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Protein

Neurogenic locus notch homolog protein 1

Gene

Notch1

Organism
Rattus norvegicus (Rat)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

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 similarity

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Metal bindingi1457 – 14571Calcium; via carbonyl oxygenPROSITE-ProRule annotation
Metal bindingi1460 – 14601CalciumPROSITE-ProRule annotation
Metal bindingi1475 – 14751CalciumPROSITE-ProRule annotation
Metal bindingi1478 – 14781CalciumPROSITE-ProRule annotation
Sitei1654 – 16552Cleavage; by furin-like proteaseBy similarity
Sitei1710 – 17112Cleavage; by ADAM17By similarity

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Activator, Developmental protein, Receptor

Keywords - Biological processi

Angiogenesis, Differentiation, Notch signaling pathway, Transcription, Transcription regulation

Keywords - Ligandi

Calcium, Metal-binding

Enzyme and pathway databases

ReactomeiREACT_274120. Activated NOTCH1 Transmits Signal to the Nucleus.
REACT_274139. NOTCH1 Intracellular Domain Regulates Transcription.
REACT_274348. Notch-HLH transcription pathway.
REACT_295597. Regulation of gene expression in late stage (branching morphogenesis) pancreatic bud precursor cells.
REACT_295660. Pre-NOTCH Processing in the Endoplasmic Reticulum.
REACT_296822. Pre-NOTCH Processing in Golgi.

Names & Taxonomyi

Protein namesi
Recommended name:
Neurogenic locus notch homolog protein 1
Short name:
Notch 1
Cleaved into the following 2 chains:
Gene namesi
Name:Notch1
OrganismiRattus norvegicus (Rat)
Taxonomic identifieri10116 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeRattus
ProteomesiUP000002494 Componenti: Chromosome 3

Organism-specific databases

RGDi3187. Notch1.

Subcellular locationi

Chain Notch 1 intracellular domain :
  • Nucleus By similarity

  • Note: Following proteolytical processing NICD is translocated to the nucleus.By similarity

Topology

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Topological domaini19 – 17231705ExtracellularSequence AnalysisAdd
BLAST
Transmembranei1724 – 174623HelicalSequence AnalysisAdd
BLAST
Topological domaini1747 – 2531785CytoplasmicSequence AnalysisAdd
BLAST

GO - Cellular componenti

  • acrosomal vesicle Source: RGD
  • cell surface Source: Ensembl
  • cytoskeleton Source: UniProtKB
  • Golgi apparatus Source: RGD
  • integral component of membrane Source: UniProtKB-KW
  • lamellipodium Source: UniProtKB
  • MAML1-RBP-Jkappa- ICN1 complex Source: Ensembl
  • nucleus Source: RGD
  • plasma membrane Source: RGD
  • receptor complex Source: Ensembl
  • ruffle Source: UniProtKB
Complete GO annotation...

