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Gene Ontology Classifications
aryl hydrocarbon receptor nuclear translocator-like

Go Annotations as Summary Text (Tabular View) (GO Graph)

GO curators for mouse genes have assigned the following annotations to the gene product of Arntl. (This text reflects annotations as of Tuesday, May 26, 2015.)
Summary from NCBI RefSeq

The protein encoded by this gene is a basic helix-loop-helix protein that forms a heterodimer with Clock. This heterodimer binds E-box enhancer elements upstream of Period (Per1, Per2, Per3) and Cryptochrome (Cry1, Cry2) genes and activates transcription of these genes. Per and Cry proteins heterodimerize and repress their own transcription by interacting in a feedback loop with Clock/Arntl complexes. Defects in this gene have been linked to infertility, problems with gluconeogenesis and lipogenesis, and altered sleep patterns. Two transcript variants encoding different isoforms have been found for this gene. [provided by RefSeq, Jan 2014]
Summary text based on GO annotations supported by experimental evidence in mouse
Summary text based on GO annotations supported by experimental evidence in other organisms
Summary text based on GO annotations supported by structural data
Summary text for additional MGI annotations
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  10. Devos J et al. (2011) Magel2, a Prader-Willi syndrome candidate gene, modulates the activities of circadian rhythm proteins in cultured cells. J Circadian Rhythms, 9:12. (PubMed:22208286)
  11. DiTacchio L et al. (2011) Histone lysine demethylase JARID1a activates CLOCK-BMAL1 and influences the circadian clock. Science, 333:1881-5. (PubMed:21960634)
  12. Doi R et al. (2010) CLOCK regulates circadian rhythms of hepatic glycogen synthesis through transcriptional activation of Gys2. J Biol Chem, 285:22114-21. (PubMed:20430893)
  13. Dudley CA et al. (2003) Altered patterns of sleep and behavioral adaptability in NPAS2-deficient mice. Science, 301:379-83. (PubMed:12843397)
  14. Duffield GE et al. (2009) A role for Id2 in regulating photic entrainment of the mammalian circadian system. Curr Biol, 19:297-304. (PubMed:19217292)
  15. Duong HA et al. (2011) A molecular mechanism for circadian clock negative feedback. Science, 332:1436-9. (PubMed:21680841)
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  17. Goriki A et al. (2014) A novel protein, CHRONO, functions as a core component of the mammalian circadian clock. PLoS Biol, 12:e1001839. (PubMed:24736997)
  18. Guo B et al. (2012) The clock gene, brain and muscle Arnt-like 1, regulates adipogenesis via Wnt signaling pathway. FASEB J, 26:3453-63. (PubMed:22611086)
  19. Hamaguchi H et al. (2004) Expression of the gene for Dec2, a basic helix-loop-helix transcription factor, is regulated by a molecular clock system. Biochem J, 382:43-50. (PubMed:15147242)
  20. Han DH et al. (2014) Modulation of glucocorticoid receptor induction properties by core circadian clock proteins. Mol Cell Endocrinol, 383:170-80. (PubMed:24378737)
  21. Honma S et al. (2002) Dec1 and Dec2 are regulators of the mammalian molecular clock. Nature, 419:841-4. (PubMed:12397359)
  22. Huang N et al. (2012) Crystal structure of the heterodimeric CLOCK:BMAL1 transcriptional activator complex. Science, 337:189-94. (PubMed:22653727)
  23. Hwang CK et al. (2013) Circadian rhythm of contrast sensitivity is regulated by a dopamine-neuronal PAS-domain protein 2-adenylyl cyclase 1 signaling pathway in retinal ganglion cells. J Neurosci, 33:14989-97. (PubMed:24048828)
  24. Itoh R et al. (2013) Imaging of heme/hemeproteins in nucleus of the living cells expressing heme-binding nuclear receptors. FEBS Lett, 587:2131-6. (PubMed:23735699)
