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Aryl hydrocarbon receptor nuclear translocator-like protein 1 (Basic-helix-loop-helix-PAS protein MOP3) (Brain and muscle ARNT-like 1) (Class E basic helix-loop-helix protein 5) (bHLHe5) (Member of PAS protein 3) (PAS domain-containing protein 3) (bHLH-PAS protein JAP3)

 BMAL1_HUMAN             Reviewed;         626 AA.
O00327; A2I2N6; A8K645; B5ME11; B7WPG7; D3DQW6; O00313; O00314;
O00315; O00316; O00317; Q4G136; Q8IUT4; Q99631; Q99649;
15-DEC-1998, integrated into UniProtKB/Swiss-Prot.
15-AUG-2003, sequence version 2.
22-NOV-2017, entry version 183.
RecName: Full=Aryl hydrocarbon receptor nuclear translocator-like protein 1;
AltName: Full=Basic-helix-loop-helix-PAS protein MOP3;
AltName: Full=Brain and muscle ARNT-like 1;
AltName: Full=Class E basic helix-loop-helix protein 5;
Short=bHLHe5;
AltName: Full=Member of PAS protein 3;
AltName: Full=PAS domain-containing protein 3;
AltName: Full=bHLH-PAS protein JAP3;
Name=ARNTL; Synonyms=BHLHE5, BMAL1, MOP3, PASD3;
Homo sapiens (Human).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
Catarrhini; Hominidae; Homo.
NCBI_TaxID=9606;
[1]
NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA], AND ALTERNATIVE SPLICING
(ISOFORMS BMAL1A; BMAL1B; BMAL1C; BMAL1D; BMAL1E AND BMAL1F).
TISSUE=Brain;
PubMed=9144434; DOI=10.1006/bbrc.1997.6371;
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).
[2]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM MOP3), AND INTERACTION WITH HSP90
AND AHR.
TISSUE=Fetal brain;
PubMed=9079689; DOI=10.1074/jbc.272.13.8581;
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).
[3]
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.
[4]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM BMAL1B).
PubMed=9576906; DOI=10.1073/pnas.95.10.5474;
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).
[5]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS BMAL1B AND 9).
TISSUE=Brain;
PubMed=14702039; DOI=10.1038/ng1285;
Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A.,
Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M.,
Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y.,
Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M.,
Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K.,
Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S.,
Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J.,
Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y.,
Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N.,
Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S.,
Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y.,
Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T.,
Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y.,
Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S.,
Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T.,
Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M.,
Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T.,
Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K.,
Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R.,
Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.;
"Complete sequencing and characterization of 21,243 full-length human
cDNAs.";
Nat. Genet. 36:40-45(2004).
[6]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
Kripke D.F., Klimecki W.;
"ARNTL resequence.";
Submitted (SEP-2006) to the EMBL/GenBank/DDBJ databases.
[7]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
PubMed=16554811; DOI=10.1038/nature04632;
Taylor T.D., Noguchi H., Totoki Y., Toyoda A., Kuroki Y., Dewar K.,
Lloyd C., Itoh T., Takeda T., Kim D.-W., She X., Barlow K.F.,
Bloom T., Bruford E., Chang J.L., Cuomo C.A., Eichler E.,
FitzGerald M.G., Jaffe D.B., LaButti K., Nicol R., Park H.-S.,
Seaman C., Sougnez C., Yang X., Zimmer A.R., Zody M.C., Birren B.W.,
Nusbaum C., Fujiyama A., Hattori M., Rogers J., Lander E.S.,
Sakaki Y.;
"Human chromosome 11 DNA sequence and analysis including novel gene
identification.";
Nature 440:497-500(2006).
[8]
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.
[9]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 8 AND BMAL1A).
TISSUE=Brain, and Skin;
PubMed=15489334; DOI=10.1101/gr.2596504;
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).
[10]
INTERACTION WITH CLOCK.
PubMed=9616112; DOI=10.1126/science.280.5369.1564;
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).
[11]
FUNCTION, DNA-BINDING, AND ENZYME REGULATION.
PubMed=11441146; DOI=10.1126/science.1060698;
Rutter J., Reick M., Wu L.C., McKnight S.L.;
"Regulation of clock and NPAS2 DNA binding by the redox state of NAD
cofactors.";
Science 293:510-514(2001).
[12]
FUNCTION.
PubMed=12738229; DOI=10.1016/S0022-2828(03)00051-8;
Schoenhard J.A., Smith L.H., Painter C.A., Eren M., Johnson C.H.,
Vaughan D.E.;
"Regulation of the PAI-1 promoter by circadian clock components:
differential activation by BMAL1 and BMAL2.";
J. Mol. Cell. Cardiol. 35:473-481(2003).
[13]
INTERACTION WITH KAT2B AND EP300.
PubMed=14645221; DOI=10.1074/jbc.M311973200;
Curtis A.M., Seo S.B., Westgate E.J., Rudic R.D., Smyth E.M.,
Chakravarti D., FitzGerald G.A., McNamara P.;
"Histone acetyltransferase-dependent chromatin remodeling and the
vascular clock.";
J. Biol. Chem. 279:7091-7097(2004).
[14]
MUTAGENESIS OF SER-9; SER-10; ALA-611 AND GLY-612.
PubMed=16474406; DOI=10.1038/ng1745;
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).
[15]
FUNCTION.
PubMed=18587630; DOI=10.1007/s11010-008-9846-x;
Li R., Yue J., Zhang Y., Zhou L., Hao W., Yuan J., Qiang B.,
Ding J.M., Peng X., Cao J.M.;
"CLOCK/BMAL1 regulates human nocturnin transcription through binding
to the E-box of nocturnin promoter.";
Mol. Cell. Biochem. 317:169-177(2008).
[16]
INTERACTION WITH KDM5A.
PubMed=21960634; DOI=10.1126/science.1206022;
DiTacchio L., Le H.D., Vollmers C., Hatori M., Witcher M., Secombe J.,
Panda S.;
"Histone lysine demethylase JARID1a activates CLOCK-BMAL1 and
influences the circadian clock.";
Science 333:1881-1885(2011).
