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Protein

Neurogenic locus notch homolog protein 3

Gene

NOTCH3

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 (By similarity).By similarity

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Activator, Developmental protein, Receptor

Keywords - Biological processi

Differentiation, Notch signaling pathway, Transcription, Transcription regulation

Enzyme and pathway databases

BioCyciZFISH:ENSG00000074181-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-1980148. Signaling by NOTCH3.
R-HSA-350054. Notch-HLH transcription pathway.
R-HSA-5083630. Defective LFNG causes SCDO3.
SignaLinkiQ9UM47.
SIGNORiQ9UM47.

Names & Taxonomyi

Protein namesi
Recommended name:
Neurogenic locus notch homolog protein 3
Short name:
Notch 3
Cleaved into the following 2 chains:
Gene namesi
Name:NOTCH3
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
Proteomesi
  • UP000005640 Componenti: Chromosome 19

Organism-specific databases

HGNCiHGNC:7883. NOTCH3.

Subcellular locationi

Notch 3 intracellular domain :
  • Nucleus

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

Topology

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Topological domaini40 – 1643ExtracellularSequence analysisAdd BLAST1604
Transmembranei1644 – 1664HelicalSequence analysisAdd BLAST21
Topological domaini1665 – 2321CytoplasmicSequence analysisAdd BLAST657

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Cell membrane, Membrane, Nucleus