Keywords - Cellular componenti

Cell membrane, Membrane, Nucleus

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Signal peptidei1 – 1818Sequence AnalysisAdd
BLAST
Chaini19 – 25312513Neurogenic locus notch homolog protein 1PRO_0000007680Add
BLAST
Chaini1711 – 2531821Notch 1 extracellular truncationBy similarityPRO_0000007681Add
BLAST
Chaini1744 – 2531788Notch 1 intracellular domainBy similarityPRO_0000007682Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Disulfide bondi24 ↔ 37By similarity
Disulfide bondi31 ↔ 46By similarity
Glycosylationi41 – 411N-linked (GlcNAc...)Sequence Analysis
Disulfide bondi48 ↔ 57By similarity
Disulfide bondi63 ↔ 74By similarity
Glycosylationi65 – 651O-linked (Glc...)By similarity
Disulfide bondi68 ↔ 87By similarity
Glycosylationi73 – 731O-linked (Fuc...)By similarity
Disulfide bondi89 ↔ 98By similarity
Disulfide bondi106 ↔ 117By similarity
Disulfide bondi111 ↔ 127By similarity
Glycosylationi116 – 1161O-linked (Fuc...)By similarity
Disulfide bondi129 ↔ 138By similarity
Disulfide bondi144 ↔ 155By similarity
Glycosylationi146 – 1461O-linked (Glc...)By similarity
Disulfide bondi149 ↔ 164By similarity
Disulfide bondi166 ↔ 175By similarity
Disulfide bondi182 ↔ 195By similarity
Disulfide bondi189 ↔ 204By similarity
Glycosylationi194 – 1941O-linked (Fuc...)By similarity
Disulfide bondi206 ↔ 215By similarity
Disulfide bondi222 ↔ 233By similarity
Disulfide bondi227 ↔ 243By similarity
Glycosylationi232 – 2321O-linked (Fuc...); alternateBy similarity
Glycosylationi232 – 2321O-linked (GalNAc...); alternateBy similarity
Disulfide bondi245 ↔ 254By similarity
Disulfide bondi261 ↔ 272By similarity
Disulfide bondi266 ↔ 281By similarity
Disulfide bondi283 ↔ 292By similarity
Disulfide bondi299 ↔ 312By similarity
Disulfide bondi306 ↔ 321By similarity
Disulfide bondi323 ↔ 332By similarity
Disulfide bondi339 ↔ 350By similarity
Glycosylationi341 – 3411O-linked (Glc...)By similarity
Disulfide bondi344 ↔ 359By similarity
Disulfide bondi361 ↔ 370By similarity
Disulfide bondi376 ↔ 387By similarity
Glycosylationi378 – 3781O-linked (Glc...)By similarity
Disulfide bondi381 ↔ 398By similarity
Disulfide bondi400 ↔ 409By similarity
Disulfide bondi416 ↔ 429By similarity
Disulfide bondi423 ↔ 438By similarity
Disulfide bondi440 ↔ 449By similarity
Disulfide bondi456 ↔ 467By similarity
Glycosylationi458 – 4581O-linked (Glc...)By similarity
Disulfide bondi461 ↔ 476By similarity
Glycosylationi466 – 4661O-linked (Fuc...)By similarity
