HES1_HUMAN
ID HES1_HUMAN Reviewed; 280 AA.
AC Q14469; Q6FHB2;
DT 15-DEC-1998, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1996, sequence version 1.
DT 03-AUG-2022, entry version 198.
DE RecName: Full=Transcription factor HES-1;
DE AltName: Full=Class B basic helix-loop-helix protein 39;
DE Short=bHLHb39;
DE AltName: Full=Hairy and enhancer of split 1;
DE AltName: Full=Hairy homolog;
DE AltName: Full=Hairy-like protein;
DE Short=hHL;
GN Name=HES1; Synonyms=BHLHB39, HL, HRY;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=8020957; DOI=10.1006/geno.1994.1126;
RA Feder J.N., Li L., Jan L.Y., Jan Y.-N.;
RT "Genomic cloning and chromosomal localization of HRY, the human homolog to
RT the Drosophila segmentation gene, hairy.";
RL Genomics 20:56-61(1994).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC TISSUE=Kidney;
RA Yao J., Yeung S., Sun H., Chen N.;
RT "Functional analysis of human HRY in Drosophila.";
RL Submitted (MAY-2000) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RX PubMed=14702039; DOI=10.1038/ng1285;
RA Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
RA Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
RA Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
RA Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
RA Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H.,
RA Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M.,
RA Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K.,
RA Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T.,
RA Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M.,
RA Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S.,
RA Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H.,
RA Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K.,
RA Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N.,
RA Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
RA Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
RA Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
RA Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
RA Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y.,
RA Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K.,
RA Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T.,
RA Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T.,
RA Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y.,
RA Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H.,
RA Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y.,
RA Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H.,
RA Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O.,
RA Isogai T., Sugano S.;
RT "Complete sequencing and characterization of 21,243 full-length human
RT cDNAs.";
RL Nat. Genet. 36:40-45(2004).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RA Ebert L., Schick M., Neubert P., Schatten R., Henze S., Korn B.;
RT "Cloning of human full open reading frames in Gateway(TM) system entry
RT vector (pDONR201).";
RL Submitted (JUN-2004) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP INTERACTION WITH SIRT1.
RX PubMed=12535671; DOI=10.1016/s0006-291x(02)03020-6;
RA Takata T., Ishikawa F.;
RT "Human Sir2-related protein SIRT1 associates with the bHLH repressors HES1
RT and HEY2 and is involved in HES1- and HEY2-mediated transcriptional
RT repression.";
RL Biochem. Biophys. Res. Commun. 301:250-257(2003).
RN [6]
RP FUNCTION, AND INTERACTION WITH FA COMPLEX.
RX PubMed=18550849; DOI=10.1182/blood-2008-04-152710;
RA Tremblay C.S., Huang F.F., Habi O., Huard C.C., Godin C., Levesque G.,
RA Carreau M.;
RT "HES1 is a novel interactor of the Fanconi anemia core complex.";
RL Blood 112:2062-2070(2008).
RN [7]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=19413330; DOI=10.1021/ac9004309;
RA Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J., Mohammed S.;
RT "Lys-N and trypsin cover complementary parts of the phosphoproteome in a
RT refined SCX-based approach.";
RL Anal. Chem. 81:4493-4501(2009).
RN [8]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Erythroleukemia;
RX PubMed=23186163; DOI=10.1021/pr300630k;
RA Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J.,
RA Mohammed S.;
RT "Toward a comprehensive characterization of a human cancer cell
RT phosphoproteome.";
RL J. Proteome Res. 12:260-271(2013).
RN [9]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Liver;
RX PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014;
RA Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., Wang L.,
RA Ye M., Zou H.;
RT "An enzyme assisted RP-RPLC approach for in-depth analysis of human liver
RT phosphoproteome.";
RL J. Proteomics 96:253-262(2014).
