| HGNC Family | Cadherins |
| Name | protocadherin alpha 4 |
| Description | This gene is a member of the protocadherin alpha gene cluster, one of three related gene clusters tandemly linked on chromosome five that demonstrate an unusual genomic organization similar to that of B-cell and T-cell receptor gene clusters. The alpha gene cluster is composed of 15 cadherin superfamily genes related to the mouse CNR genes and consists of 13 highly similar and 2 more distantly related coding sequences. The tandem array of 15 N-terminal exons, or variable exons, are followed by downstream C-terminal exons, or constant exons, which are shared by all genes in the cluster. The large, uninterrupted N-terminal exons each encode six cadherin ectodomains while the C-terminal exons encode the cytoplasmic domain. These neural cadherin-like cell adhesion proteins are integral plasma membrane proteins that most likely play a critical role in the establishment and function of specific cell-cell connections in the brain. Alternative splicing has been observed and additional variants have been suggested but their full-length nature has yet to be determined. [provided by RefSeq, Jul 2008] |
| Summary |
{"type": "root", "children": [{"type": "p", "children": [{"type": "t", "text": "\nNote: Although the query requests a summary of PCDHA4, none of the provided abstracts mention PCDHA4. Instead, they uniformly focus on the cytokine‐inducible SH2 domain–containing protein (commonly called CIS, encoded by Cish) – a member of the suppressor of cytokine signaling (SOCS) family. In immune cells, CIS acts as a pivotal negative-feedback regulator that fine‐tunes cytokine‐triggered signaling events. For example, in natural killer (NK) cells the loss of CIS amplifies IL‑15–driven activation, proliferation, and cytotoxicity against tumors, whereas in CD8⁺ T cells CIS limits T cell receptor (TCR)–induced signaling by targeting intermediates (such as PLC‑γ isoforms) for proteasomal degradation. In addition, CIS modulates T helper cell differentiation and dendritic cell maturation, thereby affecting adaptive immune responses and the efficacy of tumor immunotherapy."}, {"type": "fg", "children": [{"type": "fg_fs", "start_ref": "1", "end_ref": "8"}]}, {"type": "t", "text": "\n"}]}, {"type": "t", "text": "\n\n"}, {"type": "p", "children": [{"type": "t", "text": "\nBeyond its immune‐regulatory functions, CIS influences diverse non–immune pathways by modulating cytokine and growth factor signals. In hepatocytes, elevated CIS levels—often induced by cytokines like IL‑6—contribute to a resistance to growth hormone signaling via inhibition of the JAK2/STAT5 axis, while in erythroid progenitors and mammary epithelial cells, CIS overexpression dampens stimulatory signals (for instance, those mediated by erythropoietin and prolactin) by reducing receptor activation and downstream STAT5 phosphorylation. These effects extend to metabolic regulation, where CIS impacts gluconeogenesis and adipocyte function by modulating the transcriptional activity of key factors such as CREB; consequently, alterations in CIS expression have been linked to changes in β‑cell proliferation, appetite control, and insulin sensitivity."}, {"type": "fg", "children": [{"type": "fg_fs", "start_ref": "9", "end_ref": "20"}]}, {"type": "t", "text": "\n"}]}, {"type": "t", "text": "\n\n"}, {"type": "p", "children": [{"type": "t", "text": "\nIn oncogenic and hematopoietic contexts, CIS assumes additional roles that underscore its multifunctional nature. By interfering with overactive JAK‑STAT signaling, CIS can serve as a tumor suppressor—its enforced expression inhibiting aberrant cell proliferation and even triggering apoptotic pathways in transformed cells. Conversely, loss or knockdown of CIS can enhance oncogene‐driven proliferation, as evidenced in models driven by mutant JAK2 signaling. Furthermore, through its modulation of cytokine receptor interactions, CIS helps regulate granulopoiesis and myelopoiesis, ensuring a balanced production of immune cells."