| Name | uroplakin 3B like 1 |
| Description | Predicted to be active in membrane. [provided by Alliance of Genome Resources, Mar 2025] |
| Summary |
{"type": "root", "children": [{"type": "p", "children": [{"type": "t", "text": "\nSin3B (which in some reports may be alternatively designated UPK3BL1) functions as an essential transcriptional corepressor and molecular scaffold that assembles histone deacetylases with diverse DNA‐binding repressors. It interacts with neural transcription factors such as the Myt1 family to regulate neural differentiation ["}, {"type": "fg", "children": [{"type": "fg_f", "ref": "1"}]}, {"type": "t", "text": "], participates in chromatin remodelling via its association with ESET ["}, {"type": "fg", "children": [{"type": "fg_f", "ref": "2"}]}, {"type": "t", "text": "] and helps mediate REST/NRSF‐driven repression—as underscored by studies detailing its PAH1 domain interactions, including approaches targeting this interface for potential neuropathy therapies ["}, {"type": "fg", "children": [{"type": "fg_f", "ref": "3"}]}, {"type": "t", "text": "]. Furthermore, global analyses have highlighted Sin3B’s partnership with related Sin3 complexes in controlling gene expression programs critical for cell cycle exit, differentiation and proper embryonic development ["}, {"type": "fg", "children": [{"type": "fg_f", "ref": "5"}]}, {"type": "t", "text": "].\n"}]}, {"type": "t", "text": "\n\n"}, {"type": "p", "children": [{"type": "t", "text": "\nIn developmental and stress‐response contexts, Sin3B plays pivotal roles in mediating oncogene‐induced senescence and in enforcing cell cycle arrest. In pancreatic ductal adenocarcinoma models, Sin3B is required for KRAS‐induced senescence and concomitant regulation of a pro‐inflammatory secretome ["}, {"type": "fg", "children": [{"type": "fg_f", "ref": "6"}]}, {"type": "t", "text": "]. Its activity is likewise integral to proper myogenesis, as Sin3A/B loss in muscle cells leads to sarcomeric defects ["}, {"type": "fg", "children": [{"type": "fg_f", "ref": "7"}]}, {"type": "t", "text": "], and it is recruited by Foxk1 to modulate cell cycle kinetics in muscle progenitors ["}, {"type": "fg", "children": [{"type": "fg_f", "ref": "8"}]}, {"type": "t", "text": "]. Moreover, Sin3B’s contribution to cell cycle exit through the E2F–Rb pathway ["}, {"type": "fg", "children": [{"type": "fg_f", "ref": "9"}]}, {"type": "t", "text": "] and its regulation by Bmi‐1 in senescence ["}, {"type": "fg", "children": [{"type": "fg_f", "ref": "10"}]}, {"type": "t", "text": "] further point to its role as a tumor suppressor, a view reinforced by findings in prostate adenocarcinoma models ["}, {"type": "fg", "children": [{"type": "fg_f", "ref": "11"}]}, {"type": "t", "text": "].\n"}]}, {"type": "t", "text": "\n\n"}, {"type": "p", "children": [{"type": "t", "text": "\nSin3B also exerts tissue‐specific functions that extend beyond classical transcriptional repression. Its activity is critical for stem cell homeostasis: hematopoietic‐specific inactivation of Sin3B profoundly impairs long‐term repopulation and proper differentiation, and overall blood homeostasis is maintained through these regulatory circuits ["}, {"type": "fg", "children": [{"type": "fg_f", "ref": "12"}]}, {"type": "t", "text": "]. In brown adipocytes, Sin3B is incorporated into a complex with Sp1 and Ifrd1 to limit thermogenic and mitochondrial gene expression ["}, {"type": "fg", "children": [{"type": "fg_f", "ref": "14"}]}, {"type": "t", "text": "], while in neurons, its interaction with a defined domain of voltage‐gated sodium channels suggests a role in channel trafficking and membrane stability ["}, {"type": "fg", "children": [{"type": "fg_f", "ref": "15"}]}, {"type": "t", "text": "]. Sin3B function is further fine‐tuned by alternative splicing events that impact BMP signalling pathways ["}, {"type": "fg", "children": [{"type": "fg_f", "ref": "16"}]}, {"type": "t", "text": "], and its recruitment in cis can restrict viral DNA replication through mechanisms independent of HDAC function ["}, {"type": "fg", "children": [{"type": "fg_f", "ref": "17"}]}, {"type": "t", "text": "]. In addition, the proper functionality of endocrine pancreatic cells, including β‐cell survival and insulin vesicle regulation, has been shown to rely on Sin3 paralogs ["}, {"type": "fg", "children": [{"type": "fg_f", "ref": "18"}]}, {"type": "t", "text": "].