NOTC1_MOUSE - dbPTM
NOTC1_MOUSE - PTM Information in dbPTM
Basic Information of Protein
UniProt ID NOTC1_MOUSE
UniProt AC Q01705
Protein Name Neurogenic locus notch homolog protein 1
Gene Name Notch1
Organism Mus musculus (Mouse).
Sequence Length 2531
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 MPRLLTPLLCLTLLPALAARGLRCSQPSGTCLNGGRCEVANGTEACVCSGAFVGQRCQDSNPCLSTPCKNAGTCHVVDHGGTVDYACSCPLGFSGPLCLTPLDNACLANPCRNGGTCDLLTLTEYKCRCPPGWSGKSCQQADPCASNPCANGGQCLPFESSYICRCPPGFHGPTCRQDVNECSQNPGLCRHGGTCHNEIGSYRCACRATHTGPHCELPYVPCSPSPCQNGGTCRPTGDTTHECACLPGFAGQNCEENVDDCPGNNCKNGGACVDGVNTYNCRCPPEWTGQYCTEDVDECQLMPNACQNGGTCHNTHGGYNCVCVNGWTGEDCSENIDDCASAACFQGATCHDRVASFYCECPHGRTGLLCHLNDACISNPCNEGSNCDTNPVNGKAICTCPSGYTGPACSQDVDECALGANPCEHAGKCLNTLGSFECQCLQGYTGPRCEIDVNECISNPCQNDATCLDQIGEFQCICMPGYEGVYCEINTDECASSPCLHNGHCMDKINEFQCQCPKGFNGHLCQYDVDECASTPCKNGAKCLDGPNTYTCVCTEGYTGTHCEVDIDECDPDPCHYGSCKDGVATFTCLCQPGYTGHHCETNINECHSQPCRHGGTCQDRDNSYLCLCLKGTTGPNCEINLDDCASNPCDSGTCLDKIDGYECACEPGYTGSMCNVNIDECAGSPCHNGGTCEDGIAGFTCRCPEGYHDPTCLSEVNECNSNPCIHGACRDGLNGYKCDCAPGWSGTNCDINNNECESNPCVNGGTCKDMTSGYVCTCREGFSGPNCQTNINECASNPCLNQGTCIDDVAGYKCNCPLPYTGATCEVVLAPCATSPCKNSGVCKESEDYESFSCVCPTGWQGQTCEVDINECVKSPCRHGASCQNTNGSYRCLCQAGYTGRNCESDIDDCRPNPCHNGGSCTDGINTAFCDCLPGFQGAFCEEDINECASNPCQNGANCTDCVDSYTCTCPVGFNGIHCENNTPDCTESSCFNGGTCVDGINSFTCLCPPGFTGSYCQYDVNECDSRPCLHGGTCQDSYGTYKCTCPQGYTGLNCQNLVRWCDSAPCKNGGRCWQTNTQYHCECRSGWTGVNCDVLSVSCEVAAQKRGIDVTLLCQHGGLCVDEGDKHYCHCQAGYTGSYCEDEVDECSPNPCQNGATCTDYLGGFSCKCVAGYHGSNCSEEINECLSQPCQNGGTCIDLTNSYKCSCPRGTQGVHCEINVDDCHPPLDPASRSPKCFNNGTCVDQVGGYTCTCPPGFVGERCEGDVNECLSNPCDPRGTQNCVQRVNDFHCECRAGHTGRRCESVINGCRGKPCKNGGVCAVASNTARGFICRCPAGFEGATCENDARTCGSLRCLNGGTCISGPRSPTCLCLGSFTGPECQFPASSPCVGSNPCYNQGTCEPTSENPFYRCLCPAKFNGLLCHILDYSFTGGAGRDIPPPQIEEACELPECQVDAGNKVCNLQCNNHACGWDGGDCSLNFNDPWKNCTQSLQCWKYFSDGHCDSQCNSAGCLFDGFDCQLTEGQCNPLYDQYCKDHFSDGHCDQGCNSAECEWDGLDCAEHVPERLAAGTLVLVVLLPPDQLRNNSFHFLRELSHVLHTNVVFKRDAQGQQMIFPYYGHEEELRKHPIKRSTVGWATSSLLPGTSGGRQRRELDPMDIRGSIVYLEIDNRQCVQSSSQCFQSATDVAAFLGALASLGSLNIPYKIEAVKSEPVEPPLPSQLHLMYVAAAAFVLLFFVGCGVLLSRKRRRQHGQLWFPEGFKVSEASKKKRREPLGEDSVGLKPLKNASDGALMDDNQNEWGDEDLETKKFRFEEPVVLPDLSDQTDHRQWTQQHLDAADLRMSAMAPTPPQGEVDADCMDVNVRGPDGFTPLMIASCSGGGLETGNSEEEEDAPAVISDFIYQGASLHNQTDRTGETALHLAARYSRSDAAKRLLEASADANIQDNMGRTPLHAAVSADAQGVFQILLRNRATDLDARMHDGTTPLILAARLAVEGMLEDLINSHADVNAVDDLGKSALHWAAAVNNVDAAVVLLKNGANKDMQNNKEETPLFLAAREGSYETAKVLLDHFANRDITDHMDRLPRDIAQERMHHDIVRLLDEYNLVRSPQLHGTALGGTPTLSPTLCSPNGYLGNLKSATQGKKARKPSTKGLACGSKEAKDLKARRKKSQDGKGCLLDSSSMLSPVDSLESPHGYLSDVASPPLLPSPFQQSPSMPLSHLPGMPDTHLGISHLNVAAKPEMAALAGGSRLAFEPPPPRLSHLPVASSASTVLSTNGTGAMNFTVGAPASLNGQCEWLPRLQNGMVPSQYNPLRPGVTPGTLSTQAAGLQHSMMGPLHSSLSTNTLSPIIYQGLPNTRLATQPHLVQTQQVQPQNLQLQPQNLQPPSQPHLSVSSAANGHLGRSFLSGEPSQADVQPLGPSSLPVHTILPQESQALPTSLPSSMVPPMTTTQFLTPPSQHSYSSSPVDNTPSHQLQVPEHPFLTPSPESPDQWSSSSPHSNISDWSEGISSPPTTMPSQITHIPEAFK
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
4 (in isoform 3)Phosphorylation-10.2622871156
65O-linked_GlycosylationQDSNPCLSTPCKNAG
CCCCCCCCCCCCCCC		36.7021757702
73O-linked_GlycosylationTPCKNAGTCHVVDHG
CCCCCCCCEEEEECC		9.3121757702
94O-linked_GlycosylationCSCPLGFSGPLCLTP
ECCCCCCCCCEEECC		37.3922310717
116O-linked_GlycosylationNPCRNGGTCDLLTLT
CCCCCCCCCCEEEEE		12.3021757702
146O-linked_GlycosylationQQADPCASNPCANGG
CCCCCCCCCCCCCCC		48.2821757702
194O-linked_GlycosylationGLCRHGGTCHNEIGS
CCCCCCCCCCHHHCC		18.3821757702
232O-linked_GlycosylationSPCQNGGTCRPTGDT
CCCCCCCCCCCCCCC		13.5228089369
311O-linked_GlycosylationNACQNGGTCHNTHGG
CHHHCCCCCCCCCCC		16.4028089369
341O-linked_GlycosylationENIDDCASAACFQGA
CCHHHHHHHHHHCCC		23.8021757702
349O-linked_GlycosylationAACFQGATCHDRVAS
HHHHCCCCCCHHHHE		19.7328089369
378O-linked_GlycosylationHLNDACISNPCNEGS
ECCCCCCCCCCCCCC		34.3021757702
405O-linked_GlycosylationCTCPSGYTGPACSQD
EECCCCCCCCCCCCC		39.9722310717
435O-linked_GlycosylationKCLNTLGSFECQCLQ
HHHHHCCCEECEECC		22.4530127001
458O-linked_GlycosylationIDVNECISNPCQNDA
ECHHHHHCCCCCCCC		46.5121757702
466O-linked_GlycosylationNPCQNDATCLDQIGE
CCCCCCCCHHHHCCC		19.2321757702
496O-linked_GlycosylationINTDECASSPCLHNG
ECCHHHCCCCCCCCC		46.6121757702
534O-linked_GlycosylationYDVDECASTPCKNGA
ECHHHHCCCCCCCCC		44.5321757702
609O-linked_GlycosylationTNINECHSQPCRHGG
CCHHHHCCCCCCCCC		47.6921757702
617O-linked_GlycosylationQPCRHGGTCQDRDNS
CCCCCCCCCCCCCCC		16.1622310717
647O-linked_GlycosylationINLDDCASNPCDSGT
ECHHHHCCCCCCCCC		47.8621757702
692O-linked_GlycosylationSPCHNGGTCEDGIAG
CCCCCCCCCCCCCCC		17.7028089369
722O-linked_GlycosylationSEVNECNSNPCIHGA
HHHHHHCCCCCCCCC		54.5321757702
759O-linked_GlycosylationINNNECESNPCVNGG
CCCCCCCCCCCCCCC		58.7021757702
767O-linked_GlycosylationNPCVNGGTCKDMTSG
