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P31382

- PMT2_YEAST

UniProt

P31382 - PMT2_YEAST

Protein

Dolichyl-phosphate-mannose--protein mannosyltransferase 2

Gene

PMT2

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 142 (01 Oct 2014)
      Sequence version 2 (16 Jun 2003)
      Previous versions | rss
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    Functioni

    Transfers mannose from Dol-P-mannose to Ser or Thr residues on proteins. Seems to be active on chitinase.

    Catalytic activityi

    Dolichyl phosphate D-mannose + protein = dolichyl phosphate + O-D-mannosylprotein.

    Pathwayi

    GO - Molecular functioni

    1. dolichyl-phosphate-mannose-protein mannosyltransferase activity Source: SGD
    2. protein binding Source: IntAct

    GO - Biological processi

    1. ER-associated misfolded protein catabolic process Source: SGD
    2. protein exit from endoplasmic reticulum Source: SGD
    3. protein O-linked glycosylation Source: SGD
    4. protein O-linked mannosylation Source: SGD
    5. regulation of endoplasmic reticulum unfolded protein response Source: SGD

    Keywords - Molecular functioni

    Glycosyltransferase, Transferase

    Enzyme and pathway databases

    BioCyciYEAST:YAL023C-MONOMER.
    BRENDAi2.4.1.109. 984.
    UniPathwayiUPA00378.

    Protein family/group databases

    CAZyiGT39. Glycosyltransferase Family 39.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Dolichyl-phosphate-mannose--protein mannosyltransferase 2 (EC:2.4.1.109)
    Gene namesi
    Name:PMT2
    Ordered Locus Names:YAL023C
    ORF Names:FUN25
    OrganismiSaccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
    Taxonomic identifieri559292 [NCBI]
    Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaSaccharomycotinaSaccharomycetesSaccharomycetalesSaccharomycetaceaeSaccharomyces
    ProteomesiUP000002311: Chromosome I

    Organism-specific databases

    CYGDiYAL023c.
    SGDiS000000021. PMT2.

    Subcellular locationi

    GO - Cellular componenti

    1. dolichyl-phosphate-mannose-protein mannosyltransferase Pmt1p-Pmt2p dimer complex Source: SGD
    2. dolichyl-phosphate-mannose-protein mannosyltransferase Pmt5p-Pmt2p dimer complex Source: SGD
    3. integral component of membrane Source: UniProtKB-KW

    Keywords - Cellular componenti

    Endoplasmic reticulum, Membrane

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Initiator methioninei1 – 11Removed1 Publication
    Chaini2 – 759758Dolichyl-phosphate-mannose--protein mannosyltransferase 2PRO_0000121492Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei2 – 21N-acetylserine1 Publication
    Modified residuei32 – 321Phosphoserine1 Publication
    Modified residuei38 – 381Phosphoserine1 Publication
    Modified residuei39 – 391Phosphoserine1 Publication
    Glycosylationi131 – 1311N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi155 – 1551N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi403 – 4031N-linked (GlcNAc...)Sequence Analysis

    Keywords - PTMi

    Acetylation, Glycoprotein, Phosphoprotein

    Proteomic databases

    MaxQBiP31382.
    PaxDbiP31382.
    PeptideAtlasiP31382.

    Expressioni

    Gene expression databases

    GenevestigatoriP31382.

    Interactioni

    Binary interactionsi

    WithEntry#Exp.IntActNotes
    PMT1P337754EBI-13573,EBI-13567
    PMT5P528672EBI-13573,EBI-13591

    Protein-protein interaction databases

    BioGridi31743. 170 interactions.
    DIPiDIP-6720N.
    IntActiP31382. 3 interactions.
    MINTiMINT-655858.
    STRINGi4932.YAL023C.

    Structurei

    3D structure databases

    ProteinModelPortaliP31382.
    SMRiP31382. Positions 358-510.
    ModBaseiSearch...
    MobiDBiSearch...

    Topological domain

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Topological domaini2 – 6463CytoplasmicSequence AnalysisAdd
    BLAST
    Topological domaini86 – 16782LumenalSequence AnalysisAdd
    BLAST
    Topological domaini189 – 19810CytoplasmicSequence Analysis
    Topological domaini220 – 25132LumenalSequence AnalysisAdd
    BLAST
    Topological domaini273 – 28917CytoplasmicSequence AnalysisAdd
    BLAST
    Topological domaini311 – 609299LumenalSequence AnalysisAdd
    BLAST
    Topological domaini631 – 64717CytoplasmicSequence AnalysisAdd
    BLAST
    Topological domaini669 – 6768LumenalSequence Analysis
    Topological domaini698 – 71013CytoplasmicSequence AnalysisAdd
    BLAST
    Topological domaini732 – 75928LumenalSequence AnalysisAdd
    BLAST

