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Protein

Neurogenic locus notch homolog protein 1

Gene

NOTCH1

Organism
Homo sapiens (Human)
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).1 Publication

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Metal bindingi1457 – 14571Calcium; via carbonyl oxygen
Metal bindingi1460 – 14601Calcium
Metal bindingi1475 – 14751Calcium
Metal bindingi1478 – 14781Calcium
Sitei1664 – 16652Cleavage; by furin-like proteaseBy similarity
Sitei1710 – 17112Cleavage; by ADAM17By similarity
Sitei1720 – 17212Cleavage; by ADAM17

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_118568. Pre-NOTCH Transcription and Translation.
REACT_118614. Activated NOTCH1 Transmits Signal to the Nucleus.
REACT_118722. Pre-NOTCH Processing in the Endoplasmic Reticulum.
REACT_118780. NOTCH1 Intracellular Domain Regulates Transcription.
REACT_118798. Pre-NOTCH Processing in Golgi.
REACT_13673. Regulation of gene expression in late stage (branching morphogenesis) pancreatic bud precursor cells.
REACT_14835. Notch-HLH transcription pathway.
REACT_160089. Constitutive Signaling by NOTCH1 HD Domain Mutants.
REACT_160106. Constitutive Signaling by NOTCH1 t(7;9)(NOTCH1:M1580_K2555) Translocation Mutant.
REACT_160243. Constitutive Signaling by NOTCH1 PEST Domain Mutants.
REACT_160254. Constitutive Signaling by NOTCH1 HD+PEST Domain Mutants.
REACT_160305. Loss of Function of FBXW7 in Cancer and NOTCH1 Signaling.
SignaLinkiP46531.

Names & Taxonomyi

Protein namesi
Recommended name:
Neurogenic locus notch homolog protein 1
Short name:
Notch 1
Short name:
hN1
Alternative name(s):
Translocation-associated notch protein TAN-1
Cleaved into the following 2 chains:
Gene namesi
Name:NOTCH1
Synonyms:TAN1
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640 Componenti: Chromosome 9

Organism-specific databases

HGNCiHGNC:7881. NOTCH1.

Subcellular locationi

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 – 17351717ExtracellularSequence AnalysisAdd
BLAST
Transmembranei1736 – 175621HelicalSequence AnalysisAdd
BLAST
Topological domaini1757 – 2555799CytoplasmicSequence AnalysisAdd
BLAST

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Cell membrane, Membrane, Nucleus

Pathology & Biotechi

Involvement in diseasei

Aortic valve disease 1 (AOVD1)1 Publication

The disease is caused by mutations affecting the gene represented in this entry.

Disease descriptionA common defect in the aortic valve in which two rather than three leaflets are present. It is often associated with aortic valve calcification, stenosis and insufficiency. In extreme cases, the blood flow may be so restricted that the left ventricle fails to grow, resulting in hypoplastic left heart syndrome.

See also OMIM:109730
Adams-Oliver syndrome 5 (AOS5)1 Publication

The disease is caused by mutations affecting the gene represented in this entry.

Disease descriptionA form of Adams-Oliver syndrome, a disorder characterized by the congenital absence of skin (aplasia cutis congenita) in combination with transverse limb defects. Aplasia cutis congenita can be located anywhere on the body, but in the vast majority of the cases, it is present on the posterior parietal region where it is often associated with an underlying defect of the parietal bones. Limb abnormalities are typically limb truncation defects affecting the distal phalanges or entire digits (true ectrodactyly). Only rarely, metatarsals/metacarpals or more proximal limb structures are also affected. Apart from transverse limb defects, syndactyly, most commonly of second and third toes, can also be observed. The clinical features are highly variable and can also include cardiovascular malformations, brain abnormalities and vascular defects such as cutis marmorata and dilated scalp veins.

See also OMIM:616028
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti429 – 4291C → R in AOS5. 1 Publication
VAR_071960
Natural varianti1496 – 14961C → Y in AOS5. 1 Publication
VAR_071961
Natural varianti1989 – 19891D → N in AOS5. 1 Publication
VAR_071962

Keywords - Diseasei

Disease mutation

Organism-specific databases

MIMi109730. phenotype.
616028. phenotype.
Orphaneti974. Adams-Oliver syndrome.
402075. Familial bicuspid aortic valve.
PharmGKBiPA31683.