[17]
REVIEW.
PubMed=23576606; DOI=10.1152/ajpregu.00066.2013;
Richards J., Gumz M.L.;
"Mechanism of the circadian clock in physiology.";
Am. J. Physiol. 304:R1053-R1064(2013).
[18]
FUNCTION.
PubMed=23955654; DOI=10.1007/s00403-013-1403-0;
Watabe Y., Tomioka M., Watabe A., Aihara M., Shimba S., Inoue H.;
"The clock gene brain and muscle Arnt-like protein-1 (BMAL1) is
involved in hair growth.";
Arch. Dermatol. Res. 305:755-761(2013).
[19]
FUNCTION.
PubMed=23785138; DOI=10.1523/JNEUROSCI.2757-12.2013;
Baeza-Raja B., Eckel-Mahan K., Zhang L., Vagena E., Tsigelny I.F.,
Sassone-Corsi P., Ptacek L.J., Akassoglou K.;
"p75 neurotrophin receptor is a clock gene that regulates oscillatory
components of circadian and metabolic networks.";
J. Neurosci. 33:10221-10234(2013).
[20]
REVIEW.
PubMed=23303907; DOI=10.1152/physrev.00016.2012;
Eckel-Mahan K., Sassone-Corsi P.;
"Metabolism and the circadian clock converge.";
Physiol. Rev. 93:107-135(2013).
[21]
INTERACTION WITH CIART.
PubMed=24385426; DOI=10.1074/jbc.M113.534651;
Annayev Y., Adar S., Chiou Y.Y., Lieb J., Sancar A., Ye R.;
"Gene model 129 (Gm129) encodes a novel transcriptional repressor that
modulates circadian gene expression.";
J. Biol. Chem. 289:5013-5024(2014).
[22]
FUNCTION IN HAIR GROWTH, SUBCELLULAR LOCATION, AND TISSUE SPECIFICITY.
PubMed=24005054; DOI=10.1038/jid.2013.366;
Al-Nuaimi Y., Hardman J.A., Biro T., Haslam I.S., Philpott M.P.,
Toth B.I., Farjo N., Farjo B., Baier G., Watson R.E., Grimaldi B.,
Kloepper J.E., Paus R.;
"A meeting of two chronobiological systems: circadian proteins Period1
and BMAL1 modulate the human hair cycle clock.";
J. Invest. Dermatol. 134:610-619(2014).
[23]
INTERACTION WITH UBE3A.
PubMed=24728990; DOI=10.1093/nar/gku225;
Gossan N.C., Zhang F., Guo B., Jin D., Yoshitane H., Yao A.,
Glossop N., Zhang Y.Q., Fukada Y., Meng Q.J.;
"The E3 ubiquitin ligase UBE3A is an integral component of the
molecular circadian clock through regulating the BMAL1 transcription
factor.";
Nucleic Acids Res. 42:5765-5775(2014).
[24]
REVIEW.
PubMed=23916625; DOI=10.1016/j.tcb.2013.07.002;
Partch C.L., Green C.B., Takahashi J.S.;
"Molecular architecture of the mammalian circadian clock.";
Trends Cell Biol. 24:90-99(2014).
[25]
INTERACTION WITH PASD1.
PubMed=25936801; DOI=10.1016/j.molcel.2015.03.031;
Michael A.K., Harvey S.L., Sammons P.J., Anderson A.P., Kopalle H.M.,
Banham A.H., Partch C.L.;
"Cancer/testis antigen PASD1 silences the circadian clock.";
Mol. Cell 58:743-754(2015).
[26]
SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-259, AND IDENTIFICATION BY
MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=28112733; DOI=10.1038/nsmb.3366;
Hendriks I.A., Lyon D., Young C., Jensen L.J., Vertegaal A.C.,
Nielsen M.L.;
"Site-specific mapping of the human SUMO proteome reveals co-
modification with phosphorylation.";
Nat. Struct. Mol. Biol. 24:325-336(2017).
[27]
X-RAY CRYSTALLOGRAPHY (2.40 ANGSTROMS) OF 66-128 IN COMPLEX WITH CLOCK
AND DNA, FUNCTION, ENZYME REGULATION, SUBUNIT, PHOSPHORYLATION AT
SER-78, AND MUTAGENESIS OF SER-78; MET-88; SER-90 AND LEU-125.
PubMed=23229515; DOI=10.1038/cr.2012.170;
Wang Z., Wu Y., Li L., Su X.D.;
"Intermolecular recognition revealed by the complex structure of human
CLOCK-BMAL1 basic helix-loop-helix domains with E-box DNA.";
Cell Res. 23:213-224(2013).
-!- FUNCTION: Transcriptional activator which forms a core component
of the circadian clock. The circadian clock, an internal time-
keeping system, regulates various physiological processes through
the generation of approximately 24 hour circadian rhythms in gene
expression, which are translated into rhythms in metabolism and
behavior. It is derived from the Latin roots 'circa' (about) and
'diem' (day) and acts as an important regulator of a wide array of
physiological functions including metabolism, sleep, body
temperature, blood pressure, endocrine, immune, cardiovascular,
and renal function. Consists of two major components: the central
clock, residing in the suprachiasmatic nucleus (SCN) of the brain,
and the peripheral clocks that are present in nearly every tissue
and organ system. Both the central and peripheral clocks can be
reset by environmental cues, also known as Zeitgebers (German for
'timegivers'). The predominant Zeitgeber for the central clock is
light, which is sensed by retina and signals directly to the SCN.
