RANBP9 Gene

Name	RAN binding protein 9
Description	This gene encodes a protein that binds RAN, a small GTP binding protein belonging to the RAS superfamily that is essential for the translocation of RNA and proteins through the nuclear pore complex. The protein encoded by this gene has also been shown to interact with several other proteins, including met proto-oncogene, homeodomain interacting protein kinase 2, androgen receptor, and cyclin-dependent kinase 11. [provided by RefSeq, Jul 2008]
Summary	{"type": "root", "children": [{"type": "p", "children": [{"type": "t", "text": "\nRanBP9 (also known as RanBPM) is a versatile scaffold protein that orchestrates signal transduction by engaging multiple receptors and intracellular effectors. It directly interacts with receptor tyrosine kinases such as MET to activate downstream Ras–ERK cascades, associates with nuclear regulators like HIPK2, and modulates steroid receptor activity via binding to the androgen receptor. In addition, RanBP9 binds to cell‐surface adhesion molecules—including β1/β2 integrins—and participates in signaling through the Axl receptor, while also regulating the activity of ion channels such as the T‐type Ca²⁺ channel Cav3.1. Furthermore, its association with key apoptotic and transcriptional regulators such as CDK11(p46) and p73 (as demonstrated in two independent studies) as well as its involvement in D₁ receptor and TRAF6– and BLT2‐mediated pathways underscore its central role in integrating survival, differentiation, and inflammatory signals."}, {"type": "fg", "children": [{"type": "fg_fs", "start_ref": "1", "end_ref": "12"}]}, {"type": "t", "text": "\n"}]}, {"type": "t", "text": "\n\n"}, {"type": "p", "children": [{"type": "t", "text": "\nRanBP9 also plays a major role in regulating protein stability, complex assembly, and proteolytic processing. Its own turnover is modulated by deubiquitination via USP11, and it is an integral component of multi‐protein complexes such as the CTLH complex, with additional association with muskelin contributing to cytoskeletal organization. Binding to the ecto‐nucleotidase CD39 influences extracellular nucleotide signaling, while RanBP9’s interaction with components that govern amyloid precursor protein processing enhances amyloid‑β generation—a process implicated in Alzheimer’s disease. In parallel, its involvement in DNA damage–induced apoptotic responses further highlights its importance in maintaining cell homeostasis."}, {"type": "fg", "children": [{"type": "fg_fs", "start_ref": "13", "end_ref": "19"}]}, {"type": "t", "text": "\n"}]}, {"type": "t", "text": "\n\n"}, {"type": "p", "children": [{"type": "t", "text": "\nIn developmental and pathological contexts, RanBP9 influences both neurogenesis and tumor biology. By interacting with citron kinase, it helps regulate neurogenic mitoses and cell polarity in the developing neocortex, while its binding to the polarity protein Mgl‑1 is critical for maintaining epithelial integrity and cell migration. In cancer cells, altered RanBP9 expression is linked to gastric cancer progression, and formation of the RanBP9/TSSC3 complex promotes anoikis, thereby suppressing metastatic dissemination. Its association with histone deacetylase 6 further modulates transcriptional and cytoskeletal responses, and elevated RanBP9 levels have been correlated with resistance to DNA‐damaging therapies in non–small cell lung cancer, suggesting its potential as a prognostic biomarker."