RBBP4 Gene

HGNC Family	WD repeat domain containing (WDR)
Name	retinoblastoma binding protein 4
Description	This gene encodes a ubiquitously expressed nuclear protein which belongs to a highly conserved subfamily of WD-repeat proteins. It is present in protein complexes involved in histone acetylation and chromatin assembly. It is part of the Mi-2 complex which has been implicated in chromatin remodeling and transcriptional repression associated with histone deacetylation. This encoded protein is also part of co-repressor complexes, which is an integral component of transcriptional silencing. It is found among several cellular proteins that bind directly to retinoblastoma protein to regulate cell proliferation. This protein also seems to be involved in transcriptional repression of E2F-responsive genes. Three transcript variants encoding different isoforms have been found for this gene. [provided by RefSeq, Sep 2008]
Summary	{"type": "root", "children": [{"type": "p", "children": [{"type": "t", "text": "\nA careful review of the 43 provided abstracts reveals that none of these studies mention or address RBBP4. Instead, the literature exclusively focuses on the roles of the mitochondrial kinases and ubiquitin ligases—most notably PINK1 and Parkin—and their regulation of mitochondrial quality control, mitophagy, and downstream stress‐response pathways. These works describe how loss‐of‐function or modified activity of Parkin and its interactors leads to impaired substrate ubiquitination, defective clearance of damaged mitochondria, and consequent effects on neuronal, cardiac, and even immune as well as oncogenic processes. In short, while these studies richly document the centrality of the PINK1–Parkin axis in cellular homeostasis and survival (for example, in the context of Parkinson’s disease, myocardial infarction, and stress‐induced apoptosis), they provide no evidence to suggest any involvement of RBBP4 in these mechanisms."}, {"type": "fg", "children": [{"type": "fg_fs", "start_ref": "1", "end_ref": "43"}]}, {"type": "t", "text": "\n"}]}, {"type": "t", "text": "\n\n"}, {"type": "p", "children": [{"type": "t", "text": "\nIn light of this survey, it is evident that the functions of RBBP4 remain unaddressed within these datasets. Without any direct report on RBBP4, our understanding of its potential roles in chromatin organization, epigenetic regulation, or other cellular processes is not informed by these studies. Therefore, while the PINK1–Parkin mediated pathways represent a well‐characterized mode of regulating mitochondrial integrity and cellular stress responses, further research is necessary to elucidate whether RBBP4 might intersect with these or other pathways in health and disease."}, {"type": "fg", "children": [{"type": "fg_fs", "start_ref": "1", "end_ref": "43"}]}, {"type": "t", "text": "\n"}]}, {"type": "rg", "children": [{"type": "r", "ref": 1, "children": [{"type": "t", "text": "Leonard Petrucelli, Casey O'Farrell, Paul J Lockhart, et al. "}, {"type": "b", "children": [{"type": "t", "text": "Parkin protects against the toxicity associated with mutant alpha-synuclein: proteasome dysfunction selectively affects catecholaminergic neurons."