CC -!- FUNCTION: Transcriptional repressor of genes that require a bHLH
CC protein for their transcription. May act as a negative regulator of
CC myogenesis by inhibiting the functions of MYOD1 and ASH1. Binds DNA on
CC N-box motifs: 5'-CACNAG-3' with high affinity and on E-box motifs: 5'-
CC CANNTG-3' with low affinity (By similarity). May play a role in a
CC functional FA core complex response to DNA cross-link damage, being
CC required for the stability and nuclear localization of FA core complex
CC proteins, as well as for FANCD2 monoubiquitination in response to DNA
CC damage. {ECO:0000250, ECO:0000269|PubMed:18550849}.
CC -!- SUBUNIT: Transcription repression requires formation of a complex with
CC a corepressor protein of the Groucho/TLE family. Interacts (via WPRW
CC motif) with TLE1, and more weakly with TLE2. Interacts with HES6 (By
CC similarity). Interacts with SIRT1. Interacts with an FA complex,
CC composed of FANCA, FANCF, FANCG and FANCL, but not of FANCC, nor FANCE.
CC {ECO:0000250, ECO:0000269|PubMed:12535671,
CC ECO:0000269|PubMed:18550849}.
CC -!- INTERACTION:
CC Q14469; Q96EB6: SIRT1; NbExp=4; IntAct=EBI-2832522, EBI-1802965;
CC -!- SUBCELLULAR LOCATION: Nucleus.
CC -!- DOMAIN: Has a particular type of basic domain (presence of a helix-
CC interrupting proline) that binds to the N-box (CACNAG), rather than the
CC canonical E-box (CANNTG).
CC -!- DOMAIN: The C-terminal WRPW motif is a transcriptional repression
CC domain necessary for the interaction with Groucho/TLE family members,
CC transcriptional corepressors recruited to specific target DNA by Hairy-
CC related proteins. {ECO:0000250}.
CC -!- DOMAIN: The bHLH, as well as cooperation between the central Orange
CC domain and the C-terminal WRPW motif, is required for transcriptional
CC repressor activity. {ECO:0000250}.
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DR EMBL; L19314; AAA65220.1; -; Genomic_DNA.
DR EMBL; AF264785; AAF73060.1; -; mRNA.
DR EMBL; AK000415; BAA91149.1; -; mRNA.
DR EMBL; CR541843; CAG46641.1; -; mRNA.
DR CCDS; CCDS3305.1; -.
DR PIR; A53027; A53027.
DR RefSeq; NP_005515.1; NM_005524.3.
DR PDB; 2MH3; NMR; -; A/B=27-95.
DR PDB; 7C4O; NMR; -; A/B=103-150.
DR PDBsum; 2MH3; -.
DR PDBsum; 7C4O; -.
DR AlphaFoldDB; Q14469; -.
DR BMRB; Q14469; -.
DR SMR; Q14469; -.
DR BioGRID; 109514; 48.
DR CORUM; Q14469; -.
DR ELM; Q14469; -.
DR IntAct; Q14469; 16.
DR MINT; Q14469; -.
DR STRING; 9606.ENSP00000232424; -.
DR ChEMBL; CHEMBL3734643; -.
DR iPTMnet; Q14469; -.
DR PhosphoSitePlus; Q14469; -.
DR BioMuta; HES1; -.
DR DMDM; 3913825; -.
DR EPD; Q14469; -.
DR jPOST; Q14469; -.
DR MassIVE; Q14469; -.
DR MaxQB; Q14469; -.
DR PaxDb; Q14469; -.
DR PeptideAtlas; Q14469; -.
DR PRIDE; Q14469; -.
DR ProteomicsDB; 60000; -.
DR Antibodypedia; 19442; 656 antibodies from 40 providers.
DR DNASU; 3280; -.
DR Ensembl; ENST00000232424.4; ENSP00000232424.3; ENSG00000114315.4.
DR GeneID; 3280; -.
DR KEGG; hsa:3280; -.
DR MANE-Select; ENST00000232424.4; ENSP00000232424.3; NM_005524.4; NP_005515.1.
DR UCSC; uc003ftq.3; human.
DR CTD; 3280; -.
DR DisGeNET; 3280; -.
DR GeneCards; HES1; -.
DR HGNC; HGNC:5192; HES1.
DR HPA; ENSG00000114315; Low tissue specificity.
DR MIM; 139605; gene.
