SubmitCancel

Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.

Q07008

- NOTC1_RAT

UniProt

Q07008 - NOTC1_RAT

(max 400 entries)x

Your basket is currently empty.

Select item(s) and click on "Add to basket" to create your own collection here
(400 entries max)

Protein

Neurogenic locus notch homolog protein 1

Gene
Notch1
Organism
Rattus norvegicus (Rat)
Status
Reviewed - Annotation score: 5 out of 5 - Experimental evidence at transcript 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.1 Publication

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Metal bindingi1457 – 14571Calcium; via carbonyl oxygen By similarity
Metal bindingi1460 – 14601Calcium By similarity
Metal bindingi1475 – 14751Calcium By similarity
Metal bindingi1478 – 14781Calcium By similarity
Sitei1654 – 16552Cleavage; by furin-like protease By similarity
Sitei1710 – 17112Cleavage; by ADAM17 By similarity

GO - Molecular functioni

  1. calcium ion binding Source: InterPro
  2. core promoter binding Source: UniProtKB
  3. enzyme binding Source: UniProtKB
  4. enzyme inhibitor activity Source: UniProtKB
  5. receptor activity Source: InterPro

GO - Biological processi

  1. angiogenesis Source: UniProtKB-KW
  2. astrocyte differentiation Source: RGD
  3. cell differentiation in spinal cord Source: RGD
  4. cellular response to vascular endothelial growth factor stimulus Source: UniProtKB
  5. cilium morphogenesis Source: UniProtKB
  6. negative regulation of catalytic activity Source: UniProtKB
  7. negative regulation of cell migration involved in sprouting angiogenesis Source: UniProtKB
  8. negative regulation of cell proliferation Source: UniProtKB
  9. negative regulation of endothelial cell chemotaxis Source: UniProtKB
  10. negative regulation of glial cell proliferation Source: UniProtKB
  11. negative regulation of myotube differentiation Source: UniProtKB
  12. negative regulation of neurogenesis Source: UniProtKB
  13. negative regulation of neuron differentiation Source: RGD
  14. negative regulation of oligodendrocyte differentiation Source: UniProtKB
  15. negative regulation of pro-B cell differentiation Source: UniProtKB
  16. negative regulation of transcription from RNA polymerase II promoter Source: UniProtKB
  17. Notch signaling involved in heart development Source: UniProtKB
  18. Notch signaling pathway Source: RGD
  19. oligodendrocyte differentiation Source: RGD
  20. organ regeneration Source: RGD
  21. positive regulation of astrocyte differentiation Source: UniProtKB
  22. positive regulation of BMP signaling pathway Source: UniProtKB
  23. positive regulation of endothelial cell differentiation Source: RGD
  24. positive regulation of glial cell differentiation Source: RGD
  25. positive regulation of JAK-STAT cascade Source: UniProtKB
  26. positive regulation of neuroblast proliferation Source: RGD
  27. positive regulation of transcription, DNA-templated Source: UniProtKB
  28. positive regulation of transcription from RNA polymerase II promoter Source: RGD
  29. positive regulation of transcription from RNA polymerase II promoter in response to hypoxia Source: UniProtKB
  30. positive regulation of transcription of Notch receptor target Source: RGD
  31. regulation of cardioblast proliferation Source: RGD
  32. regulation of cell proliferation Source: RGD
  33. response to corticosteroid Source: RGD
  34. response to lipopolysaccharide Source: RGD
  35. spermatogenesis Source: RGD
  36. tissue regeneration Source: RGD
  37. transcription, DNA-templated Source: UniProtKB-KW
  38. tube formation Source: UniProtKB
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_194345. Activated NOTCH1 Transmits Signal to the Nucleus.
REACT_198299. Constitutive Signaling by NOTCH1 HD Domain Mutants.
REACT_198304. Constitutive Signaling by NOTCH1 t(7;9)(NOTCH1:M1580_K2555) Translocation Mutant.
REACT_198659. NOTCH1 Intracellular Domain Regulates Transcription.
REACT_198750. Constitutive Signaling by NOTCH1 PEST Domain Mutants.
REACT_198752. Constitutive Signaling by NOTCH1 HD+PEST Domain Mutants.
REACT_198754. Loss of Function of FBXW7 in Cancer and NOTCH1 Signaling.
REACT_198789. Pre-NOTCH Processing in Golgi.
REACT_198791. Pre-NOTCH Processing in the Endoplasmic Reticulum.

