publication1

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Transferase

Keywords - Biological processi

Glycogen biosynthesis

Keywords - Ligandi

Manganese, Metal-binding

Enzyme and pathway databases

BRENDAi2.4.1.186. 1749.
UniPathwayiUPA00164.

Protein family/group databases

CAZyiGT8. Glycosyltransferase Family 8.

Names & Taxonomyi

Protein namesi
Recommended name:
Glycogenin-1 (EC:2.4.1.186)
Short name:
GN-1
Short name:
GN1
Gene namesi
Name:GYG1
Synonyms:GYG
OrganismiOryctolagus cuniculus (Rabbit)
Taxonomic identifieri9986 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresLagomorphaLeporidaeOryctolagus
Proteomesi
  • UP000001811 Componenti: Unplaced

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Mutagenesisi86K → Q: Loss of activity. 1 Publication1
Mutagenesisi160D → N or S: Reduced trans-glucosylation activity by at least 260-fold and reduced UDP-glucose hydrolytic activity by 4 to 14-fold. 1 Publication1
Mutagenesisi163D → N: Loss of self-glucosylation activity and ability to trans-glucosylate maltose. Reduced UDP-glucose hydrolytic activity by at least 190-fold. 1 Publication1
Mutagenesisi163D → S: Loss of self-glucosylation activity and 18 to 30-fold reduction in its ability to trans-glucosylate maltose. Reduced UDP-glucose hydrolytic activity by at least 190-fold. 1 Publication1

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Initiator methionineiRemovedBy similarity1 Publication
ChainiPRO_00002151782 – 333Glycogenin-1CuratedAdd BLAST332

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei2N-acetylthreonineBy similarity1
Modified residuei44Phosphoserine; by PKA; in vitro1 Publication1
Glycosylationi195O-linked (Glc...)1 Publication1

Post-translational modificationi

Self-glycosylated by the transfer of glucose residues from UDP-glucose to itself, forming an alpha-1,4-glycan of around 10 residues attached to Tyr-195.1 Publication
Phosphorylated.1 Publication

Keywords - PTMi

Acetylation, Glycoprotein, Phosphoprotein

Proteomic databases

PRIDEiP13280.

PTM databases

iPTMnetiP13280.

Interactioni

Subunit structurei

Homodimer tightly complexed to the 86 kDa catalytic subunit of glycogen synthase GYS1 (PubMed:12051921, PubMed:15849187). Interacts (via C-terminus) with GYS2; required for GYS2-mediated glycogen synthesis (By similarity).By similarity2 Publications

Structurei

Secondary structure

1333
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Beta strandi3 – 12Combined sources10
Helixi13 – 28Combined sources16
Beta strandi33 – 39Combined sources7
Helixi45 – 54Combined sources10
Beta strandi56 – 60Combined sources5
Helixi71 – 76Combined sources6
Helixi78 – 80Combined sources3
Helixi81 – 86Combined sources6
Helixi87 – 91Combined sources5
Beta strandi96 – 101Combined sources6
Beta strandi105 – 107Combined sources3
Helixi112 – 116Combined sources5
Beta strandi119 – 124Combined sources6
Beta strandi126 – 128Combined sources3
Beta strandi131 – 139Combined sources9
Helixi143 – 155Combined sources13
Beta strandi159 – 162Combined sources4
Helixi163 – 170Combined sources8
Turni171 – 176Combined sources6
Helixi179 – 181Combined sources3
Helixi185 – 187Combined sources3
Beta strandi188 – 190Combined sources3
Helixi193 – 196Combined sources4
Helixi198 – 204Combined sources7
Helixi205 – 207Combined sources3
Beta strandi209 – 212Combined sources4
Beta strandi215 – 217Combined sources3
Helixi219 – 221Combined sources3
Beta strandi222 – 225Combined sources4
Turni226 – 229Combined sources4
Beta strandi230 – 232Combined sources3
Helixi243 – 255Combined sources13
Helixi257 – 261Combined sources5
Helixi263 – 265Combined sources3

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1LL0X-ray3.43A/B/C/D/E/F/G/H/I/J1-333[»]
1LL2X-ray1.90A1-333[»]
1LL3X-ray1.90A1-333[»]
1ZCTX-ray2.60A/B1-270[»]
1ZCUX-ray2.00A1-333[»]
1ZCVX-ray1.98A1-333[»]
1ZCYX-ray1.99A1-333[»]
1ZDFX-ray2.45A1-333[»]
1ZDGX-ray2.30A1-333[»]
3USQX-ray2.40A1-271[»]
3USRX-ray2.10A1-271[»]
3V8YX-ray2.15A1-271[»]
3V8ZX-ray2.20A1-271[»]
3V90X-ray2.00A1-271[»]
3V91X-ray2.00A1-271[»]
ProteinModelPortaliP13280.
SMRiP13280.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP13280.

