BHE40_MOUSE - PTM Information in dbPTM

Basic Information of Protein

• UniProt ID: BHE40_MOUSE
• UniProt AC: O35185
• Protein Name: Class E basic helix-loop-helix protein 40
• Gene Name: Bhlhe40
• Organism: Mus musculus (Mouse).
• Sequence Length: 411
• Subcellular Localization: Cytoplasm . Nucleus . Predominantly localized in the nucleus (By similarity).
• 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 PER1/2 and in turn is repressed by PER1/2 and CRY1/2. Represses the activity of the circadian transcriptional activator: CLOCK-ARNTL/BMAL1|ARNTL2/BMAL2 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 and NR1H3/LXRA transactivation activity. May function as a transcriptional factor for neuronal differentiation..
• Protein Sequence: MERIPSAQPPPTCLPKAPGLEHGDLSGMDFAHMYQVYKSRRGIKRSEDSKETYKLPHRLIEKKRRDRINECIAQLKDLLPEHLKLTTLGHLEKAVVLELTLKHVKALTNLIDQQQQKIIALQSGLQAGDLSGRNLEAGQEMFCSGFQTCAREVLQYLAKHENTRDLKSSQLVTHLHRVVSELLQGGASRKPLDSAPKAVDLKEKPSFLAKGSEGPGKNCVPVIQRTFAPSGGEQSGSDTDTDSGYGGELEKGDLRSEQPYFKSDHGRRFAVGERVSTIKQESEEPPTKKSRMQLSEEEGHFAGSDLMGSPFLGPHPHQPPFCLPFYLIPPSATAYLPMLEKCWYPTSVPVLYPGLNTSAAALSSFMNPDKIPTPLLLPQRLPSPLAHSSLDSSALLQALKQIPPLNLETKD

Overview of Protein Modification Sites with Functional and Structural Information

Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations	Modification	Substrate Peptides & Secondary Structure	ASA (%)	Reference
194	Phosphorylation	ASRKPLDSAPKAVDL CCCCCCCCCCCCCCC	54.90	28066266
235	Phosphorylation	APSGGEQSGSDTDTD CCCCCCCCCCCCCCC	35.64	30482847
237	Phosphorylation	SGGEQSGSDTDTDSG CCCCCCCCCCCCCCC	42.45	30482847
239	Phosphorylation	GEQSGSDTDTDSGYG CCCCCCCCCCCCCCC	42.36	23608596
282	Phosphorylation	VSTIKQESEEPPTKK HHCHHHCCCCCCCHH	44.78	19367708
383	Phosphorylation	LLPQRLPSPLAHSSL CCCCCCCCCCCCCCC	36.82	26824392
388	Phosphorylation	LPSPLAHSSLDSSAL CCCCCCCCCCCHHHH	27.30	23984901
389	Phosphorylation	PSPLAHSSLDSSALL CCCCCCCCCCHHHHH	26.74	23984901
392	Phosphorylation	LAHSSLDSSALLQAL CCCCCCCHHHHHHHH	23.86	23984901

Upstream regulatory proteins (kinases for phosphorylation sites, E3 ubiquitin ligases of ubiquitination sites, ...)

Oops, there are no upstream regulatory protein records of BHE40_MOUSE !!

Functions of PTM Sites

Oops, there are no descriptions of PTM sites of BHE40_MOUSE !!

Disease-associated PTM Sites based on SAP

* Distance = the distance between SAP position and PTM sites.

Oops, there are no SNP-PTM records of BHE40_MOUSE !!

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference
BHE40_MOUSE	Bhlhe40	physical	20211142
CEBPB_MOUSE	Cebpb	physical	22610404
HDAC1_MOUSE	Hdac1	physical	22610404

Drug and Disease Associations

• Kegg Drug
• DrugBank
• There are no disease associations of PTM sites.

Related Literatures of Post-Translational Modification

Phosphorylation

"Large scale localization of protein phosphorylation by use ofelectron capture dissociation mass spectrometry.";
Sweet S.M., Bailey C.M., Cunningham D.L., Heath J.K., Cooper H.J.;
Mol. Cell. Proteomics 8:904-912(2009).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-383, AND MASSSPECTROMETRY.
PubMed: 19131326