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findings indicate that SCYL1 (show CCL13 Proteins) does not contribute to REST turnover and thus do not support a previous study suggesting a role for SCYL1 (show CCL13 Proteins) in mediating REST degradation
Disruptive SCYL1 mutations underlie a syndrome characterized by recurrent episodes of liver failure, peripheral neuropathy, cerebellar atrophy, and ataxia.
Data identified the large GTPase (show RACGAP1 Proteins) dynamin2 as an interacting protein of NTKL, which might be responsible for the phenotype alterations caused by NTKL overexpression, such as cytokinesis failure, increased cell motility and abnormal of cell division.
Data reveal that Scyl1 (show CCL13 Proteins) is a key organizer of a subset of the COPI machinery.
TEIF is a downstream effector in EGF (show EGF Proteins)/PI3K (show PIK3CA Proteins)/Akt (show AKT1 Proteins) signaling.
TEIF as a novel MSP58 (show MCRS1 Proteins)-interacting protein.
suggested that the interaction of SCYL1BP1 (show GORAB Proteins)/Pirh2 (show RCHY1 Proteins) could accelerate Pirh2 (show RCHY1 Proteins) degradation through an ubiquitin-dependent pathway. SCYL1BP1 (show GORAB Proteins) may function as an important tumor suppressor gene in HCC (show FAM126A Proteins) development
Scyl1 (show CCL13 Proteins) interacts with 58K/formiminotransferase cyclodeaminase (FTCD (show FTCD Proteins)) and golgin p115, and is required for the maintenance of Golgi morphology
Scyl1 (show CCL13 Proteins) participates in the nuclear aminoacylation-dependent tRNA export pathway.
SCYL1-BP1 (show GORAB Proteins) can be ubiquitinated and degraded by Pirh2 (show RCHY1 Proteins) but not by MDM2 (show MDM2 Proteins), which suggests that SCYL1-BP1 (show GORAB Proteins) can be regulated by Pirh2 (show RCHY1 Proteins).
our results identify SCYL1 as a key regulator of motor neuron survival
Mutation in the Scyl1 gene encoding amino-terminal kinase-like protein (show PTK7 Proteins) causes a recessive form of spinocerebellar neurodegeneration.
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, and also to the cytoplasm and centrosomes during mitosis. Multiple transcript variants encoding different isoforms have been found for this gene.
SCY1 family protein kinase
, N-terminal kinase-like protein
, SCY1-like 1 (S. cerevisiae)
, n-terminal kinase-like protein-like
, SCY1-like protein 1
, coated vesicle-associated kinase of 90 kDa
, likely ortholog of mouse N-terminal kinase-like protein
, telomerase regulation-associated protein
, telomerase transcriptional element-interacting factor
, telomerase transcriptional elements-interacting factor
, teratoma-associated tyrosine kinase
, 105 kDa kinase-like protein
, SCY1-like 1 splice variant 13
, SCY1-like 1 splice variant 15
, mitosis-associated kinase-like protein NTKL
, ubiquitous protein kinase-like (105 kDa)