}, {"type": "fg", "children": [{"type": "fg_fs", "start_ref": "21", "end_ref": "24"}]}, {"type": "t", "text": "\n"}]}, {"type": "rg", "children": [{"type": "r", "ref": 1, "children": [{"type": "t", "text": "Julie Piessevaux, Leentje De Ceuninck, Dominiek Catteeuw, et al. "}, {"type": "b", "children": [{"type": "t", "text": "Elongin B/C recruitment regulates substrate binding by CIS."}]}, {"type": "t", "text": " "}, {"type": "i", "children": [{"type": "t", "text": "J Biol Chem (2008)"}]}, {"type": "t", "text": " DOI: "}, {"type": "a", "children": [{"type": "t", "text": "10.1074/jbc.M803742200"}], "href": "https://doi.org/10.1074/jbc.M803742200"}, {"type": "t", "text": " PMID: "}, {"type": "a", "children": [{"type": "t", "text": "18508766"}], "href": "https://pubmed.ncbi.nlm.nih.gov/18508766"}]}, {"type": "r", "ref": 2, "children": [{"type": "t", "text": "Mohammad Alam Miah, Cheol-Hee Yoon, Joonoh Kim, et al. "}, {"type": "b", "children": [{"type": "t", "text": "CISH is induced during DC development and regulates DC-mediated CTL activation."}]}, {"type": "t", "text": " "}, {"type": "i", "children": [{"type": "t", "text": "Eur J Immunol (2012)"}]}, {"type": "t", "text": " DOI: "}, {"type": "a", "children": [{"type": "t", "text": "10.1002/eji.201141846"}], "href": "https://doi.org/10.1002/eji.201141846"}, {"type": "t", "text": " PMID: "}, {"type": "a", "children": [{"type": "t", "text": "22002016"}], "href": "https://pubmed.ncbi.nlm.nih.gov/22002016"}]}, {"type": "r", "ref": 3, "children": [{"type": "t", "text": "Xuexian O Yang, Huiyuan Zhang, Byung-Seok Kim, et al. "}, {"type": "b", "children": [{"type": "t", "text": "The signaling suppressor CIS controls proallergic T cell development and allergic airway inflammation."}]}, {"type": "t", "text": " "}, {"type": "i", "children": [{"type": "t", "text": "Nat Immunol (2013)"}]}, {"type": "t", "text": " DOI: "}, {"type": "a", "children": [{"type": "t", "text": "10.1038/ni.2633"}], "href": "https://doi.org/10.1038/ni.2633"}, {"type": "t", "text": " PMID: "}, {"type": "a", "children": [{"type": "t", "text": "23727894"}], "href": "https://pubmed.ncbi.nlm.nih.gov/23727894"}]}, {"type": "r", "ref": 4, "children": [{"type": "t", "text": "Douglas C Palmer, Geoffrey C Guittard, Zulmarie Franco, et al. "}, {"type": "b", "children": [{"type": "t", "text": "Cish actively silences TCR signaling in CD8+ T cells to maintain tumor tolerance."}]}, {"type": "t", "text": " "}, {"type": "i", "children": [{"type": "t", "text": "J Exp Med (2015)"}]}, {"type": "t", "text": " DOI: "}, {"type": "a", "children": [{"type": "t", "text": "10.1084/jem.20150304"}], "href": "https://doi.org/10.1084/jem.20150304"}, {"type": "t", "text": " PMID: "}, {"type": "a", "children": [{"type": "t", "text": "26527801"}], "href": "https://pubmed.ncbi.nlm.nih.gov/26527801"}]}, {"type": "r", "ref": 5, "children": [{"type": "t", "text": "Rebecca B Delconte, Tatiana B Kolesnik, Laura F Dagley, et al. "}, {"type": "b", "children": [{"type": "t", "text": "CIS is a potent checkpoint in NK cell-mediated tumor immunity."}]}, {"type": "t", "text": " "}, {"type": "i", "children": [{"type": "t", "text": "Nat Immunol (2016)"}]}, {"type": "t", "text": " DOI: "}, {"type": "a", "children": [{"type": "t", "text": "10.1038/ni.3470"}], "href": "https://doi.org/10.1038/ni.3470"}, {"type": "t", "text": " PMID: "}, {"type": "a", "children": [{"type": "t", "text": "27213690"}], "href": "https://pubmed.ncbi.nlm.nih.gov/27213690"}]}, {"type": "r", "ref": 6, "children": [{"type": "t", "text": "Rebecca B Delconte, Geoffrey Guittard, Wilford Goh, et al. "}, {"type": "b", "children": [{"type": "t", "text": "NK Cell Priming From Endogenous Homeostatic Signals Is Modulated by CIS."}]}, {"type": "t", "text": " "}, {"type": "i", "children": [{"type": "t", "text": "Front Immunol (2020)"}]}, {"type": "t", "text": " DOI: "}, {"type": "a", "children": [{"type": "t", "text": "10.3389/fimmu.2020.00075"}], "href": "https://doi.org/10.3389/fimmu.2020.00075"}, {"type": "t", "text": " PMID: "}, {"type": "a", "children": [{"type": "t", "text": "32082327"}], "href": "https://pubmed.ncbi.nlm.nih.gov/32082327"}]}, {"type": "r", "ref": 7, "children": [{"type": "t", "text": "Maya E Kotas, Nicholas M Mroz, Satoshi Koga, et al. "}, {"type": "b", "children": [{"type": "t", "text": "CISH constrains the tuft-ILC2 circuit to set epithelial and immune tone."