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:

MDS1 and EVI1 complex locus [Source:HGNC Symbol;Acc:HGNC:3498]

Entrez Summary

The protein encoded by this gene is a transcriptional regulator and oncoprotein that may be involved in hematopoiesis, apoptosis, development, and cell differentiation and proliferation. The encoded protein can interact with CTBP1, SMAD3, CREBBP, KAT2B, MAPK8, and MAPK9. This gene can undergo translocation with the AML1 gene, resulting in overexpression of this gene and the onset of leukemia. Several transcript variants encoding a few different isoforms have been found for this gene. [provided by RefSeq, Mar 2011]

Ensembl ID:

ENSG00000085276

External Link:

CisBP

Interpro

IPR001214; IPR007087; IPR015880; ;

Protein Domain:

ENSP00000264674

Protein Domain:

ENSP00000394302

Protein Domain:

ENSP00000420466

Protein Domain:

ENSP00000417922

Protein Domain:

ENSP00000419770

Protein Domain:

ENSP00000418689

Protein Domain:

ENSP00000419757

Protein Domain:

ENSP00000420072

Protein Domain:

ENSP00000486104

Protein Domain:

ENSP00000419995

Domain:

Protein: ENSP00000264674	DBD: C2H2 ZF Containing Proteins	Other:
Protein: ENSP00000394302	DBD: C2H2 ZF Containing Proteins	Other:
Protein: ENSP00000420466	DBD: C2H2 ZF Containing Proteins	Other:
Protein: ENSP00000417922	DBD: C2H2 ZF Containing Proteins	Other:
Protein: ENSP00000419770	DBD: C2H2 ZF Containing Proteins	Other:
Protein: ENSP00000418689	DBD: C2H2 ZF Containing Proteins	Other:
Protein: ENSP00000419757	DBD: C2H2 ZF Containing Proteins	Other:
Protein: ENSP00000420072	DBD: C2H2 ZF Containing Proteins	Other:
Protein: ENSP00000486104	DBD: C2H2 ZF Containing Proteins	Other:
Protein: ENSP00000419995	DBD: C2H2 ZF Containing Proteins	Other:

Previous Annotations

Source	Annotation
TF-CAT classification	TF Gene_DNA-Binding sequence-specific_DNA Binding Transactivation_ PMIDS:15889140
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 IDA - PMID:19767769
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	2a1, Lower confidence direct evidence
TF has conditional DNA-binding requirements