The central clock entrains the peripheral clocks through neuronal
and hormonal signals, body temperature and feeding-related cues,
aligning all clocks with the external light/dark cycle. Circadian
rhythms allow an organism to achieve temporal homeostasis with its
environment at the molecular level by regulating gene expression
to create a peak of protein expression once every 24 hours to
control when a particular physiological process is most active
with respect to the solar day. Transcription and translation of
core clock components (CLOCK, NPAS2, ARNTL/BMAL1, ARNTL2/BMAL2,
PER1, PER2, PER3, CRY1 and CRY2) plays a critical role in rhythm
generation, whereas delays imposed by post-translational
modifications (PTMs) are important for determining the period
(tau) of the rhythms (tau refers to the period of a rhythm and is
the length, in time, of one complete cycle). A diurnal rhythm is
synchronized with the day/night cycle, while the ultradian and
infradian rhythms have a period shorter and longer than 24 hours,
respectively. Disruptions in the circadian rhythms contribute to
the pathology of cardiovascular diseases, cancer, metabolic
syndromes and aging. A transcription/translation feedback loop
(TTFL) forms the core of the molecular circadian clock mechanism.
Transcription factors, CLOCK or NPAS2 and ARNTL/BMAL1 or
ARNTL2/BMAL2, form the positive limb of the feedback loop, act in
the form of a heterodimer and activate the transcription of core
clock genes and clock-controlled genes (involved in key metabolic
processes), harboring E-box elements (5'-CACGTG-3') within their
promoters. The core clock genes: PER1/2/3 and CRY1/2 which are
transcriptional repressors form the negative limb of the feedback
loop and interact with the CLOCK|NPAS2-ARNTL/BMAL1|ARNTL2/BMAL2
heterodimer inhibiting its activity and thereby negatively
regulating their own expression. This heterodimer also activates
nuclear receptors NR1D1/2 and RORA/B/G, which form a second
feedback loop and which activate and repress ARNTL/BMAL1
transcription, respectively. ARNTL/BMAL1 positively regulates
myogenesis and negatively regulates adipogenesis via the
transcriptional control of the genes of the canonical Wnt
signaling pathway. Plays a role in normal pancreatic beta-cell
function; regulates glucose-stimulated insulin secretion via the
regulation of antioxidant genes NFE2L2/NRF2 and its targets SESN2,
PRDX3, CCLC and CCLM. Negatively regulates the mTORC1 signaling
pathway; regulates the expression of MTOR and DEPTOR. Controls
diurnal oscillations of Ly6C inflammatory monocytes; rhythmic
recruitment of the PRC2 complex imparts diurnal variation to
chemokine expression that is necessary to sustain Ly6C monocyte
rhythms. Regulates the expression of HSD3B2, STAR, PTGS2, CYP11A1,
CYP19A1 and LHCGR in the ovary and also the genes involved in hair
growth. Plays an important role in adult hippocampal neurogenesis
by regulating the timely entry of neural stem/progenitor cells
(NSPCs) into the cell cycle and the number of cell divisions that
take place prior to cell-cycle exit. Regulates the circadian
expression of CIART and KLF11. The CLOCK-ARNTL/BMAL1 heterodimer
regulates the circadian expression of SERPINE1/PAI1, VWF, B3,
CCRN4L/NOC, NAMPT, DBP, MYOD1, PPARGC1A, PPARGC1B, SIRT1, GYS2,
F7, NGFR, GNRHR, BHLHE40/DEC1, ATF4, MTA1, KLF10 and also genes
implicated in glucose and lipid metabolism. Represses
glucocorticoid receptor NR3C1/GR-induced transcriptional activity
by reducing the association of NR3C1/GR to glucocorticoid response
elements (GREs) via the acetylation of multiple lysine residues
located in its hinge region. Promotes rhythmic chromatin opening,
regulating the DNA accessibility of other transcription factors.
The NPAS2-ARNTL/BMAL1 heterodimer positively regulates the
expression of MAOA, F7 and LDHA and modulates the circadian rhythm
of daytime contrast sensitivity by regulating the rhythmic
expression of adenylate cyclase type 1 (ADCY1) in the retina. The
preferred binding motif for the CLOCK-ARNTL/BMAL1 heterodimer is
5'-CACGTGA-3', which contains a flanking Ala residue in addition
to the canonical 6-nucleotide E-box sequence (PubMed:23229515).
CLOCK specifically binds to the half-site 5'-CAC-3', while ARNTL
binds to the half-site 5'-GTGA-3' (PubMed:23229515). The CLOCK-
ARNTL/BMAL1 heterodimer also recognizes the non-canonical E-box
motifs 5'-AACGTGA-3' and 5'-CATGTGA-3' (PubMed:23229515).
{ECO:0000269|PubMed:11441146, ECO:0000269|PubMed:12738229,
ECO:0000269|PubMed:18587630, ECO:0000269|PubMed:23785138,
ECO:0000269|PubMed:23955654, ECO:0000269|PubMed:24005054}.
-!- ENZYME REGULATION: There is conflicting data about the effect of
NAD cofactors on activity. PubMed:11441146 suggests that the redox
state of the cell can modulate the transcriptional activity of the
CLOCK-ARNTL/BMAL1 heterodimer; NADH and NADPH enhance the DNA-
binding activity of the heterodimer. PubMed:23229515 reports that
NADH and NADPH have no significant effect on DNA-binding activity
of the CLOCK-ARNTL/BMAL1 heterodimer.
{ECO:0000269|PubMed:11441146, ECO:0000269|PubMed:23229515}.
-!- SUBUNIT: Component of the circadian clock oscillator which
includes the CRY1/2 proteins, CLOCK or NPAS2, ARNTL/BMAL1 or
ARNTL2/BMAL2, CSNK1D and/or CSNK1E, TIMELESS and the PER1/2/3
proteins (By similarity). Forms a heterodimer with CLOCK
(PubMed:9616112, PubMed:23229515). The CLOCK-ARNTL/BMAL1
heterodimer is required for E-box-dependent transactivation, for
CLOCK nuclear translocation and degradation, and, for
phosphorylation of both CLOCK and ARNTL/BMAL1 (By similarity).
Part of a nuclear complex which also includes RACK1 and PRKCA;
RACK1 and PRKCA are recruited to the complex in a circadian manner
(By similarity). Interacts with NPAS2 (By similarity). Interacts
with EZH2 (By similarity). Interacts with SUMO3 (By similarity).
