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Protein

Methionine aminopeptidase 2

Gene

MAP2

Organism
Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Status
Reviewed-Annotation score: -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.UniRule annotation5 Publications

Miscellaneous

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

Catalytic activityi

Release of N-terminal amino acids, preferentially methionine, from peptides and arylamides.UniRule annotation1 Publication

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 Fe2+-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)DescriptionActionsGraphical viewLength
Binding sitei174SubstrateUniRule annotation1
Metal bindingi194Divalent metal cation 1UniRule annotation1
Metal bindingi205Divalent metal cation 1UniRule annotation1
Metal bindingi205Divalent metal cation 2; catalyticUniRule annotation1
Metal bindingi274Divalent metal cation 2; catalytic; via tele nitrogenUniRule annotation1
Binding sitei282SubstrateUniRule annotation1
Metal bindingi307Divalent metal cation 2; catalyticUniRule annotation1
Metal bindingi402Divalent metal cation 1UniRule annotation1
Metal bindingi402Divalent metal cation 2; catalyticUniRule annotation1

GO - Molecular functioni

  • metal ion binding Source: UniProtKB-KW
  • metalloaminopeptidase activity Source: SGD

GO - Biological processi

  • protein initiator methionine removal involved in protein maturation Source: SGD

Keywordsi

Molecular functionAminopeptidase, Hydrolase, Protease
LigandMetal-binding

Enzyme and pathway databases

BioCyciYEAST:YBL091C-MONOMER
ReactomeiR-SCE-2514859 Inactivation, recovery and regulation of the phototransduction cascade
R-SCE-6798695 Neutrophil degranulation

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
Proteomesi
  • UP000002311 Componenti: Chromosome II

Organism-specific databases

EuPathDBiFungiDB:YBL091C
SGDiS000000187 MAP2

Subcellular locationi

Keywords - Cellular componenti

Cytoplasm

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Mutagenesisi174H → A: Abolishes catalytic activity. 1 Publication1

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00001489881 – 421Methionine aminopeptidase 2Add BLAST421

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei35PhosphoserineCombined sources1

Keywords - PTMi

Phosphoprotein

Proteomic databases

MaxQBiP38174
PaxDbiP38174
PRIDEiP38174

PTM databases

iPTMnetiP38174

Interactioni

Protein-protein interaction databases

BioGridi32613, 70 interactors
DIPiDIP-6459N
IntActiP38174, 3 interactors
STRINGi4932.YBL091C

Structurei

3D structure databases

ProteinModelPortaliP38174
SMRiP38174
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Compositional bias

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Compositional biasi41 – 57Lys-richAdd BLAST17

Sequence similaritiesi

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

Phylogenomic databases

GeneTreeiENSGT00530000063220
HOGENOMiHOG000226278
InParanoidiP38174
KOiK01265
OMAiTINKHFG
OrthoDBiEOG092C3NQP

Family and domain databases

CDDicd01088 MetAP2, 1 hit
Gene3Di1.10.10.10, 1 hit
HAMAPiMF_03175 MetAP_2_euk, 1 hit
InterProiView protein in InterPro
IPR036005 Creatinase/aminopeptidase-like
IPR000994 Pept_M24
IPR001714 Pept_M24_MAP
IPR002468 Pept_M24A_MAP2
IPR018349 Pept_M24A_MAP2_BS
IPR036388 WH-like_DNA-bd_sf
IPR036390 WH_DNA-bd_sf
PfamiView protein in Pfam
PF00557 Peptidase_M24, 1 hit
PRINTSiPR00599 MAPEPTIDASE
SUPFAMiSSF46785 SSF46785, 1 hit
SSF55920 SSF55920, 2 hits
TIGRFAMsiTIGR00501 met_pdase_II, 1 hit
PROSITEiView protein in PROSITE
PS01202 MAP_2, 1 hit

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 differs from that shown. Reason: Erroneous initiation. Translation N-terminally extended.Curated

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sequence conflicti86D → V in CAA56011 (PubMed:7502586).Curated1
Sequence conflicti86D → V in CAA84912 (PubMed:7813418).Curated1

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

Similar proteinsi

Entry informationi

Entry nameiMAP2_YEAST
AccessioniPrimary (citable) accession number: P38174
Secondary accession number(s): D6VPR3, P89493
Entry historyiIntegrated into UniProtKB/Swiss-Prot: October 1, 1994
Last sequence update: July 27, 2011
Last modified: June 20, 2018
This is version 169 of the entry and version 4 of the sequence. See complete history.
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programFungal Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

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