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0APBP2_HUMAN*   SwissProt (?) | Description Local Annotation Link Reference
General Information
NameAPPBP2
DescriptionAmyloid protein-binding protein 2 (amyloid beta precursor protein- binding protein 2) (app-bp2) (protein interacting with app tail 1).
SpeciesHomo sapiens (NCBI taxonomy ID: 9606)
GO0005737 cytoplasm (NAS)
0005875 microtubule associated complex (TAS)
0005634 nucleus (NAS)
0003777 microtubule motor activity (TAS)
0006886 intracellular protein transport (TAS)

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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:
Protein prenyltransferases catalyze the transfer of the carbon moiety of C15 farnesyl pyrophosphate or geranylgeranyl pyrophosphate synthase to a conserved cysteine residue in a CaaX motif of protein and peptide substrates. The addition of a farnesyl group is required to anchor proteins to the cell membrane. In the 3D structure of a mammalian Ras farnesyltransferases (Ftase).oth subunits are largely composed of alpha-helices. The alpha-2 to alpha-15 helices in the alpha subunit fold into a novel helical hairpin structure.esulting in a crescent-shape domain that envelopes part of the subunit. The 12 helices of the beta-subunit form an alpha-alpha barrel. Six additional helices connect the inner core of helices and form the outside of the helical barrel. A deep cleft surrounded by hydrophobic amino acids in the centre of the barrel is proposed as the FPP-binding pocket. A single Zn2+ ion is located at the junction between the hydrophilic surface groove near the subunit interface. The SSF signature in this entry is currently under review. Please be aware that some of the protein hits may be false positives.
  IPR008940:Protein prenyltransferase
This domain consists of a multi-helical fold comprised of two curved layers of alpha helices arranged in a regular right-handed superhelix.here the repeats that make up this structure are arranged about a common axis . These superhelical structures present an extensive solvent-accessible surface that is well suited to binding large substrates such as proteins and nucleic acids. This topology has been found with a number of repeats and domains.ncluding the tetratricopeptide repeat (TPR) (found in kinesin light chains.NAP regulatory proteins.lathrin heavy chains and bacterial aspartyl-phosphate phosphatases).nd the pentatricopeptide repeat (PPR) (RNA-processing proteins). The TRP is likely to be an ancient repeat.ince it is found in eukaryotes.acteria and archaea.hereas the PPR repeat is found predominantly in higher plants. The superhelix formed from these repeats can bind ligands at a number of different regions.nd has the ability to acquire multiple functional roles .
  IPR011990:Tetratricopeptide-like helical
IPR011990:TPR-like_helical 
Evalue:0 
Location:201-504IPR008940:Prenyl_trans 
Evalue:0 
Location:55-74IPR008940:Prenyl_trans 
Evalue:0 
Location:15-27
SequencesProtein: APBP2_HUMAN (585 aa)
mRNA: NM_006380
Local Annotation
Synapse Ontology
microtubules of the presynaptic compartment function as the tracks for the intense traffic of organelles from cell body to axon terminals and vice versa. It is generally excluded from the presynaptic vesicle cluster.Microtubules do not directly regulate synapse morphology or function
sdb:0087 microtubules  (Evidence:keywords)
KO assignmentNot mapped to KEGG
Loci Structure (Details)Loci index, Chromosomal location, Length, Possible relational loci clusterExon1: 1559 residues, 55875301-55879977Exon2: 57 residues, 55884022-55884188Exon3: 65 residues, 55886444-55886635Exon4: 30 residues, 55888438-55888524Exon5: 43 residues, 55892805-55892930Exon6: 37 residues, 55893952-55894058Exon7: 24 residues, 55894136-55894204Exon8: 32 residues, 55896163-55896253Exon9: 58 residues, 55898433-55898602Exon10: 43 residues, 55911290-55911414Exon11: 52 residues, 55926608-55926760Exon12: 31 residues, 55932541-55932630Exon13: 144 residues, 55957936-55958362Exon14: 2 residues, -Jump to APBP2_HUMAN  
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