UniProtKB - Q07008 (NOTC1_RAT)
Neurogenic locus notch homolog protein 1
Notch1
Functioni
Sites
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Metal bindingi | 432 | Calcium 1; via carbonyl oxygenCombined sources1 Publication | 1 | |
Metal bindingi | 435 | Calcium 1; via amide nitrogenCombined sources1 Publication | 1 | |
Metal bindingi | 452 | Calcium 2Combined sources1 Publication | 1 | |
Metal bindingi | 453 | Calcium 2; via carbonyl oxygenCombined sources1 Publication | 1 | |
Metal bindingi | 455 | Calcium 2Combined sources1 Publication | 1 | |
Metal bindingi | 469 | Calcium 2Combined sources1 Publication | 1 | |
Metal bindingi | 470 | Calcium 2; via carbonyl oxygenCombined sources1 Publication | 1 | |
Metal bindingi | 490 | Calcium 3Combined sources1 Publication | 1 | |
Metal bindingi | 491 | Calcium 3; via carbonyl oxygenCombined sources1 Publication | 1 | |
Metal bindingi | 493 | Calcium 3Combined sources1 Publication | 1 | |
Metal bindingi | 507 | Calcium 3Combined sources1 Publication | 1 | |
Metal bindingi | 508 | Calcium 3; via carbonyl oxygenCombined sources1 Publication | 1 | |
Metal bindingi | 1457 | Calcium 4; via carbonyl oxygenPROSITE-ProRule annotation | 1 | |
Metal bindingi | 1460 | Calcium 4PROSITE-ProRule annotation | 1 | |
Metal bindingi | 1475 | Calcium 4PROSITE-ProRule annotation | 1 | |
Metal bindingi | 1478 | Calcium 4PROSITE-ProRule annotation | 1 |
GO - Molecular functioni
- calcium ion binding Source: InterPro
- chromatin binding Source: RGD
- chromatin DNA binding Source: RGD
- enzyme binding Source: UniProtKB
- enzyme inhibitor activity Source: UniProtKB
- identical protein binding Source: RGD
- Notch binding Source: RGD
- transcription coactivator activity Source: RGD
- transmembrane signaling receptor activity Source: WormBase
GO - Biological processi
- animal organ regeneration Source: RGD
- aortic valve morphogenesis Source: RGD
- apoptotic process involved in embryonic digit morphogenesis Source: RGD
- arterial endothelial cell differentiation Source: RGD
- astrocyte differentiation Source: RGD
- atrioventricular node development Source: RGD
- atrioventricular valve morphogenesis Source: RGD
- auditory receptor cell fate commitment Source: RGD
- axonogenesis Source: RGD
- brain development Source: RGD
- branching morphogenesis of an epithelial tube Source: RGD
- cardiac atrium morphogenesis Source: RGD
- cardiac chamber formation Source: RGD
- cardiac epithelial to mesenchymal transition Source: RGD
- cardiac left ventricle morphogenesis Source: RGD
- cardiac muscle cell proliferation Source: RGD
- cardiac muscle tissue morphogenesis Source: RGD
- cardiac right atrium morphogenesis Source: RGD
- cardiac right ventricle formation Source: RGD
- cardiac septum morphogenesis Source: RGD
- cardiac vascular smooth muscle cell development Source: RGD
- cardiac ventricle morphogenesis Source: RGD
- cell cycle arrest Source: RGD
- cell differentiation Source: RGD
- cell differentiation in spinal cord Source: RGD
- cell fate commitment Source: RGD
- cell fate specification Source: RGD
- cell migration involved in endocardial cushion formation Source: RGD
- cellular response to follicle-stimulating hormone stimulus Source: RGD
- cellular response to vascular endothelial growth factor stimulus Source: UniProtKB
- central nervous system development Source: GO_Central
- cilium assembly Source: UniProtKB
- collecting duct development Source: RGD
- compartment pattern specification Source: RGD
- coronary artery morphogenesis Source: RGD
- coronary sinus valve morphogenesis Source: RGD
- coronary vein morphogenesis Source: RGD
- determination of left/right symmetry Source: RGD
- distal tubule development Source: RGD
- embryonic hindlimb morphogenesis Source: RGD
- embryonic limb morphogenesis Source: RGD
- endocardial cell differentiation Source: RGD
- endocardial cushion development Source: RGD
- endocardial cushion morphogenesis Source: RGD
- endocardium development Source: RGD
- endocardium morphogenesis Source: RGD
- endoderm development Source: RGD
- epidermis development Source: RGD
- epithelial to mesenchymal transition Source: RGD
- epithelial to mesenchymal transition involved in endocardial cushion formation Source: RGD
- forebrain development Source: RGD
- foregut morphogenesis Source: RGD
- glial cell differentiation Source: RGD
- glomerular mesangial cell development Source: RGD
- growth involved in heart morphogenesis Source: RGD
- hair follicle morphogenesis Source: RGD
- heart development Source: RGD
- heart looping Source: RGD
- heart trabecula morphogenesis Source: RGD
- homeostasis of number of cells within a tissue Source: RGD
- humoral immune response Source: RGD
- inflammatory response to antigenic stimulus Source: RGD
- interleukin-4 production Source: RGD
- in utero embryonic development Source: RGD
- keratinocyte differentiation Source: RGD
- left/right axis specification Source: RGD
- liver development Source: RGD
- lung development Source: RGD
- mesenchymal cell development Source: RGD
- mitral valve formation Source: RGD
- negative regulation of anoikis Source: RGD
- negative regulation of biomineral tissue development Source: RGD
- negative regulation of BMP signaling pathway Source: RGD
- negative regulation of calcium ion-dependent exocytosis Source: RGD
- negative regulation of canonical Wnt signaling pathway Source: RGD
- negative regulation of cardiac muscle hypertrophy Source: RGD
- negative regulation of catalytic activity Source: UniProtKB
- negative regulation of cell adhesion molecule production Source: RGD
- negative regulation of cell-cell adhesion mediated by cadherin Source: RGD
- negative regulation of cell death Source: RGD
- negative regulation of cell differentiation Source: RGD
- negative regulation of cell migration involved in sprouting angiogenesis Source: UniProtKB
- negative regulation of cell population proliferation Source: UniProtKB
- negative regulation of cell proliferation involved in heart valve morphogenesis Source: RGD
- negative regulation of cell-substrate adhesion Source: RGD
- negative regulation of cold-induced thermogenesis Source: YuBioLab
