Conclusion
Assessment
Binding Mode
Motif Status
Notes
Comments
Likely to be sequence specific TF
3 Low specificity DNA-binding protein
No motif
Description
Description:
SET domain bifurcated 2 [Source:HGNC Symbol;Acc:HGNC:20263]
Entrez Summary
TBA
Ensembl ID:
ENSG00000136169
External Link:
T113540_1.02
Interpro
IPR001214 ; IPR001739 ; IPR003606 ; IPR007728 ; IPR016177 ; ;
Protein Domain:
Protein: ENSP00000326477DBD: Methyl-CpG DNA-bindingOther: Pre-SET, SETProtein: ENSP00000346175DBD: Methyl-CpG DNA-bindingOther: Pre-SET, SETProtein: ENSP00000258672DBD: Methyl-CpG DNA-bindingOther: Pre-SET, SETProtein: ENSP00000482240DBD: Methyl-CpG DNA-bindingOther: Pre-SET, SET
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.
x
CisBP considers it as a TF?
Yes
TFclass considers it as a TF?
No
Has GO:0003700 "transcription factor activity, sequence-specific DNA binding"
No
GO-Info
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
4a, two or more datasets predict it as a TF
TF has conditional DNA-binding requirements
DNA-Binding
Published Motif Data
Structure
Experimental History
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{"regions": [{"startStyle": "curved", "end": 232, "endStyle": "curved", "aliStart": 163, "text": "MBD", "colour": "#2cb42c", "aliEnd": 228, "start": 160, "href": "http://pfam.xfam.org/family/PF01429.17", "type": "pfama", "display": "true", "metadata": {"end": 232, "description": "The Methyl-CpG binding domain (MBD) binds to DNA that contains one or more symmetrically methylated CpGs [1]. DNA methylation in animals is associated with alterations in chromatin structure and silencing of gene expression. MBD has negligible non-specific affinity for DNA. In vitro foot-printing with MeCP2 showed the MBD can protect a 12 nucleotide region surrounding a methyl CpG pair [1]. MBDs are found in several Methyl-CpG binding proteins and also DNA demethylase [2].", "database": "PfamA", "aliStart": 163, "scoreName": "E-value", "accession": "PF01429.17", "start": 160, "score": 5.2e-08, "identifier": "Methyl-CpG binding domain", "type": "DBD", "aliEnd": 228}}, {"startStyle": "straight", "end": 694, "endStyle": "straight", "aliStart": 378, "text": "SET", "colour": "#9999ff", "aliEnd": 694, "start": 378, "href": "http://pfam.xfam.org/family/PF00856.26", "type": "pfama", "display": "true", "metadata": {"end": 694, "description": "SET domains are protein lysine methyltransferase enzymes. SET domains appear to be protein-protein interaction domains. It has been demonstrated that SET domains mediate interactions with a family of proteins that display similarity with dual-specificity phosphatases (dsPTPases) [2]. A subset of SET domains have been called PR domains. These domains are divergent in sequence from other SET domains, but also appear to mediate protein-protein interaction [3]. The SET domain consists of two regions known as SET-N and SET-C. SET-C forms an unusual and conserved knot-like structure of probably functional importance. Additionally to SET-N and SET-C, an insert region (SET-I) and flanking regions of high structural variability form part of the overall structure [5].", "database": "PfamA", "aliStart": 378, "scoreName": "E-value", "accession": "PF00856.26", "start": 378, "score": 2.2e-21, "identifier": "SET domain", "type": "DBD", "aliEnd": 694}}, {"startStyle": "straight", "end": 359, "endStyle": "straight", "aliStart": 246, "text": "Pre-SET", "colour": "#9999ff", "aliEnd": 359, "start": 246, "href": "http://pfam.xfam.org/family/PF05033.14", "type": "pfama", "display": "true", "metadata": {"end": 359, "description": "This protein motif is a zinc binding motif [1]. It contains 9 conserved cysteines that coordinate three zinc ions. It is thought that this region plays a structural role in stabilising SET domains.", "database": "PfamA", "aliStart": 246, "scoreName": "E-value", "accession": "PF05033.14", "start": 246, "score": 2.2e-15, "identifier": "Pre-SET motif", "type": "DBD", "aliEnd": 359}}], "length": 720}
{"regions": [{"startStyle": "curved", "end": 220, "endStyle": "curved", "aliStart": 151, "text": "MBD", "colour": "#2cb42c", "aliEnd": 216, "start": 148, "href": "http://pfam.xfam.org/family/PF01429.17", "type": "pfama", "display": "true", "metadata": {"end": 220, "description": "The Methyl-CpG binding domain (MBD) binds to DNA that contains one or more symmetrically methylated CpGs [1]. DNA methylation in animals is associated with alterations in chromatin structure and silencing of gene expression. MBD has negligible non-specific affinity for DNA. In vitro foot-printing with MeCP2 showed the MBD can protect a 12 nucleotide region surrounding a methyl CpG pair [1]. MBDs are found in several Methyl-CpG binding proteins and also DNA demethylase [2].", "database": "PfamA", "aliStart": 151, "scoreName": "E-value", "accession": "PF01429.17", "start": 