NOTC1_HUMAN - dbPTM
NOTC1_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID NOTC1_HUMAN
UniProt AC P46531
Protein Name Neurogenic locus notch homolog protein 1
Gene Name NOTCH1
Organism Homo sapiens (Human).
Sequence Length 2555
Subcellular Localization Cell membrane
Single-pass type I membrane protein .
Notch 1 intracellular domain: Nucleus . Following proteolytical processing NICD is translocated to the nucleus. Nuclear location may require MEGF10.
Protein Description Functions as a receptor for membrane-bound ligands Jagged1, Jagged2 and Delta1 to regulate cell-fate determination. Upon ligand activation through the released notch intracellular domain (NICD) it forms a transcriptional activator complex with RBPJ/RBPSUH and activates genes of the enhancer of split locus. Affects the implementation of differentiation, proliferation and apoptotic programs. Involved in angiogenesis; negatively regulates endothelial cell proliferation and migration and angiogenic sprouting. Involved in the maturation of both CD4+ and CD8+ cells in the thymus. Important for follicular differentiation and possibly cell fate selection within the follicle. During cerebellar development, functions as a receptor for neuronal DNER and is involved in the differentiation of Bergmann glia. Represses neuronal and myogenic differentiation. May play an essential role in postimplantation development, probably in some aspect of cell specification and/or differentiation. May be involved in mesoderm development, somite formation and neurogenesis. May enhance HIF1A function by sequestering HIF1AN away from HIF1A. Required for the THBS4 function in regulating protective astrogenesis from the subventricular zone (SVZ) niche after injury. Involved in determination of left/right symmetry by modulating the balance between motile and immotile (sensory) cilia at the left-right organiser (LRO)..
Protein Sequence MPPLLAPLLCLALLPALAARGPRCSQPGETCLNGGKCEAANGTEACVCGGAFVGPRCQDPNPCLSTPCKNAGTCHVVDRRGVADYACSCALGFSGPLCLTPLDNACLTNPCRNGGTCDLLTLTEYKCRCPPGWSGKSCQQADPCASNPCANGGQCLPFEASYICHCPPSFHGPTCRQDVNECGQKPGLCRHGGTCHNEVGSYRCVCRATHTGPNCERPYVPCSPSPCQNGGTCRPTGDVTHECACLPGFTGQNCEENIDDCPGNNCKNGGACVDGVNTYNCRCPPEWTGQYCTEDVDECQLMPNACQNGGTCHNTHGGYNCVCVNGWTGEDCSENIDDCASAACFHGATCHDRVASFYCECPHGRTGLLCHLNDACISNPCNEGSNCDTNPVNGKAICTCPSGYTGPACSQDVDECSLGANPCEHAGKCINTLGSFECQCLQGYTGPRCEIDVNECVSNPCQNDATCLDQIGEFQCICMPGYEGVHCEVNTDECASSPCLHNGRCLDKINEFQCECPTGFTGHLCQYDVDECASTPCKNGAKCLDGPNTYTCVCTEGYTGTHCEVDIDECDPDPCHYGSCKDGVATFTCLCRPGYTGHHCETNINECSSQPCRHGGTCQDRDNAYLCFCLKGTTGPNCEINLDDCASSPCDSGTCLDKIDGYECACEPGYTGSMCNINIDECAGNPCHNGGTCEDGINGFTCRCPEGYHDPTCLSEVNECNSNPCVHGACRDSLNGYKCDCDPGWSGTNCDINNNECESNPCVNGGTCKDMTSGYVCTCREGFSGPNCQTNINECASNPCLNQGTCIDDVAGYKCNCLLPYTGATCEVVLAPCAPSPCRNGGECRQSEDYESFSCVCPTGWQGQTCEVDINECVLSPCRHGASCQNTHGGYRCHCQAGYSGRNCETDIDDCRPNPCHNGGSCTDGINTAFCDCLPGFRGTFCEEDINECASDPCRNGANCTDCVDSYTCTCPAGFSGIHCENNTPDCTESSCFNGGTCVDGINSFTCLCPPGFTGSYCQHDVNECDSQPCLHGGTCQDGCGSYRCTCPQGYTGPNCQNLVHWCDSSPCKNGGKCWQTHTQYRCECPSGWTGLYCDVPSVSCEVAAQRQGVDVARLCQHGGLCVDAGNTHHCRCQAGYTGSYCEDLVDECSPSPCQNGATCTDYLGGYSCKCVAGYHGVNCSEEIDECLSHPCQNGGTCLDLPNTYKCSCPRGTQGVHCEINVDDCNPPVDPVSRSPKCFNNGTCVDQVGGYSCTCPPGFVGERCEGDVNECLSNPCDARGTQNCVQRVNDFHCECRAGHTGRRCESVINGCKGKPCKNGGTCAVASNTARGFICKCPAGFEGATCENDARTCGSLRCLNGGTCISGPRSPTCLCLGPFTGPECQFPASSPCLGGNPCYNQGTCEPTSESPFYRCLCPAKFNGLLCHILDYSFGGGAGRDIPPPLIEEACELPECQEDAGNKVCSLQCNNHACGWDGGDCSLNFNDPWKNCTQSLQCWKYFSDGHCDSQCNSAGCLFDGFDCQRAEGQCNPLYDQYCKDHFSDGHCDQGCNSAECEWDGLDCAEHVPERLAAGTLVVVVLMPPEQLRNSSFHFLRELSRVLHTNVVFKRDAHGQQMIFPYYGREEELRKHPIKRAAEGWAAPDALLGQVKASLLPGGSEGGRRRRELDPMDVRGSIVYLEIDNRQCVQASSQCFQSATDVAAFLGALASLGSLNIPYKIEAVQSETVEPPPPAQLHFMYVAAAAFVLLFFVGCGVLLSRKRRRQHGQLWFPEGFKVSEASKKKRREPLGEDSVGLKPLKNASDGALMDDNQNEWGDEDLETKKFRFEEPVVLPDLDDQTDHRQWTQQHLDAADLRMSAMAPTPPQGEVDADCMDVNVRGPDGFTPLMIASCSGGGLETGNSEEEEDAPAVISDFIYQGASLHNQTDRTGETALHLAARYSRSDAAKRLLEASADANIQDNMGRTPLHAAVSADAQGVFQILIRNRATDLDARMHDGTTPLILAARLAVEGMLEDLINSHADVNAVDDLGKSALHWAAAVNNVDAAVVLLKNGANKDMQNNREETPLFLAAREGSYETAKVLLDHFANRDITDHMDRLPRDIAQERMHHDIVRLLDEYNLVRSPQLHGAPLGGTPTLSPPLCSPNGYLGSLKPGVQGKKVRKPSSKGLACGSKEAKDLKARRKKSQDGKGCLLDSSGMLSPVDSLESPHGYLSDVASPPLLPSPFQQSPSVPLNHLPGMPDTHLGIGHLNVAAKPEMAALGGGGRLAFETGPPRLSHLPVASGTSTVLGSSSGGALNFTVGGSTSLNGQCEWLSRLQSGMVPNQYNPLRGSVAPGPLSTQAPSLQHGMVGPLHSSLAASALSQMMSYQGLPSTRLATQPHLVQTQQVQPQNLQMQQQNLQPANIQQQQSLQPPPPPPQPHLGVSSAASGHLGRSFLSGEPSQADVQPLGPSSLAVHTILPQESPALPTSLPSSLVPPVTAAQFLTPPSQHSYSSPVDNTPSHQLQVPEHPFLTPSPESPDQWSSSSPHSNVSDWSEGVSSPPTSMQSQIARIPEAFK
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
41N-linked_GlycosylationGGKCEAANGTEACVC
CCCCCCCCCCEEEEE
66.04UniProtKB CARBOHYD
65O-linked_GlycosylationQDPNPCLSTPCKNAG
CCCCCCCCCCCCCCC
36.70UniProtKB CARBOHYD
73O-linked_GlycosylationTPCKNAGTCHVVDRR
CCCCCCCCEEEECCC
9.31-
116O-linked_GlycosylationNPCRNGGTCDLLTLT
CCCCCCCCCCEEEEE
12.30-
146O-linked_GlycosylationQQADPCASNPCANGG
CCCCCCCCCCCCCCC
48.28UniProtKB CARBOHYD
174O-linked_GlycosylationPPSFHGPTCRQDVNE
CHHHCCCCCCCCHHH
25.55OGP
194O-linked_GlycosylationGLCRHGGTCHNEVGS
CCCCCCCCCCCCCCC
18.38-
232O-linked_GlycosylationSPCQNGGTCRPTGDV
CCCCCCCCCCCCCCC
13.5224226769
311O-linked_GlycosylationNACQNGGTCHNTHGG
CHHHCCCCCCCCCCC
16.40-
341O-linked_GlycosylationENIDDCASAACFHGA
CCHHHHHHHHHHCCC
23.80UniProtKB CARBOHYD
349O-linked_GlycosylationAACFHGATCHDRVAS
HHHHCCCCCCHHHHE
18.24-
378O-linked_GlycosylationHLNDACISNPCNEGS
ECCCHHCCCCCCCCC
34.30UniProtKB CARBOHYD
435O-linked_GlycosylationKCINTLGSFECQCLQ
