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P36143

- GLG1_YEAST

UniProt

P36143 - GLG1_YEAST

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Protein

Glycogenin-1

Gene

GLG1

Organism
Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Status
Reviewed - Annotation score: 3 out of 5- Experimental evidence at protein leveli

Functioni

Self-glucosylating initiator of glycogen synthesis. Catalyzes the formation of a short alpha (1,4)-glucosyl chain covalently attached via a glucose 1-O-tyrosyl linkage to internal tyrosine residues. These chains act as primers for the elongation reaction catalyzed by glycogen synthase. Capable of transferring glucosyl residues to unbound acceptors such as free oligoglucans or oligoglucan derivatives.2 Publications

Catalytic activityi

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

GO - Molecular functioni

  1. glycogenin glucosyltransferase activity Source: SGD

GO - Biological processi

  1. glycogen biosynthetic process Source: SGD
Complete GO annotation...

Keywords - Molecular functioni

Transferase

Keywords - Biological processi

Glycogen biosynthesis

Enzyme and pathway databases

BioCyciYEAST:MONOMER3O-4054.
ReactomeiREACT_191292. Glycogen synthesis.
REACT_244738. Glycogen breakdown (glycogenolysis).

Protein family/group databases

CAZyiGT8. Glycosyltransferase Family 8.

Names & Taxonomyi

Protein namesi
Recommended name:
Glycogenin-1 (EC:2.4.1.186)
Alternative name(s):
Glycogen synthesis initiator protein 1
Glycogenin glucosyltransferase 1
Gene namesi
Name:GLG1
Ordered Locus Names:YKR058W
OrganismiSaccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Taxonomic identifieri559292 [NCBI]
Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaSaccharomycotinaSaccharomycetesSaccharomycetalesSaccharomycetaceaeSaccharomyces
ProteomesiUP000002311: Chromosome XI

Organism-specific databases

SGDiS000001766. GLG1.

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi230 – 2301Y → F: Eliminates glycogen accumulation; when associated with F-598. 1 Publication
Mutagenesisi598 – 5981Y → F: Eliminates glycogen accumulation; when associated with F-230. 1 Publication

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 616616Glycogenin-1PRO_0000215181Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Glycosylationi230 – 2301O-linked (Glc...)By similarity
Glycosylationi598 – 5981O-linked (Glc...)Curated

Keywords - PTMi

Glycoprotein

Proteomic databases

MaxQBiP36143.
PaxDbiP36143.
PeptideAtlasiP36143.

Expressioni

Inductioni

Induced during the diauxic transition.1 Publication

Gene expression databases

GenevestigatoriP36143.

Interactioni

Protein-protein interaction databases

BioGridi34189. 34 interactions.
IntActiP36143. 2 interactions.
MINTiMINT-2779894.
STRINGi4932.YKR058W.

Structurei

3D structure databases

ProteinModelPortaliP36143.
SMRiP36143. Positions 55-256.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Phylogenomic databases

eggNOGiNOG321063.
GeneTreeiENSGT00390000004721.
HOGENOMiHOG000112734.
InParanoidiP36143.
OMAiHFIGKHK.
OrthoDBiEOG7BS4K4.

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.

P36143-1 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
MYKKLAIATL LYSADYLPGV FALGHQVNKL LEEAGKKGDI ETCLIVTTSL
60 70 80 90 100
FNGTLSELAK NILQSIYTKI VLVEPLNCQE ESIQKNSENL ALLERPELSF
110 120 130 140 150
ALIKARLWEL TQFEQVLYLD SDTLPLNKEF LKLFDIMSKQ TTSQVGAIAD
160 170 180 190 200
IGWPDMFNSG VMMLIPDADT ASVLQNYIFE NTSIDGSDQG ILNQFFNQNC
210 220 230 240 250
CTDELVKDSF SREWVQLSFT YNVTIPNLGY QSSPAMNYFK PSIKLIHFIG
260 270 280 290 300
KHKPWSLWSQ KNFIKNEYHD QWNEVYEEFK EEHQLNNEVS KPKISDSDKT
310 320 330 340 350
ETPETITPVD APPSNEPTTN QEIDTISTVE ENVDNQNAEP VPNSDHSPAP
360 370 380 390 400
NPVPLDFTKW LTTFINKDHL TNQPVNESRE YSKENDNNII NSSSNRDQES
410 420 430 440 450
PPNSTQELNS SYSVVSTQAD SDEHQNAEEE DSTTDNASNS GEESHLDDIS
460 470 480 490 500
TAASSNNNVS NQPDGKNFSN SKENNISVES SPSNPEQKRS TDNIQKPSVS
510 520 530 540 550
TNDLPDDVEP HTSVDDNIQY LEKDKEGYEE FLPDVYESNA IDNEEEFFDD
560 570 580 590 600
DARDATEGET KTSAVADKQE DMKLTAEETN QPQQEMPNFK FDWEDSDYLS
610
KVERCFPDDI FEYAVE
Length:616
Mass (Da):69,724
Last modified:May 20, 2008 - v4
Checksum:i35DFF4A1E043FC8B
GO

