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Class E basic helix-loop-helix protein 41 (bHLHe41) (Class B basic helix-loop-helix protein 3) (bHLHb3) (Differentially expressed in chondrocytes protein 2) (hDEC2) (Enhancer-of-split and hairy-related protein 1) (SHARP-1)

 BHE41_HUMAN             Reviewed;         482 AA.
Q9C0J9; A2I2N8;
05-MAR-2002, integrated into UniProtKB/Swiss-Prot.
01-JUN-2001, sequence version 1.
20-JUN-2018, entry version 149.
RecName: Full=Class E basic helix-loop-helix protein 41;
Short=bHLHe41;
AltName: Full=Class B basic helix-loop-helix protein 3;
Short=bHLHb3;
AltName: Full=Differentially expressed in chondrocytes protein 2;
Short=hDEC2;
AltName: Full=Enhancer-of-split and hairy-related protein 1;
Short=SHARP-1;
Name=BHLHE41; Synonyms=BHLHB3, DEC2, SHARP1;
Homo sapiens (Human).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
Catarrhini; Hominidae; Homo.
NCBI_TaxID=9606;
[1]
NUCLEOTIDE SEQUENCE [MRNA].
PubMed=11162494; DOI=10.1006/bbrc.2000.4133;
Fujimoto K., Shen M., Noshiro M., Matsubara K., Shingu S., Honda K.,
Yoshida E., Suardita K., Matsuda Y., Kato Y.;
"Molecular cloning and characterization of DEC2, a new member of basic
helix-loop-helix proteins.";
Biochem. Biophys. Res. Commun. 280:164-171(2001).
[2]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
NHLBI resequencing and genotyping service (RS&G);
Submitted (SEP-2006) to the EMBL/GenBank/DDBJ databases.
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L.,
Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R.,
Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V.,
Hannenhalli S., Turner R., Yooseph S., Lu F., Nusskern D.R.,
Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H.,
Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G.,
Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W.,
Venter J.C.;
Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
[4]
FUNCTION.
PubMed=11278948; DOI=10.1074/jbc.M011619200;
Garriga-Canut M., Roopra A., Buckley N.J.;
"The basic helix-loop-helix protein, SHARP-1, represses transcription
by a histone deacetylase-dependent and histone deacetylase-independent
mechanism.";
J. Biol. Chem. 276:14821-14828(2001).
[5]
FUNCTION.
PubMed=14672706; DOI=10.1016/j.bbrc.2003.11.099;
Kawamoto T., Noshiro M., Sato F., Maemura K., Takeda N., Nagai R.,
Iwata T., Fujimoto K., Furukawa M., Miyazaki K., Honma S., Honma K.I.,
Kato Y.;
"A novel autofeedback loop of Dec1 transcription involved in circadian
rhythm regulation.";
Biochem. Biophys. Res. Commun. 313:117-124(2004).
[6]
FUNCTION, AND HETERODIMERIZATION WITH BHLHE40/DEC1.
PubMed=15193144;
Li Y., Song X., Ma Y., Liu J., Yang D., Yan B.;
"DNA binding, but not interaction with Bmal1, is responsible for DEC1-
mediated transcription regulation of the circadian gene mPer1.";
Biochem. J. 382:895-904(2004).
[7]
FUNCTION.
PubMed=15560782; DOI=10.1111/j.1432-1033.2004.04379.x;
Sato F., Kawamoto T., Fujimoto K., Noshiro M., Honda K.K., Honma S.,
Honma K., Kato Y.;
"Functional analysis of the basic helix-loop-helix transcription
factor DEC1 in circadian regulation. Interaction with BMAL1.";
Eur. J. Biochem. 271:4409-4419(2004).
[8]
FUNCTION.
PubMed=18411297; DOI=10.1128/MCB.02168-07;
Nakashima A., Kawamoto T., Honda K.K., Ueshima T., Noshiro M.,
Iwata T., Fujimoto K., Kubo H., Honma S., Yorioka N., Kohno N.,
Kato Y.;
"DEC1 modulates the circadian phase of clock gene expression.";
Mol. Cell. Biol. 28:4080-4092(2008).