DNA-Binding

Published Motif Data

Source	Annotation	Motif	Evidence
Transfac	Transfac	License required	Direct
Transfac	Transfac	License required	Direct
Transfac	Transfac	License required	Direct
Transfac	Transfac	License required	Direct
Transfac	Transfac	License required	Direct
Transfac	Transfac	License required	Direct
Transfac	Transfac	License required	Direct
Misc	HocoMoco		Direct
SELEX	JASPAR		Inferred - Mecom (97% 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 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": 798, "scoreName": "E-value", "accession": "PF00096.24", "start": 798, "score": 3.2e-47, "identifier": "Zinc finger, C2H2 type", "type": "DBD", "aliEnd": 820}}, {"startStyle": "curved", "end": 849, "endStyle": "curved", "aliStart": 826, "text": "zfC2H2", "colour": "#228B22", "aliEnd": 849, "start": 826, "href": "http://pfam.xfam.org/family/PF00096.24", "type": "pfama", "display": "true", "metadata": {"end": 849, "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": 855, "scoreName": "E-value", "accession": "PF00096.24", "start": 855, "score": 3.2e-47, "identifier": "Zinc finger, C2H2 type", "type": "DBD", "aliEnd": 877}}, {"startStyle": "jagged", "end": 220, "endStyle": "curved", "aliStart": 193, "text": "zfBED", "colour": "#2cb42c", "aliEnd": 219, "start": 185, "href": "http://pfam.xfam.org/family/PF02892.13", "type": "pfama", "display": "true", "metadata": {"end": 220, "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": 193, "scoreName": "E-value", "accession": "PF02892.13", "start": 185, "score": 0.0006799999999999999, "identifier": "BED zinc finger", "type": "DBD", "aliEnd": 219}}, {"startStyle": "jagged", "end": 821, "endStyle": "jagged", "aliStart": 793, "text": "zfBED", "colour": "#2cb42c", "aliEnd": 820, "start": 785, "href": "http://pfam.xfam.org/family/PF02892.13", "type": "pfama", "display": "true", "metadata": {"end": 821, "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": 793, "scoreName": "E-value", "accession": "PF02892.13", "start": 785, "score": 0.0006799999999999999, "identifier": "BED zinc finger", "type": "DBD", "aliEnd": 820}}, {"startStyle": "jagged", "end": 850, "endStyle": "curved", "aliStart": 822, "text": "zfBED", "colour": "#2cb42c", "aliEnd": 849, "start": 819, "href": "http://pfam.xfam.org/family/PF02892.13", "type": "pfama", "display": "true", "metadata": {"end": 850, "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. 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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": 131, "scoreName": "E-value", "accession": "PF00096.24", "start": 131, "score": 1.6999999999999998e-47, "identifier": "Zinc finger, C2H2 type", "type": "DBD", "aliEnd": 155}}, {"startStyle": "curved", "end": 183, "endStyle": "curved", "aliStart": 161, "text": "zfC2H2", "colour": "#228B22", "aliEnd": 183, "start": 161, "href": "http://pfam.xfam.org/family/PF00096.24", "type": "pfama", "display": "true", "metadata": {"end": 183, "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": 161, "scoreName": "E-value", "accession": "PF00096.24", "start": 161, "score": 1.6999999999999998e-47, "identifier": "Zinc finger, C2H2 type", "type": "DBD", "aliEnd": 183}}, {"startStyle": "curved", "end": 211, "endStyle": "curved", "aliStart": 189, "text": "zfC2H2", "colour": "#228B22", "aliEnd": 211, "start": 189, "href": "http://pfam.xfam.org/family/PF00096.24", "type": "pfama", "display": "true", "metadata": {"end": 211, "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": 