Q9QW30 · NOTC2_RAT
- ProteinNeurogenic locus notch homolog protein 2
- GeneNotch2
- StatusUniProtKB reviewed (Swiss-Prot)
- Organism
- Amino acids2471 (go to sequence)
- Protein existenceEvidence at protein level
- Annotation score5/5
Function
function
Functions as a receptor for membrane-bound ligands Jagged-1 (JAG1), Jagged-2 (JAG2) and Delta-1 (DLL1) 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).
Involved in bone remodeling and homeostasis. 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).
Involved in bone remodeling and homeostasis. 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).
Features
Showing features for site.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Site | 614 | Essential for O-xylosylation | ||||
Sequence: S |
GO annotations
all annotations | all molecular function | virus receptor activity | dna binding | rna binding | cytoskeletal motor activity | catalytic activity | gtpase activity | structural molecule activity | transporter activity | cytoskeletal protein binding | lipid binding | cyclase activity | antioxidant activity | oxidoreductase activity | transferase activity | hydrolase activity | lyase activity | isomerase activity | ligase activity | protein tag activity | cargo receptor activity | histone binding | protein folding chaperone | translation regulator activity | nutrient reservoir activity | receptor ligand activity | molecular transducer activity | molecular adaptor activity | toxin activity | cell adhesion mediator activity | molecular function regulator activity | virus coreceptor activity | catalytic activity, acting on a protein | catalytic activity, acting on dna | catalytic activity, acting on rna | molecular carrier activity | transcription regulator activity | general transcription initiation factor activity | molecular sensor activity | molecular sequestering activity | atp-dependent activity | other molecular function | all biological process | mitotic cell cycle | cytokinesis | cytoplasmic translation | immune system process | muscle system process | circulatory system process | renal system process | respiratory system process | carbohydrate metabolic process | generation of precursor metabolites and energy | dna replication | dna repair | dna recombination | chromatin organization | dna-templated transcription | regulation of dna-templated transcription | trna metabolic process | protein folding | protein glycosylation | amino acid metabolic process | modified amino acid metabolic process | lipid metabolic process | vitamin metabolic process | sulfur compound metabolic process | intracellular protein transport | nucleocytoplasmic transport | autophagy | inflammatory response | mitochondrion organization | cytoskeleton organization | microtubule-based movement | peroxisome organization | lysosome organization | chromosome segregation | cell adhesion | establishment or maintenance of cell polarity | programmed cell death | photosynthesis | mrna metabolic process | snrna metabolic process | vesicle-mediated transport | reproductive process | digestive system process | signaling | cell differentiation | protein catabolic process | extracellular matrix organization | regulatory ncrna-mediated gene silencing | telomere organization | cell junction organization | wound healing | ribosome biogenesis | cilium organization | anatomical structure development | cell motility | nervous system process | endocrine process | protein maturation | transmembrane transport | nucleobase-containing small molecule metabolic process | hepaticobiliary system process | membrane organization | protein-containing complex assembly | cell wall organization or biogenesis | nitrogen cycle metabolic process | protein localization to plasma membrane | defense response to other organism | detoxification | meiotic nuclear division | mitotic nuclear division | mitochondrial gene expression | carbohydrate derivative metabolic process | other biological process | all cellular component | nuclear chromosome | extracellular region | extracellular space | cell wall | nucleus | nuclear envelope | nucleoplasm | chromosome | nucleolus | mitochondrion | lysosome | endosome | vacuole | peroxisome | endoplasmic reticulum | golgi apparatus | lipid droplet | microtubule organizing center | cytosol | ribosome | cytoskeleton | plasma membrane | cilium | plastid | thylakoid | external encapsulating structure | extracellular matrix | cytoplasmic vesicle | organelle | other cellular component | |||
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Keywords
- Molecular function
- Biological process
Names & Taxonomy
Protein names
- Recommended nameNeurogenic locus notch homolog protein 2
- Short namesNotch 2
- Cleaved into 2 chains
Gene names
Organism names
- Organism
- Taxonomic lineageEukaryota > Metazoa > Chordata > Craniata > Vertebrata > Euteleostomi > Mammalia > Eutheria > Euarchontoglires > Glires > Rodentia > Myomorpha > Muroidea > Muridae > Murinae > Rattus
Accessions
- Primary accessionQ9QW30
Proteomes
Organism-specific databases
Subcellular Location
UniProt Annotation
GO Annotation
Notch 2 extracellular truncation
Cell membrane ; Single-pass type I membrane protein
Notch 2 intracellular domain
Note: Following proteolytical processing NICD is translocated to the nucleus. Retained at the cytoplasm by TCIM.