Interacts with SIRT1 (By similarity). Interacts with AHR
(PubMed:9079689). Interacts with ID1, ID2 and ID3 (By similarity).
Interacts with DDX4 (By similarity). Interacts with OGT (By
similarity). Interacts with EED and SUZ12 (By similarity).
Interacts with MTA1 (By similarity). Interacts with CIART
(PubMed:24385426). Interacts with HSP90 (PubMed:9079689).
Interacts with KAT2B and EP300 (PubMed:14645221). Interacts with
BHLHE40/DEC1 and BHLHE41/DEC2 (By similarity). Interacts with RELB
and the interaction is enhanced in the presence of CLOCK (By
similarity). Interacts with PER1, PER2, CRY1 and CRY2 and this
interaction requires a translocation to the nucleus (By
similarity). Interaction of the CLOCK-ARNTL/BMAL1 heterodimer with
PER or CRY inhibits transcription activation (By similarity).
Interaction of the CLOCK-ARNTL/BMAL1 with CRY1 is independent of
DNA but with PER2 is off DNA (By similarity). The CLOCK-
ARNTL/BMAL1 heterodimer interacts with GSK3B (By similarity).
Interacts with KDM5A (PubMed:21960634). Interacts with KMT2A in a
circadian manner (By similarity). Interacts with UBE3A
(PubMed:24728990). Interacts with PRKCG (By similarity). Interacts
with MAGEL2 (By similarity). Interacts with NCOA2 (By similarity).
Interacts with THRAP3 (By similarity). The CLOCK-ARNTL/BMAL1
heterodimer interacts with PASD1 (PubMed:25936801). Interacts with
PASD1 (PubMed:25936801). {ECO:0000250|UniProtKB:Q9WTL8,
ECO:0000269|PubMed:14645221, ECO:0000269|PubMed:21960634,
ECO:0000269|PubMed:23229515, ECO:0000269|PubMed:24385426,
ECO:0000269|PubMed:24728990, ECO:0000269|PubMed:25936801,
ECO:0000269|PubMed:9079689, ECO:0000269|PubMed:9616112}.
-!- INTERACTION:
O15516:CLOCK; NbExp=4; IntAct=EBI-11991546, EBI-1794265;
D0VY79:HIF1A; NbExp=3; IntAct=EBI-1794206, EBI-10179332;
Q99743:NPAS2; NbExp=4; IntAct=EBI-11991546, EBI-3932727;
-!- SUBCELLULAR LOCATION: Nucleus {ECO:0000255|PROSITE-
ProRule:PRU00981, ECO:0000269|PubMed:24005054}. Cytoplasm
{ECO:0000250|UniProtKB:Q9WTL8}. Nucleus, PML body
{ECO:0000250|UniProtKB:Q9WTL8}. Note=Shuttles between the nucleus
and the cytoplasm and this nucleocytoplasmic shuttling is
essential for the nuclear accumulation of CLOCK, target gene
transcription and the degradation of the CLOCK-ARNTL/BMAL1
heterodimer. The sumoylated form localizes in the PML body.
Sequestered to the cytoplasm in the presence of ID2.
{ECO:0000250|UniProtKB:Q9WTL8}.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=9;
Comment=Additional isoforms seem to exist.;
Name=BMAL1B; Synonyms=JAP3;
IsoId=O00327-2; Sequence=Displayed;
Name=BMAL1A;
IsoId=O00327-1; Sequence=VSP_002094;
Name=BMAL1C;
IsoId=O00327-3; Sequence=VSP_002096, VSP_002097;
Name=BMAL1D;
IsoId=O00327-4; Sequence=VSP_002098;
Name=BMAL1E;
IsoId=O00327-5; Sequence=VSP_002099, VSP_002100;
Name=BMAL1F;
IsoId=O00327-6; Sequence=VSP_002101, VSP_002102;
Name=MOP3;
IsoId=O00327-7; Sequence=VSP_002095;
Name=8;
IsoId=O00327-8; Sequence=VSP_035457;
Name=9;
IsoId=O00327-9; Sequence=VSP_002094, VSP_035457;
-!- TISSUE SPECIFICITY: Hair follicles (at protein level). Highly
expressed in the adult brain, skeletal muscle and heart.
{ECO:0000269|PubMed:24005054}.
-!- PTM: Ubiquitinated, leading to its proteasomal degradation.
{ECO:0000250|UniProtKB:Q9WTL8}.
-!- PTM: O-glycosylated; contains O-GlcNAc. O-glycosylation by OGT
prevents protein degradation by inhibiting ubiquitination. It also
stabilizes the CLOCK-ARNTL/BMAL1 heterodimer thereby increasing
CLOCK-ARNTL/BMAL1-mediated transcription of genes in the negative
loop of the circadian clock such as PER1/2/3 and CRY1/2.
{ECO:0000250|UniProtKB:Q9WTL8}.
-!- PTM: Acetylated on Lys-538 upon dimerization with CLOCK.
Acetylation facilitates CRY1-mediated repression. Deacetylated by
SIRT1, which may result in decreased protein stability.
{ECO:0000250|UniProtKB:Q9WTL8}.
-!- PTM: Phosphorylated upon dimerization with CLOCK. Phosphorylation
enhances the transcriptional activity, alters the subcellular
localization and decreases the stability of the CLOCK-ARNTL/BMAL1
heterodimer by promoting its degradation. Phosphorylation shows
circadian variations in the liver with a peak between CT10 to
CT14. Phosphorylation at Ser-90 by CK2 is essential for its
nuclear localization, its interaction with CLOCK and controls
CLOCK nuclear entry (By similarity). Dephosphorylation at Ser-78
is important for dimerization with CLOCK and transcriptional
activity (PubMed:23229515). {ECO:0000250|UniProtKB:Q9WTL8,
ECO:0000269|PubMed:23229515}.
-!- PTM: Sumoylated on Lys-259 upon dimerization with CLOCK.