189, "scoreName": "E-value", "accession": "PF00096.24", "start": 189, "score": 1.6999999999999998e-47, "identifier": "Zinc finger, C2H2 type", "type": "DBD", "aliEnd": 211}}, {"startStyle": "curved", "end": 239, "endStyle": "curved", "aliStart": 219, "text": "zfC2H2", "colour": "#228B22", "aliEnd": 238, "start": 218, "href": "http://pfam.xfam.org/family/PF00096.24", "type": "pfama", "display": "true", "metadata": {"end": 239, "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": 219, "scoreName": "E-value", "accession": "PF00096.24", "start": 218, "score": 1.6999999999999998e-47, "identifier": "Zinc finger, C2H2 type", "type": "DBD", "aliEnd": 238}}, {"startStyle": "curved", "end": 756, "endStyle": "curved", "aliStart": 734, "text": "zfC2H2", "colour": "#228B22", "aliEnd": 756, "start": 734, "href": "http://pfam.xfam.org/family/PF00096.24", "type": "pfama", "display": "true", "metadata": {"end": 756, "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": 734, "scoreName": "E-value", "accession": "PF00096.24", "start": 734, "score": 1.6999999999999998e-47, "identifier": "Zinc finger, C2H2 type", "type": "DBD", "aliEnd": 756}}, {"startStyle": "curved", "end": 785, "endStyle": "curved", "aliStart": 762, "text": "zfC2H2", "colour": "#228B22", "aliEnd": 785, "start": 762, "href": "http://pfam.xfam.org/family/PF00096.24", "type": "pfama", "display": "true", "metadata": {"end": 785, "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": 762, "scoreName": "E-value", "accession": "PF00096.24", "start": 762, "score": 1.6999999999999998e-47, "identifier": "Zinc finger, C2H2 type", "type": "DBD", "aliEnd": 785}}, {"startStyle": "curved", "end": 813, "endStyle": "curved", "aliStart": 791, "text": "zfC2H2", "colour": "#228B22", "aliEnd": 813, "start": 791, "href": "http://pfam.xfam.org/family/PF00096.24", "type": "pfama", "display": "true", "metadata": {"end": 813, "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": 791, "scoreName": "E-value", "accession": "PF00096.24", "start": 791, "score": 1.6999999999999998e-47, "identifier": "Zinc finger, C2H2 type", "type": "DBD", "aliEnd": 813}}, {"startStyle": "jagged", "end": 156, "endStyle": "curved", "aliStart": 129, "text": "zfBED", "colour": "#2cb42c", "aliEnd": 155, "start": 121, "href": "http://pfam.xfam.org/family/PF02892.13", "type": "pfama", "display": "true", "metadata": {"end": 156, "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": 129, "scoreName": "E-value", "accession": "PF02892.13", "start": 121, "score": 0.0002, "identifier": "BED zinc finger", "type": "DBD", "aliEnd": 155}}, {"startStyle": "jagged", "end": 757, "endStyle": "jagged", "aliStart": 729, "text": "zfBED", "colour": "#2cb42c", "aliEnd": 756, "start": 721, "href": "http://pfam.xfam.org/family/PF02892.13", "type": "pfama", "display": "true", "metadata": {"end": 757, "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": 729, "scoreName": "E-value", "accession": "PF02892.13", "start": 721, "score": 0.0002, "identifier": "BED zinc finger", "type": "DBD", "aliEnd": 756}}, {"startStyle": "jagged", "end": 786, "endStyle": "curved", "aliStart": 758, "text": "zfBED", "colour": "#2cb42c", "aliEnd": 785, "start": 755, "href": "http://pfam.xfam.org/family/PF02892.13", "type": "pfama", "display": "true", "metadata": {"end": 786, "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": 758, "scoreName": "E-value", "accession": "PF02892.13", "start": 755, "score": 0.0002, "identifier": "BED zinc finger", "type": "DBD", "aliEnd": 785}}], "length": 1053}

