Conclusion
Assessment
Binding Mode
Motif Status
Notes
Comments
Likely to be sequence specific TF
3 Low specificity DNA-binding protein
No motif
MYSM1 has been shown to bind DNA. This interaction requires the MYSM1 Myb but not the SWIRM domain (PMID: 17428495). Domain sequence alignment places it near DNA-binding Myb domains but scores slightly higher as a SANT rather than Myb domain based on Prosite patterns. Given that most Myb proteins that bind DNA sequence specifically have multiple Myb domains in an array, this protein could bind DNA sequence non-specifically with its single Myb domain.
Description
Description:
Myb like, SWIRM and MPN domains 1 [Source:HGNC Symbol;Acc:HGNC:29401]
Entrez Summary
TBA
Ensembl ID:
ENSG00000162601
External Link:
T118162_1.02
Interpro
IPR000555 ; IPR001005 ; IPR007526 ; IPR009057 ; IPR017884 ; ;
Protein Domain:
Protein: ENSP00000478391DBD: Myb, Myb-Like, and SANT Domain Containing GenesOther: JAB, Prok-JABProtein: ENSP00000418734DBD: Myb, Myb-Like, and SANT Domain Containing GenesOther: JAB, Prok-JAB, SWIRM
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.
c
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": "jagged", "end": 88, "endStyle": "straight", "aliStart": 3, "text": "JAB", "colour": "#9999ff", "aliEnd": 85, "start": 1, "href": "http://pfam.xfam.org/family/PF01398.19", "type": "pfama", "display": "true", "metadata": {"end": 88, "description": "Members of this family are found in proteasome regulatory subunits, eukaryotic initiation factor 3 (eIF3) subunits and regulators of transcription factors. This family is also known as the MPN domain [3] and PAD-1-like domain [4], JABP1 domain [5] or JAMM domain [7]. These are metalloenzymes that function as the ubiquitin isopeptidase/ deubiquitinase in the ubiquitin-based signalling and protein turnover pathways in eukaryotes [7]. Versions of the domain in prokaryotic cognates of the ubiquitin-modification pathway are shown to have a similar role, and the archael protein from Haloferax volcanii is found to cleave ubiquitin-like small archaeal modifier proteins (SAMP1/2) from protein conjugates [8,9].", "database": "PfamA", "aliStart": 3, "scoreName": "E-value", "accession": "PF01398.19", "start": 1, "score": 6.3e-10, "identifier": "JAB1/Mov34/MPN/PAD-1 ubiquitin protease", "type": "DBD", "aliEnd": 85}}, {"startStyle": "jagged", "end": 106, "endStyle": "jagged", "aliStart": 3, "text": "Prok-JAB", "colour": "#9999ff", "aliEnd": 81, "start": 1, "href": "http://pfam.xfam.org/family/PF14464.4", "type": "pfama", "display": "true", "metadata": {"end": 106, "description": "These are metalloenzymes that function as the ubiquitin isopeptidase/ deubiquitinase in the ubiquitin-based signaling and protein turnover pathways in eukaryotes [1]. Prokaryotic JAB domains are predicted to have a similar role in their cognates of the ubiquitin modification pathway [2,3]. The domain is widely found in bacteria, archaea and phages where they are present in several gene contexts in addition to those that correspond to the prokaryotic cognates of the eukaryotic Ub pathway. Other contexts in which JAB domains are present include gene neighbor associations with ubiquitin fold domains in cysteine and siderophore biosynthesis, and phage tail morphogenesis, where they are shown or predicted to process the associated ubiquitin [2,4]. A distinct family, the RadC-like JAB domains are widespread in bacteria and are predicted to function as nucleases [5]. In halophilic archaea the JAB domain shows strong gene-neighborhood associations with a nucleotidyltransferase suggesting a role in nucleotide metabolism [5].", "database": "PfamA", "aliStart": 3, "scoreName": "E-value", "accession": "PF14464.4", "start": 1, "score": 1.7e-08, "identifier": "Prokaryotic homologs of the JAB domain", "type": "DBD", "aliEnd": 81}}], "length": 235}