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: 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 – 17231705Extracellular Reviewed predictionAdd
BLAST
Transmembranei1724 – 174623Helical; Reviewed predictionAdd
BLAST
Topological domaini1747 – 2531785Cytoplasmic Reviewed predictionAdd
BLAST

GO - Cellular componenti

  1. acrosomal vesicle Source: RGD
  2. cytoskeleton Source: UniProtKB
  3. Golgi apparatus Source: RGD
  4. integral component of membrane Source: UniProtKB-KW
  5. lamellipodium Source: UniProtKB
  6. nucleus Source: RGD
  7. plasma membrane Source: RGD
  8. 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 – 1818 Reviewed predictionAdd
BLAST
Chaini19 – 25312513Neurogenic locus notch homolog protein 1PRO_0000007680Add
BLAST
Chaini1711 – 2531821Notch 1 extracellular truncation By similarityPRO_0000007681Add
BLAST
Chaini1744 – 2531788Notch 1 intracellular domain By similarityPRO_0000007682Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Disulfide bondi24 ↔ 37 By similarity
Disulfide bondi31 ↔ 46 By similarity
Glycosylationi41 – 411N-linked (GlcNAc...) Reviewed prediction
Disulfide bondi48 ↔ 57 By similarity
Disulfide bondi63 ↔ 74 By similarity
Glycosylationi65 – 651O-linked (Glc...) By similarity
Disulfide bondi68 ↔ 87 By similarity
Glycosylationi73 – 731O-linked (Fuc...) By similarity
Disulfide bondi89 ↔ 98 By similarity
Disulfide bondi106 ↔ 117 By similarity
Disulfide bondi111 ↔ 127 By similarity
Glycosylationi116 – 1161O-linked (Fuc...) By similarity
Disulfide bondi129 ↔ 138 By similarity
Disulfide bondi144 ↔ 155 By similarity
Glycosylationi146 – 1461O-linked (Glc...) By similarity
Disulfide bondi149 ↔ 164 By similarity
Disulfide bondi166 ↔ 175 By similarity
Disulfide bondi182 ↔ 195 By similarity
Disulfide bondi189 ↔ 204 By similarity
Glycosylationi194 – 1941O-linked (Fuc...) By similarity
Disulfide bondi206 ↔ 215 By similarity
Disulfide bondi222 ↔ 233 By similarity
Disulfide bondi227 ↔ 243 By similarity
Glycosylationi232 – 2321O-linked (Fuc...); alternate By similarity
Glycosylationi232 – 2321O-linked (GalNAc...); alternate By similarity
Disulfide bondi245 ↔ 254 By similarity
Disulfide bondi261 ↔ 272 By similarity
Disulfide bondi266 ↔ 281 By similarity
Disulfide bondi283 ↔ 292 By similarity
Disulfide bondi299 ↔ 312 By similarity
Disulfide bondi306 ↔ 321 By similarity
Disulfide bondi323 ↔ 332 By similarity
Disulfide bondi339 ↔ 350 By similarity
Glycosylationi341 – 3411O-linked (Glc...) By similarity
Disulfide bondi344 ↔ 359 By similarity
Disulfide bondi361 ↔ 370 By similarity
Disulfide bondi376 ↔ 387 By similarity
Glycosylationi378 – 3781O-linked (Glc...) By similarity
Disulfide bondi381 ↔ 398 By similarity
Disulfide bondi400 ↔ 409 By similarity
Disulfide bondi416 ↔ 429 By similarity
Disulfide bondi423 ↔ 438 By similarity
Disulfide bondi440 ↔ 449 By similarity
Disulfide bondi456 ↔ 467 By similarity
Glycosylationi458 – 4581O-linked (Glc...) By similarity
Disulfide bondi461 ↔ 476 By similarity
Glycosylationi466 – 4661O-linked (Fuc...) By similarity
Disulfide bondi478 ↔ 487 By similarity
Disulfide bondi494 ↔ 505 By similarity
Glycosylationi496 – 4961O-linked (Glc...) By similarity
Disulfide bondi499 ↔ 514 By similarity
Disulfide bondi516 ↔ 525 By similarity
Disulfide bondi532 ↔ 543 By similarity
Glycosylationi534 – 5341O-linked (Glc...) By similarity
Disulfide bondi537 ↔ 552 By similarity
Disulfide bondi554 ↔ 563 By similarity
Disulfide bondi570 ↔ 580 By similarity
Disulfide bondi575 ↔ 589 By similarity
Disulfide bondi591 ↔ 600 By similarity
Disulfide bondi607 ↔ 618 By similarity
Glycosylationi609 – 6091O-linked (Glc...) By similarity
Disulfide bondi612 ↔ 627 By similarity
Disulfide bondi629 ↔ 638 By similarity
Disulfide bondi645 ↔ 655 By similarity
Glycosylationi647 – 6471O-linked (Glc...) By similarity
Disulfide bondi650 ↔ 664 By similarity
Disulfide bondi666 ↔ 675 By similarity
Disulfide bondi682 ↔ 693 By similarity
Disulfide bondi687 ↔ 702 By similarity
Disulfide bondi704 ↔ 713 By similarity
Disulfide bondi720 ↔ 730 By similarity
Glycosylationi722 – 7221O-linked (Glc...) By similarity
