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Q13562 (NDF1_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 143. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (5) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Web links·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Neurogenic differentiation factor 1

Short name=NeuroD
Short name=NeuroD1
Alternative name(s):
Class A basic helix-loop-helix protein 3
Short name=bHLHa3
Gene names
Name:NEUROD1
Synonyms:BHLHA3, NEUROD
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length356 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 By similarity.

Subunit structure

Interacts (via helix-loop-helix motif domain) with EP300 (via C-terminus) By similarity. Heterodimer with TCF3/E47; the heterodimer is inhibited in presence of ID2, but not NR0B2, to E-box element. Efficient DNA-binding requires dimerization with another bHLH protein. Interacts with RREB1. Interacts with EP300; the interaction is inhibited by NR0B2. Interacts with TCF3; the interaction is inhibited by ID2. Ref.15 Ref.16

Subcellular location

Cytoplasm By similarity. Nucleus. Note: In pancreatic islet cells, shuttles to the nucleus in response to glucose stimulation By similarity. Colocalizes with NR0B2 in the nucleus. Ref.16

Post-translational modification

Phosphorylated. In islet cells, phosphorylated on Ser-274 upon glucose stimulation; which may be required for nuclear localization. In activated neurons, phosphorylated on Ser-335; which promotes dendritic growth. 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 By similarity.

Involvement in disease

Maturity-onset diabetes of the young 6 (MODY6) [MIM:606394]: A form of diabetes that is characterized by an autosomal dominant mode of inheritance, onset in childhood or early adulthood (usually before 25 years of age), a primary defect in insulin secretion and frequent insulin-independence at the beginning of the disease.
Note: The disease is caused by mutations affecting the gene represented in this entry. Ref.17

Sequence similarities

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

Ontologies

Keywords
   Biological processDifferentiation
Neurogenesis
Transcription
Transcription regulation
   Cellular componentCytoplasm
Nucleus
   Coding sequence diversityPolymorphism
   DiseaseDiabetes mellitus
Disease mutation
   LigandDNA-binding
   Molecular functionActivator
Developmental protein
   PTMPhosphoprotein
   Technical termComplete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processamacrine cell differentiation

Inferred from sequence or structural similarity. Source: UniProtKB

anterior/posterior pattern specification

Inferred from electronic annotation. Source: Ensembl

cellular response to glucose stimulus

Inferred from electronic annotation. Source: Ensembl

cerebellum development

Inferred from sequence or structural similarity. Source: UniProtKB

dentate gyrus development

Inferred from sequence or structural similarity. Source: UniProtKB

embryonic organ morphogenesis

Inferred from sequence or structural similarity PubMed 9308961. Source: BHF-UCL

endocrine pancreas development

Inferred from sequence or structural similarity. Source: UniProtKB

enteroendocrine cell differentiation

Inferred from sequence or structural similarity. Source: UniProtKB

glucose homeostasis

Inferred from sequence or structural similarity PubMed 9308961. Source: BHF-UCL

inner ear development

Inferred from sequence or structural similarity. Source: UniProtKB

insulin secretion

Inferred from direct assay PubMed 17941991. Source: BHF-UCL

negative regulation of JAK-STAT cascade

Inferred from electronic annotation. Source: Ensembl

negative regulation of type B pancreatic cell apoptotic process

Inferred from sequence or structural similarity PubMed 9308961. Source: BHF-UCL

neurogenesis

Traceable author statement Ref.1. Source: BHF-UCL

nitric oxide mediated signal transduction

Inferred from direct assay PubMed 17941991. Source: BHF-UCL

nucleocytoplasmic transport

Inferred from electronic annotation. Source: Ensembl

pancreatic A cell fate commitment

Inferred from electronic annotation. Source: Ensembl

pancreatic PP cell fate commitment

Inferred from electronic annotation. Source: Ensembl

positive regulation of apoptotic process

Inferred from sequence or structural similarity. Source: UniProtKB

positive regulation of cell differentiation

Inferred from sequence or structural similarity. Source: UniProtKB

positive regulation of neuron differentiation

Inferred from sequence or structural similarity. Source: UniProtKB

positive regulation of sequence-specific DNA binding transcription factor activity

