The Human Transcription Factors

Conclusion

Assessment	Binding Mode	Motif Status	Notes	Comments
Inferred motif	1 Monomer or homomultimer	In vivo/Misc source

Description

Description:	spalt like transcription factor 1 [Source:HGNC Symbol;Acc:HGNC:10524]
Entrez Summary	TBA
Ensembl ID:	ENSG00000103449
External Link:
Interpro	IPR007087; IPR015880;
Protein Domain:
Protein: ENSP00000251020	DBD: C2H2 ZF Containing Proteins	Other: IZUMO, zf-C2H2_2, zf-C2H2_4, zf-C2H2_jaz, zf-met
Protein: ENSP00000455582	DBD: C2H2 ZF Containing Proteins	Other:
Protein: ENSP00000407914	DBD: C2H2 ZF Containing Proteins	Other: IZUMO, zf-C2H2_2, zf-C2H2_4, zf-C2H2_jaz, zf-met
Protein: ENSP00000456777	DBD: C2H2 ZF Containing Proteins	Other: IZUMO, zf-C2H2_2, zf-C2H2_4, zf-C2H2_jaz, zf-met

Previous Annotations

Source	Annotation
TF-CAT classification	TF Gene_Transcription Regulatory Activity heterochromatin interaction/binding_Other TF PPI_ PMIDS:11836251
Vaquerizas 2009 TF classification "a" Has direct evidence of TF function; "b" Has evidence for an orthologous TF; "c" contains likely DBDs, but has no functional evidence; "x" is an unlikely TF such as predicted gene, genes with likely non-specific DBDs or that have function outside transcription; "other" category contains proteins without clear DBDs they curated from external sources.	a
CisBP considers it as a TF?	Yes
TFclass considers it as a TF?	Yes
Has GO:0003700 "transcription factor activity, sequence-specific DNA binding"	Yes
GO-Info	GO:0003700 sequence-specific DNA binding transcription factor activity IBA - GO_REF:0000033 \| NAS - PMID:9425907
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	2a2, orthologous lower confidence evidence
TF has conditional DNA-binding requirements

DNA-Binding

Published Motif Data

Source	Annotation	Motif	Evidence
Transfac	Transfac	License required	Inferred - Sall1 (100% AA Identity, Mus musculus)
Transfac	Transfac	License required	Inferred - Sall1 (100% AA Identity, Mus musculus)
Transfac	Transfac	License required	Inferred - Sall1 (100% 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 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": 449, "scoreName": "E-value", "accession": "PF00096.24", "start": 449, "score": 2.2999999999999997e-34, "identifier": "Zinc finger, C2H2 type", "type": "DBD", "aliEnd": 471}}, {"startStyle": "curved", "end": 499, "endStyle": "curved", "aliStart": 477, "text": "zfC2H2", "colour": "#228B22", "aliEnd": 499, "start": 477, "href": "http://pfam.xfam.org/family/PF00096.24", "type": "pfama", "display": "true", "metadata": {"end": 499, "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": 477, "scoreName": "E-value", "accession": "PF00096.24", "start": 477, "score": 2.2999999999999997e-34, "identifier": "Zinc finger, C2H2 type", "type": "DBD", "aliEnd": 499}}, {"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": 2.2999999999999997e-34, "identifier": "Zinc finger, C2H2 type", "type": "DBD", "aliEnd": 756}}, {"startStyle": "curved", "end": 788, "endStyle": "curved", "aliStart": 766, "text": "zfC2H2", "colour": "#228B22", "aliEnd": 788, "start": 766, "href": "http://pfam.xfam.org/family/PF00096.24", "type": "pfama", "display": "true", "metadata": {"end": 788, "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": 766, "scoreName": "E-value", "accession": "PF00096.24", "start": 766, "score": 2.2999999999999997e-34, "identifier": "Zinc finger, C2H2 type", "type": "DBD", "aliEnd": 788}}, {"startStyle": "jagged", "end": 1023, "endStyle": "curved", "aliStart": 1003, "text": "zfC2H2", "colour": "#228B22", "aliEnd": 