Disulfide bondi725 ↔ 739 By similarity
Disulfide bondi741 ↔ 750 By similarity
Disulfide bondi757 ↔ 768 By similarity
Glycosylationi759 – 7591O-linked (Glc...) By similarity
Disulfide bondi762 ↔ 777 By similarity
Glycosylationi767 – 7671O-linked (Fuc...) By similarity
Disulfide bondi779 ↔ 788 By similarity
Disulfide bondi795 ↔ 806 By similarity
Glycosylationi797 – 7971O-linked (Glc...) By similarity
Disulfide bondi800 ↔ 815 By similarity
Glycosylationi805 – 8051O-linked (Fuc...) By similarity
Disulfide bondi817 ↔ 826 By similarity
Disulfide bondi833 ↔ 844 By similarity
Disulfide bondi838 ↔ 855 By similarity
Disulfide bondi857 ↔ 866 By similarity
Disulfide bondi873 ↔ 884 By similarity
Disulfide bondi878 ↔ 893 By similarity
Glycosylationi888 – 8881N-linked (GlcNAc...) Reviewed prediction
Disulfide bondi895 ↔ 904 By similarity
Disulfide bondi911 ↔ 922 By similarity
Disulfide bondi916 ↔ 931 By similarity
Disulfide bondi933 ↔ 942 By similarity
Disulfide bondi949 ↔ 960 By similarity
Glycosylationi951 – 9511O-linked (Glc...) By similarity
Disulfide bondi954 ↔ 969 By similarity
Glycosylationi959 – 9591N-linked (GlcNAc...) Reviewed prediction
Disulfide bondi971 ↔ 980 By similarity
Disulfide bondi987 ↔ 998 By similarity
Disulfide bondi992 ↔ 1007 By similarity
Disulfide bondi1009 ↔ 1018 By similarity
Disulfide bondi1025 ↔ 1036 By similarity
Glycosylationi1027 – 10271O-linked (Glc...) By similarity
Disulfide bondi1030 ↔ 1045 By similarity
Glycosylationi1035 – 10351O-linked (Fuc...) By similarity
Disulfide bondi1047 ↔ 1056 By similarity
Disulfide bondi1063 ↔ 1074 By similarity
Glycosylationi1065 – 10651O-linked (Glc...) By similarity
Disulfide bondi1068 ↔ 1083 By similarity
Disulfide bondi1085 ↔ 1094 By similarity
Disulfide bondi1101 ↔ 1122 By similarity
Disulfide bondi1116 ↔ 1131 By similarity
Disulfide bondi1133 ↔ 1142 By similarity
Disulfide bondi1149 ↔ 1160 By similarity
Disulfide bondi1154 ↔ 1169 By similarity
Disulfide bondi1171 ↔ 1180 By similarity
Glycosylationi1179 – 11791N-linked (GlcNAc...) Reviewed prediction
Disulfide bondi1187 ↔ 1198 By similarity
Glycosylationi1189 – 11891O-linked (Glc...) By similarity
Disulfide bondi1192 ↔ 1207 By similarity
Glycosylationi1197 – 11971O-linked (Fuc...) By similarity
Disulfide bondi1209 ↔ 1218 By similarity
Disulfide bondi1225 ↔ 1244 By similarity
Disulfide bondi1238 ↔ 1253 By similarity
Glycosylationi1241 – 12411N-linked (GlcNAc...) Reviewed prediction
Disulfide bondi1255 ↔ 1264 By similarity
Disulfide bondi1271 ↔ 1284 By similarity
Glycosylationi1273 – 12731O-linked (Glc...) By similarity
Disulfide bondi1276 ↔ 1293 By similarity
Disulfide bondi1295 ↔ 1304 By similarity
Disulfide bondi1311 ↔ 1322 By similarity
Disulfide bondi1316 ↔ 1334 By similarity
Disulfide bondi1336 ↔ 1345 By similarity
Disulfide bondi1352 ↔ 1363 By similarity
Disulfide bondi1357 ↔ 1372 By similarity
Glycosylationi1362 – 13621O-linked (Fuc...) By similarity
Disulfide bondi1374 ↔ 1383 By similarity
Disulfide bondi1391 ↔ 1403 By similarity
Disulfide bondi1397 ↔ 1414 By similarity
Glycosylationi1402 – 14021O-linked (Fuc...); alternate By similarity
Glycosylationi1402 – 14021O-linked (GalNAc...); alternate By similarity
Disulfide bondi1416 ↔ 1425 By similarity
Disulfide bondi1449 ↔ 1472 By similarity
Disulfide bondi1454 ↔ 1467 By similarity
Disulfide bondi1463 ↔ 1479 By similarity
Glycosylationi1489 – 14891N-linked (GlcNAc...) Reviewed prediction
Disulfide bondi1490 ↔ 1514 By similarity
Disulfide bondi1496 ↔ 1509 By similarity
Disulfide bondi1505 ↔ 1521 By similarity
Disulfide bondi1536 ↔ 1549 By similarity
Disulfide bondi1545 ↔ 1561 By similarity
Glycosylationi1587 – 15871N-linked (GlcNAc...) Reviewed prediction
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 HIF1AN By similarity
Modified residuei2012 – 20121(3S)-3-hydroxyasparagine; by HIF1AN By 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.
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.
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.
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.