}]}, {"type": "t", "text": " "}, {"type": "i", "children": [{"type": "t", "text": "Neuron (2002)"}]}, {"type": "t", "text": " DOI: "}, {"type": "a", "children": [{"type": "t", "text": "10.1016/s0896-6273(02)01125-x"}], "href": "https://doi.org/10.1016/s0896-6273(02"}, {"type": "t", "text": "01125-x) PMID: "}, {"type": "a", "children": [{"type": "t", "text": "12495618"}], "href": "https://pubmed.ncbi.nlm.nih.gov/12495618"}]}, {"type": "r", "ref": 2, "children": [{"type": "t", "text": "Yien Che Tsai, Paul S Fishman, Nitish V Thakor, et al. "}, {"type": "b", "children": [{"type": "t", "text": "Parkin facilitates the elimination of expanded polyglutamine proteins and leads to preservation of proteasome function."}]}, {"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.M212235200"}], "href": "https://doi.org/10.1074/jbc.M212235200"}, {"type": "t", "text": " PMID: "}, {"type": "a", "children": [{"type": "t", "text": "12676955"}], "href": "https://pubmed.ncbi.nlm.nih.gov/12676955"}]}, {"type": "r", "ref": 3, "children": [{"type": "t", "text": "Jean-Michel Itier, Pablo Ibanez, Maria Angeles Mena, et al. "}, {"type": "b", "children": [{"type": "t", "text": "Parkin gene inactivation alters behaviour and dopamine neurotransmission in the mouse."}]}, {"type": "t", "text": " "}, {"type": "i", "children": [{"type": "t", "text": "Hum Mol Genet (2003)"}]}, {"type": "t", "text": " DOI: "}, {"type": "a", "children": [{"type": "t", "text": "10.1093/hmg/ddg239"}], "href": "https://doi.org/10.1093/hmg/ddg239"}, {"type": "t", "text": " PMID: "}, {"type": "a", "children": [{"type": "t", "text": "12915482"}], "href": "https://pubmed.ncbi.nlm.nih.gov/12915482"}]}, {"type": "r", "ref": 4, "children": [{"type": "t", "text": "Matthew S Goldberg, Sheila M Fleming, James J Palacino, et al. "}, {"type": "b", "children": [{"type": "t", "text": "Parkin-deficient mice exhibit nigrostriatal deficits but not loss of dopaminergic neurons."}]}, {"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.M308947200"}], "href": "https://doi.org/10.1074/jbc.M308947200"}, {"type": "t", "text": " PMID: "}, {"type": "a", "children": [{"type": "t", "text": "12930822"}], "href": "https://pubmed.ncbi.nlm.nih.gov/12930822"}]}, {"type": "r", "ref": 5, "children": [{"type": "t", "text": "James J Palacino, Dijana Sagi, Matthew S Goldberg, et al. "}, {"type": "b", "children": [{"type": "t", "text": "Mitochondrial dysfunction and oxidative damage in parkin-deficient mice."}]}, {"type": "t", "text": " "}, {"type": "i", "children": [{"type": "t", "text": "J Biol Chem (2004)"}]}, {"type": "t", "text": " DOI: "}, {"type": "a", "children": [{"type": "t", "text": "10.1074/jbc.M401135200"}], "href": "https://doi.org/10.1074/jbc.M401135200"}, {"type": "t", "text": " PMID: "}, {"type": "a", "children": [{"type": "t", "text": "14985362"}], "href": "https://pubmed.ncbi.nlm.nih.gov/14985362"}]}, {"type": "r", "ref": 6, "children": [{"type": "t", "text": "Kenny K K Chung, Bobby Thomas, Xiaojie Li, et al. "}, {"type": "b", "children": [{"type": "t", "text": "S-nitrosylation of parkin regulates ubiquitination and compromises parkin's protective function."}]}, {"type": "t", "text": " "}, {"type": "i", "children": [{"type": "t", "text": "Science (2004)"}]}, {"type": "t", "text": " DOI: "}, {"type": "a", "children": [{"type": "t", "text": "10.1126/science.1093891"}], "href": "https://doi.org/10.1126/science.1093891"}, {"type": "t", "text": " PMID: "}, {"type": "a", "children": [{"type": "t", "text": "15105460"}], "href": "https://pubmed.ncbi.nlm.nih.gov/15105460"}]}, {"type": "r", "ref": 7, "children": [{"type": "t", "text": "Rainer Von Coelln, Bobby Thomas, Joseph M Savitt, et al. "}, {"type": "b", "children": [{"type": "t", "text": "Loss of locus coeruleus neurons and reduced startle in parkin null mice."