NDF1_HUMAN
ID NDF1_HUMAN Reviewed; 356 AA.
AC Q13562; B2R9I8; F1T0E1; O00343; Q13340; Q5U095; Q96TH0; Q99455; Q9UEC8;
DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT 02-NOV-2010, sequence version 3.
DT 03-AUG-2022, entry version 203.
DE RecName: Full=Neurogenic differentiation factor 1;
DE Short=NeuroD;
DE Short=NeuroD1;
DE AltName: Full=Class A basic helix-loop-helix protein 3;
DE Short=bHLHa3;
GN Name=NEUROD1; Synonyms=BHLHA3, NEUROD;
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], AND VARIANT ALA-45.
RX PubMed=8786144; DOI=10.1006/geno.1996.0306;
RA Tamimi R., Steingrimsson E., Copeland N.G., Dyer-Montgomery K., Lee J.E.,
RA Hernandez R., Jenkins N.A., Tapscott S.J.;
RT "The NEUROD gene maps to human chromosome 2q32 and mouse chromosome 2.";
RL Genomics 34:418-421(1996).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA], AND VARIANT ALA-45.
RX PubMed=8915591; DOI=10.1016/s0169-328x(96)00154-4;
RA Yokoyama M., Nishi Y., Miyamoto Y., Nakamura M., Akiyama K., Matsubara K.,
RA Okubo K.;
RT "Molecular cloning of a human neuroD from a neuroblastoma cell line
RT specifically expressed in the fetal brain and adult cerebellum.";
RL Brain Res. Mol. Brain Res. 42:135-139(1996).
RN [3]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND VARIANT ALA-45.
RA Furuta H., Horikawa Y., Iwasaki N., Hara M., Sussel L., le Beau M.M.,
RA Davis E.M., Ogata M., Iwamoto Y., German M.S., Bell G.I.;
RL Submitted (JAN-1998) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND VARIANT ALA-45.
RX PubMed=10366743; DOI=10.1016/s0169-328x(99)00112-6;
RA Miyachi T., Maruyama H., Kitamura T., Nakamura S., Kawakami H.;
RT "Structure and regulation of the human NeuroD (BETA2/BHF1) gene.";
RL Brain Res. Mol. Brain Res. 69:223-231(1999).
RN [5]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND VARIANT ALA-45.
RA Noma T.;
RL Submitted (DEC-1997) to the EMBL/GenBank/DDBJ databases.
RN [6]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND VARIANT ALA-45.
RA Kuroe A., Yamada Y., Kubota A., Someya Y., Iwakura T., Watanabe R.,
RA Inada A., Miyawaki K., Ban N., Ihara Y., Seino Y.;
RT "Ala45Thr mutation of the human BETA2 gene.";
RL Submitted (JUL-1998) to the EMBL/GenBank/DDBJ databases.
RN [7]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RA Kalnine N., Chen X., Rolfs A., Halleck A., Hines L., Eisenstein S.,
RA Koundinya M., Raphael J., Moreira D., Kelley T., LaBaer J., Lin Y.,
RA Phelan M., Farmer A.;
RT "Cloning of human full-length CDSs in BD Creator(TM) system donor vector.";
RL Submitted (OCT-2004) to the EMBL/GenBank/DDBJ databases.
RN [8]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA], AND VARIANT ALA-45.
RC TISSUE=Cerebellum;
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 [9]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA], AND VARIANT ALA-45.
RX PubMed=21697133; DOI=10.1167/iovs.11-7479;
RA Oshikawa M., Tsutsui C., Ikegami T., Fuchida Y., Matsubara M., Toyama S.,
RA Usami R., Ohtoko K., Kato S.;
RT "Full-length transcriptome analysis of human retina-derived cell lines
RT ARPE-19 and Y79 using the vector-capping method.";
RL Invest. Ophthalmol. Vis. Sci. 52:6662-6670(2011).