- negative regulation of endothelial cell chemotaxis Source: UniProtKB
- negative regulation of extracellular matrix constituent secretion Source: RGD
- negative regulation of gene expression Source: RGD
- negative regulation of glial cell proliferation Source: UniProtKB
- negative regulation of growth rate Source: RGD
- negative regulation of inner ear auditory receptor cell differentiation Source: RGD
- negative regulation of myoblast differentiation Source: RGD
- negative regulation of myotube differentiation Source: UniProtKB
- negative regulation of neurogenesis Source: UniProtKB
- negative regulation of neuron differentiation Source: RGD
- negative regulation of oligodendrocyte differentiation Source: UniProtKB
- negative regulation of ossification Source: RGD
- negative regulation of osteoblast differentiation Source: RGD
- negative regulation of photoreceptor cell differentiation Source: RGD
- negative regulation of pro-B cell differentiation Source: UniProtKB
- negative regulation of stem cell differentiation Source: RGD
- negative regulation of transcription, DNA-templated Source: RGD
- negative regulation of transcription by RNA polymerase II Source: UniProtKB
- neural tube development Source: RGD
- neuronal stem cell population maintenance Source: RGD
- neuron differentiation Source: RGD
- neuron fate commitment Source: RGD
- Notch signaling involved in heart development Source: UniProtKB
- Notch signaling pathway Source: WormBase
- Notch signaling pathway involved in regulation of secondary heart field cardioblast proliferation Source: RGD
- oligodendrocyte differentiation Source: RGD
- outflow tract morphogenesis Source: RGD
- pericardium morphogenesis Source: RGD
- positive regulation of aorta morphogenesis Source: RGD
- positive regulation of apoptotic process Source: RGD
- positive regulation of apoptotic process involved in morphogenesis Source: RGD
- positive regulation of astrocyte differentiation Source: UniProtKB
- positive regulation of BMP signaling pathway Source: UniProtKB
- positive regulation of cardiac epithelial to mesenchymal transition Source: BHF-UCL
- positive regulation of cardiac muscle cell proliferation Source: RGD
- positive regulation of cell migration Source: RGD
- positive regulation of cell population proliferation Source: RGD
- positive regulation of endothelial cell differentiation Source: RGD
- positive regulation of epithelial cell proliferation Source: RGD
- positive regulation of epithelial to mesenchymal transition Source: RGD
- positive regulation of ERK1 and ERK2 cascade Source: RGD
- positive regulation of gene expression Source: BHF-UCL
- positive regulation of glial cell differentiation Source: RGD
- positive regulation of keratinocyte differentiation Source: RGD
- positive regulation of neuroblast proliferation Source: RGD
- positive regulation of Notch signaling pathway Source: RGD
- positive regulation of Ras protein signal transduction Source: RGD
- positive regulation of receptor signaling pathway via JAK-STAT Source: UniProtKB
- positive regulation of transcription, DNA-templated Source: UniProtKB
- positive regulation of transcription by RNA polymerase II Source: RGD
- positive regulation of transcription from RNA polymerase II promoter in response to hypoxia Source: UniProtKB
- positive regulation of transcription of Notch receptor target Source: RGD
- positive regulation of viral genome replication Source: RGD
- positive regulation of viral transcription Source: RGD
- prostate gland epithelium morphogenesis Source: RGD
- pulmonary valve morphogenesis Source: RGD
- regulation of cardioblast proliferation Source: RGD
- regulation of cell migration Source: RGD
- regulation of cell population proliferation Source: RGD
- regulation of epithelial cell proliferation Source: RGD
- regulation of epithelial cell proliferation involved in prostate gland development Source: RGD
- regulation of extracellular matrix assembly Source: RGD
- regulation of gene expression Source: RGD
- regulation of inner ear auditory receptor cell differentiation Source: RGD
- regulation of neurogenesis Source: RGD
- regulation of Notch signaling pathway Source: RGD
- regulation of somitogenesis Source: RGD
- regulation of transcription by RNA polymerase II Source: RGD
- regulation of transcription from RNA polymerase II promoter involved in myocardial precursor cell differentiation Source: RGD
- response to corticosteroid Source: RGD
- response to lipopolysaccharide Source: RGD
- response to muramyl dipeptide Source: RGD
- secretory columnal luminar epithelial cell differentiation involved in prostate glandular acinus development Source: RGD
- skeletal muscle cell differentiation Source: RGD
- skeletal system development Source: GO_Central
- somatic stem cell division Source: RGD
- spermatogenesis Source: RGD
- sprouting angiogenesis Source: RGD
- tissue regeneration Source: RGD
- tube formation Source: UniProtKB
- vasculogenesis involved in coronary vascular morphogenesis Source: RGD
- venous blood vessel morphogenesis Source: RGD
- venous endothelial cell differentiation Source: RGD
- ventricular septum morphogenesis Source: RGD
- ventricular trabecula myocardium morphogenesis Source: RGD
Keywordsi
Molecular function | Activator, Developmental protein, Receptor |
Biological process | Angiogenesis, Differentiation, Notch signaling pathway, Transcription, Transcription regulation |
Ligand | Calcium, Metal-binding |
Names & Taxonomyi
Protein namesi | Recommended name: Neurogenic locus notch homolog protein 1Short name: Notch 1 Cleaved into the following 2 chains: |
Gene namesi | Name:Notch1 |
Organismi | Rattus norvegicus (Rat) |
Taxonomic identifieri | 10116 [NCBI] |
Taxonomic lineagei | Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Glires › Rodentia › Myomorpha › Muroidea › Muridae › Murinae › Rattus |
Proteomesi |
|
Organism-specific databases
RGDi | 3187, Notch1 |
Subcellular locationi
Plasma membrane
- Cell membrane By similarity; Single-pass type I membrane protein By similarity
Nucleus
- Nucleus By similarity
Note: Following proteolytical processing NICD is translocated to the nucleus. Nuclear location may require MEGF10.By similarity
