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Literature summary for 2.7.7.14 extracted from

  • Pavlovic, Z.; Singh, R.K.; Bakovic, M.
    A novel murine CTP:phosphoethanolamine cytidylyltransferase splice variant is a post-translational repressor and an indicator that both cytidylyltransferase domains are required for activity (2014), Gene, 543, 58-68.
    View publication on PubMed
Search for more literature for 2.7.7.14

Protein Variants

Protein Variants Comment Organism
H244A inactive C-domain mutant, presence of the mutant reduces splice variant Pcyt2alpha homodimerization and activity Mus musculus
H244Y inactive C-domain mutant, presence of the mutant reduces splice variant Pcyt2alpha homodimerization and activity Mus musculus
H35A inactive N-domain mutant, presence of the mutant reduces splice variant Pcyt2alpha homodimerization and activity Mus musculus
H35Y inactive N-domain mutant, presence of the mutant reduces splice variant Pcyt2alpha homodimerization and activity Mus musculus

Organism

Organism UniProt Comment Textmining
Mus musculus Q540F5
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Source Tissue

Source Tissue Comment Organism Textmining
kidney splice variant Pcyt2gamma Mus musculus
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additional information splice variant Pcyt2gamma is ubiquitously expressed in embryonic and adult mouse tissues, and is the most abundant in the kidney, skeletal muscle and testis Mus musculus
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skeletal muscle splice variant Pcyt2gamma Mus musculus
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testis splice variant Pcyt2gamma Mus musculus
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Synonyms

Synonyms Comment Organism
Pcyt2
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 Mus musculus

General Information

General Information Comment Organism
physiological function mouse isoform Pcyt2 can be spliced at introns 7 and 8 to produce a unique isoform, Pcyt2gamma, in which the second cytidylyltransferase domain at the C-terminus becomes deleted. Pcyt2gamma is ubiquitously expressed in embryonic and adult mouse tissues, and is the most abundant in the kidney, skeletal muscle and testis. Pcyt2gamma splicing mechanism dominates over splice variant Pcyt2beta exon-skipping mechanism in most examined tissues. Pcyt2gamma maintains the N-terminal cytidylyltransferase domain, but the lack of the C-terminal cytidylyltransferase domain causes a complete loss of catalytic activity. Pcyt2gamma interacts with the active isoform, splice variant Pcyt2alpha, and significantly reduces Pcyt2alpha homodimerization and activity Mus musculus