Features
Showing features for topological domain, transmembrane.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Topological domain | 26-1677 | Extracellular | ||||
Sequence: LQCRGGQEPCVNEGTCVTYHNGTGYCRCPEGFLGEYCQHRDPCEKNRCQNGGTCVTQAMLGKATCRCAPGFTGEDCQYSTSHPCFVSRPCQNGGTCHMLSWDTYECTCQVGFTGKQCQWTDVCLSHPCENGSTCSSVANQFSCRCPAGITGQKCDADINECDIPGRCQHGGTCLNLPGSYRCQCPQRFTGQHCDSPYVPCAPSPCVNGGTCRQTGDFTSECHCLPGFEGSNCERNIDDCPNHKCQNGGVCVDGVNTYNCRCPPQWTGQFCTEDVDECLLQPNACQNGGTCTNRNGGYGCVCVNGWSGDDCSENIDDCAFASCTPGSTCIDRVASFSCLCPEGKAGLLCHLDDACISNPCHKGALCDTNPLNGQYICTCPQAYKGADCTEDVDECAMANSNPCEHAGKCVNTDGAFHCECLKGYAGPRCEMDINECHSDPCQNDATCLDKIGGFTCLCMPGFKGVHCELEVNECQSNPCVNNGQCVDKVNRFQCLCPPGFTGPVCQIDIDDCSSTPCLNGAKCIDHPNGYECQCATGFTGTLCDENIDNCDPDPCHHGQCQDGIDSYTCICNPGYMGAICSDQIDECYSSPCLNDGRCIDLVNGYQCNCQPGTSGLNCEINFDDCASNPCLHGACVDGINRYSCVCSPGFTGQRCNIDIDECASNPCRKDATCINDVNGFRCMCPEGPHHPSCYSQVNECLSSPCIHGNCTGGLSGYKCLCDAGWVGINCEVDKNECLSNPCQNGGTCNNLVNGYRCTCKKGFKGYNCQVNIDECASNPCLNQGTCLDDVSGYTCHCMLPYTGKNCQTVLAPCSPNPCENAAVCKEAPNFESFTCLCAPGWQGQRCTVDVDECVSKPCMNNGICHNTQGSYMCECPPGFSGMDCEEDINDCLANPCQNGGSCVDKVNTFSCLCLPGFVGDKCQTDMNECLSEPCKNGGTCSDYVNSYTCTCPAGFHGVHCENNIDECTESSCFNGGTCVDGINSFSCLCPVGFTGPFCLHDINECSSNPCLNSGTCVDGLGTYRCTCPLGYTGKNCQTLVNLCSPSPCKNKGTCAQEKARPRCLCPPGWDGAYCDVLNVSCKAAALQKGVPVEHLCQHSGICINAGNTHHCQCPLGYTGSYCEEQLDECASNPCQHGATCSDFIGGYRCECVPGYQGVNCEYEVDECQNQPCQNGGTCIDLVNHFKCSCPPGTRGLLCEENIDDCAGAPHCLNGGQCVDRIGGYSCRCLPGFAGERCEGDINECLSNPCSSEGSLDCIQLKNNYQCVCRSAFTGRHCETFLDVCPQKPCLNGGTCAVASNVPDGFICRCPPGFSGARCQSSCGQVKCRRGEQCVHTASGPHCFCPNHKDCESGCASNPCQHGGTCYPQRQPPYYSCRCSPPFWGSHCESYTAPTSTPPATCLSQYCADKARDGICDEACNSHACQWDGGDCSLTMEDPWANCTSSLRCWEYINNQCDELCNTAECLFDNFECQRNSKTCKYDKYCADHFKDNHCDKGCNNEECGWDGLDCAADQPENLAEGILVIVVLLPPEQLLQDSRSFLRALGTLLHTNLRIKQDSQGALMVYPYYGEKSAAMKKQKVARRSLPDEQEQEIIGSKVFLEIDNRQCVQDSDQCFKNTDAAAALLASHAIQGTLSYPLVSVVSESEDPRNTP | ||||||
Transmembrane | 1678-1698 | Helical | ||||
Sequence: LLYLLAVAVVIILFLILLGVI | ||||||
Topological domain | 1699-2471 | Cytoplasmic | ||||
Sequence: MAKRKRKHGFLWLPEGFTLRRDSSNHKRREPVGQDAVGLKNLSVQVSEANLIGSTTSEHWGDDEGPQPKKAKAEDDEALLSEDDPVDRRPWTQQHLEAADIRRTPSLALTPPQAEQEVDVLDVNVRGPDGCTPLMLASLRGGSSDLSDEDEDAEDSSANIITDLVYQGASLQAQTDRTGEMALHLAARYSRADAAKRLLDAGADANAQDNMGRCPLHAAVAADAQGVFQILIRNRVTDLDARMNDGTTPLILAARLAVEGMVAELINCQADVNAVDDHGKSALHWAAAVNNVEATLLLLKNGANRDMQDNKEETPLFLAAREGSYEAAKILLDHFANRDITDHMDRLPRDVARDRMHHDIVRLLDEYNVTPSPPGTVLTSALSPVLCGPNRSFLSLKHTPMGKKARRPNTKSTMPTSLPNLAKEAKDVKGSRRKKCLNEKVQLSESSVTLSPVDSLESPHTYVSDATSSPMITSPGILQASPTPLLAAAPAAPVHAQHALSFSNLHEMQPLRPGASTVLPSVSQLLSHHHIVPPGSGSAGSLGRLHSVPVPSDWMNRVEMSETQYSEMFGMVLAPAEGTHPGMAAPQSRAPEGKPIPTQREPLPPIVTFQLIPKGSLAQAAGAPQTQSGCPPAVAGPLPSMYQIPEMARLPSVAFPPTMMPQQEGQVAQTIVPTYHPFPASVGKYPTPPSQHSYASSNAAERTPNHGGHLQGEHPYLTPSPESPDQWSSSSPHSASDWSDVTTSPTPGGGGGGQRGPGTHMSEPPHSNMQVYA |
Keywords
- Cellular component
Phenotypes & Variants
Features
Showing features for mutagenesis.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Mutagenesis | 2078 | Permits Notch2 inhibitory activity upon G-CSF action on myeloid cells. | ||||
Sequence: S → A | ||||||
Mutagenesis | 2090 | No effect. | ||||
Sequence: S → A |
PTM/Processing
Features
Showing features for signal, chain, disulfide bond, glycosylation, modified residue.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Signal | 1-25 | |||||
Sequence: MPALRPAALRALLWLWLCGAGPAHA | ||||||
Chain | PRO_0000007689 | 26-2471 | Neurogenic locus notch homolog protein 2 | |||