Polymorphism and mutation databases

BioMutaiNOTCH1.
DMDMi206729936.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Signal peptidei1 – 1818Sequence AnalysisAdd
BLAST
Chaini19 – 25552537Neurogenic locus notch homolog protein 1PRO_0000007674Add
BLAST
Chaini1721 – 2555835Notch 1 extracellular truncationBy similarityPRO_0000007675Add
BLAST
Chaini1754 – 2555802Notch 1 intracellular domainBy similarityPRO_0000007676Add
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...); alternate1 Publication
Glycosylationi232 – 2321O-linked (GalNAc...); alternate1 Publication
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
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...); alternate1 Publication
Glycosylationi1402 – 14021O-linked (GalNAc...); alternate1 Publication
Disulfide bondi1416 ↔ 1425By similarity
Disulfide bondi1449 ↔ 14721 Publication
Disulfide bondi1454 ↔ 14671 Publication
Disulfide bondi1463 ↔ 14791 Publication
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
Glycosylationi1725 – 17251O-linked (GalNAc...)1 Publication
Cross-linki1759 – 1759Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)By similarity
Modified residuei1955 – 19551(3S)-3-hydroxyasparagine; by HIF1AN; partial1 Publication
Modified residuei2022 – 20221(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).1 Publication
Ubiquitinated; undergoes 'Lys-29'-linked polyubiquitination catalyzed by ITCH. Monoubiquitination at Lys-1759 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.2 Publications
Hydroxylated at Asn-1955 by HIF1AN. Hydroxylated at Asn-2022 by HIF1AN (By similarity). 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

MaxQBiP46531.
PaxDbiP46531.
PRIDEiP46531.

PTM databases

PhosphoSiteiP46531.

Expressioni

Tissue specificityi

In fetal tissues most abundant in spleen, brain stem and lung. Also present in most adult tissues where it is found mainly in lymphoid tissues.

Gene expression databases

BgeeiP46531.
CleanExiHS_NOTCH1.
GenevisibleiP46531. HS.

Organism-specific databases

HPAiCAB008112.
CAB022466.

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. Interacts with THBS4 (By similarity).By similarity

Binary interactionsi

WithEntry#Exp.IntActNotes
NFKB1P198382EBI-636374,EBI-300010
PIN1Q135269EBI-636374,EBI-714158
RBPJQ063303EBI-636374,EBI-632552
SNW1Q135733EBI-636374,EBI-632715
XIAPP981704EBI-636374,EBI-517127

Protein-protein interaction databases

BioGridi110913. 179 interactions.
DIPiDIP-29919N.
IntActiP46531. 21 interactions.
MINTiMINT-1417018.
STRINGi9606.ENSP00000277541.

Structurei

Secondary structure

1
2555
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi415 – 4173Combined sources
Beta strandi418 – 4203Combined sources
Beta strandi422 – 4243Combined 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
Turni500 – 5023Combined sources
Beta strandi504 – 5074Combined sources
Beta strandi512 – 5154Combined sources
Beta strandi520 – 5223Combined sources
Helixi1448 – 14503Combined sources
Helixi1452 – 14576Combined sources
Beta strandi1460 – 14623Combined sources
Helixi1465 – 14673Combined sources
Helixi1470 – 14723Combined sources
Helixi1473 – 14764Combined sources
Turni1477 – 14826Combined sources
Turni1486 – 14894Combined sources
Helixi1492 – 14943Combined sources
Helixi1496 – 14983Combined sources
Turni1499 – 15013Combined sources
Beta strandi1502 – 15043Combined sources
Helixi1507 – 15093Combined sources
Helixi1512 – 15198Combined sources
Turni1530 – 15323Combined sources
Helixi1533 – 15397Combined sources
Beta strandi1542 – 15443Combined sources
Helixi1547 – 15493Combined sources
Helixi1552 – 15598Combined sources
Beta strandi1563 – 15653Combined sources
Beta strandi1571 – 158010Combined sources
Helixi1582 – 15876Combined sources
Helixi1589 – 160012Combined sources
Beta strandi1602 – 16065Combined sources
Beta strandi1616 – 16205Combined sources
Beta strandi1672 – 168110Combined sources
Helixi1685 – 16884Combined sources
Helixi1696 – 170813Combined sources
Beta strandi1714 – 17163Combined sources
Beta strandi1718 – 17247Combined sources
Helixi1884 – 18907Combined sources
Helixi1909 – 19146Combined sources
Turni1925 – 19273Combined sources
Helixi1931 – 19377Combined sources
Helixi1941 – 19499Combined sources
Helixi1964 – 19707Combined sources
Helixi1974 – 19829Combined sources
Beta strandi1983 – 19853Combined sources
Helixi1998 – 20058Combined sources
Helixi2008 – 20169Combined sources
Helixi2031 – 20377Combined sources
Helixi2041 – 20499Combined sources
Helixi2064 – 20718Combined sources
Helixi2074 – 20829Combined sources
Helixi2097 – 21037Combined sources
Helixi2107 – 21159Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1PB5NMR-A1446-1480[»]
1TOZNMR-A411-526[»]
1YYHX-ray1.90A/B1872-2114[»]
2F8XX-ray3.25K1872-2126[»]
2F8YX-ray1.55A/B1905-2126[»]
2HE0X-ray1.90A/B1872-2114[»]
2VJ3X-ray2.60A411-526[»]
3ETOX-ray2.00A/B1446-1733[»]
3I08X-ray3.20A/C1446-1664[»]
B/D1665-1733[»]
3L95X-ray2.19X/Y1448-1728[»]
3NBNX-ray3.45B/E1872-2126[»]
3V79X-ray3.85K1872-2126[»]
R1759-1777[»]
4CUDX-ray1.85A411-526[»]
4CUEX-ray3.00A411-526[»]
4CUFX-ray2.29A411-526[»]
4D0EX-ray1.61A411-526[»]
4D0FX-ray2.80A411-526[»]
ProteinModelPortaliP46531.
SMRiP46531. Positions 411-526, 1448-1728, 1883-2122.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP46531.

