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0PHAR3_HUMAN*   SwissProt (?) | Description Local Annotation Link Reference
General Information
NamePHACTR3
DescriptionPhosphatase and actin regulator 3 (scapinin) (scaffold-associated pp1 inhibiting protein).
SpeciesHomo sapiens (NCBI taxonomy ID: 9606)
GON/A
Domain Architecture (Details)
InterPro domains unassigned to SynO:
The RPEL repeat is named after four conserved amino acids it contains. The function of the RPEL repeat is unknown however it might be a DNA binding repeat based on the observation that Q9VZY2 contains a SAP domain that is also implicated in DNA binding.
  IPR004018:RPEL repeat
High mobility group (HMG) proteins are a family of relatively low molecular weight non-histone componentsin chromatin. HMG-I and HMG-Y are proteins of about 100 amino acid residues which are produced by thealternative splicing of a single gene. HMG-I proteins bind preferentially to the minor groove of AT-richregions in double-stranded DNA . It is suggested that these proteins could functionin nucleosome phasing and in the 3 end processing of mRNA transcripts. They are also involved in thetranscription regulation of genes containing.r in close proximity to.T-rich regions. DNA-binding of these.nd several related.roteins is effected by an 11-residue domain known as an AT-hook. Within known HMG-Iproteins are found three highly conserved regions.losely related to the consensus sequence TPKRPRGRPKK. Asynthetic oligopeptide with this sequence specifically binds to substrate DNA in a manner reminiscent ofintact HMG-I proteins. Structure predictions suggest that the peptide has a secondary structure similar tothe anti-tumour and anti-viral drugs netropsin and distamycin.nd to the dye Hoechst 33258. These ligands.hich also preferentially bind to AT-rich DNA.ffectively compete with both the synthetic peptide and theHMG-I proteins for DNA binding. The peptide also contains novel structural features such as a predicted Asxbend.r hook.t its N-terminus.nd laterally-projecting cationic Arg/Lys bristles.hich may play arole in the binding of HMG-I proteins. The predicted peptide structure.he AT-hook.s a previouslyundescribed DNA-binding motif .
  IPR000637:HMG-I and HMG-Y, DNA-binding
IPR004018:RPEL 
Evalue:-7.32790231704712 
Location:439-464IPR004018:RPEL 
Evalue:-5.01322826573375 
Location:477-502IPR004018:RPEL 
Evalue:-3.29242982390206 
Location:401-426IPR004018:RPEL 
Evalue:0 
Location:93-118IPR000637:ATHOOK 
Evalue:0 
Location:0-0
SequencesProtein: PHAR3_HUMAN (559 aa)
mRNA: NM_080672
Local Annotation
Synapse Ontology
intermediate filaments of the presynaptic compartments. Both microtubles and intermediate filaments represent the main structural scaffold of axons.
sdb:0086 intermediate filaments  (Evidence:keywords)
KO assignmentNot mapped to KEGG
Loci Structure (Details)Loci index, Chromosomal location, Length, Possible relational loci clusterExon1: 196 residues, 57612997-57613582Exon2: 56 residues, 57751556-57751718Exon3: 28 residues, 57756207-57756285Exon4: 63 residues, 57763631-57763814Exon5: 72 residues, 57775635-57775845Exon6: 60 residues, 57781728-57781903Exon7: 84 residues, 57782692-57782940Exon8: 53 residues, 57814490-57814644Exon9: 20 residues, 57844954-57845010Exon10: 22 residues, 57848818-57848880Exon11: 49 residues, 57849844-57849985Exon12: 27 residues, 57853638-57853715Exon13: 200 residues, 57855564-57856159Exon14: 2 residues, -Jump to PHAR3_HUMAN  
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