Conclusion
Assessment
Binding Mode
Motif Status
Notes
Comments
Known motif
1 Monomer or homomultimer
High-throughput in vitro
This protein contains C2H2 ZFs missed by Pfam scanning.
Description
Description:
double PHD fingers 1 [Source:HGNC Symbol;Acc:HGNC:20225]
Entrez Summary
TBA
Ensembl ID:
ENSG00000011332
External Link:
Interpro
IPR001965 ; IPR007087 ; IPR011011 ; IPR015880 ; IPR019787 ; IPR025750 ;
Protein Domain:
Protein: ENSP00000347716DBD: OtherOther: PHD, Requiem_NProtein: ENSP00000412098DBD: OtherOther: PHD, Requiem_NProtein: ENSP00000397354DBD: OtherOther: PHD, Requiem_NProtein: ENSP00000483226DBD: OtherOther: PHD, Requiem_NProtein: ENSP00000391884DBD: OtherOther: PHD, Requiem_N
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.
b
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
1a1, Direct HQ evidence
TF has conditional DNA-binding requirements
DNA-Binding
Published Motif Data
Structure
Experimental History
{"regions": [{"startStyle": "straight", "end": 110, "endStyle": "straight", "aliStart": 40, "text": "Requiem_N", "colour": "#9999ff", "aliEnd": 110, "start": 39, "href": "http://pfam.xfam.org/family/PF14051.4", "type": "pfama", "display": "true", "metadata": {"end": 110, "description": "This putative domain has been detected on the human DPF2 protein and was subsequently targeted for structure determination by the Joint Center for Structural Genomics (JCSG). Possibly, the C-terminus extends by 30 amino acids and forms a separate domain. DPF2 interacts with estrogen related receptor alpha (Err-alpha), an orphan receptor which acts as a regulator in energy metabolism [1]. It was also identified as an adaptor molecule that links nuclear factor kappa-light-chain-enhancer of activated B cells (NF-kappa-B) dimer RelB/p52 and switch/sucrose-nonfermentable (SWI/SNF) chromatin remodeling factor [2].", "database": "PfamA", "aliStart": 40, "scoreName": "E-value", "accession": "PF14051.4", "start": 39, "score": 1.6999999999999998e-36, "identifier": "N-terminal domain of DPF2/REQ.", "type": "DBD", "aliEnd": 110}}, {"startStyle": "straight", "end": 355, "endStyle": "straight", "aliStart": 300, "text": "PHD", "colour": "#9999ff", "aliEnd": 355, "start": 300, "href": "http://pfam.xfam.org/family/PF00628.27", "type": "pfama", "display": "true", "metadata": {"end": 355, "description": "PHD folds into an interleaved type of Zn-finger chelating 2 Zn ions in a similar manner to that of the RING and FYVE domains [2]. Several PHD fingers have been identified as binding modules of methylated histone H3 [3].", "database": "PfamA", "aliStart": 300, "scoreName": "E-value", "accession": "PF00628.27", "start": 300, "score": 9.699999999999999e-22, "identifier": "PHD-finger", "type": "DBD", "aliEnd": 355}}, {"startStyle": "straight", "end": 402, "endStyle": "straight", "aliStart": 355, "text": "PHD", "colour": "#9999ff", "aliEnd": 400, "start": 354, "href": "http://pfam.xfam.org/family/PF00628.27", "type": "pfama", "display": "true", "metadata": {"end": 402, "description": "PHD folds into an interleaved type of Zn-finger chelating 2 Zn ions in a similar manner to that of the RING and FYVE domains [2]. Several PHD fingers have been identified as binding modules of methylated histone H3 [3].", "database": "PfamA", "aliStart": 355, "scoreName": "E-value", "accession": "PF00628.27", "start": 354, "score": 9.699999999999999e-22, "identifier": "PHD-finger", "type": "DBD", "aliEnd": 400}}], "length": 415}
{"regions": [{"startStyle": "straight", "end": 273, "endStyle": "straight", "aliStart": 218, "text": "PHD", "colour": "#9999ff", "aliEnd": 273, "start": 218, "href": "http://pfam.xfam.org/family/PF00628.27", "type": "pfama", "display": "true", "metadata": {"end": 273, "description": "PHD folds into an interleaved type of Zn-finger chelating 2 Zn ions in a similar manner to that of the RING and FYVE domains [2]. Several PHD fingers have been identified as binding modules of methylated histone H3 [3].", "database": "PfamA", "aliStart": 218, "scoreName": "E-value", "accession": "PF00628.27", "start": 218, "score": 4.2000000000000006e-22, "identifier": "PHD-finger", "type": "DBD", "aliEnd": 273}}, {"startStyle": "straight", "end": 320, "endStyle": "straight", "aliStart": 273, "text": "PHD", "colour": "#9999ff", "aliEnd": 318, "start": 272, "href": "http://pfam.xfam.org/family/PF00628.27", "type": "pfama", "display": "true", "metadata": {"end": 320, "description": "PHD folds into an interleaved type of