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.

Protein-protein interaction databases

STRINGi10116.ENSRNOP00000026212.

Structurei

3D structure databases

ProteinModelPortaliQ07008.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini20 – 5839EGF-like 1Add
BLAST
Domaini59 – 9941EGF-like 2Add
BLAST
Domaini102 – 13938EGF-like 3Add
BLAST
Domaini140 – 17637EGF-like 4Add
BLAST
Domaini178 – 21639EGF-like 5; calcium-binding Reviewed predictionAdd
BLAST
Domaini218 – 25538EGF-like 6Add
BLAST
Domaini257 – 29337EGF-like 7; calcium-binding Reviewed predictionAdd
BLAST
Domaini295 – 33339EGF-like 8; calcium-binding Reviewed predictionAdd
BLAST
Domaini335 – 37137EGF-like 9; calcium-binding Reviewed predictionAdd
BLAST
Domaini372 – 41039EGF-like 10Add
BLAST
Domaini412 – 45039EGF-like 11; calcium-binding Reviewed predictionAdd
BLAST
Domaini452 – 48837EGF-like 12; calcium-binding Reviewed predictionAdd
BLAST
Domaini490 – 52637EGF-like 13; calcium-binding Reviewed predictionAdd
BLAST
Domaini528 – 56437EGF-like 14; calcium-binding Reviewed predictionAdd
BLAST
Domaini566 – 60136EGF-like 15; calcium-binding Reviewed predictionAdd
BLAST
Domaini603 – 63937EGF-like 16; calcium-binding Reviewed predictionAdd
BLAST
Domaini641 – 67636EGF-like 17; calcium-binding Reviewed predictionAdd
BLAST
Domaini678 – 71437EGF-like 18; calcium-binding Reviewed predictionAdd
BLAST
Domaini716 – 75136EGF-like 19; calcium-binding Reviewed predictionAdd
BLAST
Domaini753 – 78937EGF-like 20; calcium-binding Reviewed predictionAdd
BLAST
Domaini791 – 82737EGF-like 21; calcium-binding Reviewed predictionAdd
BLAST
Domaini829 – 86739EGF-like 22Add
BLAST
Domaini869 – 90537EGF-like 23; calcium-binding Reviewed predictionAdd
BLAST
Domaini907 – 94337EGF-like 24Add
BLAST
Domaini945 – 98137EGF-like 25; calcium-binding Reviewed predictionAdd
BLAST
Domaini983 – 101937EGF-like 26Add
BLAST
Domaini1021 – 105737EGF-like 27; calcium-binding Reviewed predictionAdd
BLAST
Domaini1059 – 109537EGF-like 28Add
BLAST
Domaini1097 – 114347EGF-like 29Add
BLAST
Domaini1145 – 118137EGF-like 30; calcium-binding Reviewed predictionAdd
BLAST
Domaini1183 – 121937EGF-like 31; calcium-binding Reviewed predictionAdd
BLAST
Domaini1221 – 126545EGF-like 32; calcium-binding Reviewed predictionAdd
BLAST
Domaini1267 – 130539EGF-like 33Add
BLAST
Domaini1307 – 134640EGF-like 34Add
BLAST
Domaini1348 – 138437EGF-like 35Add
BLAST
Domaini1387 – 142640EGF-like 36Add
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-binding By similarity
Regioni2004 – 20129HIF1AN-binding By 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.
Contains 5 ANK repeats.
Contains 36 EGF-like domains.

Keywords - Domaini

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

Phylogenomic databases

eggNOGiCOG0666.
GeneTreeiENSGT00730000110611.
HOGENOMiHOG000234369.
HOVERGENiHBG052650.
InParanoidiQ07008.
KOiK02599.
OMAiGASCQNT.
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]
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

