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P50108

- MNN10_YEAST

UniProt

P50108 - MNN10_YEAST

Protein

Probable alpha-1,6-mannosyltransferase MNN10

Gene

MNN10

Organism
Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 117 (01 Oct 2014)
      Sequence version 1 (01 Oct 1996)
      Previous versions | rss
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    Functioni

    Required for polarized growth and efficient budding.
    The M-Pol II complex possesses alpha-1,6-mannosyltransferase activity and is probably involved in the elongation of the mannan backbone of N-linked glycans on cell wall and periplasmic proteins.

    GO - Molecular functioni

    1. alpha-1,6-mannosyltransferase activity Source: UniProtKB
    2. protein binding Source: IntAct

    GO - Biological processi

    1. barrier septum assembly Source: SGD
    2. cell budding Source: UniProtKB
    3. cell wall mannoprotein biosynthetic process Source: UniProtKB
    4. mannosylation Source: GOC
    5. protein N-linked glycosylation Source: SGD

    Keywords - Molecular functioni

    Glycosyltransferase, Transferase

    Enzyme and pathway databases

    BioCyciYEAST:G3O-29818-MONOMER.

    Protein family/group databases

    CAZyiGT34. Glycosyltransferase Family 34.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Probable alpha-1,6-mannosyltransferase MNN10 (EC:2.4.1.-)
    Alternative name(s):
    Bud emergence delay protein 1
    Mannan polymerase II complex MNN10 subunit
    Short name:
    M-Pol II subunit MNN10
    Gene namesi
    Name:MNN10
    Synonyms:BED1
    Ordered Locus Names:YDR245W
    ORF Names:YD8419.12
    OrganismiSaccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
    Taxonomic identifieri559292 [NCBI]
    Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaSaccharomycotinaSaccharomycetesSaccharomycetalesSaccharomycetaceaeSaccharomyces
    ProteomesiUP000002311: Chromosome IV

    Organism-specific databases

    CYGDiYDR245w.
    SGDiS000002653. MNN10.

    Subcellular locationi

    GO - Cellular componenti

    1. alpha-1,6-mannosyltransferase complex Source: UniProtKB
    2. endoplasmic reticulum membrane Source: UniProtKB-SubCell

    Keywords - Cellular componenti

    Endoplasmic reticulum, Golgi apparatus, Membrane

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 393393Probable alpha-1,6-mannosyltransferase MNN10PRO_0000215164Add
    BLAST

    Proteomic databases

    MaxQBiP50108.
    PaxDbiP50108.
    PeptideAtlasiP50108.

    Expressioni

    Gene expression databases

    GenevestigatoriP50108.

    Interactioni

    Subunit structurei

    Component of the M-Pol II complex composed of ANP1, MNN9, MNN10, MNN11 and HOC1.1 Publication

    Binary interactionsi

    WithEntry#Exp.IntActNotes
    ANP1P326293EBI-11043,EBI-2595
    HOC1P471243EBI-11043,EBI-8430
    MNN11P469855EBI-11043,EBI-11052

    Protein-protein interaction databases

    BioGridi32296. 360 interactions.
    DIPiDIP-892N.
    IntActiP50108. 21 interactions.
    MINTiMINT-670082.
    STRINGi4932.YDR245W.

    Structurei

    3D structure databases

    ProteinModelPortaliP50108.
    ModBaseiSearch...
    MobiDBiSearch...

    Topological domain

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Topological domaini1 – 5252CytoplasmicSequence AnalysisAdd
    BLAST
    Topological domaini74 – 393320LumenalSequence AnalysisAdd
    BLAST

    Transmembrane

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Transmembranei53 – 7321Helical; Signal-anchor for type II membrane proteinSequence AnalysisAdd
    BLAST

    Family & Domainsi

    Sequence similaritiesi

    Belongs to the glycosyltransferase 34 family.Curated

    Keywords - Domaini

    Signal-anchor, Transmembrane, Transmembrane helix

    Phylogenomic databases

    eggNOGiNOG266323.
    HOGENOMiHOG000165792.
    KOiK05531.
    OMAiHEYREGW.
    OrthoDBiEOG7M3J8X.

