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Neurogenic differentiation factor 1 (NeuroD1) (Beta-cell E-box transcriptional activator 2) (Beta2)

 NDF1_MOUSE              Reviewed;         357 AA.
Q60867; Q545N9; Q60897;
01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
01-FEB-1997, sequence version 2.
12-SEP-2018, entry version 162.
RecName: Full=Neurogenic differentiation factor 1;
Short=NeuroD1;
AltName: Full=Beta-cell E-box transcriptional activator 2;
Short=Beta2;
Name=Neurod1; Synonyms=Neurod;
Mus musculus (Mouse).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
Muroidea; Muridae; Murinae; Mus; Mus.
NCBI_TaxID=10090;
[1]
NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA].
STRAIN=129/Sv, and MF1;
PubMed=7754368; DOI=10.1126/science.7754368;
Lee J.E., Hollenberg S.M., Snider L., Turner D.L., Lipnick N.,
Weintraub H.;
"Conversion of Xenopus ectoderm into neurons by NeuroD, a basic helix-
loop-helix protein.";
Science 268:836-844(1995).
[2]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
STRAIN=C57BL/6J; TISSUE=Cerebellum;
PubMed=16141072; DOI=10.1126/science.1112014;
Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
Hayashizaki Y.;
"The transcriptional landscape of the mammalian genome.";
Science 309:1559-1563(2005).
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
TISSUE=Eye;
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]
FUNCTION, DISRUPTION PHENOTYPE, TISSUE SPECIFICITY, AND DEVELOPMENTAL
STAGE.
PubMed=9308961; DOI=10.1101/gad.11.18.2323;
Naya F.J., Huang H.P., Qiu Y., Mutoh H., DeMayo F.J., Leiter A.B.,
Tsai M.J.;
"Diabetes, defective pancreatic morphogenesis, and abnormal
enteroendocrine differentiation in BETA2/neuroD-deficient mice.";
Genes Dev. 11:2323-2334(1997).
[5]
FUNCTION, INTERACTION WITH EP300, AND DNA-BINDING.
PubMed=9512516; DOI=10.1101/gad.12.6.820;
Mutoh H., Naya F.J., Tsai M.J., Leiter A.B.;
"The basic helix-loop-helix protein BETA2 interacts with p300 to
coordinate differentiation of secretin-expressing enteroendocrine
cells.";
Genes Dev. 12:820-830(1998).
[6]
FUNCTION, DISRUPTION PHENOTYPE, AND TISSUE SPECIFICITY.
PubMed=10398678; DOI=10.1101/gad.13.13.1647;
Miyata T., Maeda T., Lee J.E.;
"NeuroD is required for differentiation of the granule cells in the
cerebellum and hippocampus.";
Genes Dev. 13:1647-1652(1999).
[7]
FUNCTION, DISRUPTION PHENOTYPE, AND DEVELOPMENTAL STAGE.
PubMed=10639171; DOI=10.1073/pnas.97.2.865;
Liu M., Pleasure S.J., Collins A.E., Noebels J.L., Naya F.J.,
Tsai M.J., Lowenstein D.H.;
"Loss of BETA2/NeuroD leads to malformation of the dentate gyrus and
epilepsy.";
Proc. Natl. Acad. Sci. U.S.A. 97:865-870(2000).
[8]
FUNCTION, DISRUPTION PHENOTYPE, AND DEVELOPMENTAL STAGE.
PubMed=11152640;
Kim W.Y., Fritzsch B., Serls A., Bakel L.A., Huang E.J.,
Reichardt L.F., Barth D.S., Lee J.E.;
"NeuroD-null mice are deaf due to a severe loss of the inner ear
sensory neurons during development.";
Development 128:417-426(2001).
[9]
FUNCTION, AND TISSUE SPECIFICITY.
PubMed=11861467;
Inoue T., Hojo M., Bessho Y., Tano Y., Lee J.E., Kageyama R.;
"Math3 and NeuroD regulate amacrine cell fate specification in the
retina.";
Development 129:831-842(2002).
[10]
FUNCTION, MUTAGENESIS OF 274-SER--SER-278, AND DEVELOPMENTAL STAGE.
PubMed=11970861; DOI=10.1016/S0896-6273(02)00666-9;
Moore K.B., Schneider M.L., Vetter M.L.;
"Posttranslational mechanisms control the timing of bHLH function and
regulate retinal cell fate.";
Neuron 34:183-195(2002).