Pathology & Biotechi

Involvement in diseasei

Cerebral arteriopathy, autosomal dominant, with subcortical infarcts and leukoencephalopathy, 1 (CADASIL1)21 Publications
The disease is caused by mutations affecting the gene represented in this entry.
Disease descriptionA cerebrovascular disease characterized by multiple subcortical infarcts, pseudobulbar palsy, dementia, and the presence of granular deposits in small cerebral arteries producing ischemic stroke.
See also OMIM:125310
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Natural variantiVAR_04423043C → G in CADASIL1. 2 Publications1
Natural variantiVAR_04423149C → F in CADASIL1. 2 PublicationsCorresponds to variant rs193921045dbSNPEnsembl.1
Natural variantiVAR_01287149C → Y in CADASIL1. 2 Publications1
Natural variantiVAR_04423254R → C in CADASIL1. 1 Publication1
Natural variantiVAR_04423360S → C in CADASIL1. 2 Publications1
Natural variantiVAR_04423465C → S in CADASIL1. 2 Publications1
Natural variantiVAR_04423567C → Y in CADASIL1. 1 Publication1
Natural variantiVAR_01287271W → C in CADASIL1. 1 PublicationCorresponds to variant rs28937321dbSNPEnsembl.1
Natural variantiVAR_04423676C → R in CADASIL1. 2 Publications1
Natural variantiVAR_04423776C → W in CADASIL1. 2 Publications1
Natural variantiVAR_04423877 – 82Missing in CADASIL1. 1 Publication6
Natural variantiVAR_04423980 – 84Missing in CADASIL1. 3 Publications5
Natural variantiVAR_04424087C → R in CADASIL1. 2 Publications1
Natural variantiVAR_04424187C → Y in CADASIL1. 1 Publication1
Natural variantiVAR_01287390R → C in CADASIL1. 8 Publications1
Natural variantiVAR_04424293C → F in CADASIL1. 3 Publications1
Natural variantiVAR_04424393C → Y in CADASIL1. 1 Publication1
Natural variantiVAR_044244106C → W in CADASIL1. 1 Publication1
Natural variantiVAR_044245108C → W in CADASIL1. 1 Publication1
Natural variantiVAR_044246108C → Y in CADASIL1. 2 Publications1
Natural variantiVAR_012874110R → C in CADASIL1. 7 Publications1
Natural variantiVAR_012875114 – 120Missing in CADASIL1. 2 Publications7
Natural variantiVAR_044247117C → F in CADASIL1. 4 PublicationsCorresponds to variant rs773539041dbSNPEnsembl.1
Natural variantiVAR_044248118S → C in CADASIL1. 1 Publication1
Natural variantiVAR_044249123C → F in CADASIL1. 3 Publications1
Natural variantiVAR_044250123C → Y in CADASIL1. 1 Publication1
Natural variantiVAR_044251128C → Y in CADASIL1. 1 Publication1
Natural variantiVAR_012876133R → C in CADASIL1. 10 PublicationsCorresponds to variant rs137852642dbSNPEnsembl.1
Natural variantiVAR_044252134C → W in CADASIL1. 4 Publications1
Natural variantiVAR_012877141R → C in CADASIL1. 9 Publications1
Natural variantiVAR_044253142F → C in CADASIL1. 1 Publication1
Natural variantiVAR_044254144C → F in CADASIL1. 1 Publication1
Natural variantiVAR_044255144C → S in CADASIL1. 3 Publications1
Natural variantiVAR_044256144C → Y in CADASIL1. 3 Publications1
Natural variantiVAR_044257145S → C in CADASIL1. 1 Publication1
Natural variantiVAR_012878146C → R in CADASIL1. 2 Publications1
Natural variantiVAR_044258149G → C in CADASIL1. 2 Publications1
Natural variantiVAR_044259150Y → C in CADASIL1. 3 Publications1
Natural variantiVAR_044260153 – 155Missing in CADASIL1. 2 Publications3
Natural variantiVAR_012879153R → C in CADASIL1. 8 Publications1
Natural variantiVAR_044261155C → S in CADASIL1. 1 Publication1
Natural variantiVAR_044262162C → S in CADASIL1. 1 Publication1
Natural variantiVAR_012880169R → C in CADASIL1. 8 PublicationsCorresponds to variant rs28933696dbSNPEnsembl.1
Natural variantiVAR_012882171G → C in CADASIL1. 1 Publication1
Natural variantiVAR_044263174C → F in CADASIL1. 1 Publication1
Natural variantiVAR_044264174C → R in CADASIL1. 3 Publications1
Natural variantiVAR_044265174C → Y in CADASIL1. 5 Publications1
Natural variantiVAR_044266180S → C in CADASIL1. 1 Publication1
Natural variantiVAR_012883182R → C in CADASIL1. 9 PublicationsCorresponds to variant rs28933697dbSNPEnsembl.1
Natural variantiVAR_044267183C → F in CADASIL1. 2 Publications1
Natural variantiVAR_044268183C → R in CADASIL1. 4 Publications1
Natural variantiVAR_044269183C → S in CADASIL1. 3 Publications1
Natural variantiVAR_044270185C → G in CADASIL1. 1 Publication1
Natural variantiVAR_012884185C → R in CADASIL1. 5 Publications1
Natural variantiVAR_044271189Y → C in CADASIL1. 1 Publication1
Natural variantiVAR_044272194C → F in CADASIL1. 3 Publications1
Natural variantiVAR_044273194C → R in CADASIL1. 1 Publication1
Natural variantiVAR_044274194C → S in CADASIL1. 1 Publication1
Natural variantiVAR_044275194C → Y in CADASIL1. 1 Publication1
Natural variantiVAR_044276201C → Y in CADASIL1. 1 Publication1
Natural variantiVAR_044277206C → Y in CADASIL1. 1 Publication1
Natural variantiVAR_044278207R → C in CADASIL1. 6 PublicationsCorresponds to variant rs775267348dbSNPEnsembl.1
Natural variantiVAR_012885212C → S in CADASIL1. 3 Publications1
Natural variantiVAR_044279213R → K in CADASIL1. 1 Publication1
Natural variantiVAR_012886222C → G in CADASIL1. 3 Publications1
Natural variantiVAR_044280222C → Y in CADASIL1. 1 Publication1
Natural variantiVAR_012887224C → Y in CADASIL1. 2 Publications1