{"regions": [{"startStyle": "curved", "end": 42, "endStyle": "curved", "aliStart": 21, "text": "zfC2H2", "colour": "#228B22", "aliEnd": 41, "start": 21, "href": "http://pfam.xfam.org/family/PF00096.24", "type": "pfama", "display": "true", "metadata": {"end": 42, "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": 21, "scoreName": "E-value", "accession": "PF00096.24", "start": 21, "score": 6.399999999999999e-50, "identifier": "Zinc finger, C2H2 type", "type": "DBD", "aliEnd": 41}}, {"startStyle": "curved", "end": 97, "endStyle": "curved", "aliStart": 76, "text": "zfC2H2", "colour": "#228B22", "aliEnd": 97, "start": 75, "href": "http://pfam.xfam.org/family/PF00096.24", "type": "pfama", "display": "true", "metadata": {"end": 97, "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": 76, "scoreName": "E-value", "accession": "PF00096.24", "start": 75, "score": 6.399999999999999e-50, "identifier": "Zinc finger, C2H2 type", "type": "DBD", "aliEnd": 97}}, {"startStyle": "curved", "end": 125, "endStyle": "curved", "aliStart": 103, "text": "zfC2H2", "colour": "#228B22", "aliEnd": 125, "start": 103, "href": "http://pfam.xfam.org/family/PF00096.24", "type": "pfama", "display": "true", "metadata": {"end": 125, "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": 103, "scoreName": "E-value", "accession": "PF00096.24", "start": 103, "score": 6.399999999999999e-50, "identifier": "Zinc finger, C2H2 type", "type": "DBD", "aliEnd": 125}}, {"startStyle": "curved", "end": 154, "endStyle": "curved", "aliStart": 131, "text": "zfC2H2", "colour": "#228B22", "aliEnd": 154, "start": 131, "href": "http://pfam.xfam.org/family/PF00096.24", "type": "pfama", "display": "true", "metadata": {"end": 154, "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": 131, "scoreName": "E-value", "accession": "PF00096.24", "start": 131, "score": 6.399999999999999e-50, "identifier": "Zinc finger, C2H2 type", "type": "DBD", "aliEnd": 154}}, {"startStyle": "curved", "end": 182, "endStyle": "curved", "aliStart": 160, "text": "zfC2H2", "colour": "#228B22", "aliEnd": 182, "start": 160, "href": "http://pfam.xfam.org/family/PF00096.24", "type": "pfama", "display": "true", "metadata": {"end": 182, "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": 160, "scoreName": "E-value", "accession": "PF00096.24", "start": 160, "score": 6.399999999999999e-50, "identifier": "Zinc finger, C2H2 type", "type": "DBD", "aliEnd": 182}}, {"startStyle": "curved", "end": 210, "endStyle": "curved", "aliStart": 188, "text": "zfC2H2", "colour": "#228B22", "aliEnd": 210, "start": 188, "href": "http://pfam.xfam.org/family/PF00096.24", "type": "pfama", "display": "true", "metadata": {"end": 210, "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": 188, "scoreName": "E-value", "accession": "PF00096.24", "start": 188, "score": 6.399999999999999e-50, "identifier": "Zinc finger, C2H2 type", "type": "DBD", "aliEnd": 210}}, {"startStyle": "curved", "end": 238, "endStyle": "curved", "aliStart": 218, "text": "zfC2H2", "colour": "#228B22", "aliEnd": 237, "start": 217, "href": "http://pfam.xfam.org/family/PF00096.24", "type": "pfama", "display": "true", "metadata": {"end": 