CSRNP1

CSRNP1 (Cysteine And Serine Rich Nuclear Protein 1) is a Protein Coding gene. Gene Ontology (GO) annotations related to this gene include DNA binding transcription factor activity and transcriptional activator activity, RNA polymerase II transcription regulatory region sequence-specific DNA binding. An important paralog of this gene is CSRNP3.

Cysteine And Serine Rich Nuclear Protein 1

Binds to the consensus sequence 5'-AGAGTG-3' and has transcriptional activator activity (By similarity).

May have a tumor-suppressor function. May play a role in apoptosis.

Apoptotic process Source: UniProtKB
Face morphogenesis Source: Ensembl
Platelet-derived growth factor receptor signaling pathway Source: Ensembl
Positive regulation of transcription by RNA polymerase II Source: UniProtKB
Post-embryonic development Source: Ensembl
Regulation of transcription by RNA polymerase II Source: GO_Central
Roof of mouth development Source: Ensembl
Skeletal system morphogenesis Source: Ensembl

Nucleus

SRC kinase activity has been shown to be increased in several tumor tissues and tumor cell lines such as colon carcinoma cells.
Thrombocytopenia 6 (THC6):
A form of thrombocytopenia, a hematologic disorder defined by a decrease in the number of platelets in circulating blood, resulting in the potential for increased bleeding and decreased ability for clotting. THC6 is an autosomal dominant form. Affected individuals may also have bone abnormalities and an increased risk for myelofibrosis.

Myristoylated at Gly-2, and this is essential for targeting to membranes.
Dephosphorylated at Tyr-530 by PTPRJ (By similarity). Phosphorylated on Tyr-530 by c-Src kinase (CSK). The phosphorylated form is termed pp60c-src. Dephosphorylated by PTPRJ at Tyr-419. Normally maintained in an inactive conformation with the SH2 domain engaged with Tyr-530, the SH3 domain engaged with the SH2-kinase linker, and Tyr-419 dephosphorylated. Dephosphorylation of Tyr-530 as a result of protein tyrosine phosphatase (PTP) action disrupts the intramolecular interaction between the SH2 domain and Tyr-530, Tyr-419 can then become autophosphorylated, resulting in SRC activation. Phosphorylation of Tyr-530 by CSK allows this interaction to reform, resulting in SRC inactivation. CDK5-mediated phosphorylation at Ser-75 targets SRC to ubiquitin-dependent degradation and thus leads to cytoskeletal reorganization. Phosphorylated by PTK2/FAK1; this enhances kinase activity. Phosphorylated by PTK2B/PYK2; this enhances kinase activity. Upon activation of IL6ST by IL6, Tyr-419 is phosphorylated and Tyr-530 dephosphorylated (PubMed:25731159).
S-nitrosylation is important for activation of its kinase activity.
Ubiquitinated in response to CDK5-mediated phosphorylation. Ubiquitination mediated by CBLC requires SRC autophosphorylation at Tyr-419 and may lead to lysosomal degradation.