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Last update 08 May 2025

RYBP

Last update 08 May 2025

Basic Info

Synonyms

AAP1, APAP-1, Apoptin-associating protein 1

+ [8]

Introduction

Component of a Polycomb group (PcG) multiprotein PRC1-like complex, a complex class required to maintain the transcriptionally repressive state of many genes, including Hox genes, throughout development. PcG PRC1-like complex acts via chromatin remodeling and modification of histones; it mediates monoubiquitination of histone H2A 'Lys-119', rendering chromatin heritably changed in its expressibility (PubMed:25519132). Component of a PRC1-like complex that mediates monoubiquitination of histone H2A 'Lys-119' on the X chromosome and is required for normal silencing of one copy of the X chromosome in XX females. May stimulate ubiquitination of histone H2A 'Lys-119' by recruiting the complex to target sites (By similarity). Inhibits ubiquitination and subsequent degradation of TP53, and thereby plays a role in regulating transcription of TP53 target genes (PubMed:19098711). May also regulate the ubiquitin-mediated proteasomal degradation of other proteins like FANK1 to regulate apoptosis (PubMed:14765135, PubMed:27060496). May be implicated in the regulation of the transcription as a repressor of the transcriptional activity of E4TF1 (PubMed:11953439). May bind to DNA (By similarity). May play a role in the repression of tumor growth and metastasis in breast cancer by down-regulating SRRM3 (PubMed:27748911).

Drugs associated with RYBP

VV-GMCSF-Apo(Institute of Chemical Biology and Fundamental Medicine)

Target

GM-CSF x RYBP

Mechanism

GM-CSF stimulants [+1]

Active Org.-

Originator Org.

Institute of Chemical Biology and Fundamental Medicine SB RAS

Active Indication-

Inactive Indication

Neoplasms

Drug Highest PhasePending

First Approval Ctry. / Loc.-

First Approval Date20 Jan 1800

100 Clinical Results associated with RYBP

100 Translational Medicine associated with RYBP

0 Patents (Medical) associated with RYBP

206

Literatures (Medical) associated with RYBP

01 Jun 2025·Molecular Immunology

MicroRNA-770 promotes polarization of macrophages and hemorrhoids by suppressing RYBP expression and monoubiquitination of histone H2A on Lys119 modification

Article

Author: Liu, Te ; Yang, Wei ; Zhou, Haikun ; Zhong, Shenglan

Hemorrhoid disease (HD) is a common proctological condition whose onset is associated with an abnormal inflammatory microenvironment; however, the underlying mechanisms remain unclear. In this study, pathological examination revealed a significant increase in MΦ1 macrophages in the hemorrhoidal tissue of patients with HD, along with elevated levels of inflammatory factors. qPCR results demonstrated that the expression of several members of the DLK1-DIO3 microRNA cluster, particularly miR-770, was significantly higher in the hemorrhoid tissue of patients with HD than in that of the control group. Luciferase reporter assays confirmed that RYBP is a target gene negatively regulated by miR-770. Additionally, qPCR and western blot analyses indicated that overexpression of miR-770 significantly downregulated the expression of PRC1 family genes and RYBP in THP-1 cells, while concurrently upregulating the expression of inflammatory factors such as NFKB, IL1b, IL4, TNF, and IFNG. The overexpression of miR-770 significantly induced the polarization of THP-1 cells toward MΦ1. Mechanistic studies using ChIP-seq revealed that miR-770 overexpression significantly reduced the number of gene promoters in MΦ1 cells that bind to histone H2AK119-Ub sites. Furthermore, the number of enriched DNA fragments from genes that bind to the + 1 transcription start site of histone H2AK119-Ub, such as NFKB1, IL1B, and TNF, was significantly lower than that observed in the control group. Therefore, we confirmed that miR-770, a genomic imprinted member of the DLK1-DIO3 region, negatively regulated the expression of the PRC1 family member RYBP, reduced the level of ubiquitination modification at histone H2AK119-Ub, and promoted the transcriptional activation of pro-inflammatory genes. This ultimately leads to MΦ1 polarization and the release of inflammatory factors, elucidating the epigenetic mechanisms underlying the occurrence of hemorrhoids.