[11]
FUNCTION, HETERODIMERIZATION, PHOSPHORYLATION AT SER-162; SER-259;
SER-266 AND SER-274, TISSUE SPECIFICITY, AND MUTAGENESIS OF SER-162;
SER-259; SER-266 AND SER-274.
PubMed=12810726; DOI=10.1074/jbc.M301198200;
Khoo S., Griffen S.C., Xia Y., Baer R.J., German M.S., Cobb M.H.;
"Regulation of insulin gene transcription by ERK1 and ERK2 in
pancreatic beta cells.";
J. Biol. Chem. 278:32969-32977(2003).
[12]
FUNCTION, AND DNA-BINDING.
PubMed=14697366; DOI=10.1016/j.ydbio.2003.08.027;
Lin C.H., Stoeck J., Ravanpay A.C., Guillemot F., Tapscott S.J.,
Olson J.M.;
"Regulation of neuroD2 expression in mouse brain.";
Dev. Biol. 265:234-245(2004).
[13]
TISSUE SPECIFICITY.
PubMed=14752053; DOI=10.1210/me.2003-0311;
Kim J.Y., Chu K., Kim H.J., Seong H.A., Park K.C., Sanyal S.,
Takeda J., Ha H., Shong M., Tsai M.J., Choi H.S.;
"Orphan nuclear receptor small heterodimer partner, a novel
corepressor for a basic helix-loop-helix transcription factor
BETA2/neuroD.";
Mol. Endocrinol. 18:776-790(2004).
[14]
FUNCTION, PHOSPHORYLATION AT SER-259; SER-266 AND SER-274, AND
MUTAGENESIS OF SER-259; SER-266 AND SER-274.
PubMed=15797719; DOI=10.1016/j.mcn.2004.12.004;
Dufton C., Marcora E., Chae J.H., McCullough J., Eby J., Hausburg M.,
Stein G.H., Khoo S., Cobb M.H., Lee J.E.;
"Context-dependent regulation of NeuroD activity and protein
accumulation.";
Mol. Cell. Neurosci. 28:727-736(2005).
[15]
FUNCTION, AND ASSOCIATION WITH CHROMATIN.
PubMed=18007592; DOI=10.1038/sj.emboj.7601923;
Seo S., Lim J.W., Yellajoshyula D., Chang L.W., Kroll K.L.;
"Neurogenin and NeuroD direct transcriptional targets and their
regulatory enhancers.";
EMBO J. 26:5093-5108(2007).
[16]
FUNCTION, AND DISRUPTION PHENOTYPE.
PubMed=18339630; DOI=10.1074/jbc.M708692200;
Neptune E.R., Podowski M., Calvi C., Cho J.H., Garcia J.G., Tuder R.,
Linnoila R.I., Tsai M.J., Dietz H.C.;
"Targeted disruption of NeuroD, a proneural basic helix-loop-helix
factor, impairs distal lung formation and neuroendocrine morphology in
the neonatal lung.";
J. Biol. Chem. 283:21160-21169(2008).
[17]
INTERACTION WITH ATOH8.
PubMed=18560595; DOI=10.1371/journal.pone.0002430;
Lynn F.C., Sanchez L., Gomis R., German M.S., Gasa R.;
"Identification of the bHLH factor Math6 as a novel component of the
embryonic pancreas transcriptional network.";
PLoS ONE 3:E2430-E2430(2008).
[18]
FUNCTION.
PubMed=19200230; DOI=10.1111/j.1460-9568.2008.06595.x;
Roybon L., Deierborg T., Brundin P., Li J.Y.;
"Involvement of Ngn2, Tbr and NeuroD proteins during postnatal
olfactory bulb neurogenesis.";
Eur. J. Neurosci. 29:232-243(2009).
[19]
FUNCTION, INDUCTION, AND TISSUE SPECIFICITY.
PubMed=19759004; DOI=10.1074/jbc.M109.048694;
Anderson K.R., Torres C.A., Solomon K., Becker T.C., Newgard C.B.,
Wright C.V., Hagman J., Sussel L.;
"Cooperative transcriptional regulation of the essential pancreatic
islet gene NeuroD1 (beta2) by Nkx2.2 and neurogenin 3.";
J. Biol. Chem. 284:31236-31248(2009).
[20]
INDUCTION.