RN [10]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=15815621; DOI=10.1038/nature03466;
RA Hillier L.W., Graves T.A., Fulton R.S., Fulton L.A., Pepin K.H., Minx P.,
RA Wagner-McPherson C., Layman D., Wylie K., Sekhon M., Becker M.C.,
RA Fewell G.A., Delehaunty K.D., Miner T.L., Nash W.E., Kremitzki C., Oddy L.,
RA Du H., Sun H., Bradshaw-Cordum H., Ali J., Carter J., Cordes M., Harris A.,
RA Isak A., van Brunt A., Nguyen C., Du F., Courtney L., Kalicki J.,
RA Ozersky P., Abbott S., Armstrong J., Belter E.A., Caruso L., Cedroni M.,
RA Cotton M., Davidson T., Desai A., Elliott G., Erb T., Fronick C., Gaige T.,
RA Haakenson W., Haglund K., Holmes A., Harkins R., Kim K., Kruchowski S.S.,
RA Strong C.M., Grewal N., Goyea E., Hou S., Levy A., Martinka S., Mead K.,
RA McLellan M.D., Meyer R., Randall-Maher J., Tomlinson C.,
RA Dauphin-Kohlberg S., Kozlowicz-Reilly A., Shah N., Swearengen-Shahid S.,
RA Snider J., Strong J.T., Thompson J., Yoakum M., Leonard S., Pearman C.,
RA Trani L., Radionenko M., Waligorski J.E., Wang C., Rock S.M.,
RA Tin-Wollam A.-M., Maupin R., Latreille P., Wendl M.C., Yang S.-P., Pohl C.,
RA Wallis J.W., Spieth J., Bieri T.A., Berkowicz N., Nelson J.O., Osborne J.,
RA Ding L., Meyer R., Sabo A., Shotland Y., Sinha P., Wohldmann P.E.,
RA Cook L.L., Hickenbotham M.T., Eldred J., Williams D., Jones T.A., She X.,
RA Ciccarelli F.D., Izaurralde E., Taylor J., Schmutz J., Myers R.M.,
RA Cox D.R., Huang X., McPherson J.D., Mardis E.R., Clifton S.W., Warren W.C.,
RA Chinwalla A.T., Eddy S.R., Marra M.A., Ovcharenko I., Furey T.S.,
RA Miller W., Eichler E.E., Bork P., Suyama M., Torrents D., Waterston R.H.,
RA Wilson R.K.;
RT "Generation and annotation of the DNA sequences of human chromosomes 2 and
RT 4.";
RL Nature 434:724-731(2005).
RN [11]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA], AND VARIANT ALA-45.
RA Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M.,
RA Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J.,
RA Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S.,
RA Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H.,
RA Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K.,
RA Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D.,
RA Hunkapiller M.W., Myers E.W., Venter J.C.;
RL Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
RN [12]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA], AND VARIANT ALA-45.
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 [13]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 88-200.
RC TISSUE=Retina;
RX PubMed=9144558; DOI=10.1006/bbrc.1997.6483;
RA Acharya H.R., Dooley C.M., Thoreson W.B., Ahmad I.;
RT "cDNA cloning and expression analysis of NeuroD mRNA in human retina.";
RL Biochem. Biophys. Res. Commun. 233:459-463(1997).
RN [14]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 147-198.
RC TISSUE=Rhabdomyosarcoma;
RA Shum C.H., Triche T.J.;
RL Submitted (SEP-1995) to the EMBL/GenBank/DDBJ databases.
RN [15]
RP INTERACTION WITH RREB1.
RX PubMed=12482979; DOI=10.1128/mcb.23.1.259-271.2003;
RA Ray S.K., Nishitani J., Petry M.W., Fessing M.Y., Leiter A.B.;
RT "Novel transcriptional potentiation of BETA2/NeuroD on the secretin gene
RT promoter by the DNA-binding protein Finb/RREB-1.";
RL Mol. Cell. Biol. 23:259-271(2003).
RN [16]
RP INTERACTION WITH NR0B2; EP300 AND TCF3, HETERODIMERIZATION, TISSUE
RP SPECIFICITY, AND SUBCELLULAR LOCATION.
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 [17]
RP INVOLVEMENT IN MODY6 AND NIDDM, AND VARIANT NIDDM LEU-111.
RX PubMed=10545951; DOI=10.1038/15500;
RA Malecki M.T., Jhala U.S., Antonellis A., Fields L., Doria A., Orban T.,
RA Saad M., Warram J.H., Montminy M., Krolewski A.S.;
RT "Mutations in NEUROD1 are associated with the development of type 2
RT diabetes mellitus.";
RL Nat. Genet. 23:323-328(1999).
RN [18]
RP VARIANT MODY6 LYS-110.
RX PubMed=11719843; DOI=10.1007/s001250100016;
RA Kristinsson S.Y., Thorolfsdottir E.T., Talseth B., Steingrimsson E.,
RA Thorsson A.V., Helgason T., Hreidarsson A.B., Arngrimsson R.;
RT "MODY in Iceland is associated with mutations in HNF-1alpha and a novel
RT mutation in NeuroD1.";
RL Diabetologia 44:2098-2103(2001).