Sequence: LQCRGGQEPCVNEGTCVTYHNGTGYCRCPEGFLGEYCQHRDPCEKNRCQNGGTCVTQAMLGKATCRCAPGFTGEDCQYSTSHPCFVSRPCQNGGTCHMLSWDTYECTCQVGFTGKQCQWTDVCLSHPCENGSTCSSVANQFSCRCPAGITGQKCDADINECDIPGRCQHGGTCLNLPGSYRCQCPQRFTGQHCDSPYVPCAPSPCVNGGTCRQTGDFTSECHCLPGFEGSNCERNIDDCPNHKCQNGGVCVDGVNTYNCRCPPQWTGQFCTEDVDECLLQPNACQNGGTCTNRNGGYGCVCVNGWSGDDCSENIDDCAFASCTPGSTCIDRVASFSCLCPEGKAGLLCHLDDACISNPCHKGALCDTNPLNGQYICTCPQAYKGADCTEDVDECAMANSNPCEHAGKCVNTDGAFHCECLKGYAGPRCEMDINECHSDPCQNDATCLDKIGGFTCLCMPGFKGVHCELEVNECQSNPCVNNGQCVDKVNRFQCLCPPGFTGPVCQIDIDDCSSTPCLNGAKCIDHPNGYECQCATGFTGTLCDENIDNCDPDPCHHGQCQDGIDSYTCICNPGYMGAICSDQIDECYSSPCLNDGRCIDLVNGYQCNCQPGTSGLNCEINFDDCASNPCLHGACVDGINRYSCVCSPGFTGQRCNIDIDECASNPCRKDATCINDVNGFRCMCPEGPHHPSCYSQVNECLSSPCIHGNCTGGLSGYKCLCDAGWVGINCEVDKNECLSNPCQNGGTCNNLVNGYRCTCKKGFKGYNCQVNIDECASNPCLNQGTCLDDVSGYTCHCMLPYTGKNCQTVLAPCSPNPCENAAVCKEAPNFESFTCLCAPGWQGQRCTVDVDECVSKPCMNNGICHNTQGSYMCECPPGFSGMDCEEDINDCLANPCQNGGSCVDKVNTFSCLCLPGFVGDKCQTDMNECLSEPCKNGGTCSDYVNSYTCTCPAGFHGVHCENNIDECTESSCFNGGTCVDGINSFSCLCPVGFTGPFCLHDINECSSNPCLNSGTCVDGLGTYRCTCPLGYTGKNCQTLVNLCSPSPCKNKGTCAQEKARPRCLCPPGWDGAYCDVLNVSCKAAALQKGVPVEHLCQHSGICINAGNTHHCQCPLGYTGSYCEEQLDECASNPCQHGATCSDFIGGYRCECVPGYQGVNCEYEVDECQNQPCQNGGTCIDLVNHFKCSCPPGTRGLLCEENIDDCAGAPHCLNGGQCVDRIGGYSCRCLPGFAGERCEGDINECLSNPCSSEGSLDCIQLKNNYQCVCRSAFTGRHCETFLDVCPQKPCLNGGTCAVASNVPDGFICRCPPGFSGARCQSSCGQVKCRRGEQCVHTASGPHCFCPNHKDCESGCASNPCQHGGTCYPQRQPPYYSCRCSPPFWGSHCESYTAPTSTPPATCLSQYCADKARDGICDEACNSHACQWDGGDCSLTMEDPWANCTSSLRCWEYINNQCDELCNTAECLFDNFECQRNSKTCKYDKYCADHFKDNHCDKGCNNEECGWDGLDCAADQPENLAEGILVIVVLLPPEQLLQDSRSFLRALGTLLHTNLRIKQDSQGALMVYPYYGEKSAAMKKQKVARRSLPDEQEQEIIGSKVFLEIDNRQCVQDSDQCFKNTDAAAALLASHAIQGTLSYPLVSVVSESEDPRNTPLLYLLAVAVVIILFLILLGVIMAKRKRKHGFLWLPEGFTLRRDSSNHKRREPVGQDAVGLKNLSVQVSEANLIGSTTSEHWGDDEGPQPKKAKAEDDEALLSEDDPVDRRPWTQQHLEAADIRRTPSLALTPPQAEQEVDVLDVNVRGPDGCTPLMLASLRGGSSDLSDEDEDAEDSSANIITDLVYQGASLQAQTDRTGEMALHLAARYSRADAAKRLLDAGADANAQDNMGRCPLHAAVAADAQGVFQILIRNRVTDLDARMNDGTTPLILAARLAVEGMVAELINCQADVNAVDDHGKSALHWAAAVNNVEATLLLLKNGANRDMQDNKEETPLFLAAREGSYEAAKILLDHFANRDITDHMDRLPRDVARDRMHHDIVRLLDEYNVTPSPPGTVLTSALSPVLCGPNRSFLSLKHTPMGKKARRPNTKSTMPTSLPNLAKEAKDVKGSRRKKCLNEKVQLSESSVTLSPVDSLESPHTYVSDATSSPMITSPGILQASPTPLLAAAPAAPVHAQHALSFSNLHEMQPLRPGASTVLPSVSQLLSHHHIVPPGSGSAGSLGRLHSVPVPSDWMNRVEMSETQYSEMFGMVLAPAEGTHPGMAAPQSRAPEGKPIPTQREPLPPIVTFQLIPKGSLAQAAGAPQTQSGCPPAVAGPLPSMYQIPEMARLPSVAFPPTMMPQQEGQVAQTIVPTYHPFPASVGKYPTPPSQHSYASSNAAERTPNHGGHLQGEHPYLTPSPESPDQWSSSSPHSASDWSDVTTSPTPGGGGGGQRGPGTHMSEPPHSNMQVYA | ||||||
Disulfide bond | 28↔41 | |||||
Sequence: CRGGQEPCVNEGTC | ||||||
Disulfide bond | 35↔51 | |||||
Sequence: CVNEGTCVTYHNGTGYC | ||||||
Glycosylation | 46 | N-linked (GlcNAc...) asparagine | ||||
Sequence: N | ||||||
Disulfide bond | 53↔62 | |||||
Sequence: CPEGFLGEYC | ||||||
Disulfide bond | 68↔79 | |||||
Sequence: CEKNRCQNGGTC | ||||||
Disulfide bond | 73↔90 | |||||
Sequence: CQNGGTCVTQAMLGKATC | ||||||
Disulfide bond | 92↔101 | |||||
Sequence: CAPGFTGEDC | ||||||
Disulfide bond | 109↔121 | |||||
Sequence: CFVSRPCQNGGTC | ||||||
Disulfide bond | 115↔131 | |||||
Sequence: CQNGGTCHMLSWDTYEC | ||||||
Disulfide bond | 133↔142 | |||||
Sequence: CQVGFTGKQC | ||||||
Disulfide bond | 148↔159 | |||||
Sequence: CLSHPCENGSTC | ||||||
Disulfide bond | 153↔168 | |||||
Sequence: CENGSTCSSVANQFSC | ||||||
Glycosylation | 155 | N-linked (GlcNAc...) asparagine | ||||
Sequence: N | ||||||
Disulfide bond | 170↔179 | |||||
Sequence: CPAGITGQKC | ||||||
Disulfide bond | 186↔198 | |||||
Sequence: CDIPGRCQHGGTC | ||||||
Disulfide bond | 192↔207 | |||||
Sequence: CQHGGTCLNLPGSYRC | ||||||
Disulfide bond | 209↔218 | |||||
Sequence: CPQRFTGQHC | ||||||
Disulfide bond | 225↔236 | |||||
Sequence: CAPSPCVNGGTC | ||||||
Disulfide bond | 230↔246 | |||||
Sequence: CVNGGTCRQTGDFTSEC | ||||||
Disulfide bond | 248↔257 | |||||
Sequence: CLPGFEGSNC | ||||||
Disulfide bond | 264↔275 | |||||
Sequence: CPNHKCQNGGVC | ||||||
Disulfide bond | 269↔284 | |||||
Sequence: CQNGGVCVDGVNTYNC | ||||||
Disulfide bond | 286↔295 | |||||
Sequence: CPPQWTGQFC | ||||||
Disulfide bond | 302↔315 | |||||
Sequence: CLLQPNACQNGGTC | ||||||
Disulfide bond | 309↔324 | |||||
Sequence: CQNGGTCTNRNGGYGC | ||||||
Disulfide bond | 326↔335 | |||||
Sequence: CVNGWSGDDC | ||||||
Disulfide bond | 342↔353 | |||||
Sequence: CAFASCTPGSTC | ||||||
Disulfide bond | 347↔362 | |||||