Sequence cautioni

The sequence AAA91646.1 differs from that shown. Reason: Erroneous initiation. Curated
The sequence CAA82136.1 differs from that shown. Reason: Frameshift at positions 6 and 38. Curated
The sequence CAA82136.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally extended.Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U25546 Genomic DNA. Translation: AAA91646.1. Different initiation.
Z28283 Genomic DNA. Translation: CAA82136.1. Sequence problems.
BK006944 Genomic DNA. Translation: DAA09209.1.
PIRiS38134.
RefSeqiNP_012984.2. NM_001179848.1.

Genome annotation databases

EnsemblFungiiYKR058W; YKR058W; YKR058W.
GeneIDi853932.
KEGGisce:YKR058W.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U25546 Genomic DNA. Translation: AAA91646.1 . Different initiation.
Z28283 Genomic DNA. Translation: CAA82136.1 . Sequence problems.
BK006944 Genomic DNA. Translation: DAA09209.1 .
PIRi S38134.
RefSeqi NP_012984.2. NM_001179848.1.

3D structure databases

ProteinModelPortali P36143.
SMRi P36143. Positions 55-256.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 34189. 34 interactions.
IntActi P36143. 2 interactions.
MINTi MINT-2779894.
STRINGi 4932.YKR058W.

Protein family/group databases

CAZyi GT8. Glycosyltransferase Family 8.

Proteomic databases

MaxQBi P36143.
PaxDbi P36143.
PeptideAtlasi P36143.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

EnsemblFungii YKR058W ; YKR058W ; YKR058W .
GeneIDi 853932.
KEGGi sce:YKR058W.

Organism-specific databases

SGDi S000001766. GLG1.

Phylogenomic databases

eggNOGi NOG321063.
GeneTreei ENSGT00390000004721.
HOGENOMi HOG000112734.
InParanoidi P36143.
OMAi HFIGKHK.
OrthoDBi EOG7BS4K4.

Enzyme and pathway databases

BioCyci YEAST:MONOMER3O-4054.
Reactomei REACT_191292. Glycogen synthesis.
REACT_244738. Glycogen breakdown (glycogenolysis).

Miscellaneous databases

NextBioi 975303.

Gene expression databases

Genevestigatori P36143.