148, "score": 3.4e-08, "identifier": "Methyl-CpG binding domain", "type": "DBD", "aliEnd": 216}}, {"startStyle": "straight", "end": 347, "endStyle": "straight", "aliStart": 234, "text": "Pre-SET", "colour": "#9999ff", "aliEnd": 347, "start": 234, "href": "http://pfam.xfam.org/family/PF05033.14", "type": "pfama", "display": "true", "metadata": {"end": 347, "description": "This protein motif is a zinc binding motif [1]. It contains 9 conserved cysteines that coordinate three zinc ions. It is thought that this region plays a structural role in stabilising SET domains.", "database": "PfamA", "aliStart": 234, "scoreName": "E-value", "accession": "PF05033.14", "start": 234, "score": 1.4e-15, "identifier": "Pre-SET motif", "type": "DBD", "aliEnd": 347}}, {"startStyle": "straight", "end": 507, "endStyle": "jagged", "aliStart": 366, "text": "SET", "colour": "#9999ff", "aliEnd": 427, "start": 366, "href": "http://pfam.xfam.org/family/PF00856.26", "type": "pfama", "display": "true", "metadata": {"end": 507, "description": "SET domains are protein lysine methyltransferase enzymes. SET domains appear to be protein-protein interaction domains. It has been demonstrated that SET domains mediate interactions with a family of proteins that display similarity with dual-specificity phosphatases (dsPTPases) [2]. A subset of SET domains have been called PR domains. These domains are divergent in sequence from other SET domains, but also appear to mediate protein-protein interaction [3]. The SET domain consists of two regions known as SET-N and SET-C. SET-C forms an unusual and conserved knot-like structure of probably functional importance. Additionally to SET-N and SET-C, an insert region (SET-I) and flanking regions of high structural variability form part of the overall structure [5].", "database": "PfamA", "aliStart": 366, "scoreName": "E-value", "accession": "PF00856.26", "start": 366, "score": 3.6e-05, "identifier": "SET domain", "type": "DBD", "aliEnd": 427}}], "length": 549}
{"regions": [{"startStyle": "curved", "end": 232, "endStyle": "curved", "aliStart": 163, "text": "MBD", "colour": "#2cb42c", "aliEnd": 228, "start": 160, "href": "http://pfam.xfam.org/family/PF01429.17", "type": "pfama", "display": "true", "metadata": {"end": 232, "description": "The Methyl-CpG binding domain (MBD) binds to DNA that contains one or more symmetrically methylated CpGs [1]. DNA methylation in animals is associated with alterations in chromatin structure and silencing of gene expression. MBD has negligible non-specific affinity for DNA. In vitro foot-printing with MeCP2 showed the MBD can protect a 12 nucleotide region surrounding a methyl CpG pair [1]. MBDs are found in several Methyl-CpG binding proteins and also DNA demethylase [2].", "database": "PfamA", "aliStart": 163, "scoreName": "E-value", "accession": "PF01429.17", "start": 160, "score": 5.2e-08, "identifier": "Methyl-CpG binding domain", "type": "DBD", "aliEnd": 228}}, {"startStyle": "straight", "end": 694, "endStyle": "straight", "aliStart": 378, "text": "SET", "colour": "#9999ff", "aliEnd": 694, "start": 378, "href": "http://pfam.xfam.org/family/PF00856.26", "type": "pfama", "display": "true", "metadata": {"end": 694, "description": "SET domains are protein lysine methyltransferase enzymes. SET domains appear to be protein-protein interaction domains. It has been demonstrated that SET domains mediate interactions with a family of proteins that display similarity with dual-specificity phosphatases (dsPTPases) [2]. A subset of SET domains have been called PR domains. These domains are divergent in sequence from other SET domains, but also appear to mediate protein-protein interaction [3]. The SET domain consists of two regions known as SET-N and SET-C. SET-C forms an unusual and conserved knot-like structure of probably functional importance. Additionally to SET-N and SET-C, an insert region (SET-I) and flanking regions of high structural variability form part of the overall structure [5].", "database": "PfamA", "aliStart": 378, "scoreName": "E-value", "accession": "PF00856.26", "start": 378, "score": 2.2e-21, "identifier": "SET domain", "type": "DBD", "aliEnd": 694}}, {"startStyle": "straight", "end": 359, "endStyle": "straight", "aliStart": 246, "text": "Pre-SET", "colour": "#9999ff", "aliEnd": 359, "start": 246, "href": "http://pfam.xfam.org/family/PF05033.14", "type": "pfama", "display": "true", "metadata": {"end": 359, "description": "This protein motif is a zinc binding motif [1]. It contains 9 conserved cysteines that coordinate three zinc ions. It is thought that this region plays a structural role in stabilising SET domains.", "database": "PfamA", "aliStart": 246, "scoreName": "E-value", "accession": "PF05033.14", "start": 246, "score": 2.2e-15, "identifier": "Pre-SET motif", "type": "DBD", "aliEnd": 359}}], "length": 720}