}]}, {"type": "t", "text": " "}, {"type": "i", "children": [{"type": "t", "text": "Mucosal Immunol (2021)"}]}, {"type": "t", "text": " DOI: "}, {"type": "a", "children": [{"type": "t", "text": "10.1038/s41385-021-00430-6"}], "href": "https://doi.org/10.1038/s41385-021-00430-6"}, {"type": "t", "text": " PMID: "}, {"type": "a", "children": [{"type": "t", "text": "34290377"}], "href": "https://pubmed.ncbi.nlm.nih.gov/34290377"}]}, {"type": "r", "ref": 8, "children": [{"type": "t", "text": "Pierre-Louis Bernard, Rebecca Delconte, Sonia Pastor, et al. "}, {"type": "b", "children": [{"type": "t", "text": "Targeting CISH enhances natural cytotoxicity receptor signaling and reduces NK cell exhaustion to improve solid tumor immunity."}]}, {"type": "t", "text": " "}, {"type": "i", "children": [{"type": "t", "text": "J Immunother Cancer (2022)"}]}, {"type": "t", "text": " DOI: "}, {"type": "a", "children": [{"type": "t", "text": "10.1136/jitc-2021-004244"}], "href": "https://doi.org/10.1136/jitc-2021-004244"}, {"type": "t", "text": " PMID: "}, {"type": "a", "children": [{"type": "t", "text": "35589278"}], "href": "https://pubmed.ncbi.nlm.nih.gov/35589278"}]}, {"type": "r", "ref": 9, "children": [{"type": "t", "text": "Sibylle Tonko-Geymayer, Olivier Goupille, Martin Tonko, et al. "}, {"type": "b", "children": [{"type": "t", "text": "Regulation and function of the cytokine-inducible SH-2 domain proteins, CIS and SOCS3, in mammary epithelial cells."}]}, {"type": "t", "text": " "}, {"type": "i", "children": [{"type": "t", "text": "Mol Endocrinol (2002)"}]}, {"type": "t", "text": " DOI: "}, {"type": "a", "children": [{"type": "t", "text": "10.1210/mend.16.7.0872"}], "href": "https://doi.org/10.1210/mend.16.7.0872"}, {"type": "t", "text": " PMID: "}, {"type": "a", "children": [{"type": "t", "text": "12089360"}], "href": "https://pubmed.ncbi.nlm.nih.gov/12089360"}]}, {"type": "r", "ref": 10, "children": [{"type": "t", "text": "Armin G Jegalian, Hong Wu "}, {"type": "b", "children": [{"type": "t", "text": "Differential roles of SOCS family members in EpoR signal transduction."}]}, {"type": "t", "text": " "}, {"type": "i", "children": [{"type": "t", "text": "J Interferon Cytokine Res (2002)"}]}, {"type": "t", "text": " DOI: "}, {"type": "a", "children": [{"type": "t", "text": "10.1089/107999002760274863"}], "href": "https://doi.org/10.1089/107999002760274863"}, {"type": "t", "text": " PMID: "}, {"type": "a", "children": [{"type": "t", "text": "12396724"}], "href": "https://pubmed.ncbi.nlm.nih.gov/12396724"}]}, {"type": "r", "ref": 11, "children": [{"type": "t", "text": "Robin Ketteler, Chetal S Moghraby, Jonathan G Hsiao, et al. "}, {"type": "b", "children": [{"type": "t", "text": "The cytokine-inducible Scr homology domain-containing protein negatively regulates signaling by promoting apoptosis in erythroid progenitor cells."}]}, {"type": "t", "text": " "}, {"type": "i", "children": [{"type": "t", "text": "J Biol Chem (2003)"}]}, {"type": "t", "text": " DOI: "}, {"type": "a", "children": [{"type": "t", "text": "10.1074/jbc.M211236200"}], "href": "https://doi.org/10.1074/jbc.M211236200"}, {"type": "t", "text": " PMID: "}, {"type": "a", "children": [{"type": "t", "text": "12441334"}], "href": "https://pubmed.ncbi.nlm.nih.gov/12441334"}]}, {"type": "r", "ref": 12, "children": [{"type": "t", "text": "Lee A Denson, Matthew A Held, Ram K Menon, et al. "}, {"type": "b", "children": [{"type": "t", "text": "Interleukin-6 inhibits hepatic growth hormone signaling via upregulation of Cis and Socs-3."}]}, {"type": "t", "text": " "}, {"type": "i", "children": [{"type": "t", "text": "Am J Physiol Gastrointest Liver Physiol (2003)"}]}, {"type": "t", "text": " DOI: "}, {"type": "a", "children": [{"type": "t", "text": "10.1152/ajpgi.00178.2002"}], "href": "https://doi.org/10.1152/ajpgi.00178.2002"}, {"type": "t", "text": " PMID: "}, {"type": "a", "children": [{"type": "t", "text": "12519742"}], "href": "https://pubmed.ncbi.nlm.nih.gov/12519742"}]}, {"type": "r", "ref": 13, "children": [{"type": "t", "text": "Anne Rascle, Emma Lees "}, {"type": "b", "children": [{"type": "t", "text": "Chromatin acetylation and remodeling at the Cis promoter during STAT5-induced transcription."