Predominantly conjugated to poly-SUMO2/3 rather than SUMO1 and the
level of these conjugates undergo rhythmic variation, peaking at
CT9-CT12. Sumoylation localizes it exclusively to the PML body and
promotes its ubiquitination in the PML body, ubiquitin-dependent
proteasomal degradation and the transcriptional activity of the
CLOCK-ARNTL/BMAL1 heterodimer. {ECO:0000250|UniProtKB:Q9WTL8}.
-!- MISCELLANEOUS: CLOCK-ARNTL/BMAL1 double mutations within the PAS
domains result in synergistic desensitization to high levels of
CRY on repression of CLOCK-ARNTL/BMAL1 transcriptional activity of
PER1 and, disrupt circadian rhythmicity.
-----------------------------------------------------------------------
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EMBL; D89722; BAA19968.1; -; mRNA.
EMBL; AB000812; BAA19935.1; -; mRNA.
EMBL; AB000813; BAA19936.1; -; Genomic_DNA.
EMBL; AB000814; BAA19937.1; -; mRNA.
EMBL; AB000815; BAA19938.1; -; mRNA.
EMBL; AB000816; BAA19939.1; -; mRNA.
EMBL; U51627; AAC51213.1; -; mRNA.
EMBL; U60415; AAB37248.1; -; mRNA.
EMBL; AF044288; AAC24353.1; -; mRNA.
EMBL; AK095749; BAG53120.1; -; mRNA.
EMBL; AK291510; BAF84199.1; -; mRNA.
EMBL; EF015894; ABM64205.1; -; Genomic_DNA.
EMBL; AC016884; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; AC022878; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; CH471064; EAW68504.1; -; Genomic_DNA.
EMBL; CH471064; EAW68505.1; -; Genomic_DNA.
EMBL; CH471064; EAW68510.1; -; Genomic_DNA.
EMBL; CH471064; EAW68511.1; -; Genomic_DNA.
EMBL; CH471064; EAW68513.1; -; Genomic_DNA.
EMBL; BC016674; AAH16674.1; -; mRNA.
EMBL; BC031214; AAH31214.1; -; mRNA.
EMBL; BC041129; AAH41129.2; -; mRNA.
CCDS; CCDS31430.1; -. [O00327-8]
CCDS; CCDS44543.1; -. [O00327-9]
CCDS; CCDS73259.1; -. [O00327-2]
CCDS; CCDS76387.1; -. [O00327-1]
PIR; JC5405; JC5405.
PIR; JC5407; JC5407.
PIR; PC4288; PC4288.
PIR; PC4289; PC4289.
RefSeq; NP_001025443.1; NM_001030272.2. [O00327-8]
RefSeq; NP_001025444.1; NM_001030273.2. [O00327-9]
RefSeq; NP_001169.3; NM_001178.5. [O00327-8]
RefSeq; NP_001284648.1; NM_001297719.1. [O00327-2]
RefSeq; NP_001284651.1; NM_001297722.1. [O00327-2]
RefSeq; NP_001284653.1; NM_001297724.1. [O00327-1]
RefSeq; XP_011518414.1; XM_011520112.2.
RefSeq; XP_011518415.1; XM_011520113.1.
RefSeq; XP_016873231.1; XM_017017742.1.
RefSeq; XP_016873232.1; XM_017017743.1.
RefSeq; XP_016873235.1; XM_017017746.1.
RefSeq; XP_016873236.1; XM_017017747.1.
RefSeq; XP_016873237.1; XM_017017748.1. [O00327-9]
UniGene; Hs.65734; -.
PDB; 4H10; X-ray; 2.40 A; A=66-128.
PDBsum; 4H10; -.
ProteinModelPortal; O00327; -.
SMR; O00327; -.
BioGrid; 106899; 61.
DIP; DIP-46008N; -.
IntAct; O00327; 13.
STRING; 9606.ENSP00000374357; -.
iPTMnet; O00327; -.
PhosphoSitePlus; O00327; -.
BioMuta; ARNTL; -.
PaxDb; O00327; -.
PeptideAtlas; O00327; -.
PRIDE; O00327; -.
DNASU; 406; -.
Ensembl; ENST00000389707; ENSP00000374357; ENSG00000133794. [O00327-8]
Ensembl; ENST00000401424; ENSP00000385915; ENSG00000133794. [O00327-1]
Ensembl; ENST00000403290; ENSP00000384517; ENSG00000133794. [O00327-2]
Ensembl; ENST00000403482; ENSP00000385897; ENSG00000133794. [O00327-7]
Ensembl; ENST00000403510; ENSP00000385581; ENSG00000133794. [O00327-9]
GeneID; 406; -.
KEGG; hsa:406; -.
UCSC; uc001mko.4; human. [O00327-2]
CTD; 406; -.
DisGeNET; 406; -.
EuPathDB; HostDB:ENSG00000133794.17; -.
GeneCards; ARNTL; -.
HGNC; HGNC:701; ARNTL.
HPA; CAB045962; -.
HPA; HPA050938; -.
MIM; 602550; gene.
neXtProt; NX_O00327; -.
OpenTargets; ENSG00000133794; -.
PharmGKB; PA24996; -.
eggNOG; KOG3561; Eukaryota.
eggNOG; ENOG410XRJI; LUCA.
GeneTree; ENSGT00760000118788; -.
HOGENOM; HOG000234379; -.
HOVERGEN; HBG107503; -.
InParanoid; O00327; -.
KO; K02296; -.
OMA; EKINTNC; -.
OrthoDB; EOG091G126J; -.
PhylomeDB; O00327; -.
TreeFam; TF319983; -.
Reactome; R-HSA-1368082; RORA activates gene expression.
Reactome; R-HSA-1368108; BMAL1:CLOCK,NPAS2 activates circadian gene expression.
Reactome; R-HSA-1989781; PPARA activates gene expression.
Reactome; R-HSA-400253; Circadian Clock.
SIGNOR; O00327; -.
ChiTaRS; ARNTL; human.
GeneWiki; ARNTL; -.
