The Human Transcription Factors

Conclusion

Assessment	Binding Mode	Motif Status	Notes	Comments
Known motif	1 Monomer or homomultimer	In vivo/Misc source	Only known motifs are from Transfac or HocoMoco - origin is uncertain

Description

Description:

zinc finger and SCAN domain containing 26 [Source:HGNC Symbol;Acc:HGNC:12978]

Entrez Summary

Ensembl ID:

ENSG00000197062

External Link:

CisBP

Interpro

IPR003309; IPR007087; IPR008916; IPR015880;

Protein Domain:

ENSP00000484931

Protein Domain:

ENSP00000481707

Protein Domain:

ENSP00000478769

Protein Domain:

ENSP00000481024

Protein Domain:

ENSP00000484018

Protein Domain:

ENSP00000479314

Protein Domain:

ENSP00000485228

Domain:

Protein: ENSP00000484931	DBD: C2H2 ZF Containing Proteins	Other:
Protein: ENSP00000481707	DBD: C2H2 ZF Containing Proteins	Other: SCAN
Protein: ENSP00000478769	DBD: C2H2 ZF Containing Proteins	Other:
Protein: ENSP00000481024	DBD: C2H2 ZF Containing Proteins	Other: SCAN
Protein: ENSP00000484018	DBD: C2H2 ZF Containing Proteins	Other: SCAN
Protein: ENSP00000479314	DBD: C2H2 ZF Containing Proteins	Other:
Protein: ENSP00000485228	DBD: C2H2 ZF Containing Proteins	Other: SCAN

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?	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 \| NAS - PMID:1569959
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
Transfac	Transfac	License required	Direct
PBM	Badis09		Inferred - Zscan26 (89% AA Identity, Mus musculus)

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 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 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": 233, "scoreName": "E-value", "accession": "PF00096.24", "start": 232, "score": 7e-36, "identifier": "Zinc finger, C2H2 type", "type": "DBD", "aliEnd": 254}}, {"startStyle": "curved", "end": 282, "endStyle": "curved", "aliStart": 260, "text": "zfC2H2", "colour": "#228B22", "aliEnd": 282, "start": 260, "href": "http://pfam.xfam.org/family/PF00096.24", "type": "pfama", "display": "true", "metadata": {"end": 282, "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. 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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": 451, "scoreName": "E-value", "accession": "PF00096.24", "start": 451, "score": 2.2999999999999997e-34, "identifier": "Zinc finger, C2H2 type", "type": "DBD", "aliEnd": 473}}, {"startStyle": "straight", "end": 136, "endStyle": "straight", "aliStart": 48, "text": "SCAN", "colour": "#9999ff", "aliEnd": 135, "start": 47, "href": "http://pfam.xfam.org/family/PF02023.15", "type": "pfama", "display": "true", "metadata": {"end": 136, "description": "The SCAN domain [1] (named after SRE-ZBP, CTfin51, AW-1 and Number 18 cDNA) is found in several Pfam:PF00096 proteins. The domain has been shown to be able to mediate homo- and hetero-oligomerisation [2].", "database": "PfamA", "aliStart": 48, "scoreName": "E-value", "accession": "PF02023.15", "start": 47, "score": 3.8e-38, "identifier": "SCAN domain", "type": "DBD", "aliEnd": 135}}], "length": 480}

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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": 102, "scoreName": "E-value", "accession": "PF00096.24", "start": 102, "score": 5.1e-37, "identifier": "Zinc finger, C2H2 type", "type": "DBD", "aliEnd": 124}}, {"startStyle": "jagged", "end": 152, "endStyle": "curved", "aliStart": 132, "text": "zfC2H2", "colour": "#228B22", "aliEnd": 152, "start": 130, "href": "http://pfam.xfam.org/family/PF00096.24", "type": "pfama", "display": "true", "metadata": {"end": 152, "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": 132, "scoreName": "E-value", "accession": "PF00096.24", "start": 130, "score": 5.1e-37, "identifier": "Zinc finger, C2H2 type", "type": "DBD", "aliEnd": 152}}, {"startStyle": "curved", "end": 180, "endStyle": "curved", "aliStart": 159, "text": "zfC2H2", "colour": "#228B22", "aliEnd": 180, "start": 158, "href": "http://pfam.xfam.org/family/PF00096.24", "type": "pfama", "display": "true", "metadata": {"end": 180, "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": 159, "scoreName": "E-value", "accession": "PF00096.24", "start": 158, "score": 5.1e-37, "identifier": "Zinc finger, C2H2 type", "type": "DBD", "aliEnd": 180}}, {"startStyle": "curved", "end": 208, "endStyle": "curved", "aliStart": 186, "text": "zfC2H2", "colour": "#228B22", "aliEnd": 208, "start": 186, "href": "http://pfam.xfam.org/family/PF00096.24", "type": "pfama", "display": "true", "metadata": {"end": 208, "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": 186, "scoreName": "E-value", "accession": "PF00096.24", "start": 186, "score": 5.1e-37, "identifier": "Zinc finger, C2H2 type", "type": "DBD", "aliEnd": 208}}, {"startStyle": "curved", "end": 236, "endStyle": "curved", "aliStart": 214, "text": "zfC2H2", "colour": "#228B22", "aliEnd": 236, "start": 214, "href": "http://pfam.xfam.org/family/PF00096.24", "type": "pfama", "display": "true", "metadata": {"end": 236, "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": 214, "scoreName": "E-value", "accession": "PF00096.24", "start": 214, "score": 5.1e-37, "identifier": "Zinc finger, C2H2 type", "type": "DBD", "aliEnd": 236}}, {"startStyle": "curved", "end": 265, "endStyle": "curved", "aliStart": 242, "text": "zfC2H2", "colour": "#228B22", "aliEnd": 264, "start": 242, "href": "http://pfam.xfam.org/family/PF00096.24", "type": "pfama", "display": "true", "metadata": {"end": 265, "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": 242, "scoreName": "E-value", "accession": "PF00096.24", "start": 242, "score": 5.1e-37, "identifier": "Zinc finger, C2H2 type", "type": "DBD", "aliEnd": 264}}], "length": 271}