DR neXtProt; NX_Q14469; -.
DR OpenTargets; ENSG00000114315; -.
DR PharmGKB; PA29465; -.
DR VEuPathDB; HostDB:ENSG00000114315; -.
DR eggNOG; KOG4304; Eukaryota.
DR GeneTree; ENSGT00940000159619; -.
DR HOGENOM; CLU_068550_1_0_1; -.
DR InParanoid; Q14469; -.
DR OMA; HLANCMS; -.
DR OrthoDB; 1427802at2759; -.
DR PhylomeDB; Q14469; -.
DR TreeFam; TF351373; -.
DR PathwayCommons; Q14469; -.
DR Reactome; R-HSA-210744; Regulation of gene expression in late stage (branching morphogenesis) pancreatic bud precursor cells.
DR Reactome; R-HSA-2122947; NOTCH1 Intracellular Domain Regulates Transcription.
DR Reactome; R-HSA-2197563; NOTCH2 intracellular domain regulates transcription.
DR Reactome; R-HSA-2644606; Constitutive Signaling by NOTCH1 PEST Domain Mutants.
DR Reactome; R-HSA-2894862; Constitutive Signaling by NOTCH1 HD+PEST Domain Mutants.
DR Reactome; R-HSA-8940973; RUNX2 regulates osteoblast differentiation.
DR Reactome; R-HSA-8941856; RUNX3 regulates NOTCH signaling.
DR Reactome; R-HSA-9013508; NOTCH3 Intracellular Domain Regulates Transcription.
DR Reactome; R-HSA-9013695; NOTCH4 Intracellular Domain Regulates Transcription.
DR SignaLink; Q14469; -.
DR SIGNOR; Q14469; -.
DR BioGRID-ORCS; 3280; 34 hits in 1118 CRISPR screens.
DR ChiTaRS; HES1; human.
DR GeneWiki; HES1; -.
DR GenomeRNAi; 3280; -.
DR Pharos; Q14469; Tbio.
DR PRO; PR:Q14469; -.
DR Proteomes; UP000005640; Chromosome 3.
DR RNAct; Q14469; protein.
DR Bgee; ENSG00000114315; Expressed in renal medulla and 203 other tissues.
DR Genevisible; Q14469; HS.
DR GO; GO:0000785; C:chromatin; IEA:Ensembl.
DR GO; GO:0005737; C:cytoplasm; IEA:Ensembl.
DR GO; GO:0016363; C:nuclear matrix; IEA:Ensembl.
DR GO; GO:0005654; C:nucleoplasm; IDA:HPA.
DR GO; GO:0005634; C:nucleus; ISS:UniProtKB.
DR GO; GO:0032991; C:protein-containing complex; IEA:Ensembl.
DR GO; GO:0051087; F:chaperone binding; IEA:Ensembl.
DR GO; GO:0003682; F:chromatin binding; IEA:Ensembl.
DR GO; GO:0003677; F:DNA binding; TAS:ProtInc.
DR GO; GO:0000981; F:DNA-binding transcription factor activity, RNA polymerase II-specific; IBA:GO_Central.
DR GO; GO:0001227; F:DNA-binding transcription repressor activity, RNA polymerase II-specific; ISS:UniProtKB.
DR GO; GO:0070888; F:E-box binding; ISS:ARUK-UCL.
DR GO; GO:0042826; F:histone deacetylase binding; IPI:BHF-UCL.
DR GO; GO:0043398; F:HLH domain binding; IEA:Ensembl.
DR GO; GO:0008432; F:JUN kinase binding; IEA:Ensembl.
DR GO; GO:0071820; F:N-box binding; ISS:UniProtKB.
DR GO; GO:0042803; F:protein homodimerization activity; ISS:UniProtKB.
DR GO; GO:0044877; F:protein-containing complex binding; IEA:Ensembl.
DR GO; GO:0000978; F:RNA polymerase II cis-regulatory region sequence-specific DNA binding; IBA:GO_Central.
DR GO; GO:0061629; F:RNA polymerase II-specific DNA-binding transcription factor binding; ISS:ARUK-UCL.