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 20PROSITE-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 27PROSITE-ProRule annotationAdd
BLAST
Domaini1059 – 109537EGF-like 28PROSITE-ProRule annotationAdd
BLAST
Domaini1097 – 114347EGF-like 29PROSITE-ProRule annotationAdd
BLAST
Domaini1145 – 118137EGF-like 30PROSITE-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
Repeati1928 – 196033ANK 1Add
BLAST
Repeati1961 – 199434ANK 2Add
BLAST
Repeati1995 – 202733ANK 3Add
BLAST
Repeati2028 – 206033ANK 4Add
BLAST
Repeati2061 – 209434ANK 5Add
BLAST
Repeati2095 – 212228ANK 6Add
BLAST

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni1947 – 19559HIF1AN-bindingBy similarity
Regioni2014 – 20229HIF1AN-bindingBy similarity

Compositional bias

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Compositional biasi1575 – 15784Poly-Val
Compositional biasi1661 – 16644Poly-Arg
Compositional biasi1728 – 17314Poly-Pro
Compositional biasi1740 – 17434Poly-Ala
Compositional biasi1901 – 19044Poly-Glu
Compositional biasi2259 – 22624Poly-Gly
Compositional biasi2403 – 24064Poly-Gln
Compositional biasi2410 – 24178Poly-Pro
Compositional biasi2521 – 25244Poly-Ser

Sequence similaritiesi

Belongs to the NOTCH family.Curated
Contains 6 ANK repeats.PROSITE-ProRule annotation1 Publication
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.
InParanoidiP46531.
KOiK02599.
OMAiHGGYNCV.
OrthoDBiEOG7992RD.
PhylomeDBiP46531.
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. 1 hit.
PF11936. DUF3454. 1 hit.
PF00008. EGF. 23 hits.
PF07645. EGF_CA. 5 hits.
PF12661. hEGF. 1 hit.
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. 12 hits.
SM00179. EGF_CA. 24 hits.
SM00004. NL. 3 hits.
[Graphical view]
SUPFAMiSSF48403. SSF48403. 1 hit.
SSF57184. SSF57184. 6 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. 20 hits.
PS50258. LNR. 3 hits.
[Graphical view]

Sequencei

Sequence statusi: Complete.