MPRLLAPLLC LTLLPALAAR GLRCSQPSGT CLNGGRCEVA NGTEACVCSG     50
AFVGQRCQDP SPCLSTPCKN AGTCYVVDHG GIVDYACSCP LGFSGPLCLT 100
PLANACLANP CRNGGTCDLL TLTEYKCRCP PGWSGKSCQQ ADPCASNPCA 150
NGGQCLPFES SYICGCPPGF HGPTCRQDVN ECSQNPGLCR HGGTCHNEIG 200
SYRCACRATH TGPHCELPYV PCSPSPCQNG GTCRPTGDTT HECACLPGFA 250
GQNCEENVDD CPGNNCKNGG ACVDGVNTYN CRCPPEWTGQ YCTEDVDECQ 300
LMPNACQNGG TCHNSHGGYN CVCVNGWTGE DCSENIDDCA SAACFQGATC 350
HDRVASFYCE CPHGRTGLLC HLNDACISNP CNEGSNCDTN PVNGKAICTC 400
PSGYTGPACS QDVDECALGA NPCEHAGKCL NTLGSFECQC LQGYTGPRCE 450
IDVNECISNP CQNDATCLDQ IGEFQCICMP GYEGVYCEIN TDECASSPCL 500
HNGRCVDKIN EFLCQCPKGF SGHLCQYDVD ECASTPCKNG AKCLDGPNTY 550
TCVCTEGYTG THCEVDIDEC DPDPCHYGLC KDGVATFTCL CQPGYTGHHC 600
ETNINECHSQ PCRHGGTCQD RDNYYLCLCL KGTTGPNCEI NLDDCASNPC 650
DSGTCLDKID GYECACEPGY TGSMCNVNID ECAGSPCHNG GTCEDGIAGF 700
TCRCPEGYHD PTCLSEVNEC NSNPCIHGAC RDGLNGYKCD CAPGWSGTNC 750
DINNNECESN PCVNGGTCKD MTSGYVCTCR EGFSGPNCQT NINECASNPC 800
LNQGTCIDDV AGYKCNCPLP YTGATCEVVL APCATSPCKN SGVCKESEDY 850
ESFSCVCPTG WQGQTCEIDI NECVKSPCRH GASCQNTNGS YRCLCQAGYT 900
GRNCESDIDD CRPNPCHNGG SCTDGVNAAF CDCLPGFQGA FCEEDINECA 950
SNPCQNGANC TDCVDSYTCT CPTGFNGIHC ENNTPDCTES SCFNGGTCVD 1000
GINSFTCLCP PGFTGSYCQY DVNECDSRPC LHGGTCQDSY GTYKCTCPQG 1050
YTGLNCQNLV RWCDSAPCKN GGKCWQTNTQ YHCECRSGWT GFNCDVLSVS 1100
CEVAAQKRGI DVTLLCQHGG LCVDEEDKHY CHCQAGYTGS YCEDEVDECS 1150
PNPCQNGATC TDYLGGFSCK CVAGYHGSNC SEEINECLSQ PCQNGGTCID 1200
LTNTYKCSCP RGTQGVHCEI NVDDCHPPLD PASRSPKCFN NGTCVDQVGG 1250
YTCTCPPGFV GERCEGDVNE CLSNPCDPRG TQNCVQRVND FHCECRAGHT 1300
