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

* ASA = Accessible Surface Area

Locations Modification Substrate Peptides
&
Secondary Structure
ASA (%) Reference Orthologous
Protein Cluster
2Phosphorylation------MSRSAAASG
------CCHHHHHCC
34.6424505115
4Phosphorylation----MSRSAAASGGP
----CCHHHHHCCCC
18.2323403867
8PhosphorylationMSRSAAASGGPRRPE
CCHHHHHCCCCCCCH
39.2928857561
48PhosphorylationTMNKLRQSLRRRKPA
HHHHHHHHHHHCCCC
19.8729496963
84PhosphorylationTCSFPVRYLGHVEVE
CCCCEEEEEEEEEEE
19.7828188228
96SulfoxidationEVEESRGMHVCEDAV
EEEHHCCCCCCHHHH
1.7630846556
209PhosphorylationREKECGVTAAFDASR
HHHHHCCCEEEECCC
9.50-
224PhosphorylationTSFAREGSFRLSGGG
CCCCCCCCEECCCCC
11.4825159151
228PhosphorylationREGSFRLSGGGRPAE
CCCCEECCCCCCCCC
31.0025159151
251PhosphorylationAEAAAAPTVAPGPAQ
HHHHCCCCCCCCCCC
25.2723927012
263PhosphorylationPAQPGHVSPTPATTS
CCCCCCCCCCCCCCC
19.8529255136
265PhosphorylationQPGHVSPTPATTSPG
CCCCCCCCCCCCCCC
20.3229255136
268PhosphorylationHVSPTPATTSPGEKG
CCCCCCCCCCCCCCC
29.0729255136
269PhosphorylationVSPTPATTSPGEKGE
CCCCCCCCCCCCCCC
34.7229255136
270PhosphorylationSPTPATTSPGEKGEA
CCCCCCCCCCCCCCC
26.9329255136
279PhosphorylationGEKGEAGTPVAAGTT
CCCCCCCCCCCCCCC
22.9529255136
285O-linked_GlycosylationGTPVAAGTTAAAIPR
CCCCCCCCCCCCCCC
14.4530379171
285PhosphorylationGTPVAAGTTAAAIPR
CCCCCCCCCCCCCCC
14.4525002506
286PhosphorylationTPVAAGTTAAAIPRR
CCCCCCCCCCCCCCC
17.2425002506
305PhosphorylationEQLVRQGSFRGFPAL
HHHHHCCCCCCCHHH
11.9323401153
307MethylationLVRQGSFRGFPALSQ
HHHCCCCCCCHHHCC
47.76-
313PhosphorylationFRGFPALSQKNSPFK
CCCCHHHCCCCCHHH
41.0130266825
317PhosphorylationPALSQKNSPFKRQLS
HHHCCCCCHHHHHHH
38.4629496963
324PhosphorylationSPFKRQLSLRLNELP
CHHHHHHHHHHHHCC
11.7825159151
332PhosphorylationLRLNELPSTLQRRTD
HHHHHCCHHHHHCCC
55.1425850435
333PhosphorylationRLNELPSTLQRRTDF
HHHHCCHHHHHCCCC
25.6023312004
409PhosphorylationFQPGHKRTPSEAERW
CCCCCCCCHHHHHHH
35.6525159151
411PhosphorylationPGHKRTPSEAERWLE
CCCCCCHHHHHHHHH
49.1528355574
421PhosphorylationERWLEEVSQVAKAQQ
HHHHHHHHHHHHHHH
23.4023403867
594PhosphorylationKATVEKPSNPFSGDL
CCEEECCCCCCCCCC
69.1020068231
598PhosphorylationEKPSNPFSGDLQKTF
ECCCCCCCCCCCHHE
32.4320068231
604PhosphorylationFSGDLQKTFEIEL--
CCCCCCHHEEEEC--
17.3420068231

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

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

Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

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

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 NUMBL_HUMAN !!

Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
TAB2_HUMANTAB2physical
18299187
TRAF5_HUMANTRAF5physical
22593207
TMC5_HUMANTMC5physical
21988832
TRAF5_HUMANTRAF5physical
21988832
PSA3_HUMANPSMA3physical
21988832
SIAH1_HUMANSIAH1physical
21988832
TPO_HUMANTHPOphysical
21988832
TRAF6_HUMANTRAF6physical
21988832
RIPK1_HUMANRIPK1physical
21988832
SPSB3_HUMANSPSB3physical
25416956
CBY1_HUMANCBY1physical
27173435

Drug and Disease Associations
Kegg Disease
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.
Regulatory Network of NUMBL_HUMAN

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Related Literatures of Post-Translational Modification
Phosphorylation
ReferencePubMed
"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.

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