}, {"type": "fg", "children": [{"type": "fg_fs", "start_ref": "20", "end_ref": "25"}]}, {"type": "t", "text": "\n"}]}, {"type": "rg", "children": [{"type": "r", "ref": 1, "children": [{"type": "t", "text": "Dakun Wang, Zaibo Li, Edward M Messing, et al. "}, {"type": "b", "children": [{"type": "t", "text": "Activation of Ras/Erk pathway by a novel MET-interacting protein RanBPM."}]}, {"type": "t", "text": " "}, {"type": "i", "children": [{"type": "t", "text": "J Biol Chem (2002)"}]}, {"type": "t", "text": " DOI: "}, {"type": "a", "children": [{"type": "t", "text": "10.1074/jbc.M205111200"}], "href": "https://doi.org/10.1074/jbc.M205111200"}, {"type": "t", "text": " PMID: "}, {"type": "a", "children": [{"type": "t", "text": "12147692"}], "href": "https://pubmed.ncbi.nlm.nih.gov/12147692"}]}, {"type": "r", "ref": 2, "children": [{"type": "t", "text": "Ying Wang, E Marion Schneider, Xin Li, et al. "}, {"type": "b", "children": [{"type": "t", "text": "HIPK2 associates with RanBPM."}]}, {"type": "t", "text": " "}, {"type": "i", "children": [{"type": "t", "text": "Biochem Biophys Res Commun (2002)"}]}, {"type": "t", "text": " DOI: "}, {"type": "a", "children": [{"type": "t", "text": "10.1016/s0006-291x(02)02020-x"}], "href": "https://doi.org/10.1016/s0006-291x(02"}, {"type": "t", "text": "02020-x) PMID: "}, {"type": "a", "children": [{"type": "t", "text": "12220523"}], "href": "https://pubmed.ncbi.nlm.nih.gov/12220523"}]}, {"type": "r", "ref": 3, "children": [{"type": "t", "text": "Mira A Rao, Helen Cheng, Alandra N Quayle, et al. "}, {"type": "b", "children": [{"type": "t", "text": "RanBPM, a nuclear protein that interacts with and regulates transcriptional activity of androgen receptor and glucocorticoid receptor."}]}, {"type": "t", "text": " "}, {"type": "i", "children": [{"type": "t", "text": "J Biol Chem (2002)"}]}, {"type": "t", "text": " DOI: "}, {"type": "a", "children": [{"type": "t", "text": "10.1074/jbc.M209741200"}], "href": "https://doi.org/10.1074/jbc.M209741200"}, {"type": "t", "text": " PMID: "}, {"type": "a", "children": [{"type": "t", "text": "12361945"}], "href": "https://pubmed.ncbi.nlm.nih.gov/12361945"}]}, {"type": "r", "ref": 4, "children": [{"type": "t", "text": "Monika Mikolajczyk, Jiaqi Shi, Richard R Vaillancourt, et al. "}, {"type": "b", "children": [{"type": "t", "text": "The cyclin-dependent kinase 11(p46) isoform interacts with RanBPM."}]}, {"type": "t", "text": " "}, {"type": "i", "children": [{"type": "t", "text": "Biochem Biophys Res Commun (2003)"}]}, {"type": "t", "text": " DOI: "}, {"type": "a", "children": [{"type": "t", "text": "10.1016/j.bbrc.2003.08.116"}], "href": "https://doi.org/10.1016/j.bbrc.2003.08.116"}, {"type": "t", "text": " PMID: "}, {"type": "a", "children": [{"type": "t", "text": "14511641"}], "href": "https://pubmed.ncbi.nlm.nih.gov/14511641"}]}, {"type": "r", "ref": 5, "children": [{"type": "t", "text": "Simona Denti, Alessandra Sirri, Alessandra Cheli, et al. "}, {"type": "b", "children": [{"type": "t", "text": "RanBPM is a phosphoprotein that associates with the plasma membrane and interacts with the integrin LFA-1."}]}, {"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.M313515200"}], "href": "https://doi.org/10.1074/jbc.M313515200"}, {"type": "t", "text": " PMID: "}, {"type": "a", "children": [{"type": "t", "text": "14722085"}], "href": "https://pubmed.ncbi.nlm.nih.gov/14722085"}]}, {"type": "r", "ref": 6, "children": [{"type": "t", "text": "Sonja Kramer, Toshinori Ozaki, Kou Miyazaki, et al. "}, {"type": "b", "children": [{"type": "t", "text": "Protein stability and function of p73 are modulated by a physical interaction with RanBPM in mammalian cultured cells."