The Human Transcription Factors

Conclusion

Assessment	Binding Mode	Motif Status	Notes	Comments
Known motif	1 Monomer or homomultimer	High-throughput in vitro

Description

Description:

zinc finger and BTB domain containing 7C [Source:HGNC Symbol;Acc:HGNC:31700]

Entrez Summary

Predicted to enable DNA-binding transcription factor activity, RNA polymerase II-specific and RNA polymerase II cis-regulatory region sequence-specific DNA binding activity. Involved in negative regulation of cell population proliferation. Predicted to be located in nucleus. [provided by Alliance of Genome Resources, Apr 2022]

Ensembl ID:

ENSG00000184828

External Link:

CisBP

Interpro

IPR000210; IPR007087; IPR011333; IPR013069; IPR015880; IPR016024;

Protein Domain:

ENSP00000439781

Protein Domain:

ENSP00000464724

Protein Domain:

ENSP00000466944

Protein Domain:

ENSP00000468254

Protein Domain:

ENSP00000468537

Protein Domain:

ENSP00000466006

Protein Domain:

ENSP00000465760

Protein Domain:

ENSP00000468152

Protein Domain:

ENSP00000466088

Protein Domain:

ENSP00000468814

Protein Domain:

ENSP00000467456

Protein Domain:

ENSP00000468502

Protein Domain:

ENSP00000468782

Protein Domain:

ENSP00000467147

Protein Domain:

ENSP00000467338

Protein Domain:

ENSP00000468019

Protein Domain:

ENSP00000465160

Protein Domain:

ENSP00000465494

Protein Domain:

ENSP00000467323

Protein Domain:

ENSP00000467877

Protein Domain:

ENSP00000468306

Protein Domain:

ENSP00000465265

Protein Domain:

ENSP00000467758

Protein Domain:

ENSP00000468752

Protein Domain:

ENSP00000465835

Protein Domain:

ENSP00000468087

Protein Domain:

ENSP00000465832

Domain:

Protein: ENSP00000439781	DBD: C2H2 ZF Containing Proteins	Other: BTB
Protein: ENSP00000464724	DBD: C2H2 ZF Containing Proteins	Other:
Protein: ENSP00000466944	DBD: C2H2 ZF Containing Proteins	Other:
Protein: ENSP00000468254	DBD: C2H2 ZF Containing Proteins	Other: BTB
Protein: ENSP00000468537	DBD: C2H2 ZF Containing Proteins	Other:
Protein: ENSP00000466006	DBD: C2H2 ZF Containing Proteins	Other:
Protein: ENSP00000465760	DBD: C2H2 ZF Containing Proteins	Other:
Protein: ENSP00000468152	DBD: C2H2 ZF Containing Proteins	Other:
Protein: ENSP00000466088	DBD: C2H2 ZF Containing Proteins	Other:
Protein: ENSP00000468814	DBD: C2H2 ZF Containing Proteins	Other:
Protein: ENSP00000467456	DBD: C2H2 ZF Containing Proteins	Other:
Protein: ENSP00000468502	DBD: C2H2 ZF Containing Proteins	Other:
Protein: ENSP00000468782	DBD: C2H2 ZF Containing Proteins	Other: BTB
Protein: ENSP00000467147	DBD: C2H2 ZF Containing Proteins	Other:
Protein: ENSP00000467338	DBD: C2H2 ZF Containing Proteins	Other:
Protein: ENSP00000468019	DBD: C2H2 ZF Containing Proteins	Other:
Protein: ENSP00000465160	DBD: C2H2 ZF Containing Proteins	Other:
Protein: ENSP00000465494	DBD: C2H2 ZF Containing Proteins	Other:
Protein: ENSP00000467323	DBD: C2H2 ZF Containing Proteins	Other: BTB
Protein: ENSP00000467877	DBD: C2H2 ZF Containing Proteins	Other: BTB
Protein: ENSP00000468306	DBD: C2H2 ZF Containing Proteins	Other:
Protein: ENSP00000465265	DBD: C2H2 ZF Containing Proteins	Other:
Protein: ENSP00000467758	DBD: C2H2 ZF Containing Proteins	Other:
Protein: ENSP00000468752	DBD: C2H2 ZF Containing Proteins	Other:
Protein: ENSP00000465835	DBD: C2H2 ZF Containing Proteins	Other:
Protein: ENSP00000468087	DBD: C2H2 ZF Containing Proteins	Other:
Protein: ENSP00000465832	DBD: C2H2 ZF Containing Proteins	Other:

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.	b
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