Sequence: CTPGSTCIDRVASFSC | ||||||
Disulfide bond | 364↔373 | |||||
Sequence: CPEGKAGLLC | ||||||
Disulfide bond | 379↔390 | |||||
Sequence: CISNPCHKGALC | ||||||
Disulfide bond | 384↔401 | |||||
Sequence: CHKGALCDTNPLNGQYIC | ||||||
Disulfide bond | 403↔412 | |||||
Sequence: CPQAYKGADC | ||||||
Disulfide bond | 419↔433 | |||||
Sequence: CAMANSNPCEHAGKC | ||||||
Disulfide bond | 427↔442 | |||||
Sequence: CEHAGKCVNTDGAFHC | ||||||
Disulfide bond | 444↔453 | |||||
Sequence: CLKGYAGPRC | ||||||
Disulfide bond | 460↔471 | |||||
Sequence: CHSDPCQNDATC | ||||||
Disulfide bond | 465↔480 | |||||
Sequence: CQNDATCLDKIGGFTC | ||||||
Disulfide bond | 482↔491 | |||||
Sequence: CMPGFKGVHC | ||||||
Disulfide bond | 498↔509 | |||||
Sequence: CQSNPCVNNGQC | ||||||
Disulfide bond | 503↔518 | |||||
Sequence: CVNNGQCVDKVNRFQC | ||||||
Disulfide bond | 520↔529 | |||||
Sequence: CPPGFTGPVC | ||||||
Disulfide bond | 536↔547 | |||||
Sequence: CSSTPCLNGAKC | ||||||
Disulfide bond | 541↔556 | |||||
Sequence: CLNGAKCIDHPNGYEC | ||||||
Disulfide bond | 558↔567 | |||||
Sequence: CATGFTGTLC | ||||||
Disulfide bond | 574↔584 | |||||
Sequence: CDPDPCHHGQC | ||||||
Disulfide bond | 579↔593 | |||||
Sequence: CHHGQCQDGIDSYTC | ||||||
Disulfide bond | 595↔604 | |||||
Sequence: CNPGYMGAIC | ||||||
Disulfide bond | 611↔622 | |||||
Sequence: CYSSPCLNDGRC | ||||||
Glycosylation | 613 | O-linked (Glc...) serine; alternate | ||||
Sequence: S | ||||||
Glycosylation | 613 | O-linked (Xyl...) serine; alternate | ||||
Sequence: S | ||||||
Disulfide bond | 616↔631 | |||||
Sequence: CLNDGRCIDLVNGYQC | ||||||
Disulfide bond | 633↔642 | |||||
Sequence: CQPGTSGLNC | ||||||
Disulfide bond | 649↔659 | |||||
Sequence: CASNPCLHGAC | ||||||
Disulfide bond | 654↔668 | |||||
Sequence: CLHGACVDGINRYSC | ||||||
Disulfide bond | 670↔679 | |||||
Sequence: CSPGFTGQRC | ||||||
Disulfide bond | 686↔697 | |||||
Sequence: CASNPCRKDATC | ||||||
Disulfide bond | 691↔706 | |||||
Sequence: CRKDATCINDVNGFRC | ||||||
Disulfide bond | 708↔717 | |||||
Sequence: CPEGPHHPSC | ||||||
Disulfide bond | 724↔734 | |||||
Sequence: CLSSPCIHGNC | ||||||
Disulfide bond | 729↔743 | |||||
Sequence: CIHGNCTGGLSGYKC | ||||||
Glycosylation | 733 | N-linked (GlcNAc...) asparagine | ||||
Sequence: N | ||||||
Disulfide bond | 745↔754 | |||||
Sequence: CDAGWVGINC | ||||||
Disulfide bond | 761↔772 | |||||
Sequence: CLSNPCQNGGTC | ||||||
Disulfide bond | 766↔781 | |||||
Sequence: CQNGGTCNNLVNGYRC | ||||||
Disulfide bond | 783↔792 | |||||
Sequence: CKKGFKGYNC | ||||||
Disulfide bond | 799↔810 | |||||
Sequence: CASNPCLNQGTC | ||||||
Disulfide bond | 804↔819 | |||||
Sequence: CLNQGTCLDDVSGYTC | ||||||
Disulfide bond | 821↔830 | |||||
Sequence: CMLPYTGKNC | ||||||
Disulfide bond | 837↔848 | |||||
Sequence: CSPNPCENAAVC | ||||||
Disulfide bond | 842↔859 | |||||
Sequence: CENAAVCKEAPNFESFTC | ||||||
Disulfide bond | 861↔870 | |||||
Sequence: CAPGWQGQRC | ||||||
Disulfide bond | 877↔888 | |||||
Sequence: CVSKPCMNNGIC | ||||||
Disulfide bond | 882↔897 | |||||
Sequence: CMNNGICHNTQGSYMC | ||||||
Disulfide bond | 899↔908 | |||||
Sequence: CPPGFSGMDC | ||||||
Disulfide bond | 915↔926 | |||||
Sequence: CLANPCQNGGSC | ||||||
Disulfide bond | 920↔935 | |||||
Sequence: CQNGGSCVDKVNTFSC | ||||||
Disulfide bond | 937↔946 | |||||
Sequence: CLPGFVGDKC | ||||||
Disulfide bond | 953↔964 | |||||
Sequence: CLSEPCKNGGTC | ||||||
Disulfide bond | 958↔973 | |||||
Sequence: CKNGGTCSDYVNSYTC | ||||||
Disulfide bond | 975↔984 | |||||
Sequence: CPAGFHGVHC | ||||||
Disulfide bond | 991↔1002 | |||||
Sequence: CTESSCFNGGTC | ||||||
Disulfide bond | 996↔1011 | |||||
Sequence: CFNGGTCVDGINSFSC | ||||||
Disulfide bond | 1013↔1022 | |||||
Sequence: CPVGFTGPFC | ||||||
Disulfide bond | 1029↔1040 | |||||
Sequence: CSSNPCLNSGTC | ||||||
Disulfide bond | 1034↔1049 | |||||
Sequence: CLNSGTCVDGLGTYRC | ||||||
Disulfide bond | 1051↔1060 | |||||
