The Human Transcription Factors

Conclusion

Assessment	Binding Mode	Motif Status	Notes	Comments
Known motif	1 Monomer or homomultimer	High-throughput in vitro

Description

Description:	zinc finger protein 384 [Source:HGNC Symbol;Acc:HGNC:11955]
Entrez Summary	TBA
Ensembl ID:	ENSG00000126746
External Link:	T044332_1.02
Interpro	IPR007087; IPR015880;
Protein Domain:
Protein: ENSP00000348018	DBD: C2H2 ZF Containing Proteins	Other:
Protein: ENSP00000321650	DBD: C2H2 ZF Containing Proteins	Other:
Protein: ENSP00000380019	DBD: C2H2 ZF Containing Proteins	Other:
Protein: ENSP00000439736	DBD: C2H2 ZF Containing Proteins	Other:
Protein: ENSP00000412911	DBD: C2H2 ZF Containing Proteins	Other:
Protein: ENSP00000437488	DBD: C2H2 ZF Containing Proteins	Other:
Protein: ENSP00000473311	DBD: C2H2 ZF Containing Proteins	Other: Med15, Pex14_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.	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"	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

Source	Annotation	Motif	Evidence
RCADE	Schmitges2016		Direct
HT-SELEX	Yin2017		Direct
Methyl-HT-SELEX	Yin2017		Direct
Transfac	Transfac	License required	Direct
Misc	HocoMoco		Direct

Structure

Structure	PDB	Not_Covered

Experimental History

Method	Constructs
Tried in PBM? (Whether the protein was tried in PBM or not)
Tried in HT-SELEX (Whether the protein was tried in HT-SELEX or not, and if so, then what kind of clones were tested)
Other Information? (Tried with another method and failed?)

External Contribution

Name
Email
Comment
Reference

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The accepted consensus binding sequence for Sp1 is usually defined by the asymmetric hexanucleotide core GGGCGG but this sequence does not include, among others, the GAG (=CTC) repeat that constitutes a high-affinity  site for Sp1 binding to the wt1 promoter [2].", "database": "PfamA", "aliStart": 173, "scoreName": "E-value", "accession": "PF00096.24", "start": 173, "score": 1.7e-27, "identifier": "Zinc finger, C2H2 type", "type": "DBD", "aliEnd": 195}}, {"startStyle": "curved", "end": 223, "endStyle": "curved", "aliStart": 201, "text": "zfC2H2", "colour": "#228B22", "aliEnd": 223, "start": 201, "href": "http://pfam.xfam.org/family/PF00096.24", "type": "pfama", "display": "true", "metadata": {"end": 223, "description": "The C2H2 zinc finger is the classical zinc finger domain. The two conserved cysteines and histidines co-ordinate a zinc ion. The following pattern describes the zinc finger. #-X-C-X(1-5)-C-X3-#-X5-#-X2-H-X(3-6)-[H/C] Where X can be any amino acid, and numbers in brackets indicate the number of residues. The positions marked # are those that are important for the stable fold of the zinc finger. The final position can be either his or cys. The C2H2 zinc finger is composed of two short beta strands followed by an alpha helix. The amino terminal part of the helix binds the major groove in DNA binding zinc fingers. 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The following pattern describes the zinc finger. #-X-C-X(1-5)-C-X3-#-X5-#-X2-H-X(3-6)-[H/C] Where X can be any amino acid, and numbers in brackets indicate the number of residues. The positions marked # are those that are important for the stable fold of the zinc finger. The final position can be either his or cys. The C2H2 zinc finger is composed of two short beta strands followed by an alpha helix. The amino terminal part of the helix binds the major groove in DNA binding zinc fingers. 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The following pattern describes the zinc finger. #-X-C-X(1-5)-C-X3-#-X5-#-X2-H-X(3-6)-[H/C] Where X can be any amino acid, and numbers in brackets indicate the number of residues. The positions marked # are those that are important for the stable fold of the zinc finger. The final position can be either his or cys. The C2H2 zinc finger is composed of two short beta strands followed by an alpha helix. The amino terminal part of the helix binds the major groove in DNA binding zinc fingers. The accepted consensus binding sequence for Sp1 is usually defined by the asymmetric hexanucleotide core GGGCGG but this sequence does not include, among others, the GAG (=CTC) repeat that constitutes a high-affinity  site for Sp1 binding to the wt1 promoter [2].", "database": "PfamA", "aliStart": 257, "scoreName": "E-value", "accession": "PF00096.24", "start": 257, "score": 1.7e-27, "identifier": "Zinc finger, C2H2 type", "type": "DBD", "aliEnd": 281}}, {"startStyle": "curved", "end": 309, "endStyle": "curved", "aliStart": 287, "text": "zfC2H2", "colour": "#228B22", "aliEnd": 309, "start": 287, "href": "http://pfam.xfam.org/family/PF00096.24", "type": "pfama", "display": "true", "metadata": {"end": 309, "description": "The C2H2 zinc finger is the classical zinc finger domain. The two conserved cysteines and histidines co-ordinate a zinc ion. 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The following pattern describes the zinc finger. #-X-C-X(1-5)-C-X3-#-X5-#-X2-H-X(3-6)-[H/C] Where X can be any amino acid, and numbers in brackets indicate the number of residues. The positions marked # are those that are important for the stable fold of the zinc finger. The final position can be either his or cys. The C2H2 zinc finger is composed of two short beta strands followed by an alpha helix. The amino terminal part of the helix binds the major groove in DNA binding zinc fingers. The accepted consensus binding sequence for Sp1 is usually defined by the asymmetric hexanucleotide core GGGCGG but this sequence does not include, among others, the GAG (=CTC) repeat that constitutes a high-affinity  site for Sp1 binding to the wt1 promoter [2].", "database": "PfamA", "aliStart": 317, "scoreName": "E-value", "accession": "PF00096.24", "start": 317, "score": 1.7e-27, "identifier": "Zinc finger, C2H2 type", "type": "DBD", "aliEnd": 339}}], "length": 462}