  25. Katada S et al. (2010) The histone methyltransferase MLL1 permits the oscillation of circadian gene expression. Nat Struct Mol Biol, 17:1414-21. (PubMed:21113167)
  26. Kawamoto T et al. (2004) A novel autofeedback loop of Dec1 transcription involved in circadian rhythm regulation. Biochem Biophys Res Commun, 313:117-24. (PubMed:14672706)
  27. Khapre RV et al. (2011) Circadian clock protein BMAL1 regulates cellular senescence in vivo. Cell Cycle, 10:4162-9. (PubMed:22101268)
  28. Khapre RV et al. (2014) BMAL1-dependent regulation of the mTOR signaling pathway delays aging. Aging (Albany NY), 6:48-57. (PubMed:24481314)
  29. Kojima S et al. (2007) LARK activates posttranscriptional expression of an essential mammalian clock protein, PERIOD1. Proc Natl Acad Sci U S A, 104:1859-64. (PubMed:17264215)
  30. Kondratov RV et al. (2003) BMAL1-dependent circadian oscillation of nuclear CLOCK: posttranslational events induced by dimerization of transcriptional activators of the mammalian clock system. Genes Dev, 17:1921-32. (PubMed:12897057)
  31. Koyanagi S et al. (2011) cAMP-response element (CRE)-mediated transcription by activating transcription factor-4 (ATF4) is essential for circadian expression of the Period2 gene. J Biol Chem, 286:32416-23. (PubMed:21768648)
  32. Lande-Diner L et al. (2013) A positive feedback loop links circadian clock factor CLOCK-BMAL1 to the basic transcriptional machinery. Proc Natl Acad Sci U S A, 110:16021-16026. (PubMed:24043798)
  33. Langmesser S et al. (2008) Interaction of circadian clock proteins PER2 and CRY with BMAL1 and CLOCK. BMC Mol Biol, 9:41. (PubMed:18430226)
  34. Lee J et al. (2008) Dual modification of BMAL1 by SUMO2/3 and ubiquitin promotes circadian activation of the CLOCK/BMAL1 complex. Mol Cell Biol, 28:6056-65. (PubMed:18644859)
  35. Li DQ et al. (2013) Metastasis-associated protein 1 is an integral component of the circadian molecular machinery. Nat Commun, 4:2545. (PubMed:24089055)
  36. Li MD et al. (2013) O-GlcNAc signaling entrains the circadian clock by inhibiting BMAL1/CLOCK ubiquitination. Cell Metab, 17:303-10. (PubMed:23395176)
  37. Li Y et al. (2004) DNA binding, but not interaction with Bmal1, is responsible for DEC1-mediated transcription regulation of the circadian gene mPer1. Biochem J, 382:895-904. (PubMed:15193144)
  38. Marcheva B et al. (2010) Disruption of the clock components CLOCK and BMAL1 leads to hypoinsulinaemia and diabetes. Nature, 466:627-31. (PubMed:20562852)
  39. Miki T et al. (2013) p53 regulates Period2 expression and the circadian clock. Nat Commun, 4:2444. (PubMed:24051492)
  40. Nader N et al. (2009) Circadian rhythm transcription factor CLOCK regulates the transcriptional activity of the glucocorticoid receptor by acetylating its hinge region lysine cluster: potential physiological implications. FASEB J, 23:1572-83. (PubMed:19141540)
  41. Nakahata Y et al. (2008) The NAD+-dependent deacetylase SIRT1 modulates CLOCK-mediated chromatin remodeling and circadian control. Cell, 134:329-40. (PubMed:18662547)
  42. Ozber N et al. (2010) Identification of two amino acids in the C-terminal domain of mouse CRY2 essential for PER2 interaction. BMC Mol Biol, 11:69. (PubMed:20840750)
  43. Peruquetti RL et al. (2012) Circadian proteins CLOCK and BMAL1 in the chromatoid body, a RNA processing granule of male germ cells. PLoS One, 7:e42695. (PubMed:22900038)
  44. Preitner N et al. (2002) The orphan nuclear receptor REV-ERBalpha controls circadian transcription within the positive limb of the mammalian circadian oscillator. Cell, 110:251-60. (PubMed:12150932)
  45. Ramsey KM et al. (2009) Circadian clock feedback cycle through NAMPT-mediated NAD+ biosynthesis. Science, 324:651-4. (PubMed:19299583)