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

P46531-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MPPLLAPLLC LALLPALAAR GPRCSQPGET CLNGGKCEAA NGTEACVCGG
60 70 80 90 100
AFVGPRCQDP NPCLSTPCKN AGTCHVVDRR GVADYACSCA LGFSGPLCLT
110 120 130 140 150
PLDNACLTNP CRNGGTCDLL TLTEYKCRCP PGWSGKSCQQ ADPCASNPCA
160 170 180 190 200
NGGQCLPFEA SYICHCPPSF HGPTCRQDVN ECGQKPGLCR HGGTCHNEVG
210 220 230 240 250
SYRCVCRATH TGPNCERPYV PCSPSPCQNG GTCRPTGDVT HECACLPGFT
260 270 280 290 300
GQNCEENIDD CPGNNCKNGG ACVDGVNTYN CRCPPEWTGQ YCTEDVDECQ
310 320 330 340 350
LMPNACQNGG TCHNTHGGYN CVCVNGWTGE DCSENIDDCA SAACFHGATC
360 370 380 390 400
HDRVASFYCE CPHGRTGLLC HLNDACISNP CNEGSNCDTN PVNGKAICTC
410 420 430 440 450
PSGYTGPACS QDVDECSLGA NPCEHAGKCI NTLGSFECQC LQGYTGPRCE
460 470 480 490 500
IDVNECVSNP CQNDATCLDQ IGEFQCICMP GYEGVHCEVN TDECASSPCL
510 520 530 540 550
HNGRCLDKIN EFQCECPTGF TGHLCQYDVD ECASTPCKNG AKCLDGPNTY
560 570 580 590 600
TCVCTEGYTG THCEVDIDEC DPDPCHYGSC KDGVATFTCL CRPGYTGHHC
610 620 630 640 650
ETNINECSSQ PCRHGGTCQD RDNAYLCFCL KGTTGPNCEI NLDDCASSPC
660 670 680 690 700
DSGTCLDKID GYECACEPGY TGSMCNINID ECAGNPCHNG GTCEDGINGF
710 720 730 740 750
TCRCPEGYHD PTCLSEVNEC NSNPCVHGAC RDSLNGYKCD CDPGWSGTNC
760 770 780 790 800
DINNNECESN PCVNGGTCKD MTSGYVCTCR EGFSGPNCQT NINECASNPC
810 820 830 840 850
LNQGTCIDDV AGYKCNCLLP YTGATCEVVL APCAPSPCRN GGECRQSEDY
860 870 880 890 900
ESFSCVCPTG WQGQTCEVDI NECVLSPCRH GASCQNTHGG YRCHCQAGYS
910 920 930 940 950
GRNCETDIDD CRPNPCHNGG SCTDGINTAF CDCLPGFRGT FCEEDINECA
960 970 980 990 1000
SDPCRNGANC TDCVDSYTCT CPAGFSGIHC ENNTPDCTES SCFNGGTCVD
1010 1020 1030 1040 1050
GINSFTCLCP PGFTGSYCQH DVNECDSQPC LHGGTCQDGC GSYRCTCPQG
1060 1070 1080 1090 1100
YTGPNCQNLV HWCDSSPCKN GGKCWQTHTQ YRCECPSGWT GLYCDVPSVS
1110 1120 1130 1140 1150
CEVAAQRQGV DVARLCQHGG LCVDAGNTHH CRCQAGYTGS YCEDLVDECS
1160 1170 1180 1190 1200
PSPCQNGATC TDYLGGYSCK CVAGYHGVNC SEEIDECLSH PCQNGGTCLD
1210 1220 1230 1240 1250
LPNTYKCSCP RGTQGVHCEI NVDDCNPPVD PVSRSPKCFN NGTCVDQVGG
1260 1270 1280 1290 1300
YSCTCPPGFV GERCEGDVNE CLSNPCDARG TQNCVQRVND FHCECRAGHT
1310 1320 1330 1340 1350
GRRCESVING CKGKPCKNGG TCAVASNTAR GFICKCPAGF EGATCENDAR
1360 1370 1380 1390 1400
TCGSLRCLNG GTCISGPRSP TCLCLGPFTG PECQFPASSP CLGGNPCYNQ
1410 1420 1430 1440 1450
GTCEPTSESP FYRCLCPAKF NGLLCHILDY SFGGGAGRDI PPPLIEEACE
1460 1470 1480 1490 1500
LPECQEDAGN KVCSLQCNNH ACGWDGGDCS LNFNDPWKNC TQSLQCWKYF
1510 1520 1530 1540 1550
SDGHCDSQCN SAGCLFDGFD CQRAEGQCNP LYDQYCKDHF SDGHCDQGCN
1560 1570 1580 1590 1600
SAECEWDGLD CAEHVPERLA AGTLVVVVLM PPEQLRNSSF HFLRELSRVL
1610 1620 1630 1640 1650
HTNVVFKRDA HGQQMIFPYY GREEELRKHP IKRAAEGWAA PDALLGQVKA
1660 1670 1680 1690 1700
SLLPGGSEGG RRRRELDPMD VRGSIVYLEI DNRQCVQASS QCFQSATDVA
1710 1720 1730 1740 1750
AFLGALASLG SLNIPYKIEA VQSETVEPPP PAQLHFMYVA AAAFVLLFFV
1760 1770 1780 1790 1800
GCGVLLSRKR RRQHGQLWFP EGFKVSEASK KKRREPLGED SVGLKPLKNA
1810 1820 1830 1840 1850
SDGALMDDNQ NEWGDEDLET KKFRFEEPVV LPDLDDQTDH RQWTQQHLDA
1860 1870 1880 1890 1900
ADLRMSAMAP TPPQGEVDAD CMDVNVRGPD GFTPLMIASC SGGGLETGNS
1910 1920 1930 1940 1950
EEEEDAPAVI SDFIYQGASL HNQTDRTGET ALHLAARYSR SDAAKRLLEA
1960 1970 1980 1990 2000
SADANIQDNM GRTPLHAAVS ADAQGVFQIL IRNRATDLDA RMHDGTTPLI
2010 2020 2030 2040 2050
LAARLAVEGM LEDLINSHAD VNAVDDLGKS ALHWAAAVNN VDAAVVLLKN
2060 2070 2080 2090 2100
GANKDMQNNR EETPLFLAAR EGSYETAKVL LDHFANRDIT DHMDRLPRDI
2110 2120 2130 2140 2150
AQERMHHDIV RLLDEYNLVR SPQLHGAPLG GTPTLSPPLC SPNGYLGSLK
2160 2170 2180 2190 2200
PGVQGKKVRK PSSKGLACGS KEAKDLKARR KKSQDGKGCL LDSSGMLSPV
2210 2220 2230 2240 2250
DSLESPHGYL SDVASPPLLP SPFQQSPSVP LNHLPGMPDT HLGIGHLNVA
2260 2270 2280 2290 2300
AKPEMAALGG GGRLAFETGP PRLSHLPVAS GTSTVLGSSS GGALNFTVGG
2310 2320 2330 2340 2350
STSLNGQCEW LSRLQSGMVP NQYNPLRGSV APGPLSTQAP SLQHGMVGPL
2360 2370 2380 2390 2400
HSSLAASALS QMMSYQGLPS TRLATQPHLV QTQQVQPQNL QMQQQNLQPA
2410 2420 2430 2440 2450
NIQQQQSLQP PPPPPQPHLG VSSAASGHLG RSFLSGEPSQ ADVQPLGPSS
2460 2470 2480 2490 2500
LAVHTILPQE SPALPTSLPS SLVPPVTAAQ FLTPPSQHSY SSPVDNTPSH
2510 2520 2530 2540 2550
QLQVPEHPFL TPSPESPDQW SSSSPHSNVS DWSEGVSSPP TSMQSQIARI