    Family and domain databases

    InterProiIPR008630. Glyco_trans_34.
    [Graphical view]
    PfamiPF05637. Glyco_transf_34. 1 hit.
    [Graphical view]

    Sequencei

    Sequence statusi: Complete.

    P50108-1 [UniParc]FASTAAdd to Basket

    « Hide

    MSSVPYNSQL PISNHLEYDE DEKKSRGSKL GLKYKMIYWR KTLCSSLARW    50
    RKLILLISLA LFLFIWISDS TISRNPSTTS FQGQNSNDNK LSNTGSSINS 100
    KRYVPPYSKR SRWSFWNQDP RIVIILAANE GGGVLRWKNE QEWAIEGISI 150
    ENKKAYAKRH GYALTIKDLT TSKRYSHEYR EGWQKVDILR QTFREFPNAE 200
    WFWWLDLDTM IMEPSKSLEE HIFDRLETLA DRELKSFNPL NLRDDIPYVD 250
    YSEEMEFLIT QDCGGFNLGS FLIKNSEWSK LLLDMWWDPV LYEQKHMVWE 300
    HREQDALEAL YENEPWIRSR IGFLPLRTIN AFPPGACSEY SGDSRYFYSE 350
    KDHDFVVNMA GCNFGRDCWG EMQYYTTLME KLNRKWYTRF FFP 393
    Length:393
    Mass (Da):46,748
    Last modified:October 1, 1996 - v1
    Checksum:iFAF7DBE3122ECC8E
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti238 – 2381N → I in AAC49280. (PubMed:8567719)Curated

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    L42540 Genomic DNA. Translation: AAB48372.1.
    U31446 Genomic DNA. Translation: AAC49280.1.
    Z49701 Genomic DNA. Translation: CAA89731.1.
    AY557792 Genomic DNA. Translation: AAS56118.1.
    BK006938 Genomic DNA. Translation: DAA12085.1.
    PIRiS54541.
    RefSeqiNP_010531.1. NM_001180553.1.

    Genome annotation databases

    EnsemblFungiiYDR245W; YDR245W; YDR245W.
    GeneIDi851832.
    KEGGisce:YDR245W.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    L42540 Genomic DNA. Translation: AAB48372.1 .
    U31446 Genomic DNA. Translation: AAC49280.1 .
    Z49701 Genomic DNA. Translation: CAA89731.1 .
    AY557792 Genomic DNA. Translation: AAS56118.1 .
    BK006938 Genomic DNA. Translation: DAA12085.1 .
    PIRi S54541.
    RefSeqi NP_010531.1. NM_001180553.1.

    3D structure databases

    ProteinModelPortali P50108.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 32296. 360 interactions.
    DIPi DIP-892N.
    IntActi P50108. 21 interactions.
    MINTi MINT-670082.
    STRINGi 4932.YDR245W.

    Protein family/group databases

    CAZyi GT34. Glycosyltransferase Family 34.

    Proteomic databases

    MaxQBi P50108.
    PaxDbi P50108.
    PeptideAtlasi P50108.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    EnsemblFungii YDR245W ; YDR245W ; YDR245W .
    GeneIDi 851832.
    KEGGi sce:YDR245W.

    Organism-specific databases

    CYGDi YDR245w.
    SGDi S000002653. MNN10.

    Phylogenomic databases

    eggNOGi NOG266323.
    HOGENOMi HOG000165792.
    KOi K05531.
    OMAi HEYREGW.
    OrthoDBi EOG7M3J8X.

    Enzyme and pathway databases

    BioCyci YEAST:G3O-29818-MONOMER.

    Miscellaneous databases

    NextBioi 969721.

    Gene expression databases

    Genevestigatori P50108.