}]}, {"type": "t", "text": " "}, {"type": "i", "children": [{"type": "t", "text": "Proc Natl Acad Sci U S A (2004)"}]}, {"type": "t", "text": " DOI: "}, {"type": "a", "children": [{"type": "t", "text": "10.1073/pnas.0401297101"}], "href": "https://doi.org/10.1073/pnas.0401297101"}, {"type": "t", "text": " PMID: "}, {"type": "a", "children": [{"type": "t", "text": "15249681"}], "href": "https://pubmed.ncbi.nlm.nih.gov/15249681"}]}, {"type": "r", "ref": 8, "children": [{"type": "t", "text": "Dongdong Yao, Zezong Gu, Tomohiro Nakamura, et al. "}, {"type": "b", "children": [{"type": "t", "text": "Nitrosative stress linked to sporadic Parkinson's disease: S-nitrosylation of parkin regulates its E3 ubiquitin ligase activity."}]}, {"type": "t", "text": " "}, {"type": "i", "children": [{"type": "t", "text": "Proc Natl Acad Sci U S A (2004)"}]}, {"type": "t", "text": " DOI: "}, {"type": "a", "children": [{"type": "t", "text": "10.1073/pnas.0404161101"}], "href": "https://doi.org/10.1073/pnas.0404161101"}, {"type": "t", "text": " PMID: "}, {"type": "a", "children": [{"type": "t", "text": "15252205"}], "href": "https://pubmed.ncbi.nlm.nih.gov/15252205"}]}, {"type": "r", "ref": 9, "children": [{"type": "t", "text": "Francisco A Perez, Richard D Palmiter "}, {"type": "b", "children": [{"type": "t", "text": "Parkin-deficient mice are not a robust model of parkinsonism."}]}, {"type": "t", "text": " "}, {"type": "i", "children": [{"type": "t", "text": "Proc Natl Acad Sci U S A (2005)"}]}, {"type": "t", "text": " DOI: "}, {"type": "a", "children": [{"type": "t", "text": "10.1073/pnas.0409598102"}], "href": "https://doi.org/10.1073/pnas.0409598102"}, {"type": "t", "text": " PMID: "}, {"type": "a", "children": [{"type": "t", "text": "15684050"}], "href": "https://pubmed.ncbi.nlm.nih.gov/15684050"}]}, {"type": "r", "ref": 10, "children": [{"type": "t", "text": "Tamy C Frank-Cannon, Thi Tran, Kelly A Ruhn, et al. "}, {"type": "b", "children": [{"type": "t", "text": "Parkin deficiency increases vulnerability to inflammation-related nigral degeneration."}]}, {"type": "t", "text": " "}, {"type": "i", "children": [{"type": "t", "text": "J Neurosci (2008)"}]}, {"type": "t", "text": " DOI: "}, {"type": "a", "children": [{"type": "t", "text": "10.1523/JNEUROSCI.3001-08.2008"}], "href": "https://doi.org/10.1523/JNEUROSCI.3001-08.2008"}, {"type": "t", "text": " PMID: "}, {"type": "a", "children": [{"type": "t", "text": "18945890"}], "href": "https://pubmed.ncbi.nlm.nih.gov/18945890"}]}, {"type": "r", "ref": 11, "children": [{"type": "t", "text": "A Kathrin Lutz, Nicole Exner, Mareike E Fett, et al. "}, {"type": "b", "children": [{"type": "t", "text": "Loss of parkin or PINK1 function increases Drp1-dependent mitochondrial fragmentation."}]}, {"type": "t", "text": " "}, {"type": "i", "children": [{"type": "t", "text": "J Biol Chem (2009)"}]}, {"type": "t", "text": " DOI: "}, {"type": "a", "children": [{"type": "t", "text": "10.1074/jbc.M109.035774"}], "href": "https://doi.org/10.1074/jbc.M109.035774"}, {"type": "t", "text": " PMID: "}, {"type": "a", "children": [{"type": "t", "text": "19546216"}], "href": "https://pubmed.ncbi.nlm.nih.gov/19546216"}]}, {"type": "r", "ref": 12, "children": [{"type": "t", "text": "Oliver Rothfuss, Heike Fischer, Takafumi Hasegawa, et al. "}, {"type": "b", "children": [{"type": "t", "text": "Parkin protects mitochondrial genome integrity and supports mitochondrial DNA repair."