Disulfide bondi478 ↔ 487By similarity
Disulfide bondi494 ↔ 505By similarity
Glycosylationi496 – 4961O-linked (Glc...)By similarity
Disulfide bondi499 ↔ 514By similarity
Disulfide bondi516 ↔ 525By similarity
Disulfide bondi532 ↔ 543By similarity
Glycosylationi534 – 5341O-linked (Glc...)By similarity
Disulfide bondi537 ↔ 552By similarity
Disulfide bondi554 ↔ 563By similarity
Disulfide bondi570 ↔ 580By similarity
Disulfide bondi575 ↔ 589By similarity
Disulfide bondi591 ↔ 600By similarity
Disulfide bondi607 ↔ 618By similarity
Glycosylationi609 – 6091O-linked (Glc...)By similarity
Disulfide bondi612 ↔ 627By similarity
Disulfide bondi629 ↔ 638By similarity
Disulfide bondi645 ↔ 655By similarity
Glycosylationi647 – 6471O-linked (Glc...)By similarity
Disulfide bondi650 ↔ 664By similarity
Disulfide bondi666 ↔ 675By similarity
Disulfide bondi682 ↔ 693By similarity
Disulfide bondi687 ↔ 702By similarity
Disulfide bondi704 ↔ 713By similarity
Disulfide bondi720 ↔ 730By similarity
Glycosylationi722 – 7221O-linked (Glc...)By similarity
Disulfide bondi725 ↔ 739By similarity
Disulfide bondi741 ↔ 750By similarity
Disulfide bondi757 ↔ 768By similarity
Glycosylationi759 – 7591O-linked (Glc...)By similarity
Disulfide bondi762 ↔ 777By similarity
Glycosylationi767 – 7671O-linked (Fuc...)By similarity
Disulfide bondi779 ↔ 788By similarity
Disulfide bondi795 ↔ 806By similarity
Glycosylationi797 – 7971O-linked (Glc...)By similarity
Disulfide bondi800 ↔ 815By similarity
Glycosylationi805 – 8051O-linked (Fuc...)By similarity
Disulfide bondi817 ↔ 826By similarity
Disulfide bondi833 ↔ 844By similarity
Disulfide bondi838 ↔ 855By similarity
Disulfide bondi857 ↔ 866By similarity
Disulfide bondi873 ↔ 884By similarity
Disulfide bondi878 ↔ 893By similarity
Glycosylationi888 – 8881N-linked (GlcNAc...)Sequence Analysis
Disulfide bondi895 ↔ 904By similarity
Disulfide bondi911 ↔ 922By similarity
Disulfide bondi916 ↔ 931By similarity
Disulfide bondi933 ↔ 942By similarity
Disulfide bondi949 ↔ 960By similarity
Glycosylationi951 – 9511O-linked (Glc...)By similarity
Disulfide bondi954 ↔ 969By similarity
Glycosylationi959 – 9591N-linked (GlcNAc...)Sequence Analysis
Disulfide bondi971 ↔ 980By similarity
Disulfide bondi987 ↔ 998By similarity
Disulfide bondi992 ↔ 1007By similarity
Disulfide bondi1009 ↔ 1018By similarity
Disulfide bondi1025 ↔ 1036By similarity
Glycosylationi1027 – 10271O-linked (Glc...)By similarity
Disulfide bondi1030 ↔ 1045By similarity
