BHE41_HUMAN - dbPTM
BHE41_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID BHE41_HUMAN
UniProt AC Q9C0J9
Protein Name Class E basic helix-loop-helix protein 41
Gene Name BHLHE41
Organism Homo sapiens (Human).
Sequence Length 482
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 MDEGIPHLQERQLLEHRDFIGLDYSSLYMCKPKRSMKRDDTKDTYKLPHRLIEKKRRDRINECIAQLKDLLPEHLKLTTLGHLEKAVVLELTLKHLKALTALTEQQHQKIIALQNGERSLKSPIQSDLDAFHSGFQTCAKEVLQYLSRFESWTPREPRCVQLINHLHAVATQFLPTPQLLTQQVPLSKGTGAPSAAGSAAAPCLERAGQKLEPLAYCVPVIQRTQPSAELAAENDTDTDSGYGGEAEARPDREKGKGAGASRVTIKQEPPGEDSPAPKRMKLDSRGGGSGGGPGGGAAAAAAALLGPDPAAAAALLRPDAALLSSLVAFGGGGGAPFPQPAAAAAPFCLPFCFLSPSAAAAYVQPFLDKSGLEKYLYPAAAAAPFPLLYPGIPAPAAAAAAAAAAAAAAAAFPCLSSVLSPPPEKAGAAAATLLPHEVAPLGAPHPQHPHGRTHLPFAGPREPGNPESSAQEDPSQPGKEAP
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 Orthologous
Protein Cluster
31SumoylationYSSLYMCKPKRSMKR
HHHEEEECCCCCCCC
36.7228112733
42AcetylationSMKRDDTKDTYKLPH
CCCCCCCCCCHHHHH
55.8811794097
46AcetylationDDTKDTYKLPHRLIE
CCCCCCHHHHHHHHH
58.6011794109
76UbiquitinationDLLPEHLKLTTLGHL
HHCHHHHHCCCHHHH
45.77-
119PhosphorylationALQNGERSLKSPIQS
CCCCCCCCCCCCCHH
35.5330108239
121SumoylationQNGERSLKSPIQSDL
CCCCCCCCCCCHHHH
56.2728112733
122PhosphorylationNGERSLKSPIQSDLD
CCCCCCCCCCHHHHH
32.3126657352
126PhosphorylationSLKSPIQSDLDAFHS
CCCCCCHHHHHHHHH
40.6430108239
151PhosphorylationQYLSRFESWTPREPR
HHHHCCCCCCCCCHH
33.27-
210SumoylationCLERAGQKLEPLAYC
HHHHCCCCCCCHHHH
54.63-
210SumoylationCLERAGQKLEPLAYC
HHHHCCCCCCCHHHH
54.6328112733
236PhosphorylationELAAENDTDTDSGYG
HHHHCCCCCCCCCCC
52.9924719451
266SumoylationGASRVTIKQEPPGED
CCCCEEEECCCCCCC
38.96-
266SumoylationGASRVTIKQEPPGED
CCCCEEEECCCCCCC
38.9628112733
274PhosphorylationQEPPGEDSPAPKRMK
CCCCCCCCCCCCCCC
20.7528857561
389PhosphorylationAAPFPLLYPGIPAPA
CCCCCCCCCCCCHHH
13.7027251275
416PhosphorylationAAAFPCLSSVLSPPP
HHHCHHHHHHCCCCH
25.7227251275
417PhosphorylationAAFPCLSSVLSPPPE
HHCHHHHHHCCCCHH
17.7127251275
420PhosphorylationPCLSSVLSPPPEKAG
HHHHHHCCCCHHHCC
32.9527251275

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

Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of BHE41_HUMAN !!

Disease-associated PTM Sites based on SAP

* 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_HUMAN !!

Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
CEBPB_HUMANCEBPBphysical
19029947
BHE41_HUMANBHLHE41physical
17487425
MYOD1_HUMANMYOD1physical
17487425
HDAC1_HUMANHDAC1physical
20821348
BHE40_HUMANBHLHE40physical
15560782
HIF1A_HUMANHIF1Aphysical
22801492
PSA4_HUMANPSMA4physical
22801492
BHE41_HUMANBHLHE41physical
22801492
CEBPA_HUMANCEBPAphysical
22355045
HDAC1_HUMANHDAC1physical
22355045
FBW1B_HUMANFBXW11physical
23555304
GSK3B_HUMANGSK3Bphysical
23555304
NONO_HUMANNONOphysical
23555304
2A5E_HUMANPPP2R5Ephysical
23555304
RORG_HUMANRORCphysical
23555304
BHE41_HUMANBHLHE41physical
23555304
WDR5_HUMANWDR5physical
23555304
PER2_HUMANPER2physical
23555304
2AAB_HUMANPPP2R1Bphysical
23555304
RASD1_HUMANRASD1physical
23555304
PP2AB_HUMANPPP2CBphysical
23555304
RORA_HUMANRORAphysical
23555304

Drug and Disease Associations
Kegg Drug
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of BHE41_HUMAN

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Related Literatures of Post-Translational Modification

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