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Q01662

- MAP1_YEAST

UniProt

Q01662 - MAP1_YEAST

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Protein
Methionine aminopeptidase 1
Gene
MAP1, YLR244C, L9672.12
Organism
Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Status
Reviewed - Annotation score: 5 out of 5 - Experimental evidence at protein leveli

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 the major role in N-terminal methionine removal. Less efficient when the second residue is Val.4 Publications

Catalytic activityi

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

Enzyme regulationi

In contract to the MetAP 2 isoform, is not inhibited by the fungal metabolite fumagillin, an antiangiogenic drug.1 Publication

Kineticsi

Kcat is 1173, 1416 and 507 (Min-1) with a Met-Ala-Ser, a Met-Gly-Met-Met and a Met-Ala-Ser-Trp peptide substrate, respectively.

  1. KM=2.68 mM for a Met-Ala-Ser peptide2 Publications
  2. KM=6.56 mM for a Met-Gly-Met-Met peptide
  3. KM=139 µM for a Met-Ala-Ser-Trp peptide

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei202 – 2021Substrate By similarity
Metal bindingi219 – 2191Divalent metal cation 1 By similarity
Metal bindingi230 – 2301Divalent metal cation 1 By similarity
Metal bindingi230 – 2301Divalent metal cation 2; catalytic By similarity
Metal bindingi294 – 2941Divalent metal cation 2; catalytic; via tele nitrogen By similarity
Binding sitei301 – 3011Substrate By similarity
Metal bindingi327 – 3271Divalent metal cation 2; catalytic By similarity
Metal bindingi358 – 3581Divalent metal cation 1 By similarity
Metal bindingi358 – 3581Divalent metal cation 2; catalytic By similarity

GO - Molecular functioni

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

GO - Biological processi

  1. negative regulation of gene expression Source: SGD
  2. protein initiator methionine removal involved in protein maturation Source: SGD
Complete GO annotation...

Keywords - Molecular functioni

Aminopeptidase, Hydrolase, Protease

Keywords - Ligandi

Metal-binding, Zinc

Enzyme and pathway databases

BioCyciYEAST:YLR244C-MONOMER.

Protein family/group databases

MEROPSiM24.017.

Names & Taxonomyi

Protein namesi
Recommended name:
Methionine aminopeptidase 1 (EC:3.4.11.18)
Short name:
MAP 1
Short name:
MetAP 1
Alternative name(s):
Peptidase M 1
Gene namesi
Name:MAP1
Ordered Locus Names:YLR244C
ORF Names:L9672.12
OrganismiSaccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Taxonomic identifieri559292 [NCBI]
Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaSaccharomycotinaSaccharomycetesSaccharomycetalesSaccharomycetaceaeSaccharomyces
ProteomesiUP000002311: Chromosome XII

Organism-specific databases

CYGDiYLR244c.
SGDiS000004234. MAP1.

Subcellular locationi

Cytoplasm UniRule annotation

GO - Cellular componenti

  1. cytosolic ribosome Source: SGD
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi22 – 221C → S: Changes the ribosome profile distribution of the protein and also increases its occurrence in the cytosolic fraction. 1 Publication
Mutagenesisi62 – 621H → R: Changes the ribosome profile distribution of the protein. 1 Publication
Mutagenesisi219 – 2191D → N: Reduces activity 1000-fold. 1 Publication

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Initiator methioninei1 – 11Removed1 Publication
Propeptidei2 – 109UniRule annotation
PRO_0000018596
Chaini11 – 387377Methionine aminopeptidase 1UniRule annotation
PRO_0000018597Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei2 – 21N-acetylserine1 Publication

Keywords - PTMi

Acetylation

Proteomic databases

MaxQBiQ01662.
PaxDbiQ01662.
PeptideAtlasiQ01662.

Expressioni

Gene expression databases

GenevestigatoriQ01662.

Interactioni

Subunit structurei

Associates with the 60S ribosomal subunit of the 80S translational complex.1 Publication

Protein-protein interaction databases

BioGridi31511. 21 interactions.
IntActiQ01662. 2 interactions.
MINTiMINT-2786997.
STRINGi4932.YLR244C.

Structurei

3D structure databases

ProteinModelPortaliQ01662.
SMRiQ01662. Positions 62-379.

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni22 – 6645Zinc finger-like; important for proper ribosome associationUniRule annotation
Add
BLAST

Sequence similaritiesi

Phylogenomic databases

eggNOGiCOG0024.
GeneTreeiENSGT00390000002284.
HOGENOMiHOG000030427.
KOiK01265.
OMAiCFKRNWS.
OrthoDBiEOG78WM23.