Inferred from direct assay Ref.16. Source: UniProtKB

positive regulation of transcription from RNA polymerase II promoter

Inferred from direct assay Ref.17. Source: BHF-UCL

positive regulation of transcription regulatory region DNA binding

Inferred from direct assay PubMed 19619559. Source: BHF-UCL

positive regulation of transcription, DNA-templated

Inferred from sequence or structural similarity. Source: UniProtKB

regulation of cell cycle arrest

Inferred from sequence or structural similarity. Source: UniProtKB

regulation of insulin secretion

Inferred by curator Ref.17. Source: BHF-UCL

regulation of intestinal epithelial structure maintenance

Inferred from sequence or structural similarity. Source: UniProtKB

response to drug

Inferred from electronic annotation. Source: Ensembl

response to glucose

Inferred from mutant phenotype Ref.17. Source: BHF-UCL

signal transduction involved in regulation of gene expression

Inferred from electronic annotation. Source: Ensembl

   Cellular_componentcytoplasm

Inferred from electronic annotation. Source: UniProtKB-SubCell

nucleoplasm

Traceable author statement. Source: Reactome

nucleus

Inferred from direct assay Ref.16. Source: UniProtKB

   Molecular_functionE-box binding

Inferred from direct assay Ref.16. Source: UniProtKB

RNA polymerase II activating transcription factor binding

Inferred from physical interaction PubMed 19619559. Source: BHF-UCL

RNA polymerase II transcription coactivator activity

Inferred from direct assay PubMed 19619559. Source: BHF-UCL

chromatin binding

Inferred from sequence or structural similarity. Source: UniProtKB

double-stranded DNA binding

Inferred from electronic annotation. Source: Ensembl

protein heterodimerization activity

Inferred from direct assay Ref.16. Source: UniProtKB

sequence-specific DNA binding

Inferred from electronic annotation. Source: Ensembl

sequence-specific DNA binding transcription factor activity

Inferred from direct assay Ref.17. Source: BHF-UCL

transcription coactivator activity

Inferred from direct assay Ref.16. Source: UniProtKB

transcription factor binding

Inferred from physical interaction Ref.17PubMed 16321656. Source: BHF-UCL

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 356356Neurogenic differentiation factor 1
PRO_0000127381

Regions

Domain101 – 15353bHLH
Motif87 – 937Nuclear localization signal Potential
Compositional bias58 – 7720Glu-rich (acidic)
Compositional bias67 – 759Poly-Glu
Compositional bias87 – 904Poly-Lys

Amino acid modifications

Modified residue1621Phosphoserine By similarity
Modified residue2591Phosphoserine By similarity
Modified residue2661Phosphoserine By similarity
Modified residue2741Phosphoserine By similarity
Modified residue3351Phosphoserine; by CaMK2 By similarity

Natural variations

Natural variant451T → A. Ref.1 Ref.2 Ref.3 Ref.4 Ref.5 Ref.6 Ref.8 Ref.9 Ref.11 Ref.12
Corresponds to variant rs1801262 [ dbSNP | Ensembl ].
VAR_014820
Natural variant1111R → L in MODY6. Ref.17
VAR_012487
Natural variant1971P → H.
Corresponds to variant rs8192556 [ dbSNP | Ensembl ].
VAR_031260

Experimental info

Sequence conflict1571L → S in AAA93480. Ref.1
Sequence conflict1851A → G in BAA11558. Ref.2
Sequence conflict1851A → G in BAA87605. Ref.5
Sequence conflict2321G → D in BAA36519. Ref.6

Sequences

Sequence LengthMass (Da)Tools
Q13562 [UniParc].

Last modified November 2, 2010. Version 3.
Checksum: B78075D1CF66E943

FASTA35639,920
        10         20         30         40         50         60 
MTKSYSESGL MGEPQPQGPP SWTDECLSSQ DEEHEADKKE DDLETMNAEE DSLRNGGEEE 

        70         80         90        100        110        120 
DEDEDLEEEE EEEEEDDDQK PKRRGPKKKK MTKARLERFK LRRMKANARE RNRMHGLNAA 