}]}, {"type": "t", "text": " "}, {"type": "i", "children": [{"type": "t", "text": "Oncogene (2005)"}]}, {"type": "t", "text": " DOI: "}, {"type": "a", "children": [{"type": "t", "text": "10.1038/sj.onc.1208257"}], "href": "https://doi.org/10.1038/sj.onc.1208257"}, {"type": "t", "text": " PMID: "}, {"type": "a", "children": [{"type": "t", "text": "15558019"}], "href": "https://pubmed.ncbi.nlm.nih.gov/15558019"}]}, {"type": "r", "ref": 7, "children": [{"type": "t", "text": "Sassan Hafizi, Anna Gustafsson, Jonas Stenhoff, et al. "}, {"type": "b", "children": [{"type": "t", "text": "The Ran binding protein RanBPM interacts with Axl and Sky receptor tyrosine kinases."}]}, {"type": "t", "text": " "}, {"type": "i", "children": [{"type": "t", "text": "Int J Biochem Cell Biol (2005)"}]}, {"type": "t", "text": " DOI: "}, {"type": "a", "children": [{"type": "t", "text": "10.1016/j.biocel.2005.05.006"}], "href": "https://doi.org/10.1016/j.biocel.2005.05.006"}, {"type": "t", "text": " PMID: "}, {"type": "a", "children": [{"type": "t", "text": "15964779"}], "href": "https://pubmed.ncbi.nlm.nih.gov/15964779"}]}, {"type": "r", "ref": 8, "children": [{"type": "t", "text": "L Charles Murrin, Jeffery N Talbot "}, {"type": "b", "children": [{"type": "t", "text": "RanBPM, a scaffolding protein in the immune and nervous systems."}]}, {"type": "t", "text": " "}, {"type": "i", "children": [{"type": "t", "text": "J Neuroimmune Pharmacol (2007)"}]}, {"type": "t", "text": " DOI: "}, {"type": "a", "children": [{"type": "t", "text": "10.1007/s11481-007-9079-x"}], "href": "https://doi.org/10.1007/s11481-007-9079-x"}, {"type": "t", "text": " PMID: "}, {"type": "a", "children": [{"type": "t", "text": "18040864"}], "href": "https://pubmed.ncbi.nlm.nih.gov/18040864"}]}, {"type": "r", "ref": 9, "children": [{"type": "t", "text": "Taehyun Kim, Sunoh Kim, Hyung-Mun Yun, et al. "}, {"type": "b", "children": [{"type": "t", "text": "Modulation of Ca(v)3.1 T-type Ca2+ channels by the ran binding protein RanBPM."}]}, {"type": "t", "text": " "}, {"type": "i", "children": [{"type": "t", "text": "Biochem Biophys Res Commun (2009)"}]}, {"type": "t", "text": " DOI: "}, {"type": "a", "children": [{"type": "t", "text": "10.1016/j.bbrc.2008.09.034"}], "href": "https://doi.org/10.1016/j.bbrc.2008.09.034"}, {"type": "t", "text": " PMID: "}, {"type": "a", "children": [{"type": "t", "text": "18801335"}], "href": "https://pubmed.ncbi.nlm.nih.gov/18801335"}]}, {"type": "r", "ref": 10, "children": [{"type": "t", "text": "Elizabeth B Rex, Michele L Rankin, Yu Yang, et al. "}, {"type": "b", "children": [{"type": "t", "text": "Identification of RanBP 9/10 as interacting partners for protein kinase C (PKC) gamma/delta and the D1 dopamine receptor: regulation of PKC-mediated receptor phosphorylation."}]}, {"type": "t", "text": " "}, {"type": "i", "children": [{"type": "t", "text": "Mol Pharmacol (2010)"}]}, {"type": "t", "text": " DOI: "}, {"type": "a", "children": [{"type": "t", "text": "10.1124/mol.110.063727"}], "href": "https://doi.org/10.1124/mol.110.063727"}, {"type": "t", "text": " PMID: "}, {"type": "a", "children": [{"type": "t", "text": "20395553"}], "href": "https://pubmed.ncbi.nlm.nih.gov/20395553"}]}, {"type": "r", "ref": 11, "children": [{"type": "t", "text": "Lan Wang, Chengbo Fu, Yingbin Cui, et al. "}, {"type": "b", "children": [{"type": "t", "text": "The Ran-binding protein RanBPM can depress the NF-κB pathway by interacting with TRAF6."