    Transmembrane

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Transmembranei65 – 8521HelicalSequence AnalysisAdd
    BLAST
    Transmembranei168 – 18821HelicalSequence AnalysisAdd
    BLAST
    Transmembranei199 – 21921HelicalSequence AnalysisAdd
    BLAST
    Transmembranei252 – 27221HelicalSequence AnalysisAdd
    BLAST
    Transmembranei290 – 31021HelicalSequence AnalysisAdd
    BLAST
    Transmembranei610 – 63021HelicalSequence AnalysisAdd
    BLAST
    Transmembranei648 – 66821HelicalSequence AnalysisAdd
    BLAST
    Transmembranei677 – 69721HelicalSequence AnalysisAdd
    BLAST
    Transmembranei711 – 73121HelicalSequence AnalysisAdd
    BLAST

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini339 – 39456MIR 1PROSITE-ProRule annotationAdd
    BLAST
    Domaini407 – 46357MIR 2PROSITE-ProRule annotationAdd
    BLAST
    Domaini471 – 52959MIR 3PROSITE-ProRule annotationAdd
    BLAST

    Sequence similaritiesi

    Belongs to the glycosyltransferase 39 family.Curated
    Contains 3 MIR domains.PROSITE-ProRule annotation

    Keywords - Domaini

    Repeat, Transmembrane, Transmembrane helix

    Phylogenomic databases

    eggNOGiCOG1928.
    GeneTreeiENSGT00740000115531.
    HOGENOMiHOG000157526.
    KOiK00728.
    OMAiWLCISRF.
    OrthoDBiEOG7BP89X.

    Family and domain databases

    InterProiIPR027005. GlyclTrfase_39_like.
    IPR003342. Glyco_trans_39.
    IPR016093. MIR_motif.
    [Graphical view]
    PANTHERiPTHR10050. PTHR10050. 1 hit.
    PfamiPF02815. MIR. 1 hit.
    PF02366. PMT. 1 hit.
    [Graphical view]
    SMARTiSM00472. MIR. 3 hits.
    [Graphical view]
    SUPFAMiSSF82109. SSF82109. 1 hit.
    PROSITEiPS50919. MIR. 3 hits.
    [Graphical view]

    Sequencei

    Sequence statusi: Complete.

    Sequence processingi: The displayed sequence is further processed into a mature form.

    P31382-1 [UniParc]FASTAAdd to Basket

    « Hide

    MSSSSSTGYS KNNAAHIKQE NTLRQRESSS ISVSEELSSA DERDAEDFSK    50
    EKPAAQSSLL RLESVVMPVI FTALALFTRM YKIGINNHVV WDEAHFGKFG 100
    SYYLRHEFYH DVHPPLGKML VGLSGYLAGY NGSWDFPSGE IYPDYLDYVK 150
    MRLFNASFSA LCVPLAYFTA KAIGFSLPTV WLMTVLVLFE NSYSTLGRFI 200
    LLDSMLLFFT VASFFSFVMF HNQRSKPFSR KWWKWLLITG ISLGCTISVK 250
    MVGLFIITMV GIYTVIDLWT FLADKSMSWK TYINHWLARI FGLIIVPFCI 300
    FLLCFKIHFD LLSHSGTGDA NMPSLFQARL VGSDVGQGPR DIALGSSVVS 350
    IKNQALGGSL LHSHIQTYPD GSNQQQVTCY GYKDANNEWF FNRERGLPSW 400
    SENETDIEYL KPGTSYRLVH KSTGRNLHTH PVAAPVSKTQ WEVSGYGDNV 450
    VGDNKDNWVI EIMDQRGDED PEKLHTLTTS FRIKNLEMGC YLAQTGNSLP 500
    EWGFRQQEVV CMKNPFKRDK RTWWNIETHE NERLPPRPED FQYPKTNFLK 550
    DFIHLNLAMM ATNNALVPDP DKFDYLASSA WQWPTLNVGL RLCGWGDDNP 600
    KYFLLGTPAS TWASSVAVLA FMATVVILLI RWQRQYVDLR NPSNWNVFLM 650
    GGFYPLLAWG LHYMPFVIMS RVTYVHHYLP ALYFALIILA YCFDAGLQKW 700
    SRSKCGRIMR FVLYAGFMAL VIGCFWYFSP ISFGMEGPSS NFRYLNWFST 750
    WDIADKQEA 759
    Length:759
    Mass (Da):86,870
    Last modified:June 16, 2003 - v2
    Checksum:iB1E1480C2E04BE3D
    GO

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    L05146 Genomic DNA. Translation: AAC04934.2.
    BK006935 Genomic DNA. Translation: DAA06965.1.
    PIRiS36711.
    RefSeqiNP_009379.2. NM_001178168.1.

    Genome annotation databases

    EnsemblFungiiYAL023C; YAL023C; YAL023C.
    GeneIDi851210.
    KEGGisce:YAL023C.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    L05146 Genomic DNA. Translation: AAC04934.2 .
    BK006935 Genomic DNA. Translation: DAA06965.1 .
    PIRi S36711.
    RefSeqi NP_009379.2. NM_001178168.1.

    3D structure databases

    ProteinModelPortali P31382.
    SMRi P31382. Positions 358-510.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 31743. 170 interactions.
    DIPi DIP-6720N.
    IntActi P31382. 3 interactions.
    MINTi MINT-655858.
    STRINGi 4932.YAL023C.