Sequence: CPLGYTGKNC | ||||||
Disulfide bond | 1067↔1078 | |||||
Sequence: CSPSPCKNKGTC | ||||||
Disulfide bond | 1072↔1087 | |||||
Sequence: CKNKGTCAQEKARPRC | ||||||
Disulfide bond | 1089↔1098 | |||||
Sequence: CPPGWDGAYC | ||||||
Glycosylation | 1102 | N-linked (GlcNAc...) asparagine | ||||
Sequence: N | ||||||
Disulfide bond | 1105↔1126 | |||||
Sequence: CKAAALQKGVPVEHLCQHSGIC | ||||||
Disulfide bond | 1120↔1135 | |||||
Sequence: CQHSGICINAGNTHHC | ||||||
Disulfide bond | 1137↔1146 | |||||
Sequence: CPLGYTGSYC | ||||||
Disulfide bond | 1153↔1164 | |||||
Sequence: CASNPCQHGATC | ||||||
Disulfide bond | 1158↔1173 | |||||
Sequence: CQHGATCSDFIGGYRC | ||||||
Disulfide bond | 1175↔1184 | |||||
Sequence: CVPGYQGVNC | ||||||
Disulfide bond | 1191↔1202 | |||||
Sequence: CQNQPCQNGGTC | ||||||
Disulfide bond | 1196↔1211 | |||||
Sequence: CQNGGTCIDLVNHFKC | ||||||
Disulfide bond | 1213↔1222 | |||||
Sequence: CPPGTRGLLC | ||||||
Disulfide bond | 1229↔1241 | |||||
Sequence: CAGAPHCLNGGQC | ||||||
Disulfide bond | 1235↔1250 | |||||
Sequence: CLNGGQCVDRIGGYSC | ||||||
Disulfide bond | 1252↔1261 | |||||
Sequence: CLPGFAGERC | ||||||
Disulfide bond | 1268↔1281 | |||||
Sequence: CLSNPCSSEGSLDC | ||||||
Disulfide bond | 1273↔1290 | |||||
Sequence: CSSEGSLDCIQLKNNYQC | ||||||
Disulfide bond | 1292↔1301 | |||||
Sequence: CRSAFTGRHC | ||||||
Disulfide bond | 1308↔1319 | |||||
Sequence: CPQKPCLNGGTC | ||||||
Disulfide bond | 1313↔1331 | |||||
Sequence: CLNGGTCAVASNVPDGFIC | ||||||
Disulfide bond | 1333↔1342 | |||||
Sequence: CPPGFSGARC | ||||||
Disulfide bond | 1378↔1389 | |||||
Sequence: CASNPCQHGGTC | ||||||
Disulfide bond | 1383↔1400 | |||||
Sequence: CQHGGTCYPQRQPPYYSC | ||||||
Disulfide bond | 1402↔1411 | |||||
Sequence: CSPPFWGSHC | ||||||
Disulfide bond | 1425↔1448 | |||||
Sequence: CLSQYCADKARDGICDEACNSHAC | ||||||
Disulfide bond | 1430↔1443 | |||||
Sequence: CADKARDGICDEAC | ||||||
Disulfide bond | 1439↔1455 | |||||
Sequence: CDEACNSHACQWDGGDC | ||||||
Glycosylation | 1465 | N-linked (GlcNAc...) asparagine | ||||
Sequence: N | ||||||
Disulfide bond | 1466↔1489 | |||||
Sequence: CTSSLRCWEYINNQCDELCNTAEC | ||||||
Disulfide bond | 1472↔1484 | |||||
Sequence: CWEYINNQCDELC | ||||||
Disulfide bond | 1480↔1496 | |||||
Sequence: CDELCNTAECLFDNFEC | ||||||
Disulfide bond | 1503↔1527 | |||||
Sequence: CKYDKYCADHFKDNHCDKGCNNEEC | ||||||
Disulfide bond | 1509↔1522 | |||||
Sequence: CADHFKDNHCDKGC | ||||||
Disulfide bond | 1518↔1534 | |||||
Sequence: CDKGCNNEECGWDGLDC | ||||||
Disulfide bond | 1632↔1639 | |||||
Sequence: CVQDSDQC | ||||||
Chain | PRO_0000007690 | 1666-2471 | Notch 2 extracellular truncation | |||
Sequence: VVSESEDPRNTPLLYLLAVAVVIILFLILLGVIMAKRKRKHGFLWLPEGFTLRRDSSNHKRREPVGQDAVGLKNLSVQVSEANLIGSTTSEHWGDDEGPQPKKAKAEDDEALLSEDDPVDRRPWTQQHLEAADIRRTPSLALTPPQAEQEVDVLDVNVRGPDGCTPLMLASLRGGSSDLSDEDEDAEDSSANIITDLVYQGASLQAQTDRTGEMALHLAARYSRADAAKRLLDAGADANAQDNMGRCPLHAAVAADAQGVFQILIRNRVTDLDARMNDGTTPLILAARLAVEGMVAELINCQADVNAVDDHGKSALHWAAAVNNVEATLLLLKNGANRDMQDNKEETPLFLAAREGSYEAAKILLDHFANRDITDHMDRLPRDVARDRMHHDIVRLLDEYNVTPSPPGTVLTSALSPVLCGPNRSFLSLKHTPMGKKARRPNTKSTMPTSLPNLAKEAKDVKGSRRKKCLNEKVQLSESSVTLSPVDSLESPHTYVSDATSSPMITSPGILQASPTPLLAAAPAAPVHAQHALSFSNLHEMQPLRPGASTVLPSVSQLLSHHHIVPPGSGSAGSLGRLHSVPVPSDWMNRVEMSETQYSEMFGMVLAPAEGTHPGMAAPQSRAPEGKPIPTQREPLPPIVTFQLIPKGSLAQAAGAPQTQSGCPPAVAGPLPSMYQIPEMARLPSVAFPPTMMPQQEGQVAQTIVPTYHPFPASVGKYPTPPSQHSYASSNAAERTPNHGGHLQGEHPYLTPSPESPDQWSSSSPHSASDWSDVTTSPTPGGGGGGQRGPGTHMSEPPHSNMQVYA | ||||||
Chain | PRO_0000007691 | 1697-2471 | Notch 2 intracellular domain | |||