[9]
FUNCTION, INTERACTION WITH RXRA, AND MUTAGENESIS OF 70-LEU-LEU-71.
PubMed=19786558; DOI=10.1124/mol.109.057000;
Cho Y., Noshiro M., Choi M., Morita K., Kawamoto T., Fujimoto K.,
Kato Y., Makishima M.;
"The basic helix-loop-helix proteins differentiated embryo chondrocyte
(DEC) 1 and DEC2 function as corepressors of retinoid X receptors.";
Mol. Pharmacol. 76:1360-1369(2009).
[10]
SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-210 AND LYS-266, AND
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=25755297; DOI=10.1074/mcp.O114.044792;
Xiao Z., Chang J.G., Hendriks I.A., Sigurdsson J.O., Olsen J.V.,
Vertegaal A.C.;
"System-wide analysis of SUMOylation dynamics in response to
replication stress reveals novel small ubiquitin-like modified target
proteins and acceptor lysines relevant for genome stability.";
Mol. Cell. Proteomics 14:1419-1434(2015).
[11]
SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-31; LYS-121; LYS-210 AND
LYS-266, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE
ANALYSIS].
PubMed=28112733; DOI=10.1038/nsmb.3366;
Hendriks I.A., Lyon D., Young C., Jensen L.J., Vertegaal A.C.,
Nielsen M.L.;
"Site-specific mapping of the human SUMO proteome reveals co-
modification with phosphorylation.";
Nat. Struct. Mol. Biol. 24:325-336(2017).
[12]
VARIANT ARG-384, ASSOCIATION OF VARIANT ARG-384 WITH SHORT SLEEP
PHENOTYPE, AND POLYMORPHISM.
PubMed=19679812; DOI=10.1126/science.1174443;
He Y., Jones C.R., Fujiki N., Xu Y., Guo B., Holder J.L. Jr.,
Rossner M.J., Nishino S., Fu Y.H.;
"The transcriptional repressor DEC2 regulates sleep length in
mammals.";
Science 325:866-870(2009).
-!- FUNCTION: 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. {ECO:0000269|PubMed:11278948,
ECO:0000269|PubMed:14672706, ECO:0000269|PubMed:15193144,
ECO:0000269|PubMed:15560782, ECO:0000269|PubMed:18411297,
ECO:0000269|PubMed:19786558}.
-!- SUBUNIT: Homodimer. Heterodimer with BHLHE40/DEC1. Interacts with
CIART and ARNTL/BMAL1 (By similarity). Interacts with RXRA.
{ECO:0000250, ECO:0000269|PubMed:19786558}.
-!- INTERACTION:
Q16665:HIF1A; NbExp=2; IntAct=EBI-10988877, EBI-447269;
-!- SUBCELLULAR LOCATION: Nucleus {ECO:0000255|PROSITE-
ProRule:PRU00380, ECO:0000255|PROSITE-ProRule:PRU00981}.
-!- TISSUE SPECIFICITY: Highly expressed in skeletal muscle and brain,
moderately expressed in pancreas and heart, weakly expressed in
placenta, lung, liver and kidney.
-!- POLYMORPHISM: Genetic variations in BHLHE41 are associated with
the short sleep phenotype [MIM:612975]. Individuals with this
trait require less sleep in any 24-hour period than is typical for
their age group. {ECO:0000269|PubMed:19679812}.
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EMBL; AB044088; BAB21502.1; -; mRNA.
EMBL; EF015896; ABM64207.1; -; Genomic_DNA.
EMBL; CH471094; EAW96527.1; -; Genomic_DNA.
CCDS; CCDS8706.1; -.
PIR; JC7583; JC7583.
RefSeq; NP_110389.1; NM_030762.2.
UniGene; Hs.177841; -.
ProteinModelPortal; Q9C0J9; -.
SMR; Q9C0J9; -.
BioGrid; 122654; 38.
DIP; DIP-59904N; -.
IntAct; Q9C0J9; 10.
