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0LHX5_HUMAN*   SwissProt (?) | Description Local Annotation Link Reference
General Information
NameLHX5
DescriptionLim/homeobox protein lhx5.
SpeciesHomo sapiens (NCBI taxonomy ID: 9606)
GO0005634 nucleus (ISS)
0003677 DNA binding (ISS)
0007417 central nervous system development (ISS)

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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:
Helix-turn-helix (HTH) motifs are found in all known DNA binding proteinsthat regulate gene expression. The motif consists of approximately 20 residues and is characterised by 2 alpha-helices.hich make intimate contacts with the DNA and are joined by a short turn. The second helix of the HTH motif 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 . Thefirst helix helps to stabilise the structure . The HTH motif is very similar in sequence and structure to the N-terminal region of the lamda and other repressor proteins.nd has also been identified in many other DNA-binding proteins on the basis of sequence and structural similarity . One of the principal differences between HTH motifs in these different proteins arises from the stereochemical requirement for glycine in the turn.hich is needed to avoid steric interference of the beta-carbon with the main chain: for cro and other repressors the Gly appears to be mandatory.hile for many of the homeoticand other DNA-binding proteins the requirement is relaxed.
  IPR000047:Helix-turn-helix motif, lambda-like repressor
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
Recently . number of proteins have been found to contain a conserved cysteine-rich domain of about 60 amino-acid residues. These proteins are:Caenorhabditis elegans mec-3; a protein required for the differentiation of the set of six touch receptor neurons in this nematode.C. elegans. lin-11; a protein required for the asymmetric division of vulval blast cells.Vertebrate insulin gene enhancer binding protein isl-1. Isl-1 binds to one of the two cis-acting protein-binding domains of the insulin gene.Vertebrate homeobox proteins lim-1.im-2 (lim-5) and lim3.Vertebrate lmx-1.hich acts as a transcriptional activator by binding to the FLAT element; a beta-cell-specific transcriptional enhancer found in the insulin gene.Mammalian LH-2. transcriptional regulatory protein involved in the control of cell differentiation in developing lymphoid and neural cell types.Drosophila melanogaster protein apterous.equired for the normal development of the wing and halter imaginal discs.Vertebrate protein kinases LIMK-1 and LIMK-2.Mammalian rhombotins. Rhombotin 1 (RBTN1 or TTG-1) and rhombotin-2 (RBTN2 or TTG-2) are proteins of about 160 amino acids whose genes are disrupted by chromosomal translocations in T-cell leukemia.Mammalian and avian cysteine-rich protein (CRP). 192 amino-acid protein of unknown function. Seems to interact with zyxin.Mammalian cysteine-rich intestinal protein (CRIP). small protein which seems to have a role in zinc absorption and may function as an intracellular zinc transport protein.Vertebrate paxillin. cytoskeletal focal adhesion protein.Mouse testin which should not be confused with rat testin which is a thiol protease homolog (see ).Sunflower pollen specific protein SF3.Chicken zyxin. Zyxin is a low-abundance adhesion plaque protein which has been shown to interact with CRP.Yeast protein LRG1 which is involved in sporulation .Yeast rho-type GTPase activating protein RGA1/DBM1.C. elegans homeobox protein ceh-14.C. elegans homeobox protein unc-97.Yeast hypothetical protein YKR090w.C. elegans hypothetical proteins C28H8.6.These proteins generally have two tandem copies of a domain.alled LIM (for Lin-11 Isl-1 Mec-3) in their N-terminal section. Zyxin and paxillin are exceptions in that they contains respectively three and four LIM domains at their C-terminal extremity. In apterous.sl-1.H-2.in-11.im-1 to lim-3.mx-1 and ceh-14 and mec-3 there is a homeobox domain some 50 to 95 amino acids after the LIM domains.In the LIM domain.here are seven conserved cysteine residues and a histidine. The arrangement followed by these conserved residues is C-x(2)-C-x(16.3)-H-x(2)-[CH]-x(2)-C-x(2)-C-x(16.1)-C-x(2.)-[CHD]. The LIM domain binds two zinc ions . LIM does not bind DNA.ather it seems to act as an interface for protein-protein interaction.
  IPR001781:LIM, zinc-binding
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
IPR001356:Homeobox 
Evalue:-25.2757244110107 
Location:181-237IPR001781:LIM 
Evalue:-25.1023731231689 
Location:5-61IPR001781:LIM 
Evalue:-24.2518119812012 
Location:64-124
SequencesProtein: LHX5_HUMAN (402 aa)
mRNA: NM_022363
Local Annotation
Synapse Ontology
introduce the substructure of the synapse and the location where the molecule can be seen. It will contain all the constructive special organelle and molecule we known.
sdb:0001 Structure/Biochemistry of synapse  (Evidence:keywords)
KO assignmentNot mapped to KEGG
Loci Structure (Details)Loci index, Chromosomal location, Length, Possible relational loci clusterExon1: 224 residues, 112385076-112385745Exon2: 57 residues, 112389443-112389609Exon3: 94 residues, 112390314-112390592Exon4: 76 residues, 112391309-112391533Exon5: 251 residues, 112393513-112394260Exon6: 2 residues, -Jump to LHX5_HUMAN  
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