Sequence: VIMAKRKRKHGFLWLPEGFTLRRDSSNHKRREPVGQDAVGLKNLSVQVSEANLIGSTTSEHWGDDEGPQPKKAKAEDDEALLSEDDPVDRRPWTQQHLEAADIRRTPSLALTPPQAEQEVDVLDVNVRGPDGCTPLMLASLRGGSSDLSDEDEDAEDSSANIITDLVYQGASLQAQTDRTGEMALHLAARYSRADAAKRLLDAGADANAQDNMGRCPLHAAVAADAQGVFQILIRNRVTDLDARMNDGTTPLILAARLAVEGMVAELINCQADVNAVDDHGKSALHWAAAVNNVEATLLLLKNGANRDMQDNKEETPLFLAAREGSYEAAKILLDHFANRDITDHMDRLPRDVARDRMHHDIVRLLDEYNVTPSPPGTVLTSALSPVLCGPNRSFLSLKHTPMGKKARRPNTKSTMPTSLPNLAKEAKDVKGSRRKKCLNEKVQLSESSVTLSPVDSLESPHTYVSDATSSPMITSPGILQASPTPLLAAAPAAPVHAQHALSFSNLHEMQPLRPGASTVLPSVSQLLSHHHIVPPGSGSAGSLGRLHSVPVPSDWMNRVEMSETQYSEMFGMVLAPAEGTHPGMAAPQSRAPEGKPIPTQREPLPPIVTFQLIPKGSLAQAAGAPQTQSGCPPAVAGPLPSMYQIPEMARLPSVAFPPTMMPQQEGQVAQTIVPTYHPFPASVGKYPTPPSQHSYASSNAAERTPNHGGHLQGEHPYLTPSPESPDQWSSSSPHSASDWSDVTTSPTPGGGGGGQRGPGTHMSEPPHSNMQVYA | ||||||
Modified residue | 1716 | Phosphothreonine | ||||
Sequence: T | ||||||
Modified residue | 1779 | Phosphoserine | ||||
Sequence: S | ||||||
Modified residue | 1802 | Phosphothreonine | ||||
Sequence: T | ||||||
Modified residue | 1804 | Phosphoserine | ||||
Sequence: S | ||||||
Modified residue | 1808 | Phosphothreonine | ||||
Sequence: T | ||||||
Modified residue | 1842 | Phosphoserine | ||||
Sequence: S | ||||||
Modified residue | 1845 | Phosphoserine | ||||
Sequence: S | ||||||
Modified residue | 2070 | Phosphoserine | ||||
Sequence: S | ||||||
Modified residue | 2078 | Phosphoserine | ||||
Sequence: S | ||||||
Modified residue | 2081 | Phosphoserine | ||||
Sequence: S | ||||||
Modified residue | 2097 | Phosphothreonine | ||||
Sequence: T |
Post-translational modification
Synthesized in the endoplasmic reticulum as an inactive form which is proteolytically cleaved by a furin-like convertase in the trans-Golgi network before it reaches the plasma membrane to yield an active, ligand-accessible form. Cleavage results in a C-terminal fragment N(TM) and a N-terminal fragment N(EC) (By similarity).
Following ligand binding, it is cleaved by TNF-alpha converting enzyme (TACE) to yield a membrane-associated intermediate fragment called notch extracellular truncation (NEXT) (By similarity).
This fragment is then cleaved by presenilin dependent gamma-secretase to release a notch-derived peptide containing the intracellular domain (NICD) from the membrane (By similarity).
Following ligand binding, it is cleaved by TNF-alpha converting enzyme (TACE) to yield a membrane-associated intermediate fragment called notch extracellular truncation (NEXT) (By similarity).
This fragment is then cleaved by presenilin dependent gamma-secretase to release a notch-derived peptide containing the intracellular domain (NICD) from the membrane (By similarity).
Phosphorylated. G-CSF treatment of myeloid cells specifically promotes Ser-2078 phosphorylation, which inactivates Notch2 and permits differentiation.
Hydroxylated by HIF1AN.
Can be either O-glucosylated or O-xylosylated at Ser-613 by POGLUT1.
Phosphorylated by GSK3. GSK3-mediated phosphorylation is necessary for NOTCH2 recognition by FBXW7, ubiquitination and degradation via the ubiquitin proteasome pathway.
Keywords
- PTM
Proteomic databases
PTM databases
Expression
Tissue specificity
Highly expressed in the spleen and choroid plexus in the brain. Expressed in postnatal central nervous system (CNS) germinal zones and, in early postnatal life, within numerous cells throughout the CNS. It is more highly localized to ventricular germinal zones. Also found in the heart, liver and kidney.
Developmental stage
Expressed in the brain during 14 dpc and 17 dpc.
Interaction
Subunit
Heterodimer of a C-terminal fragment N(TM) and an N-terminal fragment N(EC) which are probably linked by disulfide bonds (By similarity).
Interacts with MAML1, MAML2 and MAML3 which act as transcriptional coactivators for NOTCH2. Interacts with RELA/p65 (By similarity).
Interacts with HIF1AN. Interacts (via ANK repeats) with TCIM, the interaction inhibits the nuclear translocation of NOTCH2 N2ICD (By similarity).
Interacts with CUL1, RBX1, SKP1 and FBXW7 that are SCF(FBXW7) E3 ubiquitin-protein ligase complex components.Interacts with MINAR1; this interaction increases MINAR1 stability and function (By similarity).