}]}, {"type": "t", "text": " "}, {"type": "i", "children": [{"type": "t", "text": "Mol Cell Biochem (2012)"}]}, {"type": "t", "text": " DOI: "}, {"type": "a", "children": [{"type": "t", "text": "10.1007/s11010-011-1002-3"}], "href": "https://doi.org/10.1007/s11010-011-1002-3"}, {"type": "t", "text": " PMID: "}, {"type": "a", "children": [{"type": "t", "text": "21805090"}], "href": "https://pubmed.ncbi.nlm.nih.gov/21805090"}]}, {"type": "r", "ref": 12, "children": [{"type": "t", "text": "Sung Hoon Cho, Ariel Raybuck, Mei Wei, et al. "}, {"type": "b", "children": [{"type": "t", "text": "B cell-intrinsic and -extrinsic regulation of antibody responses by PARP14, an intracellular (ADP-ribosyl)transferase."}]}, {"type": "t", "text": " "}, {"type": "i", "children": [{"type": "t", "text": "J Immunol (2013)"}]}, {"type": "t", "text": " DOI: "}, {"type": "a", "children": [{"type": "t", "text": "10.4049/jimmunol.1301106"}], "href": "https://doi.org/10.4049/jimmunol.1301106"}, {"type": "t", "text": " PMID: "}, {"type": "a", "children": [{"type": "t", "text": "23956424"}], "href": "https://pubmed.ncbi.nlm.nih.gov/23956424"}]}, {"type": "r", "ref": 13, "children": [{"type": "t", "text": "Haruko Ideguchi, Atsuhisa Ueda, Masatsugu Tanaka, et al. "}, {"type": "b", "children": [{"type": "t", "text": "Structural and functional characterization of the USP11 deubiquitinating enzyme, which interacts with the RanGTP-associated protein RanBPM."}]}, {"type": "t", "text": " "}, {"type": "i", "children": [{"type": "t", "text": "Biochem J (2002)"}]}, {"type": "t", "text": " DOI: "}, {"type": "a", "children": [{"type": "t", "text": "10.1042/BJ20011851"}], "href": "https://doi.org/10.1042/BJ20011851"}, {"type": "t", "text": " PMID: "}, {"type": "a", "children": [{"type": "t", "text": "12084015"}], "href": "https://pubmed.ncbi.nlm.nih.gov/12084015"}]}, {"type": "r", "ref": 14, "children": [{"type": "t", "text": "Yan Wu, Xiaofeng Sun, Elzbieta Kaczmarek, et al. "}, {"type": "b", "children": [{"type": "t", "text": "RanBPM associates with CD39 and modulates ecto-nucleotidase activity."}]}, {"type": "t", "text": " "}, {"type": "i", "children": [{"type": "t", "text": "Biochem J (2006)"}]}, {"type": "t", "text": " DOI: "}, {"type": "a", "children": [{"type": "t", "text": "10.1042/BJ20051568"}], "href": "https://doi.org/10.1042/BJ20051568"}, {"type": "t", "text": " PMID: "}, {"type": "a", "children": [{"type": "t", "text": "16478441"}], "href": "https://pubmed.ncbi.nlm.nih.gov/16478441"}]}, {"type": "r", "ref": 15, "children": [{"type": "t", "text": "Nobuaki Kobayashi, Jun Yang, Atsuhisa Ueda, et al. "}, {"type": "b", "children": [{"type": "t", "text": "RanBPM, Muskelin, p48EMLP, p44CTLH, and the armadillo-repeat proteins ARMC8alpha and ARMC8beta are components of the CTLH complex."}]}, {"type": "t", "text": " "}, {"type": "i", "children": [{"type": "t", "text": "Gene (2007)"}]}, {"type": "t", "text": " DOI: "}, {"type": "a", "children": [{"type": "t", "text": "10.1016/j.gene.2007.02.032"}], "href": "https://doi.org/10.1016/j.gene.2007.02.032"}, {"type": "t", "text": " PMID: "}, {"type": "a", "children": [{"type": "t", "text": "17467196"}], "href": "https://pubmed.ncbi.nlm.nih.gov/17467196"}]}, {"type": "r", "ref": 16, "children": [{"type": "t", "text": "Manojkumar Valiyaveettil, Amber A Bentley, Priya Gursahaney, et al. "}, {"type": "b", "children": [{"type": "t", "text": "Novel role of the muskelin-RanBP9 complex as a nucleocytoplasmic mediator of cell morphology regulation."