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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)DescriptionActionsGraphical viewLength
Metal bindingi432Calcium 1; via carbonyl oxygenBy similarity1
Metal bindingi435Calcium 1; via amide nitrogenBy similarity1
Metal bindingi452Calcium 2By similarity1
Metal bindingi453Calcium 2; via carbonyl oxygenBy similarity1
Metal bindingi455Calcium 2By similarity1
Metal bindingi469Calcium 2By similarity1
Metal bindingi470Calcium 2; via carbonyl oxygenBy similarity1
Metal bindingi490Calcium 3By similarity1
Metal bindingi491Calcium 3; via carbonyl oxygenBy similarity1
Metal bindingi493Calcium 3By similarity1
Metal bindingi507Calcium 3By similarity1
Metal bindingi508Calcium 3; via carbonyl oxygenBy similarity1
Metal bindingi1457Calcium 4; via carbonyl oxygen1
Metal bindingi1460Calcium 41
Metal bindingi1475Calcium 41
Metal bindingi1478Calcium 41

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

BioCyciZFISH:ENSG00000148400-MONOMER.
ReactomeiR-HSA-1912399. Pre-NOTCH Processing in the Endoplasmic Reticulum.
R-HSA-1912408. Pre-NOTCH Transcription and Translation.
R-HSA-1912420. Pre-NOTCH Processing in Golgi.
R-HSA-210744. Regulation of gene expression in late stage (branching morphogenesis) pancreatic bud precursor cells.
R-HSA-2122947. NOTCH1 Intracellular Domain Regulates Transcription.
R-HSA-2122948. Activated NOTCH1 Transmits Signal to the Nucleus.
R-HSA-2644606. Constitutive Signaling by NOTCH1 PEST Domain Mutants.
R-HSA-2644607. Loss of Function of FBXW7 in Cancer and NOTCH1 Signaling.
R-HSA-2660826. Constitutive Signaling by NOTCH1 t(7;9)(NOTCH1:M1580_K2555) Translocation Mutant.
R-HSA-2691232. Constitutive Signaling by NOTCH1 HD Domain Mutants.
R-HSA-2894862. Constitutive Signaling by NOTCH1 HD+PEST Domain Mutants.
R-HSA-350054. Notch-HLH transcription pathway.
R-HSA-5083630. Defective LFNG causes SCDO3.
SignaLinkiP46531.
SIGNORiP46531.

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
Proteomesi
  • UP000005640 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)DescriptionActionsGraphical viewLength
Topological domaini19 – 1735ExtracellularSequence analysisAdd BLAST1717
Transmembranei1736 – 1756HelicalSequence analysisAdd BLAST21
Topological domaini1757 – 2555CytoplasmicSequence analysisAdd BLAST799

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)DescriptionActionsGraphical viewLength
Natural variantiVAR_071960429C → R in AOS5. 1 PublicationCorresponds to variant rs587777736dbSNPEnsembl.1
Natural variantiVAR_0719611496C → Y in AOS5. 1 PublicationCorresponds to variant rs587781259dbSNPEnsembl.1
Natural variantiVAR_0719621989D → N in AOS5. 1 PublicationCorresponds to variant rs587777734dbSNPEnsembl.1

Keywords - Diseasei

Disease mutation

Organism-specific databases

DisGeNETi4851.
MalaCardsiNOTCH1.
MIMi109730. phenotype.
616028. phenotype.
OpenTargetsiENSG00000148400.
Orphaneti974. Adams-Oliver syndrome.
402075. Familial bicuspid aortic valve.
PharmGKBiPA31683.

Chemistry databases

ChEMBLiCHEMBL2146346.

Polymorphism and mutation databases

BioMutaiNOTCH1.
DMDMi206729936.