01 May 2025·Archives of Microbiology

Computational prediction of Homo sapiens–Candida albicans protein–protein interactions reveal key virulence factors using dual RNA-Seq data analysis

Article

Author: Kaur, Ekjot ; Acharya, Vishal

A prevalent pathobiont, Candida albicans, accounts for approximately 70% of fungal infections worldwide owing to its virulence traits that culminate in devastating fatalities within healthcare facilities. Protein-protein interactions (PPIs) between Homo sapiens and C. albicans play a pivotal role in infection and disease progression. Additionally, scarcity of information on H. sapiens-C. albicans protein-protein interactions makes it difficult to understand the molecular mechanisms underlying infection and host immune responses. Investigating these PPIs can provide crucial insights into host-pathogen relationships and facilitate the development of novel therapeutic interventions. To address this challenge, we utilized computational techniques based on homology and domain to project 56,515 human-fungal pathogen protein-protein interactions (HF-PPIs) involving 6830 human and 486 C. albicans proteins. We have identified 16 key virulence factors of C. albicans, including SOD1, ERG10, GFA1, and VPS4, as potential therapeutic targets. As evidenced by dual RNA-Seq data acquired at various stages of infection such as 15, 30, 60, 120, and 240 min, these fungal genes interact with down-regulated human immunomodulatory genes specifically, ADRM1, DAXX, RYBP, SGTA, and SRGN. In addition to their intrinsically disordered regions, these human genes are particularly susceptible to fungal manipulation. Through the identification of experimentally validated virulence factors and their interaction partners, this investigation constructs HF-PPI between H. sapiens and C. albicans. Our knowledge of human-fungal pathogen protein-protein interactions will be improved by integrating computational and experimental data in order to facilitate the development of efficient fungal infection prevention and treatment protocols.

01 Apr 2025·Genetics in Medicine

De novo variants in RYBP are associated with a severe neurodevelopmental disorder and congenital anomalies