HHHHHCCCEECEECC
22.4530127001
458O-linked_GlycosylationIDVNECVSNPCQNDA
ECHHHHHCCCCCCCC
46.87UniProtKB CARBOHYD
466O-linked_GlycosylationNPCQNDATCLDQIGE
CCCCCCCCHHHHCCC
19.23-
496O-linked_GlycosylationVNTDECASSPCLHNG
ECCHHHCCCCCCCCC
46.61UniProtKB CARBOHYD
518PhosphorylationEFQCECPTGFTGHLC
EEECCCCCCCCCCEE
57.4922210691
534O-linked_GlycosylationYDVDECASTPCKNGA
ECHHHHCCCCCCCCC
44.53UniProtKB CARBOHYD
535PhosphorylationDVDECASTPCKNGAK
CHHHHCCCCCCCCCC
17.7422210691
609O-linked_GlycosylationTNINECSSQPCRHGG
CCHHHCCCCCCCCCC
50.21UniProtKB CARBOHYD
617O-linked_GlycosylationQPCRHGGTCQDRDNA
CCCCCCCCCCCCCCC
16.16-
647O-linked_GlycosylationINLDDCASSPCDSGT
ECHHHHCCCCCCCCC
40.94UniProtKB CARBOHYD
692O-linked_GlycosylationNPCHNGGTCEDGING
CCCCCCCCCCCCCCC
17.70-
722O-linked_GlycosylationSEVNECNSNPCVHGA
HHHHHHCCCCCCCCH
54.53UniProtKB CARBOHYD
759O-linked_GlycosylationINNNECESNPCVNGG
CCCCCCCCCCCCCCC
58.70UniProtKB CARBOHYD
767O-linked_GlycosylationNPCVNGGTCKDMTSG
CCCCCCCCCCCCCCC
20.13-
784O-linked_GlycosylationCTCREGFSGPNCQTN
EEECCCCCCCCCCCC
65.28-
797O-linked_GlycosylationTNINECASNPCLNQG
CCHHHHHCCCCCCCC
53.62UniProtKB CARBOHYD
805O-linked_GlycosylationNPCLNQGTCIDDVAG
CCCCCCCCCHHHCCC
9.12-
822O-linked_GlycosylationCNCLLPYTGATCEVV
CCEECCCCCCEEEEE
20.5728314751
825O-linked_GlycosylationLLPYTGATCEVVLAP
ECCCCCCEEEEEEEC
15.56OGP
859O-linked_GlycosylationSFSCVCPTGWQGQTC
CEEEECCCCCCCCEE
46.02OGP
900PhosphorylationCHCQAGYSGRNCETD
EEECCCCCCCCCCCC
30.29-
921O-linked_GlycosylationNPCHNGGSCTDGINT
CCCCCCCCCCCCCCH
18.42-
923O-linked_GlycosylationCHNGGSCTDGINTAF
CCCCCCCCCCCCHHH
38.67OGP
951O-linked_GlycosylationEDINECASDPCRNGA
HHHHHHCCCCCCCCC
54.46UniProtKB CARBOHYD
959N-linked_GlycosylationDPCRNGANCTDCVDS
CCCCCCCCCCCCCCE
30.53UniProtKB CARBOHYD
997O-linked_GlycosylationSSCFNGGTCVDGINS
CCCCCCCEECCCCCC
15.68-
1027O-linked_GlycosylationHDVNECDSQPCLHGG
CCHHCCCCCCCCCCC
47.91UniProtKB CARBOHYD
1035O-linked_GlycosylationQPCLHGGTCQDGCGS
CCCCCCCCCCCCCCC
16.16-
1065O-linked_GlycosylationNLVHWCDSSPCKNGG
CCEEHHCCCCCCCCC
32.80UniProtKB CARBOHYD
1159O-linked_GlycosylationSPCQNGATCTDYLGG
CCCCCCCCCCHHCCC
19.82-
1179N-linked_GlycosylationVAGYHGVNCSEEIDE
EEECCCCCCCHHHHH
28.34UniProtKB CARBOHYD
1189O-linked_GlycosylationEEIDECLSHPCQNGG
HHHHHHHCCCCCCCC
36.72UniProtKB CARBOHYD
1197O-linked_GlycosylationHPCQNGGTCLDLPNT
CCCCCCCCCCCCCCC
15.99-
1241N-linked_GlycosylationRSPKCFNNGTCVDQV
CCCCCCCCCCEEEEE
27.22UniProtKB CARBOHYD
1273O-linked_GlycosylationGDVNECLSNPCDARG
CCHHHHHCCCCCCCC
50.84UniProtKB CARBOHYD
1317AcetylationGCKGKPCKNGGTCAV
CCCCCCCCCCCEEEE
68.1319828305
1362O-linked_GlycosylationLRCLNGGTCISGPRS
EEECCCCCCCCCCCC
14.20-
1379O-linked_GlycosylationCLCLGPFTGPECQFP
EEEECCCCCCCCCCC
55.77-
1402O-linked_GlycosylationNPCYNQGTCEPTSES