Natural variantiVAR_044281233C → S in CADASIL1. 1 Publication1
Natural variantiVAR_044282233C → Y in CADASIL1. 2 Publications1
Natural variantiVAR_044283239 – 253Missing in CADASIL1. 2 PublicationsAdd BLAST15
Natural variantiVAR_044284240C → S in CADASIL1. 2 Publications1
Natural variantiVAR_044285245C → R in CADASIL1. 2 Publications1
Natural variantiVAR_044286251C → R in CADASIL1. 2 Publications1
Natural variantiVAR_012888258Y → C in CADASIL1. 2 Publications1
Natural variantiVAR_044287260C → Y in CADASIL1. 2 Publications1
Natural variantiVAR_044288319A → C in CADASIL1; requires 2 nucleotide substitutions. 1 Publication1
Natural variantiVAR_044289332R → C in CADASIL1. 4 PublicationsCorresponds to variant rs137852641dbSNPEnsembl.1
Natural variantiVAR_044290335S → C in CADASIL1. 2 Publications1
Natural variantiVAR_044291337Y → C in CADASIL1. 2 Publications1
Natural variantiVAR_044292379C → S in CADASIL1. 2 Publications1
Natural variantiVAR_044293395C → R in CADASIL1. 2 Publications1
Natural variantiVAR_044294420G → C in CADASIL1. 1 Publication1
Natural variantiVAR_044295421R → C in CADASIL1. 2 Publications1
Natural variantiVAR_044296428C → S in CADASIL1. 1 PublicationCorresponds to variant rs267606915dbSNPEnsembl.1
Natural variantiVAR_044297428C → Y in CADASIL1. 2 Publications1
Natural variantiVAR_044298440C → G in CADASIL1. 2 Publications1
Natural variantiVAR_044299440C → R in CADASIL1. 2 Publications1
Natural variantiVAR_044300446C → S in CADASIL1. 1 Publication1
Natural variantiVAR_044301449R → C in CADASIL1. 1 Publication1
Natural variantiVAR_044302455C → R in CADASIL1. 1 PublicationCorresponds to variant rs28933698dbSNPEnsembl.1
Natural variantiVAR_044303484C → F in CADASIL1. 1 Publication1
Natural variantiVAR_044304484C → Y in CADASIL1. 1 Publication1
Natural variantiVAR_044305495C → Y in CADASIL1. 2 Publications1
Natural variantiVAR_044306511C → R in CADASIL1. 2 Publications1
Natural variantiVAR_012890542C → Y in CADASIL1. 2 Publications1
Natural variantiVAR_044307544R → C in CADASIL1. 1 PublicationCorresponds to variant rs201118034dbSNPEnsembl.1
Natural variantiVAR_044308549C → Y in CADASIL1. 2 Publications1
Natural variantiVAR_012891558R → C in CADASIL1. 5 PublicationsCorresponds to variant rs75068032dbSNPEnsembl.1
Natural variantiVAR_012892578R → C in CADASIL1. 2 PublicationsCorresponds to variant rs769773673dbSNPEnsembl.1
Natural variantiVAR_044309607R → C in CADASIL1. 2 PublicationsCorresponds to variant rs777751303dbSNPEnsembl.1
Natural variantiVAR_072080710Y → C in CADASIL1; found in a compound heterozygote also carrying an intragenic frameshift deletion. 1 Publication1
Natural variantiVAR_012893728R → C in CADASIL1. 3 Publications1
Natural variantiVAR_044310775C → S in CADASIL1. 1 Publication1
Natural variantiVAR_044311953G → C in CADASIL1. 2 Publications1
Natural variantiVAR_044312984F → C in CADASIL1. 1 Publication1
Natural variantiVAR_012894985R → C in CADASIL1. 5 Publications1
Natural variantiVAR_0128951006R → C in CADASIL1. 2 Publications1
Natural variantiVAR_0443131015C → R in CADASIL1. 1 Publication1
Natural variantiVAR_0443151021Y → C in CADASIL1. 1 Publication1
Natural variantiVAR_0128961031R → C in CADASIL1. 2 Publications1
Natural variantiVAR_0443161063D → C in CADASIL1; requires 2 nucleotide substitutions. 1 Publication1
Natural variantiVAR_0128991231R → C in CADASIL1. 3 PublicationsCorresponds to variant rs201680145dbSNPEnsembl.1
Natural variantiVAR_0129001261C → R in CADASIL1. 2 Publications1
Natural variantiVAR_0443171261C → Y in CADASIL1. 2 Publications1
Myofibromatosis, infantile 2 (IMF2)1 Publication
The disease is caused by mutations affecting the gene represented in this entry.
Disease descriptionA rare mesenchymal disorder characterized by the development of benign tumors in the skin, striated muscles, bones, and, more rarely, visceral organs. Subcutaneous or soft tissue nodules commonly involve the skin of the head, neck, and trunk. Skeletal and muscular lesions occur in about half of the patients. Lesions may be solitary or multicentric, and they may be present at birth or become apparent in early infancy or occasionally in adult life. Visceral lesions are associated with high morbidity and mortality.
See also OMIM:615293
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Natural variantiVAR_0699271519L → P in IMF2. 1 PublicationCorresponds to variant rs367543285dbSNPEnsembl.1
Lateral meningocele syndrome (LMNS)1 Publication
The disease is caused by mutations affecting the gene represented in this entry.
Disease descriptionA very rare skeletal disorder with facial anomalies, hypotonia and neurologic dysfunction due to meningocele, a protrusion of the meninges, unaccompanied by neural tissue, through a bony defect in the skull or vertebral column. LMNS facial features include hypertelorism and telecanthus, high arched eyebrows, ptosis, mid-facial hypoplasia, micrognathia, high and narrow palate, low-set ears and a hypotonic appearance. Additional variable features are connective tissue abnormalities, aortic dilation, a high-pitched nasal voice, wormian bones and osteolysis.
See also OMIM:130720

