Did you know ? If you order before Friday 14h we deliver 90PCT of the the time next Tuesday, GENTAUR another in time delivery

Class E basic helix-loop-helix protein 40 (bHLHe40) (Class B basic helix-loop-helix protein 2) (bHLHb2) (Differentially expressed in chondrocytes protein 1) (DEC1) (Enhancer-of-split and hairy-related protein 2) (SHARP-2) (Stimulated by retinoic acid gene 13 protein)

 BHE40_HUMAN             Reviewed;         412 AA.
O14503; Q96TD3;
05-MAR-2002, integrated into UniProtKB/Swiss-Prot.
01-JAN-1998, sequence version 1.
25-OCT-2017, entry version 157.
RecName: Full=Class E basic helix-loop-helix protein 40;
Short=bHLHe40;
AltName: Full=Class B basic helix-loop-helix protein 2;
Short=bHLHb2;
AltName: Full=Differentially expressed in chondrocytes protein 1;
Short=DEC1;
AltName: Full=Enhancer-of-split and hairy-related protein 2;
Short=SHARP-2;
AltName: Full=Stimulated by retinoic acid gene 13 protein;
Name=BHLHE40; Synonyms=BHLHB2, DEC1, SHARP2, STRA13;
Homo sapiens (Human).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
Catarrhini; Hominidae; Homo.
NCBI_TaxID=9606;
[1]
NUCLEOTIDE SEQUENCE [MRNA].
TISSUE=Cartilage;
PubMed=9240428; DOI=10.1006/bbrc.1997.6960;
Shen M., Kawamoto T., Yan W., Nakamasu K., Tamagami M., Koyano Y.,
Noshiro M., Kato Y.;
"Molecular characterization of the novel basic helix-loop-helix
protein DEC1 expressed in differentiated human embryo chondrocytes.";
Biochem. Biophys. Res. Commun. 236:294-298(1997).
[2]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
TISSUE=Leukocyte;
PubMed=11226878; DOI=10.1093/oxfordjournals.jbchem.a002869;
Teramoto M., Nakamasu K., Noshiro M., Matsuda Y., Gotoh O., Shen M.,
Tsutsumi S., Kawamoto T., Iwamoto Y., Kato Y.;
"Gene structure and chromosomal location of a human bHLH
transcriptional factor DEC1 x Stra13 x SHARP-2/BHLHB2.";
J. Biochem. 129:391-396(2001).
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
TISSUE=Skin;
PubMed=15489334; DOI=10.1101/gr.2596504;
The MGC Project Team;
"The status, quality, and expansion of the NIH full-length cDNA
project: the Mammalian Gene Collection (MGC).";
Genome Res. 14:2121-2127(2004).
[4]
NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 4-412.
Ivanov S.V., Lerman M.I.;
"Exon-intron structure of the human STRA13(DEC1) bHLH transcription
factor gene.";
Submitted (FEB-2001) to the EMBL/GenBank/DDBJ databases.
[5]
UBIQUITINATION, INTERACTION WITH UBE2I, AND SUBCELLULAR LOCATION.
PubMed=11278694; DOI=10.1074/jbc.M010516200;
Ivanova A.V., Ivanov S.V., Danilkovitch-Miagkova A., Lerman M.I.;
"Regulation of STRA13 by the von Hippel-Lindau tumor suppressor
protein, hypoxia, and the UBC9/ubiquitin proteasome degradation
pathway.";
J. Biol. Chem. 276:15306-15315(2001).
[6]
FUNCTION, AND INTERACTION WITH ARNTL.
PubMed=12397359; DOI=10.1038/nature01123;
Honma S., Kawamoto T., Takagi Y., Fujimoto K., Sato F., Noshiro M.,
Kato Y., Honma K.I.;
"Dec1 and Dec2 are regulators of the mammalian molecular clock.";
Nature 419:841-844(2002).
[7]
