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P38174

- MAP2_YEAST

UniProt

P38174 - MAP2_YEAST

Protein

Methionine aminopeptidase 2

Gene

MAP2

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 135 (01 Oct 2014)
      Sequence version 4 (27 Jul 2011)
      Previous versions | rss
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    Functioni

    Cotranslationally removes the N-terminal methionine from nascent proteins. The N-terminal methionine is often cleaved when the second residue in the primary sequence is small and uncharged (Met-Ala-, Cys, Gly, Pro, Ser, Thr, or Val). Plays only a minor role in N-terminal methionine removal. Less efficient when the second residue is Val, Gly, Cys or Thr.5 PublicationsUniRule annotation

    Catalytic activityi

    Release of N-terminal amino acids, preferentially methionine, from peptides and arylamides.1 PublicationUniRule annotation

    Cofactori

    Binds 2 divalent metal cations per subunit. Has a high-affinity and a low affinity metal-binding site. The true nature of the physiological cofactor is under debate. The enzyme is active with cobalt, zinc, manganese or divalent iron ions. Most likely, methionine aminopeptidases function as mononuclear Fe2+-metalloproteases under physiological conditions, and the catalytically relevant metal-binding site has been assigned to the histidine-containing high-affinity site By similarity. Also zinc has been proposed to be the physiological cofactor for yeast.UniRule annotation

    Enzyme regulationi

    Irreversibly inhibited by the fungal metabolite fumagillin, an antiangiogenic drug. Subject to product inhibition by cytosolic methionine.2 Publications

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Binding sitei174 – 1741SubstrateUniRule annotation
    Metal bindingi194 – 1941Divalent metal cation 1UniRule annotation
    Metal bindingi205 – 2051Divalent metal cation 1UniRule annotation
    Metal bindingi205 – 2051Divalent metal cation 2; catalyticUniRule annotation
    Metal bindingi274 – 2741Divalent metal cation 2; catalytic; via tele nitrogenUniRule annotation
    Binding sitei282 – 2821SubstrateUniRule annotation
    Metal bindingi307 – 3071Divalent metal cation 2; catalyticUniRule annotation
    Metal bindingi402 – 4021Divalent metal cation 1UniRule annotation
    Metal bindingi402 – 4021Divalent metal cation 2; catalyticUniRule annotation

    GO - Molecular functioni

    1. metal ion binding Source: UniProtKB-HAMAP
    2. metalloaminopeptidase activity Source: SGD

    GO - Biological processi

    1. protein initiator methionine removal involved in protein maturation Source: SGD

    Keywords - Molecular functioni

    Aminopeptidase, Hydrolase, Protease

    Keywords - Ligandi

    Metal-binding

    Enzyme and pathway databases

    BioCyciYEAST:YBL091C-MONOMER.

    Protein family/group databases

    MEROPSiM24.002.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Methionine aminopeptidase 2UniRule annotation (EC:3.4.11.18UniRule annotation)
    Short name:
    MAP 2UniRule annotation
    Short name:
    MetAP 2UniRule annotation
    Alternative name(s):
    Peptidase MUniRule annotation
    Gene namesi
    Name:MAP2UniRule annotation
    Ordered Locus Names:YBL091C
    ORF Names:YBL0701
    OrganismiSaccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
    Taxonomic identifieri559292 [NCBI]
    Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaSaccharomycotinaSaccharomycetesSaccharomycetalesSaccharomycetaceaeSaccharomyces
    ProteomesiUP000002311: Chromosome II

    Organism-specific databases

    CYGDiYBL091c.
    SGDiS000000187. MAP2.

    Subcellular locationi

    Cytoplasm 1 PublicationUniRule annotation

    GO - Cellular componenti

    1. cytoplasm Source: UniProtKB-SubCell

    Keywords - Cellular componenti

    Cytoplasm

    Pathology & Biotechi

    Mutagenesis

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Mutagenesisi174 – 1741H → A: Abolishes catalytic activity. 1 Publication

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 421421Methionine aminopeptidase 2PRO_0000148988Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei35 – 351Phosphoserine2 Publications

    Keywords - PTMi

    Phosphoprotein

    Proteomic databases

    MaxQBiP38174.
    PaxDbiP38174.
    PeptideAtlasiP38174.