}]}, {"type": "t", "text": " "}, {"type": "i", "children": [{"type": "t", "text": "Nucleic Acids Res (2003)"}]}, {"type": "t", "text": " DOI: "}, {"type": "a", "children": [{"type": "t", "text": "10.1093/nar/gkg907"}], "href": "https://doi.org/10.1093/nar/gkg907"}, {"type": "t", "text": " PMID: "}, {"type": "a", "children": [{"type": "t", "text": "14627821"}], "href": "https://pubmed.ncbi.nlm.nih.gov/14627821"}]}, {"type": "r", "ref": 14, "children": [{"type": "t", "text": "Johanna G Miquet, Ana I Sotelo, Andrzej Bartke, et al. "}, {"type": "b", "children": [{"type": "t", "text": "Desensitization of the JAK2/STAT5 GH signaling pathway associated with increased CIS protein content in liver of pregnant mice."}]}, {"type": "t", "text": " "}, {"type": "i", "children": [{"type": "t", "text": "Am J Physiol Endocrinol Metab (2005)"}]}, {"type": "t", "text": " DOI: "}, {"type": "a", "children": [{"type": "t", "text": "10.1152/ajpendo.00085.2005"}], "href": "https://doi.org/10.1152/ajpendo.00085.2005"}, {"type": "t", "text": " PMID: "}, {"type": "a", "children": [{"type": "t", "text": "15899943"}], "href": "https://pubmed.ncbi.nlm.nih.gov/15899943"}]}, {"type": "r", "ref": 15, "children": [{"type": "t", "text": "Yang Jiao, Sebastian Rieck, John Le Lay, et al. "}, {"type": "b", "children": [{"type": "t", "text": "CISH has no non-redundant functions in glucose homeostasis or beta cell proliferation during pregnancy in mice."}]}, {"type": "t", "text": " "}, {"type": "i", "children": [{"type": "t", "text": "Diabetologia (2013)"}]}, {"type": "t", "text": " DOI: "}, {"type": "a", "children": [{"type": "t", "text": "10.1007/s00125-013-3014-x"}], "href": "https://doi.org/10.1007/s00125-013-3014-x"}, {"type": "t", "text": " PMID: "}, {"type": "a", "children": [{"type": "t", "text": "23949579"}], "href": "https://pubmed.ncbi.nlm.nih.gov/23949579"}]}, {"type": "r", "ref": 16, "children": [{"type": "t", "text": "Paula Mota de Sá, Allison J Richard, Jacqueline M Stephens "}, {"type": "b", "children": [{"type": "t", "text": "Bromodomain and Extraterminal Inhibition by JQ1 Produces Divergent Transcriptional Regulation of Suppressors of Cytokine Signaling Genes in Adipocytes."}]}, {"type": "t", "text": " "}, {"type": "i", "children": [{"type": "t", "text": "Endocrinology (2020)"}]}, {"type": "t", "text": " DOI: "}, {"type": "a", "children": [{"type": "t", "text": "10.1210/endocr/bqz034"}], "href": "https://doi.org/10.1210/endocr/bqz034"}, {"type": "t", "text": " PMID: "}, {"type": "a", "children": [{"type": "t", "text": "31875887"}], "href": "https://pubmed.ncbi.nlm.nih.gov/31875887"}]}, {"type": "r", "ref": 17, "children": [{"type": "t", "text": "Wasan Naser, Saeed Maymand, Leni R Rivera, et al. 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"}, {"type": "b", "children": [{"type": "t", "text": "Hepatic cytokine-inducible SH2-containing protein (CISH) regulates gluconeogenesis via cAMP-responsive element binding protein (CREB)."}]}, {"type": "t", "text": " "}, {"type": "i", "children": [{"type": "t", "text": "FASEB J (2022)"}]}, {"type": "t", "text": " DOI: "}, {"type": "a", "children": [{"type": "t", "text": "10.1096/fj.202200870R"}], "href": "https://doi.org/10.1096/fj.202200870R"}, {"type": "t", "text": " PMID: "}, {"type": "a", "children": [{"type": "t", "text": "36083102"}], "href": "https://pubmed.ncbi.nlm.nih.gov/36083102"}]}, {"type": "r", "ref": 19, "children": [{"type": "t", "text": "Wasan Naser, Saeed Maymand, Daniel Dlugolenski, et al. "}, {"type": "b", "children": [{"type": "t", "text": "The Role of Cytokine-Inducible SH2 Domain-Containing Protein (CISH) in the Regulation of Basal and Cytokine-Mediated Myelopoiesis."}]}, {"type": "t", "text": " "}, {"type": "i", "children": [{"type": "t", "text": "Int J Mol Sci (2023)"}]}, {"type": "t", "text": " DOI: "}, {"type": "a", "children": [{"type": "t", "text": "10.3390/ijms241612757"}], "href": "https://doi.org/10.3390/ijms241612757"}, {"type": "t", "text": " PMID: "}, {"type": "a", "children": [{"type": "t", "text": "37628937"}], "href": "https://pubmed.ncbi.nlm.nih.gov/37628937"}]}, {"type": "r", "ref": 20, "children": [{"type": "t", "text": "Saeed Maymand, Asha L Lakkavaram, Wasan Naser, et al. "}, {"type": "b", "children": [{"type": "t", "text": "Role of Cytokine-Inducible SH2 Domain-Containing (CISH) Protein in the Regulation of Erythropoiesis."