Source	Annotation	Motif	Evidence
HT-SELEX	Jolma2013		Direct
Transfac	Transfac	License required	Direct
HT-SELEX	Yin2017		Inferred - ZBTB7A (75% AA Identity, Homo sapiens)
Methyl-HT-SELEX	Yin2017		Inferred - ZBTB7A (75% AA Identity, Homo sapiens)
ChIP-seq	ENCODE		Inferred - ZBTB7A (75% AA Identity, Homo sapiens)
Transfac	Transfac	License required	Inferred - ZBTB7A (75% AA Identity, Homo sapiens)
Transfac	Transfac	License required	Inferred - ZBTB7A (75% AA Identity, Homo sapiens)
Transfac	Transfac	License required	Inferred - ZBTB7A (75% AA Identity, Homo sapiens)
Transfac	Transfac	License required	Inferred - ZBTB7A (75% AA Identity, Homo sapiens)
Transfac	Transfac	License required	Inferred - ZBTB7A (75% AA Identity, Homo sapiens)
Misc	HocoMoco		Inferred - ZBTB7A (75% AA Identity, Homo sapiens)

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": 386, "endStyle": "curved", "aliStart": 365, "text": "zfC2H2", "colour": "#228B22", "aliEnd": 386, "start": 364, "href": "http://pfam.xfam.org/family/PF00096.24", "type": "pfama", "display": "true", "metadata": {"end": 386, "description": "The C2H2 zinc finger is the classical zinc finger domain. The two conserved cysteines and histidines co-ordinate a zinc ion. The following pattern describes the zinc finger. #-X-C-X(1-5)-C-X3-#-X5-#-X2-H-X(3-6)-[H/C] Where X can be any amino acid, and numbers in brackets indicate the number of residues. The positions marked # are those that are important for the stable fold of the zinc finger. The final position can be either his or cys. The C2H2 zinc finger is composed of two short beta strands followed by an alpha helix. The amino terminal part of the helix binds the major groove in DNA binding zinc fingers. The accepted consensus binding sequence for Sp1 is usually defined by the asymmetric hexanucleotide core GGGCGG but this sequence does not include, among others, the GAG (=CTC) repeat that constitutes a high-affinity  site for Sp1 binding to the wt1 promoter [2].", "database": "PfamA", "aliStart": 365, "scoreName": "E-value", "accession": "PF00096.24", "start": 364, "score": 1.2e-13, "identifier": "Zinc finger, C2H2 type", "type": "DBD", "aliEnd": 386}}, {"startStyle": "curved", "end": 414, "endStyle": "curved", "aliStart": 392, "text": "zfC2H2", "colour": "#228B22", "aliEnd": 414, "start": 392, "href": "http://pfam.xfam.org/family/PF00096.24", "type": "pfama", "display": "true", "metadata": {"end": 414, "description": "The C2H2 zinc finger is the classical zinc finger domain. The two conserved cysteines and histidines co-ordinate a zinc ion. The following pattern describes the zinc finger. #-X-C-X(1-5)-C-X3-#-X5-#-X2-H-X(3-6)-[H/C] Where X can be any amino acid, and numbers in brackets indicate the number of residues. The positions marked # are those that are important for the stable fold of the zinc finger. The final position can be either his or cys. The C2H2 zinc finger is composed of two short beta strands followed by an alpha helix. The amino terminal part of the helix binds the major groove in DNA binding zinc fingers. The accepted consensus binding sequence for Sp1 is usually defined by the asymmetric hexanucleotide core GGGCGG but this sequence does not include, among others, the GAG (=CTC) repeat that constitutes a high-affinity  site for Sp1 binding to the wt1 promoter [2].", "database": "PfamA", "aliStart": 392, "scoreName": "E-value", "accession": "PF00096.24", "start": 392, "score": 1.2e-13, "identifier": "Zinc finger, C2H2 type", "type": "DBD", "aliEnd": 414}}, {"startStyle": "jagged", "end": 442, "endStyle": "curved", "aliStart": 422, "text": "zfC2H2", "colour": "#228B22", "aliEnd": 442, "start": 420, "href": "http://pfam.xfam.org/family/PF00096.24", "type": "pfama", "display": "true", "metadata": {"end": 442, "description": "The C2H2 zinc finger is the classical zinc finger domain. The two conserved cysteines and histidines co-ordinate a zinc ion. The following pattern describes the zinc finger. #-X-C-X(1-5)-C-X3-#-X5-#-X2-H-X(3-6)-[H/C] Where X can be any amino acid, and numbers in brackets indicate the number of residues. The positions marked # are those that are important for the stable fold of the zinc finger. The final position can be either his or cys. The C2H2 zinc finger is composed of two short beta strands followed by an alpha helix. The amino terminal part of the helix binds the major groove in DNA binding zinc fingers. The accepted consensus binding sequence for Sp1 is usually defined by the asymmetric hexanucleotide core GGGCGG but this sequence does not include, among others, the GAG (=CTC) repeat that constitutes a high-affinity  site for Sp1 binding to the wt1 promoter [2].", "database": "PfamA", "aliStart": 422, "scoreName": "E-value", "accession": "PF00096.24", "start": 420, "score": 1.2e-13, "identifier": "Zinc finger, C2H2 type", "type": "DBD", "aliEnd": 442}}, {"startStyle": "curved", "end": 469, "endStyle": "curved", "aliStart": 448, "text": "zfC2H2", "colour": "#228B22", "aliEnd": 469, "start": 448, "href": "http://pfam.xfam.org/family/PF00096.24", "type": "pfama", "display": "true", "metadata": {"end": 469, "description": "The C2H2 zinc finger is the classical zinc finger domain. The two conserved cysteines and histidines co-ordinate a zinc ion. The following pattern describes the zinc finger. #-X-C-X(1-5)-C-X3-#-X5-#-X2-H-X(3-6)-[H/C] Where X can be any amino acid, and numbers in brackets indicate the number of residues. The positions marked # are those that are important for the stable fold of the zinc finger. The final position can be either his or cys. The C2H2 zinc finger is composed of two short beta strands followed by an alpha helix. The amino terminal part of the helix binds the major groove in DNA binding zinc fingers. The accepted consensus binding sequence for Sp1 is usually defined by the asymmetric hexanucleotide core GGGCGG but this sequence does not include, among others, the GAG (=CTC) repeat that constitutes a high-affinity  site for Sp1 binding to the wt1 promoter [2].", "database": "PfamA", "aliStart": 448, "scoreName": "E-value", "accession": "PF00096.24", "start": 448, "score": 1.2e-13, "identifier": "Zinc finger, C2H2 type", "type": "DBD", "aliEnd": 469}}, {"startStyle": "straight", "end": 129, "endStyle": "straight", "aliStart": 24, "text": "BTB", "colour": "#9999ff", "aliEnd": 127, "start": 24, "href": "http://pfam.xfam.org/family/PF00651.29", "type": "pfama", "display": "true", "metadata": {"end": 129, "description": "The BTB (for BR-C, ttk and bab) [1] or POZ (for Pox virus and Zinc finger) [2] domain is present near the N-terminus of a fraction of zinc finger (Pfam:PF00096) proteins and in proteins that contain the Pfam:PF01344 motif such as Kelch and a family of pox virus proteins. The BTB/POZ domain mediates homomeric dimerisation and in some instances heteromeric dimerisation [2]. The structure of the dimerised PLZF BTB/POZ domain has been solved and consists of a tightly intertwined homodimer.  The central scaffolding of the protein is made up of a cluster of alpha-helices flanked by short beta-sheets at both the top and bottom of the molecule [3]. POZ domains from several zinc finger proteins have been shown to mediate transcriptional repression and to interact with components of histone deacetylase co-repressor complexes including N-CoR and SMRT [4,5,6]. The POZ or BTB domain is also known as BR-C/Ttk or ZiN.", "database": "PfamA", "aliStart": 24, "scoreName": "E-value", "accession": "PF00651.29", "start": 24, "score": 3.4e-32, "identifier": "BTB/POZ domain", "type": "DBD", "aliEnd": 127}}], "length": 620}

