NDF1_MOUSE
ID NDF1_MOUSE Reviewed; 357 AA.
AC Q60867; Q545N9; Q60897;
DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-1997, sequence version 2.
DT 03-AUG-2022, entry version 184.
DE RecName: Full=Neurogenic differentiation factor 1;
DE Short=NeuroD1;
DE AltName: Full=Beta-cell E-box transcriptional activator 2;
DE Short=Beta2;
GN Name=Neurod1; Synonyms=Neurod;
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA].
RC STRAIN=129/Sv, and MF1;
RX PubMed=7754368; DOI=10.1126/science.7754368;
RA Lee J.E., Hollenberg S.M., Snider L., Turner D.L., Lipnick N.,
RA Weintraub H.;
RT "Conversion of Xenopus ectoderm into neurons by NeuroD, a basic helix-loop-
RT helix protein.";
RL Science 268:836-844(1995).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J; TISSUE=Cerebellum;
RX PubMed=16141072; DOI=10.1126/science.1112014;
RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT "The transcriptional landscape of the mammalian genome.";
RL Science 309:1559-1563(2005).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Eye;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [4]
RP FUNCTION, DISRUPTION PHENOTYPE, TISSUE SPECIFICITY, AND DEVELOPMENTAL
RP STAGE.
RX PubMed=9308961; DOI=10.1101/gad.11.18.2323;
RA Naya F.J., Huang H.P., Qiu Y., Mutoh H., DeMayo F.J., Leiter A.B.,
RA Tsai M.J.;
RT "Diabetes, defective pancreatic morphogenesis, and abnormal enteroendocrine
RT differentiation in BETA2/neuroD-deficient mice.";
RL Genes Dev. 11:2323-2334(1997).
RN [5]
RP FUNCTION, INTERACTION WITH EP300, AND DNA-BINDING.
RX PubMed=9512516; DOI=10.1101/gad.12.6.820;
RA Mutoh H., Naya F.J., Tsai M.J., Leiter A.B.;
RT "The basic helix-loop-helix protein BETA2 interacts with p300 to coordinate
RT differentiation of secretin-expressing enteroendocrine cells.";
RL Genes Dev. 12:820-830(1998).
RN [6]
RP FUNCTION, DISRUPTION PHENOTYPE, AND TISSUE SPECIFICITY.
RX PubMed=10398678; DOI=10.1101/gad.13.13.1647;
RA Miyata T., Maeda T., Lee J.E.;
RT "NeuroD is required for differentiation of the granule cells in the
RT cerebellum and hippocampus.";
RL Genes Dev. 13:1647-1652(1999).
RN [7]
RP FUNCTION, DISRUPTION PHENOTYPE, AND DEVELOPMENTAL STAGE.
RX PubMed=10639171; DOI=10.1073/pnas.97.2.865;
RA Liu M., Pleasure S.J., Collins A.E., Noebels J.L., Naya F.J., Tsai M.J.,
RA Lowenstein D.H.;
RT "Loss of BETA2/NeuroD leads to malformation of the dentate gyrus and
RT epilepsy.";
RL Proc. Natl. Acad. Sci. U.S.A. 97:865-870(2000).
RN [8]
RP FUNCTION, DISRUPTION PHENOTYPE, AND DEVELOPMENTAL STAGE.
RX PubMed=11152640; DOI=10.1242/dev.128.3.417;
RA Kim W.Y., Fritzsch B., Serls A., Bakel L.A., Huang E.J., Reichardt L.F.,
RA Barth D.S., Lee J.E.;
RT "NeuroD-null mice are deaf due to a severe loss of the inner ear sensory
RT neurons during development.";
RL Development 128:417-426(2001).
RN [9]
RP FUNCTION, AND TISSUE SPECIFICITY.
RX PubMed=11861467; DOI=10.1242/dev.129.4.831;
RA Inoue T., Hojo M., Bessho Y., Tano Y., Lee J.E., Kageyama R.;
RT "Math3 and NeuroD regulate amacrine cell fate specification in the
RT retina.";
RL Development 129:831-842(2002).
RN [10]
RP FUNCTION, MUTAGENESIS OF 274-SER--SER-278, AND DEVELOPMENTAL STAGE.
