Conclusion
Assessment
Binding Mode
Motif Status
Notes
Comments
Known motif
1 Monomer or homomultimer
High-throughput in vitro
Description
Description:
paired box 8 [Source:HGNC Symbol;Acc:HGNC:8622]
Entrez Summary
TBA
Ensembl ID:
ENSG00000125618
External Link:
T135872_1.02
Interpro
IPR001523 ; IPR009057 ; IPR022130 ; ;
Protein Domain:
Protein: ENSP00000263334DBD: Paired BoxOther: Pax2_CProtein: ENSP00000263335DBD: Paired BoxOther: Protein: ENSP00000314750DBD: Paired BoxOther: Protein: ENSP00000380768DBD: Paired BoxOther: Protein: ENSP00000395498DBD: Paired BoxOther: Pax2_CProtein: ENSP00000452547DBD: Paired BoxOther: Pax2_CProtein: ENSP00000451240DBD: Paired BoxOther: Pax2_C
Previous Annotations
Source
Annotation
TF-CAT classification
TF Gene_DNA-Binding sequence-specific_DNA Binding Transactivation_ PMIDS:1508216
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:0001077 RNA polymerase II core promoter proximal region sequence-specific DNA binding transcription factor a IEA - GO_REF:0000019 GO:0003700 sequence-specific DNA binding transcription factor activity IDA - PMID:9388203, PMID:9590296
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
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{"regions": [{"startStyle": "curved", "end": 133, "endStyle": "curved", "aliStart": 9, "text": "PAX", "colour": "#2cb42c", "aliEnd": 133, "start": 9, "href": "http://pfam.xfam.org/family/PF00292.16", "type": "pfama", "display": "true", "metadata": {"end": 133, "description": "Paired domain proteins can function as transcription repressors or activators. The paired domain contains three subdomains, which show functional differences in DNA-binding. The crystal structures of prd and Pax proteins show that the DNA-bound paired domain is bipartite, consisting of an N-terminal subdomain (PAI or NTD) and a C-terminal subdomain (RED or CTD), connected by a linker. PAI and RED each form a three-helical fold, with the most C-terminal helices comprising a helix-turn-helix (HTH) motif that binds the DNA major groove. In addition, the PAI subdomain encompasses an N-terminal beta-turn and beta-hairpin, also named 'wing', participating in DNA-binding. The linker can bind into the DNA minor groove. Different Pax proteins and their alternatively spliced isoforms use different (sub)domains for DNA-binding to mediate the specificity of sequence recognition [PUBMED:11103953, PUBMED:15148315].", "database": "PfamA", "aliStart": 9, "scoreName": "E-value", "accession": "PF00292.16", "start": 9, "score": 1.0999999999999999e-72, "identifier": "'Paired box' domain", "type": "DBD", "aliEnd": 133}}], "length": 322}
{"regions": [{"startStyle": "curved", "end": 133, "endStyle": "curved", "aliStart": 9, "text": "PAX", "colour": "#2cb42c", "aliEnd": 133, "start": 9, "href": "http://pfam.xfam.org/family/PF00292.16", "type": "pfama", "display": "true", "metadata": {"end": 133, "description": "Paired domain proteins can function as transcription repressors or activators. The paired domain contains three subdomains, which show functional differences in DNA-binding. The crystal structures of prd and Pax proteins show that the DNA-bound paired domain is bipartite, consisting of an N-terminal subdomain (PAI or NTD) and a C-terminal subdomain (RED or CTD), connected by a linker. PAI and RED each form a three-helical fold, with the most C-terminal helices comprising a helix-turn-helix (HTH) motif that binds the DNA major groove. In addition, the PAI subdomain encompasses an N-terminal beta-turn and beta-hairpin, also named 'wing', participating in DNA-binding. The linker can bind into the DNA minor groove. Different Pax proteins and their alternatively spliced isoforms use different (sub)domains for DNA-binding to mediate the specificity of sequence recognition [PUBMED:11103953, PUBMED:15148315].", "database": "PfamA", "aliStart": 9, "scoreName": "E-value", "accession": "PF00292.16", "start": 9, "score": 1.5999999999999997e-72, "identifier": "'Paired box' domain", "type": "DBD", "aliEnd": 133}}], "length": 399}