  46. Richards J et al. (2013) A role for the circadian clock protein Per1 in the regulation of aldosterone levels and renal Na+ retention. Am J Physiol Renal Physiol, 305:F1697-704. (PubMed:24154698)
  47. Sasaki M et al. (2009) Preferential inhibition of BMAL2-CLOCK activity by PER2 reemphasizes its negative role and a positive role of BMAL2 in the circadian transcription. J Biol Chem, 284:25149-59. (PubMed:19605937)
  48. Sato F et al. (2004) Functional analysis of the basic helix-loop-helix transcription factor DEC1 in circadian regulation. Interaction with BMAL1. Eur J Biochem, 271:4409-19. (PubMed:15560782)
  49. Schmutz I et al. (2010) The mammalian clock component PERIOD2 coordinates circadian output by interaction with nuclear receptors. Genes Dev, 24:345-57. (PubMed:20159955)
  50. Shim HS et al. (2007) Rapid activation of CLOCK by Ca2+-dependent protein kinase C mediates resetting of the mammalian circadian clock. EMBO Rep, 8:366-71. (PubMed:17347670)
  51. Stashi E et al. (2014) SRC-2 is an essential coactivator for orchestrating metabolism and circadian rhythm. Cell Rep, 6:633-45. (PubMed:24529706)
  52. Takahata S et al. (1998) Transcriptionally active heterodimer formation of an Arnt-like PAS protein, Arnt3, with HIF-1a, HLF, and clock. Biochem Biophys Res Commun, 248:789-94. (PubMed:9704006)
  53. Wallach T et al. (2013) Dynamic circadian protein-protein interaction networks predict temporal organization of cellular functions. PLoS Genet, 9:e1003398. (PubMed:23555304)
  54. Ward SM et al. (2010) The transcriptional repressor ID2 can interact with the canonical clock components CLOCK and BMAL1 and mediate inhibitory effects on mPer1 expression. J Biol Chem, 285:38987-9000. (PubMed:20861012)
  55. Xu CX et al. (2010) Disruption of CLOCK-BMAL1 transcriptional activity is responsible for aryl hydrocarbon receptor-mediated regulation of Period1 gene. Toxicol Sci, 115:98-108. (PubMed:20106950)
  56. Ye R et al. (2011) Biochemical analysis of the canonical model for the mammalian circadian clock. J Biol Chem, 286:25891-902. (PubMed:21613214)
  57. Yoshii K et al. (2013) Effects of NAD(P)H and its derivatives on the DNA-binding activity of NPAS2, a mammalian circadian transcription factor. Biochem Biophys Res Commun, 437:386-91. (PubMed:23831463)
  58. Yoshitane H et al. (2012) JNK regulates the photic response of the mammalian circadian clock. EMBO Rep, 13:455-61. (PubMed:22441692)
  59. Yujnovsky I et al. (2006) Signaling mediated by the dopamine D2 receptor potentiates circadian regulation by CLOCK:BMAL1. Proc Natl Acad Sci U S A, 103:6386-91. (PubMed:16606840)
  60. Zhang L et al. (2012) PKCgamma participates in food entrainment by regulating BMAL1. Proc Natl Acad Sci U S A, 109:20679-84. (PubMed:23185022)

Go Annotations in Tabular Form (Text View) (GO Graph)

Filter Markers by: Category  Evidence Code 


Gene Ontology Evidence Code Abbreviations:

  EXP Inferred from experiment
  IAS Inferred from ancestral sequence
  IBA Inferred from biological aspect of ancestor
  IBD Inferred from biological aspect of descendant
  IC Inferred by curator
  IDA Inferred from direct assay
  IEA Inferred from electronic annotation
  IGI Inferred from genetic interaction
  IKR Inferred from key residues
  IMP Inferred from mutant phenotype
  IMR Inferred from missing residues
  IPI Inferred from physical interaction
  IRD Inferred from rapid divergence
  ISS Inferred from sequence or structural similarity
  ISO Inferred from sequence orthology
  ISA Inferred from sequence alignment
  ISM Inferred from sequence model
  NAS Non-traceable author statement
  ND No biological data available
  RCA Reviewed computational analysis
  TAS Traceable author statement


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