Cytoskeleton
- cytoskeleton Source: UniProtKB
Endoplasmic reticulum
- endoplasmic reticulum Source: RGD
Extracellular region or secreted
- extracellular matrix Source: GO_Central
Golgi apparatus
- Golgi apparatus Source: RGD
Nucleus
- nucleus Source: BHF-UCL
Plasma Membrane
- apical plasma membrane Source: UniProtKB
- plasma membrane Source: BHF-UCL
Other locations
- acrosomal vesicle Source: RGD
- adherens junction Source: UniProtKB
- cell periphery Source: RGD
- cell surface Source: RGD
- cytoplasm Source: RGD
- cytoplasmic vesicle Source: RGD
- integral component of membrane Source: UniProtKB-KW
- lamellipodium Source: UniProtKB
- MAML1-RBP-Jkappa- ICN1 complex Source: RGD
- receptor complex Source: RGD
- ruffle Source: UniProtKB
Topology
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Topological domaini | 19 – 1725 | ExtracellularCuratedAdd BLAST | 1707 | |
Transmembranei | 1726 – 1746 | HelicalBy similarityAdd BLAST | 21 | |
Topological domaini | 1747 – 2531 | CytoplasmicCuratedAdd BLAST | 785 |
Keywords - Cellular componenti
Cell membrane, Membrane, NucleusPTM / Processingi
Molecule processing
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Signal peptidei | 1 – 18 | Sequence analysisAdd BLAST | 18 | |
ChainiPRO_0000007680 | 19 – 2531 | Neurogenic locus notch homolog protein 1Add BLAST | 2513 | |
ChainiPRO_0000007681 | 1711 – 2531 | Notch 1 extracellular truncationBy similarityAdd BLAST | 821 | |
ChainiPRO_0000007682 | 1744 – 2531 | Notch 1 intracellular domainBy similarityAdd BLAST | 788 |
Amino acid modifications
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Disulfide bondi | 24 ↔ 37 | By similarity | ||
Disulfide bondi | 31 ↔ 46 | By similarity | ||
Glycosylationi | 41 | N-linked (GlcNAc...) asparagineSequence analysis | 1 | |
Disulfide bondi | 48 ↔ 57 | By similarity | ||
Disulfide bondi | 63 ↔ 74 | By similarity | ||
Glycosylationi | 65 | O-linked (Glc...) serineBy similarity | 1 | |
Disulfide bondi | 68 ↔ 87 | By similarity | ||
Glycosylationi | 73 | O-linked (Fuc...) threonineBy similarity | 1 | |
Disulfide bondi | 89 ↔ 98 | By similarity | ||
Disulfide bondi | 106 ↔ 117 | By similarity | ||
Disulfide bondi | 111 ↔ 127 | By similarity | ||
Glycosylationi | 116 | O-linked (Fuc...) threonineBy similarity | 1 | |
Disulfide bondi | 129 ↔ 138 | By similarity | ||
Disulfide bondi | 144 ↔ 155 | By similarity | ||
Glycosylationi | 146 | O-linked (Glc...) serineBy similarity | 1 | |
Disulfide bondi | 149 ↔ 164 | By similarity | ||
Disulfide bondi | 166 ↔ 175 | By similarity | ||
Disulfide bondi | 182 ↔ 195 | By similarity | ||
Disulfide bondi | 189 ↔ 204 | By similarity | ||
Glycosylationi | 194 | O-linked (Fuc...) threonineBy similarity | 1 | |
Disulfide bondi | 206 ↔ 215 | By similarity | ||
Disulfide bondi | 222 ↔ 233 | By similarity | ||
Disulfide bondi | 227 ↔ 243 | By similarity | ||
Glycosylationi | 232 | O-linked (Fuc...) threonine; alternateBy similarity | 1 | |
Glycosylationi | 232 | O-linked (GalNAc...) threonine; alternateBy similarity | 1 | |
Disulfide bondi | 245 ↔ 254 | By similarity | ||
Disulfide bondi | 261 ↔ 272 | By similarity | ||
Disulfide bondi | 266 ↔ 281 | By similarity | ||
Disulfide bondi | 283 ↔ 292 | By similarity | ||
Disulfide bondi | 299 ↔ 312 | By similarity | ||
Disulfide bondi | 306 ↔ 321 | By similarity | ||
Glycosylationi | 311 | O-linked (Fuc...) threonineBy similarity | 1 | |
Disulfide bondi | 323 ↔ 332 | By similarity | ||
Disulfide bondi | 339 ↔ 350 | By similarity | ||
Glycosylationi | 341 | O-linked (Glc...) serineBy similarity | 1 | |
Disulfide bondi | 344 ↔ 359 | By similarity | ||
Glycosylationi | 349 | O-linked (Fuc...) threonineBy similarity | 1 | |
Disulfide bondi | 361 ↔ 370 | By similarity | ||
Disulfide bondi | 376 ↔ 387 | By similarity | ||
Glycosylationi | 378 | O-linked (Glc...) serineBy similarity | 1 | |
Disulfide bondi | 381 ↔ 398 | By similarity | ||
Disulfide bondi | 400 ↔ 409 | By similarity | ||
Disulfide bondi | 416 ↔ 429 | Combined sources1 Publication | ||
Disulfide bondi | 423 ↔ 438 | Combined sources1 Publication | ||
Glycosylationi | 435 | O-linked (Glc...) serineCombined sources1 Publication | 1 | |
Disulfide bondi | 440 ↔ 449 | Combined sources1 Publication | ||
Disulfide bondi | 456 ↔ 467 | Combined sources1 Publication | ||
Glycosylationi | 458 | O-linked (Glc...) serine1 Publication | 1 | |
Disulfide bondi | 461 ↔ 476 | Combined sources1 Publication | ||
Glycosylationi | 466 | O-linked (Fuc...) threonineCombined sources1 Publication | 1 | |
Disulfide bondi | 478 ↔ 487 | Combined sources1 Publication | ||
Disulfide bondi | 494 ↔ 505 | Combined sources1 Publication | ||
Glycosylationi | 496 | O-linked (Glc...) serine1 Publication | 1 | |
Disulfide bondi | 499 ↔ 514 | Combined sources1 Publication | ||
Disulfide bondi | 516 ↔ 525 | Combined sources1 Publication | ||
Disulfide bondi | 532 ↔ 543 | By similarity | ||
Glycosylationi | 534 | O-linked (Glc...) serineBy similarity | 1 | |
Disulfide bondi | 537 ↔ 552 | By similarity | ||
Disulfide bondi | 554 ↔ 563 | By similarity | ||
Disulfide bondi | 570 ↔ 580 | By similarity | ||
Disulfide bondi | 575 ↔ 589 | By similarity | ||
Disulfide bondi | 591 ↔ 600 | By similarity | ||
Disulfide bondi | 607 ↔ 618 | By similarity | ||
Glycosylationi | 609 | O-linked (Glc...) serineBy similarity | 1 | |
Disulfide bondi | 612 ↔ 627 | By similarity | ||
Glycosylationi | 617 | O-linked (Fuc...) threonineBy similarity | 1 | |
Disulfide bondi | 629 ↔ 638 | By similarity | ||
Disulfide bondi | 645 ↔ 655 | By similarity | ||
Glycosylationi | 647 | O-linked (Glc...) serineBy similarity | 1 | |
Disulfide bondi | 650 ↔ 664 | By similarity | ||
Disulfide bondi | 666 ↔ 675 | By similarity | ||
Disulfide bondi | 682 ↔ 693 | By similarity | ||
Disulfide bondi | 687 ↔ 702 | By similarity | ||
Glycosylationi | 692 | O-linked (Fuc...) threonineBy similarity | 1 | |
Disulfide bondi | 704 ↔ 713 | By similarity | ||
Disulfide bondi | 720 ↔ 730 | By similarity | ||
Glycosylationi | 722 | O-linked (Glc...) serineBy similarity | 1 | |
Disulfide bondi | 725 ↔ 739 | By similarity | ||