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Signal peptidei1 – 18Sequence analysisAdd BLAST18
ChainiPRO_000000767419 – 2555Neurogenic locus notch homolog protein 1Add BLAST2537
ChainiPRO_00000076751721 – 2555Notch 1 extracellular truncationBy similarityAdd BLAST835
ChainiPRO_00000076761754 – 2555Notch 1 intracellular domainBy similarityAdd BLAST802

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Disulfide bondi24 ↔ 37By similarity
Disulfide bondi31 ↔ 46By similarity
Glycosylationi41N-linked (GlcNAc...)Sequence analysis1
Disulfide bondi48 ↔ 57By similarity
Disulfide bondi63 ↔ 74By similarity
Glycosylationi65O-linked (Glc...)By similarity1
Disulfide bondi68 ↔ 87By similarity
Glycosylationi73O-linked (Fuc...)By similarity1
Disulfide bondi89 ↔ 98By similarity
Disulfide bondi106 ↔ 117By similarity
Disulfide bondi111 ↔ 127By similarity
Glycosylationi116O-linked (Fuc...)By similarity1
Disulfide bondi129 ↔ 138By similarity
Disulfide bondi144 ↔ 155By similarity
Glycosylationi146O-linked (Glc...)By similarity1
Disulfide bondi149 ↔ 164By similarity
Disulfide bondi166 ↔ 175By similarity
Disulfide bondi182 ↔ 195By similarity
Disulfide bondi189 ↔ 204By similarity
Glycosylationi194O-linked (Fuc...)By similarity1
Disulfide bondi206 ↔ 215By similarity
Disulfide bondi222 ↔ 233By similarity
Disulfide bondi227 ↔ 243By similarity
Glycosylationi232O-linked (Fuc...); alternate1 Publication1
Glycosylationi232O-linked (GalNAc...); alternate1 Publication1
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
Glycosylationi341O-linked (Glc...)By similarity1
Disulfide bondi344 ↔ 359By similarity
Disulfide bondi361 ↔ 370By similarity
Disulfide bondi376 ↔ 387By similarity
Glycosylationi378O-linked (Glc...)By similarity1
Disulfide bondi381 ↔ 398By similarity
Disulfide bondi400 ↔ 409By similarity
Disulfide bondi416 ↔ 429By similarity
Disulfide bondi423 ↔ 438By similarity
Glycosylationi435O-linked (Glc...)By similarity1
Disulfide bondi440 ↔ 449By similarity
Disulfide bondi456 ↔ 467By similarity
Glycosylationi458O-linked (Glc...)By similarity1
Disulfide bondi461 ↔ 476By similarity
Glycosylationi466O-linked (Fuc...)By similarity1
Disulfide bondi478 ↔ 487By similarity
Disulfide bondi494 ↔ 505By similarity
Glycosylationi496O-linked (Glc...)By similarity1
Disulfide bondi499 ↔ 514By similarity
Disulfide bondi516 ↔ 525By similarity
Disulfide bondi532 ↔ 543By similarity
Glycosylationi534O-linked (Glc...)By similarity1
Disulfide bondi537 ↔ 552By similarity
Disulfide bondi554 ↔ 563By similarity
Disulfide bondi570 ↔ 580By similarity
Disulfide bondi575 ↔ 589By similarity
Disulfide bondi591 ↔ 600By similarity
Disulfide bondi607 ↔ 618By similarity
Glycosylationi609O-linked (Glc...)By similarity1
Disulfide bondi612 ↔ 627By similarity
Disulfide bondi629 ↔ 638By similarity
Disulfide bondi645 ↔ 655By similarity
Glycosylationi647O-linked (Glc...)By similarity1
Disulfide bondi650 ↔ 664By similarity
Disulfide bondi666 ↔ 675By similarity
Disulfide bondi682 ↔ 693By similarity
Disulfide bondi687 ↔ 702By similarity