{"regions": [{"startStyle": "curved", "end": 133, "endStyle": "curved", "aliStart": 9, "text": "PAX", "colour": "#2cb42c", "aliEnd": 133, "start": 9, "href": "http://pfam.xfam.org/family/PF00292.16", "type": "pfama", "display": "true", "metadata": {"end": 133, "description": "Paired domain proteins can function as transcription repressors or activators. The paired domain contains three subdomains, which show functional differences in DNA-binding. The crystal structures of prd and Pax proteins show that the DNA-bound paired domain is bipartite, consisting of an N-terminal subdomain (PAI or NTD) and a C-terminal subdomain (RED or CTD), connected by a linker. PAI and RED each form a three-helical fold, with the most C-terminal helices comprising a helix-turn-helix (HTH) motif that binds the DNA major groove. In addition, the PAI subdomain encompasses an N-terminal beta-turn and beta-hairpin, also named 'wing', participating in DNA-binding. The linker can bind into the DNA minor groove. Different Pax proteins and their alternatively spliced isoforms use different (sub)domains for DNA-binding to mediate the specificity of sequence recognition [PUBMED:11103953, PUBMED:15148315].", "database": "PfamA", "aliStart": 9, "scoreName": "E-value", "accession": "PF00292.16", "start": 9, "score": 8.399999999999998e-73, "identifier": "'Paired box' domain", "type": "DBD", "aliEnd": 133}}], "length": 288}
{"regions": [{"startStyle": "curved", "end": 133, "endStyle": "curved", "aliStart": 9, "text": "PAX", "colour": "#2cb42c", "aliEnd": 133, "start": 9, "href": "http://pfam.xfam.org/family/PF00292.16", "type": "pfama", "display": "true", "metadata": {"end": 133, "description": "Paired domain proteins can function as transcription repressors or activators. The paired domain contains three subdomains, which show functional differences in DNA-binding. The crystal structures of prd and Pax proteins show that the DNA-bound paired domain is bipartite, consisting of an N-terminal subdomain (PAI or NTD) and a C-terminal subdomain (RED or CTD), connected by a linker. PAI and RED each form a three-helical fold, with the most C-terminal helices comprising a helix-turn-helix (HTH) motif that binds the DNA major groove. In addition, the PAI subdomain encompasses an N-terminal beta-turn and beta-hairpin, also named 'wing', participating in DNA-binding. The linker can bind into the DNA minor groove. Different Pax proteins and their alternatively spliced isoforms use different (sub)domains for DNA-binding to mediate the specificity of sequence recognition [PUBMED:11103953, PUBMED:15148315].", "database": "PfamA", "aliStart": 9, "scoreName": "E-value", "accession": "PF00292.16", "start": 9, "score": 1.8999999999999995e-72, "identifier": "'Paired box' domain", "type": "DBD", "aliEnd": 133}}, {"startStyle": "straight", "end": 449, "endStyle": "straight", "aliStart": 339, "text": "Pax2_C", "colour": "#9999ff", "aliEnd": 449, "start": 337, "href": "http://pfam.xfam.org/family/PF12403.6", "type": "pfama", "display": "true", "metadata": {"end": 449, "description": "This domain family is found in eukaryotes, and is approximately 110 amino acids in length. The family is found in association with Pfam:PF00292. This family is the C terminal of the paired-box protein 2 which is a transcription factor involved in embryonic development and organogenesis.", "database": "PfamA", "aliStart": 339, "scoreName": "E-value", "accession": "PF12403.6", "start": 337, "score": 1.2999999999999999e-54, "identifier": "Paired-box protein 2 C terminal", "type": "DBD", "aliEnd": 449}}], "length": 451}
{"regions": [{"startStyle": "straight", "end": 98, "endStyle": "jagged", "aliStart": 2, "text": "Pax2_C", "colour": "#9999ff", "aliEnd": 70, "start": 1, "href": "http://pfam.xfam.org/family/PF12403.6", "type": "pfama", "display": "true", "metadata": {"end": 98, "description": "This domain family is found in eukaryotes, and is approximately 110 amino acids in length. The family is found in association with Pfam:PF00292. This family is the C terminal of the paired-box protein 2 which is a transcription factor involved in embryonic development and organogenesis.", "database": "PfamA", "aliStart": 2, "scoreName": "E-value", "accession": "PF12403.6", "start": 1, "score": 1.2e-24, "identifier": "Paired-box protein 2 C terminal", "type": "DBD", "aliEnd": 70}}], "length": 99}
{"regions": [{"startStyle": "straight", "end": 172, "endStyle": "straight", "aliStart": 69, "text": "Pax2_C", "colour": "#9999ff", "aliEnd": 172, "start": 62, "href": "http://pfam.xfam.org/family/PF12403.6", "type": "pfama", "display": "true", "metadata": {"end": 172, "description": "This domain family is found in eukaryotes, and is approximately 110 amino acids in length. The family is found in association with Pfam:PF00292. This family is the C terminal of the paired-box protein 2 which is a transcription factor involved in embryonic development and organogenesis.", "database": "PfamA", "aliStart": 69, "scoreName": "E-value", "accession": "PF12403.6", "start": 62, "score": 3.2999999999999997e-49, "identifier": "Paired-box protein 2 C terminal", "type": "DBD", "aliEnd": 172}}], "length": 174}