}]}, {"type": "t", "text": " "}, {"type": "i", "children": [{"type": "t", "text": "J Cell Biol (2008)"}]}, {"type": "t", "text": " DOI: "}, {"type": "a", "children": [{"type": "t", "text": "10.1083/jcb.200801133"}], "href": "https://doi.org/10.1083/jcb.200801133"}, {"type": "t", "text": " PMID: "}, {"type": "a", "children": [{"type": "t", "text": "18710924"}], "href": "https://pubmed.ncbi.nlm.nih.gov/18710924"}]}, {"type": "r", "ref": 17, "children": [{"type": "t", "text": "Madepalli K Lakshmana, Il-Sang Yoon, Eunice Chen, et al. "}, {"type": "b", "children": [{"type": "t", "text": "Novel role of RanBP9 in BACE1 processing of amyloid precursor protein and amyloid beta peptide generation."}]}, {"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.M807345200"}], "href": "https://doi.org/10.1074/jbc.M807345200"}, {"type": "t", "text": " PMID: "}, {"type": "a", "children": [{"type": "t", "text": "19251705"}], "href": "https://pubmed.ncbi.nlm.nih.gov/19251705"}]}, {"type": "r", "ref": 18, "children": [{"type": "t", "text": "Madepalli K Lakshmana, John Y Chung, Supul Wickramarachchi, et al. "}, {"type": "b", "children": [{"type": "t", "text": "A fragment of the scaffolding protein RanBP9 is increased in Alzheimer's disease brains and strongly potentiates amyloid-beta peptide generation."}]}, {"type": "t", "text": " "}, {"type": "i", "children": [{"type": "t", "text": "FASEB J (2010)"}]}, {"type": "t", "text": " DOI: "}, {"type": "a", "children": [{"type": "t", "text": "10.1096/fj.09-136457"}], "href": "https://doi.org/10.1096/fj.09-136457"}, {"type": "t", "text": " PMID: "}, {"type": "a", "children": [{"type": "t", "text": "19729516"}], "href": "https://pubmed.ncbi.nlm.nih.gov/19729516"}]}, {"type": "r", "ref": 19, "children": [{"type": "t", "text": "Ya-Chun Yang, Tzu-Hui Feng, Tse-Yao Chen, et al. "}, {"type": "b", "children": [{"type": "t", "text": "RanBPM regulates Zta-mediated transcriptional activity in Epstein-Barr virus."}]}, {"type": "t", "text": " "}, {"type": "i", "children": [{"type": "t", "text": "J Gen Virol (2015)"}]}, {"type": "t", "text": " DOI: "}, {"type": "a", "children": [{"type": "t", "text": "10.1099/vir.0.000157"}], "href": "https://doi.org/10.1099/vir.0.000157"}, {"type": "t", "text": " PMID: "}, {"type": "a", "children": [{"type": "t", "text": "25900136"}], "href": "https://pubmed.ncbi.nlm.nih.gov/25900136"}]}, {"type": "r", "ref": 20, "children": [{"type": "t", "text": "Yoonjeung Chang, Murugan Paramasivam, Matthew J Girgenti, et al. "}, {"type": "b", "children": [{"type": "t", "text": "RanBPM regulates the progression of neuronal precursors through M-phase at the surface of the neocortical ventricular zone."}]}, {"type": "t", "text": " "}, {"type": "i", "children": [{"type": "t", "text": "Dev Neurobiol (2010)"}]}, {"type": "t", "text": " DOI: "}, {"type": "a", "children": [{"type": "t", "text": "10.1002/dneu.20750"}], "href": "https://doi.org/10.1002/dneu.20750"}, {"type": "t", "text": " PMID: "}, {"type": "a", "children": [{"type": "t", "text": "19790105"}], "href": "https://pubmed.ncbi.nlm.nih.gov/19790105"}]}, {"type": "r", "ref": 21, "children": [{"type": "t", "text": "Key-Hwan Lim, Bharathi Suresh, Jung-Hyun Park, et al. "}, {"type": "b", "children": [{"type": "t", "text": "Ubiquitin-specific protease 11 functions as a tumor suppressor by modulating Mgl-1 protein to regulate cancer cell growth."