238, "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": 218, "scoreName": "E-value", "accession": "PF00096.24", "start": 217, "score": 6.399999999999999e-50, "identifier": "Zinc finger, C2H2 type", "type": "DBD", "aliEnd": 237}}, {"startStyle": "curved", "end": 746, "endStyle": "curved", "aliStart": 724, "text": "zfC2H2", "colour": "#228B22", "aliEnd": 746, "start": 724, "href": "http://pfam.xfam.org/family/PF00096.24", "type": "pfama", "display": "true", "metadata": {"end": 746, "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": 724, "scoreName": "E-value", "accession": "PF00096.24", "start": 724, "score": 6.399999999999999e-50, "identifier": "Zinc finger, C2H2 type", "type": "DBD", "aliEnd": 746}}, {"startStyle": "curved", "end": 775, "endStyle": "curved", "aliStart": 752, "text": "zfC2H2", "colour": "#228B22", "aliEnd": 775, "start": 752, "href": "http://pfam.xfam.org/family/PF00096.24", "type": "pfama", "display": "true", "metadata": {"end": 775, "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": 752, "scoreName": "E-value", "accession": "PF00096.24", "start": 752, "score": 6.399999999999999e-50, "identifier": "Zinc finger, C2H2 type", "type": "DBD", "aliEnd": 775}}, {"startStyle": "curved", "end": 803, "endStyle": "curved", "aliStart": 781, "text": "zfC2H2", "colour": "#228B22", "aliEnd": 803, "start": 781, "href": "http://pfam.xfam.org/family/PF00096.24", "type": "pfama", "display": "true", "metadata": {"end": 803, "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": 781, "scoreName": "E-value", "accession": "PF00096.24", "start": 781, "score": 6.399999999999999e-50, "identifier": "Zinc finger, C2H2 type", "type": "DBD", "aliEnd": 803}}, {"startStyle": "jagged", "end": 155, "endStyle": "curved", "aliStart": 129, "text": "zfBED", "colour": "#2cb42c", "aliEnd": 154, "start": 121, "href": "http://pfam.xfam.org/family/PF02892.13", "type": "pfama", "display": "true", "metadata": {"end": 155, "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": 129, "scoreName": "E-value", "accession": "PF02892.13", "start": 121, "score": 0.00016999999999999999, "identifier": "BED zinc finger", "type": "DBD", "aliEnd": 154}}, {"startStyle": "jagged", "end": 747, "endStyle": "jagged", "aliStart": 719, "text": "zfBED", "colour": "#2cb42c", "aliEnd": 746, "start": 711, "href": "http://pfam.xfam.org/family/PF02892.13", "type": "pfama", "display": "true", "metadata": {"end": 747, "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": 719, "scoreName": "E-value", "accession": "PF02892.13", "start": 711, "score": 0.00016999999999999999, "identifier": "BED zinc finger", "type": "DBD", "aliEnd": 746}}, {"startStyle": "jagged", "end": 776, "endStyle": "curved", "aliStart": 748, "text": "zfBED", "colour": "#2cb42c", "aliEnd": 775, "start": 745, "href": "http://pfam.xfam.org/family/PF02892.13", "type": "pfama", "display": "true", "metadata": {"end": 776, "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": 748, "scoreName": "E-value", "accession": "PF02892.13", "start": 745, "score": 0.00016999999999999999, "identifier": "BED zinc finger", "type": "DBD", "aliEnd": 775}}], "length": 1004}

