The Human Transcription Factors

Conclusion

Assessment	Binding Mode	Motif Status	Notes	Comments
Known motif	2 Obligate heteromer	In vivo/Misc source		Functions as a heterodimer with MAX.

Description

Description:	v-myc avian myelocytomatosis viral oncogene homolog [Source:HGNC Symbol;Acc:HGNC:7553]
Entrez Summary	TBA
Ensembl ID:	ENSG00000136997
External Link:
Interpro	IPR002418; IPR003327; IPR011598; IPR012682;
Protein Domain:
Protein: ENSP00000259523	DBD: bHLH	Other: Myc_N
Protein: ENSP00000367207	DBD: bHLH	Other: Myc_N, TRH
Protein: ENSP00000429441	DBD: bHLH	Other: Myc_N
Protein: ENSP00000430235	DBD: bHLH	Other: Myc_N, TRH
Protein: ENSP00000479618	DBD: bHLH	Other: Myc_N, TRH
Protein: ENSP00000478887	DBD: bHLH	Other: Myc_N, TRH
Protein: ENSP00000430226	DBD: bHLH	Other:

Previous Annotations

Source	Annotation
TF-CAT classification	TF Gene_DNA-Binding sequence-specific_DNA Binding_ PMIDS:12177005 16287840 16767079
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 IDA - PMID:10723141 GO:0003700 sequence-specific DNA binding transcription factor activity IDA - PMID:9924025
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	Obligate_Multimer

DNA-Binding

Published Motif Data

Source	Annotation	Motif	Evidence
ChIP-seq	ENCODE		Direct
ChIP-seq	ENCODE		Direct
ChIP-seq	ENCODE		Direct
ChIP-seq	ENCODE		Direct
ChIP-seq	ENCODE		Direct
ChIP-seq	ENCODE		Direct
Transfac	Transfac	License required	Direct
Transfac	Transfac	License required	Direct
Transfac	Transfac	License required	Direct
Transfac	Transfac	License required	Direct
Transfac	Transfac	License required	Direct
Misc	HocoMoco		Direct
Misc	HOMER		Direct
ChIP-seq	JASPAR		Inferred - Myc (92% AA Identity, Mus musculus)
Misc	HOMER		Inferred - Myc (92% AA Identity, Mus musculus)

Structure

Structure	PDB	1NKP

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

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They are refered as basic helix-loop-helix proteins (bHLH), and are classified in two groups: class A (ubiquitous) and class B (tissue-specific). Members of the bHLH family bind variations on the core sequence 'CANNTG', also refered to as the E-box motif. The homo- or heterodimerization mediated by the HLH domain is independent of, but necessary for DNA binding, as two basic regions are required for DNA binding activity. The HLH proteins lacking the basic domain (Emc, Id) function as negative regulators, since they form heterodimers, but fail to bind DNA. The hairy-related proteins (hairy, E(spl), deadpan) also repress transcription although they can bind DNA. 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This 'helix-loop-helix' (HLH) domain mediates protein dimerization and has been found in the proteins listed below [PUBMED:1521738]. Most of these proteins have an extra basic region of about 15 amino acid residues that is adjacent to the HLH domain and specifically binds to DNA. They are refered as basic helix-loop-helix proteins (bHLH), and are classified in two groups: class A (ubiquitous) and class B (tissue-specific). Members of the bHLH family bind variations on the core sequence 'CANNTG', also refered to as the E-box motif. The homo- or heterodimerization mediated by the HLH domain is independent of, but necessary for DNA binding, as two basic regions are required for DNA binding activity. The HLH proteins lacking the basic domain (Emc, Id) function as negative regulators, since they form heterodimers, but fail to bind DNA. The hairy-related proteins (hairy, E(spl), deadpan) also repress transcription although they can bind DNA. 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This interpretation is supported by the identification of a peptidase localised on the surface of neuronal cells which has been termed TRH-degrading ectoenzyme (TRH-DE) since it selectively inactivates TRH [1]. TRH has been used clinically for the treatment of spinocerebellar degeneration and disturbance of consciousness in humans [2].", "database": "PfamA", "aliStart": 252, "scoreName": "E-value", "accession": "PF05438.10", "start": 210, "score": 0.0023, "identifier": "Thyrotropin-releasing hormone (TRH)", "type": "DBD", "aliEnd": 284}}], "length": 440}

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They are refered as basic helix-loop-helix proteins (bHLH), and are classified in two groups: class A (ubiquitous) and class B (tissue-specific). Members of the bHLH family bind variations on the core sequence 'CANNTG', also refered to as the E-box motif. The homo- or heterodimerization mediated by the HLH domain is independent of, but necessary for DNA binding, as two basic regions are required for DNA binding activity. The HLH proteins lacking the basic domain (Emc, Id) function as negative regulators, since they form heterodimers, but fail to bind DNA. The hairy-related proteins (hairy, E(spl), deadpan) also repress transcription although they can bind DNA. 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This interpretation is supported by the identification of a peptidase localised on the surface of neuronal cells which has been termed TRH-degrading ectoenzyme (TRH-DE) since it selectively inactivates TRH [1]. TRH has been used clinically for the treatment of spinocerebellar degeneration and disturbance of consciousness in humans [2].", "database": "PfamA", "aliStart": 266, "scoreName": "E-value", "accession": "PF05438.10", "start": 224, "score": 0.0024, "identifier": "Thyrotropin-releasing hormone (TRH)", "type": "DBD", "aliEnd": 298}}], "length": 454}

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They are refered as basic helix-loop-helix proteins (bHLH), and are classified in two groups: class A (ubiquitous) and class B (tissue-specific). Members of the bHLH family bind variations on the core sequence 'CANNTG', also refered to as the E-box motif. The homo- or heterodimerization mediated by the HLH domain is independent of, but necessary for DNA binding, as two basic regions are required for DNA binding activity. The HLH proteins lacking the basic domain (Emc, Id) function as negative regulators, since they form heterodimers, but fail to bind DNA. The hairy-related proteins (hairy, E(spl), deadpan) also repress transcription although they can bind DNA. 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TF Info Page for MYC (bHLH)