STRING; 9606.ENSP00000242728; -.
iPTMnet; Q9C0J9; -.
PhosphoSitePlus; Q9C0J9; -.
BioMuta; BHLHE41; -.
DMDM; 20137459; -.
EPD; Q9C0J9; -.
MaxQB; Q9C0J9; -.
PaxDb; Q9C0J9; -.
PeptideAtlas; Q9C0J9; -.
PRIDE; Q9C0J9; -.
ProteomicsDB; 80065; -.
TopDownProteomics; Q9C0J9; -.
Ensembl; ENST00000242728; ENSP00000242728; ENSG00000123095.
GeneID; 79365; -.
KEGG; hsa:79365; -.
UCSC; uc001rhb.4; human.
CTD; 79365; -.
DisGeNET; 79365; -.
EuPathDB; HostDB:ENSG00000123095.5; -.
GeneCards; BHLHE41; -.
HGNC; HGNC:16617; BHLHE41.
HPA; HPA056035; -.
MalaCards; BHLHE41; -.
MIM; 606200; gene.
MIM; 612975; phenotype.
neXtProt; NX_Q9C0J9; -.
OpenTargets; ENSG00000123095; -.
PharmGKB; PA164716636; -.
eggNOG; KOG4304; Eukaryota.
eggNOG; ENOG4111F0X; LUCA.
GeneTree; ENSGT00510000046898; -.
HOGENOM; HOG000234381; -.
HOVERGEN; HBG050685; -.
InParanoid; Q9C0J9; -.
KO; K03730; -.
OMA; LYMCKSK; -.
OrthoDB; EOG091G0D3I; -.
PhylomeDB; Q9C0J9; -.
TreeFam; TF330859; -.
Reactome; R-HSA-1368108; BMAL1:CLOCK,NPAS2 activates circadian gene expression.
Reactome; R-HSA-400253; Circadian Clock.
SignaLink; Q9C0J9; -.
SIGNOR; Q9C0J9; -.
ChiTaRS; BHLHE41; human.
GeneWiki; BHLHB3; -.
GenomeRNAi; 79365; -.
PRO; PR:Q9C0J9; -.
Proteomes; UP000005640; Chromosome 12.
Bgee; ENSG00000123095; -.
ExpressionAtlas; Q9C0J9; baseline and differential.
Genevisible; Q9C0J9; HS.
GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
GO; GO:0043425; F:bHLH transcription factor binding; IPI:BHF-UCL.
GO; GO:0070888; F:E-box binding; IDA:BHF-UCL.
GO; GO:0042826; F:histone deacetylase binding; ISS:BHF-UCL.
GO; GO:0043426; F:MRF binding; ISS:BHF-UCL.
GO; GO:0046982; F:protein heterodimerization activity; IPI:BHF-UCL.
GO; GO:0042803; F:protein homodimerization activity; ISS:BHF-UCL.
GO; GO:0001102; F:RNA polymerase II activating transcription factor binding; ISS:BHF-UCL.
GO; GO:0000978; F:RNA polymerase II proximal promoter sequence-specific DNA binding; ISS:BHF-UCL.
GO; GO:0000981; F:RNA polymerase II transcription factor activity, sequence-specific DNA binding; ISA:NTNU_SB.
GO; GO:0003714; F:transcription corepressor activity; IDA:UniProtKB.
GO; GO:0003705; F:transcription factor activity, RNA polymerase II distal enhancer sequence-specific binding; ISS:BHF-UCL.
GO; GO:0001078; F:transcriptional repressor activity, RNA polymerase II proximal promoter sequence-specific DNA binding; ISS:BHF-UCL.
GO; GO:0001191; F:transcriptional repressor activity, RNA polymerase II transcription factor binding; ISS:BHF-UCL.
GO; GO:0009887; P:animal organ morphogenesis; NAS:UniProtKB.
GO; GO:0030154; P:cell differentiation; NAS:UniProtKB.
GO; GO:0008283; P:cell proliferation; NAS:UniProtKB.
GO; GO:0032922; P:circadian regulation of gene expression; IEA:Ensembl.