{"regions": [{"startStyle": "curved", "end": 42, "endStyle": "curved", "aliStart": 21, "text": "zfC2H2", "colour": "#228B22", "aliEnd": 41, "start": 21, "href": "http://pfam.xfam.org/family/PF00096.24", "type": "pfama", "display": "true", "metadata": {"end": 42, "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": 21, "scoreName": "E-value", "accession": "PF00096.24", "start": 21, "score": 9.5e-50, "identifier": "Zinc finger, C2H2 type", "type": "DBD", "aliEnd": 41}}, {"startStyle": "curved", "end": 97, "endStyle": "curved", "aliStart": 76, "text": "zfC2H2", "colour": "#228B22", "aliEnd": 97, "start": 75, "href": "http://pfam.xfam.org/family/PF00096.24", "type": "pfama", "display": "true", "metadata": {"end": 97, "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": 76, "scoreName": "E-value", "accession": "PF00096.24", "start": 75, "score": 9.5e-50, "identifier": "Zinc finger, C2H2 type", "type": "DBD", "aliEnd": 97}}, {"startStyle": "curved", "end": 125, "endStyle": "curved", "aliStart": 103, "text": "zfC2H2", "colour": "#228B22", "aliEnd": 125, "start": 103, "href": "http://pfam.xfam.org/family/PF00096.24", "type": "pfama", "display": "true", "metadata": {"end": 125, "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": 103, "scoreName": "E-value", "accession": "PF00096.24", "start": 103, "score": 9.5e-50, "identifier": "Zinc finger, C2H2 type", "type": "DBD", "aliEnd": 125}}, {"startStyle": "curved", "end": 154, "endStyle": "curved", "aliStart": 131, "text": "zfC2H2", "colour": "#228B22", "aliEnd": 154, "start": 131, "href": "http://pfam.xfam.org/family/PF00096.24", "type": "pfama", "display": "true", "metadata": {"end": 154, "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": 131, "scoreName": "E-value", "accession": "PF00096.24", "start": 131, "score": 9.5e-50, "identifier": "Zinc finger, C2H2 type", "type": "DBD", "aliEnd": 154}}, {"startStyle": "curved", "end": 182, "endStyle": "curved", "aliStart": 160, "text": "zfC2H2", "colour": "#228B22", "aliEnd": 182, "start": 160, "href": "http://pfam.xfam.org/family/PF00096.24", "type": "pfama", "display": "true", "metadata": {"end": 182, "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": 160, "scoreName": "E-value", "accession": "PF00096.24", "start": 160, "score": 9.5e-50, "identifier": "Zinc finger, C2H2 type", "type": "DBD", "aliEnd": 182}}, {"startStyle": "curved", "end": 210, "endStyle": "curved", "aliStart": 188, "text": "zfC2H2", "colour": "#228B22", "aliEnd": 210, "start": 188, "href": "http://pfam.xfam.org/family/PF00096.24", "type": "pfama", "display": "true", "metadata": {"end": 210, "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": 188, "scoreName": "E-value", "accession": "PF00096.24", "start": 188, "score": 9.5e-50, "identifier": "Zinc finger, C2H2 type", "type": "DBD", "aliEnd": 210}}, {"startStyle": "curved", "end": 238, "endStyle": "curved", "aliStart": 218, "text": "zfC2H2", "colour": "#228B22", "aliEnd": 237, "start": 217, "href": "http://pfam.xfam.org/family/PF00096.24", "type": "pfama", "display": "true", "metadata": {"end": 238, "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": 218, "scoreName": "E-value", "accession": "PF00096.24", "start": 217, "score": 9.5e-50, "identifier": "Zinc finger, C2H2 type", "type": "DBD", "aliEnd": 237}}, {"startStyle": "curved", "end": 746, "endStyle": "curved", "aliStart": 724, "text": "zfC2H2", "colour": "#228B22", "aliEnd": 746, "start": 724, "href": "http://pfam.xfam.org/family/PF00096.24", "type": "pfama", "display": "true", "metadata": {"end": 746, "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": 724, "scoreName": "E-value", "accession": "PF00096.24", "start": 724, "score": 9.5e-50, "identifier": "Zinc finger, C2H2 type", "type": "DBD", "aliEnd": 746}}, {"startStyle": "curved", "end": 775, "endStyle": "curved", "aliStart": 752, "text": "zfC2H2", "colour": "#228B22", "aliEnd": 775, "start": 752, "href": "http://pfam.xfam.org/family/PF00096.24", "type": "pfama", "display": "true", "metadata": {"end": 775, "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": 752, "scoreName": "E-value", "accession": "PF00096.24", "start": 752, "score": 9.5e-50, "identifier": "Zinc finger, C2H2 type", "type": "DBD", "aliEnd": 775}}, {"startStyle": "curved", "end": 803, "endStyle": "curved", "aliStart": 781, "text": "zfC2H2", "colour": "#228B22", "aliEnd": 803, "start": 781, "href": "http://pfam.xfam.org/family/PF00096.24", "type": "pfama", "display": "true", "metadata": {"end": 803, "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": 781, "scoreName": "E-value", "accession": "PF00096.24", "start": 781, "score": 9.5e-50, "identifier": "Zinc finger, C2H2 type", "type": "DBD", "aliEnd": 803}}, {"startStyle": "jagged", "end": 155, "endStyle": "curved", "aliStart": 129, "text": "zfBED", "colour": "#2cb42c", "aliEnd": 154, "start": 122, "href": "http://pfam.xfam.org/family/PF02892.13", "type": "pfama", "display": "true", "metadata": {"end": 155, "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": 129, "scoreName": "E-value", "accession": "PF02892.13", "start": 122, "score": 0.00018999999999999998, "identifier": "BED zinc finger", "type": "DBD", "aliEnd": 154}}, {"startStyle": "jagged", "end": 747, "endStyle": "jagged", "aliStart": 719, "text": "zfBED", "colour": "#2cb42c", "aliEnd": 746, "start": 711, "href": "http://pfam.xfam.org/family/PF02892.13", "type": "pfama", "display": "true", "metadata": {"end": 747, "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": 719, "scoreName": "E-value", "accession": "PF02892.13", "start": 711, "score": 0.00018999999999999998, "identifier": "BED zinc finger", "type": "DBD", "aliEnd": 746}}, {"startStyle": "jagged", "end": 776, "endStyle": "curved", "aliStart": 748, "text": "zfBED", "colour": "#2cb42c", "aliEnd": 775, "start": 745, "href": "http://pfam.xfam.org/family/PF02892.13", "type": "pfama", "display": "true", "metadata": {"end": 776, "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": 748, "scoreName": "E-value", "accession": "PF02892.13", "start": 745, "score": 0.00018999999999999998, "identifier": "BED zinc finger", "type": "DBD", "aliEnd": 775}}], "length": 1043}