1023, "start": 1001, "href": "http://pfam.xfam.org/family/PF00096.24", "type": "pfama", "display": "true", "metadata": {"end": 1023, "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": 1003, "scoreName": "E-value", "accession": "PF00096.24", "start": 1001, "score": 2.2999999999999997e-34, "identifier": "Zinc finger, C2H2 type", "type": "DBD", "aliEnd": 1023}}, {"startStyle": "curved", "end": 1051, "endStyle": "curved", "aliStart": 1029, "text": "zfC2H2", "colour": "#228B22", "aliEnd": 1051, "start": 1029, "href": "http://pfam.xfam.org/family/PF00096.24", "type": "pfama", "display": "true", "metadata": {"end": 1051, "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": 1029, "scoreName": "E-value", "accession": "PF00096.24", "start": 1029, "score": 2.2999999999999997e-34, "identifier": "Zinc finger, C2H2 type", "type": "DBD", "aliEnd": 1051}}, {"startStyle": "curved", "end": 1156, "endStyle": "curved", "aliStart": 1134, "text": "zfC2H2", "colour": "#228B22", "aliEnd": 1156, "start": 1134, "href": "http://pfam.xfam.org/family/PF00096.24", "type": "pfama", "display": "true", "metadata": {"end": 1156, "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": 1134, "scoreName": "E-value", "accession": "PF00096.24", "start": 1134, "score": 2.2999999999999997e-34, "identifier": "Zinc finger, C2H2 type", "type": "DBD", "aliEnd": 1156}}, {"startStyle": "curved", "end": 1184, "endStyle": "curved", "aliStart": 1162, "text": "zfC2H2", "colour": "#228B22", "aliEnd": 1184, "start": 1162, "href": "http://pfam.xfam.org/family/PF00096.24", "type": "pfama", "display": "true", "metadata": {"end": 1184, "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": 1162, "scoreName": "E-value", "accession": "PF00096.24", "start": 1162, "score": 2.2999999999999997e-34, "identifier": "Zinc finger, C2H2 type", "type": "DBD", "aliEnd": 1184}}, {"startStyle": "straight", "end": 729, "endStyle": "straight", "aliStart": 707, "text": "zf-C2H2_4", "colour": "#9999ff", "aliEnd": 728, "start": 706, "href": "http://pfam.xfam.org/family/PF13894.4", "type": "pfama", "display": "true", "metadata": {"end": 729, "description": "This family contains a number of divergent C2H2 type zinc fingers.", "database": "PfamA", "aliStart": 707, "scoreName": "E-value", "accession": "PF13894.4", "start": 706, "score": 2.3e-33, "identifier": "C2H2-type zinc finger", "type": "DBD", "aliEnd": 728}}, {"startStyle": "jagged", "end": 729, "endStyle": "straight", "aliStart": 708, "text": "zf-met", "colour": "#9999ff", "aliEnd": 728, "start": 707, "href": "http://pfam.xfam.org/family/PF12874.5", "type": "pfama", "display": "true", "metadata": {"end": 729, "description": "This is a zinc-finger domain with the CxxCx(12)Hx(6)H motif, found in multiple copies in a wide range of proteins from plants to metazoans. Some member proteins, particularly those from plants, are annotated as being RNA-binding.", "database": "PfamA", "aliStart": 708, "scoreName": "E-value", "accession": "PF12874.5", "start": 707, "score": 1.5e-27, "identifier": "Zinc-finger of C2H2 type", "type": "DBD", "aliEnd": 728}}, {"startStyle": "jagged", "end": 728, "endStyle": "straight", "aliStart": 707, "text": "zfC2H2", "colour": "#9999ff", "aliEnd": 728, "start": 705, "href": "http://pfam.xfam.org/family/PF12171.6", "type": "pfama", "display": "true", "metadata": {"end": 728, "description": "This domain family is found in archaea and eukaryotes, and is approximately 30 amino acids in length. The mammalian members of this group occur multiple times along the protein, joined by flexible linkers, and are referred