The Human Transcription Factors

Conclusion

Assessment	Binding Mode	Motif Status	Notes	Comments
Known motif	1 Monomer or homomultimer	High-throughput in vitro		Mouse ortholog binds a highly similar motif.

Description

Description:	myelin regulatory factor [Source:HGNC Symbol;Acc:HGNC:1181]
Entrez Summary	TBA
Ensembl ID:	ENSG00000124920
External Link:
Interpro	IPR008967; IPR024061; IPR025719; IPR026932; IPR030392; ;
Protein Domain:
Protein: ENSP00000265460	DBD: Other	Other: MRF_C1, MRF_C2, Peptidase_S74
Protein: ENSP00000278836	DBD: Other	Other: MRF_C1, MRF_C2, Peptidase_S74
Protein: ENSP00000374253	DBD: Other	Other: MRF_C1, MRF_C2, Peptidase_S74

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?	Yes
Has GO:0003700 "transcription factor activity, sequence-specific DNA binding"	No
GO-Info	GO:0003700 sequence-specific DNA binding transcription factor activity IEA - GO_REF:0000002
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

Source	Annotation	Motif	Evidence
PBM	Zoo_01		Direct
PBM	Zoo_01		Inferred - Myrf (100% AA Identity, Mus musculus)
PBM	Zoo_01		Inferred - myrf (84% AA Identity, Danio rerio)

Structure

Structure	PDB	Not_Covered

Experimental History

Method	Constructs
Tried in PBM? (Whether the protein was tried in PBM or not)
Tried in HT-SELEX (Whether the protein was tried in HT-SELEX or not, and if so, then what kind of clones were tested)
Other Information? (Tried with another method and failed?)

External Contribution

Name
Email
Comment
Reference

{"regions": [{"startStyle": "curved", "end": 531, "endStyle": "curved", "aliStart": 385, "text": "NDT80", "colour": "#228B22", "aliEnd": 530, "start": 384, "href": "http://pfam.xfam.org/family/PF05224.10", "type": "pfama", "display": "true", "metadata": {"end": 531, "description": "This family includes the DNA-binding region of NDT80 [1] as well as PhoG and its homologues. The family contains Swiss:Q05534 or VIB-1. VIB-1 is thought to be a regulator of conidiation in Neurospora crassa and shares a region of similarity to PHOG, a possible phosphate nonrepressible acid phosphatase in Aspergillus nidulans. It has been found that vib-1 is not the structural gene for nonrepressible acid phosphatase, but rather may regulate nonrepressible acid phosphatase activity [2].", "database": "PfamA", "aliStart": 385, "scoreName": "E-value", "accession": "PF05224.10", "start": 384, "score": 1.1999999999999999e-28, "identifier": "NDT80 / PhoG like DNA-binding  family", "type": "DBD", "aliEnd": 530}}, {"startStyle": "straight", "end": 1110, "endStyle": "straight", "aliStart": 976, "text": "MRF_C2", "colour": "#9999ff", "aliEnd": 1110, "start": 976, "href": "http://pfam.xfam.org/family/PF13888.4", "type": "pfama", "display": "true", "metadata": {"end": 1110, "description": "This domain is found further downstream of Peptidase_S74, Pfam:PF13884, and MRF_C1, Pfam:PF13887.  The function is not known.", "database": "PfamA", "aliStart": 976, "scoreName": "E-value", "accession": "PF13888.4", "start": 976, "score": 1.3999999999999997e-42, "identifier": "Myelin gene regulatory factor C-terminal domain 2", "type": "DBD", "aliEnd": 1110}}, {"startStyle": "straight", "end": 693, "endStyle": "straight", "aliStart": 658, "text": "MRF_C1", "colour": "#9999ff", "aliEnd": 693, "start": 658, "href": "http://pfam.xfam.org/family/PF13887.4", "type": "pfama", "display": "true", "metadata": {"end": 693, "description": "This domain is found just downstream of Peptidase_S74, Pfam:PF13884.  The function is not known.", "database": "PfamA", "aliStart": 658, "scoreName": "E-value", "accession": "PF13887.4", "start": 658, "score": 8.4e-23, "identifier": "Myelin gene regulatory factor -C-terminal domain 1", "type": "DBD", "aliEnd": 693}}, {"startStyle": "straight", "end": 638, "endStyle": "straight", "aliStart": 578, "text": "Peptidase_S74", "colour": "#9999ff", "aliEnd": 638, "start": 578, "href": "http://pfam.xfam.org/family/PF13884.4", "type": "pfama", "display": "true", "metadata": {"end": 638, "description": "This is the very C-terminal, chaperone, domain of the bacteriophage protein endosialidase. It releases itself, via the serine-lysine dyad at the N-terminus, from the remainder of the end-tail-spike. Cleavage occurs after the threonine which is the final residue of the End-tail-spike family, Pfam:PF12219. The endosialidase protein forms homotrimeric molecules in bacteriophages [1]. The catalytic dyad allows this portion of the molecule to be cleaved from the more N-terminal region such that the latter can fold and presumably bind to DNA.", "database": "PfamA", "aliStart": 578, "scoreName": "E-value", "accession": "PF13884.4", "start": 578, "score": 2.9e-13, "identifier": "Chaperone of endosialidase", "type": "DBD", "aliEnd": 638}}], "length": 1112}