Family & Domainsi

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni284 – 316Interaction with GYS1By similarityAdd BLAST33

Sequence similaritiesi

Phylogenomic databases

HOGENOMiHOG000008282.
HOVERGENiHBG000681.
InParanoidiP13280.
KOiK00750.

Family and domain databases

Gene3Di3.90.550.10. 1 hit.
InterProiIPR002495. Glyco_trans_8.
IPR029044. Nucleotide-diphossugar_trans.
[Graphical view]
PfamiPF01501. Glyco_transf_8. 1 hit.
[Graphical view]
SUPFAMiSSF53448. SSF53448. 1 hit.

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

P13280-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MTDQAFVTLT TNDAYAKGAL VLGSSLKQHR TSRRLAVLTT PQVSDTMRKA
60 70 80 90 100
LEIVFDEVIT VDILDSGDSA HLTLMKRPEL GVTLTKLHCW SLTQYSKCVF
110 120 130 140 150
MDADTLVLAN IDDLFEREEL SAAPDPGWPD CFNSGVFVYQ PSVETYNQLL
160 170 180 190 200
HVASEQGSFD GGDQGLLNTF FNSWATTDIR KHLPFIYNLS SISIYSYLPA
210 220 230 240 250
FKAFGANAKV VHFLGQTKPW NYTYDTKTKS VRSEGHDPTM THPQFLNVWW
260 270 280 290 300
DIFTTSVVPL LQQFGLVQDT CSYQHVEDVS GAVSHLSLGE TPATTQPFVS
310 320 330
SEERKERWEQ GQADYMGADS FDNIKKKLDT YLQ
Length:333
Mass (Da):37,397
Last modified:January 23, 2007 - v3
Checksum:i7C27F7B428F67571
GO

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sequence conflicti39T → L AA sequence (PubMed:3151442).Curated1
Sequence conflicti89C → S AA sequence (PubMed:2806254).Curated1
Sequence conflicti98C → L AA sequence (PubMed:2806254).Curated1

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
L01791 mRNA. Translation: AAA31404.1.
PIRiA45094.
RefSeqiNP_001075710.1. NM_001082241.1.
UniGeneiOcu.1930.

Genome annotation databases

GeneIDi100009058.
KEGGiocu:100009058.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
L01791 mRNA. Translation: AAA31404.1.
PIRiA45094.
RefSeqiNP_001075710.1. NM_001082241.1.
UniGeneiOcu.1930.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1LL0X-ray3.43A/B/C/D/E/F/G/H/I/J1-333[»]
1LL2X-ray1.90A1-333[»]
1LL3X-ray1.90A1-333[»]
1ZCTX-ray2.60A/B1-270[»]
1ZCUX-ray2.00A1-333[»]
1ZCVX-ray1.98A1-333[»]
1ZCYX-ray1.99A1-333[»]
1ZDFX-ray2.45A1-333[»]
1ZDGX-ray2.30A1-333[»]
3USQX-ray2.40A1-271[»]
3USRX-ray2.10A1-271[»]
3V8YX-ray2.15A1-271[»]
3V8ZX-ray2.20A1-271[»]
3V90X-ray2.00A1-271[»]
3V91X-ray2.00A1-271[»]
ProteinModelPortaliP13280.
SMRiP13280.
ModBaseiSearch...
MobiDBiSearch...

Protein family/group databases

CAZyiGT8. Glycosyltransferase Family 8.

PTM databases

iPTMnetiP13280.

Proteomic databases

PRIDEiP13280.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

GeneIDi100009058.
KEGGiocu:100009058.

Organism-specific databases

CTDi2992.

Phylogenomic databases

HOGENOMiHOG000008282.
HOVERGENiHBG000681.
InParanoidiP13280.
KOiK00750.

Enzyme and pathway databases

UniPathwayiUPA00164.
BRENDAi2.4.1.186. 1749.

Miscellaneous databases

EvolutionaryTraceiP13280.

Family and domain databases

Gene3Di3.90.550.10. 1 hit.
InterProiIPR002495. Glyco_trans_8.
IPR029044. Nucleotide-diphossugar_trans.
[Graphical view]
PfamiPF01501. Glyco_transf_8. 1 hit.
[Graphical view]
SUPFAMiSSF53448. SSF53448. 1 hit.
ProtoNetiSearch...

Entry informationi

Entry nameiGLYG_RABIT
AccessioniPrimary (citable) accession number: P13280
Entry historyi
Integrated into UniProtKB/Swiss-Prot: January 1, 1990
Last sequence update: January 23, 2007
Last modified: November 2, 2016
This is version 122 of the entry and version 3 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  2. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  3. 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.