}]}, {"type": "t", "text": " "}, {"type": "i", "children": [{"type": "t", "text": "Hum Mol Genet (2009)"}]}, {"type": "t", "text": " DOI: "}, {"type": "a", "children": [{"type": "t", "text": "10.1093/hmg/ddp327"}], "href": "https://doi.org/10.1093/hmg/ddp327"}, {"type": "t", "text": " PMID: "}, {"type": "a", "children": [{"type": "t", "text": "19617636"}], "href": "https://pubmed.ncbi.nlm.nih.gov/19617636"}]}, {"type": "r", "ref": 13, "children": [{"type": "t", "text": "Noriyuki Matsuda, Shigeto Sato, Kahori Shiba, et al. "}, {"type": "b", "children": [{"type": "t", "text": "PINK1 stabilized by mitochondrial depolarization recruits Parkin to damaged mitochondria and activates latent Parkin for mitophagy."}]}, {"type": "t", "text": " "}, {"type": "i", "children": [{"type": "t", "text": "J Cell Biol (2010)"}]}, {"type": "t", "text": " DOI: "}, {"type": "a", "children": [{"type": "t", "text": "10.1083/jcb.200910140"}], "href": "https://doi.org/10.1083/jcb.200910140"}, {"type": "t", "text": " PMID: "}, {"type": "a", "children": [{"type": "t", "text": "20404107"}], "href": "https://pubmed.ncbi.nlm.nih.gov/20404107"}]}, {"type": "r", "ref": 14, "children": [{"type": "t", "text": "Wen-Xing Ding, Hong-Min Ni, Min Li, et al. "}, {"type": "b", "children": [{"type": "t", "text": "Nix is critical to two distinct phases of mitophagy, reactive oxygen species-mediated autophagy induction and Parkin-ubiquitin-p62-mediated mitochondrial priming."}]}, {"type": "t", "text": " "}, {"type": "i", "children": [{"type": "t", "text": "J Biol Chem (2010)"}]}, {"type": "t", "text": " DOI: "}, {"type": "a", "children": [{"type": "t", "text": "10.1074/jbc.M110.119537"}], "href": "https://doi.org/10.1074/jbc.M110.119537"}, {"type": "t", "text": " PMID: "}, {"type": "a", "children": [{"type": "t", "text": "20573959"}], "href": "https://pubmed.ncbi.nlm.nih.gov/20573959"}]}, {"type": "r", "ref": 15, "children": [{"type": "t", "text": "George Poulogiannis, Rebecca E McIntyre, Maria Dimitriadi, et al. "}, {"type": "b", "children": [{"type": "t", "text": "PARK2 deletions occur frequently in sporadic colorectal cancer and accelerate adenoma development in Apc mutant mice."}]}, {"type": "t", "text": " "}, {"type": "i", "children": [{"type": "t", "text": "Proc Natl Acad Sci U S A (2010)"}]}, {"type": "t", "text": " DOI: "}, {"type": "a", "children": [{"type": "t", "text": "10.1073/pnas.1009941107"}], "href": "https://doi.org/10.1073/pnas.1009941107"}, {"type": "t", "text": " PMID: "}, {"type": "a", "children": [{"type": "t", "text": "20696900"}], "href": "https://pubmed.ncbi.nlm.nih.gov/20696900"}]}, {"type": "r", "ref": 16, "children": [{"type": "t", "text": "Preeti J Khandelwal, Alexander M Herman, Hyang-Sook Hoe, et al. "}, {"type": "b", "children": [{"type": "t", "text": "Parkin mediates beclin-dependent autophagic clearance of defective mitochondria and ubiquitinated Abeta in AD models."}]}, {"type": "t", "text": " "}, {"type": "i", "children": [{"type": "t", "text": "Hum Mol Genet (2011)"}]}, {"type": "t", "text": " DOI: "}, {"type": "a", "children": [{"type": "t", "text": "10.1093/hmg/ddr091"}], "href": "https://doi.org/10.1093/hmg/ddr091"}, {"type": "t", "text": " PMID: "}, {"type": "a", "children": [{"type": "t", "text": "21378096"}], "href": "https://pubmed.ncbi.nlm.nih.gov/21378096"}]}, {"type": "r", "ref": 17, "children": [{"type": "t", "text": "Saori R Yoshii, Chieko Kishi, Naotada Ishihara, et al. "}, {"type": "b", "children": [{"type": "t", "text": "Parkin mediates proteasome-dependent protein degradation and rupture of the outer mitochondrial membrane."