P53178 (ALG13_YEAST) Reviewed, UniProtKB/Swiss-Prot

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) [Reference proteome]

Taxonomic identifier

559292 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Opisthokonta › Fungi › Dikarya › Ascomycota › saccharomyceta › Saccharomycotina › Saccharomycetes › Saccharomycetales › Saccharomycetaceae › Saccharomyces › Saccharomyces cerevisiae

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.
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 PubMed 16100113. Source: SGD lipid glycosylation Inferred from electronic annotation. Source: InterPro
Cellular_component	UDP-N-acetylglucosamine transferase complex Inferred from physical interaction Ref.7PubMed 16100113. Source: SGD cytosol Inferred from direct assay PubMed 16100113. Source: SGD extrinsic to endoplasmic reticulum membrane Inferred from direct assay Ref.7. Source: SGD nucleus Inferred from direct assay PubMed 14690591. Source: SGD
Molecular_function	N-acetylglucosaminyldiphosphodolichol N-acetylglucosaminyltransferase activity Inferred from electronic annotation. Source: EC carbohydrate binding Inferred from electronic annotation. Source: InterPro
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

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202

Helix Strand Turn

Details...

Beta strand

9 – 12

4

Beta strand

15 – 17

3

Helix

20 – 26

7

Helix

29 – 36

8

Turn

37 – 39

3

Beta strand

43 – 45

3

Beta strand

49 – 51

3

Helix

58 – 62

5

Beta strand

65 – 68

4

Turn

73 – 76

4

Beta strand

83 – 87

5

Turn

88 – 90

3

Beta strand

91 – 96

6

Beta strand

99 – 102

4

Helix

103 – 110

8

Beta strand

114 – 118

5

Helix

120 – 128

9

Beta strand

133 – 136

4

Helix

145 – 156

12

Beta strand

157 – 162

6

Turn

166 – 168

3

Helix

169 – 176

8

Beta strand

187 – 189

3

Helix

192 – 199

8

Sequences

	Sequence		Length	Mass (Da)
	P53178 [UniParc]. Last modified October 1, 1996. Version 1. Checksum: 9D5CDB366BBC1ED0	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

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] [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]	Saccharomyces Genome Database Submitted (DEC-2009) to the EMBL/GenBank/DDBJ databases Cited for: GENOME REANNOTATION. 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] [Europe PMC] [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] [Europe PMC] [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] [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.
+	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. 1 interaction.

MINT

MINT-543662.

STRING

4932.YGL047W.

Protein family/group databases

CAZy

GT1. Glycosyltransferase Family 1.

Proteomic databases

PaxDb

P53178.

Protocols and materials databases

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

EnsemblFungi

YGL047W; YGL047W; YGL047W.

GeneID

852835.

KEGG

sce:YGL047W.

Organism-specific databases

CYGD

YGL047w.

SGD

S000003015. ALG13.

Phylogenomic databases

eggNOG

COG5017.

GeneTree

ENSGT00510000047493.

HOGENOM

HOG000192807.

KO

K07432.

OMA

VHANTEE.

OrthoDB

EOG4KM2CB.

Enzyme and pathway databases

BRENDA

2.4.1.141. 984.

Gene expression databases

Genevestigator

P53178.

GermOnline

YGL047W. Saccharomyces cerevisiae.

Family and domain databases

InterPro

IPR007235. Glyco_trans_28_C.
[Graphical view]

Pfam

PF04101. Glyco_tran_28_C. 1 hit.
[Graphical view]

ProtoNet

Search...

Other

EvolutionaryTrace

P53178.

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:	May 1, 2013
This is version 100 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Fungal Protein Annotation Program