RX PubMed=11970861; DOI=10.1016/s0896-6273(02)00666-9;
RA Moore K.B., Schneider M.L., Vetter M.L.;
RT "Posttranslational mechanisms control the timing of bHLH function and
RT regulate retinal cell fate.";
RL Neuron 34:183-195(2002).
RN [11]
RP FUNCTION, HETERODIMERIZATION, PHOSPHORYLATION AT SER-162; SER-259; SER-266
RP AND SER-274, TISSUE SPECIFICITY, AND MUTAGENESIS OF SER-162; SER-259;
RP SER-266 AND SER-274.
RX PubMed=12810726; DOI=10.1074/jbc.m301198200;
RA Khoo S., Griffen S.C., Xia Y., Baer R.J., German M.S., Cobb M.H.;
RT "Regulation of insulin gene transcription by ERK1 and ERK2 in pancreatic
RT beta cells.";
RL J. Biol. Chem. 278:32969-32977(2003).
RN [12]
RP FUNCTION, AND DNA-BINDING.
RX PubMed=14697366; DOI=10.1016/j.ydbio.2003.08.027;
RA Lin C.H., Stoeck J., Ravanpay A.C., Guillemot F., Tapscott S.J.,
RA Olson J.M.;
RT "Regulation of neuroD2 expression in mouse brain.";
RL Dev. Biol. 265:234-245(2004).
RN [13]
RP TISSUE SPECIFICITY.
RX PubMed=14752053; DOI=10.1210/me.2003-0311;
RA Kim J.Y., Chu K., Kim H.J., Seong H.A., Park K.C., Sanyal S., Takeda J.,
RA Ha H., Shong M., Tsai M.J., Choi H.S.;
RT "Orphan nuclear receptor small heterodimer partner, a novel corepressor for
RT a basic helix-loop-helix transcription factor BETA2/neuroD.";
RL Mol. Endocrinol. 18:776-790(2004).
RN [14]
RP FUNCTION, PHOSPHORYLATION AT SER-259; SER-266 AND SER-274, AND MUTAGENESIS
RP OF SER-259; SER-266 AND SER-274.
RX PubMed=15797719; DOI=10.1016/j.mcn.2004.12.004;
RA Dufton C., Marcora E., Chae J.H., McCullough J., Eby J., Hausburg M.,
RA Stein G.H., Khoo S., Cobb M.H., Lee J.E.;
RT "Context-dependent regulation of NeuroD activity and protein
RT accumulation.";
RL Mol. Cell. Neurosci. 28:727-736(2005).
RN [15]
RP FUNCTION, AND ASSOCIATION WITH CHROMATIN.
RX PubMed=18007592; DOI=10.1038/sj.emboj.7601923;
RA Seo S., Lim J.W., Yellajoshyula D., Chang L.W., Kroll K.L.;
RT "Neurogenin and NeuroD direct transcriptional targets and their regulatory
RT enhancers.";
RL EMBO J. 26:5093-5108(2007).
RN [16]
RP FUNCTION, AND DISRUPTION PHENOTYPE.
RX PubMed=18339630; DOI=10.1074/jbc.m708692200;
RA Neptune E.R., Podowski M., Calvi C., Cho J.H., Garcia J.G., Tuder R.,
RA Linnoila R.I., Tsai M.J., Dietz H.C.;
RT "Targeted disruption of NeuroD, a proneural basic helix-loop-helix factor,
RT impairs distal lung formation and neuroendocrine morphology in the neonatal
RT lung.";
RL J. Biol. Chem. 283:21160-21169(2008).
RN [17]
RP INTERACTION WITH ATOH8.
RX PubMed=18560595; DOI=10.1371/journal.pone.0002430;
RA Lynn F.C., Sanchez L., Gomis R., German M.S., Gasa R.;
RT "Identification of the bHLH factor Math6 as a novel component of the
RT embryonic pancreas transcriptional network.";
RL PLoS ONE 3:E2430-E2430(2008).
RN [18]
RP FUNCTION.
RX PubMed=19200230; DOI=10.1111/j.1460-9568.2008.06595.x;
RA Roybon L., Deierborg T., Brundin P., Li J.Y.;
RT "Involvement of Ngn2, Tbr and NeuroD proteins during postnatal olfactory
RT bulb neurogenesis.";
RL Eur. J. Neurosci. 29:232-243(2009).
