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Reviewed, UniProtKB/Swiss-Prot P46982 (MNN5_YEAST)

Last modified June 16, 2009. Version 52. 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 · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents

Names and origin

Protein namesRecommended name:
    Alpha-1,2-mannosyltransferase MNN5
    EC=2.4.1.-
Gene names
Name: MNN5
Ordered Locus Names: YJL186W
ORF Names: J0409
OrganismSaccharomyces cerevisiae (Baker's yeast) [Complete proteome]
Taxonomic identifier4932 [NCBI]
Taxonomic lineageEukaryotaFungiDikaryaAscomycotaSaccharomycotinaSaccharomycetesSaccharomycetalesSaccharomycetaceaeSaccharomyces

Protein attributes

Sequence length586 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level.

General annotation (Comments)

Function

Responsible for addition of first and second mannose residues to the outer chain of core N-linked polysaccharides and to O-linked mannotriose. Implicated in late Golgi modifications. Ref.2 Ref.3 Ref.4

Pathway

Protein modification; protein glycosylation.

Subcellular location

Golgi apparatuscis-Golgi network. Ref.4 Ref.5

Post-translational modification

Glycosylated. Ref.4

Miscellaneous

Present with 11400 molecules/cell in log phase SD medium. Ref.6

Sequence similarities

Belongs to the MNN1/MNT family.

Ontologies

Keywords
   Cellular componentGolgi apparatus
   DomainSignal
   Molecular functionGlycosyltransferase
Transferase
   PTMGlycoprotein
   Technical termComplete proteome
Gene Ontology (GO)
   Biological processprotein amino acid glycosylation Ref.4

Inferred from mutant phenotype. Source: SGD

   Cellular componentGolgi apparatus Ref.4

Inferred from direct assay. Source: SGD

   Molecular functionalpha-1,2-mannosyltransferase activity Ref.4

Inferred from mutant phenotype. Source: SGD

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Signal peptide1 – 2929 Potential
Chain30 – 586557Alpha-1,2-mannosyltransferase MNN5
PRO_0000203019

Amino acid modifications

Glycosylation1131N-linked (GlcNAc...) Potential
Glycosylation1361N-linked (GlcNAc...) Potential
Glycosylation2591N-linked (GlcNAc...) Potential
Glycosylation2641N-linked (GlcNAc...) Potential

Sequences

Sequence LengthMass (Da)Tools
P46982-1 [UniParc].

Last modified February 1, 1996. Version 1.
Checksum: 51E655EB5EE34FED

FASTA58667,252
        10         20         30         40         50         60 
MLIRLKKRKI LQVIVSAVVL ILFFCSVHND VSSSWLYGKK LRLPVLTRSN LKNNFYTTLV 

        70         80         90        100        110        120 
QAIVENKPAD SSPDLSKLHG AEGCSFANNV AAHDSGHDSD LSYESLSKCY NLNKTVQESL 

       130        140        150        160        170        180 
REVHSKFTDT LSGKLNFSIP QREALFSGSE GIVTIGGGKY SVLAYTMIKK LRDTGTTLPI 

       190        200        210        220        230        240 
EVIIPPQDEG EDDFCKNWLP KFNGKCIYFS DIVPSKPLSD LKLTHFQLKV FGLIISSFKR 

       250        260        270        280        290        300 
IIFLDADNYA VKNLDLAFNT TSFNDTGLIL WPDFWRRVTP PAFYNIIGSS INIGKRVRFV 

       310        320        330        340        350        360 
SDDISPVSRY DPFVSNSNDY TPKERQEHFL KHVPLHDLDG TMPDLSSESG QMVIDKIRHF 

       370        380        390        400        410        420 
NTLLLALYYN VYGPTWYYKM ISQGTAGEGD KDTFFAAAHA LNMPYYQVRT NFEFDGFFYQ 

       430        440        450        460        470        480 
KDDYKGLALL QHDFEQDYKQ YQKAQQKVKA NIEEFSKLDP DYTLDNGFLK TLMVNDDGSD 

       490        500        510        520        530        540 
LDIMFIHASF YKADPWTLYH ENRFIGPNGE QVRGFRKPHR YGMDFELFLF NDMRGSFCTT 

