NPAS2

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abbr. for neuronal PAS domain protein 2; a basic helix-loop-helix transcription factor that has two PAS domains, each of which contains a heme group. It forms a dimer with BMAL1 through which it binds to a specific DNA motif and directs transcription of over a hundred genes, including those for period and cryptochrome proteins. NPAS2 is homologous with clock and like it controls circadian activity and is regulated by the redox state of NAD(P). It has the same role in the forebrain as clock has in the hypothalamus. CO binds the heme of NPAS2 and prevents it from dimerizing with BMAL1.

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Neuronal PAS domain protein 2
Identifiers
Symbols NPAS2; FLJ23138; MGC71151; MOP4; PASD4
External IDs OMIM: 603347 MGI109232 HomoloGene1887 GeneCards: NPAS2 Gene
RNA expression pattern
PBB GE NPAS2 39548 at tn.png
PBB GE NPAS2 205459 s at tn.png
PBB GE NPAS2 205460 at tn.png
More reference expression data
Orthologs
Species Human Mouse
Entrez 4862 18143
Ensembl ENSG00000170485 ENSMUSG00000026077
UniProt Q99743 Q32ME6
RefSeq (mRNA) NM_002518 NM_008719
RefSeq (protein) NP_002509 NP_032745
Location (UCSC) Chr 2:
100.8 - 100.98 Mb
Chr 1:
39.14 - 39.31 Mb
PubMed search [1] [2]

Neuronal PAS domain-containing protein 2 is a protein that in humans is encoded by the NPAS2 gene.[1][2]

The protein encoded by this gene is a member of the basic helix-loop-helix (bHLH)-PAS family of transcription factors. A similar mouse protein may play a regulatory role in the acquisition of specific types of memory. It also may function as a part of a molecular clock operative in the mammalian forebrain.[3]

Contents

Interactions

NPAS2 has been shown to interact with Retinoic acid receptor alpha,[4] EP300,[5] ARNTL[4][6] and Retinoid X receptor alpha.[4]

References

  1. ^ Zhou YD, Barnard M, Tian H, Li X, Ring HZ, Francke U, Shelton J, Richardson J, Russell DW, McKnight SL (Mar 1997). "Molecular characterization of two mammalian bHLH-PAS domain proteins selectively expressed in the central nervous system". Proc Natl Acad Sci USA 94 (2): 713–8. doi:10.1073/pnas.94.2.713. PMID 9012850. 
  2. ^ Hogenesch JB, Chan WK, Jackiw VH, Brown RC, Gu YZ, Pray-Grant M, Perdew GH, Bradfield CA (May 1997). "Characterization of a subset of the basic-helix-loop-helix-PAS superfamily that interacts with components of the dioxin signaling pathway". J Biol Chem 272 (13): 8581–93. doi:10.1074/jbc.272.13.8581. PMID 9079689. 
  3. ^ "Entrez Gene: NPAS2 neuronal PAS domain protein 2". http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=4862. 
  4. ^ a b c McNamara, P; Seo S B, Rudic R D, Sehgal A, Chakravarti D, FitzGerald G A (Jun. 2001). "Regulation of CLOCK and MOP4 by nuclear hormone receptors in the vasculature: a humoral mechanism to reset a peripheral clock". Cell (United States) 105 (7): 877–89. doi:10.1016/S0092-8674(01)00401-9. ISSN 0092-8674. PMID 11439184. 
  5. ^ Curtis, Anne M; Seo Sang-beom, Westgate Elizabeth J, Rudic Radu Daniel, Smyth Emer M, Chakravarti Debabrata, FitzGerald Garret A, McNamara Peter (Feb. 2004). "Histone acetyltransferase-dependent chromatin remodeling and the vascular clock". J. Biol. Chem. (United States) 279 (8): 7091–7. doi:10.1074/jbc.M311973200. ISSN 0021-9258. PMID 14645221. 
  6. ^ Hogenesch, J B; Gu Y Z, Jain S, Bradfield C A (May. 1998). "The basic-helix-loop-helix-PAS orphan MOP3 forms transcriptionally active complexes with circadian and hypoxia factors". Proc. Natl. Acad. Sci. U.S.A. (UNITED STATES) 95 (10): 5474–9. doi:10.1073/pnas.95.10.5474. ISSN 0027-8424. PMID 9576906. 

Further reading

External links


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


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