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

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

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

       310        320        330        340        350 
MHYPAATLAG AQSHGSIFSG TAAPRCEIPI DNIMSFDSHS HHERVMSAQL NAIFHD 

« Hide

References

« Hide 'large scale' references
[1]"The NEUROD gene maps to human chromosome 2q32 and mouse chromosome 2."
Tamimi R., Steingrimsson E., Copeland N.G., Dyer-Montgomery K., Lee J.E., Hernandez R., Jenkins N.A., Tapscott S.J.
Genomics 34:418-421(1996) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], VARIANT ALA-45.
[2]"Molecular cloning of a human neuroD from a neuroblastoma cell line specifically expressed in the fetal brain and adult cerebellum."
Yokoyama M., Nishi Y., Miyamoto Y., Nakamura M., Akiyama K., Matsubara K., Okubo K.
Brain Res. Mol. Brain Res. 42:135-139(1996) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA], VARIANT ALA-45.
[3]Furuta H., Horikawa Y., Iwasaki N., Hara M., Sussel L., le Beau M.M., Davis E.M., Ogata M., Iwamoto Y., German M.S., Bell G.I.
Submitted (JAN-1998) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], VARIANT ALA-45.
[4]"Structure and regulation of the human NeuroD (BETA2/BHF1) gene."
Miyachi T., Maruyama H., Kitamura T., Nakamura S., Kawakami H.
Brain Res. Mol. Brain Res. 69:223-231(1999) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], VARIANT ALA-45.
[5]Noma T.
Submitted (DEC-1997) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], VARIANT ALA-45.
[6]"Ala45Thr mutation of the human BETA2 gene."
Kuroe A., Yamada Y., Kubota A., Someya Y., Iwakura T., Watanabe R., Inada A., Miyawaki K., Ban N., Ihara Y., Seino Y.
Submitted (JUL-1998) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], VARIANT ALA-45.
[7]"Cloning of human full-length CDSs in BD Creator(TM) system donor vector."
Kalnine N., Chen X., Rolfs A., Halleck A., Hines L., Eisenstein S., Koundinya M., Raphael J., Moreira D., Kelley T., LaBaer J., Lin Y., Phelan M., Farmer A.
Submitted (OCT-2004) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
[8]"Complete sequencing and characterization of 21,243 full-length human cDNAs."
Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S. expand/collapse author list , Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.
Nat. Genet. 36:40-45(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA], VARIANT ALA-45.
Tissue: Cerebellum.
[9]"Full-length transcriptome analysis of human retina-derived cell lines ARPE-19 and Y79 using the vector-capping method."
Oshikawa M., Tsutsui C., Ikegami T., Fuchida Y., Matsubara M., Toyama S., Usami R., Ohtoko K., Kato S.
Invest. Ophthalmol. Vis. Sci. 52:6662-6670(2011) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA], VARIANT ALA-45.
[10]"Generation and annotation of the DNA sequences of human chromosomes 2 and 4."
Hillier L.W., Graves T.A., Fulton R.S., Fulton L.A., Pepin K.H., Minx P., Wagner-McPherson C., Layman D., Wylie K., Sekhon M., Becker M.C., Fewell G.A., Delehaunty K.D., Miner T.L., Nash W.E., Kremitzki C., Oddy L., Du H. expand/collapse author list , Sun H., Bradshaw-Cordum H., Ali J., Carter J., Cordes M., Harris A., Isak A., van Brunt A., Nguyen C., Du F., Courtney L., Kalicki J., Ozersky P., Abbott S., Armstrong J., Belter E.A., Caruso L., Cedroni M., Cotton M., Davidson T., Desai A., Elliott G., Erb T., Fronick C., Gaige T., Haakenson W., Haglund K., Holmes A., Harkins R., Kim K., Kruchowski S.S., Strong C.M., Grewal N., Goyea E., Hou S., Levy A., Martinka S., Mead K., McLellan M.D., Meyer R., Randall-Maher J., Tomlinson C., Dauphin-Kohlberg S., Kozlowicz-Reilly A., Shah N., Swearengen-Shahid S., Snider J., Strong J.T., Thompson J., Yoakum M., Leonard S., Pearman C., Trani L., Radionenko M., Waligorski J.E., Wang C., Rock S.M., Tin-Wollam A.-M., Maupin R., Latreille P., Wendl M.C., Yang S.-P., Pohl C., Wallis J.W., Spieth J., Bieri T.A., Berkowicz N., Nelson J.O., Osborne J., Ding L., Meyer R., Sabo A., Shotland Y., Sinha P., Wohldmann P.E., Cook L.L., Hickenbotham M.T., Eldred J., Williams D., Jones T.A., She X., Ciccarelli F.D., Izaurralde E., Taylor J., Schmutz J., Myers R.M., Cox D.R., Huang X., McPherson J.D., Mardis E.R., Clifton S.W., Warren W.C., Chinwalla A.T., Eddy S.R., Marra M.A., Ovcharenko I., Furey T.S., Miller W., Eichler E.E., Bork P., Suyama M., Torrents D., Waterston R.H., Wilson R.K.
Nature 434:724-731(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[11]Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S., Turner R. expand/collapse author list , Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W., Venter J.C.
Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA], VARIANT ALA-45.
[12]"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], VARIANT ALA-45.
Tissue: Eye.
[13]"cDNA cloning and expression analysis of NeuroD mRNA in human retina."
Acharya H.R., Dooley C.M., Thoreson W.B., Ahmad I.
Biochem. Biophys. Res. Commun. 233:459-463(1997) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 88-200.
Tissue: Retina.
[14]Shum C.H., Triche T.J.
Submitted (SEP-1995) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 147-198.
Tissue: Rhabdomyosarcoma.
[15]"Novel transcriptional potentiation of BETA2/NeuroD on the secretin gene promoter by the DNA-binding protein Finb/RREB-1."
Ray S.K., Nishitani J., Petry M.W., Fessing M.Y., Leiter A.B.
Mol. Cell. Biol. 23:259-271(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH RREB1.
[16]"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: INTERACTION WITH NR0B2; EP300 AND TCF3, HETERODIMERIZATION, TISSUE SPECIFICITY, SUBCELLULAR LOCATION.
[17]"Mutations in NEUROD1 are associated with the development of type 2 diabetes mellitus."
Malecki M.T., Jhala U.S., Antonellis A., Fields L., Doria A., Orban T., Saad M., Warram J.H., Montminy M., Krolewski A.S.
Nat. Genet. 23:323-328(1999) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANT MODY6 LEU-111.
+Additional computationally mapped references.

