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Q60867 (NDF1_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 129. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Interactions·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Neurogenic differentiation factor 1

Short name=NeuroD1
Alternative name(s):
Beta-cell E-box transcriptional activator 2
Short name=Beta2
Gene names
Name:Neurod1
Synonyms:Neurod
OrganismMus musculus (Mouse) [Reference proteome]
Taxonomic identifier10090 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus

Protein attributes

Sequence length357 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

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. Ref.4 Ref.5 Ref.6 Ref.7 Ref.8 Ref.9 Ref.10 Ref.11 Ref.12 Ref.14 Ref.15 Ref.16 Ref.17 Ref.18 Ref.20

Subunit structure

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). Ref.5 Ref.11 Ref.21

Subcellular location

Cytoplasm By similarity. Nucleus By similarity. Note: In pancreatic islet cells, shuttles to the nucleus in response to glucose stimulation. Colocalizes with NR0B2 in the nucleus By similarity.

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. Ref.4 Ref.6 Ref.9 Ref.11 Ref.13 Ref.18

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. Ref.4 Ref.7 Ref.8 Ref.10 Ref.20

Induction

Up-regulated by NKX2-2 and NEUROG3. Ref.18 Ref.19

Post-translational modification

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. Ref.11 Ref.14

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. Ref.4 Ref.6 Ref.7 Ref.8 Ref.16

Sequence similarities

Contains 1 bHLH (basic helix-loop-helix) domain.

Ontologies

Keywords
   Biological processDifferentiation
Neurogenesis
Transcription
Transcription regulation
   Cellular componentCytoplasm
Nucleus
   LigandDNA-binding
   Molecular functionActivator
Developmental protein
   PTMPhosphoprotein
   Technical term3D-structure
Complete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processamacrine cell differentiation

Inferred from direct assay Ref.9. Source: UniProtKB

anterior/posterior pattern specification

Inferred from mutant phenotype PubMed 16368089. Source: MGI

camera-type eye development

Inferred from genetic interaction Ref.9. Source: MGI

cell fate commitment

Inferred from genetic interaction Ref.9. Source: MGI

cellular response to glucose stimulus

Inferred from electronic annotation. Source: Ensembl

cerebellum development

Inferred from mutant phenotype Ref.6. Source: UniProtKB

dentate gyrus development

Inferred from mutant phenotype Ref.6Ref.7. Source: UniProtKB

embryonic organ morphogenesis

Inferred from mutant phenotype Ref.4. Source: BHF-UCL

endocrine pancreas development

Inferred from mutant phenotype Ref.7. Source: UniProtKB

enteroendocrine cell differentiation

Inferred from mutant phenotype Ref.4. Source: UniProtKB

glucose homeostasis

Inferred from mutant phenotype Ref.4. Source: BHF-UCL

hindbrain development

Inferred from mutant phenotype PubMed 16368089. Source: MGI

inner ear development

Inferred from mutant phenotype Ref.8. Source: UniProtKB

insulin secretion

Inferred from electronic annotation. Source: Ensembl

negative regulation of JAK-STAT cascade

Inferred from direct assay PubMed 18848628. Source: MGI

negative regulation of type B pancreatic cell apoptotic process

Inferred from mutant phenotype Ref.4. Source: BHF-UCL

nitric oxide mediated signal transduction

Inferred from electronic annotation. Source: Ensembl

nucleocytoplasmic transport

Inferred from electronic annotation. Source: Ensembl

pancreatic A cell fate commitment

Inferred from genetic interaction PubMed 17988662. Source: MGI

pancreatic PP cell fate commitment

Inferred from genetic interaction PubMed 17988662. Source: MGI

positive regulation of apoptotic process

Inferred from direct assay Ref.5. Source: UniProtKB

positive regulation of cell differentiation

Inferred from direct assay Ref.9Ref.5. Source: UniProtKB

positive regulation of neuron differentiation

Inferred from direct assay Ref.15. Source: UniProtKB

positive regulation of sequence-specific DNA binding transcription factor activity

