[1]
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NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA], AND ALTERNATIVE SPLICING (ISOFORMS BMAL1A; BMAL1B; BMAL1C; BMAL1D; BMAL1E AND BMAL1F).
TISSUE=Brain;
DOI=10.1006/bbrc.1997.6371; PubMed=9144434 [NCBI, ExPASy, EBI, Israel, Japan]
Ikeda M.,
Nomura M.;
"cDNA cloning and tissue-specific expression of a novel basic helix-loop-helix/PAS protein (BMAL1) and identification of alternatively spliced variants with alternative translation initiation site usage.";
Biochem. Biophys. Res. Commun. 233:258-264(1997).
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[2]
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NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM MOP3), AND INTERACTION WITH HSP90 AND AHR.
TISSUE=Fetal brain;
DOI=10.1074/jbc.272.13.8581; PubMed=9079689 [NCBI, ExPASy, EBI, Israel, Japan]
Hogenesch J.B.,
Chan W.K.,
Jackiw V.H.,
Brown R.C.,
Gu Y.-Z.,
Pray-Grant M.,
Perdew G.H.,
Bradfield C.A.;
"Characterization of a subset of the basic-helix-loop-helix-PAS superfamily that interacts with components of the dioxin signaling pathway.";
J. Biol. Chem. 272:8581-8593(1997).
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[3]
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NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM BMAL1B).
Tian H.,
Russell D.W.,
McKnight S.L.;
"JAP3: a novel ARNT-like bHLH-PAS protein.";
Submitted (DEC-1996) to the EMBL/GenBank/DDBJ databases.
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[4]
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NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM BMAL1B).
DOI=10.1073/pnas.95.10.5474; PubMed=9576906 [NCBI, ExPASy, EBI, Israel, Japan]
Hogenesch J.B.,
Gu Y.Z.,
Jain S.,
Bradfield C.A.;
"The basic-helix-loop-helix-PAS orphan MOP3 forms transcriptionally active complexes with circadian and hypoxia factors.";
Proc. Natl. Acad. Sci. U.S.A. 95:5474-5479(1998).
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[5]
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NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Mural R.J.,
Istrail S.,
Sutton G.G.,
Florea L.,
Halpern A.L.,
Mobarry C.M.,
Lippert R.,
Walenz B.,
Shatkay H.,
Dew I.,
Miller J.R.,
Flanigan M.J.,
Edwards N.J.,
Bolanos R.,
Fasulo D.,
Halldorsson B.V.,
Hannenhalli S.,
Turner R.,
Yooseph S., ![]()
Lu F.,
Nusskern D.R.,
Shue B.C.,
Zheng X.H.,
Zhong F.,
Delcher A.L.,
Huson D.H.,
Kravitz S.A.,
Mouchard L.,
Reinert K.,
Remington K.A.,
Clark A.G.,
Waterman M.S.,
Eichler E.E.,
Adams M.D.,
Hunkapiller M.W.,
Myers E.W.,
Venter J.C.;
Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
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[6]
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NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 8).
TISSUE=Brain;
DOI=10.1101/gr.2596504; PubMed=15489334 [NCBI, ExPASy, EBI, Israel, Japan]
The MGC Project Team;
"The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC).";
Genome Res. 14:2121-2127(2004).
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[7]
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INTERACTION WITH CLOCK.
DOI=10.1126/science.280.5369.1564; PubMed=9616112 [NCBI, ExPASy, EBI, Israel, Japan]
Gekakis N.,
Staknis D.,
Nguyen H.B.,
Davis F.C.,
Wilsbacher L.D.,
King D.P.,
Takahashi J.S.,
Weitz C.J.;
"Role of the CLOCK protein in the mammalian circadian mechanism.";
Science 280:1564-1569(1998).
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[8]
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MUTAGENESIS OF SER-9; SER-10; ALA-611 AND GLY-612.
DOI=10.1038/ng1745; PubMed=16474406 [NCBI, ExPASy, EBI, Israel, Japan]
Sato T.K.,
Yamada R.G.,
Ukai H.,
Baggs J.E.,
Miraglia L.J.,
Kobayashi T.J.,
Welsh D.K.,
Kay S.A.,
Ueda H.R.,
Hogenesch J.B.;
"Feedback repression is required for mammalian circadian clock function.";
Nat. Genet. 38:312-319(2006).
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- FUNCTION: ARNTL-CLOCK heterodimers activate E-box element (3'-CACGTG-5') transcription of a number of proteins of the circadian clock. This transcription is inhibited in a feedback loop by PER, and also by CRY proteins (By similarity).
- SUBUNIT: Component of the circadian clock oscillator which includes the CRY proteins, CLOCK or NPAS2, ARNTL or ARNTL2, CSNK1D and/or CSNK1E, TIMELESS and the PER proteins. Efficient DNA binding requires dimerization with another bHLH protein. Heterodimerization with CLOCK is required for E-box-dependent transactivation, for CLOCK nuclear translocation and degradation, and, for phosphorylation of both CLOCK and ARNTL. Interaction with PER and CRY proteins requires translocation to the nucleus. Interaction of the CLOCK-ARNTL heterodimer with PER or CRY inhibits transcription activation. Interacts with HSP90; with AHR in vitro, but not in vivo.
- SUBCELLULAR LOCATION: Nucleus (By similarity).
- ALTERNATIVE PRODUCTS:
8 named isoforms [FASTA] produced by alternative splicing. Additional isoforms seem to exist.
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| Name | BMAL1A |
| Isoform ID | O00327-1 |
| Features which should be applied to build the isoform sequence: VSP_002094. |
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| Name | BMAL1D |
| Isoform ID | O00327-4 |
| Features which should be applied to build the isoform sequence: VSP_002098. |
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| Name | MOP3 |
| Isoform ID | O00327-7 |
| Features which should be applied to build the isoform sequence: VSP_002095. |
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| Name | 8 |
| Isoform ID | O00327-8 |
| Features which should be applied to build the isoform sequence: VSP_035457. |
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- TISSUE SPECIFICITY: Highly expressed in the adult brain, skeletal muscle and heart.
- PTM: Acetylated on Lys-538 upon dimerization with CLOCK. Acetylation facilitates CRY1-mediated repression (By similarity).
- PTM: Phosphorylated upon dimerization with CLOCK (By similarity).
- PTM: Sumoylated on Lys-259 upon dimerization with CLOCK (By similarity).
- MISCELLANEOUS: CLOCK-ARNTL double mutations within the PAS domains result in syngernistic desensitization to high levels of CRY on repression of CLOCK-ARNTL transcriptional activity of PER1 and, disrupt circadian rhythmicity.
- SIMILARITY: Contains 1 basic helix-loop-helix (bHLH) domain.
- SIMILARITY: Contains 1 PAC (PAS-associated C-terminal) domain.
- SIMILARITY: Contains 2 PAS (PER-ARNT-SIM) domains.
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