UniProtKB - Q07008 (NOTC1_RAT)
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Protein
Neurogenic locus notch homolog protein 1
Gene
Notch1
Organism
Rattus norvegicus (Rat)
Status
Functioni
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) (By similarity).By similarity1 Publication
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 DNA binding Source: Ensembl
- DNA binding transcription factor activity Source: Ensembl
- enzyme binding Source: UniProtKB
- enzyme inhibitor activity Source: UniProtKB
- Notch binding Source: Ensembl
- protein heterodimerization activity Source: Ensembl
- RNA polymerase II proximal promoter sequence-specific DNA binding Source: UniProtKB
- transcriptional activator activity, RNA polymerase II transcription factor binding Source: Ensembl
- transmembrane signaling receptor activity Source: WormBase
GO - Biological processi
- animal organ regeneration Source: RGD
- aortic valve morphogenesis Source: Ensembl
- apoptotic process involved in embryonic digit morphogenesis Source: Ensembl
- arterial endothelial cell differentiation Source: Ensembl
- astrocyte differentiation Source: RGD
- atrioventricular node development Source: Ensembl
- auditory receptor cell fate commitment Source: Ensembl
- axonogenesis Source: Ensembl
- brain development Source: RGD
- branching morphogenesis of an epithelial tube Source: Ensembl
- cardiac epithelial to mesenchymal transition Source: BHF-UCL
- cardiac left ventricle morphogenesis Source: Ensembl
- cardiac muscle cell proliferation Source: Ensembl
- cardiac right atrium morphogenesis Source: Ensembl
- cardiac right ventricle formation Source: Ensembl
- cardiac vascular smooth muscle cell development Source: Ensembl
- cell cycle arrest Source: Ensembl
- cell differentiation in spinal cord Source: RGD
- cell fate specification Source: Ensembl
- cell migration involved in endocardial cushion formation Source: Ensembl
- cellular response to follicle-stimulating hormone stimulus Source: Ensembl
- cellular response to vascular endothelial growth factor stimulus Source: UniProtKB
- cilium assembly Source: UniProtKB
- collecting duct development Source: Ensembl
- compartment pattern specification Source: Ensembl
- coronary artery morphogenesis Source: Ensembl
- coronary sinus valve morphogenesis Source: Ensembl
- coronary vein morphogenesis Source: Ensembl
- distal tubule development Source: Ensembl
- embryonic hindlimb morphogenesis Source: Ensembl
- endocardial cell differentiation Source: Ensembl
- endocardium morphogenesis Source: Ensembl
- endoderm development Source: Ensembl
- epithelial to mesenchymal transition involved in endocardial cushion formation Source: Ensembl
- forebrain development Source: Ensembl
- foregut morphogenesis Source: Ensembl
- glomerular mesangial cell development Source: Ensembl
- growth involved in heart morphogenesis Source: Ensembl
- hair follicle morphogenesis Source: Ensembl
- heart looping Source: Ensembl
- homeostasis of number of cells within a tissue Source: Ensembl
- humoral immune response Source: Ensembl
- inflammatory response to antigenic stimulus Source: Ensembl
- interleukin-4 secretion Source: Ensembl
- in utero embryonic development Source: Ensembl
- keratinocyte differentiation Source: Ensembl
- left/right axis specification Source: Ensembl
- liver development Source: Ensembl
- lung development Source: Ensembl
- mesenchymal cell development Source: Ensembl
- mitral valve formation Source: Ensembl
- negative regulation of anoikis Source: Ensembl
- negative regulation of biomineral tissue development Source: BHF-UCL
- negative regulation of BMP signaling pathway Source: Ensembl
- negative regulation of calcium ion-dependent exocytosis Source: Ensembl
- negative regulation of canonical Wnt signaling pathway Source: Ensembl
- negative regulation of cardiac muscle hypertrophy Source: Ensembl
- negative regulation of catalytic activity Source: UniProtKB
- negative regulation of cell migration involved in sprouting angiogenesis Source: UniProtKB
- negative regulation of cell proliferation Source: UniProtKB
- negative regulation of cell proliferation involved in heart valve morphogenesis Source: Ensembl
- negative regulation of cell-substrate adhesion Source: Ensembl
- negative regulation of endothelial cell chemotaxis Source: UniProtKB
- negative regulation of extracellular matrix constituent secretion Source: Ensembl
- negative regulation of glial cell proliferation Source: UniProtKB
- negative regulation of growth rate Source: Ensembl
- negative regulation of inner ear auditory receptor cell differentiation Source: Ensembl
- negative regulation of myoblast differentiation Source: Ensembl
- 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 osteoblast differentiation Source: Ensembl
- negative regulation of photoreceptor cell differentiation Source: Ensembl
- negative regulation of pro-B cell differentiation Source: UniProtKB
- negative regulation of stem cell differentiation Source: Ensembl
- negative regulation of transcription by RNA polymerase II Source: UniProtKB
- neural tube development Source: Ensembl
- neuronal stem cell population maintenance Source: Ensembl
- 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: Ensembl
- oligodendrocyte differentiation Source: RGD
- outflow tract morphogenesis Source: Ensembl
- pericardium morphogenesis Source: Ensembl
- positive regulation of aorta morphogenesis Source: Ensembl
- positive regulation of apoptotic process involved in morphogenesis Source: Ensembl