GenomeRNAi; 406; -.
PRO; PR:O00327; -.
Proteomes; UP000005640; Chromosome 11.
Bgee; ENSG00000133794; -.
ExpressionAtlas; O00327; baseline and differential.
Genevisible; O00327; HS.
GO; GO:0033391; C:chromatoid body; ISS:UniProtKB.
GO; GO:0043231; C:intracellular membrane-bounded organelle; IDA:HPA.
GO; GO:0005654; C:nucleoplasm; IDA:HPA.
GO; GO:0005634; C:nucleus; IDA:UniProtKB.
GO; GO:0016605; C:PML body; IEA:UniProtKB-SubCell.
GO; GO:0005667; C:transcription factor complex; IPI:MGI.
GO; GO:0017162; F:aryl hydrocarbon receptor binding; IPI:BHF-UCL.
GO; GO:0043425; F:bHLH transcription factor binding; IEA:Ensembl.
GO; GO:0001047; F:core promoter binding; ISS:UniProtKB.
GO; GO:0001046; F:core promoter sequence-specific DNA binding; IEA:Ensembl.
GO; GO:0003677; F:DNA binding; IDA:UniProtKB.
GO; GO:0070888; F:E-box binding; IDA:UniProtKB.
GO; GO:0051879; F:Hsp90 protein binding; IDA:BHF-UCL.
GO; GO:0046982; F:protein heterodimerization activity; IEA:Ensembl.
GO; GO:0070491; F:repressing transcription factor binding; IPI:UniProtKB.
GO; GO:0043565; F:sequence-specific DNA binding; ISS:UniProtKB.
GO; GO:0000982; F:transcription factor activity, RNA polymerase II core promoter proximal region sequence-specific binding; ISS:BHF-UCL.
GO; GO:0000976; F:transcription regulatory region sequence-specific DNA binding; ISS:UniProtKB.
GO; GO:0001190; F:transcriptional activator activity, RNA polymerase II transcription factor binding; IEA:Ensembl.
GO; GO:0032922; P:circadian regulation of gene expression; IDA:UniProtKB.
GO; GO:0007623; P:circadian rhythm; TAS:Reactome.
GO; GO:0060137; P:maternal process involved in parturition; IEA:Ensembl.
GO; GO:0045599; P:negative regulation of fat cell differentiation; ISS:UniProtKB.
GO; GO:2000323; P:negative regulation of glucocorticoid receptor signaling pathway; ISS:UniProtKB.
GO; GO:0032007; P:negative regulation of TOR signaling; ISS:UniProtKB.
GO; GO:0045892; P:negative regulation of transcription, DNA-templated; ISS:UniProtKB.
GO; GO:0090403; P:oxidative stress-induced premature senescence; ISS:UniProtKB.
GO; GO:0090263; P:positive regulation of canonical Wnt signaling pathway; ISS:UniProtKB.
GO; GO:0042753; P:positive regulation of circadian rhythm; ISS:UniProtKB.
GO; GO:2001016; P:positive regulation of skeletal muscle cell differentiation; ISS:UniProtKB.
GO; GO:0045944; P:positive regulation of transcription from RNA polymerase II promoter; IDA:BHF-UCL.
GO; GO:0045893; P:positive regulation of transcription, DNA-templated; IDA:UniProtKB.
GO; GO:0043161; P:proteasome-mediated ubiquitin-dependent protein catabolic process; ISS:UniProtKB.
GO; GO:0000060; P:protein import into nucleus, translocation; IEA:Ensembl.
GO; GO:0051726; P:regulation of cell cycle; ISS:UniProtKB.
GO; GO:2000772; P:regulation of cellular senescence; ISS:UniProtKB.
GO; GO:0042634; P:regulation of hair cycle; IMP:UniProtKB.
GO; GO:0050796; P:regulation of insulin secretion; ISS:UniProtKB.
GO; GO:0050767; P:regulation of neurogenesis; ISS:UniProtKB.
GO; GO:0042176; P:regulation of protein catabolic process; IEA:Ensembl.
GO; GO:0006355; P:regulation of transcription, DNA-templated; ISS:UniProtKB.
GO; GO:2000074; P:regulation of type B pancreatic cell development; ISS:UniProtKB.
GO; GO:0051775; P:response to redox state; IDA:UniProtKB.
GO; GO:0007283; P:spermatogenesis; ISS:UniProtKB.
CDD; cd00083; HLH; 1.
CDD; cd00130; PAS; 2.
Gene3D; 4.10.280.10; -; 1.
InterPro; IPR011598; bHLH_dom.
InterPro; IPR036638; HLH_DNA-bd_sf.
InterPro; IPR001067; Nuc_translocat.
InterPro; IPR001610; PAC.
InterPro; IPR000014; PAS.
InterPro; IPR035965; PAS-like_dom_sf.
InterPro; IPR013767; PAS_fold.
Pfam; PF00010; HLH; 1.
Pfam; PF00989; PAS; 1.
PRINTS; PR00785; NCTRNSLOCATR.
SMART; SM00353; HLH; 1.
SMART; SM00086; PAC; 1.
SMART; SM00091; PAS; 2.
SUPFAM; SSF47459; SSF47459; 1.
SUPFAM; SSF55785; SSF55785; 3.
TIGRFAMs; TIGR00229; sensory_box; 1.
PROSITE; PS50888; BHLH; 1.
PROSITE; PS50112; PAS; 2.
1: Evidence at protein level;
3D-structure; Acetylation; Activator; Alternative splicing;
Biological rhythms; Complete proteome; Cytoplasm; DNA-binding;
Isopeptide bond; Nucleus; Phosphoprotein; Reference proteome; Repeat;
Transcription; Transcription regulation; Ubl conjugation.
CHAIN 1 626 Aryl hydrocarbon receptor nuclear
translocator-like protein 1.
/FTId=PRO_0000127156.
DOMAIN 72 125 bHLH. {ECO:0000255|PROSITE-
ProRule:PRU00981}.
