NUMB_MOUSE - dbPTM
NUMB_MOUSE - PTM Information in dbPTM
Basic Information of Protein
UniProt ID NUMB_MOUSE
UniProt AC Q9QZS3
Protein Name Protein numb homolog
Gene Name Numb
Organism Mus musculus (Mouse).
Sequence Length 653
Subcellular Localization Membrane
Peripheral membrane protein.
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 neurogenesis. Also involved postnatally in the subventricular zone (SVZ) neurogenesis by regulating SVZ neuroblasts survival and ependymal wall integrity. May also mediate local repair of brain ventricular wall damage..
Protein Sequence MNKLRQSFRRKKDVYVPEASRPHQWQTDEEGVRTGKCSFPVKYLGHVEVDESRGMHICEDAVKRLKAERKFFKGFFGKTGKKAVKAVLWVSADGLRVVDEKTKDLIVDQTIEKVSFCAPDRNFDRAFSYICRDGTTRRWICHCFMAVKDTGERLSHAVGCAFAACLERKQKREKECGVTATFDASRTTFTREGSFRVTTATEQAEREEIMKQLQDAKKAETDKTVVGPSVAPGNTAPSPSSPTSPTPDGTASSEMNNPHAIPRRHAPIEQLARQGSFRGFPALSQKMSPFKRQLSLRINELPSTMQRKTDFPIKNTVPEVEGEAESISSLCSQITSAFSTPSEDPFSSAPMTKPVTLVAPQSPVLQANGTDSASHVLTAKPANTALAHVAMPVRETNPWAHVPDAANKEIAAIHPGTEWGQSSGAASPGLFQAGHRRTPSEADRWLEEVSKSVRAQQPQVSAAPLQPVLQPPPPAAIAPPAPPFQGHAFLTSQPVPVGVVPPLQPAFVPTQSYPVANGMPYPASNVPVVGITPSQMVANVFGTAGHPQTTHPHQSPSLAKQQTFPQYETSSATTSPFFKPPAQHLNGSAAFNGVDNGGLASGNRHAEVPPGTCPVDPFEAQWAALESKSKQRTNPSPTNPFSSDLQKTFEIEL
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
7Phosphorylation-MNKLRQSFRRKKDV
-CCHHHHHHHHHCCE
17.8121454597
102PhosphorylationLRVVDEKTKDLIVDQ
CEECCHHHCCEEEEC
27.95-
174UbiquitinationERKQKREKECGVTAT
HHHHHHHHHHCCEEE
63.4422790023
188PhosphorylationTFDASRTTFTREGSF
EEECCCCEEECEEEE
23.1523984901
190PhosphorylationDASRTTFTREGSFRV
ECCCCEEECEEEEEE
26.2223984901
194PhosphorylationTTFTREGSFRVTTAT
CEEECEEEEEEEEHH
12.7226824392
198PhosphorylationREGSFRVTTATEQAE
CEEEEEEEEHHHHHH
13.3726239621
199PhosphorylationEGSFRVTTATEQAER
EEEEEEEEHHHHHHH
28.8223140645
201PhosphorylationSFRVTTATEQAEREE
EEEEEEHHHHHHHHH
26.9123140645
211UbiquitinationAEREEIMKQLQDAKK
HHHHHHHHHHHHHHH
54.2222790023
224PhosphorylationKKAETDKTVVGPSVA
HHHCCCCCEECCCCC
24.1926239621
229PhosphorylationDKTVVGPSVAPGNTA
CCCEECCCCCCCCCC
25.6126239621
235PhosphorylationPSVAPGNTAPSPSSP
CCCCCCCCCCCCCCC
45.9526239621
238PhosphorylationAPGNTAPSPSSPTSP
CCCCCCCCCCCCCCC
34.6423684622
240PhosphorylationGNTAPSPSSPTSPTP
CCCCCCCCCCCCCCC
53.9726239621
241PhosphorylationNTAPSPSSPTSPTPD
CCCCCCCCCCCCCCC
35.2622942356
243PhosphorylationAPSPSSPTSPTPDGT
CCCCCCCCCCCCCCC
49.6522942356
244PhosphorylationPSPSSPTSPTPDGTA
CCCCCCCCCCCCCCC
30.1126239621
246PhosphorylationPSSPTSPTPDGTASS
CCCCCCCCCCCCCCC
33.5026239621
250PhosphorylationTSPTPDGTASSEMNN
CCCCCCCCCCCCCCC
30.6526643407
252PhosphorylationPTPDGTASSEMNNPH
CCCCCCCCCCCCCCC
27.0326239621
253PhosphorylationTPDGTASSEMNNPHA
CCCCCCCCCCCCCCC
38.1026239621
276PhosphorylationEQLARQGSFRGFPAL
HHHHHCCCCCCCHHH
11.9326824392
284PhosphorylationFRGFPALSQKMSPFK
CCCCHHHHHHCCHHH
29.8426745281
286UbiquitinationGFPALSQKMSPFKRQ
CCHHHHHHCCHHHHH
37.6622790023
288PhosphorylationPALSQKMSPFKRQLS
HHHHHHCCHHHHHHH
33.9326643407
295PhosphorylationSPFKRQLSLRINELP
CHHHHHHHHHHHCCC
13.7822942356
304PhosphorylationRINELPSTMQRKTDF
HHHCCCCCCCCCCCC
18.5129514104
345 (in isoform 4)Phosphorylation-27.2826643407
351 (in isoform 4)Phosphorylation-8.2226643407
356 (in isoform 2)Phosphorylation-24.8426643407
357 (in isoform 4)Phosphorylation-2.9226643407
362PhosphorylationVTLVAPQSPVLQANG
EEEEECCCCEEEECC
18.8629472430
362 (in isoform 4)Phosphorylation-18.8626643407
362 (in isoform 2)Phosphorylation-18.8626643407
363 (in isoform 4)Phosphorylation-26.1226643407
367 (in isoform 4)Phosphorylation-16.5626643407
368 (in isoform 2)Phosphorylation-40.7226643407
373 (in isoform 2)Phosphorylation-13.3826643407
374 (in isoform 2)Phosphorylation-20.3426643407
378 (in isoform 2)Phosphorylation-31.3926643407
417PhosphorylationIAAIHPGTEWGQSSG
EEEECCCCCCCCCCC
32.7723984901
422PhosphorylationPGTEWGQSSGAASPG
CCCCCCCCCCCCCCC
27.1423984901
423PhosphorylationGTEWGQSSGAASPGL
CCCCCCCCCCCCCCC
25.2723984901
427PhosphorylationGQSSGAASPGLFQAG
CCCCCCCCCCCHHCC
20.9726239621
438PhosphorylationFQAGHRRTPSEADRW
HHCCCCCCHHHHHHH
30.9925521595
440PhosphorylationAGHRRTPSEADRWLE
CCCCCCHHHHHHHHH
44.8225521595
450PhosphorylationDRWLEEVSKSVRAQQ
HHHHHHHHHHHHHCC
23.6125159016
555PhosphorylationQTTHPHQSPSLAKQQ
CCCCCCCCHHHHHCC
17.2727149854
557PhosphorylationTHPHQSPSLAKQQTF
CCCCCCHHHHHCCCC
46.3227149854
575PhosphorylationETSSATTSPFFKPPA
CCCCCCCCCCCCCCH
18.5028285833
613GlutathionylationAEVPPGTCPVDPFEA
CCCCCCCCCCCHHHH
3.7124333276
633PhosphorylationESKSKQRTNPSPTNP
HCCCCCCCCCCCCCC
49.3327742792
636PhosphorylationSKQRTNPSPTNPFSS
CCCCCCCCCCCCCCH
46.5625521595
638PhosphorylationQRTNPSPTNPFSSDL
CCCCCCCCCCCCHHH
60.9227742792
642PhosphorylationPSPTNPFSSDLQKTF
CCCCCCCCHHHHHHE
24.9728833060
643PhosphorylationSPTNPFSSDLQKTFE
CCCCCCCHHHHHHEE
42.6028833060

