UDP-N-acetylglucosamine transferase subunit ALG13 - Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)

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P53178 (ALG13_YEAST) Reviewed, UniProtKB/Swiss-Prot

Last modified January 25, 2012. Version 87. History...

Clusters with 100%, 90%, 50% identity |

Documents (4) |

Third-party data

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Names·Attributes·General annotation·Ontologies·Interactions·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents Customize order

Names and origin

Protein names

Recommended 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

Organism

Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)

Taxonomic identifier

559292 [NCBI]

Taxonomic lineage

Eukaryota › Fungi › Dikarya › Ascomycota › Saccharomycotina › Saccharomycetes › Saccharomycetales › Saccharomycetaceae › Saccharomyces

Protein attributes

Sequence length	202 AA.
Sequence status	Complete.
Protein existence	Evidence at protein level

General annotation (Comments)

Function	Involved in protein N-glycosylation. Essential for the second step of the dolichol-linked oligosaccharide pathway. Ref.6 Ref.7
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 Ref.4 Ref.7.
Miscellaneous	Present with 1950 molecules/cell in log phase SD medium. Ref.5
Sequence similarities	Belongs to the glycosyltransferase 28 family.

Ontologies

Keywords
Cellular component	Endoplasmic reticulum
Molecular function	Glycosyltransferase Transferase
Technical term	3D-structure Complete proteome Reference proteome
Gene Ontology (GO)
Biological process	dolichol-linked oligosaccharide biosynthetic process Inferred from direct assay. Source: SGD lipid glycosylation Inferred from electronic annotation. Source: InterPro
Cellular component	UDP-N-acetylglucosamine transferase complex Inferred from physical interaction Ref.7. Source: SGD cytosol Inferred from direct assay. Source: SGD extrinsic to endoplasmic reticulum membrane Inferred from direct assay Ref.7. Source: SGD membrane fraction Inferred from direct assay. Source: SGD nucleus Inferred from direct assay. Source: SGD
Molecular function	N-acetylglucosaminyldiphosphodolichol N-acetylglucosaminyltransferase activity Inferred from electronic annotation. Source: EC carbohydrate binding Inferred from electronic annotation. Source: InterPro protein binding Inferred from physical interaction Ref.7. Source: IntAct
Complete GO annotation...

Binary interactions

With	Entry	#Exp.	IntAct	Notes
ALG14	P38242	3	EBI-23770,EBI-21477

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 202

202

UDP-N-acetylglucosamine transferase subunit ALG13

PRO_0000215605

Secondary structure

202

Helix Strand Turn

Details...

Sequences

Sequence

Length

Mass (Da)

Tools

P53178 [UniParc].

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

202

22,661

        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' referencesShow '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]	Saccharomyces Genome Database Submitted (DEC-2009) to the EMBL/GenBank/DDBJ databases Cited for: GENOME REANNOTATION. Strain: ATCC 204508 / S288c.
[3]	"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. Kleine K. Nature 387:81-84(1997) [PubMed: 9169869] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: ATCC 204508 / S288c.
[4]	"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].
[5]	"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].
[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: 15615718] [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: 16100110] [Abstract] Cited for: FUNCTION, INTERACTION WITH ALG14, SUBCELLULAR LOCATION.
+	Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ

Z72569 Genomic DNA. Translation: CAA96749.1.
BK006941 Genomic DNA. Translation: DAA08054.1.

PIR

S64051.

RefSeq

NP_011468.1. NM_001180912.1.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
2JZC	NMR	-	A	2-202	[»]
2KS6	NMR	-	A	2-202	[»]

ProteinModelPortal

P53178.

SMR

P53178. Positions 2-202.

ModBase

Search...

Protein-protein interaction databases

DIP

DIP-4726N.

IntAct

P53178. 3 interactions.

MINT

MINT-543662.

STRING

P53178.

Protein family/group databases

CAZy

GT1. Glycosyltransferase Family 1.

Protocols and materials databases

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

EnsemblFungi

YGL047W; YGL047W; YGL047W.

GeneID

852835.

KEGG

sce:YGL047W.

NMPDR

fig|4932.3.peg.2574.

Organism-specific databases

CYGD

YGL047w.

SGD

S000003015. ALG13.

Phylogenomic databases

eggNOG

fuNOG11732.

GeneTree

EFGT00050000003312.

HOGENOM

HBG629711.

OMA

HANTEEL.

OrthoDB

EOG4KM2CB.

Enzyme and pathway databases

BRENDA

2.4.1.141. 984.

Gene expression databases

ArrayExpress

P53178.

Genevestigator

P53178.

GermOnline

YGL047W. Saccharomyces cerevisiae.

Family and domain databases

InterPro

IPR007235. Glyco_trans_28_C.
[Graphical view]

K07432.

Pfam

PF04101. Glyco_tran_28_C. 1 hit.
[Graphical view]

ProtoNet

Search...

Other

NextBio

972406.

Entry information

Entry name

ALG13_YEAST

Accession

Primary (citable) accession number: P53178
Secondary accession number(s): D6VU93

Entry history

Integrated into UniProtKB/Swiss-Prot:	October 1, 1996
Last sequence update:	October 1, 1996
Last modified:	January 25, 2012
This is version 87 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Fungal Protein Annotation Program

Relevant documents

Yeast

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

Yeast chromosome VII

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

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

SIMILARITY comments

Index of protein domains and families

Names·Attributes·General annotation·Ontologies·Interactions·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents

Preferred order of sections

Names and origin

Protein attributes

General annotation (Comments)

Ontologies

Binary interactions

With

Entry

#Exp.

IntAct

Notes

Sequence annotation (Features)

Molecule processing

Secondary structure

Sequences

References

Cross-references

Sequence databases

3D structure databases

Protein-protein interaction databases

Protein family/group databases

Protocols and materials databases

Genome annotation databases

Organism-specific databases

Phylogenomic databases

Enzyme and pathway databases

Gene expression databases

Family and domain databases

Other

Entry information

Relevant documents