Conclusion
Assessment
Binding Mode
Motif Status
Notes
Comments
Inferred motif
1 Monomer or homomultimer
High-throughput in vitro
Might also bind RNA
Description
Description:
lin-28 homolog A [Source:HGNC Symbol;Acc:HGNC:15986]
Entrez Summary
TBA
Ensembl ID:
ENSG00000131914
External Link:
T072272_1.02
Interpro
IPR001878 ; IPR002059 ; IPR011129 ; IPR012340 ;
Protein Domain:
Protein: ENSP00000254231DBD: Cold-shock protein, DNA-bindingOther: zf-CCHCProtein: ENSP00000363314DBD: Cold-shock protein, DNA-bindingOther: zf-CCHC
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.
x
CisBP considers it as a TF?
Yes
TFclass considers it as a TF?
No
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
4a, two or more datasets predict it as a TF
TF has conditional DNA-binding requirements
DNA-Binding
Published Motif Data
Structure
Experimental History
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{"regions": [{"startStyle": "curved", "end": 112, "endStyle": "curved", "aliStart": 42, "text": "CSD", "colour": "#228B22", "aliEnd": 111, "start": 40, "href": "http://pfam.xfam.org/family/PF00313.20", "type": "pfama", "display": "true", "metadata": {"end": 112, "description": "In molecular biology, the cold-shock domain (CSD) is a protein domain of about 70 amino acids which has been found in prokaryotic and eukaryotic DNA-binding proteins.", "database": "PfamA", "aliStart": 42, "scoreName": "E-value", "accession": "PF00313.20", "start": 40, "score": 8.8e-17, "identifier": "'Cold-shock' DNA-binding domain", "type": "DBD", "aliEnd": 111}}, {"startStyle": "jagged", "end": 154, "endStyle": "straight", "aliStart": 138, "text": "zf-CCHC", "colour": "#9999ff", "aliEnd": 153, "start": 137, "href": "http://pfam.xfam.org/family/PF00098.21", "type": "pfama", "display": "true", "metadata": {"end": 154, "description": "The zinc knuckle is a zinc binding motif composed of the the following CX2CX4HX4C where X can be any amino acid. The motifs are mostly from retroviral gag proteins (nucleocapsid). Prototype structure is from HIV. Also contains members involved in eukaryotic gene regulation, such as C. elegans GLH-1. Structure is an 18-residue zinc finger.", "database": "PfamA", "aliStart": 138, "scoreName": "E-value", "accession": "PF00098.21", "start": 137, "score": 6.7e-07, "identifier": "Zinc knuckle", "type": "DBD", "aliEnd": 153}}, {"startStyle": "straight", "end": 176, "endStyle": "straight", "aliStart": 159, "text": "zf-CCHC", "colour": "#9999ff", "aliEnd": 175, "start": 159, "href": "http://pfam.xfam.org/family/PF00098.21", "type": "pfama", "display": "true", "metadata": {"end": 176, "description": "The zinc knuckle is a zinc binding motif composed of the the following CX2CX4HX4C where X can be any amino acid. The motifs are mostly from retroviral gag proteins (nucleocapsid). Prototype structure is from HIV. Also contains members involved in eukaryotic gene regulation, such as C. elegans GLH-1. Structure is an 18-residue zinc finger.", "database": "PfamA", "aliStart": 159, "scoreName": "E-value", "accession": "PF00098.21", "start": 159, "score": 6.7e-07, "identifier": "Zinc knuckle", "type": "DBD", "aliEnd": 175}}], "length": 210}