Conclusion
Assessment
Binding Mode
Motif Status
Notes
Comments
Known motif
1 Monomer or homomultimer
High-throughput in vitro
Description
Description:
Kruppel like factor 1 [Source:HGNC Symbol;Acc:HGNC:6345]
Entrez Summary
TBA
Ensembl ID:
ENSG00000105610
External Link:
T044277_1.02
Interpro
IPR007087 ; IPR015880 ;
Protein Domain:
Protein: ENSP00000264834DBD: C2H2 ZF Containing ProteinsOther: EKLF_TAD1, EKLF_TAD2
Previous Annotations
Source
Annotation
TF-CAT classification
TF Gene_DNA-Binding sequence-specific_DNA Binding Transactivation_ PMIDS:11092887
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 TAS - PMID:8924208, PMID:9778250
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
Structure
Experimental History
{"regions": [{"startStyle": "curved", "end": 303, "endStyle": "curved", "aliStart": 279, "text": "zfC2H2", "colour": "#228B22", "aliEnd": 303, "start": 279, "href": "http://pfam.xfam.org/family/PF00096.24", "type": "pfama", "display": "true", "metadata": {"end": 303, "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": 279, "scoreName": "E-value", "accession": "PF00096.24", "start": 279, "score": 2.6e-16, "identifier": "Zinc finger, C2H2 type", "type": "DBD", "aliEnd": 303}}, {"startStyle": "curved", "end": 333, "endStyle": "curved", "aliStart": 309, "text": "zfC2H2", "colour": "#228B22", "aliEnd": 333, "start": 309, "href": "http://pfam.xfam.org/family/PF00096.24", "type": "pfama", "display": "true", "metadata": {"end": 333, "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": 309, "scoreName": "E-value", "accession": "PF00096.24", "start": 309, "score": 2.6e-16, "identifier": "Zinc finger, C2H2 type", "type": "DBD", "aliEnd": 333}}, {"startStyle": "curved", "end": 361, "endStyle": "curved", "aliStart": 339, "text": "zfC2H2", "colour": "#228B22", "aliEnd": 361, "start": 339, "href": "http://pfam.xfam.org/family/PF00096.24", "type": "pfama", "display": "true", "metadata": {"end": 361, "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": 339, "scoreName": "E-value", "accession": "PF00096.24", "start": 339, "score": 2.6e-16, "identifier": "Zinc finger, C2H2 type", "type": "DBD", "aliEnd": 361}}, {"startStyle": "straight", "end": 48, "endStyle": "straight", "aliStart": 22, "text": "EKLF_TAD1", "colour": "#9999ff", "aliEnd": 47, "start": 22, "href": "http://pfam.xfam.org/family/PF16832.3", "type": "pfama", "display": "true", "metadata": {"end": 48, "description": "This family is the first part of the minimal transactivation domain of erythroid-specific transcription factor EKFL in craniates. EKLF plays an important role in red blood cell development; it is posttranslationally modified by UBI on several lysine residues, and its turnover in the cell is regulated by ubiquitin-mediated degradation. In the first 90 residues at the N-terminus EKLF carries a minimal transactivation or TAD domain that is highly acidic. This minimal TAD of EKLF can be further subdivided into two independent domains EKLF_TAD1 (residues 1-40) and EKLF_TAD2 (residues 51-90), Pfam:PF16833, that are both capable of independently activating transcription. TAD1, is able to form a non-covalent interaction with ubiquitin. Both TAD1 and TAd2 are highly acidic and carry a PEST (sequence rich in proline, glutamic acid, serine, and threonine) region. Deletion of either PEST domain significantly slows down degradation of EKLF by ubiquitin. The minimal TAD has an overlapping activation/degradation function that is critical for the role of EKLF in red blood cell development [1].", "database": "PfamA", "aliStart": 22, "scoreName": "E-value", "accession": "PF16832.3", "start": 22, "score": 9.8e-18, "identifier": "Erythroid krueppel-like transcription factor, transactivation 1", "type": "DBD", "aliEnd": 47}}, {"startStyle": "straight", "end": 85, "endStyle": "straight", "aliStart": 59, "text": "EKLF_TAD2", "colour": "#9999ff", "aliEnd": 85, "start": 59, "href": "http://pfam.xfam.org/family/PF16833.3", "type": "pfama", "display": "true", "metadata": {"end": 85, "description": "This family is the second part of the minimal transactivation domain of erythroid-specific transcription factor EKFL in craniates. EKLF plays an important role in red blood cell development; it is post-translationally modified by ubiquitin on several lysine residues, and its turnover in the cell is regulated by ubiquitin-mediated degradation. In the first 90 residues at the N-terminus EKLF carries a minimal transactivation or TAD domain that is highly acidic. This minimal TAD of EKLF can be further subdivided into two independent domains EKLF_TAD1 (residues 1-40), Pfam:PF16832, and EKLF_TAD2 (residues 51-90) that are both capable of independently activating transcription. Both TAD1 and TAD2 are highly acidic and carry a PEST (sequence rich in proline, glutamic acid, serine, and threonine) region. Deletion of either PEST domain significantly slows down degradation of EKLF by ubiquitin. The minimal TAD has an overlapping activation/degradation function that is critical for the role of EKLF in red blood cell development [1].", "database": "PfamA", "aliStart": 59, "scoreName": "E-value", "accession": "PF16833.3", "start": 59, "score": 3.1e-15, "identifier": "Erythroid krueppel-like transcription factor, transactivation 2", "type": "DBD", "aliEnd": 85}}], "length": 363}