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0BAZ2B_HUMAN*   SwissProt (?) | Description Local Annotation Link Reference
General Information
DescriptionBromodomain adjacent to zinc finger domain 2b (hwalp4).
SpeciesHomo sapiens (NCBI taxonomy ID: 9606)
Domain Architecture (Details)
InterPro domains unassigned to SynO:
Bromodomains are found in a variety of mammalian.nvertebrate and yeast DNA-binding proteins . Bromodomains can interact withacetylated lysine .In some proteins.he classical bromodomain has diverged to such an extent that parts of the region are either missing or contain an insertion (e.g..ammalian protein HRX.aenorhabditis elegans hypothetical protein ZK783.4.east protein YTA7). The bromodomain may occur as a single copy.r in duplicate. The precise function of the domain is unclear.ut it may be involved in protein-protein interactions and may play a role in assembly or activity of multi-component complexes involved in transcriptional activation .
Methylation at CpG dinucleotide.he most common DNA modification been correlated with gene silencing associated with variousphenomena such as genomic imprinting.ransposon and chromosome Xinactivation.ifferenciation.nd cancer. Effects of DNA methylation aremediated through proteins which bind to symmetrically methylated CpGs. Suchproteins contain a specific domain of ~70 residues.he methyl-CpG-bindingdomain (MBD).hich is linked to additional domains associated with chromatin.uch as the bromodomain.he AT hook motif.he SET domain.r the PHD finger. MBD-containingproteins appear to act as structural proteins.hich recruit a variety ofhistone deacetylase (HDAC) complexes and chromatin remodeling factors.eadingto chromatin compaction and.onsequently.o transcriptional repression. TheMBD of MeCP2.BD1.BD2.BD4 and BAZ2 mediates binding to DNA.n case ofMeCP2.BD1 and MBD2 preferentially to methylated CpG. In case of human MBD3and SETDB1 the MBD has been shown to mediate protein-protein interactions.The MBD folds into an alpha/beta sandwich structure comprising a layer oftwisted beta sheet.acked by another layer formed by the alpha1 helix and ahairpin loop at the C terminus. These layers are bothamphipathic.ith the alpha1 helix and the beta sheet lying parallel and thehydrophobic faces tighly packed against each other. The beta sheet is composedof two long inner strands (beta2 and beta3) sandwiched by two shorter outerstrands (beta1 and beta4) .
  IPR001739:Methyl-CpG binding
The homeodomain (PHD) finger .s a C4HC3 zinc-finger-like motif found in nuclear proteins thought to be involved in chromatin-mediated transcriptional regulation. The PHD finger motif is reminiscent of.ut distinct from the C3HC4 type RING finger.The function of this domain is not yet known but in analogy with the LIM domain it could be involved in protein-protein interaction and be important for the assembly or activity of multicomponent complexes involved in transcriptional activation or repression. Alternatively.he interactions could be intra-molecular and be important in maintaining the structural integrity of the protein. In similarity to the RING finger and the LIM domain.he PHD finger is thought to bind two zinc ions.
  IPR001965:Zinc finger, PHD-type
This domain is predicted to be a DNA binding domain. The DDT domain is named after (DNA binding homeobox and Different Transcription factors). It is found in fetal Alzheimer antigen and several hypothetical and uncharacterised proteins.
SequencesProtein: BAZ2B_HUMAN (1972 aa)
mRNA: NM_013450
Local Annotation
Synapse Ontology
Calcium release from RyR (Ryanodine Receptor) in the SR (Sarcoplasmic Reticulum) is activated by the calcium induced-calcium-release
sdb:0325 RyR-CICR  (Evidence:keywords)
KO assignmentNot mapped to KEGG
Loci Structure (Details)Loci index, Chromosomal location, Length, Possible relational loci clusterExon1: 480 residues, 159883737-159885175Exon2: 50 residues, 159889567-159889711Exon3: 90 residues, 159890409-159890675Exon4: 51 residues, 159897296-159897443Exon5: 47 residues, 159901698-159901834Exon6: 70 residues, 159902323-159902529Exon7: 55 residues, 159912242-159912403Exon8: 54 residues, 159913434-159913590Exon9: 93 residues, 159913763-159914037Exon10: 218 residues, 159914464-159915114Exon11: 50 residues, 159937801-159937946Exon12: 23 residues, 159939447-159939510Exon13: 83 residues, 159947315-159947559Exon14: 27 residues, 159948362-159948437Exon15: 73 residues, 159949911-159950126Exon16: 87 residues, 159951109-159951364Exon17: 49 residues, 159954101-159954242Exon18: 24 residues, 159960525-159960591Exon19: 17 residues, 159962101-159962146Exon20: 24 residues, 159963585-159963651Exon21: 24 residues, 159965355-159965421Exon22: 22 residues, 159969605-159969667Exon23: 33 residues, 159969778-159969871Exon24: 72 residues, 159977091-159977302Exon25: 36 residues, 159992697-159992799Exon26: 38 residues, 159993067-159993176Exon27: 22 residues, 159993956-159994017Exon28: 100 residues, 159995619-159995913Exon29: 204 residues, 159997513-159998120Exon30: 133 residues, 160003059-160003452Exon31: 70 residues, 160003765-160003969Exon32: 67 residues, 160011538-160011735Exon33: 2 residues, -Jump to BAZ2B_HUMAN  
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