Disulfide bondi704 ↔ 713By similarity
Disulfide bondi720 ↔ 730By similarity
Glycosylationi722O-linked (Glc...)By similarity1
Disulfide bondi725 ↔ 739By similarity
Disulfide bondi741 ↔ 750By similarity
Disulfide bondi757 ↔ 768By similarity
Glycosylationi759O-linked (Glc...)By similarity1
Disulfide bondi762 ↔ 777By similarity
Glycosylationi767O-linked (Fuc...)By similarity1
Disulfide bondi779 ↔ 788By similarity
Disulfide bondi795 ↔ 806By similarity
Glycosylationi797O-linked (Glc...)By similarity1
Disulfide bondi800 ↔ 815By similarity
Glycosylationi805O-linked (Fuc...)By similarity1
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
Glycosylationi951O-linked (Glc...)By similarity1
Disulfide bondi954 ↔ 969By similarity
Glycosylationi959N-linked (GlcNAc...)Sequence analysis1
Disulfide bondi971 ↔ 980By similarity
Disulfide bondi987 ↔ 998By similarity
Disulfide bondi992 ↔ 1007By similarity
Disulfide bondi1009 ↔ 1018By similarity
Disulfide bondi1025 ↔ 1036By similarity
Glycosylationi1027O-linked (Glc...)By similarity1
Disulfide bondi1030 ↔ 1045By similarity
Glycosylationi1035O-linked (Fuc...)By similarity1
Disulfide bondi1047 ↔ 1056By similarity
Disulfide bondi1063 ↔ 1074By similarity
Glycosylationi1065O-linked (Glc...)By similarity1
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
Glycosylationi1179N-linked (GlcNAc...)Sequence analysis1
Disulfide bondi1187 ↔ 1198By similarity
Glycosylationi1189O-linked (Glc...)By similarity1
Disulfide bondi1192 ↔ 1207By similarity
Glycosylationi1197O-linked (Fuc...)By similarity1
Disulfide bondi1209 ↔ 1218By similarity
Disulfide bondi1225 ↔ 1244By similarity
Disulfide bondi1238 ↔ 1253By similarity
Glycosylationi1241N-linked (GlcNAc...)Sequence analysis1
Disulfide bondi1255 ↔ 1264By similarity
Disulfide bondi1271 ↔ 1284By similarity
Glycosylationi1273O-linked (Glc...)By similarity1
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
Glycosylationi1362O-linked (Fuc...)By similarity1
Disulfide bondi1374 ↔ 1383By similarity
Disulfide bondi1391 ↔ 1403By similarity
Disulfide bondi1397 ↔ 1414By similarity
Glycosylationi1402O-linked (Fuc...); alternate1 Publication1
Glycosylationi1402O-linked (GalNAc...); alternate1 Publication1
Disulfide bondi1416 ↔ 1425By similarity
Disulfide bondi1449 ↔ 14721 Publication
Disulfide bondi1454 ↔ 14671 Publication
Disulfide bondi1463 ↔ 14791 Publication
Glycosylationi1489N-linked (GlcNAc...)Sequence analysis1
Disulfide bondi1490 ↔ 1514By similarity
Disulfide bondi1496 ↔ 1509By similarity
Disulfide bondi1505 ↔ 1521By similarity
Disulfide bondi1536 ↔ 1549By similarity
Disulfide bondi1545 ↔ 1561By similarity
Glycosylationi1587N-linked (GlcNAc...)Sequence analysis1
Glycosylationi1725O-linked (GalNAc...)1 Publication1
Cross-linki1759Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)By similarity
Modified residuei1861PhosphothreonineBy similarity1
Modified residuei1955(3S)-3-hydroxyasparagine; by HIF1AN; partial1 Publication1
Modified residuei2022(3S)-3-hydroxyasparagine; by HIF1ANBy similarity1

