Conclusion
Assessment
Binding Mode
Motif Status
Notes
Comments
Known motif
1 Monomer or homomultimer
High-throughput in vitro
Description
Description:
zinc finger BED-type containing 1 [Source:HGNC Symbol;Acc:HGNC:447]
Entrez Summary
TBA
Ensembl ID:
ENSG00000214717
External Link:
T153714_1.02
Interpro
IPR003656 ; IPR008906 ; IPR012337 ; ;
Protein Domain:
Protein: ENSP00000370616DBD: BED ZFOther: DUF4413, Dimer_Tnp_hATProtein: ENSP00000370620DBD: BED ZFOther: DUF4413, Dimer_Tnp_hATProtein: ENSP00000370621DBD: BED ZFOther: DUF4413, Dimer_Tnp_hATProtein: ENSP00000419148DBD: BED ZFOther:
Previous Annotations
Source
Annotation
TF-CAT classification
No PMIDS:
Vaquerizas 2009 TF classification
"a " Has direct evidence of TF function;
"b " Has evidence for an orthologous TF;
"c " contains likely DBDs, but has no functional evidence;
"x " is an unlikely TF such as predicted gene, genes with likely non-specific DBDs or that have function outside transcription;
"other " category contains proteins without clear DBDs they curated from external sources.
a
CisBP considers it as a TF?
Yes
TFclass considers it as a TF?
Yes
Has GO:0003700 "transcription factor activity, sequence-specific DNA binding"
Yes
GO-Info
GO:0003700 sequence-specific DNA binding transcription factor activity IBA - GO_REF:0000033
Initial Assessment
1a1 Protein has a high confidence PWM (HT-SELEX, PBM or B1H model) or there is a crystal structure that supports sequence specific DNA binding;
1a2 There is high confidence data for a close ortholog (as defined in CisBP);
2a1 There is lower confidence direct evidence, such as a Jaspar, Hocomoco or Transfac model;
2a2 There is lower confidence evidence for an close ortholog;
3a There is decent circumstantial evidence for its role as a TF or not;
4a Two or more datasets predict it as a TF;
5a One of the source datasets predicts is as a TF
1a1, Direct HQ evidence
TF has conditional DNA-binding requirements
DNA-Binding
Published Motif Data
Structure
Experimental History
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{"regions": [{"startStyle": "curved", "end": 72, "endStyle": "curved", "aliStart": 23, "text": "zfBED", "colour": "#2cb42c", "aliEnd": 72, "start": 23, "href": "http://pfam.xfam.org/family/PF02892.13", "type": "pfama", "display": "true", "metadata": {"end": 72, "description": "The BED finger, which was named after the Drosophila proteins BEAF and DREF, is found in one or more copies in cellular regulatory factors and transposases from plants, animals and fungi. The BED finger is an about 50 to 60 amino acid residues domain that contains a characteristic motif with two highly conserved aromatic positions, as well as a shared pattern of cysteines and histidines that is predicted to form a zinc finger. As diverse BED fingers are able to bind DNA, it has been suggested that DNA-binding is the general function of this domain [PUBMED:10973053].", "database": "PfamA", "aliStart": 23, "scoreName": "E-value", "accession": "PF02892.13", "start": 23, "score": 1.5e-14, "identifier": "BED zinc finger", "type": "DBD", "aliEnd": 72}}, {"startStyle": "straight", "end": 651, "endStyle": "straight", "aliStart": 571, "text": "Dimer_Tnp_hAT", "colour": "#9999ff", "aliEnd": 650, "start": 571, "href": "http://pfam.xfam.org/family/PF05699.12", "type": "pfama", "display": "true", "metadata": {"end": 651, "description": "This dimerisation region is found at the C terminus of the transposases of elements belonging to the Activator superfamily (hAT element superfamily). The isolated dimerisation region forms extremely stable dimers in vitro [1].", "database": "PfamA", "aliStart": 571, "scoreName": "E-value", "accession": "PF05699.12", "start": 571, "score": 2.7e-15, "identifier": "hAT family C-terminal dimerisation region", "type": "DBD", "aliEnd": 650}}, {"startStyle": "straight", "end": 511, "endStyle": "jagged", "aliStart": 412, "text": "DUF4413", "colour": "#9999ff", "aliEnd": 499, "start": 412, "href": "http://pfam.xfam.org/family/PF14372.4", "type": "pfama", "display": "true", "metadata": {"end": 511, "description": "This domain is part of an RNase-H fold section of longer proteins some of which are transposable elements possibly of the Pong type, since some members are putative Tam3 transposases.", "database": "PfamA", "aliStart": 412, "scoreName": "E-value", "accession": "PF14372.4", "start": 412, "score": 3.7e-05, "identifier": "Domain of unknown function (DUF4413)", "type": "DBD", "aliEnd": 499}}], "length": 695}
