NUMB_HUMAN - dbPTM
NUMB_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID NUMB_HUMAN
UniProt AC P49757
Protein Name Protein numb homolog
Gene Name NUMB {ECO:0000312|HGNC:HGNC:8060}
Organism Homo sapiens (Human).
Sequence Length 651
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 MNKLRQSFRRKKDVYVPEASRPHQWQTDEEGVRTGKCSFPVKYLGHVEVDESRGMHICEDAVKRLKAERKFFKGFFGKTGKKAVKAVLWVSADGLRVVDEKTKDLIVDQTIEKVSFCAPDRNFDRAFSYICRDGTTRRWICHCFMAVKDTGERLSHAVGCAFAACLERKQKREKECGVTATFDASRTTFTREGSFRVTTATEQAEREEIMKQMQDAKKAETDKIVVGSSVAPGNTAPSPSSPTSPTSDATTSLEMNNPHAIPRRHAPIEQLARQGSFRGFPALSQKMSPFKRQLSLRINELPSTMQRKTDFPIKNAVPEVEGEAESISSLCSQITNAFSTPEDPFSSAPMTKPVTVVAPQSPTFQANGTDSAFHVLAKPAHTALAPVAMPVRETNPWAHAPDAANKEIAATCSGTEWGQSSGAASPGLFQAGHRRTPSEADRWLEEVSKSVRAQQPQASAAPLQPVLQPPPPTAISQPASPFQGNAFLTSQPVPVGVVPALQPAFVPAQSYPVANGMPYPAPNVPVVGITPSQMVANVFGTAGHPQAAHPHQSPSLVRQQTFPHYEASSATTSPFFKPPAQHLNGSAAFNGVDDGRLASADRHTEVPTGTCPVDPFEAQWAALENKSKQRTNPSPTNPFSSDLQKTFEIEL
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		17.8129496963
12UbiquitinationRQSFRRKKDVYVPEA
HHHHHHHCCEECCCC		51.09-
15PhosphorylationFRRKKDVYVPEASRP
HHHHCCEECCCCCCC		22.0325394399
20PhosphorylationDVYVPEASRPHQWQT
CEECCCCCCCCCEEC		44.6920068231
27PhosphorylationSRPHQWQTDEEGVRT
CCCCCEECCCCCCCC		42.28-
36UbiquitinationEEGVRTGKCSFPVKY
CCCCCCCCCCCEEEE		26.54-
37S-palmitoylationEGVRTGKCSFPVKYL
CCCCCCCCCCEEEEC		5.5429295957
53MethylationHVEVDESRGMHICED
EEEECCCCCCEECHH		44.39115485797
55SulfoxidationEVDESRGMHICEDAV
EECCCCCCEECHHHH		1.5530846556
63MethylationHICEDAVKRLKAERK
EECHHHHHHHHHHHH		54.45-
63UbiquitinationHICEDAVKRLKAERK
EECHHHHHHHHHHHH		54.45-
73UbiquitinationKAERKFFKGFFGKTG
HHHHHHHHHHHCHHH		58.92-
91PhosphorylationVKAVLWVSADGLRVV
HHHHEEEECCCCEEC		14.73-
101 (in isoform 9)Phosphorylation-57.3130108239
102PhosphorylationLRVVDEKTKDLIVDQ
CEECCHHHCCEEEEC		27.9522817900
107 (in isoform 9)Phosphorylation-6.0825159151
109 (in isoform 9)Phosphorylation-33.2229507054
113 (in isoform 9)Phosphorylation-39.0526657352
118 (in isoform 9)Phosphorylation-13.6630108239
119 (in isoform 9)Phosphorylation-42.1330108239
121MethylationVSFCAPDRNFDRAFS
EEEECCCCCHHHHHH		44.66115485789
123 (in isoform 9)Phosphorylation-7.5729507054
160S-palmitoylationRLSHAVGCAFAACLE
HHHHHHHHHHHHHHH		1.9529295957
165S-palmitoylationVGCAFAACLERKQKR
HHHHHHHHHHHHHHH		3.4829295957
185PhosphorylationVTATFDASRTTFTRE
CEEEEECCCCEEECE		31.8130576142
187PhosphorylationATFDASRTTFTREGS
EEEECCCCEEECEEE		24.6230576142
190PhosphorylationDASRTTFTREGSFRV
ECCCCEEECEEEEEE		26.2230576142
194PhosphorylationTTFTREGSFRVTTAT
CEEECEEEEEEEEHH		12.7225159151