}]}, {"type": "t", "text": " "}, {"type": "i", "children": [{"type": "t", "text": "Oncotarget (2016)"}]}, {"type": "t", "text": " DOI: "}, {"type": "a", "children": [{"type": "t", "text": "10.18632/oncotarget.7581"}], "href": "https://doi.org/10.18632/oncotarget.7581"}, {"type": "t", "text": " PMID: "}, {"type": "a", "children": [{"type": "t", "text": "26919101"}], "href": "https://pubmed.ncbi.nlm.nih.gov/26919101"}]}, {"type": "r", "ref": 22, "children": [{"type": "t", "text": "Shuai Shao, Ping-Hui Sun, Lucy K Satherley, et al. "}, {"type": "b", "children": [{"type": "t", "text": "Reduced RanBPM Expression Is Associated with Distant Metastasis in Gastric Cancer and Chemoresistance."}]}, {"type": "t", "text": " "}, {"type": "i", "children": [{"type": "t", "text": "Anticancer Res (2016)"}]}, {"type": "t", "text": " PMID: "}, {"type": "a", "children": [{"type": "t", "text": "26977028"}], "href": "https://pubmed.ncbi.nlm.nih.gov/26977028"}]}, {"type": "r", "ref": 23, "children": [{"type": "t", "text": "Huanzi Dai, Yang-Fan Lv, Guang-Ning Yan, et al. "}, {"type": "b", "children": [{"type": "t", "text": "RanBP9/TSSC3 complex cooperates to suppress anoikis resistance and metastasis via inhibiting Src-mediated Akt signaling in osteosarcoma."}]}, {"type": "t", "text": " "}, {"type": "i", "children": [{"type": "t", "text": "Cell Death Dis (2016)"}]}, {"type": "t", "text": " DOI: "}, {"type": "a", "children": [{"type": "t", "text": "10.1038/cddis.2016.436"}], "href": "https://doi.org/10.1038/cddis.2016.436"}, {"type": "t", "text": " PMID: "}, {"type": "a", "children": [{"type": "t", "text": "28032865"}], "href": "https://pubmed.ncbi.nlm.nih.gov/28032865"}]}, {"type": "r", "ref": 24, "children": [{"type": "t", "text": "Louisa M Salemi, Matthew E R Maitland, Eyal R Yefet, et al. "}, {"type": "b", "children": [{"type": "t", "text": "Inhibition of HDAC6 activity through interaction with RanBPM and its associated CTLH complex."}]}, {"type": "t", "text": " "}, {"type": "i", "children": [{"type": "t", "text": "BMC Cancer (2017)"}]}, {"type": "t", "text": " DOI: "}, {"type": "a", "children": [{"type": "t", "text": "10.1186/s12885-017-3430-2"}], "href": "https://doi.org/10.1186/s12885-017-3430-2"}, {"type": "t", "text": " PMID: "}, {"type": "a", "children": [{"type": "t", "text": "28668087"}], "href": "https://pubmed.ncbi.nlm.nih.gov/28668087"}]}, {"type": "r", "ref": 25, "children": [{"type": "t", "text": "Anna Tessari, Kareesma Parbhoo, Meghan Pawlikowski, et al. "}, {"type": "b", "children": [{"type": "t", "text": "RANBP9 affects cancer cells response to genotoxic stress and its overexpression is associated with worse response to platinum in NSCLC patients."}]}, {"type": "t", "text": " "}, {"type": "i", "children": [{"type": "t", "text": "Oncogene (2018)"}]}, {"type": "t", "text": " DOI: "}, {"type": "a", "children": [{"type": "t", "text": "10.1038/s41388-018-0424-8"}], "href": "https://doi.org/10.1038/s41388-018-0424-8"}, {"type": "t", "text": " PMID: "}, {"type": "a", "children": [{"type": "t", "text": "30076413"}], "href": "https://pubmed.ncbi.nlm.nih.gov/30076413"}]}]}]}
Synonyms	RanBP7, BPM-L, BPM90, RANBPM
Proteins	RANB9_HUMAN
NCBI Gene ID	10048
API
Download Associations
Predicted Functions
Co-expressed Genes
Expression in Tissues and Cell Lines

Functional Associations

RANBP9 has 7,507 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 132 datasets.

