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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)LengthDescriptionGraphical viewFeature identifierActions
Active sitei86 – 8611 Publication
Metal bindingi102 – 1021Manganese1 Publication
Metal bindingi104 – 1041Manganese1 Publication
Sitei160 – 1601Important for catalytic activity1 Publication
Sitei163 – 1631Important for catalytic activity1 Publication
Metal bindingi212 – 2121Manganese1 Publication

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)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi86 – 861K → Q: Loss of activity. 1 Publication
Mutagenesisi160 – 1601D → N or S: Reduced trans-glucosylation activity by at least 260-fold and reduced UDP-glucose hydrolytic activity by 4 to 14-fold. 1 Publication
Mutagenesisi163 – 1631D → N: Loss of self-glucosylation activity and ability to trans-glucosylate maltose. Reduced UDP-glucose hydrolytic activity by at least 190-fold. 1 Publication
Mutagenesisi163 – 1631D → 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 Publication

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Initiator methionineiRemovedBy similarity1 Publication
Chaini2 – 333332Glycogenin-1CuratedPRO_0000215178Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei2 – 21N-acetylthreonineBy similarity
Modified residuei44 – 441Phosphoserine; by PKA; in vitro1 Publication
Glycosylationi195 – 1951O-linked (Glc...)1 Publication

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

1
333
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi3 – 1210Combined sources
Helixi13 – 2816Combined sources
Beta strandi33 – 397Combined sources
Helixi45 – 5410Combined sources
Beta strandi56 – 605Combined sources
Helixi71 – 766Combined sources
Helixi78 – 803Combined sources
Helixi81 – 866Combined sources
Helixi87 – 915Combined sources
Beta strandi96 – 1016Combined sources
Beta strandi105 – 1073Combined sources
Helixi112 – 1165Combined sources
Beta strandi119 – 1246Combined sources
Beta strandi126 – 1283Combined sources
Beta strandi131 – 1399Combined sources
Helixi143 – 15513Combined sources
Beta strandi159 – 1624Combined sources
Helixi163 – 1708Combined sources
Turni171 – 1766Combined sources
Helixi179 – 1813Combined sources
Helixi185 – 1873Combined sources
Beta strandi188 – 1903Combined sources
Helixi193 – 1964Combined sources
Helixi198 – 2047Combined sources
Helixi205 – 2073Combined sources
Beta strandi209 – 2124Combined sources
Beta strandi215 – 2173Combined sources
Helixi219 – 2213Combined sources
Beta strandi222 – 2254Combined sources
Turni226 – 2294Combined sources
Beta strandi230 – 2323Combined sources
Helixi243 – 25513Combined sources
Helixi257 – 2615Combined sources
Helixi263 – 2653Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
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. Positions 1-267.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP13280.

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni284 – 31633Interaction with GYS1By similarityAdd
BLAST

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)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti39 – 391T → L AA sequence (PubMed:3151442).Curated
Sequence conflicti89 – 891C → S AA sequence (PubMed:2806254).Curated
Sequence conflicti98 – 981C → L AA sequence (PubMed:2806254).Curated

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
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. Positions 1-267.
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: January 20, 2016
This is version 120 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.