PubMed=19854889; DOI=10.1124/mol.109.060848;
Zheng H., Zeng Y., Zhang X., Chu J., Loh H.H., Law P.Y.;
"mu-Opioid receptor agonists differentially regulate the expression of
miR-190 and NeuroD.";
Mol. Pharmacol. 77:102-109(2010).
[21]
FUNCTION, AND DEVELOPMENTAL STAGE.
PubMed=21593321; DOI=10.1523/JNEUROSCI.2555-10.2011;
Cherry T.J., Wang S., Bormuth I., Schwab M., Olson J., Cepko C.L.;
"NeuroD factors regulate cell fate and neurite stratification in the
developing retina.";
J. Neurosci. 31:7365-7379(2011).
[22]
X-RAY CRYSTALLOGRAPHY (2.5 ANGSTROMS) OF 102-160 IN COMPLEX WITH TCF3
AND PROMOTER E-BOX DNA SEQUENCE, AND SUBUNIT.
PubMed=18069799; DOI=10.1021/bi701527r;
Longo A., Guanga G.P., Rose R.B.;
"Crystal structure of E47-NeuroD1/beta2 bHLH domain-DNA complex:
heterodimer selectivity and DNA recognition.";
Biochemistry 47:218-229(2008).
-!- FUNCTION: Acts as a transcriptional activator: mediates
transcriptional activation by binding to E box-containing promoter
consensus core sequences 5'-CANNTG-3'. Associates with the
p300/CBP transcription coactivator complex to stimulate
transcription of the secretin gene as well as the gene encoding
the cyclin-dependent kinase inhibitor CDKN1A. Contributes to the
regulation of several cell differentiation pathways, like those
that promote the formation of early retinal ganglion cells, inner
ear sensory neurons, granule cells forming either the cerebellum
or the dentate gyrus cell layer of the hippocampus, endocrine
islet cells of the pancreas and enteroendocrine cells of the small
intestine. Together with PAX6 or SIX3, is required for the
regulation of amacrine cell fate specification. Also required for
dendrite morphogenesis and maintenance in the cerebellar cortex.
Associates with chromatin to enhancer regulatory elements in genes
encoding key transcriptional regulators of neurogenesis.
{ECO:0000269|PubMed:10398678, ECO:0000269|PubMed:10639171,
ECO:0000269|PubMed:11152640, ECO:0000269|PubMed:11861467,
ECO:0000269|PubMed:11970861, ECO:0000269|PubMed:12810726,
ECO:0000269|PubMed:14697366, ECO:0000269|PubMed:15797719,
ECO:0000269|PubMed:18007592, ECO:0000269|PubMed:18339630,
ECO:0000269|PubMed:19200230, ECO:0000269|PubMed:19759004,
ECO:0000269|PubMed:21593321, ECO:0000269|PubMed:9308961,
ECO:0000269|PubMed:9512516}.
-!- SUBUNIT: Heterodimer with TCF3/E47; the heterodimer is inhibited
in presence of ID2, but not NR0B2, to E-box element. Interacts
with EP300; the interaction is inhibited by NR0B2. Interacts with
TCF3; the interaction is inhibited by ID2. Interacts with RREB1
(By similarity). Heterodimer with TCF3/E47. Efficient DNA-binding
requires dimerization with another bHLH protein. Interacts (via
helix-loop-helix motif domain) with EP300 (via C-terminus).
Interacts with ATOH8. {ECO:0000250, ECO:0000269|PubMed:18069799,
ECO:0000269|PubMed:18560595, ECO:0000269|PubMed:9512516}.
-!- INTERACTION:
O95273:CCNDBP1 (xeno); NbExp=4; IntAct=EBI-309315, EBI-748961;
-!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. Nucleus
{ECO:0000255|PROSITE-ProRule:PRU00981}. Note=In pancreatic islet
cells, shuttles to the nucleus in response to glucose stimulation.
Colocalizes with NR0B2 in the nucleus (By similarity).
{ECO:0000250}.
-!- TISSUE SPECIFICITY: Expressed in pancreatic beta cells, pulmonary
neuroendocrine cells and retinal interneurons amacrine cells (at
protein level). Expressed in endocrine cells of the pancreas.
Expressed in the inner layer of cerebellar external granular layer
(EGL). Expressed in the Ammon's horn (AH), which includes the CA1-
CA3 pyramidal layer and in granule cells of the dentate gyrus
(DG). Expressed in photoreceptors of the outer nuclear layer
(ONL), in a subset of cells in the lower half of the inner nuclear
layer (INL), and in a subset of cells in the ganglion cell layer
(GCL) of the retina. Expressed in cholinergic and AII amacrine
cell types. Expressed in differentiating neurons of both the
central and peripheral nervous systems.