{"regions": [{"startStyle": "curved", "end": 42, "endStyle": "curved", "aliStart": 21, "text": "zfC2H2", "colour": "#228B22", "aliEnd": 41, "start": 21, "href": "http://pfam.xfam.org/family/PF00096.24", "type": "pfama", "display": "true", "metadata": {"end": 42, "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": 21, "scoreName": "E-value", "accession": "PF00096.24", "start": 21, "score": 1e-49, "identifier": "Zinc finger, C2H2 type", "type": "DBD", "aliEnd": 41}}, {"startStyle": "curved", "end": 97, "endStyle": "curved", "aliStart": 76, "text": "zfC2H2", "colour": "#228B22", "aliEnd": 97, "start": 75, "href": "http://pfam.xfam.org/family/PF00096.24", "type": "pfama", "display": "true", "metadata": {"end": 97, "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": 76, "scoreName": "E-value", "accession": "PF00096.24", "start": 75, "score": 1e-49, "identifier": "Zinc finger, C2H2 type", "type": "DBD", "aliEnd": 97}}, {"startStyle": "curved", "end": 125, "endStyle": "curved", "aliStart": 103, "text": "zfC2H2", "colour": "#228B22", "aliEnd": 125, "start": 103, "href": "http://pfam.xfam.org/family/PF00096.24", "type": "pfama", "display": "true", "metadata": {"end": 125, "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": 103, "scoreName": "E-value", "accession": "PF00096.24", "start": 103, "score": 1e-49, "identifier": "Zinc finger, C2H2 type", "type": "DBD", "aliEnd": 125}}, {"startStyle": "curved", "end": 154, "endStyle": "curved", "aliStart": 131, "text": "zfC2H2", "colour": "#228B22", "aliEnd": 154, "start": 131, "href": "http://pfam.xfam.org/family/PF00096.24", "type": "pfama", "display": "true", "metadata": {"end": 154, "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": 131, "scoreName": "E-value", "accession": "PF00096.24", "start": 131, "score": 1e-49, "identifier": "Zinc finger, C2H2 type", "type": "DBD", "aliEnd": 154}}, {"startStyle": "curved", "end": 182, "endStyle": "curved", "aliStart": 160, "text": "zfC2H2", "colour": "#228B22", "aliEnd": 182, "start": 160, "href": "http://pfam.xfam.org/family/PF00096.24", "type": "pfama", "display": "true", "metadata": {"end": 182, "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": 160, "scoreName": "E-value", "accession": "PF00096.24", "start": 160, "score": 1e-49, "identifier": "Zinc finger, C2H2 type", "type": "DBD", "aliEnd": 182}}, {"startStyle": "curved", "end": 210, "endStyle": "curved", "aliStart": 188, "text": "zfC2H2", "colour": "#228B22", "aliEnd": 210, "start": 188, "href": "http://pfam.xfam.org/family/PF00096.24", "type": "pfama", "display": "true", "metadata": {"end": 210, "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": 188, "scoreName": "E-value", "accession": "PF00096.24", "start": 188, "score": 1e-49, "identifier": "Zinc finger, C2H2 type", "type": "DBD", "aliEnd": 210}}, {"startStyle": "curved", "end": 238, "endStyle": "curved", "aliStart": 218, "text": "zfC2H2", "colour": "#228B22", "aliEnd": 237, "start": 217, "href": "http://pfam.xfam.org/family/PF00096.24", "type": "pfama", "display": "true", "metadata": {"end": 238, "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": 218, "scoreName": "E-value", "accession": "PF00096.24", "start": 217, "score": 1e-49, "identifier": "Zinc finger, C2H2 type", "type": "DBD", "aliEnd": 237}}, {"startStyle": "curved", "end": 755, "endStyle": "curved", "aliStart": 733, "text": "zfC2H2", "colour": "#228B22", "aliEnd": 755, "start": 733, "href": "http://pfam.xfam.org/family/PF00096.24", "type": "pfama", "display": "true", "metadata": {"end": 755, "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": 733, "scoreName": "E-value", "accession": "PF00096.24", "start": 733, "score": 1e-49, "identifier": "Zinc finger, C2H2 type", "type": "DBD", "aliEnd": 755}}, {"startStyle": "curved", "end": 784, "endStyle": "curved", "aliStart": 761, "text": "zfC2H2", "colour": "#228B22", "aliEnd": 784, "start": 761, "href": "http://pfam.xfam.org/family/PF00096.24", "type": "pfama", "display": "true", "metadata": {"end": 784, "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": 761, "scoreName": "E-value", "accession": "PF00096.24", "start": 761, "score": 1e-49, "identifier": "Zinc finger, C2H2 type", "type": "DBD", "aliEnd": 784}}, {"startStyle": "curved", "end": 812, "endStyle": "curved", "aliStart": 790, "text": "zfC2H2", "colour": "#228B22", "aliEnd": 812, "start": 790, "href": "http://pfam.xfam.org/family/PF00096.24", "type": "pfama", "display": "true", "metadata": {"end": 812, "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": 790, "scoreName": "E-value", "accession": "PF00096.24", "start": 790, "score": 1e-49, "identifier": "Zinc finger, C2H2 type", "type": "DBD", "aliEnd": 812}}, {"startStyle": "jagged", "end": 155, "endStyle": "curved", "aliStart": 129, "text": "zfBED", "colour": "#2cb42c", "aliEnd": 154, "start": 122, "href": "http://pfam.xfam.org/family/PF02892.13", "type": "pfama", "display": "true", "metadata": {"end": 155, "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": 129, "scoreName": "E-value", "accession": "PF02892.13", "start": 122, "score": 0.0002, "identifier": "BED zinc finger", "type": "DBD", "aliEnd": 154}}, {"startStyle": "jagged", "end": 756, "endStyle": "jagged", "aliStart": 728, "text": "zfBED", "colour": "#2cb42c", "aliEnd": 755, "start": 720, "href": "http://pfam.xfam.org/family/PF02892.13", "type": "pfama", "display": "true", "metadata": {"end": 756, "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": 728, "scoreName": "E-value", "accession": "PF02892.13", "start": 720, "score": 0.0002, "identifier": "BED zinc finger", "type": "DBD", "aliEnd": 755}}, {"startStyle": "jagged", "end": 785, "endStyle": "curved", "aliStart": 757, "text": "zfBED", "colour": "#2cb42c", "aliEnd": 784, "start": 754, "href": "http://pfam.xfam.org/family/PF02892.13", "type": "pfama", "display": "true", "metadata": {"end": 785, "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": 757, "scoreName": "E-value", "accession": "PF02892.13", "start": 754, "score": 0.0002, "identifier": "BED zinc finger", "type": "DBD", "aliEnd": 784}}], "length": 1052}

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

Conclusion

Description

Previous Annotations

DNA-Binding

Published Motif Data

Structure

Experimental History

External Contribution