Anti-SCYL1 from rabbit, purified by affinity chromatography

N-terminal kinase-like protein (UniProt: Q96KG9; also known as Coated vesicle-associated kinase of 90 kDa, SCY1-like protein 1, Telomerase regulation-associated protein, Telomerase transcriptional element-interacting factor, Teratoma-associated tyrosine kinase) is encoded by the SCYL1 (also known as CVAK90, GKLP, NTKL, TAPK, TEIF, TRAP, HT019) gene (Gene ID: 57410) in human. SCY1-like protein 1 is ubiquitously expressed and it regulates COPI-mediated retrograde protein traffic at the interface between the Golgi apparatus and the endoplasmic reticulum. It is involved in the maintenance of the Golgi apparatus morphology. It has a divergent N-terminal kinase domain (aa 14-314), but it is catalytically inactive. It also contain three HEAT repeats (aa 350-388; 389-427; and 507-545). Six isoforms of SCY1-like protein 1 have been reported that are produced by alternative splicing. Its intracellular distribution is isoform specific. Isoforms 1 and 2 are shown to be cytoplasmic throughout the cell cycle. Isoform 3 is cytoplasmic during interphase and centrosomal during mitosis. Isoform six is generally localized to nucleus and it acts as a transcriptional activator and binds to three different types of GC-rich DNA binding sites (box-A, -B and -C) in the beta-polymerase promoter region. Mutations in SCYL1 gene are reported to cause Spinocerebellar ataxia, a clinically and genetically heterogeneous group of cerebellar disorders due to degeneration of the cerebellum with variable involvement of the brainstem and spinal cord.