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The following pattern describes the zinc finger. #-X-C-X(1-5)-C-X3-#-X5-#-X2-H-X(3-6)-[H/C] Where X can be any amino acid, and numbers in brackets indicate the number of residues. The positions marked # are those that are important for the stable fold of the zinc finger. The final position can be either his or cys. The C2H2 zinc finger is composed of two short beta strands followed by an alpha helix. The amino terminal part of the helix binds the major groove in DNA binding zinc fingers. 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The accepted consensus binding sequence for Sp1 is usually defined by the asymmetric hexanucleotide core GGGCGG but this sequence does not include, among others, the GAG (=CTC) repeat that constitutes a high-affinity  site for Sp1 binding to the wt1 promoter [2].", "database": "PfamA", "aliStart": 345, "scoreName": "E-value", "accession": "PF00096.24", "start": 345, "score": 1.3e-36, "identifier": "Zinc finger, C2H2 type", "type": "DBD", "aliEnd": 367}}, {"startStyle": "curved", "end": 397, "endStyle": "curved", "aliStart": 373, "text": "zfC2H2", "colour": "#228B22", "aliEnd": 397, "start": 373, "href": "http://pfam.xfam.org/family/PF00096.24", "type": "pfama", "display": "true", "metadata": {"end": 397, "description": "The C2H2 zinc finger is the classical zinc finger domain. The two conserved cysteines and histidines co-ordinate a zinc ion. The following pattern describes the zinc finger. #-X-C-X(1-5)-C-X3-#-X5-#-X2-H-X(3-6)-[H/C] Where X can be any amino acid, and numbers in brackets indicate the number of residues. The positions marked # are those that are important for the stable fold of the zinc finger. The final position can be either his or cys. The C2H2 zinc finger is composed of two short beta strands followed by an alpha helix. The amino terminal part of the helix binds the major groove in DNA binding zinc fingers. The accepted consensus binding sequence for Sp1 is usually defined by the asymmetric hexanucleotide core GGGCGG but this sequence does not include, among others, the GAG (=CTC) repeat that constitutes a high-affinity  site for Sp1 binding to the wt1 promoter [2].", "database": "PfamA", "aliStart": 373, "scoreName": "E-value", "accession": "PF00096.24", "start": 373, "score": 1.3e-36, "identifier": "Zinc finger, C2H2 type", "type": "DBD", "aliEnd": 397}}, {"startStyle": "curved", "end": 425, "endStyle": "curved", "aliStart": 403, "text": "zfC2H2", "colour": "#228B22", "aliEnd": 425, "start": 403, "href": "http://pfam.xfam.org/family/PF00096.24", "type": "pfama", "display": "true", "metadata": {"end": 425, "description": "The C2H2 zinc finger is the classical zinc finger domain. The two conserved cysteines and histidines co-ordinate a zinc ion. The following pattern describes the zinc finger. #-X-C-X(1-5)-C-X3-#-X5-#-X2-H-X(3-6)-[H/C] Where X can be any amino acid, and numbers in brackets indicate the number of residues. The positions marked # are those that are important for the stable fold of the zinc finger. The final position can be either his or cys. The C2H2 zinc finger is composed of two short beta strands followed by an alpha helix. The amino terminal part of the helix binds the major groove in DNA binding zinc fingers. The accepted consensus binding sequence for Sp1 is usually defined by the asymmetric hexanucleotide core GGGCGG but this sequence does not include, among others, the GAG (=CTC) repeat that constitutes a high-affinity  site for Sp1 binding to the wt1 promoter [2].", "database": "PfamA", "aliStart": 403, "scoreName": "E-value", "accession": "PF00096.24", "start": 403, "score": 1.3e-36, "identifier": "Zinc finger, C2H2 type", "type": "DBD", "aliEnd": 425}}, {"startStyle": "curved", "end": 455, "endStyle": "curved", "aliStart": 433, "text": "zfC2H2", "colour": "#228B22", "aliEnd": 455, "start": 433, "href": "http://pfam.xfam.org/family/PF00096.24", "type": "pfama", "display": "true", "metadata": {"end": 455, "description": "The C2H2 zinc finger is the classical zinc finger domain. The two conserved cysteines and histidines co-ordinate a zinc ion. The following pattern describes the zinc finger. #-X-C-X(1-5)-C-X3-#-X5-#-X2-H-X(3-6)-[H/C] Where X can be any amino acid, and numbers in brackets indicate the number of residues. The positions marked # are those that are important for the stable fold of the zinc finger. The final position can be either his or cys. The C2H2 zinc finger is composed of two short beta strands followed by an alpha helix. The amino terminal part of the helix binds the major groove in DNA binding zinc fingers. The accepted consensus binding sequence for Sp1 is usually defined by the asymmetric hexanucleotide core GGGCGG but this sequence does not include, among others, the GAG (=CTC) repeat that constitutes a high-affinity  site for Sp1 binding to the wt1 promoter [2].", "database": "PfamA", "aliStart": 433, "scoreName": "E-value", "accession": "PF00096.24", "start": 433, "score": 1.3e-36, "identifier": "Zinc finger, C2H2 type", "type": "DBD", "aliEnd": 455}}], "length": 578}