    Protein family/group databases

    CAZyi GT39. Glycosyltransferase Family 39.

    Proteomic databases

    MaxQBi P31382.
    PaxDbi P31382.
    PeptideAtlasi P31382.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    EnsemblFungii YAL023C ; YAL023C ; YAL023C .
    GeneIDi 851210.
    KEGGi sce:YAL023C.

    Organism-specific databases

    CYGDi YAL023c.
    SGDi S000000021. PMT2.

    Phylogenomic databases

    eggNOGi COG1928.
    GeneTreei ENSGT00740000115531.
    HOGENOMi HOG000157526.
    KOi K00728.
    OMAi WLCISRF.
    OrthoDBi EOG7BP89X.

    Enzyme and pathway databases

    UniPathwayi UPA00378 .
    BioCyci YEAST:YAL023C-MONOMER.
    BRENDAi 2.4.1.109. 984.

    Miscellaneous databases

    NextBioi 968085.

    Gene expression databases

    Genevestigatori P31382.

    Family and domain databases

    InterProi IPR027005. GlyclTrfase_39_like.
    IPR003342. Glyco_trans_39.
    IPR016093. MIR_motif.
    [Graphical view ]
    PANTHERi PTHR10050. PTHR10050. 1 hit.
    Pfami PF02815. MIR. 1 hit.
    PF02366. PMT. 1 hit.
    [Graphical view ]
    SMARTi SM00472. MIR. 3 hits.
    [Graphical view ]
    SUPFAMi SSF82109. SSF82109. 1 hit.
    PROSITEi PS50919. MIR. 3 hits.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "Sequencing of chromosome I from Saccharomyces cerevisiae: analysis of a 32 kb region between the LTE1 and SPO7 genes."
      Ouellette B.F.F., Clark M.W., Keng T., Storms R.K., Zhong W.-W., Zeng B., Fortin N., Delaney S., Barton A.B., Kaback D.B., Bussey H.
      Genome 36:32-42(1993) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
      Strain: ATCC 204511 / S288c / AB972.
    2. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
      Strain: ATCC 204508 / S288c.
    3. Dolinski K.J., Cherry J.M.
      Submitted (DEC-2002) to the EMBL/GenBank/DDBJ databases
      Cited for: SEQUENCE REVISION TO 137-139.
    4. Cited for: GENOME REANNOTATION.
      Strain: ATCC 204508 / S288c.
    5. "Protein O-glycosylation in yeast. The PMT2 gene specifies a second protein O-mannosyltransferase that functions in addition to the PMT1-encoded activity."
      Lussier M., Gentzsch M., Sdicu A.-M., Bussey H., Tanner W.
      J. Biol. Chem. 270:2770-2775(1995) [PubMed] [Europe PMC] [Abstract]
      Cited for: CHARACTERIZATION.
    6. "The PMT gene family: protein O-glycosylation in Saccharomyces cerevisiae is vital."
      Gaentzsch M., Tanner W.
      EMBO J. 15:5752-5759(1996) [PubMed] [Europe PMC] [Abstract]
      Cited for: CHARACTERIZATION.
    7. Cited for: LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS].
    8. "A global topology map of the Saccharomyces cerevisiae membrane proteome."
      Kim H., Melen K., Oesterberg M., von Heijne G.
      Proc. Natl. Acad. Sci. U.S.A. 103:11142-11147(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: TOPOLOGY [LARGE SCALE ANALYSIS].
      Strain: ATCC 208353 / W303-1A.
    9. "Large-scale phosphorylation analysis of alpha-factor-arrested Saccharomyces cerevisiae."
      Li X., Gerber S.A., Rudner A.D., Beausoleil S.A., Haas W., Villen J., Elias J.E., Gygi S.P.
      J. Proteome Res. 6:1190-1197(2007) [PubMed] [Europe PMC] [Abstract]
      Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Strain: ADR376.
    10. "A multidimensional chromatography technology for in-depth phosphoproteome analysis."
      Albuquerque C.P., Smolka M.B., Payne S.H., Bafna V., Eng J., Zhou H.
      Mol. Cell. Proteomics 7:1389-1396(2008) [PubMed] [Europe PMC] [Abstract]
      Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    11. "Global analysis of Cdk1 substrate phosphorylation sites provides insights into evolution."
      Holt L.J., Tuch B.B., Villen J., Johnson A.D., Gygi S.P., Morgan D.O.
      Science 325:1682-1686(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-32; SER-38 AND SER-39, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    12. Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT SER-2, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS], CLEAVAGE OF INITIATOR METHIONINE [LARGE SCALE ANALYSIS].

    Entry informationi

    Entry nameiPMT2_YEAST
    AccessioniPrimary (citable) accession number: P31382
    Secondary accession number(s): D6VPJ5
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: July 1, 1993
    Last sequence update: June 16, 2003
    Last modified: October 1, 2014
    This is version 142 of the entry and version 2 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programFungal Protein Annotation Program

    Miscellaneousi

    Miscellaneous

    Present with 6510 molecules/cell in log phase SD medium.1 Publication

    Keywords - Technical termi

    Complete proteome, Reference proteome

    Documents

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

    External Data

    Dasty 3