{"regions": [{"startStyle": "curved", "end": 540, "endStyle": "curved", "aliStart": 394, "text": "NDT80", "colour": "#228B22", "aliEnd": 539, "start": 393, "href": "http://pfam.xfam.org/family/PF05224.10", "type": "pfama", "display": "true", "metadata": {"end": 540, "description": "This family includes the DNA-binding region of NDT80 [1] as well as PhoG and its homologues. The family contains Swiss:Q05534 or VIB-1. VIB-1 is thought to be a regulator of conidiation in Neurospora crassa and shares a region of similarity to PHOG, a possible phosphate nonrepressible acid phosphatase in Aspergillus nidulans. It has been found that vib-1 is not the structural gene for nonrepressible acid phosphatase, but rather may regulate nonrepressible acid phosphatase activity [2].", "database": "PfamA", "aliStart": 394, "scoreName": "E-value", "accession": "PF05224.10", "start": 393, "score": 1.3000000000000002e-28, "identifier": "NDT80 / PhoG like DNA-binding  family", "type": "DBD", "aliEnd": 539}}, {"startStyle": "straight", "end": 1150, "endStyle": "straight", "aliStart": 1016, "text": "MRF_C2", "colour": "#9999ff", "aliEnd": 1150, "start": 1016, "href": "http://pfam.xfam.org/family/PF13888.4", "type": "pfama", "display": "true", "metadata": {"end": 1150, "description": "This domain is found further downstream of Peptidase_S74, Pfam:PF13884, and MRF_C1, Pfam:PF13887.  The function is not known.", "database": "PfamA", "aliStart": 1016, "scoreName": "E-value", "accession": "PF13888.4", "start": 1016, "score": 1.4999999999999998e-42, "identifier": "Myelin gene regulatory factor C-terminal domain 2", "type": "DBD", "aliEnd": 1150}}, {"startStyle": "straight", "end": 702, "endStyle": "straight", "aliStart": 667, "text": "MRF_C1", "colour": "#9999ff", "aliEnd": 702, "start": 667, "href": "http://pfam.xfam.org/family/PF13887.4", "type": "pfama", "display": "true", "metadata": {"end": 702, "description": "This domain is found just downstream of Peptidase_S74, Pfam:PF13884.  The function is not known.", "database": "PfamA", "aliStart": 667, "scoreName": "E-value", "accession": "PF13887.4", "start": 667, "score": 8.7e-23, "identifier": "Myelin gene regulatory factor -C-terminal domain 1", "type": "DBD", "aliEnd": 702}}, {"startStyle": "straight", "end": 647, "endStyle": "straight", "aliStart": 587, "text": "Peptidase_S74", "colour": "#9999ff", "aliEnd": 647, "start": 587, "href": "http://pfam.xfam.org/family/PF13884.4", "type": "pfama", "display": "true", "metadata": {"end": 647, "description": "This is the very C-terminal, chaperone, domain of the bacteriophage protein endosialidase. It releases itself, via the serine-lysine dyad at the N-terminus, from the remainder of the end-tail-spike. Cleavage occurs after the threonine which is the final residue of the End-tail-spike family, Pfam:PF12219. The endosialidase protein forms homotrimeric molecules in bacteriophages [1]. The catalytic dyad allows this portion of the molecule to be cleaved from the more N-terminal region such that the latter can fold and presumably bind to DNA.", "database": "PfamA", "aliStart": 587, "scoreName": "E-value", "accession": "PF13884.4", "start": 587, "score": 3e-13, "identifier": "Chaperone of endosialidase", "type": "DBD", "aliEnd": 647}}], "length": 1152}

{"regions": [{"startStyle": "straight", "end": 536, "endStyle": "straight", "aliStart": 402, "text": "MRF_C2", "colour": "#9999ff", "aliEnd": 536, "start": 402, "href": "http://pfam.xfam.org/family/PF13888.4", "type": "pfama", "display": "true", "metadata": {"end": 536, "description": "This domain is found further downstream of Peptidase_S74, Pfam:PF13884, and MRF_C1, Pfam:PF13887.  The function is not known.", "database": "PfamA", "aliStart": 402, "scoreName": "E-value", "accession": "PF13888.4", "start": 402, "score": 5.1000000000000005e-43, "identifier": "Myelin gene regulatory factor C-terminal domain 2", "type": "DBD", "aliEnd": 536}}, {"startStyle": "straight", "end": 93, "endStyle": "straight", "aliStart": 58, "text": "MRF_C1", "colour": "#9999ff", "aliEnd": 93, "start": 58, "href": "http://pfam.xfam.org/family/PF13887.4", "type": "pfama", "display": "true", "metadata": {"end": 93, "description": "This domain is found just downstream of Peptidase_S74, Pfam:PF13884.  The function is not known.", "database": "PfamA", "aliStart": 58, "scoreName": "E-value", "accession": "PF13887.4", "start": 58, "score": 3.7e-23, "identifier": "Myelin gene regulatory factor -C-terminal domain 1", "type": "DBD", "aliEnd": 93}}, {"startStyle": "jagged", "end": 38, "endStyle": "straight", "aliStart": 1, "text": "Peptidase_S74", "colour": "#9999ff", "aliEnd": 38, "start": 1, "href": "http://pfam.xfam.org/family/PF13884.4", "type": "pfama", "display": "true", "metadata": {"end": 38, "description": "This is the very C-terminal, chaperone, domain of the bacteriophage protein endosialidase. It releases itself, via the serine-lysine dyad at the N-terminus, from the remainder of the end-tail-spike. Cleavage occurs after the threonine which is the final residue of the End-tail-spike family, Pfam:PF12219. The endosialidase protein forms homotrimeric molecules in bacteriophages [1]. The catalytic dyad allows this portion of the molecule to be cleaved from the more N-terminal region such that the latter can fold and presumably bind to DNA.", "database": "PfamA", "aliStart": 1, "scoreName": "E-value", "accession": "PF13884.4", "start": 1, "score": 5.9e-07, "identifier": "Chaperone of endosialidase", "type": "DBD", "aliEnd": 38}}], "length": 538}

TF Info Page for MYRF (Ndt80/PhoG)