Glycosylationi1035 – 10351O-linked (Fuc...)By similarity
Disulfide bondi1047 ↔ 1056By similarity
Disulfide bondi1063 ↔ 1074By similarity
Glycosylationi1065 – 10651O-linked (Glc...)By similarity
Disulfide bondi1068 ↔ 1083By similarity
Disulfide bondi1085 ↔ 1094By similarity
Disulfide bondi1101 ↔ 1122By similarity
Disulfide bondi1116 ↔ 1131By similarity
Disulfide bondi1133 ↔ 1142By similarity
Disulfide bondi1149 ↔ 1160By similarity
Disulfide bondi1154 ↔ 1169By similarity
Disulfide bondi1171 ↔ 1180By similarity
Glycosylationi1179 – 11791N-linked (GlcNAc...)Sequence Analysis
Disulfide bondi1187 ↔ 1198By similarity
Glycosylationi1189 – 11891O-linked (Glc...)By similarity
Disulfide bondi1192 ↔ 1207By similarity
Glycosylationi1197 – 11971O-linked (Fuc...)By similarity
Disulfide bondi1209 ↔ 1218By similarity
Disulfide bondi1225 ↔ 1244By similarity
Disulfide bondi1238 ↔ 1253By similarity
Glycosylationi1241 – 12411N-linked (GlcNAc...)Sequence Analysis
Disulfide bondi1255 ↔ 1264By similarity
Disulfide bondi1271 ↔ 1284By similarity
Glycosylationi1273 – 12731O-linked (Glc...)By similarity
Disulfide bondi1276 ↔ 1293By similarity
Disulfide bondi1295 ↔ 1304By similarity
Disulfide bondi1311 ↔ 1322By similarity
Disulfide bondi1316 ↔ 1334By similarity
Disulfide bondi1336 ↔ 1345By similarity
Disulfide bondi1352 ↔ 1363By similarity
Disulfide bondi1357 ↔ 1372By similarity
Glycosylationi1362 – 13621O-linked (Fuc...)By similarity
Disulfide bondi1374 ↔ 1383By similarity
Disulfide bondi1391 ↔ 1403By similarity
Disulfide bondi1397 ↔ 1414By similarity
Glycosylationi1402 – 14021O-linked (Fuc...); alternateBy similarity
Glycosylationi1402 – 14021O-linked (GalNAc...); alternateBy similarity
Disulfide bondi1416 ↔ 1425By similarity
Disulfide bondi1449 ↔ 1472By similarity
Disulfide bondi1454 ↔ 1467By similarity
Disulfide bondi1463 ↔ 1479By similarity
Glycosylationi1489 – 14891N-linked (GlcNAc...)Sequence Analysis
Disulfide bondi1490 ↔ 1514By similarity
Disulfide bondi1496 ↔ 1509By similarity
Disulfide bondi1505 ↔ 1521By similarity
Disulfide bondi1536 ↔ 1549By similarity
Disulfide bondi1545 ↔ 1561By similarity
Glycosylationi1587 – 15871N-linked (GlcNAc...)Sequence Analysis
Glycosylationi1715 – 17151O-linked (GalNAc...)By similarity
Cross-linki1749 – 1749Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)By similarity
Modified residuei1945 – 19451(3S)-3-hydroxyasparagine; by HIF1ANBy similarity
Modified residuei2012 – 20121(3S)-3-hydroxyasparagine; by HIF1ANBy similarity

