Conclusion
Assessment
Binding Mode
Motif Status
Notes
Comments
Likely to be sequence specific TF
3 Low specificity DNA-binding protein
No motif
Description
Description:
peptidylprolyl cis/trans isomerase, NIMA-interacting 1 [Source:HGNC Symbol;Acc:HGNC:8988]
Entrez Summary
TBA
Ensembl ID:
ENSG00000127445
External Link:
Interpro
IPR000297 ; IPR001202 ; IPR023058 ;
Protein Domain:
Protein: ENSP00000247970DBD: Methyl-CpG DNA-bindingOther: Rotamase, Rotamase_2, Rotamase_3, WWProtein: ENSP00000466656DBD: Methyl-CpG DNA-bindingOther: Rotamase, Rotamase_3, WWProtein: ENSP00000466962DBD: Methyl-CpG DNA-bindingOther: Rotamase, Rotamase_2, Rotamase_3, WW
Previous Annotations
Source
Annotation
TF-CAT classification
TF Gene_Transcription Factor Binding tf co-factor binding_TF PPI_ PMIDS:16227615
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.
No
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
{"regions": [{"startStyle": "straight", "end": 163, "endStyle": "straight", "aliStart": 59, "text": "Rotamase", "colour": "#9999ff", "aliEnd": 162, "start": 59, "href": "http://pfam.xfam.org/family/PF00639.19", "type": "pfama", "display": "true", "metadata": {"end": 163, "description": "Rotamases increase the rate of protein folding by catalysing the interconversion of cis-proline and trans-proline.", "database": "PfamA", "aliStart": 59, "scoreName": "E-value", "accession": "PF00639.19", "start": 59, "score": 9e-24, "identifier": "PPIC-type PPIASE domain", "type": "DBD", "aliEnd": 162}}, {"startStyle": "jagged", "end": 163, "endStyle": "straight", "aliStart": 51, "text": "Rotamase_3", "colour": "#9999ff", "aliEnd": 159, "start": 42, "href": "http://pfam.xfam.org/family/PF13616.4", "type": "pfama", "display": "true", "metadata": {"end": 163, "description": "Rotamases increase the rate of protein folding by catalysing the interconversion of cis-proline and trans-proline.", "database": "PfamA", "aliStart": 51, "scoreName": "E-value", "accession": "PF13616.4", "start": 42, "score": 1.2e-21, "identifier": "PPIC-type PPIASE domain", "type": "DBD", "aliEnd": 159}}, {"startStyle": "straight", "end": 37, "endStyle": "straight", "aliStart": 7, "text": "WW", "colour": "#9999ff", "aliEnd": 37, "start": 7, "href": "http://pfam.xfam.org/family/PF00397.24", "type": "pfama", "display": "true", "metadata": {"end": 37, "description": "The WW domain is a protein module with two highly conserved tryptophans that binds proline-rich peptide motifs in vitro.", "database": "PfamA", "aliStart": 7, "scoreName": "E-value", "accession": "PF00397.24", "start": 7, "score": 2.9e-15, "identifier": "WW domain", "type": "DBD", "aliEnd": 37}}, {"startStyle": "jagged", "end": 163, "endStyle": "jagged", "aliStart": 84, "text": "Rotamase_2", "colour": "#9999ff", "aliEnd": 162, "start": 65, "href": "http://pfam.xfam.org/family/PF13145.4", "type": "pfama", "display": "true", "metadata": {"end": 163, "description": NaN, "database": "PfamA", "aliStart": 84, "scoreName": "E-value", "accession": "PF13145.4", "start": 65, "score": 0.00033, "identifier": "PPIC-type PPIASE domain", "type": "DBD", "aliEnd": 162}}], "length": 164}