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 (PubMed:24226769). Contains both O-linked fucose and O-linked glucose in the EGF-like domains 11, 12 and 13, which are interacting with the residues on DLL4 (By similarity). 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) (PubMed:24226769).By similarity1 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

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sitei1664 – 1665Cleavage; by furin-like proteaseBy similarity2
Sitei1710 – 1711Cleavage; by ADAM17By similarity2
Sitei1720 – 1721Cleavage; by ADAM172

Keywords - PTMi

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

Proteomic databases

EPDiP46531.
MaxQBiP46531.
PaxDbiP46531.
PeptideAtlasiP46531.
PRIDEiP46531.

PTM databases

iPTMnetiP46531.
PhosphoSitePlusiP46531.

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

BgeeiENSG00000148400.
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 (PubMed:11101851, PubMed:12370315). 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 (PubMed:10713164). 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 (PubMed:17573339). 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). Interacts (via the EGF-like repeat region) with NOV (via CTCK domain) (PubMed:12050162). Interacts (via EGF-like domains) with DLL4 (via N-terminal DSL and MNNL domains) (By similarity).By similarity6 Publications

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sitei469Interaction with DLL4By similarity1

Binary interactionsi

WithEntry#Exp.IntActNotes
LILRB2Q8N4238EBI-636374,EBI-2816428
NFKB1P198382EBI-636374,EBI-300010
PIN1Q135269EBI-636374,EBI-714158
RBPJQ063305EBI-636374,EBI-632552
SNW1Q135733EBI-636374,EBI-632715
XIAPP981704EBI-636374,EBI-517127

GO - Molecular functioni

Protein-protein interaction databases

BioGridi110913. 188 interactors.
DIPiDIP-29919N.
IntActiP46531. 25 interactors.
MINTiMINT-1417018.
STRINGi9606.ENSP00000277541.

Chemistry databases

BindingDBiP46531.

Structurei

Secondary structure

12555
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Helixi143 – 146Combined sources4
Beta strandi154 – 157Combined sources4
Beta strandi162 – 165Combined sources4
Beta strandi170 – 175Combined sources6
Helixi181 – 184Combined sources4
Turni190 – 192Combined sources3
Beta strandi194 – 198Combined sources5
Beta strandi201 – 205Combined sources5
Beta strandi210 – 212Combined sources3
Beta strandi232 – 235Combined sources4
Beta strandi237 – 239Combined sources3
Beta strandi241 – 244Combined sources4
Beta strandi249 – 254Combined sources6
Beta strandi271 – 274Combined sources4
Beta strandi279 – 282Combined sources4
Beta strandi289 – 292Combined sources4
Helixi415 – 417Combined sources3
Beta strandi418 – 420Combined sources3
Beta strandi422 – 424Combined sources3
Beta strandi428 – 432Combined sources5
Beta strandi435 – 439Combined sources5
Beta strandi444 – 446Combined sources3
Turni455 – 458Combined sources4
Beta strandi466 – 470Combined sources5
Beta strandi473 – 477Combined sources5
Beta strandi482 – 484Combined sources3
Turni493 – 496Combined sources4
Turni500 – 502Combined sources3
Beta strandi504 – 507Combined sources4
Beta strandi512 – 515Combined sources4
Beta strandi520 – 522Combined sources3
Helixi1448 – 1450Combined sources3
Helixi1452 – 1457Combined sources6
Beta strandi1460 – 1462Combined sources3
Helixi1465 – 1467Combined sources3
Helixi1470 – 1472Combined sources3
Helixi1473 – 1476Combined sources4
Turni1477 – 1482Combined sources6
Turni1486 – 1489Combined sources4
Helixi1492 – 1494Combined sources3
Helixi1496 – 1498Combined sources3
Turni1499 – 1501Combined sources3
Beta strandi1502 – 1504Combined sources3
Helixi1507 – 1509Combined sources3
Helixi1512 – 1519Combined sources8
Turni1530 – 1532Combined sources3
Helixi1533 – 1539Combined sources7
Beta strandi1542 – 1544Combined sources3
Helixi1547 – 1549Combined sources3
Helixi1552 – 1559Combined sources8
Beta strandi1563 – 1565Combined sources3
Beta strandi1571 – 1580Combined sources10
Helixi1582 – 1587Combined sources6
Helixi1589 – 1600Combined sources12
Beta strandi1602 – 1606Combined sources5
Beta strandi1616 – 1620Combined sources5
Beta strandi1672 – 1681Combined sources10
Helixi1685 – 1688Combined sources4
Helixi1696 – 1708Combined sources13
Beta strandi1714 – 1716Combined sources3
Beta strandi1718 – 1724Combined sources7
Helixi1884 – 1890Combined sources7
Helixi1909 – 1914Combined sources6
Turni1925 – 1927Combined sources3
Helixi1931 – 1937Combined sources7
Helixi1941 – 1949Combined sources9
Helixi1964 – 1970Combined sources7
Helixi1974 – 1982Combined sources9
Beta strandi1983 – 1985Combined sources3
Helixi1998 – 2005Combined sources8
Helixi2008 – 2016Combined sources9
Helixi2031 – 2037Combined sources7
Helixi2041 – 2049Combined sources9
Helixi2064 – 2071Combined sources8
Helixi2074 – 2082Combined sources9
Helixi2097 – 2103Combined sources7
Helixi2107 – 2115Combined sources9