to as JAZ - dsRNA-binding ZF protein - zinc-fingers. The JAZ proteins are expressed in all tissues tested and localise in the nucleus, particularly the nucleolus. JAZ preferentially binds to double-stranded (ds) RNA or RNA/DNA hybrids rather than DNA. In addition to binding double-stranded RNA, these zinc-fingers are required for nucleolar localisation.", "database": "PfamA", "aliStart": 707, "scoreName": "E-value", "accession": "PF12171.6", "start": 705, "score": 1.7000000000000002e-25, "identifier": "Zinc-finger double-stranded RNA-binding", "type": "DBD", "aliEnd": 728}}, {"startStyle": "jagged", "end": 732, "endStyle": "jagged", "aliStart": 684, "text": "zf-C2H2_2", "colour": "#9999ff", "aliEnd": 727, "start": 662, "href": "http://pfam.xfam.org/family/PF12756.5", "type": "pfama", "display": "true", "metadata": {"end": 732, "description": "This family contains two copies of a C2H2-like zinc finger domain.", "database": "PfamA", "aliStart": 684, "scoreName": "E-value", "accession": "PF12756.5", "start": 662, "score": 0.00013000000000000002, "identifier": "C2H2 type zinc-finger (2 copies)", "type": "DBD", "aliEnd": 727}}, {"startStyle": "jagged", "end": 734, "endStyle": "straight", "aliStart": 655, "text": "IZUMO", "colour": "#9999ff", "aliEnd": 724, "start": 652, "href": "http://pfam.xfam.org/family/PF15005.4", "type": "pfama", "display": "true", "metadata": {"end": 734, "description": "This IZUMO family is a domain just upstream of the immunoglobulin domain on Izumo proteins in higher eukaryotes.  The actual function of this region of the Izumo proteins is not known. The full-length protein is a molecule with a single immunoglobulin (Ig) domain. It is thought that Izumo proteins bind to putative Izumo receptors on the oocyte.  Izumo is not detectable on the surface of fresh sperm but becomes exposed only after an exocytotic process, the acrosome reaction, has occurred. Studies have shown that knock-out mice (Izumo-/- males) were sterile despite normal mating behaviour and ejaculation, indicating the importance of the protein in fertilisation [1].  There are cysteine residues thought to form a disulphide bridge. Izumo is a typical type I membrane glycoprotein with one immunoglobulin-like domain and a putative N-glycoside link motif (Asn 204) [2]. There is a conserved GCL sequence motif. Izumo expression has been found to be testis-specific [1,2].", "database": "PfamA", "aliStart": 655, "scoreName": "E-value", "accession": "PF15005.4", "start": 652, "score": 0.0044, "identifier": "Izumo sperm-egg fusion, Ig domain-associated", "type": "DBD", "aliEnd": 724}}], "length": 1325}

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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": 637, "scoreName": "E-value", "accession": "PF00096.24", "start": 637, "score": 8.499999999999999e-37, "identifier": "Zinc finger, C2H2 type", "type": "DBD", "aliEnd": 659}}, {"startStyle": "curved", "end": 691, "endStyle": "curved", "aliStart": 669, "text": "zfC2H2", "colour": "#228B22", "aliEnd": 691, "start": 669, "href": "http://pfam.xfam.org/family/PF00096.24", "type": "pfama", "display": "true", "metadata": {"end": 691, "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": 669, "scoreName": "E-value", "accession": "PF00096.24", "start": 669, "score": 8.499999999999999e-37, "identifier": "Zinc finger, C2H2 type", "type": "DBD", "aliEnd": 691}}, {"startStyle": "jagged", "end": 926, "endStyle": "curved", "aliStart": 906, "text": "zfC2H2", "colour": "#228B22", "aliEnd": 926, "start": 