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
276SPhosphorylationKinaseCAMK1Q91YS8
Uniprot
295SPhosphorylationKinaseCAMK1Q91YS8
Uniprot
295SPhosphorylationKinasePRKCZQ05513
GPS
295SPhosphorylationKinasePKCZQ02956
PSP
-KUbiquitinationE3 ubiquitin ligaseLnx1O70263
PMID:22199232

Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference
276SPhosphorylation

-
295SPhosphorylation

-

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 NUMB_MOUSE !!

Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
EPS15_MOUSEEps15physical
9303539
NOTC1_MOUSENotch1physical
20844536
LNX1_MOUSELnx1physical
9535908
CADH1_MOUSECdh1physical
17589506
NMDZ1_MOUSEGrin1physical
17589506
CTNA1_MOUSECtnna1physical
17589506
CTNB1_MOUSECtnnb1physical
17589506
AP2A2_HUMANAP2A2physical
23211419
AP2B1_HUMANAP2B1physical
23211419
AP2M1_HUMANAP2M1physical
23211419
AP2A1_HUMANAP2A1physical
23211419
EPS15_HUMANEPS15physical
23211419
REPS1_HUMANREPS1physical
23211419
EP15R_HUMANEPS15L1physical
23211419
AP2S1_HUMANAP2S1physical
23211419
AP1B1_HUMANAP1B1physical
23211419
RBP1_HUMANRALBP1physical
23211419
ECHA_HUMANHADHAphysical
23211419
SRRM2_HUMANSRRM2physical
23211419
BMP2K_HUMANBMP2Kphysical
23211419
1433E_HUMANYWHAEphysical
23211419
FXR1_HUMANFXR1physical
23211419
BCR_HUMANBCRphysical
23211419
BCLF1_HUMANBCLAF1physical
23211419

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

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Related Literatures of Post-Translational Modification
Phosphorylation
ReferencePubMed
"Large-scale phosphorylation analysis of mouse liver.";
Villen J., Beausoleil S.A., Gerber S.A., Gygi S.P.;
Proc. Natl. Acad. Sci. U.S.A. 104:1488-1493(2007).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-633 AND SER-636, ANDMASS SPECTROMETRY.

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