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).By similarity
Phosphorylated.By similarity
O-glycosylated on the EGF-like domains. Contains both O-linked fucose and O-linked glucose. 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) (By similarity).By similarity
Ubiquitinated; undergoes 'Lys-29'-linked polyubiquitination catalyzed by ITCH. 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).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

Keywords - PTMi

Disulfide bond, Glycoprotein, Hydroxylation, Isopeptide bond, Phosphoprotein, Ubl conjugation

Proteomic databases

PaxDbiQ07008.
PRIDEiQ07008.

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

GenevestigatoriQ07008.

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).By similarity

Protein-protein interaction databases

IntActiQ07008. 3 interactions.
STRINGi10116.ENSRNOP00000026212.

Structurei

Secondary structure

1
2531
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi415 – 4184Combined sources
Turni424 – 4263Combined sources
Beta strandi428 – 4325Combined sources
Beta strandi435 – 4395Combined sources
Beta strandi444 – 4463Combined sources
Turni455 – 4584Combined sources
Beta strandi466 – 4705Combined sources
Beta strandi473 – 4775Combined sources
Beta strandi482 – 4843Combined sources
Turni493 – 4964Combined sources
Beta strandi504 – 5074Combined sources
Beta strandi512 – 5154Combined sources
Turni522 – 5254Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
4XL1X-ray2.30A/D412-526[»]
4XLWX-ray3.39A/C/E/G412-526[»]
ProteinModelPortaliQ07008.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini20 – 5839EGF-like 1PROSITE-ProRule annotationAdd
BLAST
Domaini59 – 9941EGF-like 2PROSITE-ProRule annotationAdd
BLAST
Domaini102 – 13938EGF-like 3PROSITE-ProRule annotationAdd
BLAST
Domaini140 – 17637EGF-like 4PROSITE-ProRule annotationAdd
BLAST
Domaini178 – 21639EGF-like 5; calcium-bindingPROSITE-ProRule annotationAdd
BLAST
Domaini218 – 25538EGF-like 6PROSITE-ProRule annotationAdd
BLAST
Domaini257 – 29337EGF-like 7; calcium-bindingPROSITE-ProRule annotationAdd
BLAST
Domaini295 – 33339EGF-like 8; calcium-bindingPROSITE-ProRule annotationAdd
BLAST
Domaini335 – 37137EGF-like 9; calcium-bindingPROSITE-ProRule annotationAdd
BLAST
Domaini372 – 41039EGF-like 10PROSITE-ProRule annotationAdd
BLAST
Domaini412 – 45039EGF-like 11; calcium-bindingPROSITE-ProRule annotationAdd
BLAST
Domaini452 – 48837EGF-like 12; calcium-bindingPROSITE-ProRule annotationAdd
BLAST
Domaini490 – 52637EGF-like 13; calcium-bindingPROSITE-ProRule annotationAdd
BLAST
Domaini528 – 56437EGF-like 14; calcium-bindingPROSITE-ProRule annotationAdd
BLAST
Domaini566 – 60136EGF-like 15; calcium-bindingPROSITE-ProRule annotationAdd
BLAST
Domaini603 – 63937EGF-like 16; calcium-bindingPROSITE-ProRule annotationAdd
BLAST
Domaini641 – 67636EGF-like 17; calcium-bindingPROSITE-ProRule annotationAdd
BLAST
Domaini678 – 71437EGF-like 18; calcium-bindingPROSITE-ProRule annotationAdd
BLAST
Domaini716 – 75136EGF-like 19; calcium-bindingPROSITE-ProRule annotationAdd
BLAST
Domaini753 – 78937EGF-like 20; calcium-bindingPROSITE-ProRule annotationAdd
BLAST
Domaini791 – 82737EGF-like 21; calcium-bindingPROSITE-ProRule annotationAdd
BLAST
Domaini829 – 86739EGF-like 22PROSITE-ProRule annotationAdd
BLAST
Domaini869 – 90537EGF-like 23; calcium-bindingPROSITE-ProRule annotationAdd
BLAST
Domaini907 – 94337EGF-like 24PROSITE-ProRule annotationAdd
BLAST
Domaini945 – 98137EGF-like 25; calcium-bindingPROSITE-ProRule annotationAdd
BLAST
Domaini983 – 101937EGF-like 26PROSITE-ProRule annotationAdd
BLAST
Domaini1021 – 105737EGF-like 27; calcium-bindingPROSITE-ProRule annotationAdd
BLAST
Domaini1059 – 109537EGF-like 28PROSITE-ProRule annotationAdd
BLAST
Domaini1097 – 114347EGF-like 29PROSITE-ProRule annotationAdd
BLAST
Domaini1145 – 118137EGF-like 30; calcium-bindingPROSITE-ProRule annotationAdd
BLAST
Domaini1183 – 121937EGF-like 31; calcium-bindingPROSITE-ProRule annotationAdd
BLAST
Domaini1221 – 126545EGF-like 32; calcium-bindingPROSITE-ProRule annotationAdd
BLAST
Domaini1267 – 130539EGF-like 33PROSITE-ProRule annotationAdd
BLAST
Domaini1307 – 134640EGF-like 34PROSITE-ProRule annotationAdd
BLAST
Domaini1348 – 138437EGF-like 35PROSITE-ProRule annotationAdd
BLAST
Domaini1387 – 142640EGF-like 36PROSITE-ProRule annotationAdd
BLAST
Repeati1449 – 148941LNR 1Add
BLAST
Repeati1490 – 153142LNR 2Add
BLAST
Repeati1532 – 157140LNR 3Add
BLAST
Repeati1917 – 194630ANK 1Add
BLAST
Repeati1950 – 198031ANK 2Add
BLAST
Repeati1984 – 201330ANK 3Add
BLAST
Repeati2017 – 204630ANK 4Add
BLAST
Repeati2050 – 207930ANK 5Add
BLAST