RN [19]
RP VARIANT ILE-242.
RX PubMed=25477324; DOI=10.1167/iovs.14-15382;
RA Wang F., Li H., Xu M., Li H., Zhao L., Yang L., Zaneveld J.E., Wang K.,
RA Li Y., Sui R., Chen R.;
RT "A homozygous missense mutation in NEUROD1 is associated with nonsyndromic
RT autosomal recessive retinitis pigmentosa.";
RL Invest. Ophthalmol. Vis. Sci. 56:150-155(2015).
RN [20]
RP VARIANT MODY6 PRO-103.
RX PubMed=26773576; DOI=10.1016/j.ejmg.2016.01.002;
RA Szopa M., Ludwig-Galezowska A.H., Radkowski P., Skupien J., Machlowska J.,
RA Klupa T., Wolkow P., Borowiec M., Mlynarski W., Malecki M.T.;
RT "A family with the Arg103Pro mutation in the NEUROD1 gene detected by next-
RT generation sequencing - Clinical characteristics of mutation carriers.";
RL Eur. J. Med. Genet. 59:75-79(2016).
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 (By similarity).
CC {ECO:0000250|UniProtKB:Q60867}.
CC -!- SUBUNIT: Efficient DNA-binding requires dimerization with another bHLH
CC protein (By similarity). Heterodimer with TCF3/E47; the heterodimer is
CC inhibited in presence of ID2, but not NR0B2, to E-box element
CC (PubMed:14752053). Interacts with EP300; the interaction is inhibited
CC by NR0B2 (PubMed:14752053). Interacts with RREB1 (PubMed:12482979).
CC Interacts with ATOH8 (By similarity). {ECO:0000250|UniProtKB:Q60867,
CC ECO:0000269|PubMed:12482979, ECO:0000269|PubMed:14752053}.
CC -!- INTERACTION:
CC Q13562; Q0VDC6: FKBP1A; NbExp=3; IntAct=EBI-3908303, EBI-10226858;
CC Q13562; P54652: HSPA2; NbExp=3; IntAct=EBI-3908303, EBI-356991;
CC Q13562; O43464: HTRA2; NbExp=3; IntAct=EBI-3908303, EBI-517086;
CC Q13562; P42858: HTT; NbExp=6; IntAct=EBI-3908303, EBI-466029;
CC Q13562; O14901: KLF11; NbExp=3; IntAct=EBI-3908303, EBI-948266;
CC Q13562; P28331-2: NDUFS1; NbExp=3; IntAct=EBI-3908303, EBI-6190702;
CC Q13562; Q9BVL2: NUP58; NbExp=3; IntAct=EBI-3908303, EBI-2811583;
CC Q13562; P41219: PRPH; NbExp=3; IntAct=EBI-3908303, EBI-752074;
CC Q13562; Q99081-3: TCF12; NbExp=4; IntAct=EBI-3908303, EBI-11952764;
CC Q13562; P15884-3: TCF4; NbExp=3; IntAct=EBI-3908303, EBI-13636688;
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. Nucleus
CC {ECO:0000255|PROSITE-ProRule:PRU00981, ECO:0000269|PubMed:14752053}.
CC Note=In pancreatic islet cells, shuttles to the nucleus in response to
CC glucose stimulation (By similarity). Colocalizes with NR0B2 in the
CC nucleus. {ECO:0000250}.
CC -!- PTM: Phosphorylated. In islet cells, phosphorylated on Ser-274 upon
CC glucose stimulation; which may be required for nuclear localization. In
CC activated neurons, phosphorylated on Ser-335; which promotes dendritic
CC growth. Phosphorylated by MAPK1; phosphorylation regulates
CC heterodimerization and DNA-binding activities. Phosphorylation on Ser-
CC 266 and Ser-274 increases transactivation on the insulin promoter in
CC glucose-stimulated insulinoma cells (By similarity). {ECO:0000250}.
CC -!- DISEASE: Maturity-onset diabetes of the young 6 (MODY6) [MIM:606394]: A
CC form of diabetes that is characterized by an autosomal dominant mode of
CC inheritance, onset in childhood or early adulthood (usually before 25
CC years of age), a primary defect in insulin secretion and frequent
CC insulin-independence at the beginning of the disease.
