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P38062

- MAP2_RAT

UniProt

P38062 - MAP2_RAT

Protein

Methionine aminopeptidase 2

Gene

Metap2

Organism
Rattus norvegicus (Rat)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 122 (01 Oct 2014)
      Sequence version 2 (01 Oct 1996)
      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).
    Protects eukaryotic initiation factor EIF2S1 from translation-inhibiting phosphorylation by inhibitory kinases such as EIF2AK2/PKR and EIF2AK1/HCR. Plays a critical role in the regulation of protein synthesis.

    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.UniRule annotation

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Binding sitei231 – 2311SubstrateUniRule annotation
    Metal bindingi251 – 2511Divalent metal cation 1UniRule annotation
    Metal bindingi262 – 2621Divalent metal cation 1UniRule annotation
    Metal bindingi262 – 2621Divalent metal cation 2; catalyticUniRule annotation
    Metal bindingi331 – 3311Divalent metal cation 2; catalytic; via tele nitrogenUniRule annotation
    Binding sitei339 – 3391SubstrateUniRule annotation
    Metal bindingi364 – 3641Divalent metal cation 2; catalyticUniRule annotation
    Metal bindingi459 – 4591Divalent metal cation 1UniRule annotation
    Metal bindingi459 – 4591Divalent metal cation 2; catalyticUniRule annotation

    GO - Molecular functioni

    1. aminopeptidase activity Source: UniProtKB
    2. metal ion binding Source: UniProtKB-HAMAP
    3. metalloaminopeptidase activity Source: UniProtKB-HAMAP
    4. metalloexopeptidase activity Source: UniProtKB

    GO - Biological processi

    1. N-terminal protein amino acid modification Source: HGNC
    2. peptidyl-methionine modification Source: HGNC
    3. protein initiator methionine removal Source: UniProtKB-HAMAP
    4. protein processing Source: HGNC

    Keywords - Molecular functioni

    Aminopeptidase, Hydrolase, Protease

    Keywords - Ligandi

    Metal-binding

    Enzyme and pathway databases

    BRENDAi3.4.11.18. 5301.

    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):
    Initiation factor 2-associated 67 kDa glycoproteinUniRule annotation
    Short name:
    p67UniRule annotation
    Short name:
    p67eIF2UniRule annotation
    Peptidase MUniRule annotation
    Gene namesi
    Name:Metap2
    Synonyms:Mnpep, P67eif2
    OrganismiRattus norvegicus (Rat)
    Taxonomic identifieri10116 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeRattus
    ProteomesiUP000002494: Unplaced

    Organism-specific databases

    RGDi70995. Metap2.

    Subcellular locationi

    Cytoplasm
    Note: About 30% of expressed METAP2 associates with polysomes.UniRule annotation

    GO - Cellular componenti

    1. cytoplasm Source: HGNC

    Keywords - Cellular componenti

    Cytoplasm

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Initiator methioninei1 – 11RemovedBy similarity
    Chaini2 – 478477Methionine aminopeptidase 2PRO_0000148984Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei2 – 21N-acetylalanineBy similarity
    Modified residuei60 – 601Phosphoserine; alternateBy similarity
    Glycosylationi60 – 601O-linked (GlcNAc); alternate1 Publication
    Modified residuei63 – 631Phosphoserine; alternateBy similarity
    Glycosylationi63 – 631O-linked (GlcNAc); alternate1 Publication

    Post-translational modificationi

    O-glycosylated; contains 12 O-linked GlcNAc.1 Publication
    Contains approximately 12 O-linked N-acetylglucosamine (GlcNAc) residues. O-glycosylation is required for EIF2S1 binding.UniRule annotation

    Keywords - PTMi

    Acetylation, Glycoprotein, Phosphoprotein

    Proteomic databases

    PaxDbiP38062.
    PRIDEiP38062.

    Expressioni

    Inductioni

    Heat shock increases expression by more than 36-fold.1 Publication

    Gene expression databases

    GenevestigatoriP38062.

    Interactioni

    Subunit structurei

    Binds EIF2S1 at low magnesium concentrations By similarity. Interacts strongly with the eIF-2 gamma-subunit EIF2S3.1 PublicationUniRule annotation

    Protein-protein interaction databases

    STRINGi10116.ENSRNOP00000032680.

    Structurei

    3D structure databases

    ProteinModelPortaliP38062.
    SMRiP38062. Positions 110-478.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Compositional bias

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Compositional biasi36 – 10671Lys-richAdd
    BLAST

    Sequence similaritiesi

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

    Phylogenomic databases

    eggNOGiCOG0024.
    HOGENOMiHOG000226278.
    HOVERGENiHBG050495.
    KOiK01265.
    PhylomeDBiP38062.

    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]
    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.