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni1937 – 19459HIF1AN-bindingBy similarity
Regioni2004 – 20129HIF1AN-bindingBy similarity

Compositional bias

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Compositional biasi1730 – 17334Poly-Ala
Compositional biasi1891 – 18944Poly-Glu
Compositional biasi2258 – 22614Poly-Pro
Compositional biasi2497 – 25004Poly-Ser

Sequence similaritiesi

Belongs to the NOTCH family.Curated
Contains 5 ANK repeats.PROSITE-ProRule annotation
Contains 36 EGF-like domains.PROSITE-ProRule annotation
Contains 3 LNR (Lin/Notch) repeats.PROSITE-ProRule annotation

Keywords - Domaini

ANK repeat, EGF-like domain, Repeat, Signal, Transmembrane, Transmembrane helix

Phylogenomic databases

eggNOGiCOG0666.
GeneTreeiENSGT00760000118786.
HOGENOMiHOG000234369.
HOVERGENiHBG052650.
InParanoidiQ07008.
KOiK02599.
OMAiHGGYNCV.
OrthoDBiEOG7992RD.
TreeFamiTF351641.

Family and domain databases

Gene3Di1.25.40.20. 1 hit.
InterProiIPR002110. Ankyrin_rpt.
IPR020683. Ankyrin_rpt-contain_dom.
IPR024600. DUF3454_notch.
IPR000742. EG-like_dom.
IPR001881. EGF-like_Ca-bd_dom.
IPR013032. EGF-like_CS.
IPR000152. EGF-type_Asp/Asn_hydroxyl_site.
IPR018097. EGF_Ca-bd_CS.
IPR009030. Growth_fac_rcpt_N_dom.
IPR008297. Notch.
IPR022362. Notch_1.
IPR000800. Notch_dom.
IPR010660. Notch_NOD_dom.
IPR011656. Notch_NODP_dom.
[Graphical view]
PANTHERiPTHR24033:SF37. PTHR24033:SF37. 1 hit.
PfamiPF00023. Ank. 1 hit.
PF12796. Ank_2. 2 hits.
PF11936. DUF3454. 1 hit.
PF00008. EGF. 21 hits.
PF07645. EGF_CA. 5 hits.
PF12661. hEGF. 2 hits.
PF06816. NOD. 1 hit.
PF07684. NODP. 1 hit.
PF00066. Notch. 3 hits.
[Graphical view]
PIRSFiPIRSF002279. Notch. 1 hit.
PRINTSiPR01452. LNOTCHREPEAT.
PR01984. NOTCH1.
SMARTiSM00248. ANK. 6 hits.
SM00181. EGF. 11 hits.
SM00179. EGF_CA. 25 hits.
SM00004. NL. 3 hits.
[Graphical view]
SUPFAMiSSF48403. SSF48403. 1 hit.
SSF57184. SSF57184. 5 hits.
SSF90193. SSF90193. 3 hits.
PROSITEiPS50297. 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.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

Q07008-1 [UniParc]FASTAAdd to basket

« Hide

        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
Length:2,531
Mass (Da):270,822
Last modified:October 16, 2013 - v3
Checksum:i3E61AE863AA237F2
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti309 – 3091G → A in CAA40667 (PubMed:1764995).Curated
Sequence conflicti334 – 3341E → D in CAA40667 (PubMed:1764995).Curated
Sequence conflicti402 – 4021S → R in CAA40667 (PubMed:1764995).Curated
Sequence conflicti577 – 5771Y → I in CAA40667 (PubMed:1764995).Curated
Sequence conflicti951 – 9511S → T in CAA40667 (PubMed:1764995).Curated
Sequence conflicti1339 – 13391G → R in CAA40667 (PubMed:1764995).Curated
Sequence conflicti1435 – 14351G → A in CAA40667 (PubMed:1764995).Curated
Sequence conflicti1595 – 15962EL → DV in CAA40667 (PubMed:1764995).Curated
Sequence conflicti2501 – 25011P → R in CAA40667 (PubMed:1764995).Curated

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.
PIRiS18188.
RefSeqiNP_001099191.1. NM_001105721.1.
UniGeneiRn.25046.

Genome annotation databases

EnsembliENSRNOT00000026212; ENSRNOP00000026212; ENSRNOG00000019322.
GeneIDi25496.
KEGGirno:25496.
UCSCiRGD:3187. rat.

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.
PIRiS18188.
RefSeqiNP_001099191.1. NM_001105721.1.
UniGeneiRn.25046.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
4XL1X-ray2.30A/D412-526[»]
4XLWX-ray3.39A/C/E/G412-526[»]
ProteinModelPortaliQ07008.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

IntActiQ07008. 3 interactions.
STRINGi10116.ENSRNOP00000026212.

Proteomic databases

PaxDbiQ07008.
PRIDEiQ07008.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSRNOT00000026212; ENSRNOP00000026212; ENSRNOG00000019322.
GeneIDi25496.
KEGGirno:25496.
UCSCiRGD:3187. rat.

Organism-specific databases

CTDi4851.
RGDi3187. Notch1.

Phylogenomic databases

eggNOGiCOG0666.
GeneTreeiENSGT00760000118786.
HOGENOMiHOG000234369.
HOVERGENiHBG052650.
InParanoidiQ07008.
KOiK02599.
OMAiHGGYNCV.
OrthoDBiEOG7992RD.
TreeFamiTF351641.

