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Protein

Glycogenin-1

Gene

Gyg1

Organism
Mus musculus (Mouse)
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+By similarityNote: Divalent metal ions. Required for self-glucosylation. Manganese is the most effective.By similarity

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 – 861By similarity
Metal bindingi102 – 1021ManganeseBy similarity
Metal bindingi104 – 1041ManganeseBy similarity
Sitei160 – 1601Important for catalytic activityBy similarity
Sitei163 – 1631Important for catalytic activityBy similarity
Metal bindingi212 – 2121ManganeseBy similarity

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

ReactomeiR-MMU-3322077. Glycogen synthesis.
R-MMU-5357572. Lysosomal glycogen catabolism.
R-MMU-70221. Glycogen breakdown (glycogenolysis).
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
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
Proteomesi
  • UP000000589 Componenti: Chromosome 3

Organism-specific databases

MGIiMGI:1351614. Gyg.

Subcellular locationi

GO - Cellular componenti

Complete GO annotation...

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi305 – 3051K → A: No loss of interaction with GYS2. 1 Publication
Mutagenesisi308 – 3081W → A: No loss of interaction with GYS2. 1 Publication
Mutagenesisi315 – 3151Y → A: Severe loss of interaction with GYS2. 1 Publication
Mutagenesisi321 – 3211F → A: Severe loss of interaction with GYS2. 1 Publication
Mutagenesisi324 – 3241I → A: Severe loss of interaction with GYS2. 1 Publication
Mutagenesisi328 – 3281L → A: Severe loss of interaction with GYS2. 1 Publication
Mutagenesisi332 – 3321L → A: No loss of interaction with GYS2. 1 Publication

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Initiator methionineiRemovedBy similarity
Chaini2 – 333332Glycogenin-1CuratedPRO_0000215177Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei2 – 21N-acetylthreonineBy similarity
Modified residuei44 – 441PhosphoserineBy similarity
Glycosylationi195 – 1951O-linked (Glc...)By similarity

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.
Phosphorylated.By similarity

Keywords - PTMi

Acetylation, Glycoprotein, Phosphoprotein

Proteomic databases

EPDiQ9R062.
MaxQBiQ9R062.
PaxDbiQ9R062.
PeptideAtlasiQ9R062.
PRIDEiQ9R062.

2D gel databases

REPRODUCTION-2DPAGEQ9R062.

PTM databases

iPTMnetiQ9R062.
PhosphoSiteiQ9R062.

Expressioni

Tissue specificityi

Skeletal muscle, heart, to a lesser extent in kidney, lung and brain.

Gene expression databases

BgeeiQ9R062.
CleanExiMM_GYG.
ExpressionAtlasiQ9R062. baseline and differential.
GenevisibleiQ9R062. MM.

Interactioni

Subunit structurei

Homodimer tightly complexed to the 86 kDa catalytic subunit of glycogen synthase GYS1 (By similarity). Interacts (via C-terminus) with GYS2; required for GYS2-mediated glycogen synthesis (PubMed:24982189).By similarity1 Publication

Protein-protein interaction databases

IntActiQ9R062. 2 interactions.
MINTiMINT-4096202.
STRINGi10090.ENSMUSP00000136035.

Structurei

3D structure databases

ProteinModelPortaliQ9R062.
SMRiQ9R062. Positions 1-262.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Region

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

Sequence similaritiesi

Phylogenomic databases

eggNOGiKOG1950. Eukaryota.
COG5597. LUCA.
GeneTreeiENSGT00390000004721.
HOGENOMiHOG000008282.
HOVERGENiHBG000681.
InParanoidiQ9R062.
KOiK00750.
PhylomeDBiQ9R062.

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.

Q9R062-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MTDQAFVTLT TNDAYAKGAL VLGSSLKQHR TTRRMVVLTS PQVSDSMRKV
60 70 80 90 100
LETVFDDVIM VDVLDSGDSA HLTLMKRPEL GITLTKLHCW SLTQYSKCVF
110 120 130 140 150
MDADTLVLSN IDDLFEREEL SAAPDPGWPD CFNSGVFVYQ PSIETYNQLL
160 170 180 190 200
HLASEQGSFD GGDQGLLNTY FSGWATTDIT KHLPFVYNLS SISIYSYLPA
210 220 230 240 250
FKAFGKNAKV VHFLGRTKPW NYTYNPQTKS VNCDSQDPTV SHPEFLNLWW
260 270 280 290 300
DTFTTNVLPL LQHHGLVKDA SSYLMMEHVS GALSDLSFGE APAAPQPSMS
310 320 330
SEERKERWEQ GQADYMGADS FDNIKRKLDT YLQ
Length:333
Mass (Da):37,402
Last modified:January 23, 2007 - v3
Checksum:i2CE3F0C23166F2CB
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF114031 mRNA. Translation: AAD48901.1.
AK159576 mRNA. Translation: BAE35197.1.
CH466530 Genomic DNA. Translation: EDL34894.1.
BC029903 mRNA. Translation: AAH29903.1.
CCDSiCCDS50873.1.
RefSeqiNP_038783.1. NM_013755.3.
UniGeneiMm.6375.