RN [19]
RP FUNCTION, INDUCTION, AND TISSUE SPECIFICITY.
RX PubMed=19759004; DOI=10.1074/jbc.m109.048694;
RA Anderson K.R., Torres C.A., Solomon K., Becker T.C., Newgard C.B.,
RA Wright C.V., Hagman J., Sussel L.;
RT "Cooperative transcriptional regulation of the essential pancreatic islet
RT gene NeuroD1 (beta2) by Nkx2.2 and neurogenin 3.";
RL J. Biol. Chem. 284:31236-31248(2009).
RN [20]
RP INDUCTION.
RX PubMed=19854889; DOI=10.1124/mol.109.060848;
RA Zheng H., Zeng Y., Zhang X., Chu J., Loh H.H., Law P.Y.;
RT "mu-Opioid receptor agonists differentially regulate the expression of miR-
RT 190 and NeuroD.";
RL Mol. Pharmacol. 77:102-109(2010).
RN [21]
RP FUNCTION, AND DEVELOPMENTAL STAGE.
RX PubMed=21593321; DOI=10.1523/jneurosci.2555-10.2011;
RA Cherry T.J., Wang S., Bormuth I., Schwab M., Olson J., Cepko C.L.;
RT "NeuroD factors regulate cell fate and neurite stratification in the
RT developing retina.";
RL J. Neurosci. 31:7365-7379(2011).
RN [22]
RP INTERACTION WITH TCF3.
RX PubMed=23395635; DOI=10.1016/j.celrep.2013.01.017;
RA Davies O.R., Lin C.Y., Radzisheuskaya A., Zhou X., Taube J., Blin G.,
RA Waterhouse A., Smith A.J., Lowell S.;
RT "Tcf15 primes pluripotent cells for differentiation.";
RL Cell Rep. 3:472-484(2013).
RN [23]
RP X-RAY CRYSTALLOGRAPHY (2.5 ANGSTROMS) OF 102-160 IN COMPLEX WITH TCF3 AND
RP PROMOTER E-BOX DNA SEQUENCE, AND SUBUNIT.
RX PubMed=18069799; DOI=10.1021/bi701527r;
RA Longo A., Guanga G.P., Rose R.B.;
RT "Crystal structure of E47-NeuroD1/beta2 bHLH domain-DNA complex:
RT heterodimer selectivity and DNA recognition.";
RL Biochemistry 47:218-229(2008).
CC -!- FUNCTION: Acts as a transcriptional activator: mediates transcriptional
CC activation by binding to E box-containing promoter consensus core
CC sequences 5'-CANNTG-3'. Associates with the p300/CBP transcription
CC coactivator complex to stimulate transcription of the secretin gene as
CC well as the gene encoding the cyclin-dependent kinase inhibitor CDKN1A.
CC Contributes to the regulation of several cell differentiation pathways,
CC like those that promote the formation of early retinal ganglion cells,
CC inner ear sensory neurons, granule cells forming either the cerebellum
CC or the dentate gyrus cell layer of the hippocampus, endocrine islet
CC cells of the pancreas and enteroendocrine cells of the small intestine.
CC Together with PAX6 or SIX3, is required for the regulation of amacrine
CC cell fate specification. Also required for dendrite morphogenesis and
CC maintenance in the cerebellar cortex. Associates with chromatin to
CC enhancer regulatory elements in genes encoding key transcriptional
CC regulators of neurogenesis. {ECO:0000269|PubMed:10398678,
CC ECO:0000269|PubMed:10639171, ECO:0000269|PubMed:11152640,
CC ECO:0000269|PubMed:11861467, ECO:0000269|PubMed:11970861,
CC ECO:0000269|PubMed:12810726, ECO:0000269|PubMed:14697366,
CC ECO:0000269|PubMed:15797719, ECO:0000269|PubMed:18007592,
CC ECO:0000269|PubMed:18339630, ECO:0000269|PubMed:19200230,
CC ECO:0000269|PubMed:19759004, ECO:0000269|PubMed:21593321,
CC ECO:0000269|PubMed:9308961, ECO:0000269|PubMed:9512516}.