Family and domain databases

Gene3Di 3.90.550.10. 1 hit.
InterProi IPR002495. Glyco_trans_8.
IPR029044. Nucleotide-diphossugar_trans.
[Graphical view ]
Pfami PF01501. Glyco_transf_8. 1 hit.
[Graphical view ]
SUPFAMi SSF53448. SSF53448. 1 hit.
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  1. "Requirement of the self-glucosylating initiator proteins Glg1p and Glg2p for glycogen accumulation in Saccharomyces cerevisiae."
    Cheng C., Mu J., Farkas I., Huang D., Goebl M.G., Roach P.J.
    Mol. Cell. Biol. 15:6632-6640(1995) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION.
  2. "Complete DNA sequence of yeast chromosome XI."
    Dujon B., Alexandraki D., Andre B., Ansorge W., Baladron V., Ballesta J.P.G., Banrevi A., Bolle P.-A., Bolotin-Fukuhara M., Bossier P., Bou G., Boyer J., Buitrago M.J., Cheret G., Colleaux L., Daignan-Fornier B., del Rey F., Dion C.
    , Domdey H., Duesterhoeft A., Duesterhus S., Entian K.-D., Erfle H., Esteban P.F., Feldmann H., Fernandes L., Fobo G.M., Fritz C., Fukuhara H., Gabel C., Gaillon L., Garcia-Cantalejo J.M., Garcia-Ramirez J.J., Gent M.E., Ghazvini M., Goffeau A., Gonzalez A., Grothues D., Guerreiro P., Hegemann J.H., Hewitt N., Hilger F., Hollenberg C.P., Horaitis O., Indge K.J., Jacquier A., James C.M., Jauniaux J.-C., Jimenez A., Keuchel H., Kirchrath L., Kleine K., Koetter P., Legrain P., Liebl S., Louis E.J., Maia e Silva A., Marck C., Monnier A.-L., Moestl D., Mueller S., Obermaier B., Oliver S.G., Pallier C., Pascolo S., Pfeiffer F., Philippsen P., Planta R.J., Pohl F.M., Pohl T.M., Poehlmann R., Portetelle D., Purnelle B., Puzos V., Ramezani Rad M., Rasmussen S.W., Remacha M.A., Revuelta J.L., Richard G.-F., Rieger M., Rodrigues-Pousada C., Rose M., Rupp T., Santos M.A., Schwager C., Sensen C., Skala J., Soares H., Sor F., Stegemann J., Tettelin H., Thierry A., Tzermia M., Urrestarazu L.A., van Dyck L., van Vliet-Reedijk J.C., Valens M., Vandenbol M., Vilela C., Vissers S., von Wettstein D., Voss H., Wiemann S., Xu G., Zimmermann J., Haasemann M., Becker I., Mewes H.-W.
    Nature 369:371-378(1994) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: ATCC 204508 / S288c.
  3. Cited for: GENOME REANNOTATION.
    Strain: ATCC 204508 / S288c.
  4. "Initiation of glycogen synthesis in yeast. Requirement of multiple tyrosine residues for function of the self-glucosylating Glg proteins in vivo."
    Mu J., Cheng C., Roach P.J.
    J. Biol. Chem. 271:26554-26560(1996) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, MUTAGENESIS OF TYR-230 AND TYR-598.
  5. "Dynamic responses of reserve carbohydrate metabolism under carbon and nitrogen limitations in Saccharomyces cerevisiae."
    Parrou J.L., Enjalbert B., Plourde L., Bauche A., Gonzalez B., Francois J.
    Yeast 15:191-203(1999) [PubMed] [Europe PMC] [Abstract]
    Cited for: INDUCTION.
  6. "Reinvestigation of the Saccharomyces cerevisiae genome annotation by comparison to the genome of a related fungus: Ashbya gossypii."
    Brachat S., Dietrich F.S., Voegeli S., Zhang Z., Stuart L., Lerch A., Gates K., Gaffney T.D., Philippsen P.
    Genome Biol. 4:R45.1-R45.13(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION OF PROBABLE INITIATION SITE.
  7. "Finding functional features in Saccharomyces genomes by phylogenetic footprinting."
    Cliften P.F., Sudarsanam P., Desikan A., Fulton L., Fulton B., Majors J., Waterston R., Cohen B.A., Johnston M.
    Science 301:71-76(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION OF PROBABLE INITIATION SITE.
  8. "Global analysis of Cdk1 substrate phosphorylation sites provides insights into evolution."
    Holt L.J., Tuch B.B., Villen J., Johnson A.D., Gygi S.P., Morgan D.O.
    Science 325:1682-1686(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].

Entry informationi

Entry nameiGLG1_YEAST
AccessioniPrimary (citable) accession number: P36143
Secondary accession number(s): D6VXB9
Entry historyi
Integrated into UniProtKB/Swiss-Prot: June 1, 1994
Last sequence update: May 20, 2008
Last modified: November 26, 2014
This is version 96 of the entry and version 4 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programFungal Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. SIMILARITY comments
    Index of protein domains and families
  2. Yeast
    Yeast (Saccharomyces cerevisiae): entries, gene names and cross-references to SGD
  3. Yeast chromosome XI
    Yeast (Saccharomyces cerevisiae) chromosome XI: entries and gene names

External Data

Dasty 3