Disulfide bondi | 741 ↔ 750 | By similarity | ||
Disulfide bondi | 757 ↔ 768 | By similarity | ||
Glycosylationi | 759 | O-linked (Glc...) serineBy similarity | 1 | |
Disulfide bondi | 762 ↔ 777 | By similarity | ||
Glycosylationi | 767 | O-linked (Fuc...) threonineBy similarity | 1 | |
Disulfide bondi | 779 ↔ 788 | By similarity | ||
Glycosylationi | 784 | O-linked (GlcNAc) serineBy similarity | 1 | |
Disulfide bondi | 795 ↔ 806 | By similarity | ||
Glycosylationi | 797 | O-linked (Glc...) serineBy similarity | 1 | |
Disulfide bondi | 800 ↔ 815 | By similarity | ||
Glycosylationi | 805 | O-linked (Fuc...) threonineBy similarity | 1 | |
Disulfide bondi | 817 ↔ 826 | By similarity | ||
Disulfide bondi | 833 ↔ 844 | By similarity | ||
Disulfide bondi | 838 ↔ 855 | By similarity | ||
Disulfide bondi | 857 ↔ 866 | By similarity | ||
Disulfide bondi | 873 ↔ 884 | By similarity | ||
Disulfide bondi | 878 ↔ 893 | By similarity | ||
Glycosylationi | 888 | N-linked (GlcNAc...) asparagineSequence analysis | 1 | |
Disulfide bondi | 895 ↔ 904 | By similarity | ||
Glycosylationi | 900 | O-linked (GlcNAc) threonineBy similarity | 1 | |
Disulfide bondi | 911 ↔ 922 | By similarity | ||
Disulfide bondi | 916 ↔ 931 | By similarity | ||
Glycosylationi | 921 | O-linked (Fuc) serineBy similarity | 1 | |
Disulfide bondi | 933 ↔ 942 | By similarity | ||
Disulfide bondi | 949 ↔ 960 | By similarity | ||
Glycosylationi | 951 | O-linked (Glc...) serineBy similarity | 1 | |
Disulfide bondi | 954 ↔ 969 | By similarity | ||
Glycosylationi | 959 | N-linked (GlcNAc...) asparagineSequence analysis | 1 | |
Disulfide bondi | 971 ↔ 980 | By similarity | ||
Disulfide bondi | 987 ↔ 998 | By similarity | ||
Disulfide bondi | 992 ↔ 1007 | By similarity | ||
Glycosylationi | 997 | O-linked (Fuc...) threonineBy similarity | 1 | |
Disulfide bondi | 1009 ↔ 1018 | By similarity | ||
Disulfide bondi | 1025 ↔ 1036 | By similarity | ||
Glycosylationi | 1027 | O-linked (Glc...) serineBy similarity | 1 | |
Disulfide bondi | 1030 ↔ 1045 | By similarity | ||
Glycosylationi | 1035 | O-linked (Fuc...) threonineBy similarity | 1 | |
Disulfide bondi | 1047 ↔ 1056 | By similarity | ||
Disulfide bondi | 1063 ↔ 1074 | By similarity | ||
Glycosylationi | 1065 | O-linked (Glc...) serineBy similarity | 1 | |
Disulfide bondi | 1068 ↔ 1083 | By similarity | ||
Disulfide bondi | 1085 ↔ 1094 | By similarity | ||
Disulfide bondi | 1101 ↔ 1122 | Curated | ||
Disulfide bondi | 1116 ↔ 1131 | By similarity | ||
Disulfide bondi | 1133 ↔ 1142 | By similarity | ||
Disulfide bondi | 1149 ↔ 1160 | By similarity | ||
Disulfide bondi | 1154 ↔ 1169 | By similarity | ||
Glycosylationi | 1159 | O-linked (Fuc...) threonineBy similarity | 1 | |
Disulfide bondi | 1171 ↔ 1180 | By similarity | ||
Glycosylationi | 1179 | N-linked (GlcNAc...) asparagineSequence analysis | 1 | |
Disulfide bondi | 1187 ↔ 1198 | By similarity | ||
Glycosylationi | 1189 | O-linked (Glc...) serineBy similarity | 1 | |
Disulfide bondi | 1192 ↔ 1207 | By similarity | ||
Glycosylationi | 1197 | O-linked (Fuc...) threonineBy similarity | 1 | |
Disulfide bondi | 1209 ↔ 1218 | By similarity | ||
Disulfide bondi | 1225 ↔ 1244 | By similarity | ||
Disulfide bondi | 1238 ↔ 1253 | By similarity | ||
Glycosylationi | 1241 | N-linked (GlcNAc...) asparagineSequence analysis | 1 | |
Disulfide bondi | 1255 ↔ 1264 | By similarity | ||
Disulfide bondi | 1271 ↔ 1284 | By similarity | ||
Glycosylationi | 1273 | O-linked (Glc...) serineBy similarity | 1 | |
Disulfide bondi | 1276 ↔ 1293 | By similarity | ||
Disulfide bondi | 1295 ↔ 1304 | By similarity | ||
Disulfide bondi | 1311 ↔ 1322 | By similarity | ||
Disulfide bondi | 1316 ↔ 1334 | By similarity | ||
Disulfide bondi | 1336 ↔ 1345 | By similarity | ||
Disulfide bondi | 1352 ↔ 1363 | By similarity | ||
Disulfide bondi | 1357 ↔ 1372 | By similarity | ||
Glycosylationi | 1362 | O-linked (Fuc...) threonineBy similarity | 1 | |
Disulfide bondi | 1374 ↔ 1383 | By similarity | ||
Glycosylationi | 1379 | O-linked (GlcNAc...) threonineBy similarity | 1 | |
Disulfide bondi | 1391 ↔ 1403 | By similarity | ||
Disulfide bondi | 1397 ↔ 1414 | By similarity | ||
Glycosylationi | 1402 | O-linked (Fuc...) threonine; alternateBy similarity | 1 | |
Glycosylationi | 1402 | O-linked (GalNAc...) threonine; alternateBy similarity | 1 | |
Disulfide bondi | 1416 ↔ 1425 | By similarity | ||
Disulfide bondi | 1449 ↔ 1472 | By similarity | ||
Disulfide bondi | 1454 ↔ 1467 | By similarity | ||
Disulfide bondi | 1463 ↔ 1479 | By similarity | ||
Glycosylationi | 1489 | N-linked (GlcNAc...) asparagineSequence analysis | 1 | |
Disulfide bondi | 1490 ↔ 1514 | By similarity | ||
Disulfide bondi | 1496 ↔ 1509 | By similarity | ||
Disulfide bondi | 1505 ↔ 1521 | By similarity | ||
Disulfide bondi | 1536 ↔ 1549 | By similarity | ||
Disulfide bondi | 1545 ↔ 1561 | By similarity | ||
Glycosylationi | 1587 | N-linked (GlcNAc...) asparagineSequence analysis | 1 | |
Glycosylationi | 1715 | O-linked (GalNAc...) threonineBy similarity | 1 | |
Cross-linki | 1749 | Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)By similarity | ||
Modified residuei | 1851 | PhosphothreonineBy similarity | 1 | |
Modified residuei | 1945 | (3S)-3-hydroxyasparagine; by HIF1ANBy similarity | 1 | |
Modified residuei | 2012 | (3S)-3-hydroxyasparagine; by HIF1ANBy similarity | 1 |
Post-translational modificationi
Sites
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Sitei | 1654 – 1655 | Cleavage; by furin-like proteaseBy similarity | 2 | |
Sitei | 1710 – 1711 | Cleavage; by ADAM17By similarity | 2 |
Keywords - PTMi
Disulfide bond, Glycoprotein, Hydroxylation, Isopeptide bond, Phosphoprotein, Ubl conjugationProteomic databases
PaxDbi | Q07008 |
PRIDEi | Q07008 |
PTM databases
GlyGeni | Q07008, 48 sites |
iPTMneti | Q07008 |
PhosphoSitePlusi | Q07008 |
Expressioni
Tissue specificityi
Developmental stagei
Gene expression databases
Bgeei | ENSRNOG00000019322, Expressed in lung and 21 other tissues |
Genevisiblei | Q07008, RN |
Interactioni
Subunit structurei
Heterodimer of a C-terminal fragment N(TM) and an N-terminal fragment N(EC) which are probably linked by disulfide bonds.