CCCCCCCCCCCCCCC		20.1321757702
784O-linked_GlycosylationCTCREGFSGPNCQTN
EEECCCCCCCCCCCC		65.2822310717
797O-linked_GlycosylationTNINECASNPCLNQG
CCHHHHHCCCCCCCC		53.6221757702
805O-linked_GlycosylationNPCLNQGTCIDDVAG
CCCCCCCCCHHHCCC		9.1221757702
888N-linked_GlycosylationGASCQNTNGSYRCLC
CCCCCCCCCCEEEEE		44.99-
900O-linked_GlycosylationCLCQAGYTGRNCESD
EEECCCCCCCCCCCC		28.8422310717
921O-linked_GlycosylationNPCHNGGSCTDGINT
CCCCCCCCCCCCCCH		18.4228089369
951O-linked_GlycosylationEDINECASNPCQNGA
HHHHHHHCCCCCCCC		53.6221757702
959N-linked_GlycosylationNPCQNGANCTDCVDS
CCCCCCCCCCCCCCC		30.53-
997O-linked_GlycosylationSSCFNGGTCVDGINS
CCCCCCCEECCCCCC		15.6828089369
1027O-linked_GlycosylationYDVNECDSRPCLHGG
EECCCCCCCCCCCCC		50.1821757702
1035O-linked_GlycosylationRPCLHGGTCQDSYGT
CCCCCCCCCCCCCCC		16.1621757702
1065O-linked_GlycosylationNLVRWCDSAPCKNGG
CHHHHHHCCCCCCCC		30.8621757702
1159O-linked_GlycosylationNPCQNGATCTDYLGG
CCCCCCCCCCHHCCC		19.8228089369
1179N-linked_GlycosylationVAGYHGSNCSEEINE
EEECCCCCCHHHHHH		37.62-
1189O-linked_GlycosylationEEINECLSQPCQNGG
HHHHHHHCCCCCCCC		43.6721757702
1197O-linked_GlycosylationQPCQNGGTCIDLTNS
CCCCCCCCEEECCCC		14.0021757702
1241N-linked_GlycosylationRSPKCFNNGTCVDQV
CCCCCCCCCCEEEEC		27.22-
1273O-linked_GlycosylationGDVNECLSNPCDPRG
CCHHHHHCCCCCCCC		50.8421757702
1362O-linked_GlycosylationLRCLNGGTCISGPRS
EEECCCCCCCCCCCC		14.2021757702
1379O-linked_GlycosylationCLCLGSFTGPECQFP
EEEECCCCCCCCCCC		54.2328089369
1402O-linked_GlycosylationNPCYNQGTCEPTSEN
CCCCCCCCCCCCCCC		12.1628089369
1489N-linked_GlycosylationNFNDPWKNCTQSLQC
CCCCCCCCCCHHHHH		30.14-
1587N-linked_GlycosylationLPPDQLRNNSFHFLR
CCHHHHCCCCHHHHH		58.03-
1635PhosphorylationKHPIKRSTVGWATSS
HCCCCHHHCCHHHHH		27.3727357545
1640PhosphorylationRSTVGWATSSLLPGT
HHHCCHHHHHCCCCC		16.6127357545
1641PhosphorylationSTVGWATSSLLPGTS
HHCCHHHHHCCCCCC		15.9627357545
1642PhosphorylationTVGWATSSLLPGTSG
HCCHHHHHCCCCCCC		29.5727357545
1647PhosphorylationTSSLLPGTSGGRQRR
HHHCCCCCCCCCCCC		23.4327357545
1749UbiquitinationCGVLLSRKRRRQHGQ
HHHHHCHHHHHHCCC		47.0515240571
1764AcetylationLWFPEGFKVSEASKK
CCCCCCCCCCHHHHH		56.5637798803
1770AcetylationFKVSEASKKKRREPL
CCCCHHHHHHCCCCC		70.1737798847
1771AcetylationKVSEASKKKRREPLG
CCCHHHHHHCCCCCC		49.3637798819
1772AcetylationVSEASKKKRREPLGE
CCHHHHHHCCCCCCC		61.5037798811