- positive regulation of astrocyte differentiation Source: UniProtKB
- positive regulation of BMP signaling pathway Source: UniProtKB
- positive regulation of cardiac muscle cell proliferation Source: Ensembl
- positive regulation of cell migration Source: Ensembl
- positive regulation of endothelial cell differentiation Source: RGD
- positive regulation of epithelial cell proliferation Source: Ensembl
- positive regulation of epithelial to mesenchymal transition Source: Ensembl
- positive regulation of ERK1 and ERK2 cascade Source: Ensembl
- positive regulation of gene expression Source: BHF-UCL
- positive regulation of glial cell differentiation Source: RGD
- positive regulation of JAK-STAT cascade Source: UniProtKB
- positive regulation of keratinocyte differentiation Source: Ensembl
- positive regulation of neuroblast proliferation Source: RGD
- positive regulation of Notch signaling pathway Source: Ensembl
- positive regulation of Ras protein signal transduction Source: Ensembl
- 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: Ensembl
- prostate gland epithelium morphogenesis Source: Ensembl
- pulmonary valve morphogenesis Source: Ensembl
- regulation of cardioblast proliferation Source: RGD
- regulation of cell proliferation Source: RGD
- regulation of epithelial cell proliferation involved in prostate gland development Source: Ensembl
- regulation of extracellular matrix assembly Source: Ensembl
- regulation of somitogenesis Source: Ensembl
- regulation of transcription from RNA polymerase II promoter involved in myocardial precursor cell differentiation Source: Ensembl
- response to corticosteroid Source: RGD
- response to lipopolysaccharide Source: RGD
- response to muramyl dipeptide Source: Ensembl
- secretory columnal luminar epithelial cell differentiation involved in prostate glandular acinus development Source: Ensembl
- skeletal muscle cell differentiation Source: Ensembl
- somatic stem cell division Source: Ensembl
- spermatogenesis Source: RGD
- sprouting angiogenesis Source: Ensembl
- tissue regeneration Source: RGD
- tube formation Source: UniProtKB
- vasculogenesis involved in coronary vascular morphogenesis Source: Ensembl
- venous endothelial cell differentiation Source: Ensembl
- ventricular septum morphogenesis Source: Ensembl
- ventricular trabecula myocardium morphogenesis Source: Ensembl
Keywordsi
| Molecular function | Activator, Developmental protein, Receptor |
| Biological process | Angiogenesis, Differentiation, Notch signaling pathway, Transcription, Transcription regulation |
| Ligand | Calcium, Metal-binding |
Enzyme and pathway databases
| Reactomei | R-RNO-1912420 Pre-NOTCH Processing in Golgi R-RNO-2122947 NOTCH1 Intracellular Domain Regulates Transcription R-RNO-2122948 Activated NOTCH1 Transmits Signal to the Nucleus R-RNO-350054 Notch-HLH transcription pathway R-RNO-8941856 RUNX3 regulates NOTCH signaling |
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
Topology
| Feature key | Position(s) | DescriptionActions | Graphical view | Length |
|---|---|---|---|---|
| Topological domaini | 19 – 1723 | ExtracellularSequence analysisAdd BLAST | 1705 | |
| Transmembranei | 1724 – 1746 | HelicalSequence analysisAdd BLAST | 23 | |
| Topological domaini | 1747 – 2531 | CytoplasmicSequence analysisAdd 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 | By similarity | ||
| 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
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). Following ligand binding, it is cleaved by ADAM17 to yield a membrane-associated intermediate fragment called notch extracellular truncation (NEXT). Following endocytosis, 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.By similarity
O-glycosylated on the EGF-like domains. Contains both O-linked fucose and O-linked glucose in the EGF-like domains 11, 12 and 13, which are interacting with the residues on DLL4 (PubMed:25700513). O-linked glycosylation by GALNT11 is involved in determination of left/right symmetry: glycosylation promotes activation of NOTCH1, possibly by promoting cleavage by ADAM17, modulating the balance between motile and immotile (sensory) cilia at the left-right organiser (LRO). MFNG-, RFNG- and LFNG-mediated modification of O-fucose residues at specific EGF-like domains results in inhibition of its activation by JAG1 and enhancement of its activation by DLL1 via an increased binding to DLL1 (By similarity).By similarity1 Publication
Ubiquitinated. Undergoes 'Lys-29'-linked polyubiquitination by ITCH; promotes the lysosomal degradation of non-activated internalized NOTCH1. Monoubiquitination at Lys-1749 is required for activation by gamma-secretase cleavage, it promotes interaction with AAK1, which stabilizes it. Deubiquitination by EIF3F is necessary for nuclear import of activated Notch.By similarity
Hydroxylated at Asn-1945 and Asn-2012 by HIF1AN. Hydroxylation reduces affinity for HI1AN and may thus indirectly modulate negative regulation of NICD (By similarity).By similarity
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
| iPTMneti | Q07008 |
| PhosphoSitePlusi | Q07008 |
Expressioni
Tissue specificityi
Expressed in the brain, kidney and spleen. Expressed in postnatal central nervous system (CNS) germinal zones and, in early postnatal life, within numerous cells throughout the CNS. Found in both subventricular and ventricular germinal zones.2 Publications
Developmental stagei
In the embryo, highest levels occur between days 12 and 14 and decrease rapidly to much lower levels in the adult.