GRRCESVING CRGKPCRNGG VCAVASNTAR GFICRCPAGF EGATCENDAR 1350
TCGSLRCLNG GTCISGPRSP TCLCLGSFTG PECQFPASSP CVGSNPCYNQ 1400
GTCEPTSESP FYRCLCPAKF NGLLCHILDY SFTGGAGRDI PPPQIEEACE 1450
LPECQEDAGN KVCNLQCNNH ACGWDGGDCS LNFNDPWKNC TQSLQCWKYF 1500
SDGHCDSQCN SAGCLFDGFD CQLTEGQCNP LYDQYCKDHF SDGHCDQGCN 1550
SAECEWDGLD CAEHVPERLA AGTLVLVVLL PPDQLRNNSF HFLRELSHVL 1600
HTNVVFKRDA QGQQMIFPYY GREEELRKHP IKRSAVGWAT TSLLPGTNGG 1650
RQRRELDPMD IHGSIVYLEI DNRQCVQSSS QCFQSATDVA AFLGALASLG 1700
SLNIPYKIEA VKSETVEPPL PSQLHLMYVA AAAFVLLFFV GCGVLLSRKR 1750
RRQHGQLWFP EGFKVSEASK KKRREPLGED SVGLKPLKNA SDGALMDDNQ 1800
NEWGDEDLET KKFRFEEPVV LPDLDDQTDH RQWTQQHLDA ADLRVSAMAP 1850
TPPQGEVDAD CMDVNVRGPD GFTPLMIASC SGGGLETGNS EEEEDAPAVI 1900
SDFIYQGASL HNQTDRTGET ALHLAARYSR SDAAKRLLEA SADANIQDNM 1950
GRTPLHAAVS ADAQGVFQIL LRNRATDLDA RMHDGTTPLI LAARLAVEGM 2000
LEDLINSHAD VNAVDDLGKS ALHWAAAVNN VDAAVVLLKN GANKDMQNNK 2050
EETPLFLAAR EGSYETAKVL LDHFANRDIT DHMDRLPRDI AQERMHHDIV 2100
RLLDEYNLVR SPQLHGTALG GTPTLSPTLC SPNGYLGNLK SATQGKKARK 2150
PSTKGLACSS KEAKDLKARR KKSQDGKGCL LDSSSMLSPV DSLESPHGYL 2200
SDVASPPLLP SPFQQSPSMP LSHLPGMPDT HLGISHLNVA AKPEMAALAG 2250
GSRLAFEPPP PRLSHLPVAS SASTVLSTNG TGAMNFTVGA PASLNGQCEW 2300
LPRLQNGMVP SQYNPLRPGV TPGTLSTQAA GLQHGMMGPI HSSLSTNTLS 2350
PIIYQGLPNT RLATQPHLVQ TQQVQPQNLQ IQPQNLQPPS QPHLSVSSAA 2400
NGHLGRSFLS GEPSQADVQP LGPSSLPVHT ILPQESQALP TSLPSSMVPP 2450
MTTTQFLTPP SQHSYSSSPV DNTPSHQLQV PEHPFLTPSP ESPDQWSSSS 2500
PHSNISDWSE GISSPPTSMP SQITHIPEAF K 2531
Length:2,531
Mass (Da):270,822
Last modified:October 16, 2013 - v3
Checksum:i3E61AE863AA237F2
GO

