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P38174

- MAP2_YEAST

UniProt

P38174 - MAP2_YEAST

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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

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

Co2+UniRule annotation, Zn2+UniRule annotation, Mn2+UniRule annotation, Fe2+UniRule annotationNote: 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 Fe(2+)-metalloproteases under physiological conditions, and the catalytically relevant metal-binding site has been assigned to the histidine-containing high-affinity site. 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
Complete GO annotation...

Keywords - Molecular functioni

Aminopeptidase, Hydrolase, Protease

Keywords - Ligandi

Metal-binding

Enzyme and pathway databases

BioCyciYEAST:YBL091C-MONOMER.
ReactomeiREACT_241032. Inactivation, recovery and regulation of the phototransduction cascade.

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-KW
Complete GO annotation...

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. 16 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.
InParanoidiP38174.
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

        10         20         30         40         50
MTDAEIENSP ASDLKELNLE NEGVEQQDQA KADESDPVES KKKKNKKKKK
60 70 80 90 100
KKSNVKKIEL LFPDGKYPEG AWMDYHQDFN LQRTTDEESR YLKRDLERAE
110 120 130 140 150
HWNDVRKGAE IHRRVRRAIK DRIVPGMKLM DIADMIENTT RKYTGAENLL
160 170 180 190 200
AMEDPKSQGI GFPTGLSLNH CAAHFTPNAG DKTVLKYEDV MKVDYGVQVN
210 220 230 240 250
GNIIDSAFTV SFDPQYDNLL AAVKDATYTG IKEAGIDVRL TDIGEAIQEV
260 270 280 290 300
MESYEVEING ETYQVKPCRN LCGHSIAPYR IHGGKSVPIV KNGDTTKMEE
310 320 330 340 350
GEHFAIETFG STGRGYVTAG GEVSHYARSA EDHQVMPTLD SAKNLLKTID
360 370 380 390 400
RNFGTLPFCR RYLDRLGQEK YLFALNNLVR HGLVQDYPPL NDIPGSYTAQ
410 420
FEHTILLHAH KKEVVSKGDD Y
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.Curated

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:
EMBLi
GenBanki
DDBJi
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:
EMBLi
GenBanki
DDBJi
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. 16 interactions.
DIPi DIP-6459N.
IntActi P38174. 2 interactions.
MINTi MINT-710458.
STRINGi 4932.YBL091C.

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.
InParanoidi P38174.
KOi K01265.
OMAi IQICEEL.
OrthoDBi EOG7BGHW3.

Enzyme and pathway databases

BioCyci YEAST:YBL091C-MONOMER.
Reactomei REACT_241032. Inactivation, recovery and regulation of the phototransduction cascade.

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

« Hide 'large scale' publications
  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: November 26, 2014
This is version 137 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