CCCCCCCCCCCCCCC
12.1624226769
1406O-linked_GlycosylationNQGTCEPTSESPFYR
CCCCCCCCCCCCCCH
23.88OGP
1489N-linked_GlycosylationNFNDPWKNCTQSLQC
CCCCCCCCCCHHHHH
30.14UniProtKB CARBOHYD
1580UbiquitinationTLVVVVLMPPEQLRN
EEEEEEECCHHHHCC
3.3421963094
1581UbiquitinationLVVVVLMPPEQLRNS
EEEEEECCHHHHCCC
25.7223503661
1587N-linked_GlycosylationMPPEQLRNSSFHFLR
CCHHHHCCCCHHHHH
51.07UniProtKB CARBOHYD
1589O-linked_GlycosylationPEQLRNSSFHFLREL
HHHHCCCCHHHHHHH
26.7028314751
1708O-linked_GlycosylationAFLGALASLGSLNIP
HHHHHHHHHCCCCCC
33.83OGP
1725O-linked_GlycosylationIEAVQSETVEPPPPA
EEEEECCCCCCCCCH
35.1024226769
1779O-linked_GlycosylationGFKVSEASKKKRREP
CCCCCHHHHHHCCCC
40.7428314751
1791PhosphorylationREPLGEDSVGLKPLK
CCCCCCCCCCCCCCC
17.4928555341
1795AcetylationGEDSVGLKPLKNASD
CCCCCCCCCCCCCCC
42.2325953088
1795UbiquitinationGEDSVGLKPLKNASD
CCCCCCCCCCCCCCC
42.2329967540
1801PhosphorylationLKPLKNASDGALMDD
CCCCCCCCCCCCCCC
46.0730576142
1821UbiquitinationGDEDLETKKFRFEEP
CCCCHHHCCEECCCC
40.3121963094
1822UbiquitinationDEDLETKKFRFEEPV
CCCHHHCCEECCCCE
49.5521906983
1861PhosphorylationRMSAMAPTPPQGEVD
HHHHCCCCCCCCCCC
37.7518669648
1889PhosphorylationFTPLMIASCSGGGLE
CCCEEEEEECCCCCC
9.6328348404
1891PhosphorylationPLMIASCSGGGLETG
CEEEEEECCCCCCCC
37.6728348404
1897PhosphorylationCSGGGLETGNSEEEE
ECCCCCCCCCCCCCC
46.8621685388
1900PhosphorylationGGLETGNSEEEEDAP
CCCCCCCCCCCCCCC
47.9721685388
1927PhosphorylationLHNQTDRTGETALHL
CCCCCCCHHHHHHHH
42.03-
1930PhosphorylationQTDRTGETALHLAAR
CCCCHHHHHHHHHHH
35.54-
1939PhosphorylationLHLAARYSRSDAAKR
HHHHHHHCCHHHHHH
21.5428102081
1941PhosphorylationLAARYSRSDAAKRLL
HHHHHCCHHHHHHHH
26.1728102081
1946MethylationSRSDAAKRLLEASAD
CCHHHHHHHHHHHCC
39.52115385661
1951PhosphorylationAKRLLEASADANIQD
HHHHHHHHCCCCCCC
19.80-
1955HydroxylationLEASADANIQDNMGR
HHHHCCCCCCCCCCC
32.7617573339
1986PhosphorylationILIRNRATDLDARMH
HHCCCCCCCCCCCCC
33.5824719451
1996PhosphorylationDARMHDGTTPLILAA
CCCCCCCCHHHHHHH
31.16-
1997PhosphorylationARMHDGTTPLILAAR
CCCCCCCHHHHHHHH
22.94-
2022HydroxylationINSHADVNAVDDLGK
HHCCCCCCCCCHHHH
34.49-
2074PhosphorylationLAAREGSYETAKVLL
HHHCCCCHHHHHHHH
28.3122461510
2090PhosphorylationHFANRDITDHMDRLP
HHCCCCCHHHHHHCC
24.9224719451
2116PhosphorylationIVRLLDEYNLVRSPQ
HHHHHHHCCCCCCCC
17.2927642862
2121PhosphorylationDEYNLVRSPQLHGAP
HHCCCCCCCCCCCCC
14.9830108239
2132PhosphorylationHGAPLGGTPTLSPPL
CCCCCCCCCCCCCCC
15.9927080861
2134PhosphorylationAPLGGTPTLSPPLCS
CCCCCCCCCCCCCCC
39.4427080861
2136PhosphorylationLGGTPTLSPPLCSPN
CCCCCCCCCCCCCCC
27.2728450419
2141PhosphorylationTLSPPLCSPNGYLGS
CCCCCCCCCCCCCCC
29.1427080861
2145PhosphorylationPLCSPNGYLGSLKPG
CCCCCCCCCCCCCCC
17.9628450419
2148PhosphorylationSPNGYLGSLKPGVQG
CCCCCCCCCCCCCCC
30.5328450419