    Family and domain databases

    InterProi IPR008630. Glyco_trans_34.
    [Graphical view ]
    Pfami PF05637. Glyco_transf_34. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "Molecular and phenotypic analysis of the S. cerevisiae MNN10 gene identifies a family of related glycosyltransferases."
      Dean N., Poster J.B.
      Glycobiology 6:73-81(1996) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION, SUBCELLULAR LOCATION.
    2. "BED1, a gene encoding a galactosyltransferase homologue, is required for polarized growth and efficient bud emergence in Saccharomyces cerevisiae."
      Mondesert G., Reed S.I.
      J. Cell Biol. 132:137-151(1996) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION, SUBCELLULAR LOCATION.
      Strain: BF264-15DU.
    3. "The nucleotide sequence of Saccharomyces cerevisiae chromosome IV."
      Jacq C., Alt-Moerbe J., Andre B., Arnold W., Bahr A., Ballesta J.P.G., Bargues M., Baron L., Becker A., Biteau N., Bloecker H., Blugeon C., Boskovic J., Brandt P., Brueckner M., Buitrago M.J., Coster F., Delaveau T.
      , del Rey F., Dujon B., Eide L.G., Garcia-Cantalejo J.M., Goffeau A., Gomez-Peris A., Granotier C., Hanemann V., Hankeln T., Hoheisel J.D., Jaeger W., Jimenez A., Jonniaux J.-L., Kraemer C., Kuester H., Laamanen P., Legros Y., Louis E.J., Moeller-Rieker S., Monnet A., Moro M., Mueller-Auer S., Nussbaumer B., Paricio N., Paulin L., Perea J., Perez-Alonso M., Perez-Ortin J.E., Pohl T.M., Prydz H., Purnelle B., Rasmussen S.W., Remacha M.A., Revuelta J.L., Rieger M., Salom D., Saluz H.P., Saiz J.E., Saren A.-M., Schaefer M., Scharfe M., Schmidt E.R., Schneider C., Scholler P., Schwarz S., Soler-Mira A., Urrestarazu L.A., Verhasselt P., Vissers S., Voet M., Volckaert G., Wagner G., Wambutt R., Wedler E., Wedler H., Woelfl S., Harris D.E., Bowman S., Brown D., Churcher C.M., Connor R., Dedman K., Gentles S., Hamlin N., Hunt S., Jones L., McDonald S., Murphy L.D., Niblett D., Odell C., Oliver K., Rajandream M.A., Richards C., Shore L., Walsh S.V., Barrell B.G., Dietrich F.S., Mulligan J.T., Allen E., Araujo R., Aviles E., Berno A., Carpenter J., Chen E., Cherry J.M., Chung E., Duncan M., Hunicke-Smith S., Hyman R.W., Komp C., Lashkari D., Lew H., Lin D., Mosedale D., Nakahara K., Namath A., Oefner P., Oh C., Petel F.X., Roberts D., Schramm S., Schroeder M., Shogren T., Shroff N., Winant A., Yelton M.A., Botstein D., Davis R.W., Johnston M., Andrews S., Brinkman R., Cooper J., Ding H., Du Z., Favello A., Fulton L., Gattung S., Greco T., Hallsworth K., Hawkins J., Hillier L.W., Jier M., Johnson D., Johnston L., Kirsten J., Kucaba T., Langston Y., Latreille P., Le T., Mardis E., Menezes S., Miller N., Nhan M., Pauley A., Peluso D., Rifkin L., Riles L., Taich A., Trevaskis E., Vignati D., Wilcox L., Wohldman P., Vaudin M., Wilson R., Waterston R., Albermann K., Hani J., Heumann K., Kleine K., Mewes H.-W., Zollner A., Zaccaria P.
      Nature 387:75-78(1997) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
      Strain: ATCC 204508 / S288c.
    4. Cited for: GENOME REANNOTATION.
      Strain: ATCC 204508 / S288c.
    5. Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
      Strain: ATCC 204508 / S288c.
    6. "The Saccharomyces cerevisiae protein Mnn10p/Bed1p is a subunit of a Golgi mannosyltransferase complex."
      Jungmann J., Rayner J.C., Munro S.
      J. Biol. Chem. 274:6579-6585(1999) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, SUBUNIT.
    7. Cited for: LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS].

    Entry informationi

    Entry nameiMNN10_YEAST
    AccessioniPrimary (citable) accession number: P50108
    Secondary accession number(s): D6VSM5
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: October 1, 1996
    Last sequence update: October 1, 1996
    Last modified: October 1, 2014
    This is version 117 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 6280 molecules/cell in log phase SD medium.1 Publication

    Keywords - Technical termi

    Complete proteome, Reference proteome

    Documents

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

    External Data

    Dasty 3