CC -!- SUBUNIT: Efficient DNA-binding requires dimerization with another bHLH
CC protein (PubMed:12810726, PubMed:18069799). Heterodimer with TCF3/E47;
CC the heterodimer is inhibited in presence of ID2, but not NR0B2, to E-
CC box element (PubMed:18069799, PubMed:23395635). Interacts with EP300;
CC the interaction is inhibited by NR0B2 (PubMed:9512516). Interacts with
CC RREB1 (By similarity). Interacts with ATOH8 (PubMed:18560595).
CC {ECO:0000250|UniProtKB:Q13562, ECO:0000269|PubMed:12810726,
CC ECO:0000269|PubMed:18069799, ECO:0000269|PubMed:18560595,
CC ECO:0000269|PubMed:23395635, ECO:0000269|PubMed:9512516}.
CC -!- INTERACTION:
CC Q60867; O95273: CCNDBP1; Xeno; NbExp=4; IntAct=EBI-309315, EBI-748961;
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. Nucleus
CC {ECO:0000255|PROSITE-ProRule:PRU00981}. Note=In pancreatic islet cells,
CC shuttles to the nucleus in response to glucose stimulation. Colocalizes
CC with NR0B2 in the nucleus (By similarity). {ECO:0000250}.
CC -!- TISSUE SPECIFICITY: Expressed in pancreatic beta cells, pulmonary
CC neuroendocrine cells and retinal interneurons amacrine cells (at
CC protein level). Expressed in endocrine cells of the pancreas. Expressed
CC in the inner layer of cerebellar external granular layer (EGL).
CC Expressed in the Ammon's horn (AH), which includes the CA1-CA3
CC pyramidal layer and in granule cells of the dentate gyrus (DG).
CC Expressed in photoreceptors of the outer nuclear layer (ONL), in a
CC subset of cells in the lower half of the inner nuclear layer (INL), and
CC in a subset of cells in the ganglion cell layer (GCL) of the retina.
CC Expressed in cholinergic and AII amacrine cell types. Expressed in
CC differentiating neurons of both the central and peripheral nervous
CC systems. {ECO:0000269|PubMed:10398678, ECO:0000269|PubMed:11861467,
CC ECO:0000269|PubMed:12810726, ECO:0000269|PubMed:14752053,
CC ECO:0000269|PubMed:19759004, ECO:0000269|PubMed:9308961}.
CC -!- DEVELOPMENTAL STAGE: Expressed in glucagon- and ghrelin-producing cells
CC of the pancreas at 14.5 dpc. Expressed in each of the hormone-producing
CC cells population of the pancreas, except somatostatin-producing cells
CC at 16.5 dpc (at protein level). Expressed during embryonic development.
CC Expressed in the earliest islet precursor cells of the pancreas at 9.5
CC dpc. Expressed in neuronal cells in the inner ear between 9.5 and 12.5
CC dpc. Expressed within the otic epithelium and among the delaminating
CC cells migrating away from the ear to form sensory neurons at 10.5 dpc.
CC Expressed in the upper blade of the nascent dentate gyrus at 16.5 dpc.
CC {ECO:0000269|PubMed:10639171, ECO:0000269|PubMed:11152640,
CC ECO:0000269|PubMed:11970861, ECO:0000269|PubMed:21593321,
CC ECO:0000269|PubMed:9308961}.
CC -!- INDUCTION: Up-regulated by NKX2-2 and NEUROG3.
CC {ECO:0000269|PubMed:19759004, ECO:0000269|PubMed:19854889}.
CC -!- PTM: In islet cells, phosphorylated on Ser-274 upon glucose
CC stimulation; which may be required for nuclear localization. In
CC activated neurons, phosphorylated on Ser-336; which promotes dendritic
CC growth (By similarity). Phosphorylated by MAPK1; phosphorylation
CC regulates heterodimerization and DNA-binding activities.
CC Phosphorylation on Ser-266 and Ser-274 increases transactivation on the
CC insulin promoter in glucose-stimulated insulinoma cells. {ECO:0000250,
CC ECO:0000269|PubMed:12810726, ECO:0000269|PubMed:15797719}.