Sequence conflict

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti309 – 3091G → A in CAA40667. 1 Publication
Sequence conflicti334 – 3341E → D in CAA40667. 1 Publication
Sequence conflicti402 – 4021S → R in CAA40667. 1 Publication
Sequence conflicti577 – 5771Y → I in CAA40667. 1 Publication
Sequence conflicti951 – 9511S → T in CAA40667. 1 Publication
Sequence conflicti1339 – 13391G → R in CAA40667. 1 Publication
Sequence conflicti1435 – 14351G → A in CAA40667. 1 Publication
Sequence conflicti1595 – 15962EL → DV in CAA40667. 1 Publication
Sequence conflicti2501 – 25011P → R in CAA40667. 1 Publication

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
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:
EMBL
GenBank
DDBJ
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.

3D structure databases

ProteinModelPortali Q07008.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

STRINGi 10116.ENSRNOP00000026212.

Proteomic databases

PaxDbi Q07008.
PRIDEi Q07008.

Protocols and materials databases

Structural Biology Knowledgebase Search...

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 COG0666.
GeneTreei ENSGT00730000110611.
HOGENOMi HOG000234369.
HOVERGENi HBG052650.
InParanoidi Q07008.
KOi K02599.
OMAi GASCQNT.
OrthoDBi EOG7992RD.
TreeFami TF351641.

Enzyme and pathway databases

Reactomei REACT_194345. Activated NOTCH1 Transmits Signal to the Nucleus.
REACT_198299. Constitutive Signaling by NOTCH1 HD Domain Mutants.
REACT_198304. Constitutive Signaling by NOTCH1 t(7;9)(NOTCH1:M1580_K2555) Translocation Mutant.
REACT_198659. NOTCH1 Intracellular Domain Regulates Transcription.
REACT_198750. Constitutive Signaling by NOTCH1 PEST Domain Mutants.
REACT_198752. Constitutive Signaling by NOTCH1 HD+PEST Domain Mutants.
REACT_198754. Loss of Function of FBXW7 in Cancer and NOTCH1 Signaling.
REACT_198789. Pre-NOTCH Processing in Golgi.
REACT_198791. Pre-NOTCH Processing in the Endoplasmic Reticulum.

Miscellaneous databases

NextBioi 35582897.
PROi Q07008.

Gene expression databases

Genevestigatori Q07008.

Family and domain databases

Gene3Di 1.25.40.20. 1 hit.
InterProi IPR002110. 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 ]
Pfami PF00023. 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 ]
PIRSFi PIRSF002279. Notch. 1 hit.
PRINTSi PR01452. LNOTCHREPEAT.
PR01984. NOTCH1.
SMARTi SM00248. ANK. 6 hits.
SM00181. EGF. 11 hits.
SM00179. EGF_CA. 25 hits.
SM00004. NL. 3 hits.
[Graphical view ]
SUPFAMi SSF48403. SSF48403. 1 hit.
SSF57184. SSF57184. 5 hits.
SSF90193. SSF90193. 3 hits.
PROSITEi 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.
[Graphical view ]
ProtoNeti Search...

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: September 3, 2014
This is version 152 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

Complete proteome, Reference proteome

Documents

  1. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

Similar proteinsi