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).
[8]
FUNCTION, HETERODIMERIZATION WITH BHLHE41/DEC2, AND INTERACTION WITH
ARNTL.
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).
[9]
FUNCTION, INTERACTION WITH ARNTL, AND MUTAGENESIS OF HIS-57 AND
ARG-65.
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).
[10]
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).
[11]
FUNCTION, INTERACTION WITH RXRA, AND MUTAGENESIS OF 78-LEU-LEU-79.
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).
[12]
SUMOYLATION AT LYS-159 AND LYS-279, INTERACTION WITH HDAC1 AND SUMO1,
SUBCELLULAR LOCATION, AND MUTAGENESIS OF LYS-159 AND LYS-279.
PubMed=21829689; DOI=10.1371/journal.pone.0023046;
Hong Y., Xing X., Li S., Bi H., Yang C., Zhao F., Liu Y., Ao X.,
Chang A.K., Wu H.;
"SUMOylation of DEC1 protein regulates its transcriptional activity
and enhances its stability.";
PLoS ONE 6:E23046-E23046(2011).
[13]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-235, AND IDENTIFICATION
BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Erythroleukemia;
PubMed=23186163; DOI=10.1021/pr300630k;
Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J.,
Mohammed S.;
"Toward a comprehensive characterization of a human cancer cell
phosphoproteome.";
J. Proteome Res. 12:260-271(2013).
[14]
SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-279, AND IDENTIFICATION BY
MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=25218447; DOI=10.1038/nsmb.2890;
Hendriks I.A., D'Souza R.C., Yang B., Verlaan-de Vries M., Mann M.,
Vertegaal A.C.;
"Uncovering global SUMOylation signaling networks in a site-specific
manner.";
Nat. Struct. Mol. Biol. 21:927-936(2014).
[15]
SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-279, AND IDENTIFICATION BY
MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=25114211; DOI=10.1073/pnas.1413825111;
Impens F., Radoshevich L., Cossart P., Ribet D.;
"Mapping of SUMO sites and analysis of SUMOylation changes induced by
external stimuli.";
Proc. Natl. Acad. Sci. U.S.A. 111:12432-12437(2014).
[16]
SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-279, AND IDENTIFICATION BY
MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=25772364; DOI=10.1016/j.celrep.2015.02.033;
Hendriks I.A., Treffers L.W., Verlaan-de Vries M., Olsen J.V.,
Vertegaal A.C.;
"SUMO-2 orchestrates chromatin modifiers in response to DNA damage.";
Cell Rep. 10:1778-1791(2015).
[17]
SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-279, 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).
[18]
SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-167; LYS-279 AND LYS-288,
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).
-!- 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 PER1/2 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. {ECO:0000269|PubMed:12397359,
ECO:0000269|PubMed:14672706, ECO:0000269|PubMed:15193144,
ECO:0000269|PubMed:15560782, ECO:0000269|PubMed:18411297,
ECO:0000269|PubMed:19786558}.
-!- SUBUNIT: Homodimer. Heterodimer with BHLHE41/DEC2. Interacts with
