UniProt ID | NUMBL_HUMAN | |
---|---|---|
UniProt AC | Q9Y6R0 | |
Protein Name | Numb-like protein | |
Gene Name | NUMBL | |
Organism | Homo sapiens (Human). | |
Sequence Length | 609 | |
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 | MSRSAAASGGPRRPERHLPPAPCGAPGPPETCRTEPDGAGTMNKLRQSLRRRKPAYVPEASRPHQWQADEDAVRKGTCSFPVRYLGHVEVEESRGMHVCEDAVKKLKAMGRKSVKSVLWVSADGLRVVDDKTKDLLVDQTIEKVSFCAPDRNLDKAFSYICRDGTTRRWICHCFLALKDSGERLSHAVGCAFAACLERKQRREKECGVTAAFDASRTSFAREGSFRLSGGGRPAEREAPDKKKAEAAAAPTVAPGPAQPGHVSPTPATTSPGEKGEAGTPVAAGTTAAAIPRRHAPLEQLVRQGSFRGFPALSQKNSPFKRQLSLRLNELPSTLQRRTDFQVKGTVPEMEPPGAGDSDSINALCTQISSSFASAGAPAPGPPPATTGTSAWGEPSVPPAAAFQPGHKRTPSEAERWLEEVSQVAKAQQQQQQQQQQQQQQQQQQQQAASVAPVPTMPPALQPFPAPVGPFDAAPAQVAVFLPPPHMQPPFVPAYPGLGYPPMPRVPVVGITPSQMVANAFCSAAQLQPQPATLLGKAGAFPPPAIPSAPGSQARPRPNGAPWPPEPAPAPAPELDPFEAQWAALEGKATVEKPSNPFSGDLQKTFEIEL | |
Overview of Protein Modification Sites with Functional and Structural Information | ||
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* ASA = Accessible Surface Area
Locations | Modification | Substrate Peptides & Secondary Structure |
ASA (%) | Reference | Orthologous Protein Cluster |
---|---|---|---|---|---|
2 | Phosphorylation | ------MSRSAAASG ------CCHHHHHCC | 34.64 | 24505115 | |
4 | Phosphorylation | ----MSRSAAASGGP ----CCHHHHHCCCC | 18.23 | 23403867 | |
8 | Phosphorylation | MSRSAAASGGPRRPE CCHHHHHCCCCCCCH | 39.29 | 28857561 | |
48 | Phosphorylation | TMNKLRQSLRRRKPA HHHHHHHHHHHCCCC | 19.87 | 29496963 | |
84 | Phosphorylation | TCSFPVRYLGHVEVE CCCCEEEEEEEEEEE | 19.78 | 28188228 | |
96 | Sulfoxidation | EVEESRGMHVCEDAV EEEHHCCCCCCHHHH | 1.76 | 30846556 | |
209 | Phosphorylation | REKECGVTAAFDASR HHHHHCCCEEEECCC | 9.50 | - | |
224 | Phosphorylation | TSFAREGSFRLSGGG CCCCCCCCEECCCCC | 11.48 | 25159151 | |
228 | Phosphorylation | REGSFRLSGGGRPAE CCCCEECCCCCCCCC | 31.00 | 25159151 | |
251 | Phosphorylation | AEAAAAPTVAPGPAQ HHHHCCCCCCCCCCC | 25.27 | 23927012 | |
263 | Phosphorylation | PAQPGHVSPTPATTS CCCCCCCCCCCCCCC | 19.85 | 29255136 | |
265 | Phosphorylation | QPGHVSPTPATTSPG CCCCCCCCCCCCCCC | 20.32 | 29255136 | |
268 | Phosphorylation | HVSPTPATTSPGEKG CCCCCCCCCCCCCCC | 29.07 | 29255136 | |
269 | Phosphorylation | VSPTPATTSPGEKGE CCCCCCCCCCCCCCC | 34.72 | 29255136 | |
270 | Phosphorylation | SPTPATTSPGEKGEA CCCCCCCCCCCCCCC | 26.93 | 29255136 | |
279 | Phosphorylation | GEKGEAGTPVAAGTT CCCCCCCCCCCCCCC | 22.95 | 29255136 | |
285 | O-linked_Glycosylation | GTPVAAGTTAAAIPR CCCCCCCCCCCCCCC | 14.45 | 30379171 | |
285 | Phosphorylation | GTPVAAGTTAAAIPR CCCCCCCCCCCCCCC | 14.45 | 25002506 | |
286 | Phosphorylation | TPVAAGTTAAAIPRR CCCCCCCCCCCCCCC | 17.24 | 25002506 | |
305 | Phosphorylation | EQLVRQGSFRGFPAL HHHHHCCCCCCCHHH | 11.93 | 23401153 | |
307 | Methylation | LVRQGSFRGFPALSQ HHHCCCCCCCHHHCC | 47.76 | - | |
313 | Phosphorylation | FRGFPALSQKNSPFK CCCCHHHCCCCCHHH | 41.01 | 30266825 | |