1785AcetylationGEDSVGLKPLKNASD
CCCCCCCCCCCCCCC		42.2337798799
1785UbiquitinationGEDSVGLKPLKNASD
CCCCCCCCCCCCCCC		42.2322790023
1791PhosphorylationLKPLKNASDGALMDD
CCCCCCCCCCCCCCC		46.07-
1851PhosphorylationRMSAMAPTPPQGEVD
HHHHCCCCCCCCCCC		37.7525266776
1856 (in isoform 2)O-linked_Glycosylation-31.7922310717
1931PhosphorylationLAARYSRSDAAKRLL
HHHHHCCHHHHHHHH		26.1725266776
1935AcetylationYSRSDAAKRLLEASA
HCCHHHHHHHHHHHC		45.3537798843
1945HydroxylationLEASADANIQDNMGR
HHHHCCCCCCCCCCC		32.7617573339
2012HydroxylationINSHADVNAVDDLGK
HHCCCCCCCCCHHHH		34.4917573339
2050AcetylationNKDMQNNKEETPLFL
CHHHCCCCCCCCHHH		65.5637798823
2068AcetylationEGSYETAKVLLDHFA
CCCHHHHHHHHHHHC		40.6137798835
2111PhosphorylationDEYNLVRSPQLHGTA
HHCCCCCCCCCCCCC		14.9830635358
2117PhosphorylationRSPQLHGTALGGTPT
CCCCCCCCCCCCCCC		14.1530635358
2122PhosphorylationHGTALGGTPTLSPTL
CCCCCCCCCCCCCCC		15.9930635358
2124PhosphorylationTALGGTPTLSPTLCS
CCCCCCCCCCCCCCC		39.4430635358
2126PhosphorylationLGGTPTLSPTLCSPN
CCCCCCCCCCCCCCC		20.5130635358
2128PhosphorylationGTPTLSPTLCSPNGY
CCCCCCCCCCCCCCC		36.7030635358
2131PhosphorylationTLSPTLCSPNGYLGN
CCCCCCCCCCCCCCC		25.2230635358
2135PhosphorylationTLCSPNGYLGNLKSA
CCCCCCCCCCCHHHH		20.3430635358
2146AcetylationLKSATQGKKARKPST
HHHHHCCCCCCCCCC		33.1837798831
2147AcetylationKSATQGKKARKPSTK
HHHHCCCCCCCCCCC		61.3237798815
2150AcetylationTQGKKARKPSTKGLA
HCCCCCCCCCCCCCC		48.4537798807
2152PhosphorylationGKKARKPSTKGLACG
CCCCCCCCCCCCCCC		45.87-
2154AcetylationKARKPSTKGLACGSK
CCCCCCCCCCCCCCH		57.1537798853
2161AcetylationKGLACGSKEAKDLKA
CCCCCCCHHHHHHHH		47.1537798827
2164AcetylationACGSKEAKDLKARRK
CCCCHHHHHHHHHHH		65.7637798839
2253MethylationAALAGGSRLAFEPPP
HHHHCCCCCCCCCCC		33.05113703801
2253DimethylationAALAGGSRLAFEPPP
HHHHCCCCCCCCCCC		33.05-
2262DimethylationAFEPPPPRLSHLPVA
CCCCCCCCCCCCCCC		55.38-
2262MethylationAFEPPPPRLSHLPVA
CCCCCCCCCCCCCCC		55.38113703805
2303MethylationGQCEWLPRLQNGMVP
CCCCCHHHHCCCCCC		46.89113704199
2303DimethylationGQCEWLPRLQNGMVP
CCCCCHHHHCCCCCC		46.89-
2317MethylationPSQYNPLRPGVTPGT
CCCCCCCCCCCCCCC		27.47113704205
2317DimethylationPSQYNPLRPGVTPGT
CCCCCCCCCCCCCCC		27.47-
2361MethylationYQGLPNTRLATQPHL
HCCCCCCCCCCCCCE		29.03818913801
2487PhosphorylationVPEHPFLTPSPESPD
CCCCCCCCCCCCCCC		23.3117646409
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
