BHE40_HUMAN - dbPTM
BHE40_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID BHE40_HUMAN
UniProt AC O14503
Protein Name Class E basic helix-loop-helix protein 40
Gene Name BHLHE40
Organism Homo sapiens (Human).
Sequence Length 412
Subcellular Localization Cytoplasm . Nucleus . Predominantly localized in the nucleus (PubMed:11278694).
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 be involved in the regulation of chondrocyte differentiation via the cAMP pathway..
Protein Sequence MERIPSAQPPPACLPKAPGLEHGDLPGMYPAHMYQVYKSRRGIKRSEDSKETYKLPHRLIEKKRRDRINECIAQLKDLLPEHLKLTTLGHLEKAVVLELTLKHVKALTNLIDQQQQKIIALQSGLQAGELSGRNVETGQEMFCSGFQTCAREVLQYLAKHENTRDLKSSQLVTHLHRVVSELLQGGTSRKPSDPAPKVMDFKEKPSSPAKGSEGPGKNCVPVIQRTFAHSSGEQSGSDTDTDSGYGGESEKGDLRSEQPCFKSDHGRRFTMGERIGAIKQESEEPPTKKNRMQLSDDEGHFTSSDLISSPFLGPHPHQPPFCLPFYLIPPSATAYLPMLEKCWYPTSVPVLYPGLNASAAALSSFMNPDKISAPLLMPQRLPSPLPAHPSVDSSVLLQALKPIPPLNLETKD
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
6Phosphorylation--MERIPSAQPPPAC
--CCCCCCCCCCCCC		36.8524719451
16UbiquitinationPPPACLPKAPGLEHG
CCCCCCCCCCCCCCC		55.02-
37PhosphorylationPAHMYQVYKSRRGIK
CHHHHHHHHHHCCCC		6.4222817900
38AcetylationAHMYQVYKSRRGIKR
HHHHHHHHHHCCCCC		38.33155373
54AcetylationEDSKETYKLPHRLIE
CCCHHHHCCCHHHHH		64.0612432263
84UbiquitinationDLLPEHLKLTTLGHL
HHCHHHHHCCCHHHH		45.77-
105UbiquitinationELTLKHVKALTNLID
HHHHHHHHHHHHHHH		37.08-
117UbiquitinationLIDQQQQKIIALQSG
HHHHHHHHHHHHHHC		31.572190698
159SumoylationEVLQYLAKHENTRDL
HHHHHHHHCCCCCCC		49.1821829689
159SumoylationEVLQYLAKHENTRDL
HHHHHHHHCCCCCCC		49.18-
159UbiquitinationEVLQYLAKHENTRDL
HHHHHHHHCCCCCCC		49.18-
167SumoylationHENTRDLKSSQLVTH
CCCCCCCHHHHHHHH		52.96-
167SumoylationHENTRDLKSSQLVTH
CCCCCCCHHHHHHHH		52.9628112733
167UbiquitinationHENTRDLKSSQLVTH
CCCCCCCHHHHHHHH		52.96-
192PhosphorylationGGTSRKPSDPAPKVM
CCCCCCCCCCCCCCC		60.3029083192
202AcetylationAPKVMDFKEKPSSPA
CCCCCCCCCCCCCCC		61.647709511
206PhosphorylationMDFKEKPSSPAKGSE
CCCCCCCCCCCCCCC		61.0825394399
207PhosphorylationDFKEKPSSPAKGSEG
CCCCCCCCCCCCCCC		37.0924719451
212PhosphorylationPSSPAKGSEGPGKNC
CCCCCCCCCCCCCCC		38.3824719451
217UbiquitinationKGSEGPGKNCVPVIQ
CCCCCCCCCCCHHHH		50.75-
226PhosphorylationCVPVIQRTFAHSSGE
CCHHHHHHHCCCCCC		14.5928450419
230PhosphorylationIQRTFAHSSGEQSGS
HHHHHCCCCCCCCCC		36.2928450419
231PhosphorylationQRTFAHSSGEQSGSD
HHHHCCCCCCCCCCC		36.1628450419
235PhosphorylationAHSSGEQSGSDTDTD
CCCCCCCCCCCCCCC		35.6428450419
237PhosphorylationSSGEQSGSDTDTDSG
CCCCCCCCCCCCCCC		42.4528450419
239PhosphorylationGEQSGSDTDTDSGYG
CCCCCCCCCCCCCCC		42.3628450419
241PhosphorylationQSGSDTDTDSGYGGE
CCCCCCCCCCCCCCC		33.8728450419
243PhosphorylationGSDTDTDSGYGGESE
CCCCCCCCCCCCCCC		35.6923090842
245PhosphorylationDTDTDSGYGGESEKG
CCCCCCCCCCCCCCC		26.3823090842