PEAFK
Length:2,555
Mass (Da):272,505
Last modified:September 23, 2008 - v4
Checksum:iE173C872D195F028
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti187 – 1871G → R in AAG33848 (Ref. 1) Curated
Sequence conflicti187 – 1871G → R in AAA60614 (PubMed:1831692).Curated
Sequence conflicti282 – 2821R → P in AAG33848 (Ref. 1) Curated
Sequence conflicti282 – 2821R → P in AAA60614 (PubMed:1831692).Curated
Sequence conflicti477 – 4771I → M in AAG33848 (Ref. 1) Curated
Sequence conflicti477 – 4771I → M in AAA60614 (PubMed:1831692).Curated
Sequence conflicti614 – 6152HG → LR in AAG33848 (Ref. 1) Curated
Sequence conflicti614 – 6152HG → LR in AAA60614 (PubMed:1831692).Curated
Sequence conflicti621 – 6211R → P in AAG33848 (Ref. 1) Curated
Sequence conflicti621 – 6211R → P in AAA60614 (PubMed:1831692).Curated
Sequence conflicti677 – 6771I → S in AAG33848 (Ref. 1) Curated
Sequence conflicti677 – 6771I → S in AAA60614 (PubMed:1831692).Curated
Sequence conflicti775 – 7751Y → I in AAG33848 (Ref. 1) Curated
Sequence conflicti775 – 7751Y → I in AAA60614 (PubMed:1831692).Curated
Sequence conflicti803 – 8031Q → K in AAG33848 (Ref. 1) Curated
Sequence conflicti803 – 8031Q → K in AAA60614 (PubMed:1831692).Curated
Sequence conflicti860 – 8623GWQ → AGAK in AAG33848 (Ref. 1) Curated
Sequence conflicti860 – 8623GWQ → AGAK in AAA60614 (PubMed:1831692).Curated
Sequence conflicti1021 – 10211D → V in AAG33848 (Ref. 1) Curated
Sequence conflicti1021 – 10211D → V in AAA60614 (PubMed:1831692).Curated
Sequence conflicti1028 – 10281Q → R in AAG33848 (Ref. 1) Curated
Sequence conflicti1028 – 10281Q → R in AAA60614 (PubMed:1831692).Curated
Sequence conflicti1032 – 10321H → L in AAG33848 (Ref. 1) Curated
Sequence conflicti1032 – 10321H → L in AAA60614 (PubMed:1831692).Curated
Sequence conflicti1040 – 10434CGSY → RGLH in AAG33848 (Ref. 1) Curated
Sequence conflicti1040 – 10434CGSY → RGLH in AAA60614 (PubMed:1831692).Curated

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti300 – 3001Q → R.
Corresponds to variant rs11574885 [ dbSNP | Ensembl ].
VAR_034898
Natural varianti429 – 4291C → R in AOS5. 1 Publication
VAR_071960
Natural varianti879 – 8791R → W.
Corresponds to variant rs11574895 [ dbSNP | Ensembl ].
VAR_048990
Natural varianti1496 – 14961C → Y in AOS5. 1 Publication
VAR_071961
Natural varianti1671 – 16711V → I.
Corresponds to variant rs2229968 [ dbSNP | Ensembl ].
VAR_046618
Natural varianti1989 – 19891D → N in AOS5. 1 Publication
VAR_071962

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF308602 mRNA. Translation: AAG33848.1.
AL592301, AL354671 Genomic DNA. Translation: CAI13934.1.
AL354671, AL592301 Genomic DNA. Translation: CAI16149.1.
M73980 mRNA. Translation: AAA60614.1.
AB209873 mRNA. Translation: BAD93110.1.
CCDSiCCDS43905.1.
PIRiA40043.
RefSeqiNP_060087.3. NM_017617.3.
UniGeneiHs.495473.

Genome annotation databases

EnsembliENST00000277541; ENSP00000277541; ENSG00000148400.
GeneIDi4851.
KEGGihsa:4851.
UCSCiuc004chz.3. human.