TCF3/E47. Interacts with ubiquitin-conjugating enzyme UBE2I/UBC9.
Interacts with HDAC1, SUMO1, RXRA and ARNTL/BMAL1.
{ECO:0000269|PubMed:11278694, ECO:0000269|PubMed:12397359,
ECO:0000269|PubMed:15193144, ECO:0000269|PubMed:15560782,
ECO:0000269|PubMed:19786558, ECO:0000269|PubMed:21829689}.
-!- INTERACTION:
P0C206:- (xeno); NbExp=3; IntAct=EBI-711810, EBI-9675596;
C9JG97:AAMP; NbExp=3; IntAct=EBI-711810, EBI-10176499;
Q16613:AANAT; NbExp=6; IntAct=EBI-711810, EBI-7451846;
Q08117:AES; NbExp=3; IntAct=EBI-711810, EBI-717810;
O75909:CCNK; NbExp=3; IntAct=EBI-711810, EBI-739806;
Q6NVV7:CDPF1; NbExp=3; IntAct=EBI-711810, EBI-2802782;
P10606:COX5B; NbExp=3; IntAct=EBI-711810, EBI-1053725;
O75553:DAB1; NbExp=3; IntAct=EBI-711810, EBI-7875264;
Q08426:EHHADH; NbExp=3; IntAct=EBI-711810, EBI-2339219;
Q86UY5:FAM83A; NbExp=4; IntAct=EBI-711810, EBI-1384254;
Q8NEA9:GMCL1P1; NbExp=3; IntAct=EBI-711810, EBI-745707;
A1A580:KRTAP23-1; NbExp=3; IntAct=EBI-711810, EBI-10171734;
Q71RC2-6:LARP4; NbExp=3; IntAct=EBI-711810, EBI-10255841;
Q9Y5V3:MAGED1; NbExp=7; IntAct=EBI-711810, EBI-716006;
Q9GZZ1:NAA50; NbExp=5; IntAct=EBI-711810, EBI-1052523;
Q9BVI4:NOC4L; NbExp=3; IntAct=EBI-711810, EBI-395927;
P18545:PDE6G; NbExp=3; IntAct=EBI-711810, EBI-2622029;
Q96CS7:PLEKHB2; NbExp=3; IntAct=EBI-711810, EBI-373552;
Q13131:PRKAA1; NbExp=3; IntAct=EBI-711810, EBI-1181405;
Q86U06:RBM23; NbExp=3; IntAct=EBI-711810, EBI-780319;
Q86U06-2:RBM23; NbExp=3; IntAct=EBI-711810, EBI-10258579;
Q93062:RBPMS; NbExp=3; IntAct=EBI-711810, EBI-740322;
O94955:RHOBTB3; NbExp=5; IntAct=EBI-711810, EBI-2367123;
Q9H4E5:RHOJ; NbExp=3; IntAct=EBI-711810, EBI-6285694;
Q8NB12:SMYD1; NbExp=5; IntAct=EBI-711810, EBI-8463848;
O60248:SOX15; NbExp=3; IntAct=EBI-711810, EBI-5452954;
B7ZLI8:STK19; NbExp=5; IntAct=EBI-711810, EBI-10176124;
Q14106:TOB2; NbExp=3; IntAct=EBI-711810, EBI-2562000;
P04637:TP53; NbExp=11; IntAct=EBI-711810, EBI-366083;
Q5W5X9:TTC23; NbExp=3; IntAct=EBI-711810, EBI-6447954;
Q9NX01:TXNL4B; NbExp=3; IntAct=EBI-711810, EBI-10309345;
P63279:UBE2I; NbExp=3; IntAct=EBI-711810, EBI-80168;
Q08AM6:VAC14; NbExp=5; IntAct=EBI-711810, EBI-2107455;
-!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:21829689}.
Nucleus {ECO:0000269|PubMed:11278694,
ECO:0000269|PubMed:21829689}. Note=Predominantly localized in the
nucleus (PubMed:11278694). {ECO:0000269|PubMed:11278694}.
-!- TISSUE SPECIFICITY: Expressed in cartilage, spleen, intestine,
lung, and to a lesser extent in heart, brain, liver, muscle and
stomach.
-!- PTM: Ubiquitinated; which may lead to proteasomal degradation.
{ECO:0000269|PubMed:11278694}.
-!- PTM: Sumoylation inhibits its ubiquitination and promotes its
negative regulation of the CLOCK-ARNTL/BMAL1 heterodimer
transcriptional activator activity. {ECO:0000269|PubMed:11278694,
ECO:0000269|PubMed:21829689}.
-----------------------------------------------------------------------
Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms
Distributed under the Creative Commons Attribution-NoDerivs License