    Expressioni

    Gene expression databases

    GenevestigatoriP38174.

    Interactioni

    Protein-protein interaction databases

    BioGridi32613. 15 interactions.
    DIPiDIP-6459N.
    IntActiP38174. 2 interactions.
    MINTiMINT-710458.
    STRINGi4932.YBL091C.

    Structurei

    3D structure databases

    ProteinModelPortaliP38174.
    SMRiP38174. Positions 61-421.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Compositional bias

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Compositional biasi41 – 5717Lys-richAdd
    BLAST

    Sequence similaritiesi

    Belongs to the peptidase M24A family. Methionine aminopeptidase eukaryotic type 2 subfamily.UniRule annotation

    Phylogenomic databases

    eggNOGiCOG0024.
    GeneTreeiENSGT00530000063220.
    HOGENOMiHOG000226278.
    KOiK01265.
    OMAiIQICEEL.
    OrthoDBiEOG7BGHW3.

    Family and domain databases

    Gene3Di1.10.10.10. 1 hit.
    3.90.230.10. 2 hits.
    HAMAPiMF_03175. MetAP_2_euk.
    InterProiIPR001714. Pept_M24_MAP.
    IPR000994. Pept_M24_structural-domain.
    IPR002468. Pept_M24A_MAP2.
    IPR018349. Pept_M24A_MAP2_BS.
    IPR011991. WHTH_DNA-bd_dom.
    [Graphical view]
    PANTHERiPTHR10804:SF9. PTHR10804:SF9. 1 hit.
    PfamiPF00557. Peptidase_M24. 1 hit.
    [Graphical view]
    PRINTSiPR00599. MAPEPTIDASE.
    SUPFAMiSSF55920. SSF55920. 2 hits.
    TIGRFAMsiTIGR00501. met_pdase_II. 1 hit.
    PROSITEiPS01202. MAP_2. 1 hit.
    [Graphical view]

    Sequencei

    Sequence statusi: Complete.

    P38174-1 [UniParc]FASTAAdd to Basket

    « Hide

    MTDAEIENSP ASDLKELNLE NEGVEQQDQA KADESDPVES KKKKNKKKKK    50
    KKSNVKKIEL LFPDGKYPEG AWMDYHQDFN LQRTTDEESR YLKRDLERAE 100
    HWNDVRKGAE IHRRVRRAIK DRIVPGMKLM DIADMIENTT RKYTGAENLL 150
    AMEDPKSQGI GFPTGLSLNH CAAHFTPNAG DKTVLKYEDV MKVDYGVQVN 200
    GNIIDSAFTV SFDPQYDNLL AAVKDATYTG IKEAGIDVRL TDIGEAIQEV 250
    MESYEVEING ETYQVKPCRN LCGHSIAPYR IHGGKSVPIV KNGDTTKMEE 300
    GEHFAIETFG STGRGYVTAG GEVSHYARSA EDHQVMPTLD SAKNLLKTID 350
    RNFGTLPFCR RYLDRLGQEK YLFALNNLVR HGLVQDYPPL NDIPGSYTAQ 400
    FEHTILLHAH KKEVVSKGDD Y 421
    Length:421
    Mass (Da):47,518
    Last modified:July 27, 2011 - v4
    Checksum:i206E9651D88925A8
    GO

    Sequence cautioni

    The sequence CAA56011.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally extended.

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti86 – 861D → V in CAA56011. (PubMed:7502586)Curated
    Sequence conflicti86 – 861D → V in CAA84912. (PubMed:7813418)Curated

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    U17437 Genomic DNA. Translation: AAC49142.1.
    X79489 Genomic DNA. Translation: CAA56011.1. Different initiation.
    Z35851 Genomic DNA. Translation: CAA84912.1.
    Z35852 Genomic DNA. Translation: CAA84913.1.
    BK006936 Genomic DNA. Translation: DAA07033.2.
    RefSeqiNP_009462.2. NM_001178331.2.

