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0BAZ2A_HUMAN*   SwissProt (?) | Description Local Annotation Link Reference
General Information
NameBAZ2A
DescriptionBromodomain adjacent to zinc finger domain 2a (transcription termination factor i-interacting protein 5) (ttf-i-interacting protein 5) (tip5) (hwalp3).
SpeciesHomo sapiens (NCBI taxonomy ID: 9606)
GO0005731 nucleolus organizer complex (NAS)
0003677 DNA binding (NAS)
0030528 transcription regulator activity (NAS)
0006338 chromatin remodeling (NAS)
0006355 regulation of transcription, DNA-dependent (NAS)

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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:
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 .
  IPR001487:Bromodomain
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.
  IPR004022:DDT
Methylation at CpG dinucleotide.he most common DNA modification ineukaryotes.as 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
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
Zinc finger domains (ZnFs) are common.elatively small protein motifs that fold around one or more zinc ions. In addition to their role as a DNA-binding module.nFs have recently been shown to mediate protein:protein and protein:lipid interactions. There are at least 14 different classes of Zn fingers.hich differ in the nature and arrangement of their zinc-binding residues .The FYVE zinc finger domain is conserved from yeast to man.nd is named after four proteins that it has been found in: Fab1.OTB/ZK632.12.ac1.nd EEA1. It functions in the membrane recruitment of cytosolic proteins by binding to phosphatidylinositol 3-phosphate (PI3P).hich is found mainly on endosomes .The plant homeodomain (PHD) zinc finger domain has a C4HC3-type motif.nd is widely distributed in eukaryotes.eing found in many chromatin regulatory factors .Both the FYVE and the PHD zinc finger motifs display strikingly similar dimetal(zinc)-bound alpha+beta folds.The SSF signature in this entry is currently under review. Please be aware that some of the protein hits may be false positives.
  IPR011011:Zinc finger, FYVE/PHD-type
IPR001487:BROMO 
Evalue:-42.8538703918457 
Location:1764-1872IPR001739:MBD 
Evalue:-36.8860549926758 
Location:522-597IPR004022:DDT 
Evalue:-27.9586067199707 
Location:821-883IPR001965:PHD 
Evalue:-16.508638381958 
Location:1651-1699IPR000637:AT_hook 
Evalue:-2.58502674102783 
Location:643-655IPR000637:AT_hook 
Evalue:-2.06550145149231 
Location:1159-1171IPR000637:AT_hook 
Evalue:-2 
Location:622-634IPR000637:AT_hook 
Evalue:-1.88605666160583 
Location:1377-1389IPR000637:ATHOOK 
Evalue:0 
Location:1328-1339IPR001965:ZF_PHD_1 
Evalue:0 
Location:0-0
SequencesProtein: BAZ2A_HUMAN (1878 aa)
mRNA: CR749379
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: 570 residues, 55275981-55277688Exon2: 380 residues, 55277698-55278834Exon3: 50 residues, 55278918-55279062Exon4: 78 residues, 55279179-55279409Exon5: 51 residues, 55279752-55279899Exon6: 46 residues, 55280014-55280147Exon7: 98 residues, 55280251-55280541Exon8: 52 residues, 55280731-55280883Exon9: 54 residues, 55280993-55281149Exon10: 76 residues, 55281230-55281453Exon11: 217 residues, 55281596-55282243Exon12: 50 residues, 55282763-55282908Exon13: 22 residues, 55283409-55283469Exon14: 62 residues, 55283570-55283751Exon15: 27 residues, 55284267-55284342Exon16: 73 residues, 55284635-55284850Exon17: 87 residues, 55285123-55285378Exon18: 80 residues, 55285880-55286114Exon19: 24 residues, 55286297-55286363Exon20: 35 residues, 55286683-55286784Exon21: 72 residues, 55289786-55289997Exon22: 36 residues, 55290164-55290266Exon23: 38 residues, 55290459-55290568Exon24: 22 residues, 55291623-55291684Exon25: 160 residues, 55291823-55292297Exon26: 75 residues, 55293065-55293284Exon27: 64 residues, 55294003-55294189Exon28: 200 residues, 55295064-55295658Exon29: 48 residues, 55297445-55297583Exon30: 68 residues, 55316232-55316430Exon31: 2 residues, -Jump to BAZ2A_HUMAN  
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Loci Cluster (Details)Loci: 2763 54396087-54399754 ~-4K 9024(BLOC1S1)(+)Loci: 2764 54423333-54430331 ~-7K 9030(GDF11)(+)Loci: 2765 54654128-54674745 ~-21K 9056(RAB5B)(+)Loci: 2766 54677309-54685574 ~-8K 9057(SUOX)(+)Loci: 2767 54798296-54802545 ~-4K 9067(+)Loci: 4051 54843395-54869544 ~-26K 9082(SMARCC2)(-)Loci: 4052 54951749-54980442 ~-29K 9095(CS)(-)Loci: 4053 55151003-55168448 ~-17K 9108(GLS2)(-)Loci: 4054 55275981-55316430 ~-40K 9114(BAZ2A)(-)Loci: 4055 55318225-55326119 ~-8K 9115(ATP5B)(-)Loci: 4056 55708568-55730160 ~-22K 9128(MYO1A)(-)Loci: 4050 54364622-54387894 ~-23K 9022(ITGA7)(-)Link out to UCSC