Family and domain databases

Gene3Di3.90.230.10. 1 hit.
HAMAPiMF_01974. MetAP_1.
InterProiIPR001714. Pept_M24_MAP.
IPR000994. Pept_M24_structural-domain.
IPR002467. Pept_M24A_MAP1.
[Graphical view]
PfamiPF00557. Peptidase_M24. 1 hit.
[Graphical view]
PRINTSiPR00599. MAPEPTIDASE.
SUPFAMiSSF55920. SSF55920. 1 hit.
TIGRFAMsiTIGR00500. met_pdase_I. 1 hit.
PROSITEiPS00680. MAP_1. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

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

Q01662-1 [UniParc]FASTAAdd to Basket

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MSTATTTVTT SDQASHPTKI YCSGLQCGRE TSSQMKCPVC LKQGIVSIFC    50
DTSCYENNYK AHKALHNAKD GLEGAYDPFP KFKYSGKVKA SYPLTPRRYV 100
PEDIPKPDWA ANGLPVSEQR NDRLNNIPIY KKDQIKKIRK ACMLGREVLD 150
IAAAHVRPGI TTDELDEIVH NETIKRGAYP SPLNYYNFPK SLCTSVNEVI 200
CHGVPDKTVL KEGDIVNLDV SLYYQGYHAD LNETYYVGEN ISKEALNTTE 250
TSRECLKLAI KMCKPGTTFQ ELGDHIEKHA TENKCSVVRT YCGHGVGEFF 300
HCSPNIPHYA KNRTPGVMKP GMVFTIEPMI NEGTWKDMTW PDDWTSTTQD 350
GKLSAQFEHT LLVTEHGVEI LTARNKKSPG GPRQRIK 387
Length:387
Mass (Da):43,373
Last modified:February 1, 1996 - v2
Checksum:i4F0A30E9908B8A55
GO

Mass spectrometryi

Molecular mass is 43779 Da from positions 2 - 387. Determined by MALDI. The measured mass is that of a near-native protein after Factor Xa-catalyzed cleavage of a GST fusion, having a remnant Gly-Ile-Pro-Glu-Phe peptide before the native Ser-2.1 Publication

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
M77092 mRNA. Translation: AAA75193.1.
U20865 Genomic DNA. Translation: AAB67398.1.
BK006945 Genomic DNA. Translation: DAA09558.1.
PIRiS59390.
RefSeqiNP_013345.1. NM_001182131.1.

Genome annotation databases

EnsemblFungiiYLR244C; YLR244C; YLR244C.
GeneIDi850945.
KEGGisce:YLR244C.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
M77092 mRNA. Translation: AAA75193.1 .
U20865 Genomic DNA. Translation: AAB67398.1 .
BK006945 Genomic DNA. Translation: DAA09558.1 .
PIRi S59390.
RefSeqi NP_013345.1. NM_001182131.1.

3D structure databases

ProteinModelPortali Q01662.
SMRi Q01662. Positions 62-379.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 31511. 21 interactions.
IntActi Q01662. 2 interactions.
MINTi MINT-2786997.
STRINGi 4932.YLR244C.

Chemistry

BindingDBi Q01662.
ChEMBLi CHEMBL2526.

Protein family/group databases

MEROPSi M24.017.

Proteomic databases

MaxQBi Q01662.
PaxDbi Q01662.
PeptideAtlasi Q01662.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

EnsemblFungii YLR244C ; YLR244C ; YLR244C .
GeneIDi 850945.
KEGGi sce:YLR244C.

Organism-specific databases

CYGDi YLR244c.
SGDi S000004234. MAP1.

Phylogenomic databases

eggNOGi COG0024.
GeneTreei ENSGT00390000002284.
HOGENOMi HOG000030427.
KOi K01265.
OMAi CFKRNWS.
OrthoDBi EOG78WM23.

Enzyme and pathway databases

BioCyci YEAST:YLR244C-MONOMER.

Miscellaneous databases

NextBioi 967402.
PROi Q01662.

Gene expression databases

Genevestigatori Q01662.