Click the + buttons to view associations for RANBP9 from the datasets below.

If available, associations are ranked by standardized value

Harmonizome 3.0

RANBP9 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 RANBP9 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 RANBP9 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 RANBP9 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 RANBP9 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 RANBP9 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 RANBP9 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 RANBP9 gene relative to other tissues from the Allen Brain Atlas Prenatal Human Brain Tissue Gene Expression Profiles dataset.
	BioGPS Cell Line Gene Expression Profiles	cell lines with high or low expression of RANBP9 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 RANBP9 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 RANBP9 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 RANBP9 gene from the Carcinogenome Chemical Perturbation Carcinogenicity Signatures dataset.
	CCLE Cell Line Gene CNV Profiles	cell lines with high or low copy number of RANBP9 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 RANBP9 gene relative to other cell lines from the CCLE Cell Line Gene Expression Profiles dataset.
	CCLE Cell Line Gene Mutation Profiles	cell lines with RANBP9 gene mutations from the CCLE Cell Line Gene Mutation Profiles dataset.
	CCLE Cell Line Proteomics	Cell lines associated with RANBP9 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 RANBP9 gene from the CHEA Transcription Factor Binding Site Profiles dataset.
	ChEA Transcription Factor Targets	transcription factors binding the promoter of RANBP9 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 RANBP9 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 RANBP9 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 RANBP9 gene from the CMAP Signatures of Differentially Expressed Genes for Small Molecules dataset.
	COMPARTMENTS Curated Protein Localization Evidence Scores	cellular components containing RANBP9 protein from the COMPARTMENTS Curated Protein Localization Evidence Scores dataset.
	COMPARTMENTS Curated Protein Localization Evidence Scores 2025	cellular components containing RANBP9 protein from the COMPARTMENTS Curated Protein Localization Evidence Scores 2025 dataset.
	COMPARTMENTS Experimental Protein Localization Evidence Scores	cellular components containing RANBP9 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 RANBP9 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 RANBP9 protein in abstracts of biomedical publications from the COMPARTMENTS Text-mining Protein Localization Evidence Scores 2025 dataset.
	CORUM Protein Complexes	protein complexs containing RANBP9 protein from the CORUM Protein Complexes dataset.
	COSMIC Cell Line Gene CNV Profiles	cell lines with high or low copy number of RANBP9 gene relative to other cell lines from the COSMIC Cell Line Gene CNV Profiles dataset.
	COSMIC Cell Line Gene Mutation Profiles	cell lines with RANBP9 gene mutations from the COSMIC Cell Line Gene Mutation Profiles dataset.
	CTD Gene-Disease Associations	diseases associated with RANBP9 gene/protein from the curated CTD Gene-Disease Associations dataset.
	DepMap CRISPR Gene Dependency	cell lines with fitness changed by RANBP9 gene knockdown relative to other cell lines from the DepMap CRISPR Gene Dependency dataset.
	DISEASES Experimental Gene-Disease Association Evidence Scores	diseases associated with RANBP9 gene in GWAS datasets from the DISEASES Experimental Gene-Disease Assocation Evidence Scores dataset.
	DISEASES Experimental Gene-Disease Association Evidence Scores 2025	diseases associated with RANBP9 gene in GWAS datasets from the DISEASES Experimental Gene-Disease Assocation Evidence Scores 2025 dataset.
	DISEASES Text-mining Gene-Disease Association Evidence Scores	diseases co-occuring with RANBP9 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 RANBP9 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 RANBP9 gene in GWAS and other genetic association datasets from the DisGeNET Gene-Disease Associations dataset.
	DisGeNET Gene-Phenotype Associations	phenotypes associated with RANBP9 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 RANBP9 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 RANBP9 gene from the ENCODE Transcription Factor Binding Site Profiles dataset.
	ENCODE Transcription Factor Targets	transcription factors binding the promoter of RANBP9 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 RANBP9 from the ESCAPE Omics Signatures of Genes and Proteins for Stem Cells dataset.