}]}, {"type": "t", "text": " "}, {"type": "i", "children": [{"type": "t", "text": "Biomolecules (2023)"}]}, {"type": "t", "text": " DOI: "}, {"type": "a", "children": [{"type": "t", "text": "10.3390/biom13101510"}], "href": "https://doi.org/10.3390/biom13101510"}, {"type": "t", "text": " PMID: "}, {"type": "a", "children": [{"type": "t", "text": "37892192"}], "href": "https://pubmed.ncbi.nlm.nih.gov/37892192"}]}, {"type": "r", "ref": 21, "children": [{"type": "t", "text": "Delphine Lavens, Peter Ulrichts, Dominiek Catteeuw, et al. "}, {"type": "b", "children": [{"type": "t", "text": "The C-terminus of CIS defines its interaction pattern."}]}, {"type": "t", "text": " "}, {"type": "i", "children": [{"type": "t", "text": "Biochem J (2007)"}]}, {"type": "t", "text": " DOI: "}, {"type": "a", "children": [{"type": "t", "text": "10.1042/BJ20060242"}], "href": "https://doi.org/10.1042/BJ20060242"}, {"type": "t", "text": " PMID: "}, {"type": "a", "children": [{"type": "t", "text": "16961462"}], "href": "https://pubmed.ncbi.nlm.nih.gov/16961462"}]}, {"type": "r", "ref": 22, "children": [{"type": "t", "text": "Weizhou Zhang, George Zhi Cheng, Jianli Gong, et al. "}, {"type": "b", "children": [{"type": "t", "text": "RACK1 and CIS mediate the degradation of BimEL in cancer cells."}]}, {"type": "t", "text": " "}, {"type": "i", "children": [{"type": "t", "text": "J Biol Chem (2008)"}]}, {"type": "t", "text": " DOI: "}, {"type": "a", "children": [{"type": "t", "text": "10.1074/jbc.M802360200"}], "href": "https://doi.org/10.1074/jbc.M802360200"}, {"type": "t", "text": " PMID: "}, {"type": "a", "children": [{"type": "t", "text": "18420585"}], "href": "https://pubmed.ncbi.nlm.nih.gov/18420585"}]}, {"type": "r", "ref": 23, "children": [{"type": "t", "text": "Megumi Funakoshi-Tago, Takuro Moriwaki, Fumihito Ueda, et al. "}, {"type": "b", "children": [{"type": "t", "text": "Phosphorylated CIS suppresses the Epo or JAK2 V617F mutant-triggered cell proliferation through binding to EpoR."}]}, {"type": "t", "text": " "}, {"type": "i", "children": [{"type": "t", "text": "Cell Signal (2017)"}]}, {"type": "t", "text": " DOI: "}, {"type": "a", "children": [{"type": "t", "text": "10.1016/j.cellsig.2016.12.008"}], "href": "https://doi.org/10.1016/j.cellsig.2016.12.008"}, {"type": "t", "text": " PMID: "}, {"type": "a", "children": [{"type": "t", "text": "28038963"}], "href": "https://pubmed.ncbi.nlm.nih.gov/28038963"}]}, {"type": "r", "ref": 24, "children": [{"type": "t", "text": "Geoffrey Guittard, Ana Dios-Esponera, Douglas C Palmer, et al. "}, {"type": "b", "children": [{"type": "t", "text": "The Cish SH2 domain is essential for PLC-γ1 regulation in TCR stimulated CD8"}, {"type": "a", "children": [{"type": "t", "text": "sup"}], "href": "sup"}, {"type": "t", "text": "+"}, {"type": "a", "children": [{"type": "t", "text": "/sup"}], "href": "/sup"}, {"type": "t", "text": " T cells."}]}, {"type": "t", "text": " "}, {"type": "i", "children": [{"type": "t", "text": "Sci Rep (2018)"}]}, {"type": "t", "text": " DOI: "}, {"type": "a", "children": [{"type": "t", "text": "10.1038/s41598-018-23549-2"}], "href": "https://doi.org/10.1038/s41598-018-23549-2"}, {"type": "t", "text": " PMID: "}, {"type": "a", "children": [{"type": "t", "text": "29593227"}], "href": "https://pubmed.ncbi.nlm.nih.gov/29593227"}]}]}]}
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| Synonyms | CRNR1, CNRN1, PCDH-ALPHA4 |
| Proteins | PCDA4_HUMAN |
| NCBI Gene ID | 56144 |
| API | |
| Download Associations | |
| Predicted Functions |
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| Co-expressed Genes |
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| Expression in Tissues and Cell Lines |
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PCDHA4 has 4,311 functional associations with biological entities spanning 9 categories (molecular profile, organism, chemical, functional term, phrase or reference, disease, phenotype or trait, structural feature, cell line, cell type or tissue, gene, protein or microRNA, sequence feature) extracted from 80 datasets.
Click the + buttons to view associations for PCDHA4 from the datasets below.
