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Reviewed, UniProtKB/Swiss-Prot P53178 (ALG13_YEAST)

Last modified November 24, 2009. Version 67. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (4) | Third-party data | Customize display text xml rdf/xml gff fasta
Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Binary interactions · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents

Names and origin

Protein namesRecommended name:
    UDP-N-acetylglucosamine transferase subunit ALG13
    EC=2.4.1.141
Alternative name(s):
    Asparagine-linked glycosylation protein 13
Gene names
Name: ALG13
Ordered Locus Names: YGL047W
OrganismSaccharomyces cerevisiae (Baker's yeast) [Complete proteome]
Taxonomic identifier4932 [NCBI]
Taxonomic lineageEukaryotaFungiDikaryaAscomycotaSaccharomycotinaSaccharomycetesSaccharomycetalesSaccharomycetaceaeSaccharomyces

Protein attributes

Sequence length202 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is not processed.
Protein existenceEvidence at protein level.

General annotation (Comments)

Function

Involved in protein N-glycosylation. Essential for the second step of the dolichol-linked oligosaccharide pathway. Ref.5 Ref.6

Catalytic activity

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

Subunit structure

Heterodimer with ALG14 to form a functional enzyme.

Subcellular location

Endoplasmic reticulum.

Miscellaneous

Present with 1950 molecules/cell in log phase SD medium. Ref.4

Sequence similarities

Belongs to the glycosyltransferase 28 family.

Binary interactions

With

Entry

#Exp.

IntAct

Notes

ALG14P382421EBI-23770,EBI-21477

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 202202UDP-N-acetylglucosamine transferase subunit ALG13
PRO_0000215605

Secondary structure

.................................. 202
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
P53178-1 [UniParc].

Last modified October 1, 1996. Version 1.
Checksum: 9D5CDB366BBC1ED0

FASTA20222,661
        10         20         30         40         50         60 
MGIIEEKALF VTCGATVPFP KLVSCVLSDE FCQELIQYGF VRLIIQFGRN YSSEFEHLVQ 

        70         80         90        100        110        120 
ERGGQRESQK IPIDQFGCGD TARQYVLMNG KLKVIGFDFS TKMQSIIRDY SDLVISHAGT 

       130        140        150        160        170        180 
GSILDSLRLN KPLIVCVNDS LMDNHQQQIA DKFVELGYVW SCAPTETGLI AGLRASQTEK 

       190        200 
LKPFPVSHNP SFERLLVETI YS 

« Hide

References

« Hide 'large scale' references
[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: 9234674] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE 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. expand/collapse author list , 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: 9169869] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: ATCC 204508 / S288c.
[3]"Global analysis of protein localization in budding yeast."
Huh W.-K., Falvo J.V., Gerke L.C., Carroll A.S., Howson R.W., Weissman J.S., O'Shea E.K.
Nature 425:686-691(2003) [PubMed: 14562095] [Abstract]
Cited for: SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
[4]"Global analysis of protein expression in yeast."
Ghaemmaghami S., Huh W.-K., Bower K., Howson R.W., Belle A., Dephoure N., O'Shea E.K., Weissman J.S.
Nature 425:737-741(2003) [PubMed: 14562106] [Abstract]
Cited for: LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS].
[5]"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: 15615718] [Abstract]
Cited for: FUNCTION.
[6]"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: 16100110] [Abstract]
Cited for: FUNCTION, INTERACTION WITH ALG14, SUBCELLULAR LOCATION.
+Additional computationally mapped references.

Cross-references

Sequence databases

Z72569 Genomic DNA. Translation: CAA96749.1.
PIRS64051.
RefSeqNP_011468.1.

3D structure databases

EntryMethodResolution (Å)ChainPositionsPDBsum
2JZCNMR-A2-202[»]
ModBaseSearch...

Protein-protein interaction databases

DIPDIP:4726N.
IntActP53178. 3 interactions.
STRINGP53178.

Protein family/group databases

CAZyGT1. Glycosyltransferase Family 1.

Genome annotation databases

EnsemblYGL047W; YGL047W; YGL047W; Saccharomyces cerevisiae. [Genome view]
GeneID852835.
KEGGsce:YGL047W.
NMPDRfig|4932.3.peg.2574.

Organism-specific databases

CYGDYGL047w.
SGDS000003015. ALG13.

Phylogenomic databases

HOGENOMP53178.
OMAPLIVCVN
OrthoDBEOG9ZCVN9

Enzyme and pathway databases

BRENDA2.4.1.141. 250.

Gene expression databases

ArrayExpressP53178.
GenevestigatorP53178.
GermOnlineYGL047W. Saccharomyces cerevisiae.

Family and domain databases

InterProIPR007235. Glyco_trans_28_C.
[Graphical view]
PfamPF04101. Glyco_tran_28_C. 1 hit.
[Graphical view]
ProtoNetSearch...

Other Resources

NextBio972406.

Entry information

Entry nameALG13_YEAST
AccessionPrimary (citable) accession number: P53178
Entry history
Integrated into UniProtKB/Swiss-Prot: October 1, 1996
Last sequence update: October 1, 1996
Last modified: November 24, 2009
This is version 67 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation projectFPAP (Fungal Proteome Annotation Project)

Relevant documents

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

SIMILARITY comments

Index of protein domains and families

Yeast

Yeast (Saccharomyces cerevisiae): entries, gene names and cross-references to SGD

Yeast chromosome VII

Yeast (Saccharomyces cerevisiae) chromosome VII: entries and gene names

Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Binary interactions · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents