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0KU70_HUMAN*   SwissProt (?) | Description Local Annotation Link Reference
General Information
NameG22P1
DescriptionAtp-dependent dna helicase ii, 70 kda subunit (lupus ku autoantigen protein p70) (ku70) (70 kda subunit of ku antigen) (thyroid-lupus autoantigen) (tlaa) (ctc box binding factor 75 kda subunit) (ctcbf) (ctc75).
SpeciesHomo sapiens (NCBI taxonomy ID: 9606)
GO0005624 membrane fraction (TAS)
0005634 nucleus (TAS)
0005667 transcription factor complex (IDA)
0004003 ATP-dependent DNA helicase activity (TAS)
0003690 double-stranded DNA binding (TAS)
0005515 protein binding (IPI)
0006266 DNA ligation (TAS)
0006303 double-strand break repair via nonhomologou... (TAS)
0045893 positive regulation of transcription, DNA-d... (IDA)

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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:
The Ku heterodimer (composed of Ku70 and Ku80 ) contributes to genomic integrity through its ability to bind DNA double-strand breaks and facilitate repair by the non-homologous end-joining pathway. This is the N-terminal alpha/beta domain. This domain only makes a small contribution to the dimer interface. The domain comprises a six stranded beta sheet of the Rossman fold .
  IPR005161:Ku70/Ku80, N-terminal alpha/beta
The Ku heterodimer is composed of Ku70 and Ku80 (or Ku86).0 kDa and 80 kDa subunits of an ATP-dependent DNA helicase.hich contributes to genomic integrity through its ability to bind DNA double-stranded breaks and facilitate repair by the non-homologous end-joining pathway. This is the central DNA-binding beta-barrel domain and is found in both the Ku70 and Ku80 proteins. Ku makes only a few contacts with the sugar-phosphate backbone.nd none with the DNA bases.ut it fits sterically to major and minor groove contours forming a ring that encircles duplex DNA.radling two full turns of the DNA molecule. By forming a bridge between the broken DNA ends.u acts to structurally support and align the DNA ends.o protect them from degradation.nd to prevent promiscuous binding to unbroken DNA. Ku effectively aligns the DNA.hile still allowing access of polymerases.ucleases and ligases to the broken DNA ends to promote end joining .
  IPR006164:Ku
The Ku heterodimer (composed of Ku70 and Ku80 ) contributes to genomic integrity through its ability to bind DNA double-strand breaks and facilitate repair by the non-homologous end-joining pathway. This is the C-terminal arm. This alpha helical region embraces the beta-barrel domain of the opposite subunit .
  IPR005160:Ku70/Ku80 C-terminal arm
The SAP (after SAF-A/B.cinus and PIAS) motif is a putativeDNA binding domain found in diverse nuclear proteins involved in chromosomal organization .
  IPR003034:DNA-binding SAP
Members are primarily Ku70 domain-containing proteins. Ku70 is a eukaryotic domain that is involved in the repair of DNA double-strand breaks by non-homologous end-joining . Ku is a heterodimer of approximately 70 kDa and 80 kDa subunits . Both these subunits have strong sequence similarity and it has been suggested that they may have evolved by gene duplication from a homodimeric ancestor in eukaryotes . Homologs of the eukaryotic DNA-end-binding protein Ku were identified in several bacterial and one archaeal genome using iterative database searches; these prokaryotic Ku members are homodimers that have been predicted to be involved in the DNA repair system.hich is mechanistically similar to eukaryotic non-homologous end joining .hough they are not members of this family. Recent findings have implicated yeast Ku in telomeric structure maintenance in addition to non-homologous end-joining. Some of the phenotypes of Ku-knockout mice may indicate a similar role for Ku at mammalian telomeres .Evolutionary notes: With the current available phyletic information it is difficult to determine the correct evolutionary trajectory of the Ku domain. It is possible that the core Ku domain was present in bacteria and archaea even before the presence of the eukaryotes. Eukaryotes might have vertically inherited the Ku core protein from a common ancestor shared with a certain archaeal lineage.r through horizontal transfer from bacteria. Alternatively.he core Ku domain could have evolved in the eukaryotic lineage and then horizontally transferred to the prokaryotes. Sequencing of additional archaeal genomes and those of early-branching eukaryotes may help resolve the evolutionary history of the Ku domain. Structure notes: The eukaryotic Ku heterodimer is comprised of an alpha/beta N-terminal. central beta-barrel domain and a helical C-terminal arm . Structural analysis of the Ku70/80 heterodimer bound to DNA indicates that subunit contacts lead to the formation of a highly charged channel through which the DNA passes without making any contacts with the DNA bases .For additional information please see .
  IPR006165:ATP-dependent DNA helicase, 70 kDa subunit
IPR005161:Ku_N 
Evalue:-97.6989669799805 
Location:36-255IPR006164:Ku 
Evalue:-87.5376052856445 
Location:260-467IPR005160:Ku_C 
Evalue:-39.7212448120117 
Location:470-558IPR003034:SAP 
Evalue:-8.65757751464844 
Location:572-606
SequencesProtein: KU70_HUMAN (608 aa)
mRNA: NM_001469
Local Annotation
Synapse Ontology
the formation of new synapse
sdb:0316 synapse formation  (Evidence:keywords)
KO assignmentNot mapped to KEGG
Loci Structure (Details)Loci index, Chromosomal location, Length, Possible relational loci clusterExon1: 19 residues, 40347240-40347295Exon2: 34 residues, 40347939-40348036Exon3: 39 residues, 40354067-40354180Exon4: 48 residues, 40362062-40362201Exon5: 87 residues, 40362465-40362720Exon6: 63 residues, 40363557-40363741Exon7: 64 residues, 40372845-40373032Exon8: 58 residues, 40376672-40376841Exon9: 56 residues, 40379478-40379640Exon10: 45 residues, 40382852-40382982Exon11: 35 residues, 40384201-40384302Exon12: 40 residues, 40387280-40387394Exon13: 144 residues, 40389571-40389998Exon14: 2 residues, -Jump to KU70_HUMAN  
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