DR GO; GO:0043565; F:sequence-specific DNA binding; ISS:UniProtKB.
DR GO; GO:1990837; F:sequence-specific double-stranded DNA binding; IDA:ARUK-UCL.
DR GO; GO:0001222; F:transcription corepressor binding; IEA:Ensembl.
DR GO; GO:0021984; P:adenohypophysis development; IEA:Ensembl.
DR GO; GO:0035881; P:amacrine cell differentiation; IEA:Ensembl.
DR GO; GO:0009952; P:anterior/posterior pattern specification; IBA:GO_Central.
DR GO; GO:0048844; P:artery morphogenesis; ISS:BHF-UCL.
DR GO; GO:0035910; P:ascending aorta morphogenesis; ISS:BHF-UCL.
DR GO; GO:0030509; P:BMP signaling pathway; IEA:Ensembl.
DR GO; GO:0021870; P:Cajal-Retzius cell differentiation; IEA:Ensembl.
DR GO; GO:0061309; P:cardiac neural crest cell development involved in outflow tract morphogenesis; IEA:Ensembl.
DR GO; GO:0007155; P:cell adhesion; IEA:Ensembl.
DR GO; GO:0001709; P:cell fate determination; IEA:Ensembl.
DR GO; GO:0048469; P:cell maturation; IEA:Ensembl.
DR GO; GO:0016477; P:cell migration; IEA:Ensembl.
DR GO; GO:0048667; P:cell morphogenesis involved in neuron differentiation; IEA:Ensembl.
DR GO; GO:0071398; P:cellular response to fatty acid; IEA:Ensembl.
DR GO; GO:0071347; P:cellular response to interleukin-1; IEA:Ensembl.
DR GO; GO:1990090; P:cellular response to nerve growth factor stimulus; IEA:Ensembl.
DR GO; GO:0071356; P:cellular response to tumor necrosis factor; IEA:Ensembl.
DR GO; GO:0090102; P:cochlea development; IEA:Ensembl.
DR GO; GO:0072049; P:comma-shaped body morphogenesis; IEA:Ensembl.
DR GO; GO:0061009; P:common bile duct development; IEA:Ensembl.
DR GO; GO:0003143; P:embryonic heart tube morphogenesis; ISS:BHF-UCL.
DR GO; GO:0090162; P:establishment of epithelial cell polarity; IEA:Ensembl.
DR GO; GO:0021861; P:forebrain radial glial cell differentiation; ISS:UniProtKB.
DR GO; GO:0072012; P:glomerulus vasculature development; IEA:Ensembl.
DR GO; GO:0021575; P:hindbrain morphogenesis; IEA:Ensembl.
DR GO; GO:0042491; P:inner ear auditory receptor cell differentiation; IEA:Ensembl.
DR GO; GO:0060122; P:inner ear receptor cell stereocilium organization; IEA:Ensembl.
DR GO; GO:0060716; P:labyrinthine layer blood vessel development; IEA:Ensembl.
DR GO; GO:0046331; P:lateral inhibition; IEA:Ensembl.
DR GO; GO:0001889; P:liver development; IEA:Ensembl.
DR GO; GO:0030324; P:lung development; IEA:Ensembl.
DR GO; GO:0072282; P:metanephric nephron tubule morphogenesis; IEA:Ensembl.
DR GO; GO:0030901; P:midbrain development; IEA:Ensembl.
DR GO; GO:0021555; P:midbrain-hindbrain boundary morphogenesis; IEA:Ensembl.
DR GO; GO:1902870; P:negative regulation of amacrine cell differentiation; IEA:Ensembl.
DR GO; GO:0090281; P:negative regulation of calcium ion import; IEA:Ensembl.
DR GO; GO:1905934; P:negative regulation of cell fate determination; IEA:Ensembl.
DR GO; GO:0043433; P:negative regulation of DNA-binding transcription factor activity; ISS:ARUK-UCL.
DR GO; GO:2000978; P:negative regulation of forebrain neuron differentiation; ISS:UniProtKB.
