| General information | | DisProt: | DP00735_A004 | | Name: | Aryl hydrocarbon receptor nuclear translocator-like protein 1, Isoform 4 | | Synonym(s): | BMAL1_MOUSE
Arnt3
Brain and muscle ARNT-like 1
BMAL1
Q9WTL8-4
| | First appeared in release: | Release 6.01 (10/15/2012) | | UniProt: | Q9WTL8 | | UniGene: | | | SwissProt: | BMAL1_MOUSE | | TrEMBL: | | | NCBI (GI): | | | Source organism: | Mus musculus (Mouse) | | Sequence length: | 626 | | Percent disordered: | 17% | | Homologues: | |
| Native sequence |
10 20 30 40 50 60
| | | | | |
MADQRMDISS TISDFMSPGP TDLLSGSLGT SGVDCNRKRK GSATDYQESM DTDKDDPHGR - 60
LEYAEHQGRI KNAREAHSQI EKRRRDKMNS FIDELASLVP TCNAMSRKLD KLTVLRMAVQ - 120
HMKTLRGATN PYTEANYKPT FLSDDELKHL ILRAADGFLF VVGCDRGKIL FVSESVFKIL - 180
NYSQNDLIGQ SLFDYLHPKD IAKVKEQLSS SDTAPRERLI DAKTGLPVKT DITPGPSRLC - 240
SGARRSFFCR MKCNRPSVKV EDKDFASTCS KKKADRKSFC TIHSTGYLKS WPPTKMGLDE - 300
DNEPDNEGCN LSCLVAIGRL HSHMVPQPAN GEIRVKSMEY VSRHAIDGKF VFVDQRATAI - 360
LAYLPQELLG TSCYEYFHQD DIGHLAECHR QVLQTREKIT TNCYKFKIKD GSFITLRSRW - 420
FSFMNPWTKE VEYIVSTNTV VLANVLEGGD PTFPQLTAPP HSMDSMLPSG EGGPKRTHPT - 480
VPGIPGGTRA GAGKIGRMIA EEIMEIHRIR GSSPSSCGSS PLNITSTPPP DASSPGGKKI - 540
LNGGTPDIPS TGLLPGQAQE TPGYPYSDSS SILGENPHIG IDMIDNDQGS SSPSNDEAAM - 600
AVIMSLLEAD AGLGGPVDFS DLPWPL
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| Functional narrative |
DP00735_A004 is Isoform 4 of Aryl hydrocarbon receptor nuclear translocator-like protein 1.
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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 (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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| Map of ordered and disordered regions |
Note: 'Mouse' over a region to see the start and stop residues. Click on a region to see detailed information.
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| Region 1 | | Type: | Disordered | | Name: | Loop 1 (L1) | | Location: | 127 - 144 | | Length: | 18 | | Region sequence: |
GATNPYTEANYKPTFLSD | | Modification type: | Complex
Fragment
| | PDB: | 4F3L:B | | Structural/functional type: | Function arises from the disordered state
| | Functional classes: | Molecular assembly
| | Functional subclasses: | Protein-protein binding
Flexible linkers/spacers
| Detection methods:
- X-ray crystallography (293 K; pH: 8; CLOCK:BMAL1 protein complex (1:1); Hepes 100 mM; PEG 3350 6 %; NaF 75 mM)
| References:
- Huang N, Chelliah Y, Shan Y, Taylor CA, Yoo SH, Partch C, Green CB, Zhang H, Takahashi JS. "Crystal structure of the heterodimeric CLOCK:BMAL1 transcriptional activator complex." Science. 2012; 337(6091): 189-94. PubMed: 22653727
| Comments:According to Huang et al (2012), Loop 1 of CLOCK participates in intra-protein interaction, but Loop 1 of BMAL1 does not.