Zn-finger chelating 2 Zn ions in a similar manner to that of the RING and FYVE domains [2]. Several PHD fingers have been identified as binding modules of methylated histone H3 [3].", "database": "PfamA", "aliStart": 273, "scoreName": "E-value", "accession": "PF00628.27", "start": 272, "score": 4.2000000000000006e-22, "identifier": "PHD-finger", "type": "DBD", "aliEnd": 318}}, {"startStyle": "jagged", "end": 28, "endStyle": "straight", "aliStart": 1, "text": "Requiem_N", "colour": "#9999ff", "aliEnd": 28, "start": 1, "href": "http://pfam.xfam.org/family/PF14051.4", "type": "pfama", "display": "true", "metadata": {"end": 28, "description": "This putative domain has been detected on the human DPF2 protein and was subsequently targeted for structure determination by the Joint Center for Structural Genomics (JCSG). Possibly, the C-terminus extends by 30 amino acids and forms a separate domain. DPF2 interacts with estrogen related receptor alpha (Err-alpha), an orphan receptor which acts as a regulator in energy metabolism [1]. It was also identified as an adaptor molecule that links nuclear factor kappa-light-chain-enhancer of activated B cells (NF-kappa-B) dimer RelB/p52 and switch/sucrose-nonfermentable (SWI/SNF) chromatin remodeling factor [2].", "database": "PfamA", "aliStart": 1, "scoreName": "E-value", "accession": "PF14051.4", "start": 1, "score": 5.0999999999999993e-08, "identifier": "N-terminal domain of DPF2/REQ.", "type": "DBD", "aliEnd": 28}}], "length": 333}
{"regions": [{"startStyle": "straight", "end": 110, "endStyle": "straight", "aliStart": 40, "text": "Requiem_N", "colour": "#9999ff", "aliEnd": 110, "start": 39, "href": "http://pfam.xfam.org/family/PF14051.4", "type": "pfama", "display": "true", "metadata": {"end": 110, "description": "This putative domain has been detected on the human DPF2 protein and was subsequently targeted for structure determination by the Joint Center for Structural Genomics (JCSG). Possibly, the C-terminus extends by 30 amino acids and forms a separate domain. DPF2 interacts with estrogen related receptor alpha (Err-alpha), an orphan receptor which acts as a regulator in energy metabolism [1]. It was also identified as an adaptor molecule that links nuclear factor kappa-light-chain-enhancer of activated B cells (NF-kappa-B) dimer RelB/p52 and switch/sucrose-nonfermentable (SWI/SNF) chromatin remodeling factor [2].", "database": "PfamA", "aliStart": 40, "scoreName": "E-value", "accession": "PF14051.4", "start": 39, "score": 1.6999999999999998e-36, "identifier": "N-terminal domain of DPF2/REQ.", "type": "DBD", "aliEnd": 110}}, {"startStyle": "straight", "end": 311, "endStyle": "straight", "aliStart": 256, "text": "PHD", "colour": "#9999ff", "aliEnd": 311, "start": 256, "href": "http://pfam.xfam.org/family/PF00628.27", "type": "pfama", "display": "true", "metadata": {"end": 311, "description": "PHD folds into an interleaved type of Zn-finger chelating 2 Zn ions in a similar manner to that of the RING and FYVE domains [2]. Several PHD fingers have been identified as binding modules of methylated histone H3 [3].", "database": "PfamA", "aliStart": 256, "scoreName": "E-value", "accession": "PF00628.27", "start": 256, "score": 5.4e-19, "identifier": "PHD-finger", "type": "DBD", "aliEnd": 311}}, {"startStyle": "straight", "end": 368, "endStyle": "straight", "aliStart": 311, "text": "PHD", "colour": "#9999ff", "aliEnd": 366, "start": 310, "href": "http://pfam.xfam.org/family/PF00628.27", "type": "pfama", "display": "true", "metadata": {"end": 368, "description": "PHD folds into an interleaved type of Zn-finger chelating 2 Zn ions in a similar manner to that of the RING and FYVE domains [2]. Several PHD fingers have been identified as binding modules of methylated histone H3 [3].", "database": "PfamA", "aliStart": 311, "scoreName": "E-value", "accession": "PF00628.27", "start": 310, "score": 5.4e-19, "identifier": "PHD-finger", "type": "DBD", "aliEnd": 366}}], "length": 381}