Interacts with DNER, DTX1, DTX2 and RBPJ/RBPSUH.
Also interacts with MAML1, MAML2 and MAML3 which act as transcriptional coactivators for NOTCH1. Notch 1 intracellular domain interacts with SNW1; the interaction involves multimerized NOTCH1 NICD and is implicated in a formation of an intermediate preactivation complex which associates with DNA-bound CBF-1/RBPJ. The activated membrane-bound form interacts with AAK1 which promotes NOTCH1 stabilization.
Forms a trimeric complex with FBXW7 and SGK1.
Interacts with HIF1AN. HIF1AN negatively regulates the function of notch intracellular domain (NICD), accelerating myogenic differentiation.
Interacts (via NICD) with SNAI1 (via zinc fingers); the interaction induces SNAI1 degradation via MDM2-mediated ubiquitination and inhibits SNAI1-induced cell invasion.
Interacts (via NICD) with MDM2A.
Interacts (via NICD) with BCL6; the interaction decreases MAML1 recruitment by NOTCH1 NICD on target genes DNA and inhibits NOTCH1 transcractivation activity (By similarity).
Interacts with THBS4 (By similarity).
Interacts (via the EGF-like repeat region) with CCN3 (via CTCK domain) (By similarity).
Interacts (via EGF-like domains) with DLL4 (via N-terminal DSL and MNNL domains) (PubMed:25700513).
Interacts with ZMIZ1 (By similarity).
Interacts (via NICD domain) with MEGF10 (via the cytoplasmic domain).
Interacts with DLL1 and JAG1 (By similarity).
Interacts (via NICD domain) with PRAG1 (By similarity).
Forms a complex with PRAG1, N1ICD and MAML1, in a MAML1-dependent manner (By similarity).
Interacts (via transmembrane region) with PSEN1; the interaction is direct (By similarity).
By similarity1 PublicationSites
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Sitei | 469 | Interaction with DLL4Combined sources1 Publication | 1 |
GO - Molecular functioni
- enzyme binding Source: UniProtKB
- identical protein binding Source: RGD
- Notch binding Source: RGD
Protein-protein interaction databases
IntActi | Q07008, 3 interactors |
STRINGi | 10116.ENSRNOP00000026212 |
Structurei
Secondary structure
3D structure databases
SMRi | Q07008 |
ModBasei | Search... |
PDBe-KBi | Search... |
Family & Domainsi
Domains and Repeats
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Domaini | 20 – 58 | EGF-like 1PROSITE-ProRule annotationAdd BLAST | 39 | |
Domaini | 59 – 99 | EGF-like 2PROSITE-ProRule annotationAdd BLAST | 41 | |
Domaini | 102 – 139 | EGF-like 3PROSITE-ProRule annotationAdd BLAST | 38 | |
Domaini | 140 – 176 | EGF-like 4PROSITE-ProRule annotationAdd BLAST | 37 | |
Domaini | 178 – 216 | EGF-like 5; calcium-bindingPROSITE-ProRule annotationAdd BLAST | 39 | |
Domaini | 218 – 255 | EGF-like 6PROSITE-ProRule annotationAdd BLAST | 38 | |
Domaini | 257 – 293 | EGF-like 7; calcium-bindingPROSITE-ProRule annotationAdd BLAST | 37 | |
Domaini | 295 – 333 | EGF-like 8; calcium-bindingPROSITE-ProRule annotationAdd BLAST | 39 | |
Domaini | 335 – 371 | EGF-like 9; calcium-bindingPROSITE-ProRule annotationAdd BLAST | 37 | |
Domaini | 372 – 410 | EGF-like 10PROSITE-ProRule annotationAdd BLAST | 39 | |
Domaini | 412 – 450 | EGF-like 11; calcium-bindingPROSITE-ProRule annotationAdd BLAST | 39 | |
Domaini | 452 – 488 | EGF-like 12; calcium-bindingPROSITE-ProRule annotationAdd BLAST | 37 | |
Domaini | 490 – 526 | EGF-like 13; calcium-bindingPROSITE-ProRule annotationAdd BLAST | 37 | |
Domaini | 528 – 564 | EGF-like 14; calcium-bindingPROSITE-ProRule annotationAdd BLAST | 37 | |
Domaini | 566 – 601 | EGF-like 15; calcium-bindingPROSITE-ProRule annotationAdd BLAST | 36 | |
Domaini | 603 – 639 | EGF-like 16; calcium-bindingPROSITE-ProRule annotationAdd BLAST | 37 | |
Domaini | 641 – 676 | EGF-like 17; calcium-bindingPROSITE-ProRule annotationAdd BLAST | 36 | |
Domaini | 678 – 714 | EGF-like 18; calcium-bindingPROSITE-ProRule annotationAdd BLAST | 37 | |
Domaini | 716 – 751 | EGF-like 19; calcium-bindingPROSITE-ProRule annotationAdd BLAST | 36 | |
Domaini | 753 – 789 | EGF-like 20; calcium-bindingPROSITE-ProRule annotationAdd BLAST | 37 | |
Domaini | 791 – 827 | EGF-like 21; calcium-bindingPROSITE-ProRule annotationAdd BLAST | 37 | |
