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The annotation and conditions in this rule are derived from the following entries: P50579 (MAP2_HUMAN), P38062 (MAP2_RAT), P38174 (MAP2_YEAST), Q8SR45 (MAP2_ENCCU)

If a protein meets these conditions... i

Common conditions

    • Matches HAMAP signature MF_03175
    • taxon = Eukaryota
    • fragment ≠ the sequence is fragmented

Special conditions

    • Subsequence at position 262 - 262 aligns to "D" in entry P50579 (individually applies "Divalent metal cation 1")
    • Subsequence at position 339 - 339 aligns to "H" in entry P50579 (individually applies "Substrate")
    • Subsequence at position 459 - 459 aligns to "E" in entry P50579 (individually applies "Divalent metal cation 1")
    • Subsequence at position 231 - 231 aligns to "H" in entry P50579 (individually applies "Substrate")
    • Subsequence at position 262 - 262 aligns to "D" in entry P50579 (individually applies "Divalent metal cation 2; catalytic")
    • Subsequence at position 459 - 459 aligns to "E" in entry P50579 (individually applies "Divalent metal cation 2; catalytic")
    • Subsequence at position 251 - 251 aligns to "D" in entry P50579 (individually applies "Divalent metal cation 1")
    • Subsequence at position 364 - 364 aligns to "E" in entry P50579 (individually applies "Divalent metal cation 2; catalytic")
    • Subsequence at position 331 - 331 aligns to "H" in entry P50579 (individually applies "Divalent metal cation 2; catalytic; via tele nitrogen")

... then these annotations are applied i

<p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">Names and taxonomy</a> section provides an exhaustive list of all names of the protein, from commonly used to obsolete, to allow unambiguous identification of a protein.<p><a href='/help/protein_names' target='_top'>More...</a></p>Protein namesi

  • Recommended name:
    Methionine aminopeptidase 2 (EC:3.4.11.18)
    Short name:
    MAP 2
    Short name:
    MetAP 2
    Alternative name(s):
    Peptidase M
  • Alternative name(s):
    Initiation factor 2-associated 67 kDa glycoprotein
    Short name:
    p67eIF2
    Short name:
    p67

<p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">Names and taxonomy</a> section indicates the name(s) of the gene(s) that code for the protein sequence(s) described in the entry. Four distinct tokens exist: 'Name', 'Synonyms', 'Ordered locus names' and 'ORF names'.<p><a href='/help/gene_name' target='_top'>More...</a></p>Gene namesi

  • Name:METAP2
  • Name:MAP2

<p>This subsection of the <a href="http://www.uniprot.org/help/interaction%5Fsection">'Interaction'</a> section provides information about the protein quaternary structure and interaction(s) with other proteins or protein complexes (with the exception of physiological receptor-ligand interactions which are annotated in the <a href="http://www.uniprot.org/help/function%5Fsection">'Function'</a> section).<p><a href='/help/subunit_structure' target='_top'>More...</a></p>Subunit structurei

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

<p>This subsection of the 'Function' section provides information relevant to cofactors. A cofactor is any non-protein substance required for a protein to be catalytically active. Some cofactors are inorganic, such as the metal atoms zinc, iron, and copper in various oxidation states. Others, such as most vitamins, are organic.<p><a href='/help/cofactor' target='_top'>More...</a></p>Cofactori

<p>This subsection of the <a href="http://www.uniprot.org/help/function%5Fsection">Function</a> section describes the catalytic activity of an enzyme, i.e. a chemical reaction that the enzyme catalyzes.<p><a href='/help/catalytic_activity' target='_top'>More...</a></p>Catalytic activityi

    • Release of N-terminal amino acids, preferentially methionine, from peptides and arylamides. EC:3.4.11.18

<p>This subsection of the <a href="http://www.uniprot.org/help/function%5Fsection">Function</a> describes the function(s) of a protein.<p><a href='/help/function' target='_top'>More...</a></p>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.

<p>This subsection of the 'Family and domains' section provides information about the sequence similarity with other proteins.<p><a href='/help/sequence_similarities' target='_top'>More...</a></p>Sequence similaritiesi

<p>This subsection of the <a href="http://www.uniprot.org/help/ptm%5Fprocessing%5Fsection">PTM/processing</a> section describes post-translational modifications (PTMs). This subsection <strong>complements</strong> the information provided at the sequence level or describes modifications for which <strong>position-specific data is not yet available</strong>.<p><a href='/help/post-translational_modification' target='_top'>More...</a></p>Post-translational modificationi

  • Contains approximately 12 O-linked N-acetylglucosamine (GlcNAc) residues. O-glycosylation is required for EIF2S1 binding.

<p>This section provides information on the location and the topology of the mature protein in the cell.<p><a href='/help/subcellular_location_section' target='_top'>More...</a></p>Subcellular locationi

<p>This subsection of the <a href="http://www.uniprot.org/help/function%5Fsection">Function</a> section indicates at which position the protein binds a given metal ion. The nature of the metal is indicated in the 'Description' field.<p><a href='/help/metal' target='_top'>More...</a></p>Metal bindingi

  • Divalent metal cation 1 (to residues corresponding to position 262)
  • Divalent metal cation 1 (to residues corresponding to position 459)
  • Divalent metal cation 2; catalytic (to residues corresponding to position 262)
  • Divalent metal cation 2; catalytic (to residues corresponding to position 459)
  • Divalent metal cation 1 (to residues corresponding to position 251)
  • Divalent metal cation 2; catalytic (to residues corresponding to position 364)
  • Divalent metal cation 2; catalytic; via tele nitrogen (to residues corresponding to position 331)

<p>This subsection of the <a href="http://www.uniprot.org/help/function%5Fsection">Function</a> section describes the interaction between a single amino acid and another chemical entity. Priority is given to the annotation of physiological ligands.<p><a href='/help/binding' target='_top'>More...</a></p>Binding sitei

  • Substrate (to residues corresponding to position 339)
  • Substrate (to residues corresponding to position 231)

<p>UniProtKB Keywords constitute a <a href="http://www.uniprot.org/keywords">controlled vocabulary</a> with a hierarchical structure. Keywords summarise the content of a UniProtKB entry and facilitate the search for proteins of interest.<p><a href='/help/keywords' target='_top'>More...</a></p>Keywordsi

<p>The <a href="http://www.geneontology.org/">Gene Ontology (GO)</a> project provides a set of hierarchical controlled vocabulary split into 3 categories:<p><a href='/help/gene_ontology' target='_top'>More...</a></p>GO (Gene Ontology) termsi

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