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Zinc fingers were first identified in a study of transcription in the African clawed frog, Xenopus laevis in the laboratory of Aaron Klug.A study of the transcription of a particular RNA sequence revealed that the binding strength of a small transcription factor (transcription factor IIIA; TFIIIA) was due to the presence of zinc-coordinating finger-like structures. [6]
Zinc finger Y-chromosomal protein is a protein that in humans is encoded by the ZFY gene of the Y chromosome. [3] [4] This gene encodes a zinc finger-containing protein that may function as a transcription factor. This gene was once a candidate gene for the testis-determining factor (TDF) and was erroneously referred to as TDF. [4]
2735 14632 Ensembl ENSG00000111087 ENSMUSG00000025407 UniProt P08151 P47806 RefSeq (mRNA) NM_001160045 NM_001167609 NM_005269 NM_010296 RefSeq (protein) NP_001153517 NP_001161081 NP_005260 NP_034426 Location (UCSC) Chr 12: 57.46 – 57.47 Mb Chr 10: 127.17 – 127.18 Mb PubMed search Wikidata View/Edit Human View/Edit Mouse Zinc finger protein GLI1 also known as glioma-associated oncogene is a ...
The zinc finger domains do not appear to bind nucleosomes well and can be displaced by FOX factors. [ 22 ] In the skin epidermis, SOX family transcription factor, SOX9 , also behaves as a pioneer factor that governs hair follicle cell fate and can reprogram epidermal stem cells to a hair follicle fate.
This gene on the X chromosome is structurally similar to a related gene on the Y chromosome ().It encodes a member of the krüppel C2H2-type zinc-finger protein family. The full-length protein contains an acidic transcriptional activation domain (AD), a nuclear localization sequence (NLS) and a DNA binding domain (DBD) consisting of 13 C2H2-type zinc fingers.
Zinc finger protein 91 homolog is a protein that in humans is encoded by the ZFP91 gene. [5] [6] The protein encoded by this gene is a member of the zinc finger family of proteins. The gene product contains C2H2 type domains, which are the classical zinc finger domains found in numerous nucleic acid-binding proteins.
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The FYVE domain is composed of two small beta hairpins (or zinc knuckles) followed by an alpha helix. [5] The FYVE finger binds two zinc ions. The FYVE finger has eight potential zinc coordinating cysteine positions and is characterized by having basic amino acids around the cysteines.
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