Family and domain databases

Gene3Di 3.90.230.10. 1 hit.
HAMAPi MF_01974. MetAP_1.
InterProi IPR001714. Pept_M24_MAP.
IPR000994. Pept_M24_structural-domain.
IPR002467. Pept_M24A_MAP1.
[Graphical view ]
Pfami PF00557. Peptidase_M24. 1 hit.
[Graphical view ]
PRINTSi PR00599. MAPEPTIDASE.
SUPFAMi SSF55920. SSF55920. 1 hit.
TIGRFAMsi TIGR00500. met_pdase_I. 1 hit.
PROSITEi PS00680. MAP_1. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  1. "Molecular cloning, sequencing, deletion, and overexpression of a methionine aminopeptidase gene from Saccharomyces cerevisiae."
    Chang Y.-H., Teichert U., Smith J.A.
    J. Biol. Chem. 267:8007-8011(1992) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA], PROTEIN SEQUENCE OF 11-24.
  2. "The nucleotide sequence of Saccharomyces cerevisiae chromosome XII."
    Johnston M., Hillier L.W., Riles L., Albermann K., Andre B., Ansorge W., Benes V., Brueckner M., Delius H., Dubois E., Duesterhoeft A., Entian K.-D., Floeth M., Goffeau A., Hebling U., Heumann K., Heuss-Neitzel D., Hilbert H.
    , Hilger F., Kleine K., Koetter P., Louis E.J., Messenguy F., Mewes H.-W., Miosga T., Moestl D., Mueller-Auer S., Nentwich U., Obermaier B., Piravandi E., Pohl T.M., Portetelle D., Purnelle B., Rechmann S., Rieger M., Rinke M., Rose M., Scharfe M., Scherens B., Scholler P., Schwager C., Schwarz S., Underwood A.P., Urrestarazu L.A., Vandenbol M., Verhasselt P., Vierendeels F., Voet M., Volckaert G., Voss H., Wambutt R., Wedler E., Wedler H., Zimmermann F.K., Zollner A., Hani J., Hoheisel J.D.
    Nature 387:87-90(1997) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: ATCC 204508 / S288c.
  3. Cited for: GENOME REANNOTATION.
    Strain: ATCC 204508 / S288c.
  4. "Evidence that two zinc fingers in the methionine aminopeptidase from Saccharomyces cerevisiae are important for normal growth."
    Zuo S., Guo Q., Ling C., Chang Y.H.
    Mol. Gen. Genet. 246:247-253(1995) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, ZINC-BINDING, BIOPHYSICOCHEMICAL PROPERTIES.
  5. "A dominant negative mutation in Saccharomyces cerevisiae methionine aminopeptidase-1 affects catalysis and interferes with the function of methionine aminopeptidase-2."
    Klinkenberg M., Ling C., Chang Y.H.
    Arch. Biochem. Biophys. 347:193-200(1997) [PubMed] [Europe PMC] [Abstract]
    Cited for: MUTAGENESIS OF ASP-219.
  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: ENZYME REGULATION.
  7. "Yeast methionine aminopeptidase I can utilize either Zn2+ or Co2+ as a cofactor: a case of mistaken identity?"
    Walker K.W., Bradshaw R.A.
    Protein Sci. 7:2684-2687(1998) [PubMed] [Europe PMC] [Abstract]
    Cited for: COFACTOR.
  8. "Yeast (Saccharomyces cerevisiae) methionine aminopeptidase I: rapid purification and improved activity assay."
    Walker K.W., Yi E., Bradshaw R.A.
    Biotechnol. Appl. Biochem. 29:157-163(1999) [PubMed] [Europe PMC] [Abstract]
    Cited for: BIOPHYSICOCHEMICAL PROPERTIES, MASS SPECTROMETRY.
  9. "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.
  10. "Yeast methionine aminopeptidase type 1 is ribosome-associated and requires its N-terminal zinc finger domain for normal function in vivo."
    Vetro J.A., Chang Y.H.
    J. Cell. Biochem. 85:678-688(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, SUBUNIT, MUTAGENESIS OF CYS-22 AND HIS-62.
  11. "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.
  12. Cited for: LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS].
  13. 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 nameiMAP1_YEAST
AccessioniPrimary (citable) accession number: Q01662
Secondary accession number(s): D6VYP2
Entry historyi
Integrated into UniProtKB/Swiss-Prot: April 1, 1993
Last sequence update: February 1, 1996
Last modified: July 9, 2014
This is version 127 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 19600 molecules/cell in log phase SD medium.

Keywords - Technical termi

Complete proteome, Direct protein sequencing, 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 XII
    Yeast (Saccharomyces cerevisiae) chromosome XII: entries and gene names

External Data

Dasty 3

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