Domaini | 829 – 867 | EGF-like 22PROSITE-ProRule annotationAdd BLAST | 39 | |
Domaini | 869 – 905 | EGF-like 23; calcium-bindingPROSITE-ProRule annotationAdd BLAST | 37 | |
Domaini | 907 – 943 | EGF-like 24PROSITE-ProRule annotationAdd BLAST | 37 | |
Domaini | 945 – 981 | EGF-like 25; calcium-bindingPROSITE-ProRule annotationAdd BLAST | 37 | |
Domaini | 983 – 1019 | EGF-like 26PROSITE-ProRule annotationAdd BLAST | 37 | |
Domaini | 1021 – 1057 | EGF-like 27; calcium-bindingPROSITE-ProRule annotationAdd BLAST | 37 | |
Domaini | 1059 – 1095 | EGF-like 28PROSITE-ProRule annotationAdd BLAST | 37 | |
Domaini | 1097 – 1143 | EGF-like 29CuratedAdd BLAST | 47 | |
Domaini | 1145 – 1181 | EGF-like 30; calcium-bindingPROSITE-ProRule annotationAdd BLAST | 37 | |
Domaini | 1183 – 1219 | EGF-like 31; calcium-bindingPROSITE-ProRule annotationAdd BLAST | 37 | |
Domaini | 1221 – 1265 | EGF-like 32; calcium-bindingPROSITE-ProRule annotationAdd BLAST | 45 | |
Domaini | 1267 – 1305 | EGF-like 33PROSITE-ProRule annotationAdd BLAST | 39 | |
Domaini | 1307 – 1346 | EGF-like 34PROSITE-ProRule annotationAdd BLAST | 40 | |
Domaini | 1348 – 1384 | EGF-like 35PROSITE-ProRule annotationAdd BLAST | 37 | |
Domaini | 1387 – 1426 | EGF-like 36PROSITE-ProRule annotationAdd BLAST | 40 | |
Repeati | 1449 – 1489 | LNR 1Add BLAST | 41 | |
Repeati | 1490 – 1531 | LNR 2Add BLAST | 42 | |
Repeati | 1532 – 1571 | LNR 3Add BLAST | 40 | |
Repeati | 1917 – 1946 | ANK 1Add BLAST | 30 | |
Repeati | 1950 – 1980 | ANK 2Add BLAST | 31 | |
Repeati | 1984 – 2013 | ANK 3Add BLAST | 30 | |
Repeati | 2017 – 2046 | ANK 4Add BLAST | 30 | |
Repeati | 2050 – 2079 | ANK 5Add BLAST | 30 |
Region
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Regioni | 420 – 421 | Interaction with DLL4Combined sources1 Publication | 2 | |
Regioni | 448 – 452 | Interaction with DLL4Combined sources1 Publication | 5 | |
Regioni | 1718 – 1750 | Interaction with PSEN1By similarityAdd BLAST | 33 | |
Regioni | 1937 – 1945 | HIF1AN-bindingBy similarity | 9 | |
Regioni | 2004 – 2012 | HIF1AN-bindingBy similarity | 9 |
Compositional bias
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Compositional biasi | 1730 – 1733 | Poly-Ala | 4 | |
Compositional biasi | 1891 – 1894 | Poly-Glu | 4 | |
Compositional biasi | 2258 – 2261 | Poly-Pro | 4 | |
Compositional biasi | 2497 – 2500 | Poly-Ser | 4 |
Domaini
Sequence similaritiesi
Keywords - Domaini
ANK repeat, EGF-like domain, Repeat, Signal, Transmembrane, Transmembrane helixPhylogenomic databases
eggNOGi | KOG1217, Eukaryota |
GeneTreei | ENSGT00940000157157 |
HOGENOMi | CLU_000576_0_0_1 |
InParanoidi | Q07008 |
OMAi | NEGSCLD |
OrthoDBi | 7525at2759 |
TreeFami | TF351641 |
Family and domain databases
Gene3Di | 1.25.40.20, 1 hit |
InterProi | View protein in InterPro IPR002110, Ankyrin_rpt IPR020683, Ankyrin_rpt-contain_dom IPR036770, Ankyrin_rpt-contain_sf IPR024600, DUF3454_notch IPR001881, EGF-like_Ca-bd_dom IPR013032, EGF-like_CS IPR000742, EGF-like_dom IPR000152, EGF-type_Asp/Asn_hydroxyl_site IPR018097, EGF_Ca-bd_CS IPR009030, Growth_fac_rcpt_cys_sf IPR008297, Notch IPR035993, Notch-like_dom_sf IPR022362, Notch_1 IPR000800, Notch_dom IPR010660, Notch_NOD_dom IPR011656, Notch_NODP_dom |
Pfami | View protein in Pfam PF12796, Ank_2, 2 hits PF11936, DUF3454, 1 hit PF00008, EGF, 20 hits PF07645, EGF_CA, 5 hits PF12661, hEGF, 4 hits PF06816, NOD, 1 hit PF07684, NODP, 1 hit PF00066, Notch, 3 hits |
PIRSFi | PIRSF002279, Notch, 1 hit |
PRINTSi | PR01452, LNOTCHREPEAT PR01984, NOTCH1 |
SMARTi | View protein in SMART SM00248, ANK, 6 hits SM01334, DUF3454, 1 hit SM00181, EGF, 36 hits SM00179, EGF_CA, 32 hits SM00004, NL, 3 hits SM01338, NOD, 1 hit SM01339, NODP, 1 hit |
SUPFAMi | SSF48403, SSF48403, 1 hit SSF57184, SSF57184, 5 hits SSF90193, SSF90193, 3 hits |
PROSITEi | View protein in PROSITE PS50297, ANK_REP_REGION, 1 hit PS50088, ANK_REPEAT, 4 hits PS00010, ASX_HYDROXYL, 22 hits PS00022, EGF_1, 35 hits PS01186, EGF_2, 27 hits PS50026, EGF_3, 36 hits PS01187, EGF_CA, 21 hits PS50258, LNR, 3 hits |
i Sequence
Sequence statusi: Complete.