    Genome annotation databases

    EnsemblFungiiYBL091C; YBL091C; YBL091C.
    GeneIDi852187.
    KEGGisce:YBL091C.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    U17437 Genomic DNA. Translation: AAC49142.1 .
    X79489 Genomic DNA. Translation: CAA56011.1 . Different initiation.
    Z35851 Genomic DNA. Translation: CAA84912.1 .
    Z35852 Genomic DNA. Translation: CAA84913.1 .
    BK006936 Genomic DNA. Translation: DAA07033.2 .
    RefSeqi NP_009462.2. NM_001178331.2.

    3D structure databases

    ProteinModelPortali P38174.
    SMRi P38174. Positions 61-421.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 32613. 15 interactions.
    DIPi DIP-6459N.
    IntActi P38174. 2 interactions.
    MINTi MINT-710458.
    STRINGi 4932.YBL091C.

    Protein family/group databases

    MEROPSi M24.002.

    Proteomic databases

    MaxQBi P38174.
    PaxDbi P38174.
    PeptideAtlasi P38174.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    EnsemblFungii YBL091C ; YBL091C ; YBL091C .
    GeneIDi 852187.
    KEGGi sce:YBL091C.

    Organism-specific databases

    CYGDi YBL091c.
    SGDi S000000187. MAP2.

    Phylogenomic databases

    eggNOGi COG0024.
    GeneTreei ENSGT00530000063220.
    HOGENOMi HOG000226278.
    KOi K01265.
    OMAi IQICEEL.
    OrthoDBi EOG7BGHW3.

    Enzyme and pathway databases

    BioCyci YEAST:YBL091C-MONOMER.

    Miscellaneous databases

    NextBioi 970658.
    PROi P38174.

    Gene expression databases

    Genevestigatori P38174.