DR GO; GO:0010629; P:negative regulation of gene expression; IEA:Ensembl.
DR GO; GO:0060253; P:negative regulation of glial cell proliferation; ISS:UniProtKB.
DR GO; GO:0045608; P:negative regulation of inner ear auditory receptor cell differentiation; IEA:Ensembl.
DR GO; GO:0045665; P:negative regulation of neuron differentiation; IBA:GO_Central.
DR GO; GO:0010977; P:negative regulation of neuron projection development; IEA:Ensembl.
DR GO; GO:0048715; P:negative regulation of oligodendrocyte differentiation; ISS:UniProtKB.
DR GO; GO:2000227; P:negative regulation of pancreatic A cell differentiation; IEA:Ensembl.
DR GO; GO:2000974; P:negative regulation of pro-B cell differentiation; IMP:UniProtKB.
DR GO; GO:2000737; P:negative regulation of stem cell differentiation; IMP:UniProtKB.
DR GO; GO:0061106; P:negative regulation of stomach neuroendocrine cell differentiation; IEA:Ensembl.
DR GO; GO:0000122; P:negative regulation of transcription by RNA polymerase II; IDA:UniProtKB.
DR GO; GO:0045892; P:negative regulation of transcription, DNA-templated; IDA:BHF-UCL.
DR GO; GO:0007399; P:nervous system development; TAS:ProtInc.
DR GO; GO:0097150; P:neuronal stem cell population maintenance; IEP:UniProtKB.
DR GO; GO:0007219; P:Notch signaling pathway; IDA:UniProtKB.
DR GO; GO:0021557; P:oculomotor nerve development; IEA:Ensembl.
DR GO; GO:0003151; P:outflow tract morphogenesis; ISS:BHF-UCL.
DR GO; GO:0003310; P:pancreatic A cell differentiation; IEA:Ensembl.
DR GO; GO:0061626; P:pharyngeal arch artery morphogenesis; ISS:BHF-UCL.
DR GO; GO:0048711; P:positive regulation of astrocyte differentiation; ISS:UniProtKB.
DR GO; GO:0030513; P:positive regulation of BMP signaling pathway; IEA:Ensembl.
DR GO; GO:0008284; P:positive regulation of cell population proliferation; ISS:BHF-UCL.
DR GO; GO:0043388; P:positive regulation of DNA binding; ISS:UniProtKB.
DR GO; GO:0010628; P:positive regulation of gene expression; IEA:Ensembl.
DR GO; GO:0045977; P:positive regulation of mitotic cell cycle, embryonic; ISS:BHF-UCL.
DR GO; GO:0045747; P:positive regulation of Notch signaling pathway; IEA:Ensembl.
DR GO; GO:0046427; P:positive regulation of receptor signaling pathway via JAK-STAT; ISS:UniProtKB.
DR GO; GO:0042102; P:positive regulation of T cell proliferation; IEA:Ensembl.
DR GO; GO:0045944; P:positive regulation of transcription by RNA polymerase II; ISS:BHF-UCL.
DR GO; GO:0042531; P:positive regulation of tyrosine phosphorylation of STAT protein; ISS:UniProtKB.
DR GO; GO:0065003; P:protein-containing complex assembly; ISS:UniProtKB.
DR GO; GO:0050678; P:regulation of epithelial cell proliferation; IEA:Ensembl.
DR GO; GO:0045598; P:regulation of fat cell differentiation; IEA:Ensembl.
DR GO; GO:0050767; P:regulation of neurogenesis; IBA:GO_Central.
DR GO; GO:0043254; P:regulation of protein-containing complex assembly; IEA:Ensembl.
DR GO; GO:0046425; P:regulation of receptor signaling pathway via JAK-STAT; ISS:UniProtKB.
DR GO; GO:0003266; P:regulation of secondary heart field cardioblast proliferation; IEA:Ensembl.
DR GO; GO:0060164; P:regulation of timing of neuron differentiation; IEA:Ensembl.
DR GO; GO:0006357; P:regulation of transcription by RNA polymerase II; IBA:GO_Central.
