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Gene Review

OPN1LW  -  opsin 1 (cone pigments), long-wave-sensitive

Homo sapiens

Synonyms: CBBM, CBP, COD5, Long-wave-sensitive opsin 1, RCP, ...
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Disease relevance of OPN1LW

  • Adenovirus E1A proteins prepare the host cell for viral replication, stimulating cell cycling and viral transcription through interactions with critical cellular regulatory proteins such as RB and CBP [1].
  • APF/CBP, an anionic polypeptide in bile and gallstones that may regulate calcium salt and cholesterol precipitation from bile [2].
  • For the CBP pancreatic cancer line, CHS treatment increased tumor immunogenicity significantly, as demonstrated by diminished tumor growth rate and by increased duration of survival after challenge [3].
  • Tax stimulates HTLV-I transcription through high affinity binding to the KIX domain of CBP, a pleiotropic coactivator [4].
  • Mutations in transcription factors have recently been identified in a number of genetic diseases (for example, Denys-Drash syndrome, WT1 [19]; pituitary dwarfism, PIT1 [16]; Rubinstein-Taybi syndrome, CBP [20] [5].

High impact information on OPN1LW

  • Finally, our studies implicate recruitment by KLF2 of the transcriptional coactivator cyclic AMP response element-binding protein (CBP/p300) as a unifying mechanism for these various effects [6].
  • We now demonstrate that the p300 and CBP acetyltransferases play a major role in the in vivo acetylation of RelA, principally targeting lysines 218, 221 and 310 for modification [7].
  • In search of the underlying mechanism, we have found that CD44ICD potentiates transactivation mediated by the transcriptional coactivator CBP/p300 [8].
  • We recently identified and enriched a protein (CBP) from HeLa cells with binding specificity for cruciform-containing DNA [9].
  • We have now studied the interaction of CBP with stable cruciform DNA molecules containing the 27 bp palindrome of SV40 on one strand and an unrelated 26 bp palindrome on the other strand by hydroxyl radical footprinting [9].

Chemical compound and disease context of OPN1LW


Biological context of OPN1LW

  • This places L1CAM between this marker and the color vision genes (RCP, GCP), a region very dense in CpG islands, expected to contain a large fraction of the disease genes assigned to the Xq28 region [15].
  • The current study presents nucleotide sequence analyses and tests of neutrality for a 5.5-kb region of the X-linked long-wave "red" opsin gene (OPN1LW) in 236 individuals from ethnically diverse human populations [16].
  • Our analysis of the recombination landscape across OPN1LW reveals an unusual haplotype structure associated with amino acid replacement variation in exon 3 that is consistent with gene conversion [16].
  • BglII RFLP in DXS 498 between the pigment gene repeat unit, RCP and GCP [17].
  • The sequence homology reflects, at least partly, the conservation of common binding sites for the RB and CBP/p300 proteins, which are preserved in the same relative order along E2F1 and E1A [18].

Anatomical context of OPN1LW


Associations of OPN1LW with chemical compounds

  • Transplantable pancreatic carcinoma lines CBP and LSP-1 grown in inbred hamsters were tested for immunogenicity after CHS treatment [3].
  • In order to investigate the role of CBP in the regulation of endogenous genes, we isolated stable transformants that express Gal4-CBP(1-451) in response to added doxycycline [22].
  • CBP is required for sterol-regulated and sterol regulatory element-binding protein-regulated transcription [22].
  • Physical association between the histone acetyl transferase CBP and a histone methyl transferase [23].
  • TBK and RCP were measured before treatment to establish baseline values, after which all subjects received 6 mg piretanide a day for 14 days [24].

Other interactions of OPN1LW

  • The red (RCP) and green (GCP) color pigment genes are located in Xq28, a chromosomal region implicated in many genetic disorders [17].

Analytical, diagnostic and therapeutic context of OPN1LW

  • Immunizations were performed using both syngeneic and allogeneic cells and supernatants for both the CBP and LSP-1 systems for specificity experiments [3].
  • Mobility shift assays performed with the HLA-A2 ISRE revealed the presence of a constitutive binding protein (ISRE/CBP) [25].
  • Here, the in vivo association of CBP/14-3-3 with mammalian origins of DNA replication was analyzed by studying its association with the monkey replication origins ors8 and ors12, as assayed by a chromatin immunoprecipitation assay and quantitative PCR analysis [26].
  • Tertiary structure prediction of the KIX domain of CBP using Monte Carlo simulations driven by restraints derived from multiple sequence alignments [27].
  • CONCLUSION: In this study, CBP/Cat.II patients had significantly lower flowmetry parameters compared to matched age normals [28].