{"regions": [{"startStyle": "straight", "end": 83, "endStyle": "straight", "aliStart": 13, "text": "Requiem_N", "colour": "#9999ff", "aliEnd": 83, "start": 12, "href": "http://pfam.xfam.org/family/PF14051.4", "type": "pfama", "display": "true", "metadata": {"end": 83, "description": "This putative domain has been detected on the human DPF2 protein and was subsequently targeted for structure determination by the Joint Center for Structural Genomics (JCSG). Possibly, the C-terminus extends by 30 amino acids and forms a separate domain. DPF2 interacts with estrogen related receptor alpha (Err-alpha), an orphan receptor which acts as a regulator in energy metabolism [1]. It was also identified as an adaptor molecule that links nuclear factor kappa-light-chain-enhancer of activated B cells (NF-kappa-B) dimer RelB/p52 and switch/sucrose-nonfermentable (SWI/SNF) chromatin remodeling factor [2].", "database": "PfamA", "aliStart": 13, "scoreName": "E-value", "accession": "PF14051.4", "start": 12, "score": 1.6e-36, "identifier": "N-terminal domain of DPF2/REQ.", "type": "DBD", "aliEnd": 83}}, {"startStyle": "straight", "end": 328, "endStyle": "straight", "aliStart": 273, "text": "PHD", "colour": "#9999ff", "aliEnd": 328, "start": 273, "href": "http://pfam.xfam.org/family/PF00628.27", "type": "pfama", "display": "true", "metadata": {"end": 328, "description": "PHD folds into an interleaved type of Zn-finger chelating 2 Zn ions in a similar manner to that of the RING and FYVE domains [2]. Several PHD fingers have been identified as binding modules of methylated histone H3 [3].", "database": "PfamA", "aliStart": 273, "scoreName": "E-value", "accession": "PF00628.27", "start": 273, "score": 2.7e-19, "identifier": "PHD-finger", "type": "DBD", "aliEnd": 328}}, {"startStyle": "straight", "end": 385, "endStyle": "straight", "aliStart": 328, "text": "PHD", "colour": "#9999ff", "aliEnd": 383, "start": 327, "href": "http://pfam.xfam.org/family/PF00628.27", "type": "pfama", "display": "true", "metadata": {"end": 385, "description": "PHD folds into an interleaved type of Zn-finger chelating 2 Zn ions in a similar manner to that of the RING and FYVE domains [2]. Several PHD fingers have been identified as binding modules of methylated histone H3 [3].", "database": "PfamA", "aliStart": 328, "scoreName": "E-value", "accession": "PF00628.27", "start": 327, "score": 2.7e-19, "identifier": "PHD-finger", "type": "DBD", "aliEnd": 383}}], "length": 398}
{"regions": [{"startStyle": "straight", "end": 273, "endStyle": "straight", "aliStart": 218, "text": "PHD", "colour": "#9999ff", "aliEnd": 273, "start": 218, "href": "http://pfam.xfam.org/family/PF00628.27", "type": "pfama", "display": "true", "metadata": {"end": 273, "description": "PHD folds into an interleaved type of Zn-finger chelating 2 Zn ions in a similar manner to that of the RING and FYVE domains [2]. Several PHD fingers have been identified as binding modules of methylated histone H3 [3].", "database": "PfamA", "aliStart": 218, "scoreName": "E-value", "accession": "PF00628.27", "start": 218, "score": 4.2000000000000006e-22, "identifier": "PHD-finger", "type": "DBD", "aliEnd": 273}}, {"startStyle": "straight", "end": 320, "endStyle": "straight", "aliStart": 273, "text": "PHD", "colour": "#9999ff", "aliEnd": 318, "start": 272, "href": "http://pfam.xfam.org/family/PF00628.27", "type": "pfama", "display": "true", "metadata": {"end": 320, "description": "PHD folds into an interleaved type of Zn-finger chelating 2 Zn ions in a similar manner to that of the RING and FYVE domains [2]. Several PHD fingers have been identified as binding modules of methylated histone H3 [3].", "database": "PfamA", "aliStart": 273, "scoreName": "E-value", "accession": "PF00628.27", "start": 272, "score": 4.2000000000000006e-22, "identifier": "PHD-finger", "type": "DBD", "aliEnd": 318}}, {"startStyle": "jagged", "end": 28, "endStyle": "straight", "aliStart": 1, "text": "Requiem_N", "colour": "#9999ff", "aliEnd": 28, "start": 1, "href": "http://pfam.xfam.org/family/PF14051.4", "type": "pfama", "display": "true", "metadata": {"end": 28, "description": "This putative domain has been detected on the human DPF2 protein and was subsequently targeted for structure determination by the Joint Center for Structural Genomics (JCSG). Possibly, the C-terminus extends by 30 amino acids and forms a separate domain. DPF2 interacts with estrogen related receptor alpha (Err-alpha), an orphan receptor which acts as a regulator in energy metabolism [1]. It was also identified as an adaptor molecule that links nuclear factor kappa-light-chain-enhancer of activated B cells (NF-kappa-B) dimer RelB/p52 and switch/sucrose-nonfermentable (SWI/SNF) chromatin remodeling factor [2].", "database": "PfamA", "aliStart": 1, "scoreName": "E-value", "accession": "PF14051.4", "start": 1, "score": 5.0999999999999993e-08, "identifier": "N-terminal domain of DPF2/REQ.", "type": "DBD", "aliEnd": 28}}], "length": 333}