NOTC2_MOUSE - dbPTM
NOTC2_MOUSE - PTM Information in dbPTM
Basic Information of Protein
UniProt ID NOTC2_MOUSE
UniProt AC O35516
Protein Name Neurogenic locus notch homolog protein 2
Gene Name Notch2
Organism Mus musculus (Mouse).
Sequence Length 2470
Subcellular Localization Notch 2 extracellular truncation: Cell membrane
Single-pass type I membrane protein .
Notch 2 intracellular domain: Nucleus . Cytoplasm . Following proteolytical processing NICD is translocated to the nucleus. Retained at the cytoplasm by TCIM.
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 (By similarity). May play an essential role in postimplantation development, probably in some aspect of cell specification and/or differentiation. In collaboration with RELA/p65 enhances NFATc1 promoter activity and positively regulates RANKL-induced osteoclast differentiation. Positively regulates self-renewal of liver cancer cells (By similarity)..
Protein Sequence MPDLRPAALRALLWLWLCGAGPAHALQCRGGQEPCVNEGTCVTYHNGTGFCRCPEGFLGEYCQHRDPCEKNRCQNGGTCVPQGMLGKATCRCAPGFTGEDCQYSTSHPCFVSRPCQNGGTCHMLSRDTYECTCQVGFTGKQCQWTDACLSHPCENGSTCTSVASQFSCKCPAGLTGQKCEADINECDIPGRCQHGGTCLNLPGSYRCQCGQGFTGQHCDSPYVRGLPCVNGGTCRQTGDFTLECNCLPGFEGSTCERNIDDCPNHKCQNGGVCVDGVNTYNCRCPPQWTGQFCTEDVDECLLQPNACQNGGTCTNRNGGYGCVCVNGWSGDDCSENIDDCAYASCTPGSTCIDRVASFSCLCPEGKAGLLCHLDDACISNPCHKGALCDTNPLNGQYICTCPQGYKGADCTEDVDECAMANSNPCEHAGKCVNTDGAFHCECLKGYAGPRCEMDINECHSDPCQNDATCLDKIGGFTCLCMPGFKGVHCELEVNECQSNPCVNNGQCVDKVNRFQCLCPPGFTGPVCQIDIDDCSSTPCLNGAKCIDHPNGYECQCATGFTGILCDENIDNCDPDPCHHGQCQDGIDSYTCICNPGYMGAICSDQIDECYSSPCLNDGRCIDLVNGYQCNCQPGTSGLNCEINFDDCASNPCMHGVCVDGINRYSCVCSPGFTGQRCNIDIDECASNPCRKGATCINDVNGFRCICPEGPHHPSCYSQVNECLSNPCIHGNCTGGLSGYKCLCDAGWVGVNCEVDKNECLSNPCQNGGTCNNLVNGYRCTCKKGFKGYNCQVNIDECASNPCLNQGTCFDDVSGYTCHCMLPYTGKNCQTVLAPCSPNPCENAAVCKEAPNFESFSCLCAPGWQGKRCTVDVDECISKPCMNNGVCHNTQGSYVCECPPGFSGMDCEEDINDCLANPCQNGGSCVDHVNTFSCQCHPGFIGDKCQTDMNECLSEPCKNGGTCSDYVNSYTCTCPAGFHGVHCENNIDECTESSCFNGGTCVDGINSFSCLCPVGFTGPFCLHDINECSSNPCLNAGTCVDGLGTYRCICPLGYTGKNCQTLVNLCSRSPCKNKGTCVQEKARPHCLCPPGWDGAYCDVLNVSCKAAALQKGVPVEHLCQHSGICINAGNTHHCQCPLGYTGSYCEEQLDECASNPCQHGATCNDFIGGYRCECVPGYQGVNCEYEVDECQNQPCQNGGTCIDLVNHFKCSCPPGTRGLLCEENIDECAGGPHCLNGGQCVDRIGGYTCRCLPGFAGERCEGDINECLSNPCSSEGSLDCVQLKNNYNCICRSAFTGRHCETFLDVCPQKPCLNGGTCAVASNMPDGFICRCPPGFSGARLQSSCGQVKCRRGEQCIHTDSGPRCFCLNPKDCESGCASNPCQHGGTCYPQRQPPHYSCRCPPSFGGSHCELYTAPTSTPPATCQSQYCADKARDGICDEACNSHACQWDGGDCSLTMEDPWANCTSTLRCWEYINNQCDEQCNTAECLFDNFECQRNSKTCKYDKYCADHFKDNHCDQGCNSEECGWDGLDCASDQPENLAEGTLIIVVLLPPEQLLQDSRSFLRALGTLLHTNLRIKQDSQGALMVYPYFGEKSAAMKKQKMTRRSLPEEQEQEQEVIGSKIFLEIDNRQCVQDSDQCFKNTDAAAALLASHAIQGTLSYPLVSVFSELESPRNAQLLYLLAVAVVIILFFILLGVIMAKRKQAWLPLAAGRFTLRRDSSNHKRREPVGQDAVGLKNLSVQVSEANLIGSGTSEHWVDDEGPQPKKAKAEDEALLSEDDPIDRRPWTQQHLEAADISHTPSLALTPPQAEQEVDVLDVNVRGPDGCTPLMLASLRGGSSDLSDEDEDAEDSSANIITDLVYQGASLQAQTDRTGEMALHLAARYSRADAAKRLLDAGADRNAQDNMGRCPLHAAVAGDAQGVFQILIRNRVTDLDARMNDGTTPLILAARLAVEGMVAELINCQADVNAVDDHGKSALHWAAAVNNVEATLLLLKNGANRDMQDNKEETPLFLAAREGSYEAAKILLDHFANRDITDHMDRLPRDVARDRMHHDIVRLLDEYNVTPSPPGTVLTSALSPVLCGPNRSFLSLKHTPMGKKARRPNTKSTMPTSLPNLAKEAKDAKGSRRKKCLNEKVQLSESSVTLSPVDSLESPHTYVSDATSSPMITSPGILQASPTPLLAAAAPAAPVHTQHALSFSNLHDMQPLAPGASTVLPSVSQLLSHHHIAPPGSSSAGSLGRLHPVPVPADWMNRVEMNETQYSEMFGMVLAPAEGAHPGIAAPQSRPPEGKHMSTQREPLPPIVTFQLIPKRSIAQAAGAPQTQSSCPPAVAGPLPSMYQIPEMPRLPSVAFPPTMMPQQEGQVAQTIVPTYHPFPASVGKYPTPPSQHSYASSNAAERTPSHGGHLQGEHPYLTPSPESPDQWSSSSPHSASDWSDVTTSPTPGGGGGGQRGPGTHMSEPPHSNMQVYA
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
46N-linked_GlycosylationGTCVTYHNGTGFCRC
CCEEEEECCCCEECC		39.03-
155N-linked_GlycosylationCLSHPCENGSTCTSV
HHCCCCCCCCCCHHH		57.33-
357PhosphorylationTCIDRVASFSCLCPE
CHHHHHHEEEEECCC		18.1630352176
611O-linked_GlycosylationDQIDECYSSPCLNDG
HCCCHHHCCCCCCCC		39.1921949356
613O-linked_GlycosylationIDECYSSPCLNDGRC
CCHHHCCCCCCCCCE		22.2221949356
733N-linked_GlycosylationPCIHGNCTGGLSGYK
CCCCCCCCCCCCCCE		37.98-
1102N-linked_GlycosylationYCDVLNVSCKAAALQ
CCCCCCCCHHHHHHH		14.61-
1465N-linked_GlycosylationEDPWANCTSTLRCWE
CCCCCCCCHHHHHHH		25.26-
1599AcetylationGEKSAAMKKQKMTRR
CCCHHHHHHHHHHHC		47.536567351
1600AcetylationEKSAAMKKQKMTRRS
CCHHHHHHHHHHHCC		41.916567327
1604PhosphorylationAMKKQKMTRRSLPEE
HHHHHHHHHCCCCHH		29.9325619855
1607PhosphorylationKQKMTRRSLPEEQEQ
HHHHHHCCCCHHHHH		45.0130635358
1715PhosphorylationPLAAGRFTLRRDSSN
HHHHCCEEECCCCCC		20.28-
1718PhosphorylationAGRFTLRRDSSNHKR
HCCEEECCCCCCCCC		51.8023608596
1718PhosphorylationAGRFTLRRDSSNHKR
HCCEEECCCCCCCCC		51.80-
1721PhosphorylationFTLRRDSSNHKRREP
EEECCCCCCCCCCCC		47.4425338131
1723PhosphorylationLRRDSSNHKRREPVG
ECCCCCCCCCCCCCC		27.2623608596
1724PhosphorylationRRDSSNHKRREPVGQ
CCCCCCCCCCCCCCC		58.3523608596
1740PhosphorylationAVGLKNLSVQVSEAN
CCCCCCEEEEEEEEE		21.6425338131
1744PhosphorylationKNLSVQVSEANLIGS
CCEEEEEEEEEECCC		17.5629514104
1777PhosphorylationAEDEALLSEDDPIDR
HHHHHHCCCCCCCCC		39.5727566939
1780PhosphorylationEALLSEDDPIDRRPW
HHHCCCCCCCCCCCC		37.6925338131
1780PhosphorylationEALLSEDDPIDRRPW
HHHCCCCCCCCCCCC		37.6919144319
1800PhosphorylationEAADISHTPSLALTP
HHCCCCCCCCCCCCC		14.0530635358
1802PhosphorylationADISHTPSLALTPPQ
CCCCCCCCCCCCCCC		27.6830635358
1803PhosphorylationDISHTPSLALTPPQA
CCCCCCCCCCCCCCH		4.82-
1805PhosphorylationSHTPSLALTPPQAEQ
CCCCCCCCCCCCHHC		10.03-
1805PhosphorylationSHTPSLALTPPQAEQ
CCCCCCCCCCCCHHC		10.0330352176
1806PhosphorylationHTPSLALTPPQAEQE
CCCCCCCCCCCHHCE		27.5830635358
1809PhosphorylationSLALTPPQAEQEVDV
CCCCCCCCHHCEECE		59.75-
1828PhosphorylationVRGPDGCTPLMLASL
CCCCCCCCHHHHHHH		25.6130482847
