RYBP (original) (raw)

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Protein-coding gene in the species Homo sapiens

RYBP
Available structuresPDBHuman UniProt search: PDBe RCSB List of PDB id codes3IXS
Identifiers
Aliases RYBP, AAP1, DEDAF, YEAF1, APAP-1, RING1 and YY1 binding protein
External IDs OMIM: 607535; MGI: 3648043; HomoloGene: 8159; GeneCards: RYBP; OMA:RYBP - orthologs
Gene location (Human)Chromosome 3 (human)Chr.Chromosome 3 (human)[1]Chromosome 3 (human)Genomic location for RYBPGenomic location for RYBPBand3p13Start72,371,825 bp[1]End72,446,621 bp[1]
RNA expression patternBgeeHuman Mouse (ortholog)Top expressed inlower lobe of lungcartilage tissueendothelial celltrabecular boneurethraRegion I of hippocampus propermiddle frontal gyrusoptic nerveplacentainferior ganglion of vagus nerven/aMore reference expression dataBioGPSMore reference expression data
Gene ontologyMolecular function DNA binding protein binding transcription corepressor activity metal ion binding Cellular component cytoplasm PcG protein complex nucleus nucleoplasm Biological process multicellular organism development histone H2A monoubiquitination regulation of transcription, DNA-templated transcription, DNA-templated apoptotic process negative regulation of transcription by RNA polymerase II negative regulation of proteasomal ubiquitin-dependent protein catabolic process positive regulation of apoptotic process positive regulation of transcription, DNA-templated negative regulation of G0 to G1 transition Sources:Amigo / QuickGO
OrthologsSpeciesHuman MouseEntrez23429628746EnsemblENSG00000281766ENSG00000163602n/aUniProtQ8N488n/aRefSeq (mRNA)NM_012234XM_036158262RefSeq (protein)NP_036366n/aLocation (UCSC)Chr 3: 72.37 – 72.45 Mbn/aPubMed search[2][3]
Wikidata
View/Edit HumanView/Edit Mouse

RING1 and YY1-binding protein is a protein that in humans is encoded by the RYBP gene.[4][5]

RYBP has been shown to interact with:

  1. ^ a b c ENSG00000163602 GRCh38: Ensembl release 89: ENSG00000281766, ENSG00000163602Ensembl, May 2017
  2. ^ "Human PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
  3. ^ "Mouse PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
  4. ^ a b c d García E, Marcos-Gutiérrez C, del Mar Lorente M, Moreno JC, Vidal M (Jun 1999). "RYBP, a new repressor protein that interacts with components of the mammalian Polycomb complex, and with the transcription factor YY1". The EMBO Journal. 18 (12): 3404–18. doi:10.1093/emboj/18.12.3404. PMC 1171420. PMID 10369680.
  5. ^ "Entrez Gene: RYBP RING1 and YY1 binding protein".
  6. ^ Zhu J, Shore SK (Dec 1996). "c-ABL tyrosine kinase activity is regulated by association with a novel SH3-domain-binding protein". Molecular and Cellular Biology. 16 (12): 7054–62. doi:10.1128/mcb.16.12.7054. PMC 231708. PMID 8943360.
  7. ^ Zheng L, Schickling O, Peter ME, Lenardo MJ (Aug 2001). "The death effector domain-associated factor plays distinct regulatory roles in the nucleus and cytoplasm". The Journal of Biological Chemistry. 276 (34): 31945–52. doi:10.1074/jbc.M102799200. PMID 11395500.
  8. ^ a b Schlisio S, Halperin T, Vidal M, Nevins JR (Nov 2002). "Interaction of YY1 with E2Fs, mediated by RYBP, provides a mechanism for specificity of E2F function". The EMBO Journal. 21 (21): 5775–86. doi:10.1093/emboj/cdf577. PMC 131074. PMID 12411495.
  9. ^ Chen D, Zhang J, Li M, Rayburn ER, Wang H, Zhang R (Feb 2009). "RYBP stabilizes p53 by modulating MDM2". EMBO Reports. 10 (2): 166–72. doi:10.1038/embor.2008.231. PMC 2637313. PMID 19098711.
  10. ^ Rual JF, Venkatesan K, Hao T, Hirozane-Kishikawa T, Dricot A, Li N, Berriz GF, Gibbons FD, Dreze M, Ayivi-Guedehoussou N, Klitgord N, Simon C, Boxem M, Milstein S, Rosenberg J, Goldberg DS, Zhang LV, Wong SL, Franklin G, Li S, Albala JS, Lim J, Fraughton C, Llamosas E, Cevik S, Bex C, Lamesch P, Sikorski RS, Vandenhaute J, Zoghbi HY, Smolyar A, Bosak S, Sequerra R, Doucette-Stamm L, Cusick ME, Hill DE, Roth FP, Vidal M (Oct 2005). "Towards a proteome-scale map of the human protein-protein interaction network". Nature. 437 (7062): 1173–8. Bibcode:2005Natur.437.1173R. doi:10.1038/nature04209. PMID 16189514. S2CID 4427026.