The Human Transcription Factors

Conclusion

Assessment	Binding Mode	Motif Status	Notes	Comments
Inferred motif	2 Obligate heteromer	In vivo/Misc source		All three MXD proteins have very similar sequences and should behave accordingly, making heterodimers with at least MAX (PMID:8521822).

Description

Description:	MAX dimerization protein 4 [Source:HGNC Symbol;Acc:HGNC:13906]
Entrez Summary	TBA
Ensembl ID:	ENSG00000123933
External Link:	T014198_1.02
Interpro	IPR011598; ;
Protein Domain:
Protein: ENSP00000337889	DBD: bHLH	Other: Myc-LZ

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.	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"	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	3a, decent circumstantial evidence for its role as
TF has conditional DNA-binding requirements

DNA-Binding

Published Motif Data

Source	Annotation	Motif	Evidence
ChIP-seq	modENCODE		Inferred - mdl-1 (60% AA Identity, Caenorhabditis elegans)

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": 106, "endStyle": "curved", "aliStart": 55, "text": "HLH", "colour": "#2cb42c", "aliEnd": 106, "start": 54, "href": "http://pfam.xfam.org/family/PF00010.24", "type": "pfama", "display": "true", "metadata": {"end": 106, "description": "A number of eukaryotic proteins, which probably are sequence specific DNA-binding proteins that act as transcription factors, share a conserved domain of 40 to 50 amino acid residues. It has been proposed [PUBMED:2493990] that this domain is formed of two amphipathic helices joined by a variable length linker region that could form a loop. 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. The proteins of this subfamily act together with co-repressor proteins, like groucho, through their C-terminal motif WRPW.", "database": "PfamA", "aliStart": 55, "scoreName": "E-value", "accession": "PF00010.24", "start": 54, "score": 7.000000000000001e-10, "identifier": "Helix-loop-helix DNA-binding domain", "type": "DBD", "aliEnd": 106}}, {"startStyle": "jagged", "end": 135, "endStyle": "straight", "aliStart": 110, "text": "Myc-LZ", "colour": "#9999ff", "aliEnd": 134, "start": 106, "href": "http://pfam.xfam.org/family/PF02344.13", "type": "pfama", "display": "true", "metadata": {"end": 135, "description": "This family consists of the leucine zipper dimerisation domain found in both cellular c-Myc proto-oncogenes and viral v-Myc oncogenes.  Dimerisation via the leucine zipper motif with other basic helix-loop-helix-leucine zipper (b/HLH/lz) proteins such as  Max Swiss:P25912 is required for efficient DNA binding.  The Myc-Max dimer is a transactivating complex activating expression of growth related genes promoting cell proliferation. The dimerisation is facilitated via interdigitating leucine residues  every 7th position of the alpha helix.  Like charge repulsion of  adjacent residues in this region perturbs the formation of homodimers  with heterodimers being promoted by opposing charge attractions.", "database": "PfamA", "aliStart": 110, "scoreName": "E-value", "accession": "PF02344.13", "start": 106, "score": 0.0025, "identifier": "Myc leucine zipper domain", "type": "DBD", "aliEnd": 134}}], "length": 210}

TF Info Page for MXD4 (bHLH)