If available, associations are ranked by standardized value
| Dataset | Summary | |
|---|---|---|
| Achilles Cell Line Gene Essentiality Profiles | cell lines with fitness changed by PCDHA4 gene knockdown relative to other cell lines from the Achilles Cell Line Gene Essentiality Profiles dataset. | |
| Allen Brain Atlas Adult Mouse Brain Tissue Gene Expression Profiles | tissues with high or low expression of PCDHA4 gene relative to other tissues from the Allen Brain Atlas Adult Mouse Brain Tissue Gene Expression Profiles dataset. | |
| Allen Brain Atlas Aging Dementia and Traumatic Brain Injury Tissue Sample Gene Expression Profiles | tissue samples with high or low expression of PCDHA4 gene relative to other tissue samples from the Allen Brain Atlas Aging Dementia and Traumatic Brain Injury Tissue Sample Gene Expression Profiles dataset. | |
| Allen Brain Atlas Developing Human Brain Tissue Gene Expression Profiles by RNA-seq | tissue samples with high or low expression of PCDHA4 gene relative to other tissue samples from the Allen Brain Atlas Developing Human Brain Tissue Gene Expression Profiles by RNA-seq dataset. | |
| BioGPS Mouse Cell Type and Tissue Gene Expression Profiles | cell types and tissues with high or low expression of PCDHA4 gene relative to other cell types and tissues from the BioGPS Mouse Cell Type and Tissue Gene Expression Profiles dataset. | |
| Carcinogenome Chemical Perturbation Carcinogenicity Signatures | small molecule perturbations changing expression of PCDHA4 gene from the Carcinogenome Chemical Perturbation Carcinogenicity Signatures dataset. | |
| CCLE Cell Line Gene CNV Profiles | cell lines with high or low copy number of PCDHA4 gene relative to other cell lines from the CCLE Cell Line Gene CNV Profiles dataset. | |
| ChEA Transcription Factor Binding Site Profiles | transcription factor binding site profiles with transcription factor binding evidence at the promoter of PCDHA4 gene from the CHEA Transcription Factor Binding Site Profiles dataset. | |
| ChEA Transcription Factor Targets | transcription factors binding the promoter of PCDHA4 gene in low- or high-throughput transcription factor functional studies from the CHEA Transcription Factor Targets dataset. | |
| ChEA Transcription Factor Targets 2022 | transcription factors binding the promoter of PCDHA4 gene in low- or high-throughput transcription factor functional studies from the CHEA Transcription Factor Targets 2022 dataset. | |
| COMPARTMENTS Curated Protein Localization Evidence Scores | cellular components containing PCDHA4 protein from the COMPARTMENTS Curated Protein Localization Evidence Scores dataset. | |
| COMPARTMENTS Curated Protein Localization Evidence Scores 2025 | cellular components containing PCDHA4 protein from the COMPARTMENTS Curated Protein Localization Evidence Scores 2025 dataset. | |
| COMPARTMENTS Text-mining Protein Localization Evidence Scores | cellular components co-occuring with PCDHA4 protein in abstracts of biomedical publications from the COMPARTMENTS Text-mining Protein Localization Evidence Scores dataset. | |
| COMPARTMENTS Text-mining Protein Localization Evidence Scores 2025 | cellular components co-occuring with PCDHA4 protein in abstracts of biomedical publications from the COMPARTMENTS Text-mining Protein Localization Evidence Scores 2025 dataset. | |
| CORUM Protein Complexes | protein complexs containing PCDHA4 protein from the CORUM Protein Complexes dataset. | |
| COSMIC Cell Line Gene CNV Profiles | cell lines with high or low copy number of PCDHA4 gene relative to other cell lines from the COSMIC Cell Line Gene CNV Profiles dataset. | |
| COSMIC Cell Line Gene Mutation Profiles | cell lines with PCDHA4 gene mutations from the COSMIC Cell Line Gene Mutation Profiles dataset. | |
| dbGAP Gene-Trait Associations | traits associated with PCDHA4 gene in GWAS and other genetic association datasets from the dbGAP Gene-Trait Associations dataset. | |
| DepMap CRISPR Gene Dependency | cell lines with fitness changed by PCDHA4 gene knockdown relative to other cell lines from the DepMap CRISPR Gene Dependency dataset. | |
| DISEASES Experimental Gene-Disease Association Evidence Scores 2025 | diseases associated with PCDHA4 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 PCDHA4 gene in abstracts of biomedical publications from the DISEASES Text-mining Gene-Disease Assocation Evidence Scores 2025 dataset. | |
| DisGeNET Gene-Disease Associations | diseases associated with PCDHA4 gene in GWAS and other genetic association datasets from the DisGeNET Gene-Disease Associations dataset. | |
| DisGeNET Gene-Phenotype Associations | phenotypes associated with PCDHA4 gene in GWAS and other genetic association datasets from the DisGeNET Gene-Phenoptype Associations dataset. | |
| ENCODE Histone Modification Site Profiles | histone modification site profiles with high histone modification abundance at PCDHA4 gene from the ENCODE Histone Modification Site Profiles dataset. | |
| ENCODE Transcription Factor Binding Site Profiles | transcription factor binding site profiles with transcription factor binding evidence at the promoter of PCDHA4 gene from the ENCODE Transcription Factor Binding Site Profiles dataset. | |