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

    P38062-1 [UniParc]FASTAAdd to Basket

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    MAGVEEASSF GGHLNRDLDP DDREEGTSST AEEAAKKKRR KKKKGKGAVS    50
    AGQQELDKES GTSVDEVAKQ LERQALEEKE KDDDDEDGDG DGDGAAGKKK 100
    KKKKKKRGPR VQTDPPSVPI CDLYPNGVFP KGQECEYPPT QDGRTAAWRT 150
    TSEEKKALDQ ASEEIWNDFR EAAEAHRQVR KYVMSWIKPG MTMIEICEKL 200
    EDCSRKLIKE NGLNAGLAFP TGCSLNNCAA HYTPNAGDTT VLQYDDICKI 250
    DFGTHISGRI IDCAFTVTFN PKYDILLKAV KDATNTGIKC AGIDVRLCDV 300
    GEAIQEVMES YEVEIDGKTY QVKPIRNLNG HSIGPYRIHA GKTVPIVKGG 350
    EATRMEEGEV YAIETFGSTG KGVVHDDMEC SHYMKNFDVG HVPIRLPRTK 400
    HLLNVINENF GTLAFCRRWL DRLGESKYLM ALKNLCDLGI VDPYPPLCDI 450
    KGSYTAQFEH TILLRPTCKE VVSRGDDY 478
    Length:478
    Mass (Da):53,052
    Last modified:October 1, 1996 - v2
    Checksum:iBE1C0E91E0CB3D74
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti464 – 47815LRPTC…RGDDY → CAQPVKKLSAEEMTIKT in AAA41111. (PubMed:8496145)CuratedAdd
    BLAST

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    L10652 mRNA. Translation: AAA41111.1.
    PIRiA46702.
    RefSeqiNP_071984.1. NM_022539.1.
    UniGeneiRn.1984.

    Genome annotation databases

    GeneIDi64370.
    KEGGirno:64370.
    UCSCiRGD:70995. rat.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    L10652 mRNA. Translation: AAA41111.1 .
    PIRi A46702.
    RefSeqi NP_071984.1. NM_022539.1.
    UniGenei Rn.1984.

    3D structure databases

    ProteinModelPortali P38062.
    SMRi P38062. Positions 110-478.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    STRINGi 10116.ENSRNOP00000032680.

    Protein family/group databases

    MEROPSi M24.002.

    Proteomic databases

    PaxDbi P38062.
    PRIDEi P38062.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    GeneIDi 64370.
    KEGGi rno:64370.
    UCSCi RGD:70995. rat.

    Organism-specific databases

    CTDi 10988.
    RGDi 70995. Metap2.

    Phylogenomic databases

    eggNOGi COG0024.
    HOGENOMi HOG000226278.
    HOVERGENi HBG050495.
    KOi K01265.
    PhylomeDBi P38062.

    Enzyme and pathway databases

    BRENDAi 3.4.11.18. 5301.

    Miscellaneous databases

    NextBioi 613106.
    PROi P38062.

    Gene expression databases

    Genevestigatori P38062.

    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 ]
    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. "Cloning and characterization of complementary DNA encoding the eukaryotic initiation factor 2-associated 67-kDa protein (p67)."
      Wu S., Gupta S., Chatterjee N., Hileman R.E., Kinzy T.G., Denslow N.D., Merrick W.C., Chakrabarti D., Osterman J.C., Gupta N.K.
      J. Biol. Chem. 268:10796-10801(1993) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA].
      Strain: Reuber H35.
      Tissue: Liver.
    2. "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: SEQUENCE REVISION TO C-TERMINUS.
    3. Cited for: INDUCTION BY HEAT SHOCK.
    4. "A glycosylation site, 60SGTS63, of p67 is required for its ability to regulate the phosphorylation and activity of eukaryotic initiation factor 2alpha."
      Datta R., Choudhury P., Ghosh A., Datta B.
      Biochemistry 42:5453-5460(2003) [PubMed] [Europe PMC] [Abstract]
      Cited for: GLYCOSYLATION AT SER-60 AND SER-63.
    5. "The N-terminal lysine residue-rich domain II and the 340-430 amino acid segment of eukaryotic initiation factor 2-associated glycoprotein p67 are the binding sites for the gamma-subunit of eIF2."
      Ghosh A., Datta R., Majumdar A., Bhattacharya M., Datta B.
      Exp. Cell Res. 312:3184-3203(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH EIF2S3.

    Entry informationi

    Entry nameiMAP2_RAT
    AccessioniPrimary (citable) accession number: P38062
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: October 1, 1994
    Last sequence update: October 1, 1996
    Last modified: October 1, 2014
    This is version 122 of the entry and version 2 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programChordata Protein Annotation Program

    Miscellaneousi

    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

    External Data

    Dasty 3