}]}, {"type": "t", "text": " "}, {"type": "i", "children": [{"type": "t", "text": "J Biol Chem (2011)"}]}, {"type": "t", "text": " DOI: "}, {"type": "a", "children": [{"type": "t", "text": "10.1074/jbc.M110.209338"}], "href": "https://doi.org/10.1074/jbc.M110.209338"}, {"type": "t", "text": " PMID: "}, {"type": "a", "children": [{"type": "t", "text": "21454557"}], "href": "https://pubmed.ncbi.nlm.nih.gov/21454557"}]}, {"type": "r", "ref": 18, "children": [{"type": "t", "text": "Chengqun Huang, Allen M Andres, Eric P Ratliff, et al. "}, {"type": "b", "children": [{"type": "t", "text": "Preconditioning involves selective mitophagy mediated by Parkin and p62/SQSTM1."}]}, {"type": "t", "text": " "}, {"type": "i", "children": [{"type": "t", "text": "PLoS One (2011)"}]}, {"type": "t", "text": " DOI: "}, {"type": "a", "children": [{"type": "t", "text": "10.1371/journal.pone.0020975"}], "href": "https://doi.org/10.1371/journal.pone.0020975"}, {"type": "t", "text": " PMID: "}, {"type": "a", "children": [{"type": "t", "text": "21687634"}], "href": "https://pubmed.ncbi.nlm.nih.gov/21687634"}]}, {"type": "r", "ref": 19, "children": [{"type": "t", "text": "Fredrik H Sterky, Seungmin Lee, Rolf Wibom, et al. "}, {"type": "b", "children": [{"type": "t", "text": "Impaired mitochondrial transport and Parkin-independent degeneration of respiratory chain-deficient dopamine neurons in vivo."}]}, {"type": "t", "text": " "}, {"type": "i", "children": [{"type": "t", "text": "Proc Natl Acad Sci U S A (2011)"}]}, {"type": "t", "text": " DOI: "}, {"type": "a", "children": [{"type": "t", "text": "10.1073/pnas.1103295108"}], "href": "https://doi.org/10.1073/pnas.1103295108"}, {"type": "t", "text": " PMID: "}, {"type": "a", "children": [{"type": "t", "text": "21768369"}], "href": "https://pubmed.ncbi.nlm.nih.gov/21768369"}]}, {"type": "r", "ref": 20, "children": [{"type": "t", "text": "Youngil Lee, Hwa-Youn Lee, Rita A Hanna, et al. "}, {"type": "b", "children": [{"type": "t", "text": "Mitochondrial autophagy by Bnip3 involves Drp1-mediated mitochondrial fission and recruitment of Parkin in cardiac myocytes."}]}, {"type": "t", "text": " "}, {"type": "i", "children": [{"type": "t", "text": "Am J Physiol Heart Circ Physiol (2011)"}]}, {"type": "t", "text": " DOI: "}, {"type": "a", "children": [{"type": "t", "text": "10.1152/ajpheart.00368.2011"}], "href": "https://doi.org/10.1152/ajpheart.00368.2011"}, {"type": "t", "text": " PMID: "}, {"type": "a", "children": [{"type": "t", "text": "21890690"}], "href": "https://pubmed.ncbi.nlm.nih.gov/21890690"}]}, {"type": "r", "ref": 21, "children": [{"type": "t", "text": "Eisuke Itakura, Chieko Kishi-Itakura, Ikuko Koyama-Honda, et al. "}, {"type": "b", "children": [{"type": "t", "text": "Structures containing Atg9A and the ULK1 complex independently target depolarized mitochondria at initial stages of Parkin-mediated mitophagy."}]}, {"type": "t", "text": " "}, {"type": "i", "children": [{"type": "t", "text": "J Cell Sci (2012)"}]}, {"type": "t", "text": " DOI: "}, {"type": "a", "children": [{"type": "t", "text": "10.1242/jcs.094110"}], "href": "https://doi.org/10.1242/jcs.094110"}, {"type": "t", "text": " PMID: "}, {"type": "a", "children": [{"type": "t", "text": "22275429"}], "href": "https://pubmed.ncbi.nlm.nih.gov/22275429"}]}, {"type": "r", "ref": 22, "children": [{"type": "t", "text": "Qian Cai, Hesham Mostafa Zakaria, Anthony Simone, et al. "}, {"type": "b", "children": [{"type": "t", "text": "Spatial parkin translocation and degradation of damaged mitochondria via mitophagy in live cortical neurons."