CC {ECO:0000269|PubMed:10545951, ECO:0000269|PubMed:11719843,
CC ECO:0000269|PubMed:26773576}. Note=The disease is caused by variants
CC affecting the gene represented in this entry.
CC -!- DISEASE: Diabetes mellitus, non-insulin-dependent (NIDDM) [MIM:125853]:
CC A multifactorial disorder of glucose homeostasis caused by a lack of
CC sensitivity to the body's own insulin. Affected individuals usually
CC have an obese body habitus and manifestations of a metabolic syndrome
CC characterized by diabetes, insulin resistance, hypertension and
CC hypertriglyceridemia. The disease results in long-term complications
CC that affect the eyes, kidneys, nerves, and blood vessels.
CC {ECO:0000269|PubMed:10545951}. Note=The disease is caused by variants
CC affecting the gene represented in this entry.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; U50822; AAA93480.1; -; Genomic_DNA.
DR EMBL; D82347; BAA11558.1; -; mRNA.
DR EMBL; AF045152; AAC83145.1; -; Genomic_DNA.
DR EMBL; AB018693; BAA76603.1; -; Genomic_DNA.
DR EMBL; AB009997; BAA87605.1; -; Genomic_DNA.
DR EMBL; AB016079; BAA36519.1; -; Genomic_DNA.
DR EMBL; BT019731; AAV38536.1; -; mRNA.
DR EMBL; AK313799; BAG36535.1; -; mRNA.
DR EMBL; AB593068; BAJ84015.1; -; mRNA.
DR EMBL; AB593069; BAJ84016.1; -; mRNA.
DR EMBL; AB593070; BAJ84017.1; -; mRNA.
DR EMBL; AB593071; BAJ84018.1; -; mRNA.
DR EMBL; AC013733; AAY24267.1; -; Genomic_DNA.
DR EMBL; CH471058; EAX10983.1; -; Genomic_DNA.
DR EMBL; BC009046; AAH09046.1; -; mRNA.
DR EMBL; U80578; AAC51318.1; -; mRNA.
DR EMBL; U36472; AAA79702.1; -; mRNA.
DR CCDS; CCDS2283.1; -.
DR RefSeq; NP_002491.2; NM_002500.4.
DR AlphaFoldDB; Q13562; -.
DR SMR; Q13562; -.
DR BioGRID; 110833; 20.
DR CORUM; Q13562; -.
DR IntAct; Q13562; 14.
DR STRING; 9606.ENSP00000295108; -.
DR CarbonylDB; Q13562; -.
DR iPTMnet; Q13562; -.
DR PhosphoSitePlus; Q13562; -.
DR BioMuta; NEUROD1; -.
DR DMDM; 311033428; -.
DR MassIVE; Q13562; -.
DR PaxDb; Q13562; -.
DR PeptideAtlas; Q13562; -.
DR PRIDE; Q13562; -.
DR ProteomicsDB; 59561; -.
DR Antibodypedia; 922; 533 antibodies from 38 providers.
DR DNASU; 4760; -.
DR Ensembl; ENST00000295108.4; ENSP00000295108.3; ENSG00000162992.5.
DR Ensembl; ENST00000683430.1; ENSP00000506907.1; ENSG00000162992.5.
DR Ensembl; ENST00000684079.1; ENSP00000507492.1; ENSG00000162992.5.
DR GeneID; 4760; -.
DR KEGG; hsa:4760; -.
DR MANE-Select; ENST00000295108.4; ENSP00000295108.3; NM_002500.5; NP_002491.3.
DR UCSC; uc002uof.5; human.
DR CTD; 4760; -.
DR DisGeNET; 4760; -.
DR GeneCards; NEUROD1; -.
DR GeneReviews; NEUROD1; -.
DR HGNC; HGNC:7762; NEUROD1.
DR HPA; ENSG00000162992; Group enriched (brain, retina).
DR MalaCards; NEUROD1; -.
DR MIM; 125853; phenotype.
DR MIM; 601724; gene.
DR MIM; 606394; phenotype.
DR neXtProt; NX_Q13562; -.
DR OpenTargets; ENSG00000162992; -.
DR Orphanet; 552; MODY.
DR PharmGKB; PA31564; -.
DR VEuPathDB; HostDB:ENSG00000162992; -.
DR eggNOG; KOG3898; Eukaryota.
DR GeneTree; ENSGT00940000160478; -.
DR HOGENOM; CLU_055134_0_0_1; -.