2150AcetylationNGYLGSLKPGVQGKK
CCCCCCCCCCCCCCC
41.2326051181
2157AcetylationKPGVQGKKVRKPSSK
CCCCCCCCCCCCCCC
54.8437798817
2160AcetylationVQGKKVRKPSSKGLA
CCCCCCCCCCCCCCC
52.8437798809
2162PhosphorylationGKKVRKPSSKGLACG
CCCCCCCCCCCCCCC
47.9523312004
2163PhosphorylationKKVRKPSSKGLACGS
CCCCCCCCCCCCCCC
38.9923312004
2164AcetylationKVRKPSSKGLACGSK
CCCCCCCCCCCCCCH
63.3837798851
2171AcetylationKGLACGSKEAKDLKA
CCCCCCCHHHHHHHH
47.1523749302
2174AcetylationACGSKEAKDLKARRK
CCCCHHHHHHHHHHH
65.7637798841
2211PhosphorylationESPHGYLSDVASPPL
CCCCCCCCCCCCCCC
22.8926074081
2215PhosphorylationGYLSDVASPPLLPSP
CCCCCCCCCCCCCCC
27.2226074081
2221PhosphorylationASPPLLPSPFQQSPS
CCCCCCCCCCCCCCC
38.0126074081
2274O-linked_GlycosylationETGPPRLSHLPVASG
CCCCCCCCCCCCCCC
25.0228314751
2280O-linked_GlycosylationLSHLPVASGTSTVLG
CCCCCCCCCCEEEEC
42.7228314751
2282O-linked_GlycosylationHLPVASGTSTVLGSS
CCCCCCCCEEEECCC
20.8028314751
2284O-linked_GlycosylationPVASGTSTVLGSSSG
CCCCCCEEEECCCCC
21.4228314751
2323PhosphorylationSGMVPNQYNPLRGSV
CCCCCCCCCCCCCCC
25.9526356563
2461O-linked_GlycosylationHTILPQESPALPTSL
EECCCCCCCCCCCCC
15.3828314751
2466O-linked_GlycosylationQESPALPTSLPSSLV
CCCCCCCCCCCHHCC
43.6928314751
2511PhosphorylationVPEHPFLTPSPESPD
CCCCCCCCCCCCCCC
23.31-
2513PhosphorylationEHPFLTPSPESPDQW
CCCCCCCCCCCCCCC
35.74-
2516PhosphorylationFLTPSPESPDQWSSS
CCCCCCCCCCCCCCC
36.84-
2521PhosphorylationPESPDQWSSSSPHSN
CCCCCCCCCCCCCCC
18.0816880534
2522PhosphorylationESPDQWSSSSPHSNV
CCCCCCCCCCCCCCH
31.6916880534
2523PhosphorylationSPDQWSSSSPHSNVS
CCCCCCCCCCCCCHH
42.2316880534
2524PhosphorylationPDQWSSSSPHSNVSD
CCCCCCCCCCCCHHH
28.6916880534

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
1897TPhosphorylationKinaseCSNK2A1P68400
GPS
1900SPhosphorylationKinaseCSNK2A1P68400
GPS
2511TPhosphorylationKinaseCDK19Q9BWU1
PSP
2511TPhosphorylationKinaseCDK3Q00526
PSP
2511TPhosphorylationKinaseCDK8P49336
PSP
2511TPhosphorylationKinaseDYRK2Q92630
PSP
2511TPhosphorylationKinaseHIPK2Q9H2X6
PSP
2511TPhosphorylationKinaseMAP3K1Q13233
GPS
2513SPhosphorylationKinaseCDK19Q9BWU1
PSP
2513SPhosphorylationKinaseCDK3Q00526
PSP
2513SPhosphorylationKinaseCDK8P49336
PSP
2516SPhosphorylationKinaseCDK19Q9BWU1
PSP
2516SPhosphorylationKinaseCDK3Q00526
PSP
2516SPhosphorylationKinaseCDK8P49336
PSP
-KUbiquitinationE3 ubiquitin ligaseMDM2Q00987
PMID:23252402
-KUbiquitinationE3 ubiquitin ligaseFBXW7Q969H0
PMID:17274947
-KUbiquitinationE3 ubiquitin ligaseITCHQ96J02
PMID:12682059
-KUbiquitinationE3 ubiquitin ligaseNEDD4P46934
PMID:15620649

Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference
1759Kubiquitylation

23886940
1955NHydroxylation

17573339
2022NHydroxylation

-

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 NOTC1_HUMAN !!

Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
LCK_HUMANLCKphysical
14583609
PK3CA_HUMANPIK3CAphysical
14583609
CNTN1_HUMANCNTN1physical
14567914
TYY1_HUMANYY1physical
12913000
SUH_HUMANRBPJphysical
12644465
DTX1_HUMANDTX1physical
11564735
SNW1_HUMANSNW1physical
11404076
NOTC3_HUMANNOTCH3genetic
11404076
XRCC6_HUMANXRCC6physical
16169070
NFKB1_HUMANNFKB1physical
8642313
DLL1_HUMANDLL1physical
11006133
JAG1_HUMANJAG1physical
11006133
JAG2_HUMANJAG2physical
11006133
LEF1_HUMANLEF1physical
11604490
NUMB_HUMANNUMBphysical
8755477
GSK3B_HUMANGSK3Bphysical
12123574
NOTC1_HUMANNOTCH1physical
10669757
NFKB1_HUMANNFKB1physical
11418662
MAML1_HUMANMAML1physical
11101851
NOV_HUMANNOVphysical
12050162
FBXW7_HUMANFBXW7physical
11425854
MAML1_HUMANMAML1physical
12370315
MAML2_HUMANMAML2physical
12370315
MAML3_HUMANMAML3physical
12370315
SUH_HUMANRBPJphysical
9111040
ITCH_MOUSEItchphysical
18628966
FBXW7_HUMANFBXW7physical
17646408
CBL_HUMANCBLphysical
11777909
CTNB1_HUMANCTNNB1physical
19000719
SNW1_HUMANSNW1physical
15546612
SNAI1_HUMANSNAI1physical
22128911
MDM2_HUMANMDM2physical
22128911
RUNX3_HUMANRUNX3physical
19800882
SUH_HUMANRBPJphysical
19800882
SUH_HUMANRBPJphysical
17636029
A4_HUMANAPPgenetic
17368826
APBB1_HUMANAPBB1genetic
17368826
KAT5_HUMANKAT5genetic
17368826
A4_HUMANAPPphysical
17368826
APBB1_HUMANAPBB1physical
17368826
KAT5_HUMANKAT5physical
17368826
EP300_HUMANEP300physical
22100894
MAML1_HUMANMAML1physical
22100894
SUH_HUMANRBPJphysical
22100894
FBXW7_HUMANFBXW7physical
17646409
EPN1_HUMANEPN1physical
20573067
FBXW7_HUMANFBXW7physical
17526737
SUH_HUMANRBPJphysical
17526737
SUH_HUMANRBPJphysical
21820430
MAML1_HUMANMAML1physical
21820430
JAG1_HUMANJAG1physical
21820430
FBXW7_HUMANFBXW7physical
21820430
MAML1_HUMANMAML1physical
23022380
SUH_HUMANRBPJphysical
23022380
MAML3_HUMANMAML3physical
23022380
NOTC2_HUMANNOTCH2physical
23022380
NOTC3_HUMANNOTCH3physical
23022380
AAPK1_HUMANPRKAA1physical
23022380
MK01_HUMANMAPK1physical
23022380
LIMK2_HUMANLIMK2physical
23022380
ROCK1_HUMANROCK1physical
23022380
TAB1_HUMANTAB1physical
23022380
MOB1A_HUMANMOB1Aphysical
23022380
HCLS1_HUMANHCLS1physical
23022380
RANB9_HUMANRANBP9physical
23022380
RBP10_HUMANRANBP10physical
23022380
VAV_HUMANVAV1physical
23022380
ARHG2_HUMANARHGEF2physical
23022380
UBP7_HUMANUSP7physical
23022380
UBP11_HUMANUSP11physical
23022380
UBP15_HUMANUSP15physical
23022380
PP2AA_HUMANPPP2CAphysical
23022380
2AAA_HUMANPPP2R1Aphysical
23022380
2ABA_HUMANPPP2R2Aphysical
23022380
PP6R1_HUMANPPP6R1physical
23022380
PP6R3_HUMANPPP6R3physical
23022380
FBXW7_HUMANFBXW7physical
23022380
ARI1_HUMANARIH1physical
23022380
ARI2_HUMANARIH2physical
23022380
TRI32_HUMANTRIM32physical
23022380
APC7_HUMANANAPC7physical
23022380
APC1_HUMANANAPC1physical
23022380
CDC23_HUMANCDC23physical
23022380
CDC27_HUMANCDC27physical
23022380
APC5_HUMANANAPC5physical
23022380