1839PhosphorylationLASLRGGSSDLSDED
HHHHCCCCCCCCCCC		24.4121743459
1840PhosphorylationASLRGGSSDLSDEDE
HHHCCCCCCCCCCCC		45.9321659605
1843PhosphorylationRGGSSDLSDEDEDAE
CCCCCCCCCCCCCCC		43.9021659605
1846PhosphorylationSSDLSDEDEDAEDSS
CCCCCCCCCCCCCCC		65.1619144319
1852PhosphorylationEDEDAEDSSANIITD
CCCCCCCCCCHHHHH		23.9029550500
1853PhosphorylationDEDAEDSSANIITDL
CCCCCCCCCHHHHHH		37.3429550500
1858PhosphorylationDSSANIITDLVYQGA
CCCCHHHHHHHHCCC		21.3429550500
2063PhosphorylationIVRLLDEYNVTPSPP
HHHHHHHCCCCCCCC		18.0130635358
2066PhosphorylationLLDEYNVTPSPPGTV
HHHHCCCCCCCCCCE		17.8926745281
2068PhosphorylationDEYNVTPSPPGTVLT
HHCCCCCCCCCCEEE		34.0726745281
2071PhosphorylationNVTPSPPGTVLTSAL
CCCCCCCCCEEECCC		31.66-
2072PhosphorylationVTPSPPGTVLTSALS
CCCCCCCCEEECCCC		20.3726745281
2075PhosphorylationSPPGTVLTSALSPVL
CCCCCEEECCCCCEE		13.9726643407
2076PhosphorylationPPGTVLTSALSPVLC
CCCCEEECCCCCEEE		24.0526643407
2079PhosphorylationTVLTSALSPVLCGPN
CEEECCCCCEEECCC		16.8127087446
2082PhosphorylationTSALSPVLCGPNRSF
ECCCCCEEECCCCCC		2.95-
2088PhosphorylationVLCGPNRSFLSLKHT
EEECCCCCCCCCCCC		36.8628725479
2091PhosphorylationGPNRSFLSLKHTPMG
CCCCCCCCCCCCCCC		33.1028725479
2095PhosphorylationSFLSLKHTPMGKKAR
CCCCCCCCCCCCCCC		17.2426370283
2098PhosphorylationSLKHTPMGKKARRPN
CCCCCCCCCCCCCCC		29.52-
2112PhosphorylationNTKSTMPTSLPNLAK
CCCCCCCCCHHHHHH		31.8826643407
2113PhosphorylationTKSTMPTSLPNLAKE
CCCCCCCCHHHHHHH		35.6426745281
2415PhosphorylationQGEHPYLTPSPESPD
CCCCCCCCCCCCCCC		18.8425338131
2420PhosphorylationYLTPSPESPDQWSSS
CCCCCCCCCCCCCCC		36.8425338131
2426PhosphorylationESPDQWSSSSPHSAS
CCCCCCCCCCCCCCC		31.6925338131
2441PhosphorylationDWSDVTTSPTPGGGG
CCCCCCCCCCCCCCC		19.8725338131
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
2066TPhosphorylationKinaseGSK3BQ9WV60
PhosphoELM
2068SPhosphorylationKinaseGSK3BQ9WV60
PhosphoELM
2072TPhosphorylationKinaseGSK3BQ9WV60
PhosphoELM
2091SPhosphorylationKinaseGSK3BQ9WV60
PhosphoELM
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of NOTC2_MOUSE !!
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 NOTC2_MOUSE !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
EGFL7_HUMANEGFL7physical
19503073
EGFL7_MOUSEEgfl7physical
19503073
Drug and Disease Associations
Kegg Drug
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of NOTC2_MOUSE

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Related Literatures of Post-Translational Modification
Phosphorylation
ReferencePubMed
"The phagosomal proteome in interferon-gamma-activated macrophages.";
Trost M., English L., Lemieux S., Courcelles M., Desjardins M.,Thibault P.;
Immunity 30:143-154(2009).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1777, AND MASSSPECTROMETRY.

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