DR InParanoid; Q13562; -.
DR OMA; FKHEPAA; -.
DR OrthoDB; 1096531at2759; -.
DR PhylomeDB; Q13562; -.
DR TreeFam; TF315153; -.
DR PathwayCommons; Q13562; -.
DR Reactome; R-HSA-210745; Regulation of gene expression in beta cells.
DR Reactome; R-HSA-210746; Regulation of gene expression in endocrine-committed (NEUROG3+) progenitor cells.
DR SignaLink; Q13562; -.
DR SIGNOR; Q13562; -.
DR BioGRID-ORCS; 4760; 6 hits in 1095 CRISPR screens.
DR GeneWiki; NEUROD1; -.
DR GenomeRNAi; 4760; -.
DR Pharos; Q13562; Tbio.
DR PRO; PR:Q13562; -.
DR Proteomes; UP000005640; Chromosome 2.
DR RNAct; Q13562; protein.
DR Bgee; ENSG00000162992; Expressed in paraflocculus and 79 other tissues.
DR ExpressionAtlas; Q13562; baseline and differential.
DR Genevisible; Q13562; HS.
DR GO; GO:0000785; C:chromatin; ISA:NTNU_SB.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0005654; C:nucleoplasm; TAS:Reactome.
DR GO; GO:0005634; C:nucleus; IDA:UniProtKB.
DR GO; GO:0090575; C:RNA polymerase II transcription regulator complex; IDA:BHF-UCL.
DR GO; GO:0003682; F:chromatin binding; ISS:UniProtKB.
DR GO; GO:0001228; F:DNA-binding transcription activator activity, RNA polymerase II-specific; IDA:GO_Central.
DR GO; GO:0003700; F:DNA-binding transcription factor activity; IDA:BHF-UCL.
DR GO; GO:0000981; F:DNA-binding transcription factor activity, RNA polymerase II-specific; IDA:BHF-UCL.
DR GO; GO:0070888; F:E-box binding; IDA:UniProtKB.
DR GO; GO:0046982; F:protein heterodimerization activity; IDA:UniProtKB.
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; IPI:BHF-UCL.
DR GO; GO:1990837; F:sequence-specific double-stranded DNA binding; IDA:ARUK-UCL.
DR GO; GO:0035881; P:amacrine cell differentiation; ISS:UniProtKB.
DR GO; GO:0009952; P:anterior/posterior pattern specification; IEA:Ensembl.
DR GO; GO:0071333; P:cellular response to glucose stimulus; IEA:Ensembl.
DR GO; GO:0021549; P:cerebellum development; ISS:UniProtKB.
DR GO; GO:0021542; P:dentate gyrus development; ISS:UniProtKB.
DR GO; GO:0048562; P:embryonic organ morphogenesis; ISS:BHF-UCL.
DR GO; GO:0031018; P:endocrine pancreas development; ISS:UniProtKB.
DR GO; GO:0035883; P:enteroendocrine cell differentiation; ISS:UniProtKB.
DR GO; GO:0042593; P:glucose homeostasis; ISS:BHF-UCL.
DR GO; GO:0048839; P:inner ear development; ISS:UniProtKB.
DR GO; GO:0030073; P:insulin secretion; IDA:BHF-UCL.
DR GO; GO:0046426; P:negative regulation of receptor signaling pathway via JAK-STAT; IEA:Ensembl.
DR GO; GO:2000675; P:negative regulation of type B pancreatic cell apoptotic process; ISS:BHF-UCL.
DR GO; GO:0022008; P:neurogenesis; TAS: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; IDA:BHF-UCL.
DR GO; GO:0006913; P:nucleocytoplasmic transport; IEA:Ensembl.
DR GO; GO:0003326; P:pancreatic A cell fate commitment; IEA:Ensembl.
DR GO; GO:0003329; P:pancreatic PP cell fate commitment; IEA:Ensembl.
DR GO; GO:0043065; P:positive regulation of apoptotic process; ISS:UniProtKB.
DR GO; GO:0045597; P:positive regulation of cell differentiation; ISS: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; ISS:UniProtKB.
DR GO; GO:0045944; P:positive regulation of transcription by RNA polymerase II; IDA:BHF-UCL.
DR GO; GO:2000679; P:positive regulation of transcription regulatory region DNA binding; IDA:BHF-UCL.
DR GO; GO:0045893; P:positive regulation of transcription, DNA-templated; ISS:UniProtKB.