1791SPhosphorylationKinasePRKCZQ05513
GPS
2152SPhosphorylationKinasePIM1P11309
PSP
2152SPhosphorylationKinasePIM2Q9P1W9
PSP
2152SPhosphorylationKinasePIM3Q86V86
PSP
-KUbiquitinationE3 ubiquitin ligaseFbxw7Q8VBV4
PMID:22199232
-KUbiquitinationE3 ubiquitin ligaseItchQ8C863
PMID:22199232
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference
1027SGlycosylation

21757702
1749Kubiquitylation

15240571
1945NHydroxylation

18299578
2012NHydroxylation

18299578
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_MOUSE !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
SMRD3_MOUSESmarcd3physical
17210915
DLL1_MOUSEDll1physical
21985982
NUMB_MOUSENumbphysical
20844536
NUMB_HUMANNUMBphysical
21356309
SUH_MOUSERbpjphysical
17526737
XIAP_HUMANXIAPphysical
17318174
EGFL7_HUMANEGFL7physical
19503073
EGFL7_MOUSEEgfl7physical
19503073
JAG1_RATJag1physical
19503073
SUH_HUMANRBPJphysical
19503073
Drug and Disease Associations
Kegg Drug
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of NOTC1_MOUSE

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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: X-RAY CRYSTALLOGRAPHY (2.35 ANGSTROMS) OF 1899-2106 IN COMPLEX WITHHIF1AN; IRON AND 2-OXOGLUTARATE, HYDROXYLATION AT ASN-1945 ANDASN-2012, MUTAGENESIS OF ASN-1945 AND ASN-2012, AND MASS SPECTROMETRY.
"Interaction with factor inhibiting HIF-1 defines an additional modeof cross-coupling between the Notch and hypoxia signaling pathways.";
Zheng X., Linke S., Dias J.M., Zheng X., Gradin K., Wallis T.P.,Hamilton B.R., Gustafsson M., Ruas J.L., Wilkins S., Bilton R.L.,Brismar K., Whitelaw M.L., Pereira T., Gorman J.J., Ericson J.,Peet D.J., Lendahl U., Poellinger L.;
Proc. Natl. Acad. Sci. U.S.A. 105:3368-3373(2008).
Cited for: PROTEIN SEQUENCE OF 1937-1952 AND 1995-2019, FUNCTION, INTERACTIONWITH HIF1AN, HYDROXYLATION AT ASN-1945 AND ASN-2012 BY HIF1AN,MUTAGENESIS OF ASN-1945 AND ASN-2012, AND MASS SPECTROMETRY.
Ubiquitylation
ReferencePubMed
"Monoubiquitination and endocytosis direct gamma-secretase cleavage ofactivated Notch receptor.";
Gupta-Rossi N., Six E., LeBail O., Logeat F., Chastagner P., Olry A.,Israel A., Brou C.;
J. Cell Biol. 166:73-83(2004).
Cited for: UBIQUITINATION AT LYS-1749, AND ENDOCYTOSIS.

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