Keywords - Coding sequence diversityi

Polymorphism

Cross-referencesi

Web resourcesi

Atlas of Genetics and Cytogenetics in Oncology and Haematology

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF308602 mRNA. Translation: AAG33848.1.
AL592301, AL354671 Genomic DNA. Translation: CAI13934.1.
AL354671, AL592301 Genomic DNA. Translation: CAI16149.1.
M73980 mRNA. Translation: AAA60614.1.
AB209873 mRNA. Translation: BAD93110.1.
CCDSiCCDS43905.1.
PIRiA40043.
RefSeqiNP_060087.3. NM_017617.3.
UniGeneiHs.495473.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1PB5NMR-A1446-1480[»]
1TOZNMR-A411-526[»]
1YYHX-ray1.90A/B1872-2114[»]
2F8XX-ray3.25K1872-2126[»]
2F8YX-ray1.55A/B1905-2126[»]
2HE0X-ray1.90A/B1872-2114[»]
2VJ3X-ray2.60A411-526[»]
3ETOX-ray2.00A/B1446-1733[»]
3I08X-ray3.20A/C1446-1664[»]
B/D1665-1733[»]
3L95X-ray2.19X/Y1448-1728[»]
3NBNX-ray3.45B/E1872-2126[»]
3V79X-ray3.85K1872-2126[»]
R1759-1777[»]
4CUDX-ray1.85A411-526[»]
4CUEX-ray3.00A411-526[»]
4CUFX-ray2.29A411-526[»]
4D0EX-ray1.61A411-526[»]
4D0FX-ray2.80A411-526[»]
ProteinModelPortaliP46531.
SMRiP46531. Positions 411-526, 1448-1728, 1883-2122.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi110913. 179 interactions.
DIPiDIP-29919N.
IntActiP46531. 21 interactions.
MINTiMINT-1417018.
STRINGi9606.ENSP00000277541.

Chemistry

ChEMBLiCHEMBL2146346.

PTM databases

PhosphoSiteiP46531.

Polymorphism and mutation databases

BioMutaiNOTCH1.
DMDMi206729936.

Proteomic databases

MaxQBiP46531.
PaxDbiP46531.
PRIDEiP46531.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000277541; ENSP00000277541; ENSG00000148400.
GeneIDi4851.
KEGGihsa:4851.
UCSCiuc004chz.3. human.

Organism-specific databases

CTDi4851.
GeneCardsiGC09M139388.
H-InvDBHIX0008549.
HGNCiHGNC:7881. NOTCH1.
HPAiCAB008112.
CAB022466.
MIMi109730. phenotype.
190198. gene.
616028. phenotype.
neXtProtiNX_P46531.
Orphaneti974. Adams-Oliver syndrome.
402075. Familial bicuspid aortic valve.
PharmGKBiPA31683.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiCOG0666.
GeneTreeiENSGT00760000118786.
HOGENOMiHOG000234369.
HOVERGENiHBG052650.
InParanoidiP46531.
KOiK02599.
OMAiHGGYNCV.
OrthoDBiEOG7992RD.
PhylomeDBiP46531.
TreeFamiTF351641.

Enzyme and pathway databases

ReactomeiREACT_118568. Pre-NOTCH Transcription and Translation.
REACT_118614. Activated NOTCH1 Transmits Signal to the Nucleus.
REACT_118722. Pre-NOTCH Processing in the Endoplasmic Reticulum.
REACT_118780. NOTCH1 Intracellular Domain Regulates Transcription.
REACT_118798. Pre-NOTCH Processing in Golgi.
REACT_13673. Regulation of gene expression in late stage (branching morphogenesis) pancreatic bud precursor cells.
REACT_14835. Notch-HLH transcription pathway.
REACT_160089. Constitutive Signaling by NOTCH1 HD Domain Mutants.
REACT_160106. Constitutive Signaling by NOTCH1 t(7;9)(NOTCH1:M1580_K2555) Translocation Mutant.
REACT_160243. Constitutive Signaling by NOTCH1 PEST Domain Mutants.
REACT_160254. Constitutive Signaling by NOTCH1 HD+PEST Domain Mutants.
REACT_160305. Loss of Function of FBXW7 in Cancer and NOTCH1 Signaling.
SignaLinkiP46531.

Miscellaneous databases

ChiTaRSiNOTCH1. human.
EvolutionaryTraceiP46531.
GeneWikiiNotch-1.
GenomeRNAii4851.
NextBioi18684.
PROiP46531.
SOURCEiSearch...

Gene expression databases

BgeeiP46531.
CleanExiHS_NOTCH1.
GenevisibleiP46531. HS.

