human FIP1L1 Over-expression AAV

factor interacting with PAP; FIP1; FIP1 like 1; FIP1L1 cleavage and polyadenylation specific factor subunit; FIP1-like 1 protein; hFip1; pre-mRNA 3'-end-processing factor FIP1; rearranged in hypereosinophilia; Rhe

FIP1 was originally identified as Rhe (rearranged in hypereosinophilia) and part of a fusion protein encoded by a genetic rearrangement between the N-terminal region of FIP1 (Rhe) and the C-terminal region of the platelet-derived growth factor receptor alpha (PDGFRalpha). The fusion protein exhibits aberrant tyrosine kinase activity and is associated with hypereosinophilic syndrome (HES), a rare hematologic disorder characterized by an overproduction of eosinophils that results in organ damage. FIP1 was also identified as FIP1-like 1 in a database search for a human homolog of the yeast Fip1p (factor interacting with PAP), a subunit of the yeast 3’-end processing complex, CPF (cleavage and polyadenylation factor). Human FIP1 was similarly found to interact with PAP and CPSF160 as part of the human CPSF (cleavage and polyadenylation specificity factor) complex. In association with CPSF160, FIP1 is able to recognize U-rich elements on pre-mRNA and stimulate PAP activity.

FIP1L1 encodes a subunit of the CPSF (cleavage and polyadenylation specificity factor) complex that polyadenylates the 3' end of mRNA precursors. This gene, the homolog of yeast Fip1 (factor interacting with PAP), binds to U-rich sequences of pre-mRNA and stimulates poly(A) polymerase activity. Its N-terminus contains a PAP-binding site and its C-terminus an RNA-binding domain. An interstitial chromosomal deletion on 4q12 creates an in-frame fusion of human genes FIP1L1 and PDGFRA (platelet-derived growth factor receptor, alpha). The FIP1L1-PDGFRA fusion gene encodes a constitutively activated tyrosine kinase that joins the first 233 amino acids of FIP1L1 to the last 523 amino acids of PDGFRA. FIP1L1 fusion and chromosomal deletion is the cause of some forms of idiopathic hypereosinophilic syndrome (HES). This syndrome, recently reclassified as chronic eosinophilic leukemia (CEL), is responsive to treatment with tyrosine kinase inhibitors. Alternative splicing results in multiple transcript variants encoding distinct isoforms.

81608

factor interacting with PAPOLA and CPSF1

factor interacting with PAPOLA and CPSF1

FIP1L1

HGNC:19124

9606.0

1137

1137 bp

Pre-mRNA 3'-end-processing factor FIP1

NM_030917

NM_030917, NM_001134938, NM_001134937, BC110383, BC052959, BC024016, BC017724,

mRNA Processing,RNA Binding,RNA Processing

cell_biology,genetics,transcription_translation

human

FIP1 was originally identified as Rhe (rearranged in hypereosinophilia) and part of a fusion protein encoded by a genetic rearrangement between the N-terminal region of FIP1 (Rhe) and the C-terminal region of the platelet-derived growth factor receptor alpha (PDGFRalpha). The fusion protein exhibits aberrant tyrosine kinase activity and is associated with hypereosinophilic syndrome (HES), a rare hematologic disorder characterized by an overproduction of eosinophils that results in organ damage. FIP1 was also identified as FIP1-like 1 in a database search for a human homolog of the yeast Fip1p (factor interacting with PAP), a subunit of the yeast 3’-end processing complex, CPF (cleavage and polyadenylation factor). Human FIP1 was similarly found to interact with PAP and CPSF160 as part of the human CPSF (cleavage and polyadenylation specificity factor) complex. In association with CPSF160, FIP1 is able to recognize U-rich elements on pre-mRNA and stimulate PAP activity.

Hs.624245

Q6UN15