NPAS2

NPAS2
Neuronal PAS domain protein 2
Identifiers
Symbols NPAS2; FLJ23138; MGC71151; MOP4; PASD4; bHLHe9
External IDs OMIM603347 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_002518.3 NM_008719.2
RefSeq (protein) NP_002509.2 NP_032745.2
Location (UCSC) Chr 2:
101.44 – 101.61 Mb
Chr 1:
39.25 – 39.42 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. PMC 19579. PMID 9012850. http://www.pubmedcentral.nih.gov/articlerender.fcgi?tool=pmcentrez&artid=19579. 
  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. PMC 20401. PMID 9576906. http://www.pubmedcentral.nih.gov/articlerender.fcgi?tool=pmcentrez&artid=20401. 

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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