317 | Phosphorylation | PALSQKNSPFKRQLS HHHCCCCCHHHHHHH | 38.46 | 29496963 | |
324 | Phosphorylation | SPFKRQLSLRLNELP CHHHHHHHHHHHHCC | 11.78 | 25159151 | |
332 | Phosphorylation | LRLNELPSTLQRRTD HHHHHCCHHHHHCCC | 55.14 | 25850435 | |
333 | Phosphorylation | RLNELPSTLQRRTDF HHHHCCHHHHHCCCC | 25.60 | 23312004 | |
409 | Phosphorylation | FQPGHKRTPSEAERW CCCCCCCCHHHHHHH | 35.65 | 25159151 | |
411 | Phosphorylation | PGHKRTPSEAERWLE CCCCCCHHHHHHHHH | 49.15 | 28355574 | |
421 | Phosphorylation | ERWLEEVSQVAKAQQ HHHHHHHHHHHHHHH | 23.40 | 23403867 | |
594 | Phosphorylation | KATVEKPSNPFSGDL CCEEECCCCCCCCCC | 69.10 | 20068231 | |
598 | Phosphorylation | EKPSNPFSGDLQKTF ECCCCCCCCCCCHHE | 32.43 | 20068231 | |
604 | Phosphorylation | FSGDLQKTFEIEL-- CCCCCCHHEEEEC-- | 17.34 | 20068231 |
Modified Location | Modified Residue | Modification | Type of Upstream Proteins | Gene Name of Upstream Proteins | UniProt AC of Upstream Proteins | Sources |
---|---|---|---|---|---|---|
Oops, there are no upstream regulatory protein records of NUMBL_HUMAN !! |
Modified Location | Modified Residue | Modification | Function | Reference | ||
---|---|---|---|---|---|---|
Oops, there are no descriptions of PTM sites of NUMBL_HUMAN !! |
* 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 NUMBL_HUMAN !! |
Interacting Protein | Gene Name | Interaction Type | PPI Reference | Domain-Domain Interactions |
---|---|---|---|---|
TAB2_HUMAN | TAB2 | physical | 18299187 | |
TRAF5_HUMAN | TRAF5 | physical | 22593207 | |
TMC5_HUMAN | TMC5 | physical | 21988832 | |
TRAF5_HUMAN | TRAF5 | physical | 21988832 | |
PSA3_HUMAN | PSMA3 | physical | 21988832 | |
SIAH1_HUMAN | SIAH1 | physical | 21988832 | |
TPO_HUMAN | THPO | physical | 21988832 | |
TRAF6_HUMAN | TRAF6 | physical | 21988832 | |
RIPK1_HUMAN | RIPK1 | physical | 21988832 | |
SPSB3_HUMAN | SPSB3 | physical | 25416956 | |
CBY1_HUMAN | CBY1 | physical | 27173435 |
Kegg Disease | ||||||
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There are no disease associations of PTM sites. | ||||||
OMIM Disease | ||||||
There are no disease associations of PTM sites. | ||||||
Kegg Drug | ||||||
There are no disease associations of PTM sites. | ||||||
DrugBank | ||||||
There are no disease associations of PTM sites. |
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Phosphorylation | |
Reference | PubMed |
"A quantitative atlas of mitotic phosphorylation."; Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,Elledge S.J., Gygi S.P.; Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-263; THR-268 ANDTHR-279, AND MASS SPECTROMETRY. | |
"Global, in vivo, and site-specific phosphorylation dynamics insignaling networks."; Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P.,Mann M.; Cell 127:635-648(2006). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-263 AND SER-411, ANDMASS SPECTROMETRY. |