| ENCODE Transcription Factor Targets | transcription factors binding the promoter of PCDHA4 gene in ChIP-seq datasets from the ENCODE Transcription Factor Targets dataset. | |
| ESCAPE Omics Signatures of Genes and Proteins for Stem Cells | PubMedIDs of publications reporting gene signatures containing PCDHA4 from the ESCAPE Omics Signatures of Genes and Proteins for Stem Cells dataset. | |
| GAD Gene-Disease Associations | diseases associated with PCDHA4 gene in GWAS and other genetic association datasets from the GAD Gene-Disease Associations dataset. | |
| GeneSigDB Published Gene Signatures | PubMedIDs of publications reporting gene signatures containing PCDHA4 from the GeneSigDB Published Gene Signatures dataset. | |
| GEO Signatures of Differentially Expressed Genes for Gene Perturbations | gene perturbations changing expression of PCDHA4 gene from the GEO Signatures of Differentially Expressed Genes for Gene Perturbations dataset. | |
| GEO Signatures of Differentially Expressed Genes for Kinase Perturbations | kinase perturbations changing expression of PCDHA4 gene from the GEO Signatures of Differentially Expressed Genes for Kinase Perturbations dataset. | |
| GEO Signatures of Differentially Expressed Genes for Viral Infections | virus perturbations changing expression of PCDHA4 gene from the GEO Signatures of Differentially Expressed Genes for Viral Infections dataset. | |
| GO Biological Process Annotations 2015 | biological processes involving PCDHA4 gene from the curated GO Biological Process Annotations 2015 dataset. | |
| GO Biological Process Annotations 2025 | biological processes involving PCDHA4 gene from the curated GO Biological Process Annotations2025 dataset. | |
| GO Cellular Component Annotations 2015 | cellular components containing PCDHA4 protein from the curated GO Cellular Component Annotations 2015 dataset. | |
| GO Cellular Component Annotations 2025 | cellular components containing PCDHA4 protein from the curated GO Cellular Component Annotations 2025 dataset. | |
| GO Molecular Function Annotations 2015 | molecular functions performed by PCDHA4 gene from the curated GO Molecular Function Annotations 2015 dataset. | |
| GO Molecular Function Annotations 2023 | molecular functions performed by PCDHA4 gene from the curated GO Molecular Function Annotations 2023 dataset. | |
| GO Molecular Function Annotations 2025 | molecular functions performed by PCDHA4 gene from the curated GO Molecular Function Annotations 2025 dataset. | |
| GTEx eQTL 2025 | SNPs regulating expression of PCDHA4 gene from the GTEx eQTL 2025 dataset. | |
| GTEx Tissue Gene Expression Profiles | tissues with high or low expression of PCDHA4 gene relative to other tissues from the GTEx Tissue Gene Expression Profiles dataset. | |
| GTEx Tissue Gene Expression Profiles 2023 | tissues with high or low expression of PCDHA4 gene relative to other tissues from the GTEx Tissue Gene Expression Profiles 2023 dataset. | |
| GTEx Tissue Sample Gene Expression Profiles | tissue samples with high or low expression of PCDHA4 gene relative to other tissue samples from the GTEx Tissue Sample Gene Expression Profiles dataset. | |
| GTEx Tissue-Specific Aging Signatures | tissue samples with high or low expression of PCDHA4 gene relative to other tissue samples from the GTEx Tissue-Specific Aging Signatures dataset. | |
| GWAS Catalog SNP-Phenotype Associations 2025 | phenotypes associated with PCDHA4 gene in GWAS datasets from the GWAS Catalog SNP-Phenotype Associations 2025 dataset. | |
| GWASdb SNP-Disease Associations | diseases associated with PCDHA4 gene in GWAS and other genetic association datasets from the GWASdb SNP-Disease Associations dataset. | |
| GWASdb SNP-Phenotype Associations | phenotypes associated with PCDHA4 gene in GWAS datasets from the GWASdb SNP-Phenotype Associations dataset. | |
| HMDB Metabolites of Enzymes | interacting metabolites for PCDHA4 protein from the curated HMDB Metabolites of Enzymes dataset. | |
| HPA Tissue Gene Expression Profiles | tissues with high or low expression of PCDHA4 gene relative to other tissues from the HPA Tissue Gene Expression Profiles dataset. | |
| HPA Tissue Protein Expression Profiles | tissues with high or low expression of PCDHA4 protein relative to other tissues from the HPA Tissue Protein Expression Profiles dataset. | |
| HPA Tissue Sample Gene Expression Profiles | tissue samples with high or low expression of PCDHA4 gene relative to other tissue samples from the HPA Tissue Sample Gene Expression Profiles dataset. | |
| Hub Proteins Protein-Protein Interactions | interacting hub proteins for PCDHA4 from the curated Hub Proteins Protein-Protein Interactions dataset. | |
| InterPro Predicted Protein Domain Annotations | protein domains predicted for PCDHA4 protein from the InterPro Predicted Protein Domain Annotations dataset. | |
| JASPAR Predicted Human Transcription Factor Targets 2025 | transcription factors regulating expression of PCDHA4 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 PCDHA4 gene predicted using known transcription factor binding site motifs from the JASPAR Predicted Mouse Transcription Factor Targets 2025 dataset. | |