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. 1 hit.
PF11936. DUF3454. 1 hit.
PF00008. EGF. 23 hits.
PF07645. EGF_CA. 5 hits.
PF12661. hEGF. 1 hit.
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. 12 hits.
SM00179. EGF_CA. 24 hits.
SM00004. NL. 3 hits.
[Graphical view]
SUPFAMiSSF48403. SSF48403. 1 hit.
SSF57184. SSF57184. 6 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. 20 hits.
PS50258. LNR. 3 hits.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "Complete human notch 1 (hN1) cDNA sequence."
    Mann R.S., Blaumueller C.M., Zagouras P.
    Submitted (SEP-2000) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
    Tissue: Brain.
  2. "DNA sequence and analysis of human chromosome 9."
    Humphray S.J., Oliver K., Hunt A.R., Plumb R.W., Loveland J.E., Howe K.L., Andrews T.D., Searle S., Hunt S.E., Scott C.E., Jones M.C., Ainscough R., Almeida J.P., Ambrose K.D., Ashwell R.I.S., Babbage A.K., Babbage S., Bagguley C.L.
    , Bailey J., Banerjee R., Barker D.J., Barlow K.F., Bates K., Beasley H., Beasley O., Bird C.P., Bray-Allen S., Brown A.J., Brown J.Y., Burford D., Burrill W., Burton J., Carder C., Carter N.P., Chapman J.C., Chen Y., Clarke G., Clark S.Y., Clee C.M., Clegg S., Collier R.E., Corby N., Crosier M., Cummings A.T., Davies J., Dhami P., Dunn M., Dutta I., Dyer L.W., Earthrowl M.E., Faulkner L., Fleming C.J., Frankish A., Frankland J.A., French L., Fricker D.G., Garner P., Garnett J., Ghori J., Gilbert J.G.R., Glison C., Grafham D.V., Gribble S., Griffiths C., Griffiths-Jones S., Grocock R., Guy J., Hall R.E., Hammond S., Harley J.L., Harrison E.S.I., Hart E.A., Heath P.D., Henderson C.D., Hopkins B.L., Howard P.J., Howden P.J., Huckle E., Johnson C., Johnson D., Joy A.A., Kay M., Keenan S., Kershaw J.K., Kimberley A.M., King A., Knights A., Laird G.K., Langford C., Lawlor S., Leongamornlert D.A., Leversha M., Lloyd C., Lloyd D.M., Lovell J., Martin S., Mashreghi-Mohammadi M., Matthews L., McLaren S., McLay K.E., McMurray A., Milne S., Nickerson T., Nisbett J., Nordsiek G., Pearce A.V., Peck A.I., Porter K.M., Pandian R., Pelan S., Phillimore B., Povey S., Ramsey Y., Rand V., Scharfe M., Sehra H.K., Shownkeen R., Sims S.K., Skuce C.D., Smith M., Steward C.A., Swarbreck D., Sycamore N., Tester J., Thorpe A., Tracey A., Tromans A., Thomas D.W., Wall M., Wallis J.M., West A.P., Whitehead S.L., Willey D.L., Williams S.A., Wilming L., Wray P.W., Young L., Ashurst J.L., Coulson A., Blocker H., Durbin R.M., Sulston J.E., Hubbard T., Jackson M.J., Bentley D.R., Beck S., Rogers J., Dunham I.
    Nature 429:369-374(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  3. "TAN-1, the human homolog of the Drosophila notch gene, is broken by chromosomal translocations in T lymphoblastic neoplasms."
    Ellisen L.W., Bird J., West D.C., Soreng A.L., Reynolds T.C., Smith S.D., Sklar J.
    Cell 66:649-661(1991) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 1-2443.
  4. Totoki Y., Toyoda A., Takeda T., Sakaki Y., Tanaka A., Yokoyama S., Ohara O., Nagase T., Kikuno R.F.
    Submitted (MAR-2005) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 489-2555.
    Tissue: Aortic endothelium.
  5. Cited for: PROTEIN SEQUENCE OF 1947-1962, INTERACTION WITH HIF1AN, HYDROXYLATION AT ASN-1955, IDENTIFICATION BY MASS SPECTROMETRY.
  6. Cited for: IDENTIFICATION OF LIGANDS.
  7. Cited for: INTERACTION WITH DTX1.
  8. "SKIP, a CBF1-associated protein, interacts with the ankyrin repeat domain of NotchIC To facilitate NotchIC function."
    Zhou S., Fujimuro M., Hsieh J.J., Chen L., Miyamoto A., Weinmaster G., Hayward S.D.
    Mol. Cell. Biol. 20:2400-2410(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH SNW1.
  9. "MAML1, a human homologue of Drosophila mastermind, is a transcriptional co-activator for NOTCH receptors."
    Wu L., Aster J.C., Blacklow S.C., Lake R., Artavanis-Tsakonas S., Griffin J.D.
    Nat. Genet. 26:484-489(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH MAML1.
  10. "Identification of a family of mastermind-like transcriptional coactivators for mammalian notch receptors."
    Wu L., Sun T., Kobayashi K., Gao P., Griffin J.D.
    Mol. Cell. Biol. 22:7688-7700(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH MAML2 AND MAML3.
  11. "AIP4/Itch regulates Notch receptor degradation in the absence of ligand."