Enzyme and pathway databases

ReactomeiREACT_274120. Activated NOTCH1 Transmits Signal to the Nucleus.
REACT_274139. NOTCH1 Intracellular Domain Regulates Transcription.
REACT_274348. Notch-HLH transcription pathway.
REACT_295597. Regulation of gene expression in late stage (branching morphogenesis) pancreatic bud precursor cells.
REACT_295660. Pre-NOTCH Processing in the Endoplasmic Reticulum.
REACT_296822. Pre-NOTCH Processing in Golgi.

Miscellaneous databases

NextBioi35582897.
PROiQ07008.

Gene expression databases

GenevestigatoriQ07008.

Family and domain databases

Gene3Di1.25.40.20. 1 hit.
InterProiIPR002110. Ankyrin_rpt.
IPR020683. Ankyrin_rpt-contain_dom.
IPR024600. DUF3454_notch.
IPR000742. EG-like_dom.
IPR001881. EGF-like_Ca-bd_dom.
IPR013032. EGF-like_CS.
IPR000152. EGF-type_Asp/Asn_hydroxyl_site.
IPR018097. EGF_Ca-bd_CS.
IPR009030. Growth_fac_rcpt_N_dom.
IPR008297. Notch.
IPR022362. Notch_1.
IPR000800. Notch_dom.
IPR010660. Notch_NOD_dom.
IPR011656. Notch_NODP_dom.
[Graphical view]
PANTHERiPTHR24033:SF37. PTHR24033:SF37. 1 hit.
PfamiPF00023. Ank. 1 hit.
PF12796. Ank_2. 2 hits.
PF11936. DUF3454. 1 hit.
PF00008. EGF. 21 hits.
PF07645. EGF_CA. 5 hits.
PF12661. hEGF. 2 hits.
PF06816. NOD. 1 hit.
PF07684. NODP. 1 hit.
PF00066. Notch. 3 hits.
[Graphical view]
PIRSFiPIRSF002279. Notch. 1 hit.
PRINTSiPR01452. LNOTCHREPEAT.
PR01984. NOTCH1.
SMARTiSM00248. ANK. 6 hits.
SM00181. EGF. 11 hits.
SM00179. EGF_CA. 25 hits.
SM00004. NL. 3 hits.
[Graphical view]
SUPFAMiSSF48403. SSF48403. 1 hit.
SSF57184. SSF57184. 5 hits.
SSF90193. SSF90193. 3 hits.
PROSITEiPS50297. 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.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "A homolog of Drosophila Notch expressed during mammalian development."
    Weinmaster G., Roberts V.J., Lemke G.
    Development 113:199-205(1991) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
    Tissue: Schwann cell.
  2. Weinmaster G.
    Submitted (APR-1998) to the EMBL/GenBank/DDBJ databases
    Cited for: SEQUENCE REVISION TO 1652-1653.
  3. "Genome sequence of the Brown Norway rat yields insights into mammalian evolution."
    Gibbs R.A., Weinstock G.M., Metzker M.L., Muzny D.M., Sodergren E.J., Scherer S., Scott G., Steffen D., Worley K.C., Burch P.E., Okwuonu G., Hines S., Lewis L., Deramo C., Delgado O., Dugan-Rocha S., Miner G., Morgan M.
    , Hawes A., Gill R., Holt R.A., Adams M.D., Amanatides P.G., Baden-Tillson H., Barnstead M., Chin S., Evans C.A., Ferriera S., Fosler C., Glodek A., Gu Z., Jennings D., Kraft C.L., Nguyen T., Pfannkoch C.M., Sitter C., Sutton G.G., Venter J.C., Woodage T., Smith D., Lee H.-M., Gustafson E., Cahill P., Kana A., Doucette-Stamm L., Weinstock K., Fechtel K., Weiss R.B., Dunn D.M., Green E.D., Blakesley R.W., Bouffard G.G., De Jong P.J., Osoegawa K., Zhu B., Marra M., Schein J., Bosdet I., Fjell C., Jones S., Krzywinski M., Mathewson C., Siddiqui A., Wye N., McPherson J., Zhao S., Fraser C.M., Shetty J., Shatsman S., Geer K., Chen Y., Abramzon S., Nierman W.C., Havlak P.H., Chen R., Durbin K.J., Egan A., Ren Y., Song X.