KHDRBS1: A Potential Drug Target for Cellular Processes (G10657)

Target Name: KHDRBS1

NCBI ID: G10657

Other Name(s): GAP-associated tyrosine phosphoprotein p62 (Sam68) | src-associated in mitosis 68 kDa protein | KH domain containing, RNA binding, signal transduction associated 1 | GAP-associated tyrosine phosphoprotein p62 | Src-associated in mitosis 68 kDa protein | p21 Ras GTPase-activating protein-associated p62 | p62 | KH domain-containing, RNA-binding, signal transduction-associated protein 1 (isoform 1) | KH RNA binding domain containing, signal transduction associated 1, transcript variant 1 | KH RNA binding domain containing, signal transduction associated 1 | KH domain-containing, RNA-binding, signal transduction-associated protein 1 | KHDR1_HUMAN | KHDRBS1 variant 1 | p68 | Sam68 | FLJ34027

KHDRBS1: A Potential Drug Target for Cellular Processes

KHDRBS1 (GAP-associated tyrosine phosphoprotein p62) is a protein that is expressed in various tissues throughout the body, including the brain, heart, and kidneys. It is a member of the GAP-associated tyrosine phosphoprotein (GAP-TP) family, which is a group of proteins that are involved in a variety of cellular processes, including cell signaling, protein synthesis, and stress response.

One of the unique features of KHDRBS1 is its ability to interact with the protein p62, which is also known as Sam68. p62 is a protein that is involved in the regulation of the cytoskeleton, and it has been shown to play a role in a variety of cellular processes, including cell signaling and the regulation of cytoskeleton-associated structures.

KHDRBS1 has been shown to interact with p62 in a number of different ways. For example, studies have shown that KHDRBS1 and p62 can form a complex in cells, and that this complex is involved in the regulation of a variety of cellular processes, including cell signaling, protein synthesis, and stress response.

In addition to its interactions with p62, KHDRBS1 has also been shown to play a role in the regulation of cellular processes that are independent of its interaction with p62. For example, studies have shown that KHDRBS1 is involved in the regulation of the cytoskeleton, cell adhesion, and cell migration.

Given the unique role that KHDRBS1 plays in the regulation of cellular processes, it is a promising target for drug development. Studies have shown that inhibiting the activity of KHDRBS1 has the potential to treat a variety of diseases, including cancer, neurodegenerative diseases, and autoimmune disorders.

In conclusion, KHDRBS1 is a protein that is involved in a variety of cellular processes, including cell signaling, protein synthesis, and stress response. Its interaction with the protein p62 makes it a promising target for drug development, and its role in the regulation of cellular processes makes it a valuable biomarker for a variety of diseases. Further research is needed to fully understand the function of KHDRBS1 and its potential as a drug target.

Protein Name: KH RNA Binding Domain Containing, Signal Transduction Associated 1

Functions: Recruited and tyrosine phosphorylated by several receptor systems, for example the T-cell, leptin and insulin receptors. Once phosphorylated, functions as an adapter protein in signal transduction cascades by binding to SH2 and SH3 domain-containing proteins. Role in G2-M progression in the cell cycle. Represses CBP-dependent transcriptional activation apparently by competing with other nuclear factors for binding to CBP. Also acts as a putative regulator of mRNA stability and/or translation rates and mediates mRNA nuclear export. Positively regulates the association of constitutive transport element (CTE)-containing mRNA with large polyribosomes and translation initiation. According to some authors, is not involved in the nucleocytoplasmic export of unspliced (CTE)-containing RNA species according to (PubMed:22253824). RNA-binding protein that plays a role in the regulation of alternative splicing and influences mRNA splice site selection and exon inclusion. Binds to RNA containing 5'-[AU]UAA-3' as a bipartite motif spaced by more than 15 nucleotides. Binds poly(A). Can regulate CD44 alternative splicing in a Ras pathway-dependent manner (By similarity). In cooperation with HNRNPA1 modulates alternative splicing of BCL2L1 by promoting splicing toward isoform Bcl-X(S), and of SMN1 (PubMed:17371836, PubMed:20186123). Can regulate alternative splicing of NRXN1 and NRXN3 in the laminin G-like domain 6 containing the evolutionary conserved neurexin alternative spliced segment 4 (AS4) involved in neurexin selective targeting to postsynaptic partners. In a neuronal activity-dependent manner cooperates synergistically with KHDRBS2/SLIM-1 in regulation of NRXN1 exon skipping at AS4. The cooperation with KHDRBS2/SLIM-1 is antagonistic for regulation of NXRN3 alternative splicing at AS4 (By similarity)

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