Interacts with MDK; this interaction mediates a nuclear accumulation of NOTCH2 and therefore activation of NOTCH2 signaling leading to interaction between HES1 and STAT3 (By similarity).
Interacts with MINAR2 (By similarity).
Interacts with MAML1, MAML2 and MAML3 which act as transcriptional coactivators for NOTCH2. Interacts with RELA/p65 (By similarity).
Interacts with HIF1AN. Interacts (via ANK repeats) with TCIM, the interaction inhibits the nuclear translocation of NOTCH2 N2ICD (By similarity).
Interacts with CUL1, RBX1, SKP1 and FBXW7 that are SCF(FBXW7) E3 ubiquitin-protein ligase complex components.Interacts with MINAR1; this interaction increases MINAR1 stability and function (By similarity).
Interacts with MDK; this interaction mediates a nuclear accumulation of NOTCH2 and therefore activation of NOTCH2 signaling leading to interaction between HES1 and STAT3 (By similarity).
Interacts with MINAR2 (By similarity).
Protein-protein interaction databases
Structure
Family & Domains
Features
Showing features for domain, repeat, region, compositional bias.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Domain | 26-63 | EGF-like 1 | ||||
Sequence: LQCRGGQEPCVNEGTCVTYHNGTGYCRCPEGFLGEYCQ | ||||||
Domain | 64-102 | EGF-like 2 | ||||
Sequence: HRDPCEKNRCQNGGTCVTQAMLGKATCRCAPGFTGEDCQ | ||||||
Domain | 105-143 | EGF-like 3 | ||||
Sequence: TSHPCFVSRPCQNGGTCHMLSWDTYECTCQVGFTGKQCQ | ||||||
Domain | 144-180 | EGF-like 4 | ||||
Sequence: WTDVCLSHPCENGSTCSSVANQFSCRCPAGITGQKCD | ||||||
Domain | 182-219 | EGF-like 5; calcium-binding | ||||
Sequence: DINECDIPGRCQHGGTCLNLPGSYRCQCPQRFTGQHCD | ||||||
Domain | 221-258 | EGF-like 6 | ||||
Sequence: PYVPCAPSPCVNGGTCRQTGDFTSECHCLPGFEGSNCE | ||||||
Domain | 260-296 | EGF-like 7; calcium-binding | ||||
Sequence: NIDDCPNHKCQNGGVCVDGVNTYNCRCPPQWTGQFCT | ||||||
Domain | 298-336 | EGF-like 8; calcium-binding | ||||
Sequence: DVDECLLQPNACQNGGTCTNRNGGYGCVCVNGWSGDDCS | ||||||
Domain | 338-374 | EGF-like 9; calcium-binding | ||||
Sequence: NIDDCAFASCTPGSTCIDRVASFSCLCPEGKAGLLCH | ||||||
Domain | 375-413 | EGF-like 10 | ||||
Sequence: LDDACISNPCHKGALCDTNPLNGQYICTCPQAYKGADCT | ||||||
Domain | 415-454 | EGF-like 11; calcium-binding | ||||
Sequence: DVDECAMANSNPCEHAGKCVNTDGAFHCECLKGYAGPRCE | ||||||
Domain | 456-492 | EGF-like 12; calcium-binding | ||||
Sequence: DINECHSDPCQNDATCLDKIGGFTCLCMPGFKGVHCE | ||||||
Domain | 494-530 | EGF-like 13; calcium-binding | ||||
Sequence: EVNECQSNPCVNNGQCVDKVNRFQCLCPPGFTGPVCQ | ||||||
Domain | 532-568 | EGF-like 14; calcium-binding | ||||
Sequence: DIDDCSSTPCLNGAKCIDHPNGYECQCATGFTGTLCD | ||||||
Domain | 570-605 | EGF-like 15; calcium-binding | ||||
Sequence: NIDNCDPDPCHHGQCQDGIDSYTCICNPGYMGAICS | ||||||
Domain | 607-643 | EGF-like 16; calcium-binding | ||||
Sequence: QIDECYSSPCLNDGRCIDLVNGYQCNCQPGTSGLNCE | ||||||
Domain | 645-680 | EGF-like 17; calcium-binding | ||||
Sequence: NFDDCASNPCLHGACVDGINRYSCVCSPGFTGQRCN | ||||||
Domain | 682-718 | EGF-like 18; calcium-binding | ||||
Sequence: DIDECASNPCRKDATCINDVNGFRCMCPEGPHHPSCY | ||||||
Domain | 720-755 | EGF-like 19 | ||||
Sequence: QVNECLSSPCIHGNCTGGLSGYKCLCDAGWVGINCE | ||||||
Domain | 757-793 | EGF-like 20; calcium-binding | ||||
Sequence: DKNECLSNPCQNGGTCNNLVNGYRCTCKKGFKGYNCQ | ||||||
Domain | 795-831 | EGF-like 21; calcium-binding | ||||
Sequence: NIDECASNPCLNQGTCLDDVSGYTCHCMLPYTGKNCQ | ||||||
Domain | 833-871 | EGF-like 22 | ||||
Sequence: VLAPCSPNPCENAAVCKEAPNFESFTCLCAPGWQGQRCT | ||||||
Domain | 873-909 | EGF-like 23; calcium-binding | ||||
Sequence: DVDECVSKPCMNNGICHNTQGSYMCECPPGFSGMDCE | ||||||
Domain | 911-947 | EGF-like 24; calcium-binding | ||||
Sequence: DINDCLANPCQNGGSCVDKVNTFSCLCLPGFVGDKCQ | ||||||
Domain | 949-985 | EGF-like 25; calcium-binding | ||||
Sequence: DMNECLSEPCKNGGTCSDYVNSYTCTCPAGFHGVHCE | ||||||
Domain | 987-1023 | EGF-like 26; calcium-binding | ||||
Sequence: NIDECTESSCFNGGTCVDGINSFSCLCPVGFTGPFCL | ||||||
Domain | 1025-1061 | EGF-like 27; calcium-binding | ||||