-Z., Li B., Liu Y., Qin X., Cawley S., Cooney A.J., D'Souza L.M., Martin K., Wu J.Q., Gonzalez-Garay M.L., Jackson A.R., Kalafus K.J., McLeod M.P., Milosavljevic A., Virk D., Volkov A., Wheeler D.A., Zhang Z., Bailey J.A., Eichler E.E., Tuzun E., Birney E., Mongin E., Ureta-Vidal A., Woodwark C., Zdobnov E., Bork P., Suyama M., Torrents D., Alexandersson M., Trask B.J., Young J.M., Huang H., Wang H., Xing H., Daniels S., Gietzen D., Schmidt J., Stevens K., Vitt U., Wingrove J., Camara F., Mar Alba M., Abril J.F., Guigo R., Smit A., Dubchak I., Rubin E.M., Couronne O., Poliakov A., Huebner N., Ganten D., Goesele C., Hummel O., Kreitler T., Lee Y.-A., Monti J., Schulz H., Zimdahl H., Himmelbauer H., Lehrach H., Jacob H.J., Bromberg S., Gullings-Handley J., Jensen-Seaman M.I., Kwitek A.E., Lazar J., Pasko D., Tonellato P.J., Twigger S., Ponting C.P., Duarte J.M., Rice S., Goodstadt L., Beatson S.A., Emes R.D., Winter E.E., Webber C., Brandt P., Nyakatura G., Adetobi M., Chiaromonte F., Elnitski L., Eswara P., Hardison R.C., Hou M., Kolbe D., Makova K., Miller W., Nekrutenko A., Riemer C., Schwartz S., Taylor J., Yang S., Zhang Y., Lindpaintner K., Andrews T.D., Caccamo M., Clamp M., Clarke L., Curwen V., Durbin R.M., Eyras E., Searle S.M., Cooper G.M., Batzoglou S., Brudno M., Sidow A., Stone E.A., Payseur B.A., Bourque G., Lopez-Otin C., Puente X.S., Chakrabarti K., Chatterji S., Dewey C., Pachter L., Bray N., Yap V.B., Caspi A., Tesler G., Pevzner P.A., Haussler D., Roskin K.M., Baertsch R., Clawson H., Furey T.S., Hinrichs A.S., Karolchik D., Kent W.J., Rosenbloom K.R., Trumbower H., Weirauch M., Cooper D.N., Stenson P.D., Ma B., Brent M., Arumugam M., Shteynberg D., Copley R.R., Taylor M.S., Riethman H., Mudunuri U., Peterson J., Guyer M., Felsenfeld A., Old S., Mockrin S., Collins F.S.
    Nature 428:493-521(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: Brown Norway.
  4. Mural R.J., Adams M.D., Myers E.W., Smith H.O., Venter J.C.
    Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  5. "Notch1 and Notch3 instructively restrict bFGF-responsive multipotent neural progenitor cells to an astroglial fate."
    Tanigaki K., Nogaki F., Takahashi J., Tashiro K., Kurooka H., Honjo T.
    Neuron 29:45-55(2001) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION.
  6. "Notch2: a second mammalian Notch gene."
    Weinmaster G., Roberts V.J., Lemke G.
    Development 116:931-941(1992) [PubMed] [Europe PMC] [Abstract]
    Cited for: TISSUE SPECIFICITY.
  7. "Expression patterns of Notch1, Notch2, and Notch3 suggest multiple functional roles for the Notch-DSL signaling system during brain development."
    Irvin D.K., Zurcher S.D., Nguyen T., Weinmaster G., Kornblum H.I.
    J. Comp. Neurol. 436:167-181(2001) [PubMed] [Europe PMC] [Abstract]
    Cited for: TISSUE SPECIFICITY.

Entry informationi

Entry nameiNOTC1_RAT
AccessioniPrimary (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: May 27, 2015
This is version 161 of the entry and version 3 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

Documents

  1. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  2. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into Uniref entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.