-----------------------------------------------------------------------
EMBL; AB004066; BAA21720.1; -; mRNA.
EMBL; AB043885; BAB18565.1; -; Genomic_DNA.
EMBL; BC082238; AAH82238.1; -; mRNA.
EMBL; AH010709; AAK49525.1; -; Genomic_DNA.
CCDS; CCDS2565.1; -.
PIR; JC5547; JC5547.
RefSeq; NP_003661.1; NM_003670.2.
UniGene; Hs.744856; -.
ProteinModelPortal; O14503; -.
SMR; O14503; -.
BioGrid; 114123; 57.
DIP; DIP-36698N; -.
IntAct; O14503; 108.
MINT; MINT-1374397; -.
STRING; 9606.ENSP00000256495; -.
iPTMnet; O14503; -.
PhosphoSitePlus; O14503; -.
BioMuta; BHLHE40; -.
PaxDb; O14503; -.
PeptideAtlas; O14503; -.
PRIDE; O14503; -.
DNASU; 8553; -.
Ensembl; ENST00000256495; ENSP00000256495; ENSG00000134107.
GeneID; 8553; -.
KEGG; hsa:8553; -.
CTD; 8553; -.
DisGeNET; 8553; -.
EuPathDB; HostDB:ENSG00000134107.4; -.
GeneCards; BHLHE40; -.
HGNC; HGNC:1046; BHLHE40.
HPA; HPA028922; -.
MIM; 604256; gene.
neXtProt; NX_O14503; -.
OpenTargets; ENSG00000134107; -.
PharmGKB; PA25347; -.
eggNOG; KOG4304; Eukaryota.
eggNOG; ENOG4111F0X; LUCA.
GeneTree; ENSGT00510000046898; -.
HOGENOM; HOG000234381; -.
InParanoid; O14503; -.
KO; K03729; -.
OMA; AGQEMFC; -.
OrthoDB; EOG091G0D3I; -.
PhylomeDB; O14503; -.
TreeFam; TF330859; -.
Reactome; R-HSA-1368108; BMAL1:CLOCK,NPAS2 activates circadian gene expression.
SignaLink; O14503; -.
SIGNOR; O14503; -.
ChiTaRS; BHLHE40; human.
GeneWiki; BHLHB2; -.
GenomeRNAi; 8553; -.
PRO; PR:O14503; -.
Proteomes; UP000005640; Chromosome 3.
Bgee; ENSG00000134107; -.
CleanEx; HS_DEC1; -.
CleanEx; HS_STRA13; -.
ExpressionAtlas; O14503; baseline and differential.
Genevisible; O14503; HS.
GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
GO; GO:0016604; C:nuclear body; IDA:HPA.
GO; GO:0005634; C:nucleus; IDA:BHF-UCL.
GO; GO:0043425; F:bHLH transcription factor binding; IPI:BHF-UCL.
GO; GO:0070888; F:E-box binding; IDA:BHF-UCL.
GO; GO:0043426; F:MRF binding; ISS:BHF-UCL.
GO; GO:0019904; F:protein domain specific binding; IPI:BHF-UCL.
GO; GO:0046982; F:protein heterodimerization activity; IPI:BHF-UCL.
GO; GO:0042803; F:protein homodimerization activity; IDA:BHF-UCL.
GO; GO:0001102; F:RNA polymerase II activating transcription factor binding; ISS:BHF-UCL.
GO; GO:0000981; F:RNA polymerase II transcription factor activity, sequence-specific DNA binding; IDA:BHF-UCL.
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:0003700; F:transcription factor activity, sequence-specific DNA binding; NAS:UniProtKB.
GO; GO:0001078; F:transcriptional repressor activity, RNA polymerase II core promoter proximal region sequence-specific binding; IDA:BHF-UCL.
GO; GO:0001191; F:transcriptional repressor activity, RNA polymerase II transcription factor binding; IDA:BHF-UCL.
GO; GO:0032922; P:circadian regulation of gene expression; IDA:BHF-UCL.
GO; GO:0043153; P:entrainment of circadian clock by photoperiod; ISS:BHF-UCL.
GO; GO:0043433; P:negative regulation of sequence-specific DNA binding transcription factor activity; IDA:BHF-UCL.
GO; GO:0000122; P:negative regulation of transcription from RNA polymerase II promoter; IDA:BHF-UCL.