904, "href": "http://pfam.xfam.org/family/PF00096.24", "type": "pfama", "display": "true", "metadata": {"end": 926, "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": 906, "scoreName": "E-value", "accession": "PF00096.24", "start": 904, "score": 8.499999999999999e-37, "identifier": "Zinc finger, C2H2 type", "type": "DBD", "aliEnd": 926}}, {"startStyle": "curved", "end": 954, "endStyle": "curved", "aliStart": 932, "text": "zfC2H2", "colour": "#228B22", "aliEnd": 954, "start": 932, "href": "http://pfam.xfam.org/family/PF00096.24", "type": "pfama", "display": "true", "metadata": {"end": 954, "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": 932, "scoreName": "E-value", "accession": "PF00096.24", "start": 932, "score": 8.499999999999999e-37, "identifier": "Zinc finger, C2H2 type", "type": "DBD", "aliEnd": 954}}, {"startStyle": "curved", "end": 1059, "endStyle": "curved", "aliStart": 1037, "text": "zfC2H2", "colour": "#228B22", "aliEnd": 1059, "start": 1037, "href": "http://pfam.xfam.org/family/PF00096.24", "type": "pfama", "display": "true", "metadata": {"end": 1059, "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": 1037, "scoreName": "E-value", "accession": "PF00096.24", "start": 1037, "score": 8.499999999999999e-37, "identifier": "Zinc finger, C2H2 type", "type": "DBD", "aliEnd": 1059}}, {"startStyle": "curved", "end": 1087, "endStyle": "curved", "aliStart": 1065, "text": "zfC2H2", "colour": "#228B22", "aliEnd": 1087, "start": 1065, "href": "http://pfam.xfam.org/family/PF00096.24", "type": "pfama", "display": "true", "metadata": {"end": 1087, "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": 1065, "scoreName": "E-value", "accession": "PF00096.24", "start": 1065, "score": 8.499999999999999e-37, "identifier": "Zinc finger, C2H2 type", "type": "DBD", "aliEnd": 1087}}, {"startStyle": "straight", "end": 632, "endStyle": "straight", "aliStart": 610, "text": "zf-C2H2_4", "colour": "#9999ff", "aliEnd": 631, "start": 609, "href": "http://pfam.xfam.org/family/PF13894.4", "type": "pfama", "display": "true", "metadata": {"end": 632, "description": "This family contains a number of divergent C2H2 type zinc fingers.", "database": "PfamA", "aliStart": 610, "scoreName": "E-value", "accession": "PF13894.4", "start": 609, "score": 2.3999999999999996e-35, "identifier": "C2H2-type zinc finger", "type": "DBD", "aliEnd": 631}}, {"startStyle": "jagged", "end": 632, "endStyle": "straight", "aliStart": 611, "text": "zf-met", "colour": "#9999ff", "aliEnd": 631, "start": 610, "href": "http://pfam.xfam.org/family/PF12874.5", "type": "pfama", "display": "true", "metadata": {"end": 632, "description": "This is a zinc-finger domain with the CxxCx(12)Hx(6)H motif, found in multiple copies in a wide range of proteins from plants to metazoans. Some member proteins, particularly those from plants, are annotated as being RNA-binding.", "database": "PfamA", "aliStart": 611, "scoreName": "E-value", "accession": "PF12874.5", "start": 610, "score": 7.7e-28, "identifier": "Zinc-finger of C2H2 type", "type": "DBD", "aliEnd": 631}}, {"startStyle": "jagged", "end": 631, "endStyle": "straight", "aliStart": 610, "text": "zfC2H2", "colour": "#9999ff", "aliEnd": 631, "start": 608, "href": "http://pfam.xfam.org/family/PF12171.6", "type": "pfama", "display": "true", "metadata": {"end": 631, "description": "This domain family is found in archaea and eukaryotes, and is approximately 30 amino acids in length. The mammalian members of this group occur multiple times along the protein, joined by flexible linkers, and are referred to as JAZ - dsRNA-binding ZF protein - zinc-fingers. The