    Family and domain databases

    Gene3Di 1.10.10.10. 1 hit.
    3.90.230.10. 2 hits.
    HAMAPi MF_03175. MetAP_2_euk.
    InterProi IPR001714. Pept_M24_MAP.
    IPR000994. Pept_M24_structural-domain.
    IPR002468. Pept_M24A_MAP2.
    IPR018349. Pept_M24A_MAP2_BS.
    IPR011991. WHTH_DNA-bd_dom.
    [Graphical view ]
    PANTHERi PTHR10804:SF9. PTHR10804:SF9. 1 hit.
    Pfami PF00557. Peptidase_M24. 1 hit.
    [Graphical view ]
    PRINTSi PR00599. MAPEPTIDASE.
    SUPFAMi SSF55920. SSF55920. 2 hits.
    TIGRFAMsi TIGR00501. met_pdase_II. 1 hit.
    PROSITEi PS01202. MAP_2. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "Amino-terminal protein processing in Saccharomyces cerevisiae is an essential function that requires two distinct methionine aminopeptidases."
      Li X., Chang Y.-H.
      Proc. Natl. Acad. Sci. U.S.A. 92:12357-12361(1995) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION, CATALYTIC ACTIVITY.
      Strain: ATCC 76626 / YPH500.
    2. "Sequence analysis of a 78.6 kb segment of the left end of Saccharomyces cerevisiae chromosome II."
      Obermaier B., Gassenhuber J., Piravandi E., Domdey H.
      Yeast 11:1103-1112(1995) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
      Strain: ATCC 204508 / S288c.
    3. "Complete DNA sequence of yeast chromosome II."
      Feldmann H., Aigle M., Aljinovic G., Andre B., Baclet M.C., Barthe C., Baur A., Becam A.-M., Biteau N., Boles E., Brandt T., Brendel M., Brueckner M., Bussereau F., Christiansen C., Contreras R., Crouzet M., Cziepluch C.
      , Demolis N., Delaveau T., Doignon F., Domdey H., Duesterhus S., Dubois E., Dujon B., El Bakkoury M., Entian K.-D., Feuermann M., Fiers W., Fobo G.M., Fritz C., Gassenhuber J., Glansdorff N., Goffeau A., Grivell L.A., de Haan M., Hein C., Herbert C.J., Hollenberg C.P., Holmstroem K., Jacq C., Jacquet M., Jauniaux J.-C., Jonniaux J.-L., Kallesoee T., Kiesau P., Kirchrath L., Koetter P., Korol S., Liebl S., Logghe M., Lohan A.J.E., Louis E.J., Li Z.Y., Maat M.J., Mallet L., Mannhaupt G., Messenguy F., Miosga T., Molemans F., Mueller S., Nasr F., Obermaier B., Perea J., Pierard A., Piravandi E., Pohl F.M., Pohl T.M., Potier S., Proft M., Purnelle B., Ramezani Rad M., Rieger M., Rose M., Schaaff-Gerstenschlaeger I., Scherens B., Schwarzlose C., Skala J., Slonimski P.P., Smits P.H.M., Souciet J.-L., Steensma H.Y., Stucka R., Urrestarazu L.A., van der Aart Q.J.M., Van Dyck L., Vassarotti A., Vetter I., Vierendeels F., Vissers S., Wagner G., de Wergifosse P., Wolfe K.H., Zagulski M., Zimmermann F.K., Mewes H.-W., Kleine K.
      EMBO J. 13:5795-5809(1994) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
      Strain: ATCC 204508 / S288c.
    4. Cited for: GENOME REANNOTATION, SEQUENCE REVISION TO 86.
      Strain: ATCC 204508 / S288c.
    5. "Eukaryotic methionyl aminopeptidases: two classes of cobalt-dependent enzymes."
      Arfin S.M., Kendall R.L., Hall L., Weaver L.H., Stewart A.E., Matthews B.W., Bradshaw R.A.
      Proc. Natl. Acad. Sci. U.S.A. 92:7714-7718(1995) [PubMed] [Europe PMC] [Abstract]
      Cited for: IDENTIFICATION.
    6. "The anti-angiogenic agent fumagillin covalently binds and inhibits the methionine aminopeptidase, MetAP-2."
      Sin N., Meng L., Wang M.Q., Wen J.J., Bornmann W.G., Crews C.M.
      Proc. Natl. Acad. Sci. U.S.A. 94:6099-6103(1997) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, ENZYME REGULATION.
    7. "The specificity in vivo of two distinct methionine aminopeptidases in Saccharomyces cerevisiae."
      Chen S., Vetro J.A., Chang Y.H.
      Arch. Biochem. Biophys. 398:87-93(2002) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, SUBSTRATE SPECIFICITY.
    8. "N-terminal methionine removal and methionine metabolism in Saccharomyces cerevisiae."
      Dummitt B., Micka W.S., Chang Y.H.
      J. Cell. Biochem. 89:964-974(2003) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, ENZYME REGULATION.
    9. Cited for: SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
    10. Cited for: LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS].
    11. "Evidence of a dominant negative mutant of yeast methionine aminopeptidase type 2 in Saccharomyces cerevisiae."
      Vetro J.A., Dummitt B., Micka W.S., Chang Y.H.
      J. Cell. Biochem. 94:656-668(2005) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, MUTAGENESIS OF HIS-174.
    12. "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: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-35, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    13. "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-35, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].

    Entry informationi

    Entry nameiMAP2_YEAST
    AccessioniPrimary (citable) accession number: P38174
    Secondary accession number(s): D6VPR3, P89493
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: October 1, 1994
    Last sequence update: July 27, 2011
    Last modified: October 1, 2014
    This is version 135 of the entry and version 4 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programFungal Protein Annotation Program

    Miscellaneousi

    Miscellaneous

    Present with 1080 molecules/cell in log phase SD medium.1 Publication

    Keywords - Technical termi

    Complete proteome, Reference proteome

    Documents

    1. Peptidase families
      Classification of peptidase families and list of entries
    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 II
      Yeast (Saccharomyces cerevisiae) chromosome II: entries and gene names

    External Data

    Dasty 3