GO; GO:0045892; P:negative regulation of transcription, DNA-templated; IDA:UniProtKB.
GO; GO:0006355; P:regulation of transcription, DNA-templated; NAS: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; Cytoplasm; DNA-binding;
Isopeptide bond; Nucleus; Phosphoprotein; Reference proteome;
Repressor; Transcription; Transcription regulation; Ubl conjugation.
CHAIN 1 412 Class E basic helix-loop-helix protein
40.
/FTId=PRO_0000127144.
DOMAIN 52 107 bHLH. {ECO:0000255|PROSITE-
ProRule:PRU00981}.
DOMAIN 142 175 Orange. {ECO:0000255|PROSITE-
ProRule:PRU00380}.
REGION 1 139 Essential for interaction with
ARNTL/BMAL1, E-box binding and repressor
activity against the CLOCK-ARNTL/BMAL1
heterodimer.
REGION 75 79 Necessary for interaction with RXRA and
repressor activity against RXRA.
{ECO:0000269|PubMed:19786558}.
MOD_RES 235 235 Phosphoserine.
{ECO:0000244|PubMed:23186163}.
MOD_RES 383 383 Phosphoserine.
{ECO:0000250|UniProtKB:O35185}.
CROSSLNK 159 159 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in SUMO1, SUMO2
and SUMO3).
{ECO:0000269|PubMed:21829689}.
CROSSLNK 167 167 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in SUMO2).
{ECO:0000244|PubMed:28112733}.
CROSSLNK 279 279 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in SUMO1);
alternate. {ECO:0000244|PubMed:25114211}.
CROSSLNK 279 279 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in SUMO1, SUMO2
and SUMO3); alternate.
CROSSLNK 279 279 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in SUMO2);
alternate. {ECO:0000244|PubMed:25218447,
ECO:0000244|PubMed:25755297,
ECO:0000244|PubMed:25772364,
ECO:0000244|PubMed:28112733}.
CROSSLNK 288 288 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in SUMO2).
{ECO:0000244|PubMed:28112733}.
MUTAGEN 57 57 H->A: No effect on its interaction with
ARNTL/BMAL1 or its repressor activity
against the CLOCK-ARNTL/BMAL1
heterodimer. Significant reduction in E-
box binding.
{ECO:0000269|PubMed:15560782}.
MUTAGEN 65 65 R->A: Loss of interaction with
ARNTL/BMAL1 and E-box binding.
Significant reduction in its repressor
activity against the CLOCK-ARNTL/BMAL1
heterodimer.
{ECO:0000269|PubMed:15560782}.
MUTAGEN 78 79 LL->AA: Abolishes RXRA repression.
{ECO:0000269|PubMed:19786558}.
MUTAGEN 159 159 K->R: Partial loss of sumoylation.
Complete loss of sumoylation; when
associated with R-279.
{ECO:0000269|PubMed:21829689}.
MUTAGEN 279 279 K->R: Partial loss of sumoylation.
Complete loss of sumoylation; when
associated with R-159.
{ECO:0000269|PubMed:21829689}.
SEQUENCE 412 AA; 45510 MW; 2D73A3D4980793E5 CRC64;
MERIPSAQPP PACLPKAPGL EHGDLPGMYP AHMYQVYKSR RGIKRSEDSK ETYKLPHRLI
EKKRRDRINE CIAQLKDLLP EHLKLTTLGH LEKAVVLELT LKHVKALTNL IDQQQQKIIA
LQSGLQAGEL SGRNVETGQE MFCSGFQTCA REVLQYLAKH ENTRDLKSSQ LVTHLHRVVS
ELLQGGTSRK PSDPAPKVMD FKEKPSSPAK GSEGPGKNCV PVIQRTFAHS SGEQSGSDTD
TDSGYGGESE KGDLRSEQPC FKSDHGRRFT MGERIGAIKQ ESEEPPTKKN RMQLSDDEGH
FTSSDLISSP FLGPHPHQPP FCLPFYLIPP SATAYLPMLE KCWYPTSVPV LYPGLNASAA
ALSSFMNPDK ISAPLLMPQR LPSPLPAHPS VDSSVLLQAL KPIPPLNLET KD


