UniProt ID | BHE41_MOUSE | |
---|---|---|
UniProt AC | Q99PV5 | |
Protein Name | Class E basic helix-loop-helix protein 41 | |
Gene Name | Bhlhe41 | |
Organism | Mus musculus (Mouse). | |
Sequence Length | 410 | |
Subcellular Localization | Nucleus . | |
Protein Description | Transcriptional repressor involved in the regulation of the circadian rhythm by negatively regulating the activity of the clock genes and clock-controlled genes. Acts as the negative limb of a novel autoregulatory feedback loop (DEC loop) which differs from the one formed by the PER and CRY transcriptional repressors (PER/CRY loop). Both these loops are interlocked as it represses the expression of PER1 and in turn is repressed by PER1/2 and CRY1/2. Represses the activity of the circadian transcriptional activator: CLOCK-ARNTL/BMAL1 heterodimer by competing for the binding to E-box elements (5'-CACGTG-3') found within the promoters of its target genes. Negatively regulates its own expression and the expression of DBP and BHLHE41/DEC2. Acts as a corepressor of RXR and the RXR-LXR heterodimers and represses the ligand-induced RXRA/B/G, NR1H3/LXRA, NR1H4 and VDR transactivation activity.. | |
Protein Sequence | MDEGIPHLQERQLLEHRDFIGLDYSSLYMCKPKRSLKRDDTKDTYKLPHRLIEKKRRDRINECIAQLKDLLPEHLKLTTLGHLEKAVVLELTLKHLKALTALTEQQHQKIIALQNGERSLKSPVQADLDAFHSGFQTCAKEVLQYLARFESWTPREPRCAQLVSHLHAVATQLLTPQVPSGRGSGRAPCSAGAAAASGPERVARCVPVIQRTQPGTEPEHDTDTDSGYGGEAEQGRAAVKQEPPGDSSPAPKRPKLEARGALLGPEPALLGSLVALGGGAPFAQPAAAPFCLPFYLLSPSAAAYVQPWLDKSGLDKYLYPAAAAPFPLLYPGIPAAAAAAAAAAFPCLSSVLSPPPEKAGATAGAPFLAHEVAPPGPLRPQHAHSRTHLPRAVNPESSQEDATQPAKDAP | |
Overview of Protein Modification Sites with Functional and Structural Information | ||
* ASA = Accessible Surface Area
Locations | Modification | Substrate Peptides & Secondary Structure |
ASA (%) | Reference | Orthologous Protein Cluster |
---|---|---|---|---|---|
119 | Phosphorylation | ALQNGERSLKSPVQA CCCCCCCCCCCCCHH | 35.53 | 24719451 | |
121 | Acetylation | QNGERSLKSPVQADL CCCCCCCCCCCHHCH | 54.69 | 7718667 | |
122 | Phosphorylation | NGERSLKSPVQADLD CCCCCCCCCCHHCHH | 35.28 | 25521595 | |
140 | Acetylation | SGFQTCAKEVLQYLA HHHHHHHHHHHHHHH | 50.97 | 7718679 | |
164 | Phosphorylation | PRCAQLVSHLHAVAT HHHHHHHHHHHHHHH | 28.99 | 22817900 | |
171 | Phosphorylation | SHLHAVATQLLTPQV HHHHHHHHHHHCCCC | 17.10 | 22817900 | |
175 | Phosphorylation | AVATQLLTPQVPSGR HHHHHHHCCCCCCCC | 21.92 | 22817900 | |
212 | Phosphorylation | CVPVIQRTQPGTEPE HHEEEEECCCCCCCC | 23.80 | 26643407 | |
216 | Phosphorylation | IQRTQPGTEPEHDTD EEECCCCCCCCCCCC | 55.86 | 26643407 | |
222 | Phosphorylation | GTEPEHDTDTDSGYG CCCCCCCCCCCCCCC | 42.58 | 26643407 | |
224 | Phosphorylation | EPEHDTDTDSGYGGE CCCCCCCCCCCCCCC | 33.87 | 26643407 | |
226 | Phosphorylation | EHDTDTDSGYGGEAE CCCCCCCCCCCCCHH | 35.69 | 26643407 | |
247 | Phosphorylation | KQEPPGDSSPAPKRP CCCCCCCCCCCCCCC | 44.10 | 30635358 | |
248 | Phosphorylation | QEPPGDSSPAPKRPK CCCCCCCCCCCCCCC | 29.80 | 30635358 | |
397 | Phosphorylation | PRAVNPESSQEDATQ CCCCCCCCCCCCCCC | 38.28 | 30635358 | |
398 | Phosphorylation | RAVNPESSQEDATQP CCCCCCCCCCCCCCC | 35.61 | 30635358 |
Modified Location | Modified Residue | Modification | Type of Upstream Proteins | Gene Name of Upstream Proteins | UniProt AC of Upstream Proteins | Sources |
---|---|---|---|---|---|---|
Oops, there are no upstream regulatory protein records of BHE41_MOUSE !! |
Modified Location | Modified Residue | Modification | Function | Reference | ||
---|---|---|---|---|---|---|
Oops, there are no descriptions of PTM sites of BHE41_MOUSE !! |
* Distance = the distance between SAP position and PTM sites.
Modified Location | Modification | Variant Position (Distance <= 10) |
Residue Change | SAP | Related Disease | Reference |
---|---|---|---|---|---|---|
Oops, there are no SNP-PTM records of BHE41_MOUSE !! |
Interacting Protein | Gene Name | Interaction Type | PPI Reference | Domain-Domain Interactions |
---|---|---|---|---|
TFE2_MOUSE | Tcf3 | physical | 12657651 | |
MYOD1_MOUSE | Myod1 | physical | 12657651 |
Kegg Drug | ||||||
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DrugBank | ||||||
There are no disease associations of PTM sites. |
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