SCYL1 [SEP] found in taxon
SCYL1
SCY1-like 1 (S. cerevisiae), also known as SCYL1, is a human gene which is highly conserved throughout evolution.
Function.
This gene encodes a transcriptional regulator belonging to the SCY1-like family of kinase-like proteins. The protein has a divergent N-terminal kinase domain that is thought to be catalytically inactive, and can bind specific DNA sequences through its C-terminal domain. It activates transcription of the telomerase reverse transcriptase and DNA polymerase beta genes. The protein has been localized to the nucleus,
also contains multiple dibasic motifs, and ends in the dibasic motif RKLD-COOH.
Scyl1 localizes to the cis-Golgi and ER-Golgi Intermediate Compartment (ERGIC). Scyl1 binds to Coatomer I (COPI) and colocalizes with beta-COPI and ERGIC53. siRNA mediated knockdown of the protein disrupted retrograde flow of the KDEL receptor from the Golgi to the ER. Furthermore, Scyl1 localization in rat hippocampal neurons also demonstrates a similar relationship to COPI.
Clinical significance.
Mutations in Scyl1 are the genetic defect resulting