{"regions": [{"startStyle": "straight", "end": 37, "endStyle": "straight", "aliStart": 7, "text": "WW", "colour": "#9999ff", "aliEnd": 37, "start": 7, "href": "http://pfam.xfam.org/family/PF00397.24", "type": "pfama", "display": "true", "metadata": {"end": 37, "description": "The WW domain is a protein module with two highly conserved tryptophans that binds proline-rich peptide motifs in vitro.", "database": "PfamA", "aliStart": 7, "scoreName": "E-value", "accession": "PF00397.24", "start": 7, "score": 2.3e-15, "identifier": "WW domain", "type": "DBD", "aliEnd": 37}}, {"startStyle": "straight", "end": 137, "endStyle": "jagged", "aliStart": 59, "text": "Rotamase", "colour": "#9999ff", "aliEnd": 129, "start": 59, "href": "http://pfam.xfam.org/family/PF00639.19", "type": "pfama", "display": "true", "metadata": {"end": 137, "description": "Rotamases increase the rate of protein folding by catalysing the interconversion of cis-proline and trans-proline.", "database": "PfamA", "aliStart": 59, "scoreName": "E-value", "accession": "PF00639.19", "start": 59, "score": 2.0000000000000002e-11, "identifier": "PPIC-type PPIASE domain", "type": "DBD", "aliEnd": 129}}, {"startStyle": "jagged", "end": 134, "endStyle": "jagged", "aliStart": 51, "text": "Rotamase_3", "colour": "#9999ff", "aliEnd": 128, "start": 42, "href": "http://pfam.xfam.org/family/PF13616.4", "type": "pfama", "display": "true", "metadata": {"end": 134, "description": "Rotamases increase the rate of protein folding by catalysing the interconversion of cis-proline and trans-proline.", "database": "PfamA", "aliStart": 51, "scoreName": "E-value", "accession": "PF13616.4", "start": 42, "score": 3.1e-09, "identifier": "PPIC-type PPIASE domain", "type": "DBD", "aliEnd": 128}}], "length": 146}
{"regions": [{"startStyle": "straight", "end": 163, "endStyle": "straight", "aliStart": 59, "text": "Rotamase", "colour": "#9999ff", "aliEnd": 162, "start": 59, "href": "http://pfam.xfam.org/family/PF00639.19", "type": "pfama", "display": "true", "metadata": {"end": 163, "description": "Rotamases increase the rate of protein folding by catalysing the interconversion of cis-proline and trans-proline.", "database": "PfamA", "aliStart": 59, "scoreName": "E-value", "accession": "PF00639.19", "start": 59, "score": 9e-24, "identifier": "PPIC-type PPIASE domain", "type": "DBD", "aliEnd": 162}}, {"startStyle": "jagged", "end": 163, "endStyle": "straight", "aliStart": 51, "text": "Rotamase_3", "colour": "#9999ff", "aliEnd": 159, "start": 42, "href": "http://pfam.xfam.org/family/PF13616.4", "type": "pfama", "display": "true", "metadata": {"end": 163, "description": "Rotamases increase the rate of protein folding by catalysing the interconversion of cis-proline and trans-proline.", "database": "PfamA", "aliStart": 51, "scoreName": "E-value", "accession": "PF13616.4", "start": 42, "score": 1.2e-21, "identifier": "PPIC-type PPIASE domain", "type": "DBD", "aliEnd": 159}}, {"startStyle": "straight", "end": 37, "endStyle": "straight", "aliStart": 7, "text": "WW", "colour": "#9999ff", "aliEnd": 37, "start": 7, "href": "http://pfam.xfam.org/family/PF00397.24", "type": "pfama", "display": "true", "metadata": {"end": 37, "description": "The WW domain is a protein module with two highly conserved tryptophans that binds proline-rich peptide motifs in vitro.", "database": "PfamA", "aliStart": 7, "scoreName": "E-value", "accession": "PF00397.24", "start": 7, "score": 2.9e-15, "identifier": "WW domain", "type": "DBD", "aliEnd": 37}}, {"startStyle": "jagged", "end": 163, "endStyle": "jagged", "aliStart": 84, "text": "Rotamase_2", "colour": "#9999ff", "aliEnd": 162, "start": 65, "href": "http://pfam.xfam.org/family/PF13145.4", "type": "pfama", "display": "true", "metadata": {"end": 163, "description": NaN, "database": "PfamA", "aliStart": 84, "scoreName": "E-value", "accession": "PF13145.4", "start": 65, "score": 0.00033, "identifier": "PPIC-type PPIASE domain", "type": "DBD", "aliEnd": 162}}], "length": 164}