}]}, {"type": "t", "text": " "}, {"type": "i", "children": [{"type": "t", "text": "Curr Biol (2012)"}]}, {"type": "t", "text": " DOI: "}, {"type": "a", "children": [{"type": "t", "text": "10.1016/j.cub.2012.02.005"}], "href": "https://doi.org/10.1016/j.cub.2012.02.005"}, {"type": "t", "text": " PMID: "}, {"type": "a", "children": [{"type": "t", "text": "22342752"}], "href": "https://pubmed.ncbi.nlm.nih.gov/22342752"}]}, {"type": "r", "ref": 23, "children": [{"type": "t", "text": "Bethann N Johnson, Alison K Berger, Giuseppe P Cortese, et al. "}, {"type": "b", "children": [{"type": "t", "text": "The ubiquitin E3 ligase parkin regulates the proapoptotic function of Bax."}]}, {"type": "t", "text": " "}, {"type": "i", "children": [{"type": "t", "text": "Proc Natl Acad Sci U S A (2012)"}]}, {"type": "t", "text": " DOI: "}, {"type": "a", "children": [{"type": "t", "text": "10.1073/pnas.1113248109"}], "href": "https://doi.org/10.1073/pnas.1113248109"}, {"type": "t", "text": " PMID: "}, {"type": "a", "children": [{"type": "t", "text": "22460798"}], "href": "https://pubmed.ncbi.nlm.nih.gov/22460798"}]}, {"type": "r", "ref": 24, "children": [{"type": "t", "text": "Dieter A Kubli, Xiaoxue Zhang, Youngil Lee, et al. "}, {"type": "b", "children": [{"type": "t", "text": "Parkin protein deficiency exacerbates cardiac injury and reduces survival following myocardial infarction."}]}, {"type": "t", "text": " "}, {"type": "i", "children": [{"type": "t", "text": "J Biol Chem (2013)"}]}, {"type": "t", "text": " DOI: "}, {"type": "a", "children": [{"type": "t", "text": "10.1074/jbc.M112.411363"}], "href": "https://doi.org/10.1074/jbc.M112.411363"}, {"type": "t", "text": " PMID: "}, {"type": "a", "children": [{"type": "t", "text": "23152496"}], "href": "https://pubmed.ncbi.nlm.nih.gov/23152496"}]}, {"type": "r", "ref": 25, "children": [{"type": "t", "text": "Kahori Shiba-Fukushima, Yuzuru Imai, Shigeharu Yoshida, et al. "}, {"type": "b", "children": [{"type": "t", "text": "PINK1-mediated phosphorylation of the Parkin ubiquitin-like domain primes mitochondrial translocation of Parkin and regulates mitophagy."}]}, {"type": "t", "text": " "}, {"type": "i", "children": [{"type": "t", "text": "Sci Rep (2012)"}]}, {"type": "t", "text": " DOI: "}, {"type": "a", "children": [{"type": "t", "text": "10.1038/srep01002"}], "href": "https://doi.org/10.1038/srep01002"}, {"type": "t", "text": " PMID: "}, {"type": "a", "children": [{"type": "t", "text": "23256036"}], "href": "https://pubmed.ncbi.nlm.nih.gov/23256036"}]}, {"type": "r", "ref": 26, "children": [{"type": "t", "text": "Anne Kathrin Müller-Rischart, Anna Pilsl, Patrick Beaudette, et al. "}, {"type": "b", "children": [{"type": "t", "text": "The E3 ligase parkin maintains mitochondrial integrity by increasing linear ubiquitination of NEMO."}]}, {"type": "t", "text": " "}, {"type": "i", "children": [{"type": "t", "text": "Mol Cell (2013)"}]}, {"type": "t", "text": " DOI: "}, {"type": "a", "children": [{"type": "t", "text": "10.1016/j.molcel.2013.01.036"}], "href": "https://doi.org/10.1016/j.molcel.2013.01.036"}, {"type": "t", "text": " PMID: "}, {"type": "a", "children": [{"type": "t", "text": "23453807"}], "href": "https://pubmed.ncbi.nlm.nih.gov/23453807"}]}, {"type": "r", "ref": 27, "children": [{"type": "t", "text": "Yun Chen, Gerald W Dorn "}, {"type": "b", "children": [{"type": "t", "text": "PINK1-phosphorylated mitofusin 2 is a Parkin receptor for culling damaged mitochondria."}]}, {"type": "t", "text": " "}, {"type": "i", "children": [{"type": "t", "text": "Science (2013)"}]}, {"type": "t", "text": " DOI: "}, {"type": "a", "children": [{"type": "t", "text": "10.1126/science.1231031"}], "href": "https://doi.org/10.1126/science.1231031"}, {"type": "t", "text": " PMID: "}, {"type": "a", "children": [{"type": "t", "text": "23620051"}], "href": "https://pubmed.ncbi.nlm.nih.gov/23620051"}]}, {"type": "r", "ref": 28, "children": [{"type": "t", "text": "Masahiro Iguchi, Yuki Kujuro, Kei Okatsu, et al. 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Synonyms	NURF55, RBAP48, LIN-53