DOMAIN 143 215 PAS 1. {ECO:0000255|PROSITE-
ProRule:PRU00140}.
DOMAIN 326 396 PAS 2. {ECO:0000255|PROSITE-
ProRule:PRU00140}.
DOMAIN 401 444 PAC.
REGION 508 588 Interaction with CIART.
{ECO:0000250|UniProtKB:Q9WTL8}.
MOTIF 36 41 Nuclear localization signal.
{ECO:0000250|UniProtKB:Q9WTL8}.
MOTIF 142 152 Nuclear export signal 1.
{ECO:0000250|UniProtKB:Q9WTL8}.
MOTIF 361 369 Nuclear export signal 2.
{ECO:0000250|UniProtKB:Q9WTL8}.
SITE 77 77 Interaction with E-box DNA.
{ECO:0000269|PubMed:23229515}.
SITE 80 80 Interaction with E-box DNA.
{ECO:0000269|PubMed:23229515}.
SITE 81 81 Interaction with E-box DNA.
{ECO:0000269|PubMed:23229515}.
SITE 85 85 Interaction with E-box DNA.
{ECO:0000269|PubMed:23229515}.
SITE 125 125 Important for interaction with CLOCK.
{ECO:0000269|PubMed:23229515}.
MOD_RES 17 17 Phosphoserine; by GSK3-beta.
{ECO:0000250|UniProtKB:Q9WTL8}.
MOD_RES 21 21 Phosphothreonine; by GSK3-beta.
{ECO:0000250|UniProtKB:Q9WTL8}.
MOD_RES 78 78 Phosphoserine.
{ECO:0000305|PubMed:23229515}.
MOD_RES 90 90 Phosphoserine; by CK2.
{ECO:0000250|UniProtKB:Q9WTL8}.
MOD_RES 538 538 N6-acetyllysine.
{ECO:0000250|UniProtKB:Q9WTL8}.
CROSSLNK 252 252 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in SUMO2 and
SUMO3). {ECO:0000250|UniProtKB:Q9WTL8}.
CROSSLNK 259 259 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in SUMO2).
{ECO:0000244|PubMed:28112733}.
VAR_SEQ 1 59 MADQRMDISSTISDFMSPGPTDLLSSSLGTSGVDCNRKRKG
SSTDYQESMDTDKDDPHG -> MSKEAVSLWALTVSLQPPV
PLCVCREMTGSGRRKQQCVTLPFISRELCFYLLLFPPP
(in isoform MOP3).
{ECO:0000303|PubMed:9079689}.
/FTId=VSP_002095.
VAR_SEQ 1 47 MADQRMDISSTISDFMSPGPTDLLSSSLGTSGVDCNRKRKG
SSTDYQ -> MINI (in isoform BMAL1A and
isoform 9). {ECO:0000303|PubMed:14702039,
ECO:0000303|PubMed:15489334}.
/FTId=VSP_002094.
VAR_SEQ 224 224 T -> R (in isoform BMAL1C).
{ECO:0000305}.
/FTId=VSP_002096.
VAR_SEQ 225 626 Missing (in isoform BMAL1C).
{ECO:0000305}.
/FTId=VSP_002097.
VAR_SEQ 274 391 Missing (in isoform BMAL1D).
{ECO:0000305}.
/FTId=VSP_002098.
VAR_SEQ 274 274 Missing (in isoform 8 and isoform 9).
{ECO:0000303|PubMed:14702039,
ECO:0000303|PubMed:15489334}.
/FTId=VSP_035457.
VAR_SEQ 278 301 SFCTIHSTGYLKSWPPTKMGLDED -> AFCTIHSTGYFGI
FTTRTSRHIVL (in isoform BMAL1E).
{ECO:0000305}.
/FTId=VSP_002099.
VAR_SEQ 302 626 Missing (in isoform BMAL1E).
{ECO:0000305}.
/FTId=VSP_002100.
VAR_SEQ 443 526 ANVLEGGDPTFPQLTASPHSMDSMLPSGEGGPKRTHPTVPG
IPGGTRAGAGKIGRMIAEEIMEIHRIRGSSPSSCGSSPLNI
TS -> SRVDTGHLGQVERCTVLSRPNSRFLIAGMFTEPTS
WKAGTQPSHSSQHPPTAWTACCPLEKVAQRGPTPLFQGFQG
EPGLGQEK (in isoform BMAL1F).
{ECO:0000305}.
/FTId=VSP_002101.
VAR_SEQ 527 626 Missing (in isoform BMAL1F).
{ECO:0000305}.
/FTId=VSP_002102.
MUTAGEN 9 9 S->A,E: Enhanced PER1 reporter activity
by CLOCK-ARNTL/BMAL1.
{ECO:0000269|PubMed:16474406}.
MUTAGEN 9 9 S->F: 2-2.5-fold increase in CLOCK-BMAL1
transcriptional activity in the absence
of CRY1. No change in repression activity
in the presence of CRY1.
{ECO:0000269|PubMed:16474406}.
MUTAGEN 10 10 S->A,E: Enhanced PER1 reporter activity
by CLOCK-ARNTL/BMAL1.
{ECO:0000269|PubMed:16474406}.
MUTAGEN 10 10 S->L: 2-2.5-fold increase in CLOCK-
ARNTL/BMAL1 transcriptional activity in
the absence of CRY1. No change in
repression activity in the presence of
CRY1. {ECO:0000269|PubMed:16474406}.
MUTAGEN 78 78 S->E: Phosphomimetic mutant which
severely impairs DNA binding and CLOCK-
ARNTL/BMAL1 transcriptional activity.
{ECO:0000269|PubMed:23229515}.
MUTAGEN 88 88 M->F: No effect on CLOCK binding.
{ECO:0000269|PubMed:23229515}.
MUTAGEN 90 90 S->E: Phosphomimetic mutant with no
effect on DNA binding or CLOCK-
ARNTL/BMAL1 transcriptional activity.
{ECO:0000269|PubMed:23229515}.
MUTAGEN 125 125 L->H: Impaired CLOCK binding.
