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Q3ZC89

- MAP2_BOVIN

UniProt

Q3ZC89 - MAP2_BOVIN

Protein

Methionine aminopeptidase 2

Gene

METAP2

Organism
Bos taurus (Bovine)
Status
Reviewed - Annotation score: 4 out of 5- Experimental evidence at transcript leveli
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    • History
      Entry version 71 (01 Oct 2014)
      Sequence version 1 (27 Sep 2005)
      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).UniRule annotation
    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.UniRule annotation

    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 sitei230 – 2301SubstrateUniRule annotation
    Metal bindingi250 – 2501Divalent metal cation 1UniRule annotation
    Metal bindingi261 – 2611Divalent metal cation 1UniRule annotation
    Metal bindingi261 – 2611Divalent metal cation 2; catalyticUniRule annotation
    Metal bindingi330 – 3301Divalent metal cation 2; catalytic; via tele nitrogenUniRule annotation
    Binding sitei338 – 3381SubstrateUniRule annotation
    Metal bindingi363 – 3631Divalent metal cation 2; catalyticUniRule annotation
    Metal bindingi458 – 4581Divalent metal cation 1UniRule annotation
    Metal bindingi458 – 4581Divalent metal cation 2; catalyticUniRule annotation

    GO - Molecular functioni

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

    GO - Biological processi

    1. protein initiator methionine removal Source: UniProtKB-HAMAP

    Keywords - Molecular functioni

    Aminopeptidase, Hydrolase, Protease

    Keywords - Ligandi

    Metal-binding

    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:METAP2UniRule annotation
    OrganismiBos taurus (Bovine)
    Taxonomic identifieri9913 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaLaurasiatheriaCetartiodactylaRuminantiaPecoraBovidaeBovinaeBos
    ProteomesiUP000009136: Unplaced

    Subcellular locationi

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

    GO - Cellular componenti

    1. cytoplasm Source: UniProtKB-SubCell

    Keywords - Cellular componenti

    Cytoplasm

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Initiator methioninei1 – 11RemovedBy similarity
    Chaini2 – 477476Methionine aminopeptidase 2PRO_0000246091Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei2 – 21N-acetylalanineBy similarity
    Modified residuei45 – 451PhosphoserineBy similarity
    Modified residuei62 – 621Phosphoserine; alternateBy similarity
    Glycosylationi62 – 621O-linked (GlcNAc); alternateBy similarity

    Post-translational modificationi

    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

    PaxDbiQ3ZC89.
    PRIDEiQ3ZC89.

    Interactioni

    Subunit structurei

    Binds EIF2S1 at low magnesium concentrations. Interacts strongly with the eIF-2 gamma-subunit EIF2S3.UniRule annotation

    Protein-protein interaction databases

    STRINGi9913.ENSBTAP00000026568.

    Structurei

    3D structure databases

    ProteinModelPortaliQ3ZC89.
    SMRiQ3ZC89. Positions 109-477.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Compositional bias

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Compositional biasi36 – 10974Lys-richAdd
    BLAST

    Sequence similaritiesi

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

    Phylogenomic databases

    eggNOGiCOG0024.
    HOGENOMiHOG000226278.
    HOVERGENiHBG050495.
    InParanoidiQ3ZC89.
    KOiK01265.

    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.

    Q3ZC89-1 [UniParc]FASTAAdd to Basket

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    MAGVEEAASC GSHLNGDLDP DEREEGAAST AEEAAKKKKR KKKKSKGAAT    50
    GQQEPDKEAG ASVDEVTRQL ERQALEEKEK DDDDEDGDGD GDGATGKKKK 100
    KKKKKRGPKV QTDPPSVPIC DLYPNGVFPK GQECEYPPTQ DGRTAAWRTT 150
    SEEKKALDQA SEEIWNDFRE AAEAHRQVRK YVMSWIKPGM TMIEICEKME 200
    DCSRKLIKEN GLNAGLAFPT GCSLNNCAAH YTPNAGDTTV LQYDDICKID 250
    FGTHISGRII DCAFTVTFNP KYDTLLKAVK DATNTGIKCA GIDVRLCDVG 300
    EAIQEVMESY EVEIDGKTYQ VKPIRNLNGH SIGPYRIHAG KTVPIVKGGE 350
    ATRMEEGEVY AIETFGSTGK GVVHDDMECS HYMKNFDVGH VPIRLPRTKH 400
    LLNVINENFG TLAFCRRWLD RLGESKYLMA LKNLCDLGIV DPYPPLCDIK 450
    GSYTAQFEHT ILLRPTCKEV VSRGDDY 477
    Length:477
    Mass (Da):52,812
    Last modified:September 27, 2005 - v1
    Checksum:i4D10309613D2F0F1
    GO

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    BC102824 mRNA. Translation: AAI02825.1.
    RefSeqiNP_001035583.1. NM_001040493.1.
    UniGeneiBt.49424.

    Genome annotation databases

    GeneIDi404150.
    KEGGibta:404150.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    BC102824 mRNA. Translation: AAI02825.1 .
    RefSeqi NP_001035583.1. NM_001040493.1.
    UniGenei Bt.49424.

    3D structure databases

    ProteinModelPortali Q3ZC89.
    SMRi Q3ZC89. Positions 109-477.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    STRINGi 9913.ENSBTAP00000026568.

    Protein family/group databases

    MEROPSi M24.002.

    Proteomic databases

    PaxDbi Q3ZC89.
    PRIDEi Q3ZC89.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    GeneIDi 404150.
    KEGGi bta:404150.

    Organism-specific databases

    CTDi 10988.

    Phylogenomic databases

    eggNOGi COG0024.
    HOGENOMi HOG000226278.
    HOVERGENi HBG050495.
    InParanoidi Q3ZC89.
    KOi K01265.

    Miscellaneous databases

    NextBioi 20817584.

    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. NIH - Mammalian Gene Collection (MGC) project
      Submitted (AUG-2005) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
      Strain: Crossbred X Angus.
      Tissue: Ileum.

    Entry informationi

    Entry nameiMAP2_BOVIN
    AccessioniPrimary (citable) accession number: Q3ZC89
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: July 11, 2006
    Last sequence update: September 27, 2005
    Last modified: October 1, 2014
    This is version 71 of the entry and version 1 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