STK38_HUMANSTK38physical
23022380
CSN1_HUMANGPS1physical
23022380
CAND1_HUMANCAND1physical
23022380
SLFN5_HUMANSLFN5physical
23022380
SLN11_HUMANSLFN11physical
23022380
CARL2_HUMANRLTPRphysical
23022380
LRCH1_HUMANLRCH1physical
23022380
WDR11_HUMANWDR11physical
23022380
NCKPL_HUMANNCKAP1Lphysical
23022380
ARMC8_HUMANARMC8physical
23022380
ERH_HUMANERHphysical
23022380
WDR6_HUMANWDR6physical
23022380
MIC1_HUMANC18orf8physical
23022380
PTBP3_HUMANPTBP3physical
23022380
SMCA4_HUMANSMARCA4physical
23022380
PB1_HUMANPBRM1physical
23022380
SMRC2_HUMANSMARCC2physical
23022380
SMRC1_HUMANSMARCC1physical
23022380
HLTF_HUMANHLTFphysical
23022380
SMCA5_HUMANSMARCA5physical
23022380
SMC1A_HUMANSMC1Aphysical
23022380
SMC3_HUMANSMC3physical
23022380
PDS5A_HUMANPDS5Aphysical
23022380
SCC4_HUMANMAU2physical
23022380
SMHD1_HUMANSMCHD1physical
23022380
TIF1B_HUMANTRIM28physical
23022380
WIZ_HUMANWIZphysical
23022380
RB_HUMANRB1physical
23022380
PHF8_HUMANPHF8physical
23022380
BRE1B_HUMANRNF40physical
23022380
CHD4_HUMANCHD4physical
23022380
RBBP4_HUMANRBBP4physical
23022380
P66B_HUMANGATAD2Bphysical
23022380
HDAC1_HUMANHDAC1physical
23022380
KDM1A_HUMANKDM1Aphysical
23022380
RING1_HUMANRING1physical
23022380
RING2_HUMANRNF2physical
23022380
FRYL_HUMANFRYLphysical
23022380
HCFC1_HUMANHCFC1physical
23022380
CN166_HUMANC14orf166physical
23022380
ASCC3_HUMANASCC3physical
23022380
SRRT_HUMANSRRTphysical
23022380
TBL1R_HUMANTBL1XR1physical
23022380
WWTR1_HUMANWWTR1physical
23022380
DDX17_HUMANDDX17physical
23022380
HTSF1_HUMANHTATSF1physical
23022380
MED23_HUMANMED23physical
23022380
MED25_HUMANMED25physical
23022380
BC11B_HUMANBCL11Bphysical
23022380
IKZF1_HUMANIKZF1physical
23022380
IKZF2_HUMANIKZF2physical
23022380
IKZF3_HUMANIKZF3physical
23022380
HTF4_HUMANTCF12physical
23022380
RUNX1_HUMANRUNX1physical
23022380
SMAD9_HUMANSMAD9physical
23022380
ZBTB2_HUMANZBTB2physical
23022380
ZBED4_HUMANZBED4physical
23022380
RFX1_HUMANRFX1physical
23022380
IF16_HUMANIFI16physical
23022380
PRKDC_HUMANPRKDCphysical
23022380
PARP1_HUMANPARP1physical
23022380
TOP2B_HUMANTOP2Bphysical
23022380
MCM3_HUMANMCM3physical
23022380
MCM5_HUMANMCM5physical
23022380
RFC1_HUMANRFC1physical
23022380
RFC4_HUMANRFC4physical
23022380
MMS19_HUMANMMS19physical
23022380
RIF1_HUMANRIF1physical
23022380
PRP6_HUMANPRPF6physical
23022380
PRP8_HUMANPRPF8physical
23022380
PRP19_HUMANPRPF19physical
23022380
RBM10_HUMANRBM10physical
23022380
DHX15_HUMANDHX15physical
23022380
DHX8_HUMANDHX8physical
23022380
SNUT1_HUMANSART1physical
23022380
PTBP1_HUMANPTBP1physical
23022380
CNOT1_HUMANCNOT1physical
23022380
XPO5_HUMANXPO5physical
23022380
NBEA_HUMANNBEAphysical
23022380
LRBA_HUMANLRBAphysical
23022380
MDN1_HUMANMDN1physical
23022380
TNPO1_HUMANTNPO1physical
23022380
IMB1_HUMANKPNB1physical
23022380
IPO5_HUMANIPO5physical
23022380
TPPC9_HUMANTRAPPC9physical
23022380
TPC10_HUMANTRAPPC10physical
23022380