Inferred from direct assay Ref.12. Source: UniProtKB

positive regulation of transcription from RNA polymerase II promoter

Inferred from direct assay Ref.15Ref.5. Source: UniProtKB

positive regulation of transcription regulatory region DNA binding

Inferred from electronic annotation. Source: Ensembl

positive regulation of transcription, DNA-templated

Inferred from direct assay Ref.12. Source: UniProtKB

regulation of cell cycle arrest

Inferred from mutant phenotype Ref.5. Source: UniProtKB

regulation of intestinal epithelial structure maintenance

Inferred from direct assay Ref.5. Source: UniProtKB

regulation of neuron differentiation

Inferred from genetic interaction PubMed 22513373. Source: MGI

response to drug

Inferred from electronic annotation. Source: Ensembl

signal transduction involved in regulation of gene expression

Inferred from direct assay PubMed 18462699. Source: MGI

   Cellular_componentcytoplasm

Inferred from direct assay PubMed 18388149. Source: MGI

intracellular

Inferred from direct assay PubMed 10868931PubMed 15793245. Source: MGI

nucleoplasm

Traceable author statement. Source: Reactome

nucleus

Inferred from direct assay PubMed 11891657PubMed 18388149. Source: MGI

   Molecular_functionDNA binding

Inferred from direct assay PubMed 12368292. Source: MGI

E-box binding

Inferred from direct assay Ref.12. Source: UniProtKB

RNA polymerase II transcription coactivator activity

Inferred from electronic annotation. Source: Ensembl

chromatin binding

Inferred from direct assay Ref.15. Source: UniProtKB

double-stranded DNA binding

Inferred from electronic annotation. Source: Ensembl

protein binding

Inferred from physical interaction Ref.5. Source: UniProtKB

protein heterodimerization activity

Inferred from physical interaction PubMed 18388149. Source: MGI

sequence-specific DNA binding

Inferred from direct assay PubMed 15793245PubMed 18388149. Source: MGI

sequence-specific DNA binding transcription factor activity

Inferred from electronic annotation. Source: Ensembl

Complete GO annotation...

Binary interactions

With

Entry

#Exp.

IntAct

Notes

CCNDBP1O952734EBI-309315,EBI-748961From a different organism.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 357357Neurogenic differentiation factor 1
PRO_0000127383

Regions

Domain101 – 15353bHLH
Motif87 – 937Nuclear localization signal Potential
Compositional bias58 – 7720Glu-rich (acidic)
Compositional bias58 – 647Poly-Glu
Compositional bias67 – 7711Poly-Glu
Compositional bias87 – 904Poly-Lys

Amino acid modifications

Modified residue1621Phosphoserine Ref.11
Modified residue2591Phosphoserine Ref.11 Ref.14
Modified residue2661Phosphoserine Ref.11 Ref.14
Modified residue2741Phosphoserine Ref.11 Ref.14
Modified residue3361Phosphoserine; by CaMK2 By similarity

Experimental info

Mutagenesis1621S → A: Reduces weakly phosphorylation. Reduces strongly phosphorylation; when associated with A-259 and A-266. Ref.11
Mutagenesis2591S → 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. Ref.11 Ref.14
Mutagenesis2661S → 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. Ref.11 Ref.14
Mutagenesis2741S → A: Reduces strongly phosphorylation. Reduces transactivation on the insulin promoter in glucose-stimulated insulinoma cells; when associated with A-259 and A-266. Ref.11 Ref.14
Mutagenesis2791I → V: Promotes the formation of differentiated late retinal amacrine cells.

Secondary structure

......... 357
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
Q60867 [UniParc].

Last modified February 1, 1997. Version 2.
Checksum: B6626E1315E31027

FASTA35739,999
        10         20         30         40         50         60 
MTKSYSESGL MGEPQPQGPP SWTDECLSSQ DEEHEADKKE DELEAMNAEE DSLRNGGEEE 

        70         80         90        100        110        120 
EEDEDLEEEE EEEEEEEDQK PKRRGPKKKK MTKARLERFK LRRMKANARE RNRMHGLNAA 

       130        140        150        160        170        180 
LDNLRKVVPC YSKTQKLSKI ETLRLAKNYI WALSEILRSG KSPDLVSFVQ TLCKGLSQPT 

       190        200        210        220        230        240 
TNLVAGCLQL NPRTFLPEQN PDMPPHLPTA SASFPVHPYS YQSPGLPSPP YGTMDSSHVF 

       250        260        270        280        290        300 
HVKPPPHAYS AALEPFFESP LTDCTSPSFD GPLSPPLSIN GNFSFKHEPS AEFEKNYAFT 