  1. Mammalian Srb/Mediator complex is targeted by adenovirus E1A protein. Boyer, T.G., Martin, M.E., Lees, E., Ricciardi, R.P., Berk, A.J. Nature (1999) [Pubmed]
  2. APF/CBP, an anionic polypeptide in bile and gallstones that may regulate calcium salt and cholesterol precipitation from bile. Ostrow, J.D. Hepatology (1992) [Pubmed]
  3. Active immunization of hamsters against pancreatic carcinoma with lipid-treated cells or their shed antigens. Skornick, Y., Kurman, C.C., Sindelar, W.F. Cancer Res. (1984) [Pubmed]
  4. Binding of the human T-cell leukemia virus Tax protein to the coactivator CBP interferes with CBP-mediated transcriptional control. Van Orden, K., Yan, J.P., Ulloa, A., Nyborg, J.K. Oncogene (1999) [Pubmed]
  5. The alpha-thalassemia/mental retardation syndromes. Gibbons, R.J., Higgs, D.R. Medicine (Baltimore) (1996) [Pubmed]
  6. KLF2 Is a novel transcriptional regulator of endothelial proinflammatory activation. SenBanerjee, S., Lin, Z., Atkins, G.B., Greif, D.M., Rao, R.M., Kumar, A., Feinberg, M.W., Chen, Z., Simon, D.I., Luscinskas, F.W., Michel, T.M., Gimbrone, M.A., García-Cardeña, G., Jain, M.K. J. Exp. Med. (2004) [Pubmed]
  7. Acetylation of RelA at discrete sites regulates distinct nuclear functions of NF-kappaB. Chen, L.F., Mu, Y., Greene, W.C. EMBO J. (2002) [Pubmed]
  8. Proteolytic release of CD44 intracellular domain and its role in the CD44 signaling pathway. Okamoto, I., Kawano, Y., Murakami, D., Sasayama, T., Araki, N., Miki, T., Wong, A.J., Saya, H. J. Cell Biol. (2001) [Pubmed]
  9. A novel type of interaction between cruciform DNA and a cruciform binding protein from HeLa cells. Pearson, C.E., Zannis-Hadjopoulos, M., Price, G.B., Zorbas, H. EMBO J. (1995) [Pubmed]
  10. Hypoxia-activated metabolic pathway stimulates phosphorylation of p300 and CBP in oxygen-sensitive cells. Zakrzewska, A., Schnell, P.O., Striet, J.B., Hui, A., Robbins, J.R., Petrovic, M., Conforti, L., Gozal, D., Wathelet, M.G., Czyzyk-Krzeska, M.F. J. Neurochem. (2005) [Pubmed]
  11. The versatile functions of the transcriptional coactivators p300 and CBP and their roles in disease. Janknecht, R. Histol. Histopathol. (2002) [Pubmed]
  12. The bedtime administration of doxazosin controls morning hypertension and albuminuria in patients with type-2 diabetes: evaluation using home-based blood pressure measurements. Kamoi, K., Ikarashi, T. Clin. Exp. Hypertens. (2005) [Pubmed]
  13. Demonstration of type-R and type-C virus particles in hamster pancreatic adenocarcinomas. Sindelar, W.F., Tralka, T.S., Kurman, C.C., Hyatt, C.L., Henson, E.R. Cancer Lett. (1983) [Pubmed]
  14. Multiple myeloma resistant to melphalan: treatment with cyclophosphamide, prednisone, and BCNU. Kyle, R.A., Gailani, S., Seligman, B.R., Blom, J., McIntyre, O.R., Pajak, T.F., Holland, J.F. Cancer treatment reports. (1979) [Pubmed]
  15. Completion of the physical map of Xq28: the location of the gene for L1CAM on the human X chromosome. Dietrich, A., Korn, B., Poustka, A. Mamm. Genome (1992) [Pubmed]
  16. Signatures of selection and gene conversion associated with human color vision variation. Verrelli, B.C., Tishkoff, S.A. Am. J. Hum. Genet. (2004) [Pubmed]
  17. BglII RFLP in DXS 498 between the pigment gene repeat unit, RCP and GCP. Vits, L., Willems, P.J. Hum. Genet. (1992) [Pubmed]
  18. E2F1 and E1A(12S) have a homologous activation domain regulated by RB and CBP. Trouche, D., Kouzarides, T. Proc. Natl. Acad. Sci. U.S.A. (1996) [Pubmed]
  19. The cytoskeletal system of nucleated erythrocytes. II. presence of a high molecular weight calmodulin-binding protein. Bartelt, D.C., Carlin, R.K., Scheele, G.A., Cohen, W.D. J. Cell Biol. (1982) [Pubmed]
  20. E1A represses apolipoprotein AI enhancer activity in liver cells through a pRb- and CBP-independent pathway. Kilbourne, E.J., Evans, M.J., Karathanasis, S.K. Nucleic Acids Res. (1998) [Pubmed]
  21. Long-term follow-up of persisting mixed chimerism after partially T cell-depleted allogeneic stem cell transplantation. Schaap, N., Schattenberg, A., Mensink, E., Preijers, F., Hillegers, M., Knops, R., Pennings, A., Boezeman, J., Geurts van Kessel, A., de Pauw, B., de Witte, T. Leukemia (2002) [Pubmed]
  22. CBP is required for sterol-regulated and sterol regulatory element-binding protein-regulated transcription. Ericsson, J., Edwards, P.A. J. Biol. Chem. (1998) [Pubmed]
  23. Physical association between the histone acetyl transferase CBP and a histone methyl transferase. Vandel, L., Trouche, D. EMBO Rep. (2001) [Pubmed]
  24. Potassium balance in piretanide and digoxin treatment. Muller, F.O., Meyer, B.H., de Waal, A., van Reenen, O.R., Grigoleit, H.G. Clin. Pharmacol. Ther. (1982) [Pubmed]
  25. The human leukocyte antigen A2 interferon-stimulated response element consensus sequence binds a nuclear factor required for constitutive expression. Waring, J.F., Radford, J.E., Burns, L.J., Ginder, G.D. J. Biol. Chem. (1995) [Pubmed]
  26. The human cruciform-binding protein, CBP, is involved in DNA replication and associates in vivo with mammalian replication origins. Novac, O., Alvarez, D., Pearson, C.E., Price, G.B., Zannis-Hadjopoulos, M. J. Biol. Chem. (2002) [Pubmed]
  27. Tertiary structure prediction of the KIX domain of CBP using Monte Carlo simulations driven by restraints derived from multiple sequence alignments. Ortiz, A.R., Kolinski, A., Skolnick, J. Proteins (1998) [Pubmed]
  28. Voiding dysfunction associated with "chronic bacterial prostatitis". Ghobish, A. Eur. Urol. (2002) [Pubmed]
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