: The displayed sequence is further processed into a mature form. Sequence processingi
10 20 30 40 50
MPRLLAPLLC LTLLPALAAR GLRCSQPSGT CLNGGRCEVA NGTEACVCSG
60 70 80 90 100
AFVGQRCQDP SPCLSTPCKN AGTCYVVDHG GIVDYACSCP LGFSGPLCLT
110 120 130 140 150
PLANACLANP CRNGGTCDLL TLTEYKCRCP PGWSGKSCQQ ADPCASNPCA
160 170 180 190 200
NGGQCLPFES SYICGCPPGF HGPTCRQDVN ECSQNPGLCR HGGTCHNEIG
210 220 230 240 250
SYRCACRATH TGPHCELPYV PCSPSPCQNG GTCRPTGDTT HECACLPGFA
260 270 280 290 300
GQNCEENVDD CPGNNCKNGG ACVDGVNTYN CRCPPEWTGQ YCTEDVDECQ
310 320 330 340 350
LMPNACQNGG TCHNSHGGYN CVCVNGWTGE DCSENIDDCA SAACFQGATC
360 370 380 390 400
HDRVASFYCE CPHGRTGLLC HLNDACISNP CNEGSNCDTN PVNGKAICTC
410 420 430 440 450
PSGYTGPACS QDVDECALGA NPCEHAGKCL NTLGSFECQC LQGYTGPRCE
460 470 480 490 500
IDVNECISNP CQNDATCLDQ IGEFQCICMP GYEGVYCEIN TDECASSPCL
510 520 530 540 550
HNGRCVDKIN EFLCQCPKGF SGHLCQYDVD ECASTPCKNG AKCLDGPNTY
560 570 580 590 600
TCVCTEGYTG THCEVDIDEC DPDPCHYGLC KDGVATFTCL CQPGYTGHHC
610 620 630 640 650
ETNINECHSQ PCRHGGTCQD RDNYYLCLCL KGTTGPNCEI NLDDCASNPC
660 670 680 690 700
DSGTCLDKID GYECACEPGY TGSMCNVNID ECAGSPCHNG GTCEDGIAGF
710 720 730 740 750
TCRCPEGYHD PTCLSEVNEC NSNPCIHGAC RDGLNGYKCD CAPGWSGTNC
760 770 780 790 800
DINNNECESN PCVNGGTCKD MTSGYVCTCR EGFSGPNCQT NINECASNPC
810 820 830 840 850
LNQGTCIDDV AGYKCNCPLP YTGATCEVVL APCATSPCKN SGVCKESEDY
860 870 880 890 900
ESFSCVCPTG WQGQTCEIDI NECVKSPCRH GASCQNTNGS YRCLCQAGYT
910 920 930 940 950
GRNCESDIDD CRPNPCHNGG SCTDGVNAAF CDCLPGFQGA FCEEDINECA
960 970 980 990 1000
SNPCQNGANC TDCVDSYTCT CPTGFNGIHC ENNTPDCTES SCFNGGTCVD
1010 1020 1030 1040 1050
GINSFTCLCP PGFTGSYCQY DVNECDSRPC LHGGTCQDSY GTYKCTCPQG
1060 1070 1080 1090 1100
YTGLNCQNLV RWCDSAPCKN GGKCWQTNTQ YHCECRSGWT GFNCDVLSVS
1110 1120 1130 1140 1150
CEVAAQKRGI DVTLLCQHGG LCVDEEDKHY CHCQAGYTGS YCEDEVDECS
1160 1170 1180 1190 1200
PNPCQNGATC TDYLGGFSCK CVAGYHGSNC SEEINECLSQ PCQNGGTCID
1210 1220 1230 1240 1250
LTNTYKCSCP RGTQGVHCEI NVDDCHPPLD PASRSPKCFN NGTCVDQVGG
1260 1270 1280 1290 1300
YTCTCPPGFV GERCEGDVNE CLSNPCDPRG TQNCVQRVND FHCECRAGHT
1310 1320 1330 1340 1350
GRRCESVING CRGKPCRNGG VCAVASNTAR GFICRCPAGF EGATCENDAR
1360 1370 1380 1390 1400
TCGSLRCLNG GTCISGPRSP TCLCLGSFTG PECQFPASSP CVGSNPCYNQ
1410 1420 1430 1440 1450
GTCEPTSESP FYRCLCPAKF NGLLCHILDY SFTGGAGRDI PPPQIEEACE
1460 1470 1480 1490 1500
LPECQEDAGN KVCNLQCNNH ACGWDGGDCS LNFNDPWKNC TQSLQCWKYF
1510 1520 1530 1540 1550
SDGHCDSQCN SAGCLFDGFD CQLTEGQCNP LYDQYCKDHF SDGHCDQGCN
1560 1570 1580 1590 1600
SAECEWDGLD CAEHVPERLA AGTLVLVVLL PPDQLRNNSF HFLRELSHVL
1610 1620 1630 1640 1650
HTNVVFKRDA QGQQMIFPYY GREEELRKHP IKRSAVGWAT TSLLPGTNGG
1660 1670 1680 1690 1700
RQRRELDPMD IHGSIVYLEI DNRQCVQSSS QCFQSATDVA AFLGALASLG
1710 1720 1730 1740 1750
SLNIPYKIEA VKSETVEPPL PSQLHLMYVA AAAFVLLFFV GCGVLLSRKR
1760 1770 1780 1790 1800
RRQHGQLWFP EGFKVSEASK KKRREPLGED SVGLKPLKNA SDGALMDDNQ
1810 1820 1830 1840 1850
NEWGDEDLET KKFRFEEPVV LPDLDDQTDH RQWTQQHLDA ADLRVSAMAP
1860 1870 1880 1890 1900
TPPQGEVDAD CMDVNVRGPD GFTPLMIASC SGGGLETGNS EEEEDAPAVI
1910 1920 1930 1940 1950
SDFIYQGASL HNQTDRTGET ALHLAARYSR SDAAKRLLEA SADANIQDNM
1960 1970 1980 1990 2000
GRTPLHAAVS ADAQGVFQIL LRNRATDLDA RMHDGTTPLI LAARLAVEGM
2010 2020 2030 2040 2050
LEDLINSHAD VNAVDDLGKS ALHWAAAVNN VDAAVVLLKN GANKDMQNNK
2060 2070 2080 2090 2100
EETPLFLAAR EGSYETAKVL LDHFANRDIT DHMDRLPRDI AQERMHHDIV
2110 2120 2130 2140 2150
RLLDEYNLVR SPQLHGTALG GTPTLSPTLC SPNGYLGNLK SATQGKKARK
2160 2170 2180 2190 2200
PSTKGLACSS KEAKDLKARR KKSQDGKGCL LDSSSMLSPV DSLESPHGYL
2210 2220 2230 2240 2250
SDVASPPLLP SPFQQSPSMP LSHLPGMPDT HLGISHLNVA AKPEMAALAG
2260 2270 2280 2290 2300
GSRLAFEPPP PRLSHLPVAS SASTVLSTNG TGAMNFTVGA PASLNGQCEW
2310 2320 2330 2340 2350
LPRLQNGMVP SQYNPLRPGV TPGTLSTQAA GLQHGMMGPI HSSLSTNTLS
2360 2370 2380 2390 2400
PIIYQGLPNT RLATQPHLVQ TQQVQPQNLQ IQPQNLQPPS QPHLSVSSAA
2410 2420 2430 2440 2450
NGHLGRSFLS GEPSQADVQP LGPSSLPVHT ILPQESQALP TSLPSSMVPP
2460 2470 2480 2490 2500
MTTTQFLTPP SQHSYSSSPV DNTPSHQLQV PEHPFLTPSP ESPDQWSSSS
2510 2520 2530
PHSNISDWSE GISSPPTSMP SQITHIPEAF K
Experimental Info
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Sequence conflicti | 309 | G → A in CAA40667 (PubMed:1764995).Curated | 1 | |
Sequence conflicti | 334 | E → D in CAA40667 (PubMed:1764995).Curated | 1 | |
Sequence conflicti | 402 | S → R in CAA40667 (PubMed:1764995).Curated | 1 | |
Sequence conflicti | 577 | Y → I in CAA40667 (PubMed:1764995).Curated | 1 | |
Sequence conflicti | 951 | S → T in CAA40667 (PubMed:1764995).Curated | 1 | |
