The Human Transcription Factors

Conclusion

Assessment	Binding Mode	Motif Status	Notes	Comments
Known motif	1 Monomer or homomultimer	High-throughput in vitro	ChIP-seq motif is consistent with recognition code (RCADE)

Description

Description:

PR domain 9 [Source:HGNC Symbol;Acc:HGNC:13994]

Entrez Summary

The protein encoded by this gene is a zinc finger protein with histone methyltransferase activity that catalyzes histone H3 lysine 4 trimethylation (H3K4me3) during meiotic prophase. This protein contains multiple domains, including a Kruppel-associated box (KRAB) domain, an SSX repression domain (SSXRD), a PRD1-BF1 and RIZ homologous region, a subclass of SET (PR/SET) domain, and a tandem array of C2H2 zinc fingers. The zinc finger array recognizes a short sequence motif, leading to local H3K4me3, and meiotic recombination hotspot activity. The observed allelic variation alters the DNA-binding sequence specificity of the protein, resulting in distinct meiotic recombination hotspots amongst individuals and populations. Multiple alternate alleles of this gene have been described. [provided by RefSeq, Jul 2015]

Ensembl ID:

ENSG00000164256

External Link:

CisBP

Interpro

IPR001214; IPR001909; IPR003655; IPR007087; IPR015880; IPR019041;

Protein Domain:

ENSP00000296682

Protein Domain:

ENSP00000425471

Protein Domain:

ENSP00000489227

Domain:

Protein: ENSP00000296682	DBD: C2H2 ZF Containing Proteins	Other: KRAB, SET, SSXRD, zf-C2H2_4
Protein: ENSP00000425471	DBD: C2H2 ZF Containing Proteins	Other: KRAB, Phage_F
Protein: ENSP00000489227	DBD: C2H2 ZF Containing Proteins	Other: SET, SSXRD

Previous Annotations

Source	Annotation
TF-CAT classification	No PMIDS:
Vaquerizas 2009 TF classification "a" Has direct evidence of TF function; "b" Has evidence for an orthologous TF; "c" contains likely DBDs, but has no functional evidence; "x" is an unlikely TF such as predicted gene, genes with likely non-specific DBDs or that have function outside transcription; "other" category contains proteins without clear DBDs they curated from external sources.	b
CisBP considers it as a TF?	Yes
TFclass considers it as a TF?	Yes
Has GO:0003700 "transcription factor activity, sequence-specific DNA binding"	No
GO-Info
Initial Assessment 1a1 Protein has a high confidence PWM (HT-SELEX, PBM or B1H model) or there is a crystal structure that supports sequence specific DNA binding; 1a2 There is high confidence data for a close ortholog (as defined in CisBP); 2a1 There is lower confidence direct evidence, such as a Jaspar, Hocomoco or Transfac model; 2a2 There is lower confidence evidence for an close ortholog; 3a There is decent circumstantial evidence for its role as a TF or not; 4a Two or more datasets predict it as a TF; 5a One of the source datasets predicts is as a TF	1a1, Direct HQ evidence
TF has conditional DNA-binding requirements

DNA-Binding

Published Motif Data

Source	Annotation	Motif	Evidence
RCADE	Imbeault2017		Direct - consistent with recognition code (RCADE)

