NUMBL_MOUSE - PTM Information in dbPTM

Basic Information of Protein

• UniProt ID: NUMBL_MOUSE
• UniProt AC: O08919
• Protein Name: Numb-like protein
• Gene Name: Numbl
• Organism: Mus musculus (Mouse).
• Sequence Length: 604
• Subcellular Localization: Cytoplasm . Symmetrically distributed throughout the cytoplasm in non dividing neuroblasts of the CNS.
• Protein Description: Plays a role in the process of neurogenesis. Required throughout embryonic neurogenesis to maintain neural progenitor cells, also called radial glial cells (RGCs), by allowing their daughter cells to choose progenitor over neuronal cell fate. Not required for the proliferation of neural progenitor cells before the onset of embryonic neurogenesis. Also required postnatally in the subventricular zone (SVZ) neurogenesis by regulating SVZ neuroblasts survival and ependymal wall integrity. Negative regulator of NF-kappa-B signaling pathway. The inhibition of NF-kappa-B activation is mediated at least in part, by preventing MAP3K7IP2 to interact with polyubiquitin chains of TRAF6 and RIPK1 and by stimulating the 'Lys-48'-linked polyubiquitination and degradation of TRAF6 in cortical neurons..
• Protein Sequence: MSRSAAASGGPRRPDQHLSPAPCGASGPPETFRTESDGAGTMNKLRQSLRRRKPAYVPEASRPHQWQADEDAVRKGTCSFPVRYLGHVEVEESRGMHVCEDAVKKLKAMGRKSVKSVLWVSADGLRVVDDKTKDLLVDQTIEKVSFCAPDRNLDKAFSYICRDGTTRRWICHCFLALKDSGERLSHAVGCAFAACLERKQRREKECGVTAAFDASRTSFAREGSFRLSGGGRPAEREAGDKKKAEAAAAPAVAPGPAQPGHVSPTPATTSPGEKGEAGTPVAAGTTAAAIPRRHAPLEQLVRQGSFRGFPALSQKNSPFKRQLSLRLNELPSTLQRRTDFQVKGTVPEMEPPGTGDSDGINALCTQISSSFASAGAPASGPPPATTGTSAWGEPSVPAAAAFQPGHKRTPSEAERWLEEVSQVAKAQQQQQQQQQQQQQQQATSVPPMPTMAPTLQPFSAPVGPFDTAAAQVAVFLPPTHMQPPFVPAYPGLGYPPMPRVPVVGITPSQMVANAFCSAAQLQPQPATLLGKAGAFPPPAAPSAPGGQARPRPNGAPWPPEPAPAPAPELDPFEAQWAALEGKPAVEKPSNPFSGDLQKTFEIEL

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
2	Phosphorylation	------MSRSAAASG ------CCHHHHHCC	34.64	27717184
48	Phosphorylation	TMNKLRQSLRRRKPA HHHHHHHHHHHCCCC	19.87	26824392
56	Phosphorylation	LRRRKPAYVPEASRP HHHCCCCCCCCCCCC	25.68	-
61	Phosphorylation	PAYVPEASRPHQWQA CCCCCCCCCCCCCCC	44.69	-
224	Phosphorylation	TSFAREGSFRLSGGG CCCCCCCCEECCCCC	11.48	26824392
228	Phosphorylation	REGSFRLSGGGRPAE CCCCEECCCCCCCCC	31.00	26824392
263	Phosphorylation	PAQPGHVSPTPATTS CCCCCCCCCCCCCCC	19.85	25521595
265	Phosphorylation	QPGHVSPTPATTSPG CCCCCCCCCCCCCCC	20.32	25521595
268	Phosphorylation	HVSPTPATTSPGEKG CCCCCCCCCCCCCCC	29.07	24925903
269	Phosphorylation	VSPTPATTSPGEKGE CCCCCCCCCCCCCCC	34.72	25521595
270	Phosphorylation	SPTPATTSPGEKGEA CCCCCCCCCCCCCCC	26.93	25521595
279	Phosphorylation	GEKGEAGTPVAAGTT CCCCCCCCCCCCCCC	22.95	25521595
285	Phosphorylation	GTPVAAGTTAAAIPR CCCCCCCCCCCCCCC	14.45	22817900
286	Phosphorylation	TPVAAGTTAAAIPRR CCCCCCCCCCCCCCC	17.24	25777480
305	Phosphorylation	EQLVRQGSFRGFPAL HHHHHCCCCCCCHHH	11.93	26824392
313	Phosphorylation	FRGFPALSQKNSPFK CCCCHHHCCCCCHHH	41.01	26745281
317	Phosphorylation	PALSQKNSPFKRQLS HHHCCCCCHHHHHHH	38.46	29899451
324	Phosphorylation	SPFKRQLSLRLNELP CHHHHHHHHHHHHCC	11.78	26824392
333	Phosphorylation	RLNELPSTLQRRTDF HHHHCCHHHHHCCCC	25.60	29514104
409	Phosphorylation	FQPGHKRTPSEAERW CCCCCCCCHHHHHHH	35.65	25521595
411	Phosphorylation	PGHKRTPSEAERWLE CCCCCCHHHHHHHHH	49.15	25521595
421	Phosphorylation	ERWLEEVSQVAKAQQ HHHHHHHHHHHHHHH	23.40	22324799

Upstream regulatory proteins (kinases for phosphorylation sites, E3 ubiquitin ligases of ubiquitination sites, ...)

Oops, there are no upstream regulatory protein records of NUMBL_MOUSE !!

Functions of PTM Sites

Oops, there are no descriptions of PTM sites of NUMBL_MOUSE !!

Disease-associated PTM Sites based on SAP

* Distance = the distance between SAP position and PTM sites.

Oops, there are no SNP-PTM records of NUMBL_MOUSE !!

Protein-Protein Interaction

Oops, there are no PPI records of NUMBL_MOUSE !!

Drug and Disease Associations

• Kegg Drug
• DrugBank
• There are no disease associations of PTM sites.

Related Literatures of Post-Translational Modification

Phosphorylation

"Qualitative and quantitative analyses of protein phosphorylation innaive and stimulated mouse synaptosomal preparations.";
Munton R.P., Tweedie-Cullen R., Livingstone-Zatchej M., Weinandy F.,Waidelich M., Longo D., Gehrig P., Potthast F., Rutishauser D.,Gerrits B., Panse C., Schlapbach R., Mansuy I.M.;
Mol. Cell. Proteomics 6:283-293(2007).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-263 AND THR-279, ANDMASS SPECTROMETRY.
PubMed: 17114649