Sequence conflicti | 1339 | G → R in CAA40667 (PubMed:1764995).Curated | 1 | |
Sequence conflicti | 1435 | G → A in CAA40667 (PubMed:1764995).Curated | 1 | |
Sequence conflicti | 1595 – 1596 | EL → DV in CAA40667 (PubMed:1764995).Curated | 2 | |
Sequence conflicti | 2501 | P → R in CAA40667 (PubMed:1764995).Curated | 1 |
Sequence databases
Select the link destinations: EMBLi GenBanki DDBJi Links Updated | X57405 mRNA Translation: CAA40667.1 AABR06021907 Genomic DNA No translation available. AABR06021908 Genomic DNA No translation available. CH474001 Genomic DNA Translation: EDL93491.1 |
PIRi | S18188 |
RefSeqi | NP_001099191.1, NM_001105721.1 |
Genome annotation databases
Ensembli | ENSRNOT00000026212; ENSRNOP00000026212; ENSRNOG00000019322 |
GeneIDi | 25496 |
KEGGi | rno:25496 |
UCSCi | RGD:3187, rat |
Similar proteinsi
Cross-referencesi
Sequence databases
Select the link destinations: EMBLi GenBanki DDBJi Links Updated | X57405 mRNA Translation: CAA40667.1 AABR06021907 Genomic DNA No translation available. AABR06021908 Genomic DNA No translation available. CH474001 Genomic DNA Translation: EDL93491.1 |
PIRi | S18188 |
RefSeqi | NP_001099191.1, NM_001105721.1 |
3D structure databases
Select the link destinations: PDBei RCSB PDBi PDBji Links Updated | PDB entry | Method | Resolution (Å) | Chain | Positions | PDBsum |
4XL1 | X-ray | 2.30 | A/D | 412-526 | [»] | |
4XLW | X-ray | 3.39 | A/C/E/G | 412-526 | [»] | |
5UK5 | X-ray | 2.51 | A | 295-488 | [»] | |
SMRi | Q07008 | |||||
ModBasei | Search... | |||||
PDBe-KBi | Search... |
Protein-protein interaction databases
IntActi | Q07008, 3 interactors |
STRINGi | 10116.ENSRNOP00000026212 |
PTM databases
GlyGeni | Q07008, 48 sites |
iPTMneti | Q07008 |
PhosphoSitePlusi | Q07008 |
Proteomic databases
PaxDbi | Q07008 |
PRIDEi | Q07008 |
Genome annotation databases
Ensembli | ENSRNOT00000026212; ENSRNOP00000026212; ENSRNOG00000019322 |
GeneIDi | 25496 |
KEGGi | rno:25496 |
UCSCi | RGD:3187, rat |
Organism-specific databases
CTDi | 4851 |
RGDi | 3187, Notch1 |
Phylogenomic databases
eggNOGi | KOG1217, Eukaryota |
GeneTreei | ENSGT00940000157157 |
HOGENOMi | CLU_000576_0_0_1 |
InParanoidi | Q07008 |
OMAi | NEGSCLD |
OrthoDBi | 7525at2759 |
TreeFami | TF351641 |
Miscellaneous databases
PROi | PR:Q07008 |
Gene expression databases
Bgeei | ENSRNOG00000019322, Expressed in lung and 21 other tissues |
Genevisiblei | Q07008, RN |
Family and domain databases
Gene3Di | 1.25.40.20, 1 hit |
InterProi | View protein in InterPro IPR002110, Ankyrin_rpt IPR020683, Ankyrin_rpt-contain_dom IPR036770, Ankyrin_rpt-contain_sf IPR024600, DUF3454_notch IPR001881, EGF-like_Ca-bd_dom IPR013032, EGF-like_CS IPR000742, EGF-like_dom IPR000152, EGF-type_Asp/Asn_hydroxyl_site IPR018097, EGF_Ca-bd_CS IPR009030, Growth_fac_rcpt_cys_sf IPR008297, Notch IPR035993, Notch-like_dom_sf IPR022362, Notch_1 IPR000800, Notch_dom IPR010660, Notch_NOD_dom IPR011656, Notch_NODP_dom |
Pfami | View protein in Pfam PF12796, Ank_2, 2 hits PF11936, DUF3454, 1 hit PF00008, EGF, 20 hits PF07645, EGF_CA, 5 hits PF12661, hEGF, 4 hits PF06816, NOD, 1 hit PF07684, NODP, 1 hit PF00066, Notch, 3 hits |
PIRSFi | PIRSF002279, Notch, 1 hit |
PRINTSi | PR01452, LNOTCHREPEAT PR01984, NOTCH1 |
SMARTi | View protein in SMART SM00248, ANK, 6 hits SM01334, DUF3454, 1 hit SM00181, EGF, 36 hits SM00179, EGF_CA, 32 hits SM00004, NL, 3 hits SM01338, NOD, 1 hit SM01339, NODP, 1 hit |
SUPFAMi | SSF48403, SSF48403, 1 hit SSF57184, SSF57184, 5 hits SSF90193, SSF90193, 3 hits |
PROSITEi | View protein in PROSITE PS50297, ANK_REP_REGION, 1 hit PS50088, ANK_REPEAT, 4 hits PS00010, ASX_HYDROXYL, 22 hits PS00022, EGF_1, 35 hits PS01186, EGF_2, 27 hits PS50026, EGF_3, 36 hits PS01187, EGF_CA, 21 hits PS50258, LNR, 3 hits |
ProtoNeti | Search... |
MobiDBi | Search... |
Entry informationi
Entry namei | NOTC1_RAT | |
Accessioni | Q07008Primary (citable) accession number: Q07008 Secondary accession number(s): F1M9E7 | |
Entry historyi | Integrated into UniProtKB/Swiss-Prot: | November 1, 1995 |
Last sequence update: | October 16, 2013 | |
Last modified: | December 2, 2020 | |
This is version 209 of the entry and version 3 of the sequence. See complete history. | ||
Entry statusi | Reviewed (UniProtKB/Swiss-Prot) | |
Annotation program | Chordata Protein Annotation Program |
Miscellaneousi
Keywords - Technical termi
3D-structure, Reference proteomeDocuments
- PDB cross-references
Index of Protein Data Bank (PDB) cross-references - SIMILARITY comments
Index of protein domains and families