NFYA

Also known as CBF-A, CBF-B, HAP2, NF-YA, nuclear transcription factor Y subunit alpha

Nuclear transcription factor Y subunit alpha is a protein that in humans is encoded by the NFYA gene.

Gene data

NFYA

Name: nuclear transcription factor Y subunit alpha
Type: protein-coding
Aliases: CBF-A, CBF-B, HAP2, NF-YA

The protein encoded by this gene is one subunit of a trimeric complex, forming a highly conserved transcription factor that binds to CCAAT motifs in the promoter regions in a variety of genes. Subunit A associates with a tight dimer composed of the B and C subunits, resulting in a trimer that binds to DNA with high specificity and affinity. The sequence specific interactions of the complex are made by the A subunit, suggesting a role as the regulatory subunit. In addition, there is evidence of post-transcriptional regulation in this gene product, either by protein degradation or control of translation. Further regulation is represented by alternative splicing in the glutamine-rich activation domain, with clear tissue-specific preferences for the two isoforms. [provided by RefSeq, Jul 2008].

via MyGene.info

Wikidata facts

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HomoloGene ID: 32114
exact match: identifiers.org/ncbigene/4800
genomic end: 41102403
genomic start: 41072974
cytogenetic location: 6p21.1

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Article

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Contents

Function
Interactions
Structure
References
Further reading
External links

Nuclear transcription factor Y subunit alpha is a protein that in humans is encoded by the NFYA gene.

== Function == The protein encoded by this gene is one subunit of a trimeric complex NF-Y, forming a highly conserved transcription factor that binds to CCAAT motifs in the promoter regions in a variety of genes. Subunit NFYA associates with a tight dimer composed of the NFYB and NFYC subunits, resulting in a trimer that binds to DNA with high specificity and affinity. The sequence specific interactions of the complex are made by the NFYA subunit, suggesting a role as the regulatory subunit. In addition, there is evidence of post-transcriptional regulation in this gene product, either by protein degradation or control of translation. Further regulation is represented by alternative splicing in the glutamine-rich activation domain, with clear tissue-specific preferences for the two isoforms.