{"regions": [{"startStyle": "curved", "end": 72, "endStyle": "curved", "aliStart": 23, "text": "zfBED", "colour": "#2cb42c", "aliEnd": 72, "start": 23, "href": "http://pfam.xfam.org/family/PF02892.13", "type": "pfama", "display": "true", "metadata": {"end": 72, "description": "The BED finger, which was named after the Drosophila proteins BEAF and DREF, is found in one or more copies in cellular regulatory factors and transposases from plants, animals and fungi. The BED finger is an about 50 to 60 amino acid residues domain that contains a characteristic motif with two highly conserved aromatic positions, as well as a shared pattern of cysteines and histidines that is predicted to form a zinc finger. As diverse BED fingers are able to bind DNA, it has been suggested that DNA-binding is the general function of this domain [PUBMED:10973053].", "database": "PfamA", "aliStart": 23, "scoreName": "E-value", "accession": "PF02892.13", "start": 23, "score": 1.5e-14, "identifier": "BED zinc finger", "type": "DBD", "aliEnd": 72}}, {"startStyle": "straight", "end": 651, "endStyle": "straight", "aliStart": 571, "text": "Dimer_Tnp_hAT", "colour": "#9999ff", "aliEnd": 650, "start": 571, "href": "http://pfam.xfam.org/family/PF05699.12", "type": "pfama", "display": "true", "metadata": {"end": 651, "description": "This dimerisation region is found at the C terminus of the transposases of elements belonging to the Activator superfamily (hAT element superfamily). The isolated dimerisation region forms extremely stable dimers in vitro [1].", "database": "PfamA", "aliStart": 571, "scoreName": "E-value", "accession": "PF05699.12", "start": 571, "score": 2.7e-15, "identifier": "hAT family C-terminal dimerisation region", "type": "DBD", "aliEnd": 650}}, {"startStyle": "straight", "end": 511, "endStyle": "jagged", "aliStart": 412, "text": "DUF4413", "colour": "#9999ff", "aliEnd": 499, "start": 412, "href": "http://pfam.xfam.org/family/PF14372.4", "type": "pfama", "display": "true", "metadata": {"end": 511, "description": "This domain is part of an RNase-H fold section of longer proteins some of which are transposable elements possibly of the Pong type, since some members are putative Tam3 transposases.", "database": "PfamA", "aliStart": 412, "scoreName": "E-value", "accession": "PF14372.4", "start": 412, "score": 3.7e-05, "identifier": "Domain of unknown function (DUF4413)", "type": "DBD", "aliEnd": 499}}], "length": 695}
{"regions": [{"startStyle": "curved", "end": 72, "endStyle": "curved", "aliStart": 23, "text": "zfBED", "colour": "#2cb42c", "aliEnd": 72, "start": 23, "href": "http://pfam.xfam.org/family/PF02892.13", "type": "pfama", "display": "true", "metadata": {"end": 72, "description": "The BED finger, which was named after the Drosophila proteins BEAF and DREF, is found in one or more copies in cellular regulatory factors and transposases from plants, animals and fungi. The BED finger is an about 50 to 60 amino acid residues domain that contains a characteristic motif with two highly conserved aromatic positions, as well as a shared pattern of cysteines and histidines that is predicted to form a zinc finger. As diverse BED fingers are able to bind DNA, it has been suggested that DNA-binding is the general function of this domain [PUBMED:10973053].", "database": "PfamA", "aliStart": 23, "scoreName": "E-value", "accession": "PF02892.13", "start": 23, "score": 4.2e-15, "identifier": "BED zinc finger", "type": "DBD", "aliEnd": 72}}], "length": 272}