NDF1_MOUSE - dbPTM
NDF1_MOUSE - PTM Information in dbPTM
Basic Information of Protein
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
Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations Modification Substrate Peptides
&
Secondary Structure
ASA (%) Reference Orthologous
Protein Cluster
162PhosphorylationEILRSGKSPDLVSFV
HHHHCCCCHHHHHHH
27.4622817900
259PhosphorylationALEPFFESPLTDCTS
CCHHHHCCCCCCCCC
21.7615797719
266PhosphorylationSPLTDCTSPSFDGPL
CCCCCCCCCCCCCCC
25.5215797719
274PhosphorylationPSFDGPLSPPLSING
CCCCCCCCCCEEECC
27.8315797719
336PhosphorylationIPIDNIMSFDSHSHH
CCCCCCCCCCCCCHH
23.31-

Upstream regulatory proteins (kinases for phosphorylation sites, E3 ubiquitin ligases of ubiquitination sites, ...)
Modified Location Modified Residue Modification Type of Upstream Proteins Gene Name of Upstream Proteins UniProt AC of Upstream Proteins Sources
162SPhosphorylationKinaseMAPK1P28482
GPS
162SPhosphorylationKinaseMK01P63085
PhosphoELM
259SPhosphorylationKinaseMAPK1P28482
GPS
259SPhosphorylationKinaseMK01P63085
PhosphoELM
266SPhosphorylationKinaseMAPK1P28482
GPS
266SPhosphorylationKinaseMK01P63085
PhosphoELM
274SPhosphorylationKinaseMAPK1P28482
GPS
274SPhosphorylationKinaseMK01P63085
PhosphoELM
336SPhosphorylationKinaseCAMK2-Uniprot

Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference
266SPhosphorylation

12810726
274SPhosphorylation

12810726
274SPhosphorylation

12810726
336SPhosphorylation

15797719

Disease-associated PTM Sites based on SAP

* 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 !!

Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
MIXL1_MOUSEMixl1physical
20211142
NDF1_MOUSENeurod1physical
15701640
RBL1_MOUSERbl1physical
15701640
NR4A1_MOUSENr4a1physical
15701640
RB_MOUSERb1physical
15701640

Drug and Disease Associations
Kegg Drug
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of NDF1_MOUSE

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Related Literatures of Post-Translational Modification
Phosphorylation
ReferencePubMed
"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.

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