249PhosphorylationDSGYGGESEKGDLRS
CCCCCCCCCCCCCCC		48.1323090842
251UbiquitinationGYGGESEKGDLRSEQ
CCCCCCCCCCCCCCC		67.99-
262UbiquitinationRSEQPCFKSDHGRRF
CCCCCCCCCCCCCCC		62.79-
279SumoylationGERIGAIKQESEEPP
HHHHHCHHCCCCCCC		47.6925114211
279SumoylationGERIGAIKQESEEPP
HHHHHCHHCCCCCCC		47.69-
288SumoylationESEEPPTKKNRMQLS
CCCCCCCCCCCCCCC		54.5528112733
380MethylationAPLLMPQRLPSPLPA
CCCCCCCCCCCCCCC		42.57-
383PhosphorylationLMPQRLPSPLPAHPS
CCCCCCCCCCCCCCC		43.6028450419
393PhosphorylationPAHPSVDSSVLLQAL
CCCCCCCHHHHHHHH		21.8627251275
394PhosphorylationAHPSVDSSVLLQALK
CCCCCCHHHHHHHHC		16.6027251275
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
243SPhosphorylationKinaseCK1AP48729
PSP
-KUbiquitinationE3 ubiquitin ligaseBTRCQ9Y297
PMID:25202122
-KUbiquitinationE3 ubiquitin ligaseFBXW11Q9UKB1
PMID:25202122
-KUbiquitinationE3 ubiquitin ligaseVHLP40337
PMID:11278694
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of BHE40_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 BHE40_HUMAN !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
BRD7_HUMANBRD7physical
16169070
SETB1_HUMANSETDB1physical
16169070
VIME_HUMANVIMphysical
16169070
CHD3_HUMANCHD3physical
16169070
ZHX1_HUMANZHX1physical
16169070
STAT3_HUMANSTAT3physical
15223310
SIN3A_HUMANSIN3Aphysical
10737769
HDAC1_HUMANHDAC1physical
10737769
UBC9_HUMANUBE2Iphysical
11278694
P53_HUMANTP53physical
17347673
ZEP1_HUMANHIVEP1physical
21988832
FBLN1_HUMANFBLN1physical
21988832
CALL3_HUMANCALML3physical
21988832
ENOA_HUMANENO1physical
21988832
NUMBL_HUMANNUMBLphysical
21988832
UBP21_HUMANUSP21physical
25202122
FBW1A_HUMANBTRCphysical
25202122
BHE40_HUMANBHLHE40physical
25416956
CCNK_HUMANCCNKphysical
25416956
STK19_HUMANSTK19physical
25416956
MAGD1_HUMANMAGED1physical
25416956
TOB2_HUMANTOB2physical
25416956
RBPMS_HUMANRBPMSphysical
25416956
RHBT3_HUMANRHOBTB3physical
25416956
TXN4B_HUMANTXNL4Bphysical
25416956
PKHB2_HUMANPLEKHB2physical
25416956
RBM23_HUMANRBM23physical
25416956
VAC14_HUMANVAC14physical
25416956
RHOJ_HUMANRHOJphysical
25416956
TTC23_HUMANTTC23physical
25416956
NOC4L_HUMANNOC4Lphysical
25416956
NAA50_HUMANNAA50physical
25416956
LARP4_HUMANLARP4physical
25416956
CDPF1_HUMANCDPF1physical
25416956
SMYD1_HUMANSMYD1physical
25416956
KR231_HUMANKRTAP23-1physical
25416956
Drug and Disease Associations
Kegg Disease
There are no disease associations of PTM sites.
OMIM Disease
There are no disease associations of PTM sites.
Kegg Drug
There are no disease associations of PTM sites.
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of BHE40_HUMAN

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Related Literatures of Post-Translational Modification

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