{ECO:0000269|PubMed:10398678, ECO:0000269|PubMed:11861467,
ECO:0000269|PubMed:12810726, ECO:0000269|PubMed:14752053,
ECO:0000269|PubMed:19759004, ECO:0000269|PubMed:9308961}.
-!- DEVELOPMENTAL STAGE: Expressed in glucagon- and ghrelin-producing
cells of the pancreas at 14.5 dpc. Expressed in each of the
hormone-producing cells population of the pancreas, except
somatostatin-producing cells at 16.5 dpc (at protein level).
Expressed during embryonic development. Expressed in the earliest
islet precursor cells of the pancreas at 9.5 dpc. Expressed in
neuronal cells in the inner ear between 9.5 and 12.5 dpc.
Expressed within the otic epithelium and among the delaminating
cells migrating away from the ear to form sensory neurons at
E10.5. Expressed in the upper blade of the nascent dentate gyrus
at 16.5 dpc. {ECO:0000269|PubMed:10639171,
ECO:0000269|PubMed:11152640, ECO:0000269|PubMed:11970861,
ECO:0000269|PubMed:21593321, ECO:0000269|PubMed:9308961}.
-!- INDUCTION: Up-regulated by NKX2-2 and NEUROG3.
{ECO:0000269|PubMed:19759004, ECO:0000269|PubMed:19854889}.
-!- PTM: In islet cells, phosphorylated on Ser-274 upon glucose
stimulation; which may be required for nuclear localization. In
activated neurons, phosphorylated on Ser-336; which promotes
dendritic growth (By similarity). Phosphorylated by MAPK1;
phosphorylation regulates heterodimerization and DNA-binding
activities. Phosphorylation on Ser-266 and Ser-274 increases
transactivation on the insulin promoter in glucose-stimulated
insulinoma cells. {ECO:0000250, ECO:0000269|PubMed:12810726,
ECO:0000269|PubMed:15797719}.
-!- DISRUPTION PHENOTYPE: Mice are deaf and die shortly after birth
due to neonatal diabetes that results from developmental and
functional defects of the pancreatic endocrine cells. Show a loss
of enteroendocrine cells in the small intestine, airway and
alveolar epithelial cells in the lung, granular neuronal cells in
the cerebellum, hippocampal dentate gyrus and sensory neurons in
the inner ear due to extensive cell death that occurs during the
early stages of differentiation. {ECO:0000269|PubMed:10398678,
ECO:0000269|PubMed:10639171, ECO:0000269|PubMed:11152640,
ECO:0000269|PubMed:18339630, ECO:0000269|PubMed:9308961}.
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EMBL; U28068; AAC52203.1; -; mRNA.
EMBL; U28888; AAC52204.1; -; Genomic_DNA.
EMBL; AK005073; BAB23797.1; -; mRNA.
EMBL; AK018781; BAB31405.1; -; mRNA.
EMBL; BC018241; AAH18241.1; -; mRNA.
CCDS; CCDS16169.1; -.
PIR; I49338; I49338.
RefSeq; NP_035024.1; NM_010894.2.
UniGene; Mm.4636; -.
PDB; 2QL2; X-ray; 2.50 A; B/D=102-160.
PDBsum; 2QL2; -.
ProteinModelPortal; Q60867; -.
SMR; Q60867; -.
BioGrid; 201733; 10.
CORUM; Q60867; -.
IntAct; Q60867; 2.
MINT; Q60867; -.
STRING; 10090.ENSMUSP00000040364; -.
iPTMnet; Q60867; -.
PhosphoSitePlus; Q60867; -.
MaxQB; Q60867; -.
PaxDb; Q60867; -.
PRIDE; Q60867; -.
Ensembl; ENSMUST00000041099; ENSMUSP00000040364; ENSMUSG00000034701.
GeneID; 18012; -.
KEGG; mmu:18012; -.
UCSC; uc008kgt.1; mouse.
CTD; 4760; -.
MGI; MGI:1339708; Neurod1.
eggNOG; ENOG410IQ4I; Eukaryota.
eggNOG; ENOG410Z6FG; LUCA.
GeneTree; ENSGT00680000099860; -.
HOGENOM; HOG000049256; -.
HOVERGEN; HBG000250; -.
InParanoid; Q60867; -.
