Q60867 (NDF1_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended 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

Organism

Mus musculus (Mouse) [Reference proteome]

Taxonomic identifier

10090 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Opisthokonta › Metazoa › Eumetazoa › Bilateria › Deuterostomia › Chordata › Craniata › Vertebrata › Gnathostomata › Teleostomi › Euteleostomi › Sarcopterygii › Tetrapoda › Amniota › Mammalia › Theria › Eutheria › Euarchontoglires › Glires › Rodentia › Sciurognathi › Muroidea › Muridae › Murinae › Mus › Mus

Protein attributes

Sequence length	357 AA.
Sequence status	Complete.
Protein existence	Evidence 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 process	Differentiation Neurogenesis Transcription Transcription regulation
Cellular component	Cytoplasm Nucleus
Ligand	DNA-binding
Molecular function	Activator Developmental protein
PTM	Phosphoprotein
Technical term	3D-structure Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	amacrine cell differentiation Inferred from direct assay Ref.9. Source: UniProtKB anterior/posterior pattern specification Inferred from mutant phenotype PubMed 16368089. Source: MGI cellular response to glucose stimulus Inferred from electronic annotation. Source: Compara 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 enteroendocrine cell differentiation Inferred from mutant phenotype Ref.4. Source: UniProtKB glucose homeostasis Inferred from mutant phenotype Ref.4. Source: BHF-UCL inner ear development Inferred from mutant phenotype Ref.8. Source: UniProtKB insulin secretion Inferred from electronic annotation. Source: Compara negative regulation of JAK-STAT cascade Inferred from direct assay PubMed 18848628. Source: MGI negative regulation of apoptotic process Inferred from mutant phenotype Ref.4. Source: BHF-UCL nitric oxide mediated signal transduction Inferred from electronic annotation. Source: Compara nucleocytoplasmic transport Inferred from electronic annotation. Source: Compara 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 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: Compara 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 response to drug Inferred from electronic annotation. Source: Compara signal transduction involved in regulation of gene expression Inferred from direct assay PubMed 18462699. Source: MGI
Cellular_component	cytoplasm Inferred from direct assay PubMed 18388149. Source: MGI nucleoplasm Traceable author statement. Source: Reactome
Molecular_function	E-box binding Inferred from direct assay Ref.12. Source: UniProtKB RNA polymerase II transcription coactivator activity Inferred from electronic annotation. Source: Compara chromatin binding Inferred from direct assay Ref.15. Source: UniProtKB double-stranded DNA binding Inferred from electronic annotation. Source: Compara 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: Compara
Complete GO annotation...

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 357

357

Neurogenic differentiation factor 1

PRO_0000127383

Regions

Domain

101 – 153

53

bHLH

Motif

87 – 93

7

Nuclear localization signal Potential

Compositional bias

58 – 77

20

Glu-rich (acidic)

Compositional bias

58 – 64

7

Poly-Glu

Compositional bias

67 – 77

11

Poly-Glu

Compositional bias

87 – 90

4

Poly-Lys

Amino acid modifications

Modified residue

162

1

Phosphoserine Ref.11

Modified residue

259

1

Phosphoserine Ref.11 Ref.14

Modified residue

266

1

Phosphoserine Ref.11 Ref.14

Modified residue

274

1

Phosphoserine Ref.11 Ref.14

Modified residue

336

1

Phosphoserine; by CaMK2 By similarity

Experimental info

Mutagenesis

162

1

S → A: Reduces weakly phosphorylation. Reduces strongly phosphorylation; when associated with A-259 and A-266. Ref.11

Mutagenesis

259

1

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. Ref.11 Ref.14

Mutagenesis

266

1

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. Ref.11 Ref.14

Mutagenesis

274

1

S → 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

Mutagenesis

279

1

I → V: Promotes the formation of differentiated late retinal amacrine cells.

Secondary structure

1

.

.

.

.

.

.

.

.

.

357

Helix Strand Turn

Details...

Helix

102 – 126

25

Beta strand

128 – 130

3

Beta strand

133 – 135

3

Helix

139 – 156

18

Sequences

	Sequence		Length	Mass (Da)
	Q60867 [UniParc]. Last modified February 1, 1997. Version 2. Checksum: B6626E1315E31027	FASTA	357	39,999
	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

References

	« Hide 'large scale' referencesShow '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. , 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.

IPI

IPI00121519.

PIR

I49338.

RefSeq

NP_035024.1. NM_010894.2.

UniGene

Mm.4636.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
2QL2	X-ray	2.50	B/D	102-160	[»]

ProteinModelPortal

Q60867.

SMR

Q60867. Positions 102-158.

ModBase

Search...

Protein-protein interaction databases

IntAct

Q60867. 1 interaction.

PTM databases

PhosphoSite

Q60867.

Proteomic databases

PRIDE

Q60867.

Protocols and materials databases

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

Ensembl

ENSMUST00000041099; ENSMUSP00000040364; ENSMUSG00000034701.

GeneID

18012.

KEGG

mmu:18012.

Organism-specific databases

CTD

4760.

MGI

MGI:1339708. Neurod1.

Phylogenomic databases

eggNOG

NOG287211.

GeneTree

ENSGT00680000099860.

HOGENOM

HOG000049256.

HOVERGEN

HBG000250.

InParanoid

Q60867.

KO

K08033.

OMA

DEEHETD.

OrthoDB

EOG44F69G.

Enzyme and pathway databases

Reactome

REACT_13641. Regulation of Beta-Cell Development.

Gene expression databases

ArrayExpress

Q60867.

Bgee

Q60867.

CleanEx

MM_NEUROD1.

Genevestigator

Q60867.

GermOnline

ENSMUSG00000034701. Mus musculus.

Family and domain databases

Gene3D

4.10.280.10. 1 hit.

InterPro

IPR011598. bHLH_dom.
IPR022575. Neurogenic_DUF.
IPR016637. TF_bHLH_NeuroD.
[Graphical view]

Pfam

PF00010. HLH. 1 hit.
PF12533. Neuro_bHLH. 1 hit.
[Graphical view]

PIRSF

PIRSF015618. bHLH_NeuroD. 1 hit.

SMART

SM00353. HLH. 1 hit.
[Graphical view]

SUPFAM

SSF47459. HLH_basic. 1 hit.

PROSITE

PS50888. BHLH. 1 hit.
[Graphical view]

ProtoNet

Search...

Other

EvolutionaryTrace

Q60867.

NextBio

293037.

SOURCE

Search...

Entry information

Entry name

NDF1_MOUSE

Accession

Primary (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:	May 1, 2013
This is version 117 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program