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB 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[»]
5FM9X-ray2.92A140-294[»]
5FMAX-ray2.46A/B142-294[»]
ProteinModelPortaliP46531.
SMRiP46531.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP46531.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Domaini20 – 58EGF-like 1PROSITE-ProRule annotationAdd BLAST39
Domaini59 – 99EGF-like 2PROSITE-ProRule annotationAdd BLAST41
Domaini102 – 139EGF-like 3PROSITE-ProRule annotationAdd BLAST38
Domaini140 – 176EGF-like 4PROSITE-ProRule annotationAdd BLAST37
Domaini178 – 216EGF-like 5; calcium-bindingPROSITE-ProRule annotationAdd BLAST39
Domaini218 – 255EGF-like 6PROSITE-ProRule annotationAdd BLAST38
Domaini257 – 293EGF-like 7; calcium-bindingPROSITE-ProRule annotationAdd BLAST37
Domaini295 – 333EGF-like 8; calcium-bindingPROSITE-ProRule annotationAdd BLAST39
Domaini335 – 371EGF-like 9; calcium-bindingPROSITE-ProRule annotationAdd BLAST37
Domaini372 – 410EGF-like 10PROSITE-ProRule annotationAdd BLAST39
Domaini412 – 450EGF-like 11; calcium-bindingPROSITE-ProRule annotationAdd BLAST39
Domaini452 – 488EGF-like 12; calcium-bindingPROSITE-ProRule annotationAdd BLAST37
Domaini490 – 526EGF-like 13; calcium-bindingPROSITE-ProRule annotationAdd BLAST37
Domaini528 – 564EGF-like 14; calcium-bindingPROSITE-ProRule annotationAdd BLAST37
Domaini566 – 601EGF-like 15; calcium-bindingPROSITE-ProRule annotationAdd BLAST36
Domaini603 – 639EGF-like 16; calcium-bindingPROSITE-ProRule annotationAdd BLAST37
Domaini641 – 676EGF-like 17; calcium-bindingPROSITE-ProRule annotationAdd BLAST36
Domaini678 – 714EGF-like 18; calcium-bindingPROSITE-ProRule annotationAdd BLAST37
Domaini716 – 751EGF-like 19; calcium-bindingPROSITE-ProRule annotationAdd BLAST36
Domaini753 – 789EGF-like 20PROSITE-ProRule annotationAdd BLAST37
Domaini791 – 827EGF-like 21; calcium-bindingPROSITE-ProRule annotationAdd BLAST37
Domaini829 – 867EGF-like 22PROSITE-ProRule annotationAdd BLAST39
Domaini869 – 905EGF-like 23; calcium-bindingPROSITE-ProRule annotationAdd BLAST37
Domaini907 – 943EGF-like 24PROSITE-ProRule annotationAdd BLAST37
Domaini945 – 981EGF-like 25; calcium-bindingPROSITE-ProRule annotationAdd BLAST37
Domaini983 – 1019EGF-like 26PROSITE-ProRule annotationAdd BLAST37
Domaini1021 – 1057EGF-like 27PROSITE-ProRule annotationAdd BLAST37
Domaini1059 – 1095EGF-like 28PROSITE-ProRule annotationAdd BLAST37
Domaini1097 – 1143EGF-like 29PROSITE-ProRule annotationAdd BLAST47
Domaini1145 – 1181EGF-like 30PROSITE-ProRule annotationAdd BLAST37
Domaini1183 – 1219EGF-like 31; calcium-bindingPROSITE-ProRule annotationAdd BLAST37
Domaini1221 – 1265EGF-like 32; calcium-bindingPROSITE-ProRule annotationAdd BLAST45
Domaini1267 – 1305EGF-like 33PROSITE-ProRule annotationAdd BLAST39
Domaini1307 – 1346EGF-like 34PROSITE-ProRule annotationAdd BLAST40
Domaini1348 – 1384EGF-like 35PROSITE-ProRule annotationAdd BLAST37
Domaini1387 – 1426EGF-like 36PROSITE-ProRule annotationAdd BLAST40
Repeati1449 – 1489LNR 1Add BLAST41
Repeati1490 – 1531LNR 2Add BLAST42
Repeati1532 – 1571LNR 3Add BLAST40
Repeati1928 – 1960ANK 1Add BLAST33
Repeati1961 – 1994ANK 2Add BLAST34
Repeati1995 – 2027ANK 3Add BLAST33
Repeati2028 – 2060ANK 4Add BLAST33
Repeati2061 – 2094ANK 5Add BLAST34
Repeati2095 – 2122ANK 6Add BLAST28