{"regions": [{"startStyle": "curved", "end": 163, "endStyle": "curved", "aliStart": 120, "text": "Myb", "colour": "#228B22", "aliEnd": 162, "start": 118, "href": "http://pfam.xfam.org/family/PF00249.29", "type": "pfama", "display": "true", "metadata": {"end": 163, "description": "This family contains the DNA binding domains from Myb proteins, as well as the SANT domain family.", "database": "PfamA", "aliStart": 120, "scoreName": "E-value", "accession": "PF00249.29", "start": 118, "score": 8.8e-12, "identifier": "Myb-like DNA-binding domain", "type": "DBD", "aliEnd": 162}}, {"startStyle": "straight", "end": 461, "endStyle": "straight", "aliStart": 382, "text": "SWIRM", "colour": "#9999ff", "aliEnd": 461, "start": 375, "href": "http://pfam.xfam.org/family/PF04433.15", "type": "pfama", "display": "true", "metadata": {"end": 461, "description": "This SWIRM domain is a small alpha-helical domain of about 85 amino acid residues found in chromosomal proteins. It contains a helix-turn helix motif and binds to DNA [1].", "database": "PfamA", "aliStart": 382, "scoreName": "E-value", "accession": "PF04433.15", "start": 375, "score": 6.7000000000000005e-21, "identifier": "SWIRM domain", "type": "DBD", "aliEnd": 461}}, {"startStyle": "straight", "end": 682, "endStyle": "straight", "aliStart": 576, "text": "JAB", "colour": "#9999ff", "aliEnd": 679, "start": 572, "href": "http://pfam.xfam.org/family/PF01398.19", "type": "pfama", "display": "true", "metadata": {"end": 682, "description": "Members of this family are found in proteasome regulatory subunits, eukaryotic initiation factor 3 (eIF3) subunits and regulators of transcription factors. This family is also known as the MPN domain [3] and PAD-1-like domain [4], JABP1 domain [5] or JAMM domain [7]. These are metalloenzymes that function as the ubiquitin isopeptidase/ deubiquitinase in the ubiquitin-based signalling and protein turnover pathways in eukaryotes [7]. Versions of the domain in prokaryotic cognates of the ubiquitin-modification pathway are shown to have a similar role, and the archael protein from Haloferax volcanii is found to cleave ubiquitin-like small archaeal modifier proteins (SAMP1/2) from protein conjugates [8,9].", "database": "PfamA", "aliStart": 576, "scoreName": "E-value", "accession": "PF01398.19", "start": 572, "score": 3.2e-11, "identifier": "JAB1/Mov34/MPN/PAD-1 ubiquitin protease", "type": "DBD", "aliEnd": 679}}, {"startStyle": "straight", "end": 699, "endStyle": "jagged", "aliStart": 589, "text": "Prok-JAB", "colour": "#9999ff", "aliEnd": 675, "start": 580, "href": "http://pfam.xfam.org/family/PF14464.4", "type": "pfama", "display": "true", "metadata": {"end": 699, "description": "These are metalloenzymes that function as the ubiquitin isopeptidase/ deubiquitinase in the ubiquitin-based signaling and protein turnover pathways in eukaryotes [1]. Prokaryotic JAB domains are predicted to have a similar role in their cognates of the ubiquitin modification pathway [2,3]. The domain is widely found in bacteria, archaea and phages where they are present in several gene contexts in addition to those that correspond to the prokaryotic cognates of the eukaryotic Ub pathway. Other contexts in which JAB domains are present include gene neighbor associations with ubiquitin fold domains in cysteine and siderophore biosynthesis, and phage tail morphogenesis, where they are shown or predicted to process the associated ubiquitin [2,4]. A distinct family, the RadC-like JAB domains are widespread in bacteria and are predicted to function as nucleases [5]. In halophilic archaea the JAB domain shows strong gene-neighborhood associations with a nucleotidyltransferase suggesting a role in nucleotide metabolism [5].", "database": "PfamA", "aliStart": 589, "scoreName": "E-value", "accession": "PF14464.4", "start": 580, "score": 2.2999999999999998e-08, "identifier": "Prokaryotic homologs of the JAB domain", "type": "DBD", "aliEnd": 675}}], "length": 829}