KO; K08033; -.
OMA; EEHETDK; -.
OrthoDB; EOG091G15AI; -.
PhylomeDB; Q60867; -.
TreeFam; TF315153; -.
EvolutionaryTrace; Q60867; -.
PRO; PR:Q60867; -.
Proteomes; UP000000589; Chromosome 2.
Bgee; ENSMUSG00000034701; Expressed in 194 organ(s), highest expression level in cerebellum lobe.
CleanEx; MM_NEUROD1; -.
Genevisible; Q60867; MM.
GO; GO:0005737; C:cytoplasm; IDA:MGI.
GO; GO:0005622; C:intracellular; IDA:MGI.
GO; GO:0005654; C:nucleoplasm; TAS:Reactome.
GO; GO:0005634; C:nucleus; IDA:MGI.
GO; GO:0090575; C:RNA polymerase II transcription factor complex; ISO:MGI.
GO; GO:0003682; F:chromatin binding; IDA:UniProtKB.
GO; GO:0003677; F:DNA binding; IDA:MGI.
GO; GO:0003700; F:DNA-binding transcription factor activity; ISO:MGI.
GO; GO:0003690; F:double-stranded DNA binding; ISO:MGI.
GO; GO:0070888; F:E-box binding; IDA:UniProtKB.
GO; GO:0046982; F:protein heterodimerization activity; IPI:MGI.
GO; GO:0001102; F:RNA polymerase II activating transcription factor binding; ISO:MGI.
GO; GO:0000978; F:RNA polymerase II proximal promoter sequence-specific DNA binding; IDA:NTNU_SB.
GO; GO:0043565; F:sequence-specific DNA binding; IDA:MGI.
GO; GO:0003713; F:transcription coactivator activity; ISO:MGI.
GO; GO:0008134; F:transcription factor binding; ISO:MGI.
GO; GO:0001077; F:transcriptional activator activity, RNA polymerase II proximal promoter sequence-specific DNA binding; IDA:NTNU_SB.
GO; GO:0035881; P:amacrine cell differentiation; IDA:UniProtKB.
GO; GO:0009952; P:anterior/posterior pattern specification; IMP:MGI.
GO; GO:0043010; P:camera-type eye development; IGI:MGI.
GO; GO:0045165; P:cell fate commitment; IGI:MGI.
GO; GO:0071333; P:cellular response to glucose stimulus; ISO:MGI.
GO; GO:0021549; P:cerebellum development; IMP:UniProtKB.
GO; GO:0021542; P:dentate gyrus development; IMP:UniProtKB.
GO; GO:0048562; P:embryonic organ morphogenesis; IMP:BHF-UCL.
GO; GO:0031018; P:endocrine pancreas development; IMP:UniProtKB.
GO; GO:0035883; P:enteroendocrine cell differentiation; IMP:UniProtKB.
GO; GO:0042593; P:glucose homeostasis; IMP:BHF-UCL.
GO; GO:0030902; P:hindbrain development; IMP:MGI.
GO; GO:0048839; P:inner ear development; IMP:UniProtKB.
GO; GO:0030073; P:insulin secretion; ISO:MGI.
GO; GO:0046426; P:negative regulation of JAK-STAT cascade; IDA:MGI.
GO; GO:2000675; P:negative regulation of type B pancreatic cell apoptotic process; IMP:BHF-UCL.
GO; GO:0048666; P:neuron development; IEA:InterPro.
GO; GO:0007263; P:nitric oxide mediated signal transduction; ISO:MGI.
GO; GO:0006913; P:nucleocytoplasmic transport; ISO:MGI.
GO; GO:0003326; P:pancreatic A cell fate commitment; IGI:MGI.
GO; GO:0003329; P:pancreatic PP cell fate commitment; IGI:MGI.
GO; GO:0043065; P:positive regulation of apoptotic process; IDA:UniProtKB.
GO; GO:0045597; P:positive regulation of cell differentiation; IDA:UniProtKB.
GO; GO:0051091; P:positive regulation of DNA-binding transcription factor activity; IDA:UniProtKB.
GO; GO:0045666; P:positive regulation of neuron differentiation; IDA:UniProtKB.
GO; GO:0045944; P:positive regulation of transcription by RNA polymerase II; IDA:UniProtKB.
GO; GO:2000679; P:positive regulation of transcription regulatory region DNA binding; ISO:MGI.
GO; GO:0045893; P:positive regulation of transcription, DNA-templated; IDA:UniProtKB.