DR GO; GO:0007259; P:receptor signaling pathway via JAK-STAT; IEA:Ensembl.
DR GO; GO:0050796; P:regulation of insulin secretion; IC:BHF-UCL.
DR GO; GO:0060730; P:regulation of intestinal epithelial structure maintenance; ISS:UniProtKB.
DR GO; GO:0006357; P:regulation of transcription by RNA polymerase II; IBA:GO_Central.
DR GO; GO:0009749; P:response to glucose; IMP:BHF-UCL.
DR GO; GO:0009410; P:response to xenobiotic stimulus; IEA:Ensembl.
DR GO; GO:0023019; P:signal transduction involved in regulation of gene expression; IEA:Ensembl.
DR GO; GO:0006366; P:transcription by RNA polymerase II; IEA:Ensembl.
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 Activator; Cytoplasm; Developmental protein; Diabetes mellitus;
KW Differentiation; Disease variant; DNA-binding; Neurogenesis; Nucleus;
KW Phosphoprotein; Reference proteome; Transcription;
KW Transcription regulation.
FT CHAIN 1..356
FT /note="Neurogenic differentiation factor 1"
FT /id="PRO_0000127381"
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:0000250|UniProtKB:Q60867"
FT MOD_RES 259
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q60867"
FT MOD_RES 266
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q60867"
FT MOD_RES 274
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q60867"
FT MOD_RES 335
FT /note="Phosphoserine; by CaMK2"
FT /evidence="ECO:0000250|UniProtKB:Q64289"
FT VARIANT 45
FT /note="T -> A (in dbSNP:rs1801262)"
FT /evidence="ECO:0000269|PubMed:10366743,
FT ECO:0000269|PubMed:14702039, ECO:0000269|PubMed:15489334,
FT ECO:0000269|PubMed:21697133, ECO:0000269|PubMed:8786144,
FT ECO:0000269|PubMed:8915591, ECO:0000269|Ref.11,
FT ECO:0000269|Ref.3, ECO:0000269|Ref.5, ECO:0000269|Ref.6"
FT /id="VAR_014820"
FT VARIANT 103
FT /note="R -> P (in MODY6)"
FT /evidence="ECO:0000269|PubMed:26773576"
FT /id="VAR_076552"
FT VARIANT 110
FT /note="E -> K (in MODY6; unknown pathological significance;
FT dbSNP:rs763092306)"
FT /evidence="ECO:0000269|PubMed:11719843"
FT /id="VAR_076553"
FT VARIANT 111
FT /note="R -> L (in NIDDM; dbSNP:rs104893649)"
FT /evidence="ECO:0000269|PubMed:10545951"
FT /id="VAR_012487"
FT VARIANT 197
FT /note="P -> H (in dbSNP:rs8192556)"
FT /id="VAR_031260"
FT VARIANT 242
FT /note="V -> I (found in one consanguineous family with non-
FT syndromic autosomal recessive retinitis pigmentosa; unknown
FT pathological significance; dbSNP:rs786205158)"
FT /evidence="ECO:0000269|PubMed:25477324"
FT /id="VAR_076554"
FT CONFLICT 157
FT /note="L -> S (in Ref. 1; AAA93480)"
FT /evidence="ECO:0000305"
FT CONFLICT 185
FT /note="A -> G (in Ref. 2; BAA11558 and 5; BAA87605)"
FT /evidence="ECO:0000305"
FT CONFLICT 232
FT /note="G -> D (in Ref. 6; BAA36519)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 356 AA; 39920 MW; B78075D1CF66E943 CRC64;
MTKSYSESGL MGEPQPQGPP SWTDECLSSQ DEEHEADKKE DDLETMNAEE DSLRNGGEEE
DEDEDLEEEE EEEEEDDDQK PKRRGPKKKK MTKARLERFK LRRMKANARE RNRMHGLNAA
LDNLRKVVPC YSKTQKLSKI ETLRLAKNYI WALSEILRSG KSPDLVSFVQ TLCKGLSQPT
TNLVAGCLQL NPRTFLPEQN QDMPPHLPTA SASFPVHPYS YQSPGLPSPP YGTMDSSHVF
HVKPPPHAYS AALEPFFESP LTDCTSPSFD GPLSPPLSIN GNFSFKHEPS AEFEKNYAFT
MHYPAATLAG AQSHGSIFSG TAAPRCEIPI DNIMSFDSHS HHERVMSAQL NAIFHD
