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0AMPB_HUMAN*   SwissProt (?) | Description Local Annotation Link Reference
General Information
DescriptionAminopeptidase b (ec (ap-b) (arginyl aminopeptidase) (arginine aminopeptidase).
SpeciesHomo sapiens (NCBI taxonomy ID: 9606)
GO0005576 extracellular region (TAS)
0005794 Golgi apparatus (ISS)
0005886 plasma membrane (TAS)
0030601 aminopeptidase B activity (NAS)
0004301 epoxide hydrolase activity (NAS)
0008235 metalloexopeptidase activity (NAS)
0008270 zinc ion binding (NAS)
0016485 protein processing (ISS)
0006508 proteolysis and peptidolysis (IC)

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schematic display of those terms with internal associations, click the node and browse the corresponding GO term
Domain Architecture (Details)
InterPro domains unassigned to SynO:
Metalloproteases are the most diverse of the four main types of protease.ith more than 30 families identified to date . In these enzymes. divalent cation.sually zinc.ctivates the water molecule. The metal ion is held in place by amino acid ligands.sually three in number. The known metal ligands are or Lys and at least one other residue is required for catalysis.hich may play an electrophillic role. Of the known metalloproteases.round half contain an HEXXH motif.hich has been shown in crystallographic studies to form part of the metal-binding site . The HEXXH motif is relatively common.ut can be more stringently defined for metalloproteases as a is most often valine or threonine and forms part of the S1 subsite in thermolysin and neprilysin. is an uncharged residue.nd c a hydrophobic residue. Proline is never found in this site.ossibly because it would break the helical structure adopted by this motif in metalloproteases .Peptidases are grouped into clans and families. Clans are groups of families for which there is evidence of common ancestry. Families are grouped by their catalytic type.he first character representing the catalytic type: A.spartic; C.ysteine; G.lutamic acid; M.etallo; S.erine; T.hreonine; and U.nknown. A clan that contains families of more than one type is described as being of type P. The serine.hreonine and cysteine peptidases utilise the catalytic part of an amino acid as a nucleophile and form an acyl intermediate - these peptidases can also readily act as transferases. In the case of aspartic.lutamic and metallopeptidases.he nucleophile is an activated water molecule. This group of metallopeptidases belong to the MEROPS peptidase family M1 (clan MA(E)).he type example being aminopeptidase N from Homo sapiens. The protein fold of the peptidase domain for members of this family resembles that of thermolysin.he type example for clan MA.Membrane alanine aminopeptidase () is part of the HEXXH+Egroup; it consists entirely of aminopeptidases.pread across a widevariety of species . Functional studies show that CD13/APN catalyzes the removal of single amino acids from the amino terminus of small peptides and probably plays a role in their final digestion; one family member (leukotriene-A4 hydrolase) is known to hydrolyse the epoxide leukotriene-A4to form an inflammatory mediator . This hydrolase has been shown tohave aminopeptidase activity .nd the zinc ligands of the M1 familywere identified by site-directed mutagenesis on this enzyme CD13 participates in trimming peptides bound to MHC class II molecules and cleaves MIP-1 chemokine.hich alters target cell specificity from basophils to eosinophils . CD13 acts as a receptor for specific strains of RNA viruses (coronaviruses) which cause a relatively large percentage of upper respiratory trace infections.CD molecules are leucocyte antigens on cell surfaces. CD antigens nomenclature is updated at
  IPR001930:Peptidase M1, membrane alanine aminopeptidase
SequencesProtein: AMPB_HUMAN (650 aa)
mRNA: NM_020216
Local Annotation
Synapse Ontology
the generation of action potential at soma of neurons.
sdb:0313 generation of AP at soma  (Evidence:keywords)
KO assignmentK01260
  Level 3 annotation:
    aminopeptidase B
  Level 2 annotation:
    Other amino acid metabolism
Loci Structure (Details)Loci index, Chromosomal location, Length, Possible relational loci clusterExon1: 159 residues, 200218388-200218864Exon2: 49 residues, 200224654-200224795Exon3: 51 residues, 200225133-200225282Exon4: 41 residues, 200231897-200232014Exon5: 80 residues, 200233069-200233305Exon6: 40 residues, 200235652-200235766Exon7: 39 residues, 200237126-200237239Exon8: 38 residues, 200237409-200237518Exon9: 77 residues, 200238987-200239212Exon10: 49 residues, 200240104-200240247Exon11: 198 residues, 200241308-200241897Exon12: 2 residues, -Jump to AMPB_HUMAN  
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Loci Cluster (Details)Loci: 2581 200218388-200241897 ~-24K 3661(RNPEP)(+)Loci: 2580 200191270-200206410 ~-15K 3660(TIMM17A)(+)Link out to UCSC