    Chastagner P., Israel A., Brou C.
    PLoS ONE 3:E2735-E2735(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: UBIQUITINATION BY ITCH.
  12. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  13. "Integrin cytoplasmic domain-associated protein-1 attenuates sprouting angiogenesis."
    Brutsch R., Liebler S.S., Wustehube J., Bartol A., Herberich S.E., Adam M.G., Telzerow A., Augustin H.G., Fischer A.
    Circ. Res. 107:592-601(2010) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION.
  14. "Notch1 binds and induces degradation of Snail in hepatocellular carcinoma."
    Lim S.O., Kim H.S., Quan X., Ahn S.M., Kim H., Hsieh D., Seong J.K., Jung G.
    BMC Biol. 9:83-83(2011) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH SNAI1 AND MDM2A.
  15. "The adaptor-associated kinase 1, AAK1, is a positive regulator of the Notch pathway."
    Gupta-Rossi N., Ortica S., Meas-Yedid V., Heuss S., Moretti J., Olivo-Marin J.C., Israel A.
    J. Biol. Chem. 286:18720-18730(2011) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH AAK1.
  16. "Serum- and glucocorticoid-inducible kinase 1 (SGK1) controls Notch1 signaling by downregulation of protein stability through Fbw7 ubiquitin ligase."
    Mo J.S., Ann E.J., Yoon J.H., Jung J., Choi Y.H., Kim H.Y., Ahn J.S., Kim S.M., Kim M.Y., Hong J.A., Seo M.S., Lang F., Choi E.J., Park H.S.
    J. Cell Sci. 124:100-112(2011) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH SGK1 AND FBXW7.
  17. Cited for: INTERACTION WITH SNW1.
  18. "The heterotaxy gene GALNT11 glycosylates Notch to orchestrate cilia type and laterality."
    Boskovski M.T., Yuan S., Pedersen N.B., Goth C.K., Makova S., Clausen H., Brueckner M., Khokha M.K.
    Nature 504:456-459(2013) [PubMed] [Europe PMC] [Abstract]
    Cited for: GLYCOSYLATION AT THR-232; THR-1402 AND THR-1725, PROTEOLYTIC PROCESSING.
  19. "Identifying tandem Ankyrin repeats in protein structures."
    Chakrabarty B., Parekh N.
    BMC Bioinformatics 15:6599-6599(2014) [PubMed] [Europe PMC] [Abstract]
    Cited for: ANKYRIN REPEATS.
  20. "Nuclear magnetic resonance structure of a prototype Lin12-Notch repeat module from human Notch1."
    Vardar D., North C.L., Sanchez-Irizarry C., Aster J.C., Blacklow S.C.
    Biochemistry 42:7061-7067(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: STRUCTURE BY NMR OF 1446-1480 IN COMPLEX WITH CALCIUM IONS, DISULFIDE BONDS.
  21. "Structural and functional properties of the human notch-1 ligand binding region."
    Hambleton S., Valeyev N.V., Muranyi A., Knott V., Werner J.M., McMichael A.J., Handford P.A., Downing A.K.
    Structure 12:2173-2183(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: STRUCTURE BY NMR OF 411-526.
  22. "High-resolution crystal structure of the human Notch 1 ankyrin domain."
    Ehebauer M.T., Chirgadze D.Y., Hayward P., Martinez Arias A., Blundell T.L.
    Biochem. J. 392:13-20(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (1.9 ANGSTROMS) OF 1872-2114.
  23. "Structural basis for cooperativity in recruitment of MAML coactivators to Notch transcription complexes."
    Nam Y., Sliz P., Song L., Aster J.C., Blacklow S.C.
    Cell 124:973-983(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (3.25 ANGSTROMS) OF 1872-2126 IN COMPLEX WITH RBPSUH AND MAML1.
  24. Cited for: INVOLVEMENT IN AOVD1.
  25. Cited for: INVOLVEMENT IN AOS5, VARIANTS AOS5 ARG-429; TYR-1496 AND ASN-1989.

Entry informationi

Entry nameiNOTC1_HUMAN
AccessioniPrimary (citable) accession number: P46531
Secondary accession number(s): Q59ED8, Q5SXM3
Entry historyi
Integrated into UniProtKB/Swiss-Prot: November 1, 1995
Last sequence update: September 23, 2008
Last modified: June 24, 2015
This is version 188 of the entry and version 4 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. Human chromosome 9
    Human chromosome 9: entries, gene names and cross-references to MIM
  2. Human entries with polymorphisms or disease mutations
    List of human entries with polymorphisms or disease mutations
  3. Human polymorphisms and disease mutations
    Index of human polymorphisms and disease mutations
  4. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  5. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  6. 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.