CC -!- DISRUPTION PHENOTYPE: Mice are deaf and die shortly after birth due to
CC neonatal diabetes that results from developmental and functional
CC defects of the pancreatic endocrine cells. Show a loss of
CC enteroendocrine cells in the small intestine, airway and alveolar
CC epithelial cells in the lung, granular neuronal cells in the
CC cerebellum, hippocampal dentate gyrus and sensory neurons in the inner
CC ear due to extensive cell death that occurs during the early stages of
CC differentiation. {ECO:0000269|PubMed:10398678,
CC ECO:0000269|PubMed:10639171, ECO:0000269|PubMed:11152640,
CC ECO:0000269|PubMed:18339630, ECO:0000269|PubMed:9308961}.
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DR EMBL; U28068; AAC52203.1; -; mRNA.
DR EMBL; U28888; AAC52204.1; -; Genomic_DNA.
DR EMBL; AK005073; BAB23797.1; -; mRNA.
DR EMBL; AK018781; BAB31405.1; -; mRNA.
DR EMBL; BC018241; AAH18241.1; -; mRNA.
DR CCDS; CCDS16169.1; -.
DR PIR; I49338; I49338.
DR RefSeq; NP_035024.1; NM_010894.2.
DR PDB; 2QL2; X-ray; 2.50 A; B/D=102-160.
DR PDBsum; 2QL2; -.
DR AlphaFoldDB; Q60867; -.
DR SMR; Q60867; -.
DR BioGRID; 201733; 12.
DR CORUM; Q60867; -.
DR IntAct; Q60867; 4.
DR MINT; Q60867; -.
DR STRING; 10090.ENSMUSP00000040364; -.
DR iPTMnet; Q60867; -.
DR PhosphoSitePlus; Q60867; -.
DR MaxQB; Q60867; -.
DR PaxDb; Q60867; -.
DR PRIDE; Q60867; -.
DR ProteomicsDB; 287623; -.
DR Antibodypedia; 922; 533 antibodies from 38 providers.
DR DNASU; 18012; -.
DR Ensembl; ENSMUST00000041099; ENSMUSP00000040364; ENSMUSG00000034701.
DR GeneID; 18012; -.
DR KEGG; mmu:18012; -.
DR UCSC; uc008kgt.1; mouse.
DR CTD; 4760; -.
DR MGI; MGI:1339708; Neurod1.
DR VEuPathDB; HostDB:ENSMUSG00000034701; -.
DR eggNOG; KOG3898; Eukaryota.
DR GeneTree; ENSGT00940000160478; -.
DR HOGENOM; CLU_055134_0_0_1; -.
DR InParanoid; Q60867; -.
DR OMA; FKHEPAA; -.
DR OrthoDB; 1096531at2759; -.
DR PhylomeDB; Q60867; -.
DR TreeFam; TF315153; -.
DR BioGRID-ORCS; 18012; 2 hits in 74 CRISPR screens.
DR EvolutionaryTrace; Q60867; -.
DR PRO; PR:Q60867; -.
DR Proteomes; UP000000589; Chromosome 2.
DR RNAct; Q60867; protein.
DR Bgee; ENSMUSG00000034701; Expressed in cerebellum lobe and 155 other tissues.
DR Genevisible; Q60867; MM.
DR GO; GO:0005737; C:cytoplasm; IDA:MGI.
DR GO; GO:0005634; C:nucleus; IDA:MGI.
DR GO; GO:0090575; C:RNA polymerase II transcription regulator complex; ISO:MGI.
DR GO; GO:0003682; F:chromatin binding; IDA:UniProtKB.
DR GO; GO:0003677; F:DNA binding; IDA:MGI.
DR GO; GO:0001228; F:DNA-binding transcription activator activity, RNA polymerase II-specific; IDA:NTNU_SB.
DR GO; GO:0003700; F:DNA-binding transcription factor activity; ISO:MGI.
DR GO; GO:0000981; F:DNA-binding transcription factor activity, RNA polymerase II-specific; ISO:MGI.
DR GO; GO:0003690; F:double-stranded DNA binding; ISO:MGI.
DR GO; GO:0070888; F:E-box binding; IDA:UniProtKB.
DR GO; GO:0046982; F:protein heterodimerization activity; ISO:MGI.
DR GO; GO:0000978; F:RNA polymerase II cis-regulatory region sequence-specific DNA binding; IDA:NTNU_SB.