{"regions": [{"startStyle": "curved", "end": 234, "endStyle": "curved", "aliStart": 212, "text": "zfC2H2", "colour": "#228B22", "aliEnd": 234, "start": 212, "href": "http://pfam.xfam.org/family/PF00096.24", "type": "pfama", "display": "true", "metadata": {"end": 234, "description": "The C2H2 zinc finger is the classical zinc finger domain. The two conserved cysteines and histidines co-ordinate a zinc ion. The following pattern describes the zinc finger. #-X-C-X(1-5)-C-X3-#-X5-#-X2-H-X(3-6)-[H/C] Where X can be any amino acid, and numbers in brackets indicate the number of residues. The positions marked # are those that are important for the stable fold of the zinc finger. The final position can be either his or cys. The C2H2 zinc finger is composed of two short beta strands followed by an alpha helix. The amino terminal part of the helix binds the major groove in DNA binding zinc fingers. The accepted consensus binding sequence for Sp1 is usually defined by the asymmetric hexanucleotide core GGGCGG but this sequence does not include, among others, the GAG (=CTC) repeat that constitutes a high-affinity  site for Sp1 binding to the wt1 promoter [2].", "database": "PfamA", "aliStart": 212, "scoreName": "E-value", "accession": "PF00096.24", "start": 212, "score": 1.2e-07, "identifier": "Zinc finger, C2H2 type", "type": "DBD", "aliEnd": 234}}, {"startStyle": "curved", "end": 262, "endStyle": "curved", "aliStart": 240, "text": "zfC2H2", "colour": "#228B22", "aliEnd": 262, "start": 240, "href": "http://pfam.xfam.org/family/PF00096.24", "type": "pfama", "display": "true", "metadata": {"end": 262, "description": "The C2H2 zinc finger is the classical zinc finger domain. The two conserved cysteines and histidines co-ordinate a zinc ion. The following pattern describes the zinc finger. #-X-C-X(1-5)-C-X3-#-X5-#-X2-H-X(3-6)-[H/C] Where X can be any amino acid, and numbers in brackets indicate the number of residues. The positions marked # are those that are important for the stable fold of the zinc finger. The final position can be either his or cys. The C2H2 zinc finger is composed of two short beta strands followed by an alpha helix. The amino terminal part of the helix binds the major groove in DNA binding zinc fingers. The accepted consensus binding sequence for Sp1 is usually defined by the asymmetric hexanucleotide core GGGCGG but this sequence does not include, among others, the GAG (=CTC) repeat that constitutes a high-affinity  site for Sp1 binding to the wt1 promoter [2].", "database": "PfamA", "aliStart": 240, "scoreName": "E-value", "accession": "PF00096.24", "start": 240, "score": 1.2e-07, "identifier": "Zinc finger, C2H2 type", "type": "DBD", "aliEnd": 262}}], "length": 277}

