Y box binding protein 1

(Redirected from YB-1)

Y box binding protein 1 also known as Y-box transcription factor or nuclease-sensitive element-binding protein 1 is a protein that in humans is encoded by the YBX1 gene.[5] YBX1 is an RNA binding protein[6] that stabilises messenger RNAs modified with N6-methyladenosine.[7]

YBX1
Available structures
PDBOrtholog search: PDBe RCSB
Identifiers
AliasesYBX1, BP-8, CSDA2, CSDB, DBPB, MDR-NF1, NSEP-1, NSEP1, YB-1, YB1, CBF-A, EFI-A, Y-box binding protein 1
External IDsOMIM: 154030; MGI: 99146; HomoloGene: 88707; GeneCards: YBX1; OMA:YBX1 - orthologs
Orthologs
SpeciesHumanMouse
Entrez
Ensembl
UniProt
RefSeq (mRNA)

NM_004559

NM_011732

RefSeq (protein)

NP_004550

NP_035862

Location (UCSC)Chr 1: 42.68 – 42.7 MbChr 4: 119.14 – 119.15 Mb
PubMed search[3][4]
Wikidata
View/Edit HumanView/Edit Mouse

Clinical significance

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YBX1 is a potential drug target in cancer therapy.[8] YB-1 helps the replication of adenovirus type 5, a commonly used vector in gene therapy.[8] Thus, YB-1 can cause an "oncolytic" effect in YB-1 positive cancer cells treated with adenoviruses.

Interactions

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Y box binding protein 1 has been shown to interact with:

References

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  1. ^ a b c GRCh38: Ensembl release 89: ENSG00000065978Ensembl, May 2017
  2. ^ a b c GRCm38: Ensembl release 89: ENSMUSG00000028639Ensembl, May 2017
  3. ^ "Human PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
  4. ^ "Mouse PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
  5. ^ EntrezGene 4904 YBX1 Y-box binding protein 1
  6. ^ Kwon E, Todorova K, Wang J, Horos R, Lee KK, Neel VA, et al. (April 2018). "The RNA-binding protein YBX1 regulates epidermal progenitors at a posttranscriptional level". Nature Communications. 9 (1): 1734. Bibcode:2018NatCo...9.1734K. doi:10.1038/s41467-018-04092-0. PMC 5928080. PMID 29712925.
  7. ^ Feng M, Xie X, Han G, Zhang T, Li Y, Li Y, et al. (July 2021). "YBX1 is required for maintaining myeloid leukemia cell survival by regulating BCL2 stability in an m6A-dependent manner". Blood. 138 (1): 71–85. doi:10.1182/blood.2020009676. PMC 8667054. PMID 33763698.
  8. ^ a b Lage H, Surowiak P, Holm PS (November 2008). "[YB-1 as a potential target in cancer therapy]". Der Pathologe (in German). 29 (Suppl 2): 187–190. doi:10.1007/s00292-008-1030-2. PMID 18773210.
  9. ^ a b Kojic S, Medeot E, Guccione E, Krmac H, Zara I, Martinelli V, et al. (May 2004). "The Ankrd2 protein, a link between the sarcomere and the nucleus in skeletal muscle". Journal of Molecular Biology. 339 (2): 313–325. doi:10.1016/j.jmb.2004.03.071. PMID 15136035.
  10. ^ Chernukhin IV, Shamsuddin S, Robinson AF, Carne AF, Paul A, El-Kady AI, et al. (September 2000). "Physical and functional interaction between two pluripotent proteins, the Y-box DNA/RNA-binding factor, YB-1, and the multivalent zinc finger factor, CTCF". The Journal of Biological Chemistry. 275 (38): 29915–29921. doi:10.1074/jbc.M001538200. PMID 10906122.
  11. ^ Okamoto T, Izumi H, Imamura T, Takano H, Ise T, Uchiumi T, et al. (December 2000). "Direct interaction of p53 with the Y-box binding protein, YB-1: a mechanism for regulation of human gene expression". Oncogene. 19 (54): 6194–6202. doi:10.1038/sj.onc.1204029. PMID 11175333.
  12. ^ Ise T, Nagatani G, Imamura T, Kato K, Takano H, Nomoto M, et al. (January 1999). "Transcription factor Y-box binding protein 1 binds preferentially to cisplatin-modified DNA and interacts with proliferating cell nuclear antigen". Cancer Research. 59 (2): 342–346. PMID 9927044.
  13. ^ Chibi M, Meyer M, Skepu A, G Rees DJ, Moolman-Smook JC, Pugh DJ (December 2008). "RBBP6 interacts with multifunctional protein YB-1 through its RING finger domain, leading to ubiquitination and proteosomal degradation of YB-1". Journal of Molecular Biology. 384 (4): 908–916. doi:10.1016/j.jmb.2008.09.060. PMID 18851979.
  14. ^ Raffetseder U, Frye B, Rauen T, Jürchott K, Royer HD, Jansen PL, et al. (May 2003). "Splicing factor SRp30c interaction with Y-box protein-1 confers nuclear YB-1 shuttling and alternative splice site selection". The Journal of Biological Chemistry. 278 (20): 18241–18248. doi:10.1074/jbc.M212518200. PMID 12604611.

Further reading

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This article incorporates text from the United States National Library of Medicine, which is in the public domain.