DR GO; GO:0061629; F:RNA polymerase II-specific DNA-binding transcription factor binding; ISO:MGI.
DR GO; GO:0043565; F:sequence-specific DNA binding; IDA:MGI.
DR GO; GO:1990837; F:sequence-specific double-stranded DNA binding; ISO:MGI.
DR GO; GO:0035881; P:amacrine cell differentiation; IDA:UniProtKB.
DR GO; GO:0009952; P:anterior/posterior pattern specification; IMP:MGI.
DR GO; GO:0043010; P:camera-type eye development; IGI:MGI.
DR GO; GO:0045165; P:cell fate commitment; IGI:MGI.
DR GO; GO:0071333; P:cellular response to glucose stimulus; ISO:MGI.
DR GO; GO:0021549; P:cerebellum development; IMP:UniProtKB.
DR GO; GO:0021542; P:dentate gyrus development; IMP:UniProtKB.
DR GO; GO:0048562; P:embryonic organ morphogenesis; IMP:BHF-UCL.
DR GO; GO:0031018; P:endocrine pancreas development; IMP:UniProtKB.
DR GO; GO:0035883; P:enteroendocrine cell differentiation; IMP:UniProtKB.
DR GO; GO:0042593; P:glucose homeostasis; IMP:BHF-UCL.
DR GO; GO:0030902; P:hindbrain development; IMP:MGI.
DR GO; GO:0048839; P:inner ear development; IMP:UniProtKB.
DR GO; GO:0030073; P:insulin secretion; ISO:MGI.
DR GO; GO:0046426; P:negative regulation of receptor signaling pathway via JAK-STAT; IDA:MGI.
DR GO; GO:2000675; P:negative regulation of type B pancreatic cell apoptotic process; IMP:BHF-UCL.
DR GO; GO:0048666; P:neuron development; IEA:InterPro.
DR GO; GO:0030182; P:neuron differentiation; IBA:GO_Central.
DR GO; GO:0007263; P:nitric oxide mediated signal transduction; ISO:MGI.
DR GO; GO:0006913; P:nucleocytoplasmic transport; ISO:MGI.
DR GO; GO:0003326; P:pancreatic A cell fate commitment; IGI:MGI.
DR GO; GO:0003329; P:pancreatic PP cell fate commitment; IGI:MGI.
DR GO; GO:0043065; P:positive regulation of apoptotic process; IDA:UniProtKB.
DR GO; GO:0045597; P:positive regulation of cell differentiation; IDA:UniProtKB.
DR GO; GO:0051091; P:positive regulation of DNA-binding transcription factor activity; IDA:UniProtKB.
DR GO; GO:0045666; P:positive regulation of neuron differentiation; IDA:UniProtKB.
DR GO; GO:0045944; P:positive regulation of transcription by RNA polymerase II; IDA:UniProtKB.
DR GO; GO:2000679; P:positive regulation of transcription regulatory region DNA binding; ISO:MGI.
DR GO; GO:0045893; P:positive regulation of transcription, DNA-templated; IDA:UniProtKB.
DR GO; GO:0007259; P:receptor signaling pathway via JAK-STAT; IDA:MGI.
DR GO; GO:0060730; P:regulation of intestinal epithelial structure maintenance; IDA:UniProtKB.
DR GO; GO:0045664; P:regulation of neuron differentiation; IGI:MGI.
DR GO; GO:0006357; P:regulation of transcription by RNA polymerase II; IBA:GO_Central.
DR GO; GO:0009749; P:response to glucose; ISO:MGI.
DR GO; GO:0009410; P:response to xenobiotic stimulus; IEA:Ensembl.
DR GO; GO:0023019; P:signal transduction involved in regulation of gene expression; IDA:MGI.
DR GO; GO:0006366; P:transcription by RNA polymerase II; IMP:MGI.
DR Gene3D; 4.10.280.10; -; 1.
DR InterPro; IPR011598; bHLH_dom.
DR InterPro; IPR036638; HLH_DNA-bd_sf.
DR InterPro; IPR032652; Neurod1.
DR InterPro; IPR022575; Neurogenic_DUF.
DR InterPro; IPR016637; TF_bHLH_NeuroD.
DR PANTHER; PTHR19290:SF88; PTHR19290:SF88; 1.
DR Pfam; PF00010; HLH; 1.