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| Region 2 | | Type: | Disordered | | Name: | disorder a | | Location: | 211 - 243 | | Length: | 33 | | Region sequence: |
SDTAPRERLIDAKTGLPVKTDITPGPSRLCSGA | | Modification type: | Complex
Fragment
| | PDB: | 4F3L:B | | Structural/functional type: | Function arises from the disordered state
| | Functional classes: | Molecular assembly
| | Functional subclasses: | Intraprotein interaction
Protein-protein binding
| Detection methods:
- X-ray crystallography (293 K; pH: 8; CLOCK:BMAL1 protein complex (1:1); Hepes 100 mM; NaF 75 mM; PEG 3350 6 %)
| References:
- Huang N, Chelliah Y, Shan Y, Taylor CA, Yoo SH, Partch C, Green CB, Zhang H, Takahashi JS. "Crystal structure of the heterodimeric CLOCK:BMAL1 transcriptional activator complex." Science. 2012; 337(6091): 189-94. PubMed: 22653727
| Comments:
|
| Region 3 | | Type: | Disordered | | Name: | disorder b | | Location: | 254 - 278 | | Length: | 25 | | Region sequence: |
NRPSVKVEDKDFASTCSKKKADRKS | | Modification type: | Complex
Fragment
| | PDB: | 4F3L:B | | Structural/functional type: | Function arises from the disordered state
| | Functional classes: | Molecular assembly
| | Functional subclasses: | Intraprotein interaction
Protein-protein binding
| Detection methods:
- X-ray crystallography (293 K; pH: 8; CLOCK:BMAL1 protein complex (1:1); Hepes 100 mM; NaF 75 mM; PEG 3350 6 %)
| References:
- Huang N, Chelliah Y, Shan Y, Taylor CA, Yoo SH, Partch C, Green CB, Zhang H, Takahashi JS. "Crystal structure of the heterodimeric CLOCK:BMAL1 transcriptional activator complex." Science. 2012; 337(6091): 189-94. PubMed: 22653727
| Comments:
|
| Region 4 | | Type: | Disordered | | Name: | disorder c | | Location: | 292 - 311 | | Length: | 20 | | Region sequence: |
PPTKMGLDEDNEPDNEGCNL | | Modification type: | Complex
Fragment
| | PDB: | 4F3L:B | | Structural/functional type: | Function arises from the disordered state
| | Functional classes: | Molecular assembly
| | Functional subclasses: | Intraprotein interaction
Protein-protein binding
| Detection methods:
- X-ray crystallography (293 K; pH: 8; CLOCK:BMAL1 protein complex (1:1); Hepes 100 mM; NaF 75 mM; PEG 3350 6 %)
| References:
- Huang N, Chelliah Y, Shan Y, Taylor CA, Yoo SH, Partch C, Green CB, Zhang H, Takahashi JS. "Crystal structure of the heterodimeric CLOCK:BMAL1 transcriptional activator complex." Science. 2012; 337(6091): 189-94. PubMed: 22653727
| Comments:
|
| Region 5 | | Type: | Disordered | | Name: | Linker, PAS-A to PAS-B domains | | Location: | 323 - 333 | | Length: | 11 | | Region sequence: |
HMVPQPANGEI | | Modification type: | Complex
Fragment
| | PDB: | 4F3L:B | | Structural/functional type: | Function arises from the disordered state
| | Functional classes: | Molecular assembly
| | Functional subclasses: | Intraprotein interaction
Flexible linkers/spacers
Protein-protein binding
| Detection methods:
- X-ray crystallography (293 K; pH: 8; CLOCK:BMAL1 protein complex (1:1); Hepes 100 mM; NaF 75 mM; PEG 3350 6 %)
| References:
- Huang N, Chelliah Y, Shan Y, Taylor CA, Yoo SH, Partch C, Green CB, Zhang H, Takahashi JS. "Crystal structure of the heterodimeric CLOCK:BMAL1 transcriptional activator complex." Science. 2012; 337(6091): 189-94. PubMed: 22653727
| Comments:According to Huang et al (2012), the PAS-A to PAS-B Domain Linker of CLOCK is well-ordered, but the corresponding linker in BMAL1 is highly flexible.
|
| Comments |
Huang et al (2012) describe the PAS domains of CLOCK and BMAL1 differently than UniProt:
For CLOCK, Huang et al describe PAS-A domain at E95-L257 (encompassing UniProt's PAS 1 domain at N107-S177) and PAS-B at E270-R387 (encompassing UniProt's PAS 2 and PAC domains, F262-G332 and S336-A379 respectively).
For BMAL1, Huang et al describe PAS-A domain at A135-S322 (encompassing UniProt's PAS 1 domain at S150-P222) and PAS-B at R334-T452 (encompassing UniProt's PAS 2 and PAC domains).
AV sent 10/3/2012 (PMID 22653727)
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