Structure

Structure	PDB	5EGB

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

{"regions": [{"startStyle": "jagged", "end": 546, "endStyle": "curved", "aliStart": 528, "text": "zfC2H2", "colour": "#228B22", "aliEnd": 546, "start": 527, "href": "http://pfam.xfam.org/family/PF00096.24", "type": "pfama", "display": "true", "metadata": {"end": 546, "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": 528, "scoreName": "E-value", "accession": "PF00096.24", "start": 527, "score": 1.3999999999999997e-64, "identifier": "Zinc finger, C2H2 type", "type": "DBD", "aliEnd": 546}}, {"startStyle": "curved", "end": 574, "endStyle": "curved", "aliStart": 552, "text": "zfC2H2", "colour": "#228B22", "aliEnd": 574, "start": 552, "href": "http://pfam.xfam.org/family/PF00096.24", "type": "pfama", "display": "true", "metadata": {"end": 574, "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": 552, "scoreName": "E-value", "accession": "PF00096.24", "start": 552, "score": 1.3999999999999997e-64, "identifier": "Zinc finger, C2H2 type", "type": "DBD", "aliEnd": 574}}, {"startStyle": "curved", "end": 602, "endStyle": "curved", "aliStart": 580, "text": "zfC2H2", "colour": "#228B22", "aliEnd": 602, "start": 580, "href": "http://pfam.xfam.org/family/PF00096.24", "type": "pfama", "display": "true", "metadata": {"end": 602, "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": 580, "scoreName": "E-value", "accession": "PF00096.24", "start": 580, "score": 1.3999999999999997e-64, "identifier": "Zinc finger, C2H2 type", "type": "DBD", "aliEnd": 602}}, {"startStyle": "curved", "end": 630, "endStyle": "curved", "aliStart": 608, "text": "zfC2H2", "colour": "#228B22", "aliEnd": 630, "start": 608, "href": "http://pfam.xfam.org/family/PF00096.24", "type": "pfama", "display": "true", "metadata": {"end": 630, "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": 608, "scoreName": "E-value", "accession": "PF00096.24", "start": 608, "score": 1.3999999999999997e-64, "identifier": "Zinc finger, C2H2 type", "type": "DBD", "aliEnd": 630}}, {"startStyle": "curved", "end": 658, "endStyle": "curved", "aliStart": 636, "text": "zfC2H2", "colour": "#228B22", "aliEnd": 658, "start": 636, "href": "http://pfam.xfam.org/family/PF00096.24", "type": "pfama", "display": "true", "metadata": {"end": 658, "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": 636, "scoreName": "E-value", "accession": "PF00096.24", "start": 636, "score": 1.3999999999999997e-64, "identifier": "Zinc finger, C2H2 type", "type": "DBD", "aliEnd": 658}}, {"startStyle": "curved", "end": 686, "endStyle": "curved", "aliStart": 664, "text": "zfC2H2", "colour": "#228B22", "aliEnd": 686, "start": 664, "href": "http://pfam.xfam.org/family/PF00096.24", "type": "pfama", "display": "true", "metadata": {"end": 686, "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": 664, "scoreName": "E-value", "accession": "PF00096.24", "start": 664, "score": 1.3999999999999997e-64, "identifier": "Zinc finger, C2H2 type", "type": "DBD", "aliEnd": 686}}, {"startStyle": "curved", "end": 714, "endStyle": "curved", "aliStart": 692, "text": "zfC2H2", "colour": "#228B22", "aliEnd": 714, "start": 692, "href": "http://pfam.xfam.org/family/PF00096.24", "type": "pfama", "display": "true", "metadata": {"end": 714, "description": "The C2H2 zinc finger is the classical zinc finger domain. The two conserved cysteines and histidines co-ordinate a zinc ion. The following pattern describes the zinc finger. #-X-C-X(1-5)-C-X3-#-X5-#-X2-H-X(3-6)-[H/C] Where X can be any amino acid, and numbers in brackets indicate the number of residues. The positions marked # are those that are important for the stable fold of the zinc finger. The final position can be either his or cys. The C2H2 zinc finger is composed of two short beta strands followed by an alpha helix. The amino terminal part of the helix binds the major groove in DNA binding zinc fingers. 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The following pattern describes the zinc finger. #-X-C-X(1-5)-C-X3-#-X5-#-X2-H-X(3-6)-[H/C] Where X can be any amino acid, and numbers in brackets indicate the number of residues. The positions marked # are those that are important for the stable fold of the zinc finger. The final position can be either his or cys. The C2H2 zinc finger is composed of two short beta strands followed by an alpha helix. The amino terminal part of the helix binds the major groove in DNA binding zinc fingers. 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": 720, "scoreName": "E-value", "accession": "PF00096.24", "start": 720, "score": 1.3999999999999997e-64, "identifier": "Zinc finger, C2H2 type", "type": "DBD", "aliEnd": 742}}, {"startStyle": "curved", "end": 770, "endStyle": "curved", "aliStart": 748, "text": "zfC2H2", "colour": "#228B22", "aliEnd": 770, "start": 748, "href": "http://pfam.xfam.org/family/PF00096.24", "type": "pfama", "display": "true", "metadata": {"end": 770, "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": 748, "scoreName": "E-value", "accession": "PF00096.24", "start": 748, "score": 1.3999999999999997e-64, "identifier": "Zinc finger, C2H2 type", "type": "DBD", "aliEnd": 770}}, {"startStyle": "curved", "end": 798, "endStyle": "curved", "aliStart": 776, "text": "zfC2H2", "colour": "#228B22", "aliEnd": 798, "start": 776, "href": "http://pfam.xfam.org/family/PF00096.24", "type": "pfama", "display": "true", "metadata": {"end": 798, "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": 776, "scoreName": "E-value", "accession": "PF00096.24", "start": 776, "score": 1.3999999999999997e-64, "identifier": "Zinc finger, C2H2 type", "type": "DBD", "aliEnd": 798}}, {"startStyle": "curved", "end": 826, "endStyle": "curved", "aliStart": 804, "text": "zfC2H2", "colour": "#228B22", "aliEnd": 826, "start": 804, "href": "http://pfam.xfam.org/family/PF00096.24", "type": "pfama", "display": "true", "metadata": {"end": 826, "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": 804, "scoreName": "E-value", "accession": "PF00096.24", "start": 804, "score": 1.3999999999999997e-64, "identifier": "Zinc finger, C2H2 type", "type": "DBD", "aliEnd": 826}}, {"startStyle": "curved", "end": 854, "endStyle": "curved", "aliStart": 832, "text": "zfC2H2", "colour": "#228B22", "aliEnd": 854, "start": 832, "href": "http://pfam.xfam.org/family/PF00096.24", "type": "pfama", "display": "true", "metadata": {"end": 854, "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": 832, "scoreName": "E-value", "accession": "PF00096.24", "start": 832, "score": 1.3999999999999997e-64, "identifier": "Zinc finger, C2H2 type", "type": "DBD", "aliEnd": 854}}, {"startStyle": "curved", "end": 882, "endStyle": "curved", "aliStart": 860, "text": "zfC2H2", "colour": "#228B22", "aliEnd": 882, "start": 860, "href": "http://pfam.xfam.org/family/PF00096.24", "type": "pfama", "display": "true", "metadata": {"end": 882, "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": 860, "scoreName": "E-value", "accession": "PF00096.24", "start": 860, "score": 1.3999999999999997e-64, "identifier": "Zinc finger, C2H2 type", "type": "DBD", "aliEnd": 882}}, {"startStyle": "straight", "end": 411, "endStyle": "straight", "aliStart": 388, "text": "zf-C2H2_4", "colour": "#9999ff", "aliEnd": 411, "start": 388, "href": "http://pfam.xfam.org/family/PF13894.4", "type": "pfama", "display": "true", "metadata": {"end": 411, "description": "This family contains a number of divergent C2H2 type zinc fingers.", "database": "PfamA", "aliStart": 388, "scoreName": "E-value", "accession": "PF13894.4", "start": 388, "score": 5.9e-44, "identifier": "C2H2-type zinc finger", "type": "DBD", "aliEnd": 411}}, {"startStyle": "straight", "end": 201, "endStyle": "straight", "aliStart": 171, "text": "SSXRD", "colour": "#9999ff", "aliEnd": 201, "start": 171, "href": "http://pfam.xfam.org/family/PF09514.8", "type": "pfama", "display": "true", "metadata": {"end": 201, "description": "SSX1 can repress transcription, and this has been attributed to a putative Kruppel associated box (KRAB) repression domain at the N-terminus. However, from the analysis of these deletion constructs further repression activity was found at the C-terminus of SSX1. Which has been called the SSXRD (SSX Repression Domain). The potent repression exerted by full-length SSX1 appears to localise to this region [1].", "database": "PfamA", "aliStart": 171, "scoreName": "E-value", "accession": "PF09514.8", "start": 171, "score": 2.7e-15, "identifier": "SSXRD motif", "type": "DBD", "aliEnd": 201}}, {"startStyle": "straight", "end": 65, "endStyle": "straight", "aliStart": 27, "text": "KRAB", "colour": "#9999ff", "aliEnd": 65, "start": 27, "href": "http://pfam.xfam.org/family/PF01352.25", "type": "pfama", "display": "true", "metadata": {"end": 65, "description": "The KRAB domain (or Kruppel-associated box) is present in about a third of zinc finger proteins containing C2H2 fingers.  The KRAB domain is found to be involved in protein-protein interactions [2,3].  The KRAB domain is generally encoded by two exons.  The regions coded by the two exons are known as KRAB-A and KRAB-B. The A box plays an important role in repression by binding to corepressors, while the B box is thought to enhance this repression brought about by the A box. KRAB-containing proteins are thought to have critical functions in cell proliferation and differentiation, apoptosis and neoplastic transformation [4].", "database": "PfamA", "aliStart": 27, "scoreName": "E-value", "accession": "PF01352.25", "start": 27, "score": 3.5e-07, "identifier": "KRAB box", "type": "DBD", "aliEnd": 65}}, {"startStyle": "jagged", "end": 358, "endStyle": "straight", "aliStart": 194, "text": "SET", "colour": "#9999ff", "aliEnd": 358, "start": 33, "href": "http://pfam.xfam.org/family/PF00856.26", "type": "pfama", "display": "true", "metadata": {"end": 358, "description": "SET domains are protein lysine methyltransferase enzymes. SET domains appear to be protein-protein interaction domains. It has been demonstrated that SET domains mediate interactions with a family of proteins that display similarity with dual-specificity phosphatases (dsPTPases) [2].  A subset of SET domains have been called PR domains.  These domains are divergent in sequence from other SET domains, but also appear to mediate protein-protein interaction [3].  The SET domain consists of two regions known as SET-N and SET-C.  SET-C forms an unusual and conserved knot-like structure of probably functional importance.  Additionally to SET-N and SET-C, an insert region (SET-I) and flanking regions of high structural variability form part of the overall structure [5].", "database": "PfamA", "aliStart": 194, "scoreName": "E-value", "accession": "PF00856.26", "start": 33, "score": 4.6e-06, "identifier": "SET domain", "type": "DBD", "aliEnd": 358}}], "length": 895}