198PhosphorylationREGSFRVTTATEQAE
CEEEEEEEEHHHHHH		13.3723403867
199PhosphorylationEGSFRVTTATEQAER
EEEEEEEEHHHHHHH		28.8223403867
201PhosphorylationSFRVTTATEQAEREE
EEEEEEHHHHHHHHH		26.9123403867
210SulfoxidationQAEREEIMKQMQDAK
HHHHHHHHHHHHHHH		2.5221406390
228PhosphorylationTDKIVVGSSVAPGNT
CCEEEEECCCCCCCC		15.2729978859
229PhosphorylationDKIVVGSSVAPGNTA
CEEEEECCCCCCCCC		19.1718669648
235PhosphorylationSSVAPGNTAPSPSSP
CCCCCCCCCCCCCCC		45.9528102081
238PhosphorylationAPGNTAPSPSSPTSP
CCCCCCCCCCCCCCC		34.6430278072
240PhosphorylationGNTAPSPSSPTSPTS
CCCCCCCCCCCCCCC		53.9730278072
241PhosphorylationNTAPSPSSPTSPTSD
CCCCCCCCCCCCCCC		35.2628355574
243PhosphorylationAPSPSSPTSPTSDAT
CCCCCCCCCCCCCCC		49.6528102081
244PhosphorylationPSPSSPTSPTSDATT
CCCCCCCCCCCCCCC		29.5728355574
246PhosphorylationPSSPTSPTSDATTSL
CCCCCCCCCCCCCCE		38.7219276368
246 (in isoform 6)Phosphorylation-38.7230108239
247PhosphorylationSSPTSPTSDATTSLE
CCCCCCCCCCCCCEE		28.7328102081
250PhosphorylationTSPTSDATTSLEMNN
CCCCCCCCCCEECCC		23.1630278072
251PhosphorylationSPTSDATTSLEMNNP
CCCCCCCCCEECCCC		32.7930177828
252PhosphorylationPTSDATTSLEMNNPH
CCCCCCCCEECCCCC		20.2721130716
252 (in isoform 6)Phosphorylation-20.2725159151
254 (in isoform 6)Phosphorylation-39.3629507054
257 (in isoform 5)Phosphorylation-28.5530108239
258 (in isoform 6)Phosphorylation-17.1826657352
263 (in isoform 5)Phosphorylation-36.5825159151
263 (in isoform 6)Phosphorylation-36.5830108239
264 (in isoform 6)Phosphorylation-25.6030108239
265 (in isoform 5)Phosphorylation-36.8229507054
268 (in isoform 6)Phosphorylation-5.6729507054
269 (in isoform 5)Phosphorylation-38.1826657352
274 (in isoform 5)Phosphorylation-46.4030108239
275UbiquitinationIEQLARQGSFRGFPA
HHHHHHCCCCCCCHH		24.1721890473
275UbiquitinationIEQLARQGSFRGFPA
HHHHHHCCCCCCCHH		24.1721890473
275UbiquitinationIEQLARQGSFRGFPA
HHHHHHCCCCCCCHH		24.1721890473
275UbiquitinationIEQLARQGSFRGFPA
HHHHHHCCCCCCCHH		24.1721890473
275UbiquitinationIEQLARQGSFRGFPA
HHHHHHCCCCCCCHH		24.1721890473
275 (in isoform 3)Ubiquitination-24.1721890473
275 (in isoform 4)Ubiquitination-24.1721890473
275 (in isoform 5)Phosphorylation-24.1730108239
276PhosphorylationEQLARQGSFRGFPAL
HHHHHCCCCCCCHHH		11.9323401153
278MethylationLARQGSFRGFPALSQ
HHHCCCCCCCHHHHH		47.76-
279 (in isoform 5)Phosphorylation-30.7729507054
284PhosphorylationFRGFPALSQKMSPFK
CCCCHHHHHHCCHHH		29.8430266825
286UbiquitinationGFPALSQKMSPFKRQ
CCHHHHHHCCHHHHH		37.6621890473
286UbiquitinationGFPALSQKMSPFKRQ
CCHHHHHHCCHHHHH		37.6621890473
286 (in isoform 1)Ubiquitination-37.6621890473