       550        560        570        580 
PKSQVIKFKY FTDKVNTPEW DAMCEYLTNH VNYLESTHKE AMGEKN 

« Hide

References

« Hide 'large scale' references
[1]"Complete nucleotide sequence of Saccharomyces cerevisiae chromosome X."
Galibert F., Alexandraki D., Baur A., Boles E., Chalwatzis N., Chuat J.-C., Coster F., Cziepluch C., de Haan M., Domdey H., Durand P., Entian K.-D., Gatius M., Goffeau A., Grivell L.A., Hennemann A., Herbert C.J., Heumann K. expand/collapse author list , Hilger F., Hollenberg C.P., Huang M.-E., Jacq C., Jauniaux J.-C., Katsoulou C., Kirchrath L., Kleine K., Kordes E., Koetter P., Liebl S., Louis E.J., Manus V., Mewes H.-W., Miosga T., Obermaier B., Perea J., Pohl T.M., Portetelle D., Pujol A., Purnelle B., Ramezani Rad M., Rasmussen S.W., Rose M., Rossau R., Schaaff-Gerstenschlaeger I., Smits P.H.M., Scarcez T., Soriano N., To Van D., Tzermia M., Van Broekhoven A., Vandenbol M., Wedler H., von Wettstein D., Wambutt R., Zagulski M., Zollner A., Karpfinger-Hartl L.
EMBO J. 15:2031-2049(1996) [PubMed: 8641269] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: ATCC 96604 / S288c / FY1679.
[2]"Saccharomyces cerevisiae mannoprotein mutants. Isolation of the mnn5 mutant and comparison with the mnn3 strain."
Cohen R.E., Ballou L., Ballou C.E.
J. Biol. Chem. 255:7700-7707(1980) [PubMed: 6995454] [Abstract]
Cited for: FUNCTION.
[3]"Effects of mannoprotein mutations on Saccharomyces cerevisiae core oligosaccharide structure."
Cohen R.E., Zhang W., Ballou C.E.
J. Biol. Chem. 257:5730-5737(1982) [PubMed: 6802821] [Abstract]
Cited for: FUNCTION.
[4]"Identification of the MNN2 and MNN5 mannosyltransferases required for forming and extending the mannose branches of the outer chain mannans of Saccharomyces cerevisiae."
Rayner J.C., Munro S.
J. Biol. Chem. 273:26836-26843(1998) [PubMed: 9756928] [Abstract]
Cited for: FUNCTION, GLYCOSYLATION, SUBCELLULAR LOCATION.
[5]"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].
[6]"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].
+Additional computationally mapped references.

Cross-references

Sequence databases

Z49461 Genomic DNA. Translation: CAA89481.1.
PIRS56969.
RefSeqNP_012349.1.

3D structure databases

ModBaseSearch...

Protein-protein interaction databases

DIPDIP:2868N.
IntActP46982. 1 interaction.

Protein family/group databases

CAZyGT71. Glycosyltransferase Family 71.

Proteomic databases

PeptideAtlasP46982.

Genome annotation databases

EnsemblYJL186W. Saccharomyces cerevisiae. [Contig view]
GeneID853253.
GenomeReviewsGene locus YJL186W in contig Y13136_GR.
KEGGsce:YJL186W.
NMPDRfig|4932.3.peg.3313.

Organism-specific databases

CYGDYJL186w.
SGDS000003722. MNN5.
Yeast-GFPSearch...

Phylogenomic databases

HOGENOMP46982.
OMAP46982. ALLQHDF.

Gene expression databases

ArrayExpressP46982.
GermOnlineYJL186W. Saccharomyces cerevisiae.

Family and domain databases

ProtoNetSearch...

Other Resources

NextBio973499.

Entry information

Entry nameMNN5_YEAST
AccessionPrimary (citable) accession number: P46982
Entry history
Integrated into UniProtKB/Swiss-Prot: February 1, 1996
Last sequence update: February 1, 1996
Last modified: June 16, 2009
This is version 52 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation projectFPAP (Fungal Proteome Annotation Project)

Relevant documents

PATHWAY comments

Index of metabolic and biosynthesis pathways

SIMILARITY comments

Index of protein domains and families

Yeast

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

Yeast chromosome X

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

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