{"regions": [{"startStyle": "straight", "end": 65, "endStyle": "straight", "aliStart": 27, "text": "KRAB", "colour": "#9999ff", "aliEnd": 65, "start": 27, "href": "http://pfam.xfam.org/family/PF01352.25", "type": "pfama", "display": "true", "metadata": {"end": 65, "description": "The KRAB domain (or Kruppel-associated box) is present in about a third of zinc finger proteins containing C2H2 fingers.  The KRAB domain is found to be involved in protein-protein interactions [2,3].  The KRAB domain is generally encoded by two exons.  The regions coded by the two exons are known as KRAB-A and KRAB-B. The A box plays an important role in repression by binding to corepressors, while the B box is thought to enhance this repression brought about by the A box. KRAB-containing proteins are thought to have critical functions in cell proliferation and differentiation, apoptosis and neoplastic transformation [4].", "database": "PfamA", "aliStart": 27, "scoreName": "E-value", "accession": "PF01352.25", "start": 27, "score": 1.8e-08, "identifier": "KRAB box", "type": "DBD", "aliEnd": 65}}, {"startStyle": "jagged", "end": 100, "endStyle": "jagged", "aliStart": 35, "text": "Phage_F", "colour": "#9999ff", "aliEnd": 97, "start": 28, "href": "http://pfam.xfam.org/family/PF02305.15", "type": "pfama", "display": "true", "metadata": {"end": 100, "description": "This is a family of proteins from single-stranded DNA bacteriophages. Protein F is the major capsid component, sixty copies of which are found in the virion.", "database": "PfamA", "aliStart": 35, "scoreName": "E-value", "accession": "PF02305.15", "start": 28, "score": 0.00066, "identifier": "Capsid protein (F protein)", "type": "DBD", "aliEnd": 97}}], "length": 100}