Proteins	RBBP4_HUMAN
NCBI Gene ID	5928
API
Download Associations
Predicted Functions
Co-expressed Genes
Expression in Tissues and Cell Lines

Functional Associations

RBBP4 has 12,199 functional associations with biological entities spanning 9 categories (molecular profile, organism, functional term, phrase or reference, chemical, disease, phenotype or trait, structural feature, cell line, cell type or tissue, gene, protein or microRNA, sequence feature) extracted from 127 datasets.

Click the + buttons to view associations for RBBP4 from the datasets below.

If available, associations are ranked by standardized value

Harmonizome 3.0

RBBP4 Gene

Functional Associations

Please acknowledge the Harmonizome in your publications by citing the following reference(s):

	Dataset	Summary
	Achilles Cell Line Gene Essentiality Profiles	cell lines with fitness changed by RBBP4 gene knockdown relative to other cell lines from the Achilles Cell Line Gene Essentiality Profiles dataset.
	Allen Brain Atlas Adult Human Brain Tissue Gene Expression Profiles	tissues with high or low expression of RBBP4 gene relative to other tissues from the Allen Brain Atlas Adult Human Brain Tissue Gene Expression Profiles dataset.
	Allen Brain Atlas Adult Mouse Brain Tissue Gene Expression Profiles	tissues with high or low expression of RBBP4 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 RBBP4 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 Microarray	tissue samples with high or low expression of RBBP4 gene relative to other tissue samples from the Allen Brain Atlas Developing Human Brain Tissue Gene Expression Profiles by Microarray dataset.
	Allen Brain Atlas Developing Human Brain Tissue Gene Expression Profiles by RNA-seq	tissue samples with high or low expression of RBBP4 gene relative to other tissue samples from the Allen Brain Atlas Developing Human Brain Tissue Gene Expression Profiles by RNA-seq dataset.
	Allen Brain Atlas Prenatal Human Brain Tissue Gene Expression Profiles	tissues with high or low expression of RBBP4 gene relative to other tissues from the Allen Brain Atlas Prenatal Human Brain Tissue Gene Expression Profiles dataset.
	Biocarta Pathways	pathways involving RBBP4 protein from the Biocarta Pathways dataset.
	BioGPS Cell Line Gene Expression Profiles	cell lines with high or low expression of RBBP4 gene relative to other cell lines from the BioGPS Cell Line Gene Expression Profiles dataset.
	BioGPS Human Cell Type and Tissue Gene Expression Profiles	cell types and tissues with high or low expression of RBBP4 gene relative to other cell types and tissues from the BioGPS Human Cell Type and Tissue Gene Expression Profiles dataset.
	BioGPS Mouse Cell Type and Tissue Gene Expression Profiles	cell types and tissues with high or low expression of RBBP4 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 RBBP4 gene from the Carcinogenome Chemical Perturbation Carcinogenicity Signatures dataset.
	CCLE Cell Line Gene CNV Profiles	cell lines with high or low copy number of RBBP4 gene relative to other cell lines from the CCLE Cell Line Gene CNV Profiles dataset.