Related products :

Catalog number Product name Quantity
18-003-43865 Class B basic helix-loop-helix protein 2 - bHLHB2; Differentially expressed in chondrocytes protein 1; DEC1; Enhancer-of-split and hairy-related protein 2; SHARP-2; Stimulated by retinoic acid gene 13 0.05 mg Aff Pur
EIAAB37697 Basic helix-loop-helix transcription factor scleraxis,bHLHa41,BHLHA41,bHLHa48,Class A basic helix-loop-helix protein 41,Class A basic helix-loop-helix protein 48,Homo sapiens,Human,SCX,SCXA
U2004h CLIA Basic-helix-loop-helix-PAS protein MOP2,bHLHe73,BHLHE73,Class E basic helix-loop-helix protein 73,Endothelial PAS domain-containing protein 1,EPAS1,EPAS-1,HIF-1-alpha-like factor,HIF2A,HIF-2-alph 96T
U2004h CLIA kit Basic-helix-loop-helix-PAS protein MOP2,bHLHe73,BHLHE73,Class E basic helix-loop-helix protein 73,Endothelial PAS domain-containing protein 1,EPAS1,EPAS-1,HIF-1-alpha-like factor,HIF2A,HIF-2 96T
E2004h ELISA kit Basic-helix-loop-helix-PAS protein MOP2,bHLHe73,BHLHE73,Class E basic helix-loop-helix protein 73,Endothelial PAS domain-containing protein 1,EPAS1,EPAS-1,HIF-1-alpha-like factor,HIF2A,HIF- 96T
E2004h ELISA Basic-helix-loop-helix-PAS protein MOP2,bHLHe73,BHLHE73,Class E basic helix-loop-helix protein 73,Endothelial PAS domain-containing protein 1,EPAS1,EPAS-1,HIF-1-alpha-like factor,HIF2A,HIF-2-alp 96T
EIAAB28826 bHLHb1,BHLHB1,bHLHe19,BHLHE19,Class B basic helix-loop-helix protein 1,Class E basic helix-loop-helix protein 19,Homo sapiens,Human,OLIG2,Oligo2,Oligodendrocyte transcription factor 2,PRKCBP2,Protein
E0255h ELISA kit ATH1,ATOH1,bHLHa14,BHLHA14,Class A basic helix-loop-helix protein 14,hATH1,Helix-loop-helix protein hATH-1,Homo sapiens,Human,Protein atonal homolog 1 96T
U0255h CLIA ATH1,ATOH1,bHLHa14,BHLHA14,Class A basic helix-loop-helix protein 14,hATH1,Helix-loop-helix protein hATH-1,Homo sapiens,Human,Protein atonal homolog 1 96T
E0255h ELISA ATH1,ATOH1,bHLHa14,BHLHA14,Class A basic helix-loop-helix protein 14,hATH1,Helix-loop-helix protein hATH-1,Homo sapiens,Human,Protein atonal homolog 1 96T
U0798h CLIA ARNT-interacting protein,Basic-helix-loop-helix-PAS protein MOP1,bHLHe78,BHLHE78,Class E basic helix-loop-helix protein 78,HIF1A,HIF-1-alpha,HIF1-alpha,Homo sapiens,Human,Hypoxia-inducible factor 96T
E0798h ELISA ARNT-interacting protein,Basic-helix-loop-helix-PAS protein MOP1,bHLHe78,BHLHE78,Class E basic helix-loop-helix protein 78,HIF1A,HIF-1-alpha,HIF1-alpha,Homo sapiens,Human,Hypoxia-inducible facto 96T
E0798h ELISA kit ARNT-interacting protein,Basic-helix-loop-helix-PAS protein MOP1,bHLHe78,BHLHE78,Class E basic helix-loop-helix protein 78,HIF1A,HIF-1-alpha,HIF1-alpha,Homo sapiens,Human,Hypoxia-inducible 96T
EIAAB14718 Basic helix-loop-helix protein N-twist,bHLHa31,BHLHA31,Class A basic helix-loop-helix protein 31,Fer3-like protein,FERD3L,Homo sapiens,Human,NATO3,Nephew of atonal 3,Neuronal twist,NTWIST
EIAAB28828 bHLHb7,BHLHB7,bHLHe20,BHLHE20,Class B basic helix-loop-helix protein 7,Class E basic helix-loop-helix protein 20,Homo sapiens,Human,OLIG3,Oligo3,Oligodendrocyte transcription factor 3
EIAAB28821 bHLHb6,BHLHB6,bHLHe21,BHLHE21,Class B basic helix-loop-helix protein 6,Class E basic helix-loop-helix protein 21,Homo sapiens,Human,OLIG1,Oligo1,Oligodendrocyte transcription factor 1
27-987 BHLHB2 is a basic helix-loop-helix protein expressed in various tissues. Expression in the chondrocytes is responsive to the addition of Bt2cAMP. Differentiated embryo chondrocyte expressed gene 1 is 0.05 mg
18-272-195616 SHARP2 - Rabbit polyclonal to SHARP2; bHLHB2; Differentially expressed in chondrocytes protein 1; DEC1; Enhancer-of-split and hairy-related protein 2; SHARP-2; Stimulated by retinoic acid gene 13 prot 0.05 mg
BHE40_HUMAN ELISA Kit FOR Class E basic helix-loop-helix protein 40; organism: Human; gene name: BHLHE40 96T
BHE40_BOVIN ELISA Kit FOR Class E basic helix-loop-helix protein 40; organism: Bovine; gene name: BHLHE40 96T
BHE40_MOUSE ELISA Kit FOR Class E basic helix-loop-helix protein 40; organism: Mouse; gene name: Bhlhe40 96T
EIAAB27612 Basic-helix-loop-helix-PAS protein MOP5,bHLHe11,BHLHE11,Class E basic helix-loop-helix protein 11,Homo sapiens,Human,Member of PAS protein 5,MOP5,Neuronal PAS domain-containing protein 1,Neuronal PAS1
EIAAB27618 Basic-helix-loop-helix-PAS protein MOP6,bHLHe12,BHLHE12,Class E basic helix-loop-helix protein 12,Homo sapiens,Human,Member of PAS protein 6,MOP6,Neuronal PAS domain-containing protein 3,Neuronal PAS3
EIAAB27615 Basic-helix-loop-helix-PAS protein MOP4,bHLHe9,BHLHE9,Class E basic helix-loop-helix protein 9,Homo sapiens,Human,Member of PAS protein 4,MOP4,Neuronal PAS domain-containing protein 2,Neuronal PAS2,NP
EIAAB27132 bHLHa6,BHLHA6,Class A basic helix-loop-helix protein 6,Homo sapiens,Human,NeuroD3,NEUROD3,NEUROG1,Neurogenic basic-helix-loop-helix protein,Neurogenic differentiation factor 3,Neurogenin-1,NGN,NGN1,NG