DR Pfam; PF12533; Neuro_bHLH; 1.
DR PIRSF; PIRSF015618; bHLH_NeuroD; 1.
DR SMART; SM00353; HLH; 1.
DR SUPFAM; SSF47459; SSF47459; 1.
DR PROSITE; PS50888; BHLH; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Activator; Cytoplasm; Developmental protein; Differentiation;
KW DNA-binding; Neurogenesis; Nucleus; Phosphoprotein; Reference proteome;
KW Transcription; Transcription regulation.
FT CHAIN 1..357
FT /note="Neurogenic differentiation factor 1"
FT /id="PRO_0000127383"
FT DOMAIN 101..153
FT /note="bHLH"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00981"
FT REGION 1..94
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 87..93
FT /note="Nuclear localization signal"
FT /evidence="ECO:0000255"
FT COMPBIAS 27..53
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 54..76
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 162
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:12810726"
FT MOD_RES 259
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:12810726,
FT ECO:0000269|PubMed:15797719"
FT MOD_RES 266
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:12810726,
FT ECO:0000269|PubMed:15797719"
FT MOD_RES 274
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:12810726,
FT ECO:0000269|PubMed:15797719"
FT MOD_RES 336
FT /note="Phosphoserine; by CaMK2"
FT /evidence="ECO:0000250|UniProtKB:Q64289"
FT MUTAGEN 162
FT /note="S->A: Reduces weakly phosphorylation. Reduces
FT strongly phosphorylation; when associated with A-259 and A-
FT 266."
FT /evidence="ECO:0000269|PubMed:12810726"
FT MUTAGEN 259
FT /note="S->A: Reduces weakly phosphorylation. Reduces
FT strongly phosphorylation; when associated with A-162 and A-
FT 266. Reduces transactivation on the insulin promoter in
FT glucose-stimulated insulinoma cells; when associated with
FT A-266 and A-274."
FT /evidence="ECO:0000269|PubMed:12810726,
FT ECO:0000269|PubMed:15797719"
FT MUTAGEN 266
FT /note="S->A: Reduces weakly phosphorylation. Reduces
FT strongly phosphorylation; when associated with A-162 and A-
FT 259. Reduces transactivation on the insulin promoter in
FT glucose-stimulated insulinoma cells; when associated with
FT A-259 and A-274."
FT /evidence="ECO:0000269|PubMed:12810726,
FT ECO:0000269|PubMed:15797719"
FT MUTAGEN 274
FT /note="S->A: Reduces strongly phosphorylation. Reduces
FT transactivation on the insulin promoter in glucose-
FT stimulated insulinoma cells; when associated with A-259 and
FT A-266."
FT /evidence="ECO:0000269|PubMed:12810726,
FT ECO:0000269|PubMed:15797719"
FT MUTAGEN 279
FT /note="I->V: Promotes the formation of differentiated late
FT retinal amacrine cells."
FT HELIX 102..126
FT /evidence="ECO:0007829|PDB:2QL2"
FT STRAND 128..130
FT /evidence="ECO:0007829|PDB:2QL2"
FT STRAND 133..135
FT /evidence="ECO:0007829|PDB:2QL2"
FT HELIX 139..156
FT /evidence="ECO:0007829|PDB:2QL2"
SQ SEQUENCE 357 AA; 39999 MW; B6626E1315E31027 CRC64;
MTKSYSESGL MGEPQPQGPP SWTDECLSSQ DEEHEADKKE DELEAMNAEE DSLRNGGEEE
EEDEDLEEEE EEEEEEEDQK PKRRGPKKKK MTKARLERFK LRRMKANARE RNRMHGLNAA
LDNLRKVVPC YSKTQKLSKI ETLRLAKNYI WALSEILRSG KSPDLVSFVQ TLCKGLSQPT
TNLVAGCLQL NPRTFLPEQN PDMPPHLPTA SASFPVHPYS YQSPGLPSPP YGTMDSSHVF
HVKPPPHAYS AALEPFFESP LTDCTSPSFD GPLSPPLSIN GNFSFKHEPS AEFEKNYAFT
MHYPAATLAG PQSHGSIFSS GAAAPRCEIP IDNIMSFDSH SHHERVMSAQ LNAIFHD