{"regions": [{"startStyle": "curved", "end": 24, "endStyle": "curved", "aliStart": 2, "text": "zfC2H2", "colour": "#228B22", "aliEnd": 24, "start": 2, "href": "http://pfam.xfam.org/family/PF00096.24", "type": "pfama", "display": "true", "metadata": {"end": 24, "description": "The C2H2 zinc finger is the classical zinc finger domain. The two conserved cysteines and histidines co-ordinate a zinc ion. The following pattern describes the zinc finger. #-X-C-X(1-5)-C-X3-#-X5-#-X2-H-X(3-6)-[H/C] Where X can be any amino acid, and numbers in brackets indicate the number of residues. The positions marked # are those that are important for the stable fold of the zinc finger. The final position can be either his or cys. The C2H2 zinc finger is composed of two short beta strands followed by an alpha helix. The amino terminal part of the helix binds the major groove in DNA binding zinc fingers. The accepted consensus binding sequence for Sp1 is usually defined by the asymmetric hexanucleotide core GGGCGG but this sequence does not include, among others, the GAG (=CTC) repeat that constitutes a high-affinity  site for Sp1 binding to the wt1 promoter [2].", "database": "PfamA", "aliStart": 2, "scoreName": "E-value", "accession": "PF00096.24", "start": 2, "score": 8e-07, "identifier": "Zinc finger, C2H2 type", "type": "DBD", "aliEnd": 24}}, {"startStyle": "curved", "end": 45, "endStyle": "jagged", "aliStart": 32, "text": "zfC2H2", "colour": "#228B22", "aliEnd": 44, "start": 32, "href": "http://pfam.xfam.org/family/PF00096.24", "type": "pfama", "display": "true", "metadata": {"end": 45, "description": "The C2H2 zinc finger is the classical zinc finger domain. The two conserved cysteines and histidines co-ordinate a zinc ion. The following pattern describes the zinc finger. #-X-C-X(1-5)-C-X3-#-X5-#-X2-H-X(3-6)-[H/C] Where X can be any amino acid, and numbers in brackets indicate the number of residues. The positions marked # are those that are important for the stable fold of the zinc finger. The final position can be either his or cys. The C2H2 zinc finger is composed of two short beta strands followed by an alpha helix. The amino terminal part of the helix binds the major groove in DNA binding zinc fingers. The accepted consensus binding sequence for Sp1 is usually defined by the asymmetric hexanucleotide core GGGCGG but this sequence does not include, among others, the GAG (=CTC) repeat that constitutes a high-affinity  site for Sp1 binding to the wt1 promoter [2].", "database": "PfamA", "aliStart": 32, "scoreName": "E-value", "accession": "PF00096.24", "start": 32, "score": 8e-07, "identifier": "Zinc finger, C2H2 type", "type": "DBD", "aliEnd": 44}}, {"startStyle": "jagged", "end": 142, "endStyle": "jagged", "aliStart": 45, "text": "Med15", "colour": "#9999ff", "aliEnd": 124, "start": 28, "href": "http://pfam.xfam.org/family/PF09606.8", "type": "pfama", "display": "true", "metadata": {"end": 142, "description": "The approx. 70 residue Med15 domain of the ARC-Mediator co-activator is a three-helix bundle with marked similarity to the KIX domain. The sterol regulatory element binding protein (SREBP) family of transcription activators use the ARC105 subunit to activate target genes in the regulation of cholesterol and fatty acid homeostasis. In addition, Med15 is a critical transducer of gene activation signals that control early metazoan development [1].", "database": "PfamA", "aliStart": 45, "scoreName": "E-value", "accession": "PF09606.8", "start": 28, "score": 0.0025, "identifier": "ARC105 or Med15 subunit of Mediator complex non-fungal", "type": "DBD", "aliEnd": 124}}, {"startStyle": "jagged", "end": 151, "endStyle": "jagged", "aliStart": 47, "text": "Pex14_N", "colour": "#9999ff", "aliEnd": 103, "start": 16, "href": "http://pfam.xfam.org/family/PF04695.11", "type": "pfama", "display": "true", "metadata": {"end": 151, "description": "Family of peroxisomal membrane anchor proteins which bind the PTS1 (peroxisomal targeting signal) receptor and are required for the import of PTS1-containing proteins into peroxisomes.  Loss of functional Pex14p results in defects in both the PTS1 and PTS2-dependent import pathways. Deletion analysis of this conserved region implicates it in selective peroxisome degradation. In the majority of members this region is situated at the N-terminus of the protein [1,2].", "database": "PfamA", "aliStart": 47, "scoreName": "E-value", "accession": "PF04695.11", "start": 16, "score": 0.003, "identifier": "Peroxisomal membrane anchor protein (Pex14p) conserved region", "type": "DBD", "aliEnd": 103}}], "length": 160}

TF Info Page for ZNF384 (C2H2 ZF(non-KRAB))