286 (in isoform 2)Ubiquitination-37.6621890473
288PhosphorylationPALSQKMSPFKRQLS
HHHHHHCCHHHHHHH		33.9329496963
295PhosphorylationSPFKRQLSLRINELP
CHHHHHHHHHHHCCC		13.7817203073
303PhosphorylationLRINELPSTMQRKTD
HHHHCCCCCCCCCCC		49.4929255136
304PhosphorylationRINELPSTMQRKTDF
HHHCCCCCCCCCCCC		18.5129255136
344 (in isoform 4)Phosphorylation-29.3830108239
350 (in isoform 4)Phosphorylation-8.2225159151
352 (in isoform 4)Phosphorylation-31.1029507054
355PhosphorylationAPMTKPVTVVAPQSP
CCCCCCEEEECCCCC		20.1422199227
355 (in isoform 2)Phosphorylation-20.1430108239
356 (in isoform 4)Phosphorylation-3.3526657352
361PhosphorylationVTVVAPQSPTFQANG
EEEECCCCCCEECCC		25.5025159151
361 (in isoform 2)Phosphorylation-25.5025159151
361 (in isoform 4)Phosphorylation-25.5030108239
362 (in isoform 4)Phosphorylation-31.8030108239
363PhosphorylationVVAPQSPTFQANGTD
EECCCCCCEECCCCC		33.3625159151
363 (in isoform 2)Phosphorylation-33.3629507054
366 (in isoform 4)Phosphorylation-16.5429507054
367 (in isoform 2)Phosphorylation-43.0126657352
369PhosphorylationPTFQANGTDSAFHVL
CCEECCCCCCCHHHH		26.9626657352
371PhosphorylationFQANGTDSAFHVLAK
EECCCCCCCHHHHCC		32.4525850435
372 (in isoform 2)Phosphorylation-11.0230108239
373 (in isoform 2)Phosphorylation-4.7930108239
377 (in isoform 2)Phosphorylation-18.0729507054
411PhosphorylationANKEIAATCSGTEWG
HCCHHHHCCCCCCCC		9.7430108239
413PhosphorylationKEIAATCSGTEWGQS
CHHHHCCCCCCCCCC		44.3830108239
415PhosphorylationIAATCSGTEWGQSSG
HHHCCCCCCCCCCCC		16.5730108239
420PhosphorylationSGTEWGQSSGAASPG
CCCCCCCCCCCCCCC		27.1430266825
421PhosphorylationGTEWGQSSGAASPGL
CCCCCCCCCCCCCCC		25.2730266825
425PhosphorylationGQSSGAASPGLFQAG
CCCCCCCCCCCCCCC		20.9730266825
436PhosphorylationFQAGHRRTPSEADRW
CCCCCCCCHHHHHHH		30.9922167270
438PhosphorylationAGHRRTPSEADRWLE
CCCCCCHHHHHHHHH		44.8222167270
448PhosphorylationDRWLEEVSKSVRAQQ
HHHHHHHHHHHHHCC		23.6123927012
553PhosphorylationQAAHPHQSPSLVRQQ
CCCCCCCCHHHHHCC		17.2726657352
561PhosphorylationPSLVRQQTFPHYEAS
HHHHHCCCCCCCCCC		30.6927251275
565PhosphorylationRQQTFPHYEASSATT
HCCCCCCCCCCCCCC		17.2723898821
568PhosphorylationTFPHYEASSATTSPF
CCCCCCCCCCCCCCC		14.4723898821
569PhosphorylationFPHYEASSATTSPFF
CCCCCCCCCCCCCCC		36.3627251275
571PhosphorylationHYEASSATTSPFFKP
CCCCCCCCCCCCCCC		29.7427251275
572PhosphorylationYEASSATTSPFFKPP
CCCCCCCCCCCCCCC		33.8327251275
573PhosphorylationEASSATTSPFFKPPA
CCCCCCCCCCCCCCH		18.5027251275
586PhosphorylationPAQHLNGSAAFNGVD
CHHHCCCCCCCCCCC		18.4919664995
627PhosphorylationWAALENKSKQRTNPS
HHHHHCCCCCCCCCC		45.6726074081
