UniProt ID | NDF1_MOUSE | |
---|---|---|
UniProt AC | Q60867 | |
Protein Name | Neurogenic differentiation factor 1 | |
Gene Name | Neurod1 | |
Organism | Mus musculus (Mouse). | |
Sequence Length | 357 | |
Subcellular Localization | Cytoplasm. Nucleus . In pancreatic islet cells, shuttles to the nucleus in response to glucose stimulation. Colocalizes with NR0B2 in the nucleus (By similarity).. | |
Protein Description | 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.. | |
Protein Sequence | MTKSYSESGLMGEPQPQGPPSWTDECLSSQDEEHEADKKEDELEAMNAEEDSLRNGGEEEEEDEDLEEEEEEEEEEEDQKPKRRGPKKKKMTKARLERFKLRRMKANARERNRMHGLNAALDNLRKVVPCYSKTQKLSKIETLRLAKNYIWALSEILRSGKSPDLVSFVQTLCKGLSQPTTNLVAGCLQLNPRTFLPEQNPDMPPHLPTASASFPVHPYSYQSPGLPSPPYGTMDSSHVFHVKPPPHAYSAALEPFFESPLTDCTSPSFDGPLSPPLSINGNFSFKHEPSAEFEKNYAFTMHYPAATLAGPQSHGSIFSSGAAAPRCEIPIDNIMSFDSHSHHERVMSAQLNAIFHD | |
Overview of Protein Modification Sites with Functional and Structural Information | ||
* ASA = Accessible Surface Area
Locations | Modification | Substrate Peptides & Secondary Structure |
ASA (%) | Reference | Orthologous Protein Cluster |
---|---|---|---|---|---|
162 | Phosphorylation | EILRSGKSPDLVSFV HHHHCCCCHHHHHHH | 27.46 | 22817900 | |
259 | Phosphorylation | ALEPFFESPLTDCTS CCHHHHCCCCCCCCC | 21.76 | 15797719 | |
266 | Phosphorylation | SPLTDCTSPSFDGPL CCCCCCCCCCCCCCC | 25.52 | 15797719 | |
274 | Phosphorylation | PSFDGPLSPPLSING CCCCCCCCCCEEECC | 27.83 | 15797719 | |
336 | Phosphorylation | IPIDNIMSFDSHSHH CCCCCCCCCCCCCHH | 23.31 | - |
Modified Location | Modified Residue | Modification | Type of Upstream Proteins | Gene Name of Upstream Proteins | UniProt AC of Upstream Proteins | Sources |
---|---|---|---|---|---|---|
162 | S | Phosphorylation | Kinase | MAPK1 | P28482 | GPS |
162 | S | Phosphorylation | Kinase | MK01 | P63085 | PhosphoELM |
259 | S | Phosphorylation | Kinase | MAPK1 | P28482 | GPS |
259 | S | Phosphorylation | Kinase | MK01 | P63085 | PhosphoELM |
266 | S | Phosphorylation | Kinase | MAPK1 | P28482 | GPS |
266 | S | Phosphorylation | Kinase | MK01 | P63085 | PhosphoELM |
274 | S | Phosphorylation | Kinase | MAPK1 | P28482 | GPS |
274 | S | Phosphorylation | Kinase | MK01 | P63085 | PhosphoELM |
336 | S | Phosphorylation | Kinase | CAMK2 | - | Uniprot |
* Distance = the distance between SAP position and PTM sites.
Modified Location | Modification | Variant Position (Distance <= 10) |
Residue Change | SAP | Related Disease | Reference |
---|---|---|---|---|---|---|
Oops, there are no SNP-PTM records of NDF1_MOUSE !! |
Interacting Protein | Gene Name | Interaction Type | PPI Reference | Domain-Domain Interactions |
---|---|---|---|---|
MIXL1_MOUSE | Mixl1 | physical | 20211142 | |
NDF1_MOUSE | Neurod1 | physical | 15701640 | |
RBL1_MOUSE | Rbl1 | physical | 15701640 | |
NR4A1_MOUSE | Nr4a1 | physical | 15701640 | |
RB_MOUSE | Rb1 | physical | 15701640 |
Kegg Drug | ||||||
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DrugBank | ||||||
There are no disease associations of PTM sites. |
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Phosphorylation | |
Reference | PubMed |
"Context-dependent regulation of NeuroD activity and proteinaccumulation."; 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). Cited for: FUNCTION, PHOSPHORYLATION AT SER-259; SER-266 AND SER-274, ANDMUTAGENESIS OF SER-259; SER-266 AND SER-274. | |
"Regulation of insulin gene transcription by ERK1 and ERK2 inpancreatic 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). Cited for: FUNCTION, HETERODIMERIZATION, PHOSPHORYLATION AT SER-162; SER-259;SER-266 AND SER-274, TISSUE SPECIFICITY, AND MUTAGENESIS OF SER-162;SER-259; SER-266 AND SER-274. |