       310        320        330        340        350 
MHYPAATLAG PQSHGSIFSS GAAAPRCEIP IDNIMSFDSH SHHERVMSAQ LNAIFHD 

« Hide

References

« Hide 'large scale' references
[1]"Conversion of Xenopus ectoderm into neurons by NeuroD, a basic helix-loop-helix protein."
Lee J.E., Hollenberg S.M., Snider L., Turner D.L., Lipnick N., Weintraub H.
Science 268:836-844(1995) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA].
Strain: 129/Sv and MF1.
[2]"The transcriptional landscape of the mammalian genome."
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. expand/collapse author list , 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.
Science 309:1559-1563(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Strain: C57BL/6J.
Tissue: Cerebellum.
[3]"The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
The MGC Project Team
Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Tissue: Eye.
[4]"Diabetes, defective pancreatic morphogenesis, and abnormal enteroendocrine differentiation in BETA2/neuroD-deficient mice."
Naya F.J., Huang H.P., Qiu Y., Mutoh H., DeMayo F.J., Leiter A.B., Tsai M.J.
Genes Dev. 11:2323-2334(1997) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, DISRUPTION PHENOTYPE, TISSUE SPECIFICITY, DEVELOPMENTAL STAGE.
[5]"The basic helix-loop-helix protein BETA2 interacts with p300 to coordinate differentiation of secretin-expressing enteroendocrine cells."
Mutoh H., Naya F.J., Tsai M.J., Leiter A.B.
Genes Dev. 12:820-830(1998) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, INTERACTION WITH EP300, DNA-BINDING.
[6]"NeuroD is required for differentiation of the granule cells in the cerebellum and hippocampus."
Miyata T., Maeda T., Lee J.E.
Genes Dev. 13:1647-1652(1999) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, DISRUPTION PHENOTYPE, TISSUE SPECIFICITY.
[7]"Loss of BETA2/NeuroD leads to malformation of the dentate gyrus and epilepsy."
Liu M., Pleasure S.J., Collins A.E., Noebels J.L., Naya F.J., Tsai M.J., Lowenstein D.H.
Proc. Natl. Acad. Sci. U.S.A. 97:865-870(2000) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, DISRUPTION PHENOTYPE, DEVELOPMENTAL STAGE.
[8]"NeuroD-null mice are deaf due to a severe loss of the inner ear sensory neurons during development."
Kim W.Y., Fritzsch B., Serls A., Bakel L.A., Huang E.J., Reichardt L.F., Barth D.S., Lee J.E.
Development 128:417-426(2001) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, DISRUPTION PHENOTYPE, DEVELOPMENTAL STAGE.
[9]"Math3 and NeuroD regulate amacrine cell fate specification in the retina."
Inoue T., Hojo M., Bessho Y., Tano Y., Lee J.E., Kageyama R.
Development 129:831-842(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, TISSUE SPECIFICITY.
[10]"Posttranslational mechanisms control the timing of bHLH function and regulate retinal cell fate."
Moore K.B., Schneider M.L., Vetter M.L.
Neuron 34:183-195(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, MUTAGENESIS OF 274-SER--SER-278, DEVELOPMENTAL STAGE.
[11]"Regulation of insulin gene transcription by ERK1 and ERK2 in pancreatic beta cells."
Khoo S., Griffen S.C., Xia Y., Baer R.J., German M.S., Cobb M.H.
J. Biol. Chem. 278:32969-32977(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, HETERODIMERIZATION, PHOSPHORYLATION AT SER-162; SER-259; SER-266 AND SER-274, TISSUE SPECIFICITY, MUTAGENESIS OF SER-162; SER-259; SER-266 AND SER-274.
[12]"Regulation of neuroD2 expression in mouse brain."
Lin C.H., Stoeck J., Ravanpay A.C., Guillemot F., Tapscott S.J., Olson J.M.
Dev. Biol. 265:234-245(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, DNA-BINDING.
[13]"Orphan nuclear receptor small heterodimer partner, a novel corepressor for a basic helix-loop-helix transcription factor BETA2/neuroD."
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.
Mol. Endocrinol. 18:776-790(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: TISSUE SPECIFICITY.
[14]"Context-dependent regulation of NeuroD activity and protein accumulation."
Dufton C., Marcora E., Chae J.H., McCullough J., Eby J., Hausburg M., Stein G.H., Khoo S., Cobb M.H., Lee J.E.
Mol. Cell. Neurosci. 28:727-736(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, PHOSPHORYLATION AT SER-259; SER-266 AND SER-274, MUTAGENESIS OF SER-259; SER-266 AND SER-274.
[15]"Neurogenin and NeuroD direct transcriptional targets and their regulatory enhancers."
Seo S., Lim J.W., Yellajoshyula D., Chang L.W., Kroll K.L.
EMBO J. 26:5093-5108(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, ASSOCIATION WITH CHROMATIN.
[16]"Targeted disruption of NeuroD, a proneural basic helix-loop-helix factor, impairs distal lung formation and neuroendocrine morphology in the neonatal lung."
Neptune E.R., Podowski M., Calvi C., Cho J.H., Garcia J.G., Tuder R., Linnoila R.I., Tsai M.J., Dietz H.C.
J. Biol. Chem. 283:21160-21169(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, DISRUPTION PHENOTYPE.
[17]"Involvement of Ngn2, Tbr and NeuroD proteins during postnatal olfactory bulb neurogenesis."
Roybon L., Deierborg T., Brundin P., Li J.Y.
Eur. J. Neurosci. 29:232-243(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION.
[18]"Cooperative transcriptional regulation of the essential pancreatic islet gene NeuroD1 (beta2) by Nkx2.2 and neurogenin 3."
Anderson K.R., Torres C.A., Solomon K., Becker T.C., Newgard C.B., Wright C.V., Hagman J., Sussel L.
J. Biol. Chem. 284:31236-31248(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, INDUCTION, TISSUE SPECIFICITY.
[19]"mu-Opioid receptor agonists differentially regulate the expression of miR-190 and NeuroD."
Zheng H., Zeng Y., Zhang X., Chu J., Loh H.H., Law P.Y.
Mol. Pharmacol. 77:102-109(2010) [PubMed] [Europe PMC] [Abstract]
Cited for: INDUCTION.
[20]"NeuroD factors regulate cell fate and neurite stratification in the developing retina."
Cherry T.J., Wang S., Bormuth I., Schwab M., Olson J., Cepko C.L.
J. Neurosci. 31:7365-7379(2011) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, DEVELOPMENTAL STAGE.
[21]"Crystal structure of E47-NeuroD1/beta2 bHLH domain-DNA complex: heterodimer selectivity and DNA recognition."
Longo A., Guanga G.P., Rose R.B.
Biochemistry 47:218-229(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.5 ANGSTROMS) OF 102-160 IN COMPLEX WITH TCF3 AND PROMOTER E-BOX DNA SEQUENCE, SUBUNIT.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
U28068 mRNA. Translation: AAC52203.1.
U28888 Genomic DNA. Translation: AAC52204.1.
AK005073 mRNA. Translation: BAB23797.1.
AK018781 mRNA. Translation: BAB31405.1.
BC018241 mRNA. Translation: AAH18241.1.
CCDSCCDS16169.1.
PIRI49338.
RefSeqNP_035024.1. NM_010894.2.
UniGeneMm.4636.

