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Protein

UDP-N-acetylglucosamine transferase subunit ALG13

Gene

ALG13

Organism
Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Status
Reviewed-Annotation score: Annotation score: 4 out of 5-Experimental evidence at protein leveli

Functioni

Involved in protein N-glycosylation. Essential for the second step of the dolichol-linked oligosaccharide pathway.2 Publications

Catalytic activityi

UDP-N-acetyl-D-glucosamine + N-acetyl-D-glucosaminyl-diphosphodolichol = UDP + N,N'-diacetylchitobiosyl-diphosphodolichol.

GO - Molecular functioni

GO - Biological processi

  • dolichol-linked oligosaccharide biosynthetic process Source: SGD
Complete GO annotation...

Keywords - Molecular functioni

Glycosyltransferase, Transferase

Enzyme and pathway databases

BioCyciYEAST:G3O-30557-MONOMER.
YEAST:MONOMER3O-20.
BRENDAi2.4.1.141. 984.

Protein family/group databases

CAZyiGT1. Glycosyltransferase Family 1.

Names & Taxonomyi

Protein namesi
Recommended name:
UDP-N-acetylglucosamine transferase subunit ALG13 (EC:2.4.1.141)
Alternative name(s):
Asparagine-linked glycosylation protein 13
Gene namesi
Name:ALG13
Ordered Locus Names:YGL047W
OrganismiSaccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Taxonomic identifieri559292 [NCBI]
Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaSaccharomycotinaSaccharomycetesSaccharomycetalesSaccharomycetaceaeSaccharomyces
Proteomesi
  • UP000002311 Componenti: Chromosome VII

Organism-specific databases

EuPathDBiFungiDB:YGL047W.
SGDiS000003015. ALG13.

Subcellular locationi

GO - Cellular componenti

  • cytoplasm Source: SGD
  • cytosol Source: SGD
  • extrinsic component of endoplasmic reticulum membrane Source: SGD
  • UDP-N-acetylglucosamine transferase complex Source: SGD
Complete GO annotation...

Keywords - Cellular componenti

Endoplasmic reticulum

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 202202UDP-N-acetylglucosamine transferase subunit ALG13PRO_0000215605Add
BLAST

Proteomic databases

MaxQBiP53178.

Interactioni

Subunit structurei

Heterodimer with ALG14 to form a functional enzyme.

Binary interactionsi

WithEntry#Exp.IntActNotes
ALG14P382423EBI-23770,EBI-21477

Protein-protein interaction databases

BioGridi33201. 22 interactions.
DIPiDIP-4726N.
IntActiP53178. 1 interaction.
MINTiMINT-543662.

Structurei

Secondary structure

1
202
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi9 – 124Combined sources
Beta strandi15 – 173Combined sources
Helixi20 – 267Combined sources
Helixi29 – 368Combined sources
Turni37 – 393Combined sources
Beta strandi43 – 453Combined sources
Beta strandi49 – 513Combined sources
Helixi58 – 625Combined sources
Beta strandi65 – 684Combined sources
Turni73 – 764Combined sources
Beta strandi83 – 875Combined sources
Turni88 – 903Combined sources
Beta strandi91 – 966Combined sources
Beta strandi99 – 1024Combined sources
Helixi103 – 1108Combined sources
Beta strandi114 – 1185Combined sources
Helixi120 – 1289Combined sources
Beta strandi133 – 1364Combined sources
Helixi145 – 15612Combined sources
Beta strandi157 – 1626Combined sources
Turni166 – 1683Combined sources
Helixi169 – 1768Combined sources
Beta strandi187 – 1893Combined sources
Helixi192 – 1998Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
2JZCNMR-A2-202[»]
2KS6NMR-A2-202[»]
ProteinModelPortaliP53178.
SMRiP53178. Positions 2-202.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP53178.

Family & Domainsi

Sequence similaritiesi

Belongs to the glycosyltransferase 28 family.Curated

Phylogenomic databases

GeneTreeiENSGT00510000047493.
HOGENOMiHOG000192807.
InParanoidiP53178.
KOiK07432.
OMAiCGPDISW.
OrthoDBiEOG7NKKXH.

Family and domain databases

InterProiIPR007235. Glyco_trans_28_C.
[Graphical view]
PfamiPF04101. Glyco_tran_28_C. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

P53178-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MGIIEEKALF VTCGATVPFP KLVSCVLSDE FCQELIQYGF VRLIIQFGRN
60 70 80 90 100
YSSEFEHLVQ ERGGQRESQK IPIDQFGCGD TARQYVLMNG KLKVIGFDFS
110 120 130 140 150
TKMQSIIRDY SDLVISHAGT GSILDSLRLN KPLIVCVNDS LMDNHQQQIA
160 170 180 190 200
DKFVELGYVW SCAPTETGLI AGLRASQTEK LKPFPVSHNP SFERLLVETI

YS
Length:202
Mass (Da):22,661
Last modified:October 1, 1996 - v1
Checksum:i9D5CDB366BBC1ED0
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
Z72569 Genomic DNA. Translation: CAA96749.1.
BK006941 Genomic DNA. Translation: DAA08054.1.
PIRiS64051.
RefSeqiNP_011468.1. NM_001180912.1.

Genome annotation databases

EnsemblFungiiYGL047W; YGL047W; YGL047W.
GeneIDi852835.
KEGGisce:YGL047W.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
Z72569 Genomic DNA. Translation: CAA96749.1.
BK006941 Genomic DNA. Translation: DAA08054.1.
PIRiS64051.
RefSeqiNP_011468.1. NM_001180912.1.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
2JZCNMR-A2-202[»]
2KS6NMR-A2-202[»]
ProteinModelPortaliP53178.
SMRiP53178. Positions 2-202.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi33201. 22 interactions.
DIPiDIP-4726N.
IntActiP53178. 1 interaction.
MINTiMINT-543662.

Protein family/group databases

CAZyiGT1. Glycosyltransferase Family 1.

Proteomic databases

MaxQBiP53178.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblFungiiYGL047W; YGL047W; YGL047W.
GeneIDi852835.
KEGGisce:YGL047W.

Organism-specific databases

EuPathDBiFungiDB:YGL047W.
SGDiS000003015. ALG13.

Phylogenomic databases

GeneTreeiENSGT00510000047493.
HOGENOMiHOG000192807.
InParanoidiP53178.
KOiK07432.
OMAiCGPDISW.
OrthoDBiEOG7NKKXH.

Enzyme and pathway databases

BioCyciYEAST:G3O-30557-MONOMER.
YEAST:MONOMER3O-20.
BRENDAi2.4.1.141. 984.

Miscellaneous databases

EvolutionaryTraceiP53178.
PROiP53178.

Family and domain databases

InterProiIPR007235. Glyco_trans_28_C.
[Graphical view]
PfamiPF04101. Glyco_tran_28_C. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "The characterization of two new clusters of duplicated genes suggests a 'Lego' organization of the yeast Saccharomyces cerevisiae chromosomes."
    Feuermann M., de Montigny J., Potier S., Souciet J.-L.
    Yeast 13:861-869(1997) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    Strain: ATCC 204508 / S288c.
  2. "The nucleotide sequence of Saccharomyces cerevisiae chromosome VII."
    Tettelin H., Agostoni-Carbone M.L., Albermann K., Albers M., Arroyo J., Backes U., Barreiros T., Bertani I., Bjourson A.J., Brueckner M., Bruschi C.V., Carignani G., Castagnoli L., Cerdan E., Clemente M.L., Coblenz A., Coglievina M., Coissac E.
    , Defoor E., Del Bino S., Delius H., Delneri D., de Wergifosse P., Dujon B., Durand P., Entian K.-D., Eraso P., Escribano V., Fabiani L., Fartmann B., Feroli F., Feuermann M., Frontali L., Garcia-Gonzalez M., Garcia-Saez M.I., Goffeau A., Guerreiro P., Hani J., Hansen M., Hebling U., Hernandez K., Heumann K., Hilger F., Hofmann B., Indge K.J., James C.M., Klima R., Koetter P., Kramer B., Kramer W., Lauquin G., Leuther H., Louis E.J., Maillier E., Marconi A., Martegani E., Mazon M.J., Mazzoni C., McReynolds A.D.K., Melchioretto P., Mewes H.-W., Minenkova O., Mueller-Auer S., Nawrocki A., Netter P., Neu R., Nombela C., Oliver S.G., Panzeri L., Paoluzi S., Plevani P., Portetelle D., Portillo F., Potier S., Purnelle B., Rieger M., Riles L., Rinaldi T., Robben J., Rodrigues-Pousada C., Rodriguez-Belmonte E., Rodriguez-Torres A.M., Rose M., Ruzzi M., Saliola M., Sanchez-Perez M., Schaefer B., Schaefer M., Scharfe M., Schmidheini T., Schreer A., Skala J., Souciet J.-L., Steensma H.Y., Talla E., Thierry A., Vandenbol M., van der Aart Q.J.M., Van Dyck L., Vanoni M., Verhasselt P., Voet M., Volckaert G., Wambutt R., Watson M.D., Weber N., Wedler E., Wedler H., Wipfli P., Wolf K., Wright L.F., Zaccaria P., Zimmermann M., Zollner A., Kleine K.
    Nature 387:81-84(1997) [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. Cited for: SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
  5. Cited for: LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS].
  6. "Two proteins homologous to the N- and C-terminal domains of the bacterial glycosyltransferase Murg are required for the second step of dolichyl-linked oligosaccharide synthesis in Saccharomyces cerevisiae."
    Chantret I., Dancourt J., Barbat A., Moore S.E.H.
    J. Biol. Chem. 280:9236-9242(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION.
  7. "Alg14 recruits Alg13 to the cytoplasmic face of the endoplasmic reticulum to form a novel bipartite UDP-N-acetylglucosamine transferase required for the second step of N-linked glycosylation."
    Gao X.-D., Tachikawa H., Sato T., Jigami Y., Dean N.
    J. Biol. Chem. 280:36254-36262(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, INTERACTION WITH ALG14, SUBCELLULAR LOCATION.

Entry informationi

Entry nameiALG13_YEAST
AccessioniPrimary (citable) accession number: P53178
Secondary accession number(s): D6VU93
Entry historyi
Integrated into UniProtKB/Swiss-Prot: October 1, 1996
Last sequence update: October 1, 1996
Last modified: June 8, 2016
This is version 120 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programFungal Protein Annotation Program

Miscellaneousi

Miscellaneous

Present with 1950 molecules/cell in log phase SD medium.1 Publication

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

Documents

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

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.