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni420 – 421Interaction with DLL4By similarity2
Regioni448 – 452Interaction with DLL4By similarity5
Regioni1947 – 1955HIF1AN-bindingBy similarity9
Regioni2014 – 2022HIF1AN-bindingBy similarity9

Compositional bias

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Compositional biasi1575 – 1578Poly-Val4
Compositional biasi1661 – 1664Poly-Arg4
Compositional biasi1728 – 1731Poly-Pro4
Compositional biasi1740 – 1743Poly-Ala4
Compositional biasi1901 – 1904Poly-Glu4
Compositional biasi2259 – 2262Poly-Gly4
Compositional biasi2403 – 2406Poly-Gln4
Compositional biasi2410 – 2417Poly-Pro8
Compositional biasi2521 – 2524Poly-Ser4

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

eggNOGiENOG410IR7G. Eukaryota.
COG0666. LUCA.
GeneTreeiENSGT00810000125346.
HOGENOMiHOG000234369.
HOVERGENiHBG052650.
InParanoidiP46531.
KOiK02599.
OMAiILDYSFV.
OrthoDBiEOG091G01NU.
PhylomeDBiP46531.
TreeFamiTF351641.

Family and domain databases

Gene3Di1.25.40.20. 1 hit.
InterProiIPR002110. Ankyrin_rpt.
IPR020683. Ankyrin_rpt-contain_dom.
IPR024600. DUF3454_notch.
IPR001881. EGF-like_Ca-bd_dom.
IPR013032. EGF-like_CS.
IPR000742. EGF-like_dom.
IPR000152. EGF-type_Asp/Asn_hydroxyl_site.
IPR018097. EGF_Ca-bd_CS.
IPR009030. Growth_fac_rcpt_.
IPR008297. Notch.
IPR022362. Notch_1.
IPR000800. Notch_dom.
IPR010660. Notch_NOD_dom.
IPR011656. Notch_NODP_dom.
[Graphical view]
PfamiPF12796. Ank_2. 2 hits.
PF11936. DUF3454. 1 hit.
PF00008. EGF. 25 hits.
PF07645. EGF_CA. 4 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.
SM01334. DUF3454. 1 hit.
SM00181. EGF. 36 hits.
SM00179. EGF_CA. 33 hits.
SM00004. NL. 3 hits.
SM01338. NOD. 1 hit.
SM01339. NODP. 1 hit.
[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)DescriptionActionsGraphical viewLength
Sequence conflicti187G → R in AAG33848 (Ref. 1) Curated1
Sequence conflicti187G → R in AAA60614 (PubMed:1831692).Curated1
Sequence conflicti282R → P in AAG33848 (Ref. 1) Curated1
Sequence conflicti282R → P in AAA60614 (PubMed:1831692).Curated1
Sequence conflicti477I → M in AAG33848 (Ref. 1) Curated1
Sequence conflicti477I → M in AAA60614 (PubMed:1831692).Curated1
Sequence conflicti614 – 615HG → LR in AAG33848 (Ref. 1) Curated2
Sequence conflicti614 – 615HG → LR in AAA60614 (PubMed:1831692).Curated2
Sequence conflicti621R → P in AAG33848 (Ref. 1) Curated1
Sequence conflicti621R → P in AAA60614 (PubMed:1831692).Curated1
Sequence conflicti677I → S in AAG33848 (Ref. 1) Curated1
Sequence conflicti677I → S in AAA60614 (PubMed:1831692).Curated1
Sequence conflicti775Y → I in AAG33848 (Ref. 1) Curated1
Sequence conflicti775Y → I in AAA60614 (PubMed:1831692).Curated1
Sequence conflicti803Q → K in AAG33848 (Ref. 1) Curated1
Sequence conflicti803Q → K in AAA60614 (PubMed:1831692).Curated1
Sequence conflicti860 – 862GWQ → AGAK in AAG33848 (Ref. 1) Curated3
Sequence conflicti860 – 862GWQ → AGAK in AAA60614 (PubMed:1831692).Curated3
Sequence conflicti1021D → V in AAG33848 (Ref. 1) Curated1
Sequence conflicti1021D → V in AAA60614 (PubMed:1831692).Curated1
Sequence conflicti1028Q → R in AAG33848 (Ref. 1) Curated1
Sequence conflicti1028Q → R in AAA60614 (PubMed:1831692).Curated1
Sequence conflicti1032H → L in AAG33848 (Ref. 1) Curated1
Sequence conflicti1032H → L in AAA60614 (PubMed:1831692).Curated1
Sequence conflicti1040 – 1043CGSY → RGLH in AAG33848 (Ref. 1) Curated4
Sequence conflicti1040 – 1043CGSY → RGLH in AAA60614 (PubMed:1831692).Curated4

Natural variant

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Natural variantiVAR_034898300Q → R.Corresponds to variant rs11574885dbSNPEnsembl.1
Natural variantiVAR_071960429C → R in AOS5. 1 PublicationCorresponds to variant rs587777736dbSNPEnsembl.1
Natural variantiVAR_048990879R → W.Corresponds to variant rs11574895dbSNPEnsembl.1
Natural variantiVAR_0719611496C → Y in AOS5. 1 PublicationCorresponds to variant rs587781259dbSNPEnsembl.1
Natural variantiVAR_0466181671V → I.Corresponds to variant rs2229968dbSNPEnsembl.1
Natural variantiVAR_0719621989D → N in AOS5. 1 PublicationCorresponds to variant rs587777734dbSNPEnsembl.1

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_017617.4.
UniGeneiHs.495473.

Genome annotation databases

EnsembliENST00000277541; ENSP00000277541; ENSG00000148400.
GeneIDi4851.
KEGGihsa:4851.
UCSCiuc004chz.4. 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_017617.4.
UniGeneiHs.495473.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB 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[»]
5FM9X-ray2.92A140-294[»]
5FMAX-ray2.46A/B142-294[»]
ProteinModelPortaliP46531.
SMRiP46531.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi110913. 188 interactors.
DIPiDIP-29919N.
IntActiP46531. 25 interactors.
MINTiMINT-1417018.
STRINGi9606.ENSP00000277541.

Chemistry databases

BindingDBiP46531.
ChEMBLiCHEMBL2146346.

PTM databases

iPTMnetiP46531.
PhosphoSitePlusiP46531.

Polymorphism and mutation databases

BioMutaiNOTCH1.
DMDMi206729936.

Proteomic databases

EPDiP46531.
MaxQBiP46531.
PaxDbiP46531.
PeptideAtlasiP46531.
PRIDEiP46531.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000277541; ENSP00000277541; ENSG00000148400.
GeneIDi4851.
KEGGihsa:4851.
UCSCiuc004chz.4. human.

Organism-specific databases

CTDi4851.
DisGeNETi4851.
GeneCardsiNOTCH1.
H-InvDBHIX0008549.
HGNCiHGNC:7881. NOTCH1.
HPAiCAB008112.
CAB022466.
MalaCardsiNOTCH1.
MIMi109730. phenotype.
190198. gene.
616028. phenotype.
neXtProtiNX_P46531.
OpenTargetsiENSG00000148400.
Orphaneti974. Adams-Oliver syndrome.
402075. Familial bicuspid aortic valve.
PharmGKBiPA31683.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiENOG410IR7G. Eukaryota.
COG0666. LUCA.
GeneTreeiENSGT00810000125346.
HOGENOMiHOG000234369.
HOVERGENiHBG052650.
InParanoidiP46531.
KOiK02599.
OMAiILDYSFV.
OrthoDBiEOG091G01NU.
PhylomeDBiP46531.
TreeFamiTF351641.

Enzyme and pathway databases

BioCyciZFISH:ENSG00000148400-MONOMER.
ReactomeiR-HSA-1912399. Pre-NOTCH Processing in the Endoplasmic Reticulum.
R-HSA-1912408. Pre-NOTCH Transcription and Translation.
R-HSA-1912420. Pre-NOTCH Processing in Golgi.
R-HSA-210744. Regulation of gene expression in late stage (branching morphogenesis) pancreatic bud precursor cells.
R-HSA-2122947. NOTCH1 Intracellular Domain Regulates Transcription.
R-HSA-2122948. Activated NOTCH1 Transmits Signal to the Nucleus.
R-HSA-2644606. Constitutive Signaling by NOTCH1 PEST Domain Mutants.
R-HSA-2644607. Loss of Function of FBXW7 in Cancer and NOTCH1 Signaling.
R-HSA-2660826. Constitutive Signaling by NOTCH1 t(7;9)(NOTCH1:M1580_K2555) Translocation Mutant.
R-HSA-2691232. Constitutive Signaling by NOTCH1 HD Domain Mutants.
R-HSA-2894862. Constitutive Signaling by NOTCH1 HD+PEST Domain Mutants.
R-HSA-350054. Notch-HLH transcription pathway.
R-HSA-5083630. Defective LFNG causes SCDO3.
SignaLinkiP46531.
SIGNORiP46531.

Miscellaneous databases

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

Gene expression databases

BgeeiENSG00000148400.
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.
IPR001881. EGF-like_Ca-bd_dom.
IPR013032. EGF-like_CS.
IPR000742. EGF-like_dom.
IPR000152. EGF-type_Asp/Asn_hydroxyl_site.
IPR018097. EGF_Ca-bd_CS.
IPR009030. Growth_fac_rcpt_.
IPR008297. Notch.
IPR022362. Notch_1.
IPR000800. Notch_dom.
IPR010660. Notch_NOD_dom.
IPR011656. Notch_NODP_dom.
[Graphical view]
PfamiPF12796. Ank_2. 2 hits.
PF11936. DUF3454. 1 hit.
PF00008. EGF. 25 hits.
PF07645. EGF_CA. 4 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.
SM01334. DUF3454. 1 hit.
SM00181. EGF. 36 hits.
SM00179. EGF_CA. 33 hits.
SM00004. NL. 3 hits.
SM01338. NOD. 1 hit.
SM01339. NODP. 1 hit.
[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...

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: November 30, 2016
This is version 203 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

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 one 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.