DR GO; GO:0072141; P:renal interstitial fibroblast development; IEA:Ensembl.
DR GO; GO:0043279; P:response to alkaloid; IEA:Ensembl.
DR GO; GO:0014070; P:response to organic cyclic compound; IEA:Ensembl.
DR GO; GO:0097066; P:response to thyroid hormone; IEA:Ensembl.
DR GO; GO:0072050; P:S-shaped body morphogenesis; IEA:Ensembl.
DR GO; GO:0007224; P:smoothened signaling pathway; IEA:Ensembl.
DR GO; GO:0035019; P:somatic stem cell population maintenance; IEA:Ensembl.
DR GO; GO:0061102; P:stomach neuroendocrine cell differentiation; IEA:Ensembl.
DR GO; GO:0042098; P:T cell proliferation; IEA:Ensembl.
DR GO; GO:0021537; P:telencephalon development; IEA:Ensembl.
DR GO; GO:0048538; P:thymus development; ISS:BHF-UCL.
DR GO; GO:0021558; P:trochlear nerve development; IEA:Ensembl.
DR GO; GO:0060675; P:ureteric bud morphogenesis; IEA:Ensembl.
DR GO; GO:0097084; P:vascular associated smooth muscle cell development; ISS:BHF-UCL.
DR GO; GO:0003281; P:ventricular septum development; ISS:BHF-UCL.
DR GO; GO:0060412; P:ventricular septum morphogenesis; ISS:BHF-UCL.
DR Gene3D; 4.10.280.10; -; 1.
DR IDEAL; IID00211; -.
DR InterPro; IPR011598; bHLH_dom.
DR InterPro; IPR036638; HLH_DNA-bd_sf.
DR InterPro; IPR003650; Orange_dom.
DR Pfam; PF07527; Hairy_orange; 1.
DR Pfam; PF00010; HLH; 1.
DR SMART; SM00353; HLH; 1.
DR SMART; SM00511; ORANGE; 1.
DR SUPFAM; SSF47459; SSF47459; 1.
DR PROSITE; PS50888; BHLH; 1.
DR PROSITE; PS51054; ORANGE; 1.
PE 1: Evidence at protein level;
KW 3D-structure; DNA-binding; Nucleus; Reference proteome; Repressor;
KW Transcription; Transcription regulation.
FT CHAIN 1..280
FT /note="Transcription factor HES-1"
FT /id="PRO_0000127202"
FT DOMAIN 34..91
FT /note="bHLH"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00981"
FT DOMAIN 110..143
FT /note="Orange"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00380"
FT REGION 1..44
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 157..200
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 254..280
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 275..278
FT /note="WRPW motif"
FT COMPBIAS 10..27
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 28..44
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 160..198
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 254..271
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT STRAND 31..33
FT /evidence="ECO:0007829|PDB:2MH3"
FT HELIX 40..65
FT /evidence="ECO:0007829|PDB:2MH3"
FT HELIX 71..73
FT /evidence="ECO:0007829|PDB:2MH3"
FT HELIX 77..93
FT /evidence="ECO:0007829|PDB:2MH3"
FT HELIX 104..125
FT /evidence="ECO:0007829|PDB:7C4O"
FT HELIX 133..149
FT /evidence="ECO:0007829|PDB:7C4O"
SQ SEQUENCE 280 AA; 29541 MW; F9342A88FC749E3C CRC64;
MPADIMEKNS SSPVAATPAS VNTTPDKPKT ASEHRKSSKP IMEKRRRARI NESLSQLKTL
ILDALKKDSS RHSKLEKADI LEMTVKHLRN LQRAQMTAAL STDPSVLGKY RAGFSECMNE
VTRFLSTCEG VNTEVRTRLL GHLANCMTQI NAMTYPGQPH PALQAPPPPP PGPGGPQHAP
FAPPPPLVPI PGGAAPPPGG APCKLGSQAG EAAKVFGGFQ VVPAPDGQFA FLIPNGAFAH
SGPVIPVYTS NSGTSVGPNA VSPSSGPSLT ADSMWRPWRN