| JASPAR Predicted Transcription Factor Targets | transcription factors regulating expression of PCDHA4 gene predicted using known transcription factor binding site motifs from the JASPAR Predicted Transcription Factor Targets dataset. | |
| KEGG Pathways 2026 | pathways involving PCDHA4 protein from the KEGG Pathways 2026 dataset. | |
| Klijn et al., Nat. Biotechnol., 2015 Cell Line Gene CNV Profiles | cell lines with high or low copy number of PCDHA4 gene relative to other cell lines from the Klijn et al., Nat. Biotechnol., 2015 Cell Line Gene CNV Profiles dataset. | |
| Klijn et al., Nat. Biotechnol., 2015 Cell Line Gene Mutation Profiles | cell lines with PCDHA4 gene mutations from the Klijn et al., Nat. Biotechnol., 2015 Cell Line Gene Mutation Profiles dataset. | |
| KnockTF Gene Expression Profiles with Transcription Factor Perturbations | transcription factor perturbations changing expression of PCDHA4 gene from the KnockTF Gene Expression Profiles with Transcription Factor Perturbations dataset. | |
| LOCATE Curated Protein Localization Annotations | cellular components containing PCDHA4 protein in low- or high-throughput protein localization assays from the LOCATE Curated Protein Localization Annotations dataset. | |
| LOCATE Predicted Protein Localization Annotations | cellular components predicted to contain PCDHA4 protein from the LOCATE Predicted Protein Localization Annotations dataset. | |
| MiRTarBase microRNA Targets | microRNAs targeting PCDHA4 gene in low- or high-throughput microRNA targeting studies from the MiRTarBase microRNA Targets dataset. | |
| MotifMap Predicted Transcription Factor Targets | transcription factors regulating expression of PCDHA4 gene predicted using known transcription factor binding site motifs from the MotifMap Predicted Transcription Factor Targets dataset. | |
| PANTHER Pathways | pathways involving PCDHA4 protein from the PANTHER Pathways dataset. | |
| Pathway Commons Protein-Protein Interactions | interacting proteins for PCDHA4 from the Pathway Commons Protein-Protein Interactions dataset. | |
| PerturbAtlas Signatures of Differentially Expressed Genes for Gene Perturbations | gene perturbations changing expression of PCDHA4 gene from the PerturbAtlas Signatures of Differentially Expressed Genes for Gene Perturbations dataset. | |
| PFOCR Pathway Figure Associations 2024 | pathways involving PCDHA4 protein from the Wikipathways PFOCR 2024 dataset. | |
| Roadmap Epigenomics Cell and Tissue DNA Methylation Profiles | cell types and tissues with high or low DNA methylation of PCDHA4 gene relative to other cell types and tissues from the Roadmap Epigenomics Cell and Tissue DNA Methylation Profiles dataset. | |
| Roadmap Epigenomics Histone Modification Site Profiles | histone modification site profiles with high histone modification abundance at PCDHA4 gene from the Roadmap Epigenomics Histone Modification Site Profiles dataset. | |
| RummaGEO Drug Perturbation Signatures | drug perturbations changing expression of PCDHA4 gene from the RummaGEO Drug Perturbation Signatures dataset. | |
| RummaGEO Gene Perturbation Signatures | gene perturbations changing expression of PCDHA4 gene from the RummaGEO Gene Perturbation Signatures dataset. | |
| TargetScan Predicted Conserved microRNA Targets | microRNAs regulating expression of PCDHA4 gene predicted using conserved miRNA seed sequences from the TargetScan Predicted Conserved microRNA Targets dataset. | |
| TargetScan Predicted Nonconserved microRNA Targets | microRNAs regulating expression of PCDHA4 gene predicted using nonconserved miRNA seed sequences from the TargetScan Predicted Nonconserved microRNA Targets dataset. | |
| TCGA Signatures of Differentially Expressed Genes for Tumors | tissue samples with high or low expression of PCDHA4 gene relative to other tissue samples from the TCGA Signatures of Differentially Expressed Genes for Tumors dataset. | |
| TISSUES Curated Tissue Protein Expression Evidence Scores | tissues with high expression of PCDHA4 protein from the TISSUES Curated Tissue Protein Expression Evidence Scores dataset. | |
| TISSUES Curated Tissue Protein Expression Evidence Scores 2025 | tissues with high expression of PCDHA4 protein from the TISSUES Curated Tissue Protein Expression Evidence Scores 2025 dataset. | |
| TISSUES Experimental Tissue Protein Expression Evidence Scores 2025 | tissues with high expression of PCDHA4 protein in proteomics datasets from the TISSUES Experimental Tissue Protein Expression Evidence Scores 2025 dataset. | |
| TISSUES Text-mining Tissue Protein Expression Evidence Scores | tissues co-occuring with PCDHA4 protein in abstracts of biomedical publications from the TISSUES Text-mining Tissue Protein Expression Evidence Scores dataset. | |
| TISSUES Text-mining Tissue Protein Expression Evidence Scores 2025 | tissues co-occuring with PCDHA4 protein in abstracts of biomedical publications from the TISSUES Text-mining Tissue Protein Expression Evidence Scores 2025 dataset. | |
