KHDRBS1 Antibody
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Product Specs
Buffer
PBS with 0.1% Sodium Azide, 50% Glycerol, pH 7.3. Store at -20°C. Avoid freeze/thaw cycles.
Lead Time
Typically, we can ship the products within 1-3 business days after receiving your order. Delivery times may vary depending on the purchasing method or location. Please consult your local distributors for specific delivery timeframes.
Synonyms
FLJ34027 antibody; GAP associated tyrosine phosphoprotein p62 antibody; GAP-associated tyrosine phosphoprotein p62 antibody; KH domain containing RNA binding signal transduction associated 1 antibody; KH domain-containing antibody; KHDR1_HUMAN antibody; Khdrbs1 antibody; p21 Ras GTPase activating protein associated p62 antibody; p21 Ras GTPase-activating protein-associated p62 antibody; p62 antibody; p68 antibody; RNA-binding antibody; Sam68 antibody; signal transduction-associated protein 1 antibody; Src associated in mitosis 68 kDa protein antibody; Src-associated in mitosis 68 kDa protein antibody
Target Names
KHDRBS1
Uniprot No.
Target Background
Function
KHDRBS1, also known as Sam68, is a protein that is recruited and tyrosine phosphorylated by various receptor systems, including the T-cell, leptin, and insulin receptors. Following phosphorylation, it acts as an adapter protein in signal transduction cascades by interacting with SH2 and SH3 domain-containing proteins. It plays a crucial role in G2-M progression during the cell cycle and represses CBP-dependent transcriptional activation by competing with other nuclear factors for binding to CBP. Additionally, KHDRBS1 acts as a potential regulator of mRNA stability and/or translation rates, mediating mRNA nuclear export. It positively regulates the association of constitutive transport element (CTE)-containing mRNA with large polyribosomes and translation initiation. According to some authors, it is not involved in the nucleocytoplasmic export of unspliced (CTE)-containing RNA species. It is an RNA-binding protein involved in regulating alternative splicing, influencing mRNA splice site selection and exon inclusion. It binds to RNA containing 5'-[AU]UAA-3' as a bipartite motif spaced by more than 15 nucleotides and binds poly(A). It can regulate CD44 alternative splicing in a Ras pathway-dependent manner. In collaboration with HNRNPA1, it modulates alternative splicing of BCL2L1 by promoting splicing towards the isoform Bcl-X(S), and of SMN1. It can also regulate alternative splicing of NRXN1 and NRXN3 in the laminin G-like domain 6 containing the evolutionary conserved neurexin alternative spliced segment 4 (AS4), which is involved in neurexin selective targeting to postsynaptic partners. In a neuronal activity-dependent manner, it cooperates synergistically with KHDRBS2/SLIM-1 in regulating NRXN1 exon skipping at AS4. This cooperation with KHDRBS2/SLIM-1 is antagonistic for the regulation of NXRN3 alternative splicing at AS4. Isoform 3, specifically expressed in growth-arrested cells, inhibits S phase.
Gene References Into Functions
- Furthermore, SRSF10, hnRNP A1/A2, and Sam68 collaborate to drive the DNA damage-induced splicing response of several transcripts that produce components involved in apoptosis, cell-cycle control, and DNA repair. PMID: 29396485
- SAM68 is essential for the efficient recruitment of PUM2 to NORAD, regulation of Pum activity by NORAD, and proper chromosome segregation in mammalian cells. PMID: 29386330
- Research has shown that upregulation of Sam68 significantly inhibits cisplatin-induced apoptosis in oral tongue squamous cell carcinoma cells. PMID: 27473117
- The PRMT2 interacts with SAM68 in cells and regulates its subcellular localization via the SH3 domain of PRMT2, leading to an investigation into the potential role of PRMT2 in BCL-X alternative splicing. PMID: 28057797
- Data suggests that the first 22 bp of exon 3 in BIRC5 contain cis-acting elements that enhance the exclusion of exon 3 to generate the survivin DEx3 mRNA isoform via exclusion/deletion of exon 3. Sam68 is a possible trans-acting factor that binds to this cis-acting element and regulates exon 3 splicing. (BIRC5/survivin = baculoviral IAP repeat containing 5; Sam68 = GAP-associated tyrosine phosphoprotein p62) PMID: 28655776
- Our findings indicate that Sam68 modulates apoptosis of intestinal epithelial cells by mediating NF-kappaB activation in ulcerative colitis. PMID: 27235792
- Sam68 potentially participates in the progression of T-acute lymphoblastic leukemia, at least partially through the AKT/mTOR signaling pathway. PMID: 27107742
- Sam68 is essential for DNA damage-induced NF-kappaB activation and colon tumorigenesis. PMID: 27458801
- These discoveries define a novel mechanism of action for Sam68 in governing p53 transcriptional activation and represent the first report of Sam68 in the regulation of tumor suppressor activities. PMID: 27365047
- HNRNPL functions as the adaptor to combine the two substructures and form the intact Sam68 nuclear body through the interaction of two sets of RNA recognition motifs with the putative architectural RNA in the respective substructures. PMID: 27377249
- Sam68 was overexpressed in EOC tissue in association with cancer malignant factors such as FIGO stage, histological grade, and lymph node metastasis. It also positively regulates the proliferation of EOC cells. PMID: 27623016
- Collectively, these results demonstrate that enterovirus 71 infections can induce stress granule formation, and Sam68, as a stress granule component, migrates along with stress granules, dependent on intact microtubules, upon viral infections. PMID: 27057671
- The host factor Sam68 interacts with both foot-and-mouth disease virus RNA motifs in the internal ribosome binding site and viral non-structural proteins 3C(pro) and 3D(pol). PMID: 26695943
- Sam68 has separable effects on the regulation of AR-V7 expression and transcriptional activity, through its RNA-binding capacity. PMID: 26310125
- The RNA-binding protein Sam68 regulates tumor cell viability and hepatic carcinogenesis by inhibiting the transcriptional activity of FOXOs. PMID: 26438629
- Sam68 Promotes NF-kappaB Activation and Apoptosis Signaling in Articular Chondrocytes during Osteoarthritis. PMID: 26350037
- MicroRNA-203 inhibits the malignant progression of neuroblastoma by targeting Sam68. PMID: 26136151
- This review summarizes recent studies on the role of SAM68 in splicing regulation and discusses its contribution to aberrant pre-mRNA processing in cancer. PMID: 26273626
- Sam68 could promote esophageal squamous cell carcinoma (ESCC) cell proliferation via the activation of the Akt/GSK-3beta pathway. This research suggests that Sam68 might accelerate cell cycle progression and be considered as a new therapeutic target in ESCC. PMID: 26050229
- Results show that SAM68 expression is increased in muscle invasive bladder cancer (MIBC) and correlated with poor prognosis, suggesting it as a potentially useful prognostic marker for MIBC. PMID: 25944080
- Conclusively, the cleavage of Sam68 is a new indicator for the cell-damaging effects of ionizing radiation. PMID: 25666188
- The nuclear protein Sam68 is identified as an additional new host factor that interacts with the enterovirus 71 IRES during infection and could potentially enhance the translation of virus protein. PMID: 26202240
- Results reveal the complex molecular mechanism underlying SMAR1-mediated signal-dependent and -independent regulation of alternative splicing via Sam68 deacetylation. PMID: 26080397
- Sam68 may be a useful prognostic marker for EC and plays an important role in promoting cellular proliferation. PMID: 25874492
- The expression of Sam68 was significantly elevated in non-small cell lung carcinoma tissues compared to adjacent non-cancerous tissues. PMID: 24522888
- This study provides evidence that both high expression level and nuclear localization of Sam68 correlate with invasiveness and aggressive characteristics in colorectal cancer, and poorer survival. PMID: 23937454
- Sam68 plays a role in the regulation of differential expression and mRNA processing and translation according to internal and external signals. PMID: 24287914
- FBI-1 affects the recruitment of SAM68 on the BCL-X transcript through an HDAC-dependent mechanism. PMID: 24514149
- These data, along with the fact that Sam68 is known to be a signaling adaptor protein, indicate that Sam68 is a signal molecule with a functional role in the PI3K/Akt signal pathway during enterovirus 71 infection. PMID: 24316008
- Deficient SAM68 expression was observed in the human testis with maturation arrest at the spermatocyte stage and Sertoli cell-only syndrome. PMID: 24794312
- Sam68 is identified as a novel non-Rel component in the nuclear factor-kappaB (NF-kappaB) complex that confers CD25 transcription. PMID: 23715268
- Emerging roles for Sam68 in adipogenesis and neuronal development. PMID: 23018781
- The study proposes that Sam68 functions as a classical scaffold protein in this context, assembling components of an osteoclast-specific signaling pathway. PMID: 22745667
- Sam68 could induce cervical cancer lymph node metastasis by regulating epithelial-mesenchymal transition. PMID: 21700735
- The results show that DDX3, eIF5A, and hRIP enhanced HIV-1 internal ribosomal entry site-mediated translation, whereas Sam68 does not. PMID: 21360055
- The tyrosine-rich domain of Sam68 is bound in a bent conformation to the APC groove. PMID: 22000517
- Sam68 interacts with insulin receptor substrate (IRS)-1 in basal conditions, and insulin increases the affinity between these two partners. PMID: 22005517
- Sam68 is required for both NF-kappaB activation and apoptosis signaling by the TNF receptor. PMID: 21620750
- High Sam68 expression is associated with pancreatic cancer progression. PMID: 21642356
- These results demonstrate for the first time that Hsp22 regulates Sam68 expression, and the ratio of Sam68 to Hsp22 may determine the proliferative potential of glioblastoma cells. PMID: 21678403
- Met receptors induce Sam68-dependent cell migration by activating alternate extracellular signal-regulated kinase family members. PMID: 21489997
- These results strongly suggest the participation of Sam68 in leptin receptor signaling in human trophoblastic cells, indicating that Sam68 may mediate some of the leptin effects in the placenta. PMID: 21035519
- Sam68 modulation of SF2/ASF splicing is controlled by epithelial cell-derived soluble factors that act through the ERK1/2 signaling pathway to regulate Sam68 phosphorylation. PMID: 20876280
- The Qua1 homodimerization domain is required for regulation of alternative splicing by Sam68. PMID: 20610388
- Sam68 is sequestered by expanded CGG repeats and thereby loses its splicing-regulatory function. PMID: 20186122
- In vivo splicing assays showed that Sam68 triggers SMN2 exon-7 skipping. PMID: 20186123
- SAM68 could represent a novel and useful prognostic marker for renal cell carcinoma. High SAM68 expression and cytoplasmic localization are associated with poor overall survival in renal cell carcinoma patients. PMID: 19755649
- Sam68 interacts with HIV-1 Rev protein and directly participates in the nuclear exportation of HIV-1 unspliced or singly spliced RNA. PMID: 19535902
- Our results identify Sam68 as the first splicing factor to affect CCND1 alternative splicing in prostate cancer cells. PMID: 20028857
- Sam68 is recruited into stress granules through complexing with TIA-1 in response to oxidative stress. PMID: 19615357
Database Links
Protein Families
KHDRBS family
Subcellular Location
Nucleus. Cytoplasm. Membrane.
Tissue Specificity
Ubiquitously expressed in all tissue examined. Isoform 1 is expressed at lower levels in brain, skeletal muscle, and liver whereas isoform 3 is intensified in skeletal muscle and in liver.
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