{"regions": [{"startStyle": "straight", "end": 67, "endStyle": "jagged", "aliStart": 24, "text": "BTB", "colour": "#9999ff", "aliEnd": 66, "start": 24, "href": "http://pfam.xfam.org/family/PF00651.29", "type": "pfama", "display": "true", "metadata": {"end": 67, "description": "The BTB (for BR-C, ttk and bab) [1] or POZ (for Pox virus and Zinc finger) [2] domain is present near the N-terminus of a fraction of zinc finger (Pfam:PF00096) proteins and in proteins that contain the Pfam:PF01344 motif such as Kelch and a family of pox virus proteins. The BTB/POZ domain mediates homomeric dimerisation and in some instances heteromeric dimerisation [2]. The structure of the dimerised PLZF BTB/POZ domain has been solved and consists of a tightly intertwined homodimer.  The central scaffolding of the protein is made up of a cluster of alpha-helices flanked by short beta-sheets at both the top and bottom of the molecule [3]. POZ domains from several zinc finger proteins have been shown to mediate transcriptional repression and to interact with components of histone deacetylase co-repressor complexes including N-CoR and SMRT [4,5,6]. The POZ or BTB domain is also known as BR-C/Ttk or ZiN.", "database": "PfamA", "aliStart": 24, "scoreName": "E-value", "accession": "PF00651.29", "start": 24, "score": 4.4e-15, "identifier": "BTB/POZ domain", "type": "DBD", "aliEnd": 66}}], "length": 67}

TF Info Page for ZBTB7C (C2H2 ZF(non-KRAB))

Conclusion

Description

Previous Annotations

DNA-Binding

Published Motif Data

Structure

Experimental History

External Contribution