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0ANTR2_HUMAN*   SwissProt (?) | Description Local Annotation Link Reference
General Information
NameANTXR2
DescriptionAnthrax toxin receptor 2 precursor (capillary morphogenesis gene 2 protein) (cmg-2).
SpeciesHomo sapiens (NCBI taxonomy ID: 9606)
GO0005515 protein binding (IPI)
Domain Architecture (Details)
InterPro domains unassigned to SynO:
This region is found in the putatively extracellular N-terminal half of the anthrax receptor. It is probably part of the Ig superfamily and most closely related to .
  IPR008400:Anthrax receptor extracellular
This region is found in the putatively cytoplasmic C terminus of the anthrax receptor.
  IPR008399:Anthrax receptor, C-terminal
The von Willebrand factor is a large multimeric glycoprotein found in bloodplasma. Mutant forms are involved in the aetiology of bleeding disorders . In von Willebrand factor.he type A domain (vWF) is the prototype fora protein superfamily. The vWF domain is found in various plasma proteins:complement factors B.2.R3 and CR4; the integrins (I-domains); collagen types VI.II.II and XIV; and other extracellular proteins . Although the majority of VWA-containing proteins are extracellular.he most ancient ones present in all eukaryotes are all intracellular proteins involved in functions such as transcription.NA repair.ibosomal and membrane transport and the proteasome. A common feature appears to be involvement in multiprotein complexes. Proteinsthat incorporate vWF domains participate in numerous biological events(e.g. cell adhesion.igration.oming.attern formation.nd signaltransduction).nvolving interaction with a large array of ligands . A number of human diseases arise from mutations in VWA domains. Secondary structure prediction from 75 aligned vWF sequences has revealed a largely alternating sequence of alpha-helices and beta-strands . Foldrecognition algorithms were used to score sequence compatibility with alibrary of known structures: the vWF domain fold was predicted to be adoubly-wound.pen.wisted beta-sheet flanked by alpha-helices . 3D structures have been determined for the I-domains of integrins CD11b(with bound magnesium) and CD11a (with bound manganese) . The domain adopts a classic alpha/beta Rossmann fold and contains an unusual metal ion coordination site at its surface. It has been suggested that this siterepresents a general metal ion-dependent adhesion site (MIDAS) for binding protein ligands . The residues constituting the MIDAS motif in the CD11band CD11a I-domains are completely conserved.ut the manner in which the metal ion is coordinated differs slightly .
  IPR002035:von Willebrand factor, type A
IPR008400:Anth_Ig 
Evalue:-76.259635925293 
Location:214-318IPR008399:Ant_C 
Evalue:-49.0087738037109 
Location:394-486IPR002035:VWA 
Evalue:-23.7447280883789 
Location:44-213
SequencesProtein: ANTR2_HUMAN (489 aa)
mRNA: NM_058172
Local Annotation
Synapse Ontology
endocytosis may be initiated or blocked by all kinds of signal.
sdb:0257 regulation of endocytosis  (Evidence:keywords)
KO assignmentNot mapped to KEGG
Loci Structure (Details)Loci index, Chromosomal location, Length, Possible relational loci clusterExon1: 633 residues, 81045748-81047645Exon2: 29 residues, 81117798-81117879Exon3: 58 residues, 81118184-81118352Exon4: 33 residues, 81124055-81124148Exon5: 17 residues, 81124996-81125041Exon6: 34 residues, 81148698-81148794Exon7: 28 residues, 81159075-81159154Exon8: 25 residues, 81171800-81171870Exon9: 35 residues, 81173649-81173748Exon10: 22 residues, 81176149-81176210Exon11: 29 residues, 81194449-81194530Exon12: 25 residues, 81195327-81195396Exon13: 38 residues, 81195537-81195645Exon14: 29 residues, 81196109-81196191Exon15: 26 residues, 81209613-81209685Exon16: 26 residues, 81211760-81211832Exon17: 232 residues, 81212586-81213277Exon18: 2 residues, -Jump to ANTR2_HUMAN  
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Loci Cluster (Details)Loci: 3417 81337681-81344499 ~-7K 27804(PRDM8)(+)Loci: 4679 81045748-81213277 ~-168K 27801(ANTXR2)(-)Link out to UCSC