Sequence: DINECSSNPCLNSGTCVDGLGTYRCTCPLGYTGKNCQ | ||||||
Domain | 1063-1099 | EGF-like 28 | ||||
Sequence: LVNLCSPSPCKNKGTCAQEKARPRCLCPPGWDGAYCD | ||||||
Domain | 1101-1147 | EGF-like 29 | ||||
Sequence: LNVSCKAAALQKGVPVEHLCQHSGICINAGNTHHCQCPLGYTGSYCE | ||||||
Domain | 1149-1185 | EGF-like 30; calcium-binding | ||||
Sequence: QLDECASNPCQHGATCSDFIGGYRCECVPGYQGVNCE | ||||||
Domain | 1187-1223 | EGF-like 31; calcium-binding | ||||
Sequence: EVDECQNQPCQNGGTCIDLVNHFKCSCPPGTRGLLCE | ||||||
Domain | 1225-1262 | EGF-like 32; calcium-binding | ||||
Sequence: NIDDCAGAPHCLNGGQCVDRIGGYSCRCLPGFAGERCE | ||||||
Domain | 1264-1302 | EGF-like 33 | ||||
Sequence: DINECLSNPCSSEGSLDCIQLKNNYQCVCRSAFTGRHCE | ||||||
Domain | 1304-1343 | EGF-like 34 | ||||
Sequence: FLDVCPQKPCLNGGTCAVASNVPDGFICRCPPGFSGARCQ | ||||||
Domain | 1374-1412 | EGF-like 35 | ||||
Sequence: CESGCASNPCQHGGTCYPQRQPPYYSCRCSPPFWGSHCE | ||||||
Repeat | 1425-1465 | LNR 1 | ||||
Sequence: CLSQYCADKARDGICDEACNSHACQWDGGDCSLTMEDPWAN | ||||||
Region | 1425-1677 | Negative regulatory region (NRR) | ||||
Sequence: CLSQYCADKARDGICDEACNSHACQWDGGDCSLTMEDPWANCTSSLRCWEYINNQCDELCNTAECLFDNFECQRNSKTCKYDKYCADHFKDNHCDKGCNNEECGWDGLDCAADQPENLAEGILVIVVLLPPEQLLQDSRSFLRALGTLLHTNLRIKQDSQGALMVYPYYGEKSAAMKKQKVARRSLPDEQEQEIIGSKVFLEIDNRQCVQDSDQCFKNTDAAAALLASHAIQGTLSYPLVSVVSESEDPRNTP | ||||||
Repeat | 1466-1502 | LNR 2 | ||||
Sequence: CTSSLRCWEYINNQCDELCNTAECLFDNFECQRNSKT | ||||||
Repeat | 1503-1544 | LNR 3 | ||||
Sequence: CKYDKYCADHFKDNHCDKGCNNEECGWDGLDCAADQPENLAE | ||||||
Region | 1751-1788 | Disordered | ||||
Sequence: GSTTSEHWGDDEGPQPKKAKAEDDEALLSEDDPVDRRP | ||||||
Compositional bias | 1760-1788 | Basic and acidic residues | ||||
Sequence: DDEGPQPKKAKAEDDEALLSEDDPVDRRP | ||||||
Region | 1794-1813 | Disordered | ||||
Sequence: LEAADIRRTPSLALTPPQAE | ||||||
Repeat | 1827-1871 | ANK 1 | ||||
Sequence: DGCTPLMLASLRGGSSDLSDEDEDAEDSSANIITDLVYQGASLQA | ||||||
Repeat | 1876-1905 | ANK 2 | ||||
Sequence: TGEMALHLAARYSRADAAKRLLDAGADANA | ||||||
Repeat | 1909-1939 | ANK 3 | ||||
Sequence: MGRCPLHAAVAADAQGVFQILIRNRVTDLDA | ||||||
Repeat | 1943-1972 | ANK 4 | ||||
Sequence: DGTTPLILAARLAVEGMVAELINCQADVNA | ||||||
Repeat | 1976-2005 | ANK 5 | ||||
Sequence: HGKSALHWAAAVNNVEATLLLLKNGANRDM | ||||||
Repeat | 2009-2038 | ANK 6 | ||||
Sequence: KEETPLFLAAREGSYEAAKILLDHFANRDI | ||||||
Region | 2097-2116 | Disordered | ||||
Sequence: TPMGKKARRPNTKSTMPTSL | ||||||
Region | 2380-2471 | Disordered | ||||
Sequence: VGKYPTPPSQHSYASSNAAERTPNHGGHLQGEHPYLTPSPESPDQWSSSSPHSASDWSDVTTSPTPGGGGGGQRGPGTHMSEPPHSNMQVYA | ||||||
Compositional bias | 2384-2402 | Polar residues | ||||
Sequence: PTPPSQHSYASSNAAERTP | ||||||
Compositional bias | 2419-2447 | Polar residues | ||||
Sequence: PESPDQWSSSSPHSASDWSDVTTSPTPGG |
Sequence similarities
Belongs to the NOTCH family.
Keywords
- Domain
Phylogenomic databases
Family and domain databases
Sequence
- Sequence statusComplete
- Sequence processingThe displayed sequence is further processed into a mature form.
- Length2,471
- Mass (Da)265,370
- Last updated2000-05-01 v1
- Checksum7D5C8E18DDE95FE8
Computationally mapped potential isoform sequences
There are 4 potential isoforms mapped to this entry
Entry | Entry name | Gene name | Length | ||
---|---|---|---|---|---|
A0A8I6B3I0 | A0A8I6B3I0_RAT | Notch2 | 2450 | ||
A0A8I6GM47 | A0A8I6GM47_RAT | Notch2 | 2421 | ||
G3V8G9 | G3V8G9_RAT | Notch2 | 2471 | ||
A0A1W2Q619 | A0A1W2Q619_RAT | Notch2 | 79 |
Features
Showing features for compositional bias.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Compositional bias | 1760-1788 | Basic and acidic residues | ||||
Sequence: DDEGPQPKKAKAEDDEALLSEDDPVDRRP | ||||||
Compositional bias | 2384-2402 | Polar residues | ||||
Sequence: PTPPSQHSYASSNAAERTP | ||||||
Compositional bias | 2419-2447 | Polar residues | ||||
Sequence: PESPDQWSSSSPHSASDWSDVTTSPTPGG |
Keywords
- Technical term
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
M93661 EMBL· GenBank· DDBJ | AAK13558.1 EMBL· GenBank· DDBJ | mRNA |