Gene expression databases
| Bgeei | ENSRNOG00000019322 |
| 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 NOV (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).By similarity1 Publication
Sites
| Feature key | Position(s) | DescriptionActions | Graphical view | Length |
|---|---|---|---|---|
| Sitei | 469 | Interaction with DLL4Combined sources1 Publication | 1 |
GO - Molecular functioni
- enzyme binding Source: UniProtKB
- Notch binding Source: Ensembl
- protein heterodimerization activity Source: Ensembl
Protein-protein interaction databases
| IntActi | Q07008, 3 interactors |
| STRINGi | 10116.ENSRNOP00000026212 |
Structurei
Secondary structure
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details| Feature key | Position(s) | DescriptionActions | Graphical view | Length |
|---|---|---|---|---|
| Beta strandi | 301 – 303 | Combined sources | 3 | |
| Turni | 307 – 309 | Combined sources | 3 | |
| Beta strandi | 311 – 314 | Combined sources | 4 | |
| Beta strandi | 319 – 322 | Combined sources | 4 | |
| Beta strandi | 327 – 331 | Combined sources | 5 | |
| Beta strandi | 349 – 353 | Combined sources | 5 | |
| Beta strandi | 356 – 360 | Combined sources | 5 | |
| Beta strandi | 366 – 370 | Combined sources | 5 | |
| Helixi | 375 – 378 | Combined sources | 4 | |
| Beta strandi | 386 – 389 | Combined sources | 4 | |
| Turni | 391 – 393 | Combined sources | 3 | |
| Beta strandi | 396 – 399 | Combined sources | 4 | |
| Beta strandi | 404 – 406 | Combined sources | 3 | |
| Helixi | 415 – 418 | Combined sources | 4 | |
| Turni | 424 – 426 | Combined sources | 3 | |
| Beta strandi | 428 – 432 | Combined sources | 5 | |
| Beta strandi | 435 – 439 | Combined sources | 5 | |
| Beta strandi | 444 – 446 | Combined sources | 3 | |
| Turni | 455 – 458 | Combined sources | 4 | |
| Beta strandi | 466 – 470 | Combined sources | 5 | |
| Beta strandi | 473 – 477 | Combined sources | 5 | |
| Beta strandi | 482 – 484 | Combined sources | 3 | |
| Turni | 493 – 496 | Combined sources | 4 | |
| Beta strandi | 504 – 507 | Combined sources | 4 | |
| Beta strandi | 512 – 515 | Combined sources | 4 | |
| Turni | 522 – 525 | Combined sources | 4 |
3D structure databases
| ProteinModelPortali | Q07008 |
| SMRi | Q07008 |
| ModBasei | Search... |
| MobiDBi | 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 29PROSITE-ProRule annotationAdd 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 | 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 |
Sequence similaritiesi
Belongs to the NOTCH family.Curated
Keywords - Domaini
ANK repeat, EGF-like domain, Repeat, Signal, Transmembrane, Transmembrane helixPhylogenomic databases
| eggNOGi | ENOG410IR7G Eukaryota COG0666 LUCA |
| GeneTreei | ENSGT00810000125346 |
| HOGENOMi | HOG000234369 |
| HOVERGENi | HBG052650 |
| InParanoidi | Q07008 |
| KOi | K02599 |
| OMAi | QYVNSYT |
| OrthoDBi | EOG091G01NU |
| TreeFami | TF351641 |
Family and domain databases
| CDDi | cd00204 ANK, 2 hits |
| 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 |
Sequencei
Sequence statusi: Complete.
Sequence processingi: The displayed sequence is further processed into a mature form.
Q07008-1 [UniParc]FASTAAdd to basket
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 |
| UniGenei | Rn.25046 |
Genome annotation databases
| Ensembli | ENSRNOT00000026212; ENSRNOP00000026212; ENSRNOG00000019322 |
| GeneIDi | 25496 |
| KEGGi | rno:25496 |
| UCSCi | RGD:3187 rat |
Similar proteinsi
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: | July 18, 2018 | |
| This is version 192 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, Complete proteome, Reference proteomeDocuments
- PDB cross-references
Index of Protein Data Bank (PDB) cross-references - SIMILARITY comments
Index of protein domains and families