3D structure databases

PDBe
RCSB-PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
2QL2X-ray2.50B/D102-160[»]
ProteinModelPortalQ60867.
SMRQ60867. Positions 102-158.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid201733. 8 interactions.
IntActQ60867. 2 interactions.
MINTMINT-8396397.

PTM databases

PhosphoSiteQ60867.

Proteomic databases

PRIDEQ60867.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENSMUST00000041099; ENSMUSP00000040364; ENSMUSG00000034701.
GeneID18012.
KEGGmmu:18012.
UCSCuc008kgt.1. mouse.

Organism-specific databases

CTD4760.
MGIMGI:1339708. Neurod1.

Phylogenomic databases

eggNOGNOG287211.
GeneTreeENSGT00680000099860.
HOGENOMHOG000049256.
HOVERGENHBG000250.
InParanoidQ60867.
KOK08033.
OMAMNAQLNA.
OrthoDBEOG722J8S.
PhylomeDBQ60867.
TreeFamTF315153.

Enzyme and pathway databases

ReactomeREACT_13641. Regulation of Beta-Cell Development.

Gene expression databases

BgeeQ60867.
CleanExMM_NEUROD1.
GenevestigatorQ60867.

Family and domain databases

Gene3D4.10.280.10. 1 hit.
InterProIPR011598. bHLH_dom.
IPR022575. Neurogenic_DUF.
IPR016637. TF_bHLH_NeuroD.
[Graphical view]
PfamPF00010. HLH. 1 hit.
PF12533. Neuro_bHLH. 1 hit.
[Graphical view]
PIRSFPIRSF015618. bHLH_NeuroD. 1 hit.
SMARTSM00353. HLH. 1 hit.
[Graphical view]
SUPFAMSSF47459. SSF47459. 1 hit.
PROSITEPS50888. BHLH. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

EvolutionaryTraceQ60867.
NextBio293037.
PROQ60867.
SOURCESearch...

Entry information

Entry nameNDF1_MOUSE
AccessionPrimary (citable) accession number: Q60867
Secondary accession number(s): Q545N9, Q60897
Entry history
Integrated into UniProtKB/Swiss-Prot: November 1, 1997
Last sequence update: February 1, 1997
Last modified: July 9, 2014
This is version 129 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

MGD cross-references

Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot