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0SATB2_HUMAN*   SwissProt (?) | Description Local Annotation Link Reference
General Information
NameSATB2
DescriptionDna-binding protein satb2 (special at-rich sequence-binding protein 2).
SpeciesHomo sapiens (NCBI taxonomy ID: 9606)
GON/A
Domain Architecture (Details)
InterPro domains unassigned to SynO:
A class.lso called ONECUT.f homeodomain proteins. The CUT domain is a DNA-binding motif which can bind independently or in cooperation with the homeodomain ().ften found downstream of the CUT domain. Proteins display two modes of DNA binding.hich hinge on the homeodomain and on the linker that separates it from the cut domain.nd two modes of transcriptional stimulation.hich hinge on the homeodomain .
  IPR003350:Homeodomain protein CUT
The homeobox domain was first identified in a number of drosophila homeotic and segmentation proteins.ut is now known to be well-conserved in many other animals.ncluding vertebrates . Hox genes encode homeodomain-containing transcriptional regulators that operate differential genetic programs along the anterior-posterior axis of animal bodies . The domain binds DNA through a helix-turn-helix (HTH) structure. The HTH motif is characterised by two alpha-helices.hich make intimate contacts with the DNA and are joined by a short turn. The second helix binds to DNA via a number of hydrogen bonds and hydrophobic interactions.hich occur between specific side chains and the exposed bases and thymine methyl groups within the major groove of the DNA . The first helix helps to stabilise the structure. The motif is very similar in sequence and structure in a wide range of DNA-binding proteins (e.g..ro and repressor proteins.omeotic proteins.tc.). One of the principal differences between HTH motifs in these different proteins arises from the stereo-chemical requirement for glycine in the turn which is needed to avoid steric interference of the beta-carbon with the main chain: for cro and repressor proteins the glycine appears to be mandatory.hile for many of the homeotic and other DNA-binding proteins the requirement is relaxed.
  IPR001356:Homeobox
Homeodomain proteins are transcription factors that share a related DNA binding homeodomain . The homeodomain was first identified in a number of Drosophila homeotic and segmentation proteins.ut is now known to be well conserved in many other animals.ncluding vertebrates. The domain binds DNA through a helix-turn-helix (HTH) structure. The HTH motif is characterised by two alpha-helices.hich make intimate contacts with the DNA and are joined by a short turn. The second helix binds to DNA via a number of hydrogen bonds and hydrophobic interactions.hich occur between specific side chains and the exposed bases and thymine methyl groups within the major groove of the DNA. The first helix helps to stabilise the structure. Many proteins contain homeodomains.ncluding Drosophila Engrailed.east mating type proteins.epatocyte nuclear factor 1a and HOX proteins.The homeodomain motif is very similar in sequence and structure to domains in a wide range of DNA-binding proteins.ncluding recombinases.yb proteins.ARP response regulators.uman telomeric proteins (hTRF1).aired domain proteins (PAX).east RAP1.entromere-binding proteins CENP-B and ABP-1.ranscriptional regulators (TyrR).raC-type transcriptional activators.nd tetracycline repressor-like proteins (TetR.acR.cdC) .
  IPR009057:Homeodomain-like
Homeodomain proteins are transcription factors that share a related DNA binding homeodomain . The homeodomain was first identified in a number of Drosophila homeotic and segmentation proteins.ut is now known to be well conserved in many other animals.ncluding vertebrates. The domain binds DNA through a helix-turn-helix (HTH) structure. The HTH motif is characterised by two alpha helices.hich make intimate contacts with the DNA and are joined by a short turn. The second helix binds to DNA via a number of hydrogen bonds and hydrophobic interactions.hich occur between specific side chains and the exposed bases and thymine methyl groups within the major groove of the DNA. The first helix helps to stabilise the structure. Many proteins contain homeodomains.ncluding Drosophila Engrailed.east mating type proteins.epatocyte nuclear factor 1a and HOX proteins.The homeodomain motif is very similar in sequence and structure to domains in a wide range of DNA-binding proteins.ncluding recombinases.yb proteins.ARP response regulators.uman telomeric proteins (hTRF1).aired domain proteins (PAX).east RAP1.entromere-binding proteins CENP-B and ABP-1.ranscriptional regulators (TyrR).raC-type transcriptional activators.nd tetracycline repressor-like proteins (TetR.acR.cdC) .
  IPR012287:Homeodomain-related
IPR003350:CUT 
Evalue:-36.8538703918457 
Location:355-437IPR003350:CUT 
Evalue:-31.4317989349365 
Location:473-560IPR001356:HOX 
Evalue:-6.95860731484177 
Location:614-677IPR001356:HOMEOBOX_1 
Evalue:0 
Location:0-0
SequencesProtein: SATB2_HUMAN (733 aa)
mRNA: NM_015265
Local Annotation
Synapse Ontology
?
sdb:0265 cAMP mediated STP  (Evidence:keywords)
KO assignmentNot mapped to KEGG
Loci Structure (Details)Loci index, Chromosomal location, Length, Possible relational loci clusterExon1: 1058 residues, 199842468-199845640Exon2: 68 residues, 199881727-199881925Exon3: 54 residues, 199896770-199896926Exon4: 73 residues, 199901665-199901878Exon5: 159 residues, 199921668-199922141Exon6: 36 residues, 199941572-199941675Exon7: 43 residues, 199953331-199953455Exon8: 44 residues, 199954661-199954788Exon9: 61 residues, 200006305-200006482Exon10: 78 residues, 200028836-200029064Exon11: 11 residues, 200033419-200033446Exon12: 2 residues, -Jump to SATB2_HUMAN  
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