10         20         30         40         50         60
         |          |          |          |          |          |
MADQRMDISS TISDFMSPGP TDLLSGSLGT SGVDCNRKRK GSATDYQLDD FAFEESMDTD - 60
KDDPHGRLEY AEHQGRIKNA REAHSQIEKR RRDKMNSFID ELASLVPTCN AMSRKLDKLT - 120
VLRMAVQHMK TLRGATNPYT EANYKPTFLS DDELKHLILR AADGFLFVVG CDRGKILFVS - 180
ESVFKILNYS QNDLIGQSLF DYLHPKDIAK VKEQLSSSDT APRERLIDAK TGLPVKTDIT - 240
PGPSRLCSGA RRSFFCRMKC NRPSVKVEDK DFASTCSKKK DRKSFCTIHS TGYLKSWPPT - 300
KMGLDEDNEP DNEGCNLSCL VAIGRLHSHM VPQPANGEIR VKSMEYVSRH AIDGKFVFVD - 360
QRATAILAYL PQELLGTSCY EYFHQDDIGH LAECHRQVLQ TREKITTNCY KFKIKDGSFI - 420
TLRSRWFSFM NPWTKEVEYI VSTNTVVLAN VLEGGDPTFP QLTAPPHSMD SMLPSGEGGP - 480
KRTHPTVPGI PGGTRAGAGK IGRMIAEEIM EIHRIRGSSP SSCGSSPLNI TSTPPPDASS - 540
PGGKKILNGG TPDIPSTGLL PGQAQETPGY PYSDSSSILG ENPHIGIDMI DNDQGSSSPS - 600
NDEAAMAVIM SLLEADAGLG GPVDFSDLPW PL

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 (By similarity). Part of a nuclear complex which also includes GNB2L1/RACK1 and PRKCA; GNB2L1 and PRKCA are recruited to the complex in a circadian manner. Interacts with CRY2. O08785:Clock; NbExp=18; IntAct=EBI-644534, EBI-79859; P97784:Cry1; NbExp=10; IntAct=EBI-644534, EBI-1266607; Q99JJ1:Cry2; NbExp=4; IntAct=EBI-644534, EBI-1794634; Q9R194:Cry2; NbExp=5; IntAct=EBI-644534, EBI-1266619; P11103:Parp1; NbExp=7; IntAct=EBI-644534, EBI-642213; O54943:Per2; NbExp=8; IntAct=EBI-644534, EBI-1266779;


Subcellular Location: Nucleus. Event=Alternative splicing; Named isoforms=5; Name=1; Synonyms=b'; IsoId=Q9WTL8-1; Sequence=Displayed; Name=2; Synonyms=b; IsoId=Q9WTL8-2; Sequence=VSP_007992; Name=3; IsoId=Q9WTL8-3; Sequence=VSP_007993, VSP_007994; Name=4; IsoId=Q9WTL8-4; Sequence=VSP_007992, VSP_007994; Name=5; Synonyms=g'; IsoId=Q9WTL8-5; Sequence=VSP_007992, VSP_007995, VSP_007996;
PTM: Acetylated on Lys-544 upon dimerization with CLOCK. Acetylation facilitates CRY1- mediated repression.
PTM: Phosphorylated upon dimerization with CLOCK.
PTM: Sumoylated on Lys-266 upon dimerization with CLOCK.
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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Characterization of disorder is found on an alternatively spliced product of canonical Aryl hydrocarbon receptor nuclear translocator-like protein 1 (BMAL1), designated by UniProt as Isoform 4 (DP00735_A004).