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RABIT:GLYG

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Species (Taxon ID) Oryctolagus cuniculus (Rabbit). (9986)
Gene Name(s) GYG1 (synonyms: GYG)
Protein Name(s) Glycogenin-1

GN-1 GN1

External Links
UniProt P13280
EMBL L01791
PIR A45094
RefSeq NP_001075710.1
UniGene Ocu.1930
PDB 1LL0
1LL2
1LL3
1ZCT
1ZCU
1ZCV
1ZCY
1ZDF
1ZDG
3USQ
3USR
3V8Y
3V8Z
3V90
3V91
PDBsum 1LL0
1LL2
1LL3
1ZCT
1ZCU
1ZCV
1ZCY
1ZDF
1ZDG
3USQ
3USR
3V8Y
3V8Z
3V90
3V91
ProteinModelPortal P13280
SMR P13280
STRING 9986.ENSOCUP00000003049
CAZy GT8
PRIDE P13280
GeneID 100009058
CTD 2992
eggNOG COG5597
HOGENOM HOG000008282
HOVERGEN HBG000681
InParanoid P13280
BRENDA 2.4.1.186
UniPathway UPA00164
EvolutionaryTrace P13280
Proteomes UP000001811
GO GO:0008466
GO:0046872
GO:0005978
Gene3D 3.90.550.10
InterPro IPR002495
IPR029044
Pfam PF01501
SUPFAM SSF53448

Annotations

Qualifier GO ID GO term name Reference ECO ID ECO term name with/from Aspect Extension Notes Status

enables

GO:0030145

manganese ion binding

PMID:2526735[1]

ECO:0000314

direct assay evidence used in manual assertion

F

Seeded From UniProt

complete

enables

GO:0008466

glycogenin glucosyltransferase activity

PMID:2526735[1]

ECO:0000314

direct assay evidence used in manual assertion

F

Seeded From UniProt

complete

enables

GO:0102751

UDP-alpha-D-glucose:glucosyl-glycogenin alpha-D-glucosyltransferase activity

PMID:2526735[1]

ECO:0000314

direct assay evidence used in manual assertion

F

Seeded From UniProt

complete

enables

GO:0008466

glycogenin glucosyltransferase activity

PMID:1281472[2]

ECO:0000314

direct assay evidence used in manual assertion

F

Seeded From UniProt

complete

involved_in

GO:0005978

glycogen biosynthetic process

PMID:1281472[2]

ECO:0000314

direct assay evidence used in manual assertion

P

Seeded From UniProt

complete

enables

GO:0102751

UDP-alpha-D-glucose:glucosyl-glycogenin alpha-D-glucosyltransferase activity

GO_REF:0000024

ECO:0000250

sequence similarity evidence used in manual assertion

UniProtKB:P46976

F

Seeded From UniProt

complete

enables

GO:0042803

protein homodimerization activity

GO_REF:0000024

ECO:0000250

sequence similarity evidence used in manual assertion

UniProtKB:P46976

F

Seeded From UniProt

complete

enables

GO:0030145

manganese ion binding

GO_REF:0000024

ECO:0000250

sequence similarity evidence used in manual assertion

UniProtKB:P46976

F

Seeded From UniProt

complete

enables

GO:0008466

glycogenin glucosyltransferase activity

GO_REF:0000024

ECO:0000250

sequence similarity evidence used in manual assertion

UniProtKB:P46976

F

Seeded From UniProt

complete

involved_in

GO:0005978

glycogen biosynthetic process

GO_REF:0000024

ECO:0000250

sequence similarity evidence used in manual assertion

UniProtKB:P46976

P

Seeded From UniProt

complete

enables

GO:0016757

transferase activity, transferring glycosyl groups

GO_REF:0000002

ECO:0000256

match to sequence model evidence used in automatic assertion

InterPro:IPR002495

F

Seeded From UniProt

complete

enables

GO:0008466

glycogenin glucosyltransferase activity

GO_REF:0000003

ECO:0000501

evidence used in automatic assertion

EC:2.4.1.186

F

Seeded From UniProt

complete

enables

GO:0102751

UDP-alpha-D-glucose:glucosyl-glycogenin alpha-D-glucosyltransferase activity

GO_REF:0000003

ECO:0000501

evidence used in automatic assertion

EC:2.4.1.186

F

Seeded From UniProt

complete

involved_in

GO:0005978

glycogen biosynthetic process

GO_REF:0000037
GO_REF:0000041

ECO:0000322

imported manually asserted information used in automatic assertion

UniProtKB-KW:KW-0320
UniPathway:UPA00164

P

Seeded From UniProt

complete

enables

GO:0046872

metal ion binding

GO_REF:0000037

ECO:0000322

imported manually asserted information used in automatic assertion

UniProtKB-KW:KW-0479

F

Seeded From UniProt

complete

enables

GO:0016740

transferase activity

GO_REF:0000037

ECO:0000322

imported manually asserted information used in automatic assertion

UniProtKB-KW:KW-0808

F

Seeded From UniProt

complete

Notes

References

See Help:References for how to manage references in GONUTS.

  1. 1.0 1.1 1.2 Smythe, C et al. (1989) Structural and functional studies on rabbit liver glycogenin. Eur. J. Biochem. 183 205-9 PubMed GONUTS page
  2. 2.0 2.1 Viskupic, E et al. (1992) Rabbit skeletal muscle glycogenin. Molecular cloning and production of fully functional protein in Escherichia coli. J. Biol. Chem. 267 25759-63 PubMed GONUTS page