JAZ proteins are expressed in all tissues tested and localise in the nucleus, particularly the nucleolus. JAZ preferentially binds to double-stranded (ds) RNA or RNA/DNA hybrids rather than DNA. In addition to binding double-stranded RNA, these zinc-fingers are required for nucleolar localisation.", "database": "PfamA", "aliStart": 610, "scoreName": "E-value", "accession": "PF12171.6", "start": 608, "score": 8.8e-26, "identifier": "Zinc-finger double-stranded RNA-binding", "type": "DBD", "aliEnd": 631}}, {"startStyle": "jagged", "end": 635, "endStyle": "jagged", "aliStart": 587, "text": "zf-C2H2_2", "colour": "#9999ff", "aliEnd": 630, "start": 565, "href": "http://pfam.xfam.org/family/PF12756.5", "type": "pfama", "display": "true", "metadata": {"end": 635, "description": "This family contains two copies of a C2H2-like zinc finger domain.", "database": "PfamA", "aliStart": 587, "scoreName": "E-value", "accession": "PF12756.5", "start": 565, "score": 9.4e-05, "identifier": "C2H2 type zinc-finger (2 copies)", "type": "DBD", "aliEnd": 630}}, {"startStyle": "jagged", "end": 637, "endStyle": "straight", "aliStart": 558, "text": "IZUMO", "colour": "#9999ff", "aliEnd": 627, "start": 555, "href": "http://pfam.xfam.org/family/PF15005.4", "type": "pfama", "display": "true", "metadata": {"end": 637, "description": "This IZUMO family is a domain just upstream of the immunoglobulin domain on Izumo proteins in higher eukaryotes.  The actual function of this region of the Izumo proteins is not known. The full-length protein is a molecule with a single immunoglobulin (Ig) domain. It is thought that Izumo proteins bind to putative Izumo receptors on the oocyte.  Izumo is not detectable on the surface of fresh sperm but becomes exposed only after an exocytotic process, the acrosome reaction, has occurred. Studies have shown that knock-out mice (Izumo-/- males) were sterile despite normal mating behaviour and ejaculation, indicating the importance of the protein in fertilisation [1].  There are cysteine residues thought to form a disulphide bridge. Izumo is a typical type I membrane glycoprotein with one immunoglobulin-like domain and a putative N-glycoside link motif (Asn 204) [2]. There is a conserved GCL sequence motif. Izumo expression has been found to be testis-specific [1,2].", "database": "PfamA", "aliStart": 558, "scoreName": "E-value", "accession": "PF15005.4", "start": 555, "score": 0.0038, "identifier": "Izumo sperm-egg fusion, Ig domain-associated", "type": "DBD", "aliEnd": 627}}], "length": 1228}

{"regions": [{"startStyle": "curved", "end": 374, "endStyle": "curved", "aliStart": 352, "text": "zfC2H2", "colour": "#228B22", "aliEnd": 374, "start": 352, "href": "http://pfam.xfam.org/family/PF00096.24", "type": "pfama", "display": "true", "metadata": {"end": 374, "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": 352, "scoreName": "E-value", "accession": "PF00096.24", "start": 352, "score": 4.5e-37, "identifier": "Zinc finger, C2H2 type", "type": "DBD", "aliEnd": 374}}, {"startStyle": "curved", "end": 402, "endStyle": "curved", "aliStart": 380, "text": "zfC2H2", "colour": "#228B22", "aliEnd": 402, "start": 380, "href": "http://pfam.xfam.org/family/PF00096.24", "type": "pfama", "display": "true", "metadata": {"end": 402, "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": 380, "scoreName": "E-value", "accession": "PF00096.24", "start": 380, "score": 4.5e-37, "identifier": "Zinc finger, C2H2 type", "type": "DBD", "aliEnd": 402}}, {"startStyle": "curved", "end": 659, "endStyle": "curved", "aliStart": 