Article

Author: Berry, Gerard T. ; Craigen, William J. ; Lanpher, Brendan C. ; Rydzanicz, Malgorzata ; Davis, Joie ; Allenspach, Eric ; Wener, Mark ; High, Frances ; Potocki, Lorraine ; Fu, Jiayu ; Doherty, Daniel ; Whitlock, Jordan ; Eng, Christine M. ; Rossignol, Francis ; Neumann, Serena ; Maghiro, AudreyStephannie ; Petcharet, Leoyklang ; Martínez-Agosto, Julian A. ; Delgado, Margaret ; Rebelo, Adriana ; Malicdan, May Christine V. ; Andrews, Ashley ; Bivona, Stephanie ; Marom, Ronit ; Morimoto, Marie ; Yamamoto, Shinya ; Tekin, Mustafa ; Chung, Wendy K. ; Karasozen, Yigit ; Callaway, Kaitlin ; Korrick, Susan ; Bennett, Jimmy ; Thorson, Willa ; Hernan, Rebecca R. ; Scott, Daryl A. ; Dai, Hongzheng ; Fisher, Paul G. ; Solomon, Ben ; Parker, Neil H. ; Barbouth, Deborah ; Alvarez, Raquel L. ; Latchman, Kumarie ; Narayanan, Vinodh ; Bayrak-Toydemir, Pinar ; Heide, Solveig ; Corona, Rosario I. ; Velinder, Matt ; Bacino, Carlos ; Korf, Bruce ; Worley, Kim ; Dipple, Katrina ; Cole, F. Sessions ; Earl, Dawn ; Fieg, Elizabeth L. ; Lim, Foong Y. ; Glanton, Emily ; Rosenfeld, Jill A. ; Bacino, Carlos A. ; Huang, Yan ; Bejerano, Gill ; Klee, Eric ; Hanchard, Neal ; Tifft, Cynthia J. ; Wegner, Daniel ; Shelkowitz, Emily ; Sampson, Jacinda B. ; Burrage, Lindsay C. ; Taylor, Herman ; Smith, Kevin S. ; Walker, Melissa ; Bale, Jim ; Lee, Brendan H. ; Weisz-Hubshman, Monika ; Rodriguez, Martin ; Mahoney, Rachel ; Cobban, Laurel A. ; Rajagopalan, Ramakrishnan ; Stembalska, Agnieszka ; Jangam, Sharayu V. ; Keren, Boris ; Shashi, Vandana ; Balasubramanyam, Ashok ; Quinlan, Aaron ; Huang, Alden ; Orengo, James P. ; Beck, Anita ; McMinn, Ashley ; Hurst, Anna ; Ketkar, Shamika ; Gahl, William A. ; Krakow, Deborah ; Bergmann, Anke ; Lam, Christina ; Halley, Meghan C. ; Introne, Wendy ; Vogel, Tiphanie P. ; Kravets, Elijah ; Westerfield, Monte ; Hisama, Fuki M. ; Leppig, Kathleen A. ; Sutton, Shirley ; Kohane, Isaac S. ; Stergachis, Andrew ; Brunet, Theresa ; Ashley, Euan A. ; Butte, Manish J. ; Glass, Ian ; Ward, Patricia A. ; Bademci, Guney ; Zuchner, Stephan ; von Hardenberg, Sandra ; Lalani, Seema R. ; Ruzhnikov, Maura ; Hom, Jason ; e Vairo, Filippo Pinto ; Schedl, Timothy ; Sheppeard, Sam ; Jean-Marie, Orpa ; Chanprasert, Sirisak ; Sweetser, David A. ; Jarvik, Gail P. ; Blue, Elizabeth ; Murdock, David R. ; Mikati, Mohamad ; Zhang, Zhe ; Pusey Swerdzewski, Barbara N. ; Chinn, Ivan ; Novacic, Donna ; Raskind, Wendy ; Dell’Angelica, Esteban C. ; Martin, Martin G. ; Wambach, Jennifer ; Graves, Hillary K. ; Richter, Manuela Friederike ; Pace, Laura ; Sirugo, Giorgio ; Mitchell, Breanna ; Acosta, Maria T. ; Rader, Daniel J. ; Sisco, Kathy ; Holm, Ingrid A. ; Wahl, Colleen E. ; Bernstein, Jonathan A. ; Raper, Anna ; Lee, Brendan ; Dawson, Brian ; Seto, Elaine ; Sybert, Virginia ; Schoch, Kelly ; Might, Matthew ; Dargie, Nitsuh K. ; Ploski, Rafal ; Cuddapah, Vishnu ; Solnica-Krezel, Lilianna ; Sullivan, Kathleen ; Carey, John ; Rao, Deepak A. ; Toro, Camilo ; Hing, Anne ; Kiley, Dana ; Skraban, Cara ; Dasari, Surendra ; Martin, Beth A. ; Crouse, Andrew B. ; Coakley, Terra R. ; Rives, Lynette ; Maduro, Valerie V. ; Pallais, J. Carl ; Burke, Elizabeth A. ; Beggs, Alan H. ; Afzali, Ben ; Spillmann, Rebecca C. ; Shin, Jimann ; Emrick, Lisa T. ; Briere, Lauren C. ; Tran, Alyssa A. ; Tan, Queenie ; Coggins, Matthew ; Viskochil, Dave ; Bellen, Hugo J. ; Esteves, Cecilia ; Loscalzo, Joseph ; Rosenthal, Elizabeth ; Wheeler, Matthew T. ; Kobren, Shilpa N. ; Moretti, Paolo ; Nakano-Okuno, Mariko ; Cogan, Joy D. ; Oglesbee, Devin ; Gropman, Andrea ; Maas, Richard L. ; Liu, Pengfei ; D’Souza, Precilla ; Mulvihill, Lindsay ; Jobanputra, Vaidehi ; Schimmenti, Lisa ; Horike-Pyne, Martha ; Corner, Brian ; Wood, Heidi ; Ungar, Rachel A. ; Bohnsack, John ; Cassini, Thomas ; Adams, David R. ; Mulvihill, John J. ; Behrens, Edward ; Longo, Nicola ; Gonzalez, Joanna M. ; Smith, Carson A. ; Byers, Peter ; Botto, Lorenzo ; Miller, Danny ; Ganetzky, Rebecca ; Kilich, Gonench ; Baldridge, Dustin ; Stoler, Joan M. ; Bamshad, Michael ; Allworth, Aimee ; Hayes, Nichole ; Pak, Stephen ; Wenger, Tara ; Darr, Kahlen ; Posey, Jennifer E. ; LeBlanc, Kimberly ; Rodan, Lance H. ; Wangler, Michael F. ; Silverman, Edwin K. ; McConkie-Rosell, Allyn ; Al-Beshri, Ali ; Reuter, Chloe M. ; Fogel, Brent L. ; Macnamara, Ellen F. ; Vanderver, Adeline ; Carvalho, George ; Bonner, Devon ; Syrbe, Steffen ; Peart, LéShon ; Borja, Nicholas ; Dorrani, Naghmeh ; Goddard, Page C. ; Nelson, Stanley F. ; Alvey, Justin ; Balton, Elsa ; Kohler, Jennefer N. ; Clark, Gary D. ; Jayadev, Suman ; Chao, Hsiao-Tuan ; Kanca, Oguz ; Ezell, Kimberly ; Wolfe, Lynne A. ; Byrd, William E. ; Hassey, Kelly ; Xia, Fan ; MacRae, Calum A. ; Walley, Nicole M. ; Tarakad, Arjun ; Sabaii, Marla ; Phillips, John A. ; Marwaha, Shruti ; Baldwin, Erin ; Lanza, Ian R. ; Lewis, Richard A. ; Tabor, Holly K. ; Sunyaev, Shamil R. ; Mao, Rong ; Marth, Gabor ; Mirzaa, Ghayda ; Douine, Emilie D. ; Hamid, Rizwan ; Skelton, Tammi ; Douglas, Jessica