TCPG_HUMANCCT3physical
23022380
TCPZ_HUMANCCT6Aphysical
23022380
TCPQ_HUMANCCT8physical
23022380
VPS39_HUMANVPS39physical
23022380
VPS11_HUMANVPS11physical
23022380
KIF3A_HUMANKIF3Aphysical
23022380
KIF2A_HUMANKIF2Aphysical
23022380
PP2AB_HUMANPPP2CBphysical
23022380
KCC4_HUMANCAMK4physical
23103515
MDM2_HUMANMDM2physical
23252402
XIAP_HUMANXIAPphysical
17318174
SUH_HUMANRBPJphysical
11997524
MAML1_HUMANMAML1physical
11997524
MAML1_HUMANMAML1physical
11390662
SUH_HUMANRBPJphysical
11390662
SUH_HUMANRBPJphysical
22143792
WWP1_HUMANWWP1physical
16785210
TGFR1_HUMANTGFBR1physical
24399296
CBL_HUMANCBLphysical
26052821
SUH_HUMANRBPJphysical
26033182
RND3_HUMANRND3physical
26108681
KPCD_HUMANPRKCDphysical
24662486
RAB5A_HUMANRAB5Aphysical
24662486
RAB7A_HUMANRAB7Aphysical
24662486
LAMP1_HUMANLAMP1physical
24662486
SQSTM_HUMANSQSTM1physical
27806347
FBXW7_HUMANFBXW7physical
27806347
FANCC_HUMANFANCCphysical
19321451
FANCF_HUMANFANCFphysical
19321451
FANCA_HUMANFANCAphysical
19321451
FANCG_HUMANFANCGphysical
19321451
SUH_HUMANRBPJphysical
19321451
MAGA1_HUMANMAGEA1physical
28459460
FBXW7_HUMANFBXW7physical
28459460
PRAF3_HUMANARL6IP5physical
27229929
B3GT4_HUMANB3GALT4physical
27229929
CE57L_HUMANCEP57L1physical
27229929
CI062_HUMANC9orf62physical
27229929
CO4A6_HUMANCOL4A6physical
27229929
EXT1_HUMANEXT1physical
27229929
F185A_HUMANFAM185Aphysical
27229929
P33MX_HUMANKIAA1191physical
27229929
LNX2_HUMANLNX2physical
27229929
RHOA_HUMANRHOAphysical
27229929
GOGA2_HUMANGOLGA2physical
27229929
HMGN5_HUMANHMGN5physical
27229929
MAGD1_HUMANMAGED1physical
27229929
GOPC_HUMANGOPCphysical
27229929
OBF1_HUMANPOU2AF1physical
27229929
TLE3_HUMANTLE3physical
27229929
DAZP2_HUMANDAZAP2physical
27229929
FBXW7_HUMANFBXW7physical
27229929
BACD3_HUMANKCTD10physical
25401743
CUL3_HUMANCUL3physical
25401743
DTX4_HUMANDTX4physical
28611181
ADA10_HUMANADAM10physical
28611181

Drug and Disease Associations
Kegg Disease
H00002 Acute lymphoblastic leukemia (ALL) (precursor T lymphoblastic leukemia)
H00554 Bicuspid aortic valve
OMIM Disease
109730Aortic valve disease 1 (AOVD1)
616028Adams-Oliver syndrome 5 (AOS5)
Kegg Drug
There are no disease associations of PTM sites.
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of NOTC1_HUMAN

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Related Literatures of Post-Translational Modification
Hydroxylation
ReferencePubMed
"Asparaginyl hydroxylation of the Notch ankyrin repeat domain byfactor inhibiting hypoxia-inducible factor.";
Coleman M.L., McDonough M.A., Hewitson K.S., Coles C., Mecinovic J.,Edelmann M., Cook K.M., Cockman M.E., Lancaster D.E., Kessler B.M.,Oldham N.J., Ratcliffe P.J., Schofield C.J.;
J. Biol. Chem. 282:24027-24038(2007).
Cited for: PROTEIN SEQUENCE OF 1947-1962, INTERACTION WITH HIF1AN, HYDROXYLATIONAT ASN-1955, AND MASS SPECTROMETRY.

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