 

GENTAUR Belgium BVBA BE0473327336
Voortstraat 49, 1910 Kampenhout BELGIUM
Tel 0032 16 58 90 45

Fax 0032 16 50 90 45
info@gentaur.com | Gentaur





GENTAUR Ltd.
Howard Frank Turnberry House
1404-1410 High Road
Whetstone London N20 9BH
Tel 020 3393 8531 Fax 020 8445 9411
uk@gentaur.com | Gentaur

 

 




GENTAUR France SARL
9, rue Lagrange, 75005 Paris
Tel 01 43 25 01 50

Fax 01 43 25 01 60
RCS Paris B 484 237 888

SIRET 48423788800017

BNP PARIBAS PARIS PL MAUBERT BIC BNPAFRPPPRG

france@gentaur.com | Gentaur

GENTAUR GmbH
Marienbongard 20
52062 Aachen Deutschland
Support Karolina Elandt
Tel: 0035929830070
Fax: (+49) 241 56 00 47 88

Logistic :0241 40 08 90 86
Bankleitzahl 39050000
IBAN lautet DE8839050000107569353
Handelsregister Aachen HR B 16058
Umsatzsteuer-Identifikationsnummer *** DE 815175831
Steuernummer 201/5961/3925
de@gentaur.com | Gentaur

GENTAUR U.S.A
Genprice Inc, Logistics
547, Yurok Circle
San Jose, CA 95123
CA 95123
Tel (408) 780-0908,
Fax (408) 780-0908,
sales@genprice.com

Genprice Inc, Invoices and accounting
6017 Snell Ave, Ste 357
San Jose, CA 95123




GENTAUR Nederland BV
NL850396268B01 KVK nummer 52327027
Kuiper 1
5521 DG Eersel Nederland
Tel:  0208-080893  Fax: 0497-517897
nl@gentaur.com | Gentaur
IBAN: NL04 RABO 0156 9854 62   SWIFT RABONL2U






GENTAUR Spain
tel:0911876558
spain@gentaur.com | Gentaur






ГЕНТАУЪР БЪЛГАРИЯ
ID # 201 358 931 /BULSTAT
София 1000, ул. "Граф Игнатиев" 53 вх. В, ет. 2
Tel 0035924682280 Fax 0035924808322
e-mail: Sofia@gentaur.com | Gentaur
IBAN: BG11FINV91501014771636
BIC: FINVBGSF

GENTAUR Poland Sp. z o.o.


ul. Grunwaldzka 88/A m.2
81-771 Sopot, Poland
TEL Gdansk 058 710 33 44 FAX  058 710 33 48              

poland@gentaur.com | Gentaur

Other countries

Österreich +43720880899

Canada Montreal +15149077481

Ceská republika Praha +420246019719

Danmark +4569918806

Finland Helsset +358942419041

Magyarország Budapest +3619980547

Ireland Dublin+35316526556

Luxembourg+35220880274

Norge Oslo+4721031366

Sverige Stockholm+46852503438

Schweiz Züri+41435006251

US New York+17185132983

GENTAUR Italy
SRL IVA IT03841300167
Piazza Giacomo Matteotti, 6
24122 Bergamo Tel 02 36 00 65 93
Fax 02 36 00 65 94
italia@gentaur.com | Gentaur