{"regions": [{"startStyle": "curved", "end": 304, "endStyle": "curved", "aliStart": 282, "text": "zfC2H2", "colour": "#228B22", "aliEnd": 304, "start": 282, "href": "http://pfam.xfam.org/family/PF00096.24", "type": "pfama", "display": "true", "metadata": {"end": 304, "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": 282, "scoreName": "E-value", "accession": "PF00096.24", "start": 282, "score": 2.2999999999999997e-34, "identifier": "Zinc finger, C2H2 type", "type": "DBD", "aliEnd": 304}}, {"startStyle": "curved", "end": 332, "endStyle": "curved", "aliStart": 310, "text": "zfC2H2", "colour": "#228B22", "aliEnd": 332, "start": 310, "href": "http://pfam.xfam.org/family/PF00096.24", "type": "pfama", "display": "true", "metadata": {"end": 332, "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": 310, "scoreName": "E-value", "accession": "PF00096.24", "start": 310, "score": 2.2999999999999997e-34, "identifier": "Zinc finger, C2H2 type", "type": "DBD", "aliEnd": 332}}, {"startStyle": "jagged", "end": 360, "endStyle": "curved", "aliStart": 340, "text": "zfC2H2", "colour": "#228B22", "aliEnd": 360, "start": 338, "href": "http://pfam.xfam.org/family/PF00096.24", "type": "pfama", "display": "true", "metadata": {"end": 360, "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": 340, "scoreName": "E-value", "accession": "PF00096.24", "start": 338, "score": 2.2999999999999997e-34, "identifier": "Zinc finger, C2H2 type", "type": "DBD", "aliEnd": 360}}, {"startStyle": "curved", "end": 388, "endStyle": "curved", "aliStart": 367, "text": "zfC2H2", "colour": "#228B22", "aliEnd": 388, "start": 366, "href": "http://pfam.xfam.org/family/PF00096.24", "type": "pfama", "display": "true", "metadata": {"end": 388, "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": 367, "scoreName": "E-value", "accession": "PF00096.24", "start": 366, "score": 2.2999999999999997e-34, "identifier": "Zinc finger, C2H2 type", "type": "DBD", "aliEnd": 388}}, {"startStyle": "curved", "end": 416, "endStyle": "curved", "aliStart": 394, "text": "zfC2H2", "colour": "#228B22", "aliEnd": 416, "start": 394, "href": "http://pfam.xfam.org/family/PF00096.24", "type": "pfama", "display": "true", "metadata": {"end": 416, "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": 394, "scoreName": "E-value", "accession": "PF00096.24", "start": 394, "score": 2.2999999999999997e-34, "identifier": "Zinc finger, C2H2 type", "type": "DBD", "aliEnd": 416}}, {"startStyle": "curved", "end": 444, "endStyle": "curved", "aliStart": 422, "text": "zfC2H2", "colour": "#228B22", "aliEnd": 444, "start": 422, "href": "http://pfam.xfam.org/family/PF00096.24", "type": "pfama", "display": "true", "metadata": {"end": 444, "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": 422, "scoreName": "E-value", "accession": "PF00096.24", "start": 422, "score": 2.2999999999999997e-34, "identifier": "Zinc finger, C2H2 type", "type": "DBD", "aliEnd": 444}}, {"startStyle": "curved", "end": 473, "endStyle": "curved", "aliStart": 450, "text": "zfC2H2", "colour": "#228B22", "aliEnd": 472, "start": 450, "href": "http://pfam.xfam.org/family/PF00096.24", "type": "pfama", "display": "true", "metadata": {"end": 473, "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": 450, "scoreName": "E-value", "accession": "PF00096.24", "start": 450, "score": 2.2999999999999997e-34, "identifier": "Zinc finger, C2H2 type", "type": "DBD", "aliEnd": 472}}, {"startStyle": "straight", "end": 136, "endStyle": "straight", "aliStart": 48, "text": "SCAN", "colour": "#9999ff", "aliEnd": 135, "start": 47, "href": "http://pfam.xfam.org/family/PF02023.15", "type": "pfama", "display": "true", "metadata": {"end": 136, "description": "The SCAN domain [1] (named after SRE-ZBP, CTfin51, AW-1 and Number 18 cDNA) is found in several Pfam:PF00096 proteins. The domain has been shown to be able to mediate homo- and hetero-oligomerisation [2].", "database": "PfamA", "aliStart": 48, "scoreName": "E-value", "accession": "PF02023.15", "start": 47, "score": 3.7000000000000005e-38, "identifier": "SCAN domain", "type": "DBD", "aliEnd": 135}}], "length": 479}

TF Info Page for ZSCAN26 (C2H2 ZF(non-KRAB))

Conclusion

Description

Previous Annotations

DNA-Binding

Published Motif Data

Structure

Experimental History

External Contribution