GO; GO:0010832; P:negative regulation of myotube differentiation; ISS:BHF-UCL.
GO; GO:0010944; P:negative regulation of transcription by competitive promoter binding; ISS:BHF-UCL.
GO; GO:0000122; P:negative regulation of transcription by RNA polymerase II; IDA:BHF-UCL.
GO; GO:0045892; P:negative regulation of transcription, DNA-templated; ISS:UniProtKB.
GO; GO:0006351; P:transcription, DNA-templated; IEA:UniProtKB-KW.
CDD; cd00083; HLH; 1.
Gene3D; 4.10.280.10; -; 1.
InterPro; IPR011598; bHLH_dom.
InterPro; IPR036638; HLH_DNA-bd_sf.
InterPro; IPR003650; Orange_dom.
Pfam; PF07527; Hairy_orange; 1.
Pfam; PF00010; HLH; 1.
SMART; SM00353; HLH; 1.
SMART; SM00511; ORANGE; 1.
SUPFAM; SSF47459; SSF47459; 1.
PROSITE; PS50888; BHLH; 1.
PROSITE; PS51054; ORANGE; 1.
1: Evidence at protein level;
Biological rhythms; Complete proteome; DNA-binding; Isopeptide bond;
Nucleus; Polymorphism; Reference proteome; Repressor; Transcription;
Transcription regulation; Ubl conjugation.
CHAIN 1 482 Class E basic helix-loop-helix protein
41.
/FTId=PRO_0000127147.
DOMAIN 44 99 bHLH. {ECO:0000255|PROSITE-
ProRule:PRU00981}.
DOMAIN 131 166 Orange. {ECO:0000255|PROSITE-
ProRule:PRU00380}.
REGION 67 71 Necessary for interaction with RXRA and
repressor activity towards RXRA.
{ECO:0000269|PubMed:19786558}.
COMPBIAS 297 431 Ala/Gly-rich.
CROSSLNK 31 31 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in SUMO2).
{ECO:0000244|PubMed:28112733}.
CROSSLNK 121 121 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in SUMO2).
{ECO:0000244|PubMed:28112733}.
CROSSLNK 210 210 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in SUMO2).
{ECO:0000244|PubMed:25755297,
ECO:0000244|PubMed:28112733}.
CROSSLNK 266 266 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in SUMO2).
{ECO:0000244|PubMed:25755297,
ECO:0000244|PubMed:28112733}.
VARIANT 384 384 P -> R (associated with short sleep
phenotype; dbSNP:rs121912617).
{ECO:0000269|PubMed:19679812}.
/FTId=VAR_063259.
MUTAGEN 70 71 LL->AA: Abolishes RXRA repression.
{ECO:0000269|PubMed:19786558}.
SEQUENCE 482 AA; 50498 MW; 2BECDC2FDEB7CE14 CRC64;
MDEGIPHLQE RQLLEHRDFI GLDYSSLYMC KPKRSMKRDD TKDTYKLPHR LIEKKRRDRI
NECIAQLKDL LPEHLKLTTL GHLEKAVVLE LTLKHLKALT ALTEQQHQKI IALQNGERSL
KSPIQSDLDA FHSGFQTCAK EVLQYLSRFE SWTPREPRCV QLINHLHAVA TQFLPTPQLL
TQQVPLSKGT GAPSAAGSAA APCLERAGQK LEPLAYCVPV IQRTQPSAEL AAENDTDTDS
GYGGEAEARP DREKGKGAGA SRVTIKQEPP GEDSPAPKRM KLDSRGGGSG GGPGGGAAAA
AAALLGPDPA AAAALLRPDA ALLSSLVAFG GGGGAPFPQP AAAAAPFCLP FCFLSPSAAA
AYVQPFLDKS GLEKYLYPAA AAAPFPLLYP GIPAPAAAAA AAAAAAAAAA AFPCLSSVLS
PPPEKAGAAA ATLLPHEVAP LGAPHPQHPH GRTHLPFAGP REPGNPESSA QEDPSQPGKE
AP


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