PURPOSEPolycomb group proteins are key epigenetic transcriptional regulators. Multiple neurodevelopmental disorders are associated with pathogenic variants of the genes encoding Polycomb group proteins. RYBP is a core component of the noncanonical Polycomb Repressor Complex 1; however, its role in disease is unclear.METHODSFunctional consequences of RYBP variants were assessed using in vitro cellular and in vivo Drosophila melanogaster studies.RESULTSWe described 7 individuals with heterozygous de novo variants of RYBP and their clinical findings, including severe developmental delay, dysmorphisms, and multiple congenital anomalies. We showed that all single-nucleotide variants in RYBP localize to the N-terminal domain of the gene, which encodes the zinc-finger domain and ubiquitin-binding moiety. In vitro studies have demonstrated that the RYBP c.132C>G p.(Cys44Trp) variant causes reduced protein expression but does not affect the binding of YY1, RING1B, or ubiquitin. In vivo overexpression studies in Drosophila melanogaster showed a dramatic functional difference between human RYBP and its variant forms, affecting the C44 amino acid residue. DNA methylation studies suggested a possible episignature associated with RYBP-related disorder.CONCLUSIONHeterozygous de novo variants in RYBP are associated with an identifiable syndromic neurodevelopmental disorder with multiple congenital anomalies.

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RYBP

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