637, "text": "zfC2H2", "colour": "#228B22", "aliEnd": 659, "start": 637, "href": "http://pfam.xfam.org/family/PF00096.24", "type": "pfama", "display": "true", "metadata": {"end": 659, "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": 637, "scoreName": "E-value", "accession": "PF00096.24", "start": 637, "score": 4.5e-37, "identifier": "Zinc finger, C2H2 type", "type": "DBD", "aliEnd": 659}}, {"startStyle": "curved", "end": 691, "endStyle": "curved", "aliStart": 669, "text": "zfC2H2", "colour": "#228B22", "aliEnd": 691, "start": 669, "href": "http://pfam.xfam.org/family/PF00096.24", "type": "pfama", "display": "true", "metadata": {"end": 691, "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": 669, "scoreName": "E-value", "accession": "PF00096.24", "start": 669, "score": 4.5e-37, "identifier": "Zinc finger, C2H2 type", "type": "DBD", "aliEnd": 691}}, {"startStyle": "jagged", "end": 926, "endStyle": "curved", "aliStart": 906, "text": "zfC2H2", "colour": "#228B22", "aliEnd": 926, "start": 904, "href": "http://pfam.xfam.org/family/PF00096.24", "type": "pfama", "display": "true", "metadata": {"end": 926, "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": 906, "scoreName": "E-value", "accession": "PF00096.24", "start": 904, "score": 4.5e-37, "identifier": "Zinc finger, C2H2 type", "type": "DBD", "aliEnd": 926}}, {"startStyle": "curved", "end": 954, "endStyle": "curved", "aliStart": 932, "text": "zfC2H2", "colour": "#228B22", "aliEnd": 954, "start": 932, "href": "http://pfam.xfam.org/family/PF00096.24", "type": "pfama", "display": "true", "metadata": {"end": 954, "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": 932, "scoreName": "E-value", "accession": "PF00096.24", "start": 932, "score": 4.5e-37, "identifier": "Zinc finger, C2H2 type", "type": "DBD", "aliEnd": 954}}, {"startStyle": "curved", "end": 1059, "endStyle": "curved", "aliStart": 1037, "text": "zfC2H2", "colour": "#228B22", "aliEnd": 1059, "start": 1037, "href": "http://pfam.xfam.org/family/PF00096.24", "type": "pfama", "display": "true", "metadata": {"end": 1059, "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": 1037, "scoreName": "E-value", "accession": "PF00096.24", "start": 1037, "score": 4.5e-37, "identifier": "Zinc finger, C2H2 type", "type": "DBD", "aliEnd": 1059}}, {"startStyle": "curved", "end": 1087, "endStyle": "curved", "aliStart": 1065, "text": "zfC2H2", "colour": "#228B22", "aliEnd": 1087, "start": 1065, "href": "http://pfam.xfam.org/family/PF00096.24", "type": "pfama", "display": "true", "metadata": {"end": 1087, "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": 1065, "scoreName": "E-value", "accession": "PF00096.24", "start": 1065, "score": 4.5e-37, "identifier": "Zinc finger, C2H2 type", "type": "DBD", "aliEnd": 1087}}, {"startStyle": "straight", "end": 632, "endStyle": "straight", "aliStart": 610, "text": "zf-C2H2_4", "colour": "#9999ff", "aliEnd": 631, "start": 609, "href": "http://pfam.xfam.org/family/PF13894.4", "type": "pfama", "display": "true", "metadata": {"end": 632, "description": "This family contains a number of divergent C2H2 type zinc fingers.", "database": "PfamA", "aliStart": 610, "scoreName": "E-value", "accession": "PF13894.4", "start": 609, "score": 1.2999999999999998e-35, "identifier": "C2H2-type zinc finger", "type": "DBD", "aliEnd": 631}}, {"startStyle": "jagged", "end": 632, "endStyle": "straight", "aliStart": 611, "text": "zf-met", "colour": "#9999ff", "aliEnd": 631, "start": 610, "href": "http://pfam.xfam.org/family/PF12874.5", "type": "pfama", "display": "true", "metadata": {"end": 632, "description": "This