{"regions": [{"startStyle": "straight", "end": 142, "endStyle": "straight", "aliStart": 112, "text": "SSXRD", "colour": "#9999ff", "aliEnd": 142, "start": 112, "href": "http://pfam.xfam.org/family/PF09514.8", "type": "pfama", "display": "true", "metadata": {"end": 142, "description": "SSX1 can repress transcription, and this has been attributed to a putative Kruppel associated box (KRAB) repression domain at the N-terminus. However, from the analysis of these deletion constructs further repression activity was found at the C-terminus of SSX1. Which has been called the SSXRD (SSX Repression Domain). The potent repression exerted by full-length SSX1 appears to localise to this region [1].", "database": "PfamA", "aliStart": 112, "scoreName": "E-value", "accession": "PF09514.8", "start": 112, "score": 1.4e-15, "identifier": "SSXRD motif", "type": "DBD", "aliEnd": 142}}, {"startStyle": "jagged", "end": 299, "endStyle": "straight", "aliStart": 130, "text": "SET", "colour": "#9999ff", "aliEnd": 299, "start": 11, "href": "http://pfam.xfam.org/family/PF00856.26", "type": "pfama", "display": "true", "metadata": {"end": 299, "description": "SET domains are protein lysine methyltransferase enzymes. SET domains appear to be protein-protein interaction domains. It has been demonstrated that SET domains mediate interactions with a family of proteins that display similarity with dual-specificity phosphatases (dsPTPases) [2].  A subset of SET domains have been called PR domains.  These domains are divergent in sequence from other SET domains, but also appear to mediate protein-protein interaction [3].  The SET domain consists of two regions known as SET-N and SET-C.  SET-C forms an unusual and conserved knot-like structure of probably functional importance.  Additionally to SET-N and SET-C, an insert region (SET-I) and flanking regions of high structural variability form part of the overall structure [5].", "database": "PfamA", "aliStart": 130, "scoreName": "E-value", "accession": "PF00856.26", "start": 11, "score": 9.5e-07, "identifier": "SET domain", "type": "DBD", "aliEnd": 299}}], "length": 411}

TF Info Page for PRDM9 (C2H2 ZF(KRAB))

Conclusion

Description

Previous Annotations

DNA-Binding

Published Motif Data

Structure

Experimental History

External Contribution