GO; GO:0071156; P:regulation of cell cycle arrest; IMP:UniProtKB.
GO; GO:0060730; P:regulation of intestinal epithelial structure maintenance; IDA:UniProtKB.
GO; GO:0045664; P:regulation of neuron differentiation; IGI:MGI.
GO; GO:0042493; P:response to drug; IEA:Ensembl.
GO; GO:0009749; P:response to glucose; ISO:MGI.
GO; GO:0023019; P:signal transduction involved in regulation of gene expression; IDA:MGI.
CDD; cd00083; HLH; 1.
Gene3D; 4.10.280.10; -; 1.
InterPro; IPR011598; bHLH_dom.
InterPro; IPR036638; HLH_DNA-bd_sf.
InterPro; IPR032652; Neurod1.
InterPro; IPR022575; Neurogenic_DUF.
InterPro; IPR016637; TF_bHLH_NeuroD.
PANTHER; PTHR19290:SF88; PTHR19290:SF88; 1.
Pfam; PF00010; HLH; 1.
Pfam; PF12533; Neuro_bHLH; 1.
PIRSF; PIRSF015618; bHLH_NeuroD; 1.
SMART; SM00353; HLH; 1.
SUPFAM; SSF47459; SSF47459; 1.
PROSITE; PS50888; BHLH; 1.
1: Evidence at protein level;
3D-structure; Activator; Complete proteome; Cytoplasm;
Developmental protein; Differentiation; DNA-binding; Neurogenesis;
Nucleus; Phosphoprotein; Reference proteome; Transcription;
Transcription regulation.
CHAIN 1 357 Neurogenic differentiation factor 1.
/FTId=PRO_0000127383.
DOMAIN 101 153 bHLH. {ECO:0000255|PROSITE-
ProRule:PRU00981}.
MOTIF 87 93 Nuclear localization signal.
{ECO:0000255}.
COMPBIAS 58 77 Glu-rich (acidic).
COMPBIAS 58 64 Poly-Glu.
COMPBIAS 67 77 Poly-Glu.
COMPBIAS 87 90 Poly-Lys.
MOD_RES 162 162 Phosphoserine.
{ECO:0000269|PubMed:12810726}.
MOD_RES 259 259 Phosphoserine.
{ECO:0000269|PubMed:12810726,
ECO:0000269|PubMed:15797719}.
MOD_RES 266 266 Phosphoserine.
{ECO:0000269|PubMed:12810726,
ECO:0000269|PubMed:15797719}.
MOD_RES 274 274 Phosphoserine.
{ECO:0000269|PubMed:12810726,
ECO:0000269|PubMed:15797719}.
MOD_RES 336 336 Phosphoserine; by CaMK2.
{ECO:0000250|UniProtKB:Q64289}.
MUTAGEN 162 162 S->A: Reduces weakly phosphorylation.
Reduces strongly phosphorylation; when
associated with A-259 and A-266.
{ECO:0000269|PubMed:12810726}.
MUTAGEN 259 259 S->A: Reduces weakly phosphorylation.
Reduces strongly phosphorylation; when
associated with A-162 and A-266. Reduces
transactivation on the insulin promoter
in glucose-stimulated insulinoma cells;
when associated with A-266 and A-274.
{ECO:0000269|PubMed:12810726,
ECO:0000269|PubMed:15797719}.
MUTAGEN 266 266 S->A: Reduces weakly phosphorylation.
Reduces strongly phosphorylation; when
associated with A-162 and A-259. Reduces
transactivation on the insulin promoter
in glucose-stimulated insulinoma cells;
when associated with A-259 and A-274.
{ECO:0000269|PubMed:12810726,
ECO:0000269|PubMed:15797719}.
MUTAGEN 274 274 S->A: Reduces strongly phosphorylation.
Reduces transactivation on the insulin
promoter in glucose-stimulated insulinoma
cells; when associated with A-259 and A-
266. {ECO:0000269|PubMed:12810726,
ECO:0000269|PubMed:15797719}.
MUTAGEN 279 279 I->V: Promotes the formation of
differentiated late retinal amacrine
cells.
HELIX 102 126 {ECO:0000244|PDB:2QL2}.
STRAND 128 130 {ECO:0000244|PDB:2QL2}.
STRAND 133 135 {ECO:0000244|PDB:2QL2}.
HELIX 139 156 {ECO:0000244|PDB:2QL2}.
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


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