is a zinc-finger domain with the CxxCx(12)Hx(6)H motif, found in multiple copies in a wide range of proteins from plants to metazoans. Some member proteins, particularly those from plants, are annotated as being RNA-binding.", "database": "PfamA", "aliStart": 611, "scoreName": "E-value", "accession": "PF12874.5", "start": 610, "score": 4.2e-28, "identifier": "Zinc-finger of C2H2 type", "type": "DBD", "aliEnd": 631}}, {"startStyle": "jagged", "end": 631, "endStyle": "straight", "aliStart": 610, "text": "zfC2H2", "colour": "#9999ff", "aliEnd": 631, "start": 608, "href": "http://pfam.xfam.org/family/PF12171.6", "type": "pfama", "display": "true", "metadata": {"end": 631, "description": "This domain family is found in archaea and eukaryotes, and is approximately 30 amino acids in length. The mammalian members of this group occur multiple times along the protein, joined by flexible linkers, and are referred to as JAZ - dsRNA-binding ZF protein - zinc-fingers. The JAZ proteins are expressed in all tissues tested and localise in the nucleus, particularly the nucleolus. JAZ preferentially binds to double-stranded (ds) RNA or RNA/DNA hybrids rather than DNA. In addition to binding double-stranded RNA, these zinc-fingers are required for nucleolar localisation.", "database": "PfamA", "aliStart": 610, "scoreName": "E-value", "accession": "PF12171.6", "start": 608, "score": 4.8e-26, "identifier": "Zinc-finger double-stranded RNA-binding", "type": "DBD", "aliEnd": 631}}, {"startStyle": "jagged", "end": 635, "endStyle": "jagged", "aliStart": 587, "text": "zf-C2H2_2", "colour": "#9999ff", "aliEnd": 630, "start": 565, "href": "http://pfam.xfam.org/family/PF12756.5", "type": "pfama", "display": "true", "metadata": {"end": 635, "description": "This family contains two copies of a C2H2-like zinc finger domain.", "database": "PfamA", "aliStart": 587, "scoreName": "E-value", "accession": "PF12756.5", "start": 565, "score": 5.7999999999999994e-05, "identifier": "C2H2 type zinc-finger (2 copies)", "type": "DBD", "aliEnd": 630}}, {"startStyle": "jagged", "end": 637, "endStyle": "straight", "aliStart": 558, "text": "IZUMO", "colour": "#9999ff", "aliEnd": 627, "start": 555, "href": "http://pfam.xfam.org/family/PF15005.4", "type": "pfama", "display": "true", "metadata": {"end": 637, "description": "This IZUMO family is a domain just upstream of the immunoglobulin domain on Izumo proteins in higher eukaryotes.  The actual function of this region of the Izumo proteins is not known. The full-length protein is a molecule with a single immunoglobulin (Ig) domain. It is thought that Izumo proteins bind to putative Izumo receptors on the oocyte.  Izumo is not detectable on the surface of fresh sperm but becomes exposed only after an exocytotic process, the acrosome reaction, has occurred. Studies have shown that knock-out mice (Izumo-/- males) were sterile despite normal mating behaviour and ejaculation, indicating the importance of the protein in fertilisation [1].  There are cysteine residues thought to form a disulphide bridge. Izumo is a typical type I membrane glycoprotein with one immunoglobulin-like domain and a putative N-glycoside link motif (Asn 204) [2]. There is a conserved GCL sequence motif. Izumo expression has been found to be testis-specific [1,2].", "database": "PfamA", "aliStart": 558, "scoreName": "E-value", "accession": "PF15005.4", "start": 555, "score": 0.0033, "identifier": "Izumo sperm-egg fusion, Ig domain-associated", "type": "DBD", "aliEnd": 627}}], "length": 1154}

TF Info Page for SALL1 (C2H2 ZF(non-KRAB))