	CCLE Cell Line Gene Expression Profiles	cell lines with high or low expression of RBBP4 gene relative to other cell lines from the CCLE Cell Line Gene Expression Profiles dataset.
	CCLE Cell Line Proteomics	Cell lines associated with RBBP4 protein from the CCLE Cell Line Proteomics dataset.
	ChEA Transcription Factor Binding Site Profiles	transcription factor binding site profiles with transcription factor binding evidence at the promoter of RBBP4 gene from the CHEA Transcription Factor Binding Site Profiles dataset.
	ChEA Transcription Factor Targets	transcription factors binding the promoter of RBBP4 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 RBBP4 gene in low- or high-throughput transcription factor functional studies from the CHEA Transcription Factor Targets 2022 dataset.
	CM4AI U2OS Cell Map Protein Localization Assemblies	assemblies containing RBBP4 protein from integrated AP-MS and IF data from the CM4AI U2OS Cell Map Protein Localization Assemblies dataset.
	CMAP Signatures of Differentially Expressed Genes for Small Molecules	small molecule perturbations changing expression of RBBP4 gene from the CMAP Signatures of Differentially Expressed Genes for Small Molecules dataset.
	COMPARTMENTS Curated Protein Localization Evidence Scores	cellular components containing RBBP4 protein from the COMPARTMENTS Curated Protein Localization Evidence Scores dataset.
	COMPARTMENTS Curated Protein Localization Evidence Scores 2025	cellular components containing RBBP4 protein from the COMPARTMENTS Curated Protein Localization Evidence Scores 2025 dataset.
	COMPARTMENTS Experimental Protein Localization Evidence Scores	cellular components containing RBBP4 protein in low- or high-throughput protein localization assays from the COMPARTMENTS Experimental Protein Localization Evidence Scores dataset.
	COMPARTMENTS Text-mining Protein Localization Evidence Scores	cellular components co-occuring with RBBP4 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 RBBP4 protein in abstracts of biomedical publications from the COMPARTMENTS Text-mining Protein Localization Evidence Scores 2025 dataset.
	CORUM Protein Complexes	protein complexs containing RBBP4 protein from the CORUM Protein Complexes dataset.
	COSMIC Cell Line Gene CNV Profiles	cell lines with high or low copy number of RBBP4 gene relative to other cell lines from the COSMIC Cell Line Gene CNV Profiles dataset.
	COSMIC Cell Line Gene Mutation Profiles	cell lines with RBBP4 gene mutations from the COSMIC Cell Line Gene Mutation Profiles dataset.
	CTD Gene-Chemical Interactions	chemicals interacting with RBBP4 gene/protein from the curated CTD Gene-Chemical Interactions dataset.
	CTD Gene-Disease Associations	diseases associated with RBBP4 gene/protein from the curated CTD Gene-Disease Associations dataset.
	dbGAP Gene-Trait Associations	traits associated with RBBP4 gene in GWAS and other genetic association datasets from the dbGAP Gene-Trait Associations dataset.
	DeepCoverMOA Drug Mechanisms of Action	small molecule perturbations with high or low expression of RBBP4 protein relative to other small molecule perturbations from the DeepCoverMOA Drug Mechanisms of Action dataset.
	DISEASES Text-mining Gene-Disease Association Evidence Scores	diseases co-occuring with RBBP4 gene in abstracts of biomedical publications from the DISEASES Text-mining Gene-Disease Assocation Evidence Scores dataset.
	DISEASES Text-mining Gene-Disease Association Evidence Scores 2025	diseases co-occuring with RBBP4 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 RBBP4 gene in GWAS and other genetic association datasets from the DisGeNET Gene-Disease Associations dataset.
	DisGeNET Gene-Phenotype Associations	phenotypes associated with RBBP4 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 RBBP4 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 RBBP4 gene from the ENCODE Transcription Factor Binding Site Profiles dataset.
	ENCODE Transcription Factor Targets	transcription factors binding the promoter of RBBP4 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 RBBP4 from the ESCAPE Omics Signatures of Genes and Proteins for Stem Cells dataset.