Genome annotation databases

EnsembliENSMUST00000178328; ENSMUSP00000136035; ENSMUSG00000019528.
GeneIDi27357.
KEGGimmu:27357.
UCSCiuc056zrp.1. mouse.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF114031 mRNA. Translation: AAD48901.1.
AK159576 mRNA. Translation: BAE35197.1.
CH466530 Genomic DNA. Translation: EDL34894.1.
BC029903 mRNA. Translation: AAH29903.1.
CCDSiCCDS50873.1.
RefSeqiNP_038783.1. NM_013755.3.
UniGeneiMm.6375.

3D structure databases

ProteinModelPortaliQ9R062.
SMRiQ9R062. Positions 1-262.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

IntActiQ9R062. 2 interactions.
MINTiMINT-4096202.
STRINGi10090.ENSMUSP00000136035.

Protein family/group databases

CAZyiGT8. Glycosyltransferase Family 8.

PTM databases

iPTMnetiQ9R062.
PhosphoSiteiQ9R062.

2D gel databases

REPRODUCTION-2DPAGEQ9R062.

Proteomic databases

EPDiQ9R062.
MaxQBiQ9R062.
PaxDbiQ9R062.
PeptideAtlasiQ9R062.
PRIDEiQ9R062.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSMUST00000178328; ENSMUSP00000136035; ENSMUSG00000019528.
GeneIDi27357.
KEGGimmu:27357.
UCSCiuc056zrp.1. mouse.

Organism-specific databases

CTDi27357.
MGIiMGI:1351614. Gyg.

Phylogenomic databases

eggNOGiKOG1950. Eukaryota.
COG5597. LUCA.
GeneTreeiENSGT00390000004721.
HOGENOMiHOG000008282.
HOVERGENiHBG000681.
InParanoidiQ9R062.
KOiK00750.
PhylomeDBiQ9R062.

Enzyme and pathway databases

UniPathwayiUPA00164.
ReactomeiR-MMU-3322077. Glycogen synthesis.
R-MMU-5357572. Lysosomal glycogen catabolism.
R-MMU-70221. Glycogen breakdown (glycogenolysis).

Miscellaneous databases

PROiQ9R062.
SOURCEiSearch...

Gene expression databases

BgeeiQ9R062.
CleanExiMM_GYG.
ExpressionAtlasiQ9R062. baseline and differential.
GenevisibleiQ9R062. MM.

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...

Publicationsi

« Hide 'large scale' publications
  1. "Characterization of mouse glycogenin-1 cDNA and promoter region."
    van Maanen M.-H., Fournier P.A., Palmer T.N., Abraham L.J.
    Biochim. Biophys. Acta 1447:284-290(1999) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
    Tissue: Skeletal muscle.
  2. "The transcriptional landscape of the mammalian genome."
    Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.
    , Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.
    Science 309:1559-1563(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Strain: C57BL/6JImported.
  3. Mural R.J., Adams M.D., Myers E.W., Smith H.O., Venter J.C.
    Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  4. "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
    The MGC Project Team
    Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Strain: FVB/N.
    Tissue: Mammary gland.
  5. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Brown adipose tissue, Heart, Kidney, Liver, Lung and Spleen.
  6. Cited for: INTERACTION WITH GYS2, MUTAGENESIS OF LYS-305; TRP-308; TYR-315; PHE-321; ILE-324; LEU-328 AND LEU-332.

Entry informationi

Entry nameiGLYG_MOUSE
AccessioniPrimary (citable) accession number: Q9R062
Secondary accession number(s): Q3TWR9
Entry historyi
Integrated into UniProtKB/Swiss-Prot: April 27, 2001
Last sequence update: January 23, 2007
Last modified: July 6, 2016
This is version 121 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

Complete proteome, Reference proteome

Documents

  1. MGD cross-references
    Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
  2. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  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.