Conclusion
Assessment
Binding Mode
Motif Status
Notes
Comments
Inferred motif
1 Monomer or homomultimer
High-throughput in vitro
Description
Description:
high mobility group 20B [Source:HGNC Symbol;Acc:HGNC:5002]
Entrez Summary
TBA
Ensembl ID:
ENSG00000064961
External Link:
Interpro
IPR009071 ; ;
Protein Domain:
Protein: ENSP00000328269DBD: HMGOther: Protein: ENSP00000402877DBD: HMGOther: Protein: ENSP00000410924DBD: HMGOther: Protein: ENSP00000465293DBD: HMGOther: IncA
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?
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
Structure
Experimental History
{"regions": [{"startStyle": "curved", "end": 138, "endStyle": "curved", "aliStart": 70, "text": "HMG", "colour": "#228B22", "aliEnd": 137, "start": 70, "href": "http://pfam.xfam.org/family/PF00505.17", "type": "pfama", "display": "true", "metadata": {"end": 138, "description": "High mobility group (HMG) box domains are involved in binding DNA, and may be involved in protein-protein interactions as well. The structure of the HMG-box domain consists of three helices in an irregular array. HMG-box domains are found in one or more copies in HMG-box proteins, which form a large, diverse family involved in the regulation of DNA-dependent processes such as transcription, replication, and strand repair, all of which require the bending and unwinding of chromatin. Many of these proteins are regulators of gene expression. HMG-box proteins are found in a variety of eukaryotic organisms, and can be broadly divided into two groups, based on sequence-dependent and sequence-independent DNA recognition; the former usually contain one HMG-box motif, while the latter can contain multiple HMG-box motifs.", "database": "PfamA", "aliStart": 70, "scoreName": "E-value", "accession": "PF00505.17", "start": 70, "score": 1.6000000000000002e-19, "identifier": "HMG (high mobility group) box", "type": "DBD", "aliEnd": 137}}], "length": 318}
{"regions": [{"startStyle": "curved", "end": 138, "endStyle": "curved", "aliStart": 70, "text": "HMG", "colour": "#228B22", "aliEnd": 137, "start": 70, "href": "http://pfam.xfam.org/family/PF00505.17", "type": "pfama", "display": "true", "metadata": {"end": 138, "description": "High mobility group (HMG) box domains are involved in binding DNA, and may be involved in protein-protein interactions as well. The structure of the HMG-box domain consists of three helices in an irregular array. HMG-box domains are found in one or more copies in HMG-box proteins, which form a large, diverse family involved in the regulation of DNA-dependent processes such as transcription, replication, and strand repair, all of which require the bending and unwinding of chromatin. Many of these proteins are regulators of gene expression. HMG-box proteins are found in a variety of eukaryotic organisms, and can be broadly divided into two groups, based on sequence-dependent and sequence-independent DNA recognition; the former usually contain one HMG-box motif, while the latter can contain multiple HMG-box motifs.", "database": "PfamA", "aliStart": 70, "scoreName": "E-value", "accession": "PF00505.17", "start": 70, "score": 2.0000000000000002e-20, "identifier": "HMG (high mobility group) box", "type": "DBD", "aliEnd": 137}}], "length": 142}
{"regions": [{"startStyle": "curved", "end": 138, "endStyle": "curved", "aliStart": 70, "text": "HMG", "colour": "#228B22", "aliEnd": 137, "start": 70, "href": "http://pfam.xfam.org/family/PF00505.17", "type": "pfama", "display": "true", "metadata": {"end": 138, "description": "High mobility group (HMG) box domains are involved in binding DNA, and may be involved in protein-protein interactions as well. The structure of the HMG-box domain consists of three helices in an irregular array. HMG-box domains are found in one or more copies in HMG-box proteins, which form a large, diverse family involved in the regulation of DNA-dependent processes such as transcription, replication, and strand repair, all of which require the bending and unwinding of chromatin. Many of these proteins are regulators of gene expression. HMG-box proteins are found in a variety of eukaryotic organisms, and can be broadly divided into two groups, based on sequence-dependent and sequence-independent DNA recognition; the former usually contain one HMG-box motif, while the latter can contain multiple HMG-box motifs.", "database": "PfamA", "aliStart": 70, "scoreName": "E-value", "accession": "PF00505.17", "start": 70, "score": 7.8e-20, "identifier": "HMG (high mobility group) box", "type": "DBD", "aliEnd": 137}}], "length": 215}
{"regions": [{"startStyle": "jagged", "end": 119, "endStyle": "jagged", "aliStart": 5, "text": "IncA", "colour": "#9999ff", "aliEnd": 66, "start": 2, "href": "http://pfam.xfam.org/family/PF04156.12", "type": "pfama", "display": "true", "metadata": {"end": 119, "description": "Chlamydia trachomatis is an obligate intracellular bacterium that develops within a parasitophorous vacuole termed an inclusion. The inclusion is non-fusogenic with lysosomes but intercepts lipids from a host cell exocytic pathway. Initiation of chlamydial development is concurrent with modification of the inclusion membrane by a set of C. trachomatis-encoded proteins collectively designated Incs. One of these Incs, IncA, is functionally associated with the homotypic fusion of inclusions [1]. This family probably includes members of the wider Inc family rather than just IncA. Members are usually either 2 or 4TM proteins.", "database": "PfamA", "aliStart": 5, "scoreName": "E-value", "accession": "PF04156.12", "start": 2, "score": 0.0047, "identifier": "IncA protein", "type": "DBD", "aliEnd": 66}}], "length": 185}