{ECO:0000269|PubMed:23229515}.
MUTAGEN 611 611 A->S,T: Increased desensitization to
CRY1, in the presence of CLOCK.
Approximately 2-fold increase in CLOCK-
ARNTL/BMAL1 transcriptional activity in
the absence of CRY1; when associated with
E-407. {ECO:0000269|PubMed:16474406}.
MUTAGEN 612 612 G->E: Increased desensitization to CRY1,
in the presence of CLOCK. Approximately
2-fold increase in CLOCK-ARNTL/BMAL1
transcriptional activity in the absence
of CRY1. {ECO:0000269|PubMed:16474406}.
CONFLICT 69 69 R -> G (in Ref. 2; AAC51213).
{ECO:0000305}.
CONFLICT 123 123 K -> R (in Ref. 1; BAA19935).
{ECO:0000305}.
CONFLICT 173 173 S -> P (in Ref. 1; BAA19939).
{ECO:0000305}.
CONFLICT 259 259 K -> N (in Ref. 1; BAA19938).
{ECO:0000305}.
CONFLICT 264 264 D -> N (in Ref. 1; BAA19938).
{ECO:0000305}.
CONFLICT 418 418 S -> N (in Ref. 1; BAA19937).
{ECO:0000305}.
CONFLICT 513 514 SP -> LR (in Ref. 2; AAC51213).
{ECO:0000305}.
HELIX 71 98 {ECO:0000244|PDB:4H10}.
HELIX 100 103 {ECO:0000244|PDB:4H10}.
HELIX 111 125 {ECO:0000244|PDB:4H10}.
SEQUENCE 626 AA; 68762 MW; 820F0E07DC6265A6 CRC64;
MADQRMDISS TISDFMSPGP TDLLSSSLGT SGVDCNRKRK GSSTDYQESM DTDKDDPHGR
LEYTEHQGRI KNAREAHSQI EKRRRDKMNS FIDELASLVP TCNAMSRKLD KLTVLRMAVQ
HMKTLRGATN PYTEANYKPT FLSDDELKHL ILRAADGFLF VVGCDRGKIL FVSESVFKIL
NYSQNDLIGQ SLFDYLHPKD IAKVKEQLSS SDTAPRERLI DAKTGLPVKT DITPGPSRLC
SGARRSFFCR MKCNRPSVKV EDKDFPSTCS KKKADRKSFC TIHSTGYLKS WPPTKMGLDE
DNEPDNEGCN LSCLVAIGRL HSHVVPQPVN GEIRVKSMEY VSRHAIDGKF VFVDQRATAI
LAYLPQELLG TSCYEYFHQD DIGHLAECHR QVLQTREKIT TNCYKFKIKD GSFITLRSRW
FSFMNPWTKE VEYIVSTNTV VLANVLEGGD PTFPQLTASP HSMDSMLPSG EGGPKRTHPT
VPGIPGGTRA GAGKIGRMIA EEIMEIHRIR GSSPSSCGSS PLNITSTPPP DASSPGGKKI
LNGGTPDIPS SGLLSGQAQE NPGYPYSDSS SILGENPHIG IDMIDNDQGS SSPSNDEAAM
AVIMSLLEAD AGLGGPVDFS DLPWPL


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EIAAB27615 Basic-helix-loop-helix-PAS protein MOP4,bHLHe9,BHLHE9,Class E basic helix-loop-helix protein 9,Homo sapiens,Human,Member of PAS protein 4,MOP4,Neuronal PAS domain-containing protein 2,Neuronal PAS2,NP
EIAAB27612 Basic-helix-loop-helix-PAS protein MOP5,bHLHe11,BHLHE11,Class E basic helix-loop-helix protein 11,Homo sapiens,Human,Member of PAS protein 5,MOP5,Neuronal PAS domain-containing protein 1,Neuronal PAS1
EIAAB27618 Basic-helix-loop-helix-PAS protein MOP6,bHLHe12,BHLHE12,Class E basic helix-loop-helix protein 12,Homo sapiens,Human,Member of PAS protein 6,MOP6,Neuronal PAS domain-containing protein 3,Neuronal PAS3
E0255h ELISA kit ATH1,ATOH1,bHLHa14,BHLHA14,Class A basic helix-loop-helix protein 14,hATH1,Helix-loop-helix protein hATH-1,Homo sapiens,Human,Protein atonal homolog 1 96T
E0255h ELISA ATH1,ATOH1,bHLHa14,BHLHA14,Class A basic helix-loop-helix protein 14,hATH1,Helix-loop-helix protein hATH-1,Homo sapiens,Human,Protein atonal homolog 1 96T
U0255h CLIA ATH1,ATOH1,bHLHa14,BHLHA14,Class A basic helix-loop-helix protein 14,hATH1,Helix-loop-helix protein hATH-1,Homo sapiens,Human,Protein atonal homolog 1 96T
EIAAB14718 Basic helix-loop-helix protein N-twist,bHLHa31,BHLHA31,Class A basic helix-loop-helix protein 31,Fer3-like protein,FERD3L,Homo sapiens,Human,NATO3,Nephew of atonal 3,Neuronal twist,NTWIST
EIAAB28826 bHLHb1,BHLHB1,bHLHe19,BHLHE19,Class B basic helix-loop-helix protein 1,Class E basic helix-loop-helix protein 19,Homo sapiens,Human,OLIG2,Oligo2,Oligodendrocyte transcription factor 2,PRKCBP2,Protein
27-482 MYCN is a member of the MYC family and encodes a protein with a basic helix-loop-helix (bHLH) domain. It is located in the nucleus and must dimerize with another bHLH protein in order to bind DNA. Amp 0.1 mg
EIAAB28828 bHLHb7,BHLHB7,bHLHe20,BHLHE20,Class B basic helix-loop-helix protein 7,Class E basic helix-loop-helix protein 20,Homo sapiens,Human,OLIG3,Oligo3,Oligodendrocyte transcription factor 3


 

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