631PhosphorylationENKSKQRTNPSPTNP
HCCCCCCCCCCCCCC		49.3323927012
634PhosphorylationSKQRTNPSPTNPFSS
CCCCCCCCCCCCCCH		46.5619664994
636PhosphorylationQRTNPSPTNPFSSDL
CCCCCCCCCCCCHHH		60.9228355574
640PhosphorylationPSPTNPFSSDLQKTF
CCCCCCCCHHHHHHE		24.9730266825
641PhosphorylationSPTNPFSSDLQKTFE
CCCCCCCHHHHHHEE		42.6023403867
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
7SPhosphorylationKinasePKCIP41743
PSP
7SPhosphorylationKinasePKCZQ05513
PSP
102TPhosphorylationKinaseAAK1Q2M2I8
Uniprot
265SPhosphorylationKinasePKCZQ05513
PSP
276SPhosphorylationKinaseCAMK1Q14012
Uniprot
276SPhosphorylationKinaseCAMK1Q63450
GPS
276SPhosphorylationKinaseCAMK2AP11275
PSP
276SPhosphorylationKinaseCAMK4P13234
PSP
276SPhosphorylationKinasePKCIP41743
PSP
284SPhosphorylationKinasePKCZQ05513
PSP
295SPhosphorylationKinaseCAMK1Q14012
Uniprot
295SPhosphorylationKinasePKCIP41743
PSP
-KUbiquitinationE3 ubiquitin ligaseMDM2Q00987
PMID:12646252
-KUbiquitinationE3 ubiquitin ligaseLNX2Q8N448
PMID:26451611
-KUbiquitinationE3 ubiquitin ligaseLNX1Q8TBB1
PMID:14990566
-KUbiquitinationE3 ubiquitin ligaseSIAH1Q8IUQ4
PMID:18213731
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_HUMAN !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
AP2A1_HUMANAP2A1physical
12942088
DPYL2_HUMANDPYSL2physical
12942088
L1CAM_HUMANL1CAMphysical
12942088
ITCH_HUMANITCHphysical
12682059
MDM2_HUMANMDM2physical
12646252
LNX1_HUMANLNX1physical
11782429
SIAH1_HUMANSIAH1physical
11752454
P53_HUMANTP53physical
18172499
MDM2_HUMANMDM2physical
18172499
GLI1_HUMANGLI1physical
20818436
ITCH_HUMANITCHphysical
20818436
P53_HUMANTP53physical
22157679
MDM2_HUMANMDM2physical
22337874
MDM2_MOUSEMdm2physical
9632782
EPS15_HUMANEPS15physical
10953014
A4_HUMANAPPphysical
21832049
NOTC1_HUMANNOTCH1physical
23252402
P53_HUMANTP53physical
23881403
RL3_HUMANRPL3physical
21988832
SIAH1_HUMANSIAH1physical
21988832
OLIG1_HUMANOLIG1physical
25814554
LNX2_HUMANLNX2physical
25814554
TERF2_HUMANTERF2physical
25814554
A4_HUMANAPPphysical
25241761
P53_HUMANTP53physical
27106262
MDM2_HUMANMDM2physical
27106262
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 NUMB_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-240; SER-241 ANDSER-244, AND MASS SPECTROMETRY.
"A probability-based approach for high-throughput proteinphosphorylation analysis and site localization.";
Beausoleil S.A., Villen J., Gerber S.A., Rush J., Gygi S.P.;
Nat. Biotechnol. 24:1285-1292(2006).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-634, AND MASSSPECTROMETRY.

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