ZBTB6,
https://www.ncbi.nlm.nih.gov/gene/10773
- Official
Symbol ZBTB6
- Official
Full Name zinc finger and BTB domain containing 6provided by HGNC
- Also known as ZID; ZNF482
- Expression Ubiquitous expression in lymph node (RPKM 5.7), thyroid (RPKM 5.5) and 25 other tissues See more Orthologs mouse
all
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NM_006626.6 → NP_006617.1 zinc finger and BTB domain-containing protein 6
See identical proteins and their annotated locations for NP_006617.1
- Conserved Domains (5) summary
-
- sd00017
Location:328 → 348
- ZF_C2H2; C2H2 Zn finger [structural motif]
- pfam00096
Location:326 → 348
- zf-C2H2; Zinc finger, C2H2 type
- pfam00651
Location:23 → 127
- BTB; BTB/POZ domain
- pfam13465
Location:340 → 364
- zf-H2C2_2; Zinc-finger double domain
- pfam15909
Location:331 → 401
- zf-C2H2_8; C2H2-type zinc ribbon
Related articles in PubMed
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The POZ domain: a conserved protein-protein interaction motif.
Bardwell VJ, et al. Genes Dev, 1994 Jul 15. PMID 795884 Abstract
We describe a novel
zinc finger protein, ZID (zinc finger protein with interaction domain).
At its amino terminus ZID contains a 120-amino-acid conserved motif
present in a large family of proteins that includes both the otherwise
unrelated zinc finger proteins, such as Ttk, GAGA, and ZF5, and a group
of poxvirus proteins: We therefore refer to this domain as the POZ
(poxvirus and zinc finger) domain. The POZ domains of ZID, Ttk, and GAGA
act to inhibit the interaction of their associated finger regions with
DNA. This inhibitory effect is not dependent on interactions with other
proteins and does not appear dependent on specific interactions between
the POZ domain and the finger region. The POZ domain acts as a specific
protein-protein interaction domain: The POZ domains of ZID and Ttk can
interact with themselves but not with each other, POZ domains from ZF5,
or the viral protein SalF17R. However, the POZ domain of GAGA can
interact efficiently with the POZ domain of Ttk. In transfection
experiments, the ZID POZ domain inhibits DNA binding in NIH-3T3 cells
and appears to localize the protein to discrete regions of the nucleus.
We discuss the implications of multimerization for the function of POZ
domain proteins.
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NAC1, a POZ/BTB protein that functions as a corepressor.
Korutla L, et al. Neurochem Int, 2009 Mar-Apr. PMID 19121354We now demonstrate that NAC1 acts as a corepressor for other POZ/BTB
proteins. NAC1 is a POZ/BTB motif containing transcriptional repressor
protein. In a mammalian two hybrid assay in neuronal (N2A) cells and
non-neuronal (HEK 293T) cells, VP16 activation domain tagged NAC1
resulted in significant reversal of transcriptional inhibition with the
Gal4-ZID, Gal4-BCL6, Gal4-ZF5, and kelch proteins Gal4-MAYVEN (KLHL2) and
Gal4-NRP/B fusion proteins. We also observed similar results with
another corepressor, BCoR Gal4 fusion protein. NAC1 potentiated ZF5
mediated repression in Gal4-DBD fusion transient assays. GST pulldown
assays further confirmed protein-protein interactions between these
proteins and NAC1. Both the NAC1 isoforms demonstrated selective
interaction through the POZ/BTB domain but not with the non-POZ/BTB
region. Endogenous NAC1 and BCL6 physically associated in CNS regions.
Strikingly, NAC1 did not interact with the pro-myelocytic leukemia zinc
finger protein (PLZF/ZBTB16) ), another POZ/BTB protein that is not found in the
adult brain. Therefore, we conclude that NAC1 functions as a corepressor
for POZ/BTB proteins expressed in the mature CNS.
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Functional proteomics mapping of a human signaling pathway.
Colland F, et al. Genome Res, 2004 Jul. PMID 15231748, Free PMC Article
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An atlas of combinatorial transcriptional regulation in mouse and man.
Ravasi T, et al. Cell, 2010 Mar 5. PMID 20211142, Free PMC Article
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A proteome-scale map of the human interactome network.
Rolland T, et al. Cell, 2014 Nov 20. PMID 25416956, Free PMC Article
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