Web resources

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
U50822 Genomic DNA. Translation: AAA93480.1.
D82347 mRNA. Translation: BAA11558.1.
AF045152 Genomic DNA. Translation: AAC83145.1.
AB018693 Genomic DNA. Translation: BAA76603.1.
AB009997 Genomic DNA. Translation: BAA87605.1.
AB016079 Genomic DNA. Translation: BAA36519.1.
BT019731 mRNA. Translation: AAV38536.1.
AK313799 mRNA. Translation: BAG36535.1.
AB593068 mRNA. Translation: BAJ84015.1.
AB593069 mRNA. Translation: BAJ84016.1.
AB593070 mRNA. Translation: BAJ84017.1.
AB593071 mRNA. Translation: BAJ84018.1.
AC013733 Genomic DNA. Translation: AAY24267.1.
CH471058 Genomic DNA. Translation: EAX10983.1.
BC009046 mRNA. Translation: AAH09046.1.
U80578 mRNA. Translation: AAC51318.1.
U36472 mRNA. Translation: AAA79702.1.
RefSeqNP_002491.2. NM_002500.4.
UniGeneHs.574626.
Hs.709709.

3D structure databases

ProteinModelPortalQ13562.
SMRQ13562. Positions 102-159.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid110833. 9 interactions.
IntActQ13562. 1 interaction.
STRING9606.ENSP00000295108.

PTM databases

PhosphoSiteQ13562.

Polymorphism databases

DMDM311033428.

Proteomic databases

PaxDbQ13562.
PRIDEQ13562.

Protocols and materials databases

DNASU4760.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000295108; ENSP00000295108; ENSG00000162992.
GeneID4760.
KEGGhsa:4760.
UCSCuc002uof.4. human.

Organism-specific databases

CTD4760.
GeneCardsGC02M182505.
HGNCHGNC:7762. NEUROD1.
HPACAB022450.
HPA003278.
MIM125853. phenotype.
601724. gene.
606391. phenotype.
606394. phenotype.
neXtProtNX_Q13562.
Orphanet552. MODY syndrome.
PharmGKBPA31564.
GenAtlasSearch...

Phylogenomic databases

eggNOGNOG287211.
HOVERGENHBG000250.
InParanoidQ13562.
KOK08033.
OMAQDEEHET.
OrthoDBEOG722J8S.
PhylomeDBQ13562.
TreeFamTF315153.

Enzyme and pathway databases

ReactomeREACT_111045. Developmental Biology.

Gene expression databases

BgeeQ13562.
CleanExHS_NEUROD1.
GenevestigatorQ13562.

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

GeneWikiNEUROD1.
GenomeRNAi4760.
NextBio18336.
PROQ13562.
SOURCESearch...

Entry information

Entry nameNDF1_HUMAN
AccessionPrimary (citable) accession number: Q13562
Secondary accession number(s): B2R9I8 expand/collapse secondary AC list , F1T0E1, O00343, Q13340, Q5U095, Q96TH0, Q99455, Q9UEC8
Entry history
Integrated into UniProtKB/Swiss-Prot: November 1, 1997
Last sequence update: November 2, 2010
Last modified: April 16, 2014
This is version 143 of the entry and version 3 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

Relevant documents

SIMILARITY comments

Index of protein domains and families

MIM cross-references

Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot

Human polymorphisms and disease mutations

Index of human polymorphisms and disease mutations

Human entries with polymorphisms or disease mutations

List of human entries with polymorphisms or disease mutations

Human chromosome 2

Human chromosome 2: entries, gene names and cross-references to MIM