\n"}]}, {"type": "rg", "children": [{"type": "r", "ref": 1, "children": [{"type": "t", "text": "Elena Romm, Joseph A Nielsen, Jin G Kim, et al. "}, {"type": "b", "children": [{"type": "t", "text": "Myt1 family recruits histone deacetylase to regulate neural transcription."}]}, {"type": "t", "text": " "}, {"type": "i", "children": [{"type": "t", "text": "J Neurochem (2005)"}]}, {"type": "t", "text": " DOI: "}, {"type": "a", "children": [{"type": "t", "text": "10.1111/j.1471-4159.2005.03131.x"}], "href": "https://doi.org/10.1111/j.1471-4159.2005.03131.x"}, {"type": "t", "text": " PMID: "}, {"type": "a", "children": [{"type": "t", "text": "15935060"}], "href": "https://pubmed.ncbi.nlm.nih.gov/15935060"}]}, {"type": "r", "ref": 2, "children": [{"type": "t", "text": "Liu Yang, Qi Mei, Anna Zielinska-Kwiatkowska, et al. "}, {"type": "b", "children": [{"type": "t", "text": "An ERG (ets-related gene)-associated histone methyltransferase interacts with histone deacetylases 1/2 and transcription co-repressors mSin3A/B."}]}, {"type": "t", "text": " "}, {"type": "i", "children": [{"type": "t", "text": "Biochem J (2003)"}]}, {"type": "t", "text": " DOI: "}, {"type": "a", "children": [{"type": "t", "text": "10.1042/BJ20020854"}], "href": "https://doi.org/10.1042/BJ20020854"}, {"type": "t", "text": " PMID: "}, {"type": "a", "children": [{"type": "t", "text": "12398767"}], "href": "https://pubmed.ncbi.nlm.nih.gov/12398767"}]}, {"type": "r", "ref": 3, "children": [{"type": "t", "text": "Mitsuru Nomura, Hiroko Uda-Tochio, Kiyohito Murai, et al. "}, {"type": "b", "children": [{"type": "t", "text": "The neural repressor NRSF/REST binds the PAH1 domain of the Sin3 corepressor by using its distinct short hydrophobic helix."}]}, {"type": "t", "text": " "}, {"type": "i", "children": [{"type": "t", "text": "J Mol Biol (2005)"}]}, {"type": "t", "text": " DOI: "}, {"type": "a", "children": [{"type": "t", "text": "10.1016/j.jmb.2005.10.008"}], "href": "https://doi.org/10.1016/j.jmb.2005.10.008"}, {"type": "t", "text": " PMID: "}, {"type": "a", "children": [{"type": "t", "text": "16288918"}], "href": "https://pubmed.ncbi.nlm.nih.gov/16288918"}]}, {"type": "r", "ref": 4, "children": [{"type": "t", "text": "Jun-Ichi Kurita, Yuuka Hirao, Hirofumi Nakano, et al. "}, {"type": "b", "children": [{"type": "t", "text": "Sertraline, chlorprothixene, and chlorpromazine characteristically interact with the REST-binding site of the corepressor mSin3, showing medulloblastoma cell growth inhibitory activities."}]}, {"type": "t", "text": " "}, {"type": "i", "children": [{"type": "t", "text": "Sci Rep (2018)"}]}, {"type": "t", "text": " DOI: "}, {"type": "a", "children": [{"type": "t", "text": "10.1038/s41598-018-31852-1"}], "href": "https://doi.org/10.1038/s41598-018-31852-1"}, {"type": "t", "text": " PMID: "}, {"type": "a", "children": [{"type": "t", "text": "30213984"}], "href": "https://pubmed.ncbi.nlm.nih.gov/30213984"}]}, {"type": "r", "ref": 5, "children": [{"type": "t", "text": "Gregory David, Kathryn B Grandinetti, Patricia M Finnerty, et al. 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"}, {"type": "b", "children": [{"type": "t", "text": "Coregulator Sin3a Promotes Postnatal Murine β-Cell Fitness by Regulating Genes in Ca"}, {"type": "a", "children": [{"type": "t", "text": "sup"}], "href": "sup"}, {"type": "t", "text": "2+"}, {"type": "a", "children": [{"type": "t", "text": "/sup"}], "href": "/sup"}, {"type": "t", "text": " Homeostasis, Cell Survival, Vesicle Biosynthesis, Glucose Metabolism, and Stress Response."}]}, {"type": "t", "text": " "}, {"type": "i", "children": [{"type": "t", "text": "Diabetes (2020)"}]}, {"type": "t", "text": " DOI: "}, {"type": "a", "children": [{"type": "t", "text": "10.2337/db19-0721"}], "href": "https://doi.org/10.2337/db19-0721"}, {"type": "t", "text": " PMID: "}, {"type": "a", "children": [{"type": "t", "text": "32245798"}], "href": "https://pubmed.ncbi.nlm.nih.gov/32245798"}]}]}]}
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| NCBI Gene ID | 100134938 |
| API | |
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| Predicted Functions |
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| Co-expressed Genes |
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| Expression in Tissues and Cell Lines |
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UPK3BL1 has 638 functional associations with biological entities spanning 6 categories (functional term, phrase or reference, disease, phenotype or trait, chemical, cell line, cell type or tissue, gene, protein or microRNA, sequence feature) extracted from 20 datasets.
Click the + buttons to view associations for UPK3BL1 from the datasets below.
If available, associations are ranked by standardized value
| Dataset | Summary | |
|---|---|---|
| Allen Brain Atlas Aging Dementia and Traumatic Brain Injury Tissue Sample Gene Expression Profiles | tissue samples with high or low expression of UPK3BL1 gene relative to other tissue samples from the Allen Brain Atlas Aging Dementia and Traumatic Brain Injury Tissue Sample Gene Expression Profiles dataset. | |
| CellMarker Gene-Cell Type Associations | cell types associated with UPK3BL1 gene from the CellMarker Gene-Cell Type Associations dataset. | |
| CM4AI KOLF21J CRISPRi Gene Perturbation Atlas | gene perturbations changing expression of UPK3BL1 gene from the CM4AI KOLF21J CRISPRi Gene Perturbation Atlas dataset. | |
| COMPARTMENTS Text-mining Protein Localization Evidence Scores 2025 | cellular components co-occuring with UPK3BL1 protein in abstracts of biomedical publications from the COMPARTMENTS Text-mining Protein Localization Evidence Scores 2025 dataset. | |
| DISEASES Experimental Gene-Disease Association Evidence Scores 2025 | diseases associated with UPK3BL1 gene in GWAS datasets from the DISEASES Experimental Gene-Disease Assocation Evidence Scores 2025 dataset. | |
| DISEASES Text-mining Gene-Disease Association Evidence Scores 2025 | diseases co-occuring with UPK3BL1 gene in abstracts of biomedical publications from the DISEASES Text-mining Gene-Disease Assocation Evidence Scores 2025 dataset. | |
| GlyGen Glycosylated Proteins | ligands (chemical) binding UPK3BL1 protein from the GlyGen Glycosylated Proteins dataset. | |
| GTEx eQTL 2025 | SNPs regulating expression of UPK3BL1 gene from the GTEx eQTL 2025 dataset. | |
| GTEx Tissue Gene Expression Profiles 2023 | tissues with high or low expression of UPK3BL1 gene relative to other tissues from the GTEx Tissue Gene Expression Profiles 2023 dataset. | |
| JASPAR Predicted Human Transcription Factor Targets 2025 | transcription factors regulating expression of UPK3BL1 gene predicted using known transcription factor binding site motifs from the JASPAR Predicted Human Transcription Factor Targets dataset. | |
| JASPAR Predicted Mouse Transcription Factor Targets 2025 | transcription factors regulating expression of UPK3BL1 gene predicted using known transcription factor binding site motifs from the JASPAR Predicted Mouse Transcription Factor Targets 2025 dataset. | |
| NIBR DRUG-seq U2OS MoA Box Gene Expression Profiles | drug perturbations changing expression of UPK3BL1 gene from the NIBR DRUG-seq U2OS MoA Box dataset. | |
| Replogle et al., Cell, 2022 K562 Essential Perturb-seq Gene Perturbation Signatures | gene perturbations changing expression of UPK3BL1 gene from the Replogle et al., Cell, 2022 K562 Essential Perturb-seq Gene Perturbation Signatures dataset. | |
| Replogle et al., Cell, 2022 K562 Genome-wide Perturb-seq Gene Perturbation Signatures | gene perturbations changing expression of UPK3BL1 gene from the Replogle et al., Cell, 2022 K562 Genome-wide Perturb-seq Gene Perturbation Signatures dataset. | |
| Replogle et al., Cell, 2022 RPE1 Essential Perturb-seq Gene Perturbation Signatures | gene perturbations changing expression of UPK3BL1 gene from the Replogle et al., Cell, 2022 RPE1 Essential Perturb-seq Gene Perturbation Signatures dataset. | |
| Rummagene Transcription Factor Associations 2026 | transcription factors regulating expression of UPK3BL1 gene from the Rummagene Transcription Factor Associations 2026 dataset. | |
| RummaGEO Drug Perturbation Signatures | drug perturbations changing expression of UPK3BL1 gene from the RummaGEO Drug Perturbation Signatures dataset. | |
| RummaGEO Gene Perturbation Signatures | gene perturbations changing expression of UPK3BL1 gene from the RummaGEO Gene Perturbation Signatures dataset. | |
| TISSUES Curated Tissue Protein Expression Evidence Scores 2025 | tissues with high expression of UPK3BL1 protein from the TISSUES Curated Tissue Protein Expression Evidence Scores 2025 dataset. | |
| TISSUES Text-mining Tissue Protein Expression Evidence Scores 2025 | tissues co-occuring with UPK3BL1 protein in abstracts of biomedical publications from the TISSUES Text-mining Tissue Protein Expression Evidence Scores 2025 dataset. | |