Keywords - Diseasei

Disease mutation

Organism-specific databases

DisGeNETi4854.
MalaCardsiNOTCH3.
MIMi125310. phenotype.
130720. phenotype.
615293. phenotype.
OpenTargetsiENSG00000074181.
Orphaneti136. CADASIL.
2591. Infantile myofibromatosis.
PharmGKBiPA31685.

Chemistry databases

ChEMBLiCHEMBL3407319.
GuidetoPHARMACOLOGYi2860.

Polymorphism and mutation databases

BioMutaiNOTCH3.
DMDMi322510053.

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Signal peptidei1 – 39Sequence analysisAdd BLAST39
ChainiPRO_000000769240 – 2321Neurogenic locus notch homolog protein 3Add BLAST2282
ChainiPRO_00000076931629 – 2321Notch 3 extracellular truncationBy similarityAdd BLAST693
ChainiPRO_00000076941662 – 2321Notch 3 intracellular domainBy similarityAdd BLAST660

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Disulfide bondi43 ↔ 55By similarity
Disulfide bondi49 ↔ 65By similarity
Disulfide bondi67 ↔ 76By similarity
Disulfide bondi82 ↔ 93By similarity
Disulfide bondi87 ↔ 106By similarity
Disulfide bondi108 ↔ 117By similarity
Disulfide bondi123 ↔ 134By similarity
Disulfide bondi128 ↔ 144By similarity
Disulfide bondi146 ↔ 155By similarity
Disulfide bondi162 ↔ 174By similarity
Disulfide bondi168 ↔ 183By similarity
Disulfide bondi185 ↔ 194By similarity
Disulfide bondi201 ↔ 212By similarity
Disulfide bondi206 ↔ 222By similarity
Disulfide bondi224 ↔ 233By similarity
Disulfide bondi240 ↔ 251By similarity
Disulfide bondi245 ↔ 260By similarity
Disulfide bondi262 ↔ 271By similarity
Disulfide bondi278 ↔ 291By similarity
Disulfide bondi285 ↔ 300By similarity
Disulfide bondi302 ↔ 311By similarity
Disulfide bondi318 ↔ 329By similarity
Disulfide bondi323 ↔ 338By similarity
Disulfide bondi340 ↔ 349By similarity
Disulfide bondi355 ↔ 366By similarity
Disulfide bondi360 ↔ 377By similarity
Disulfide bondi379 ↔ 388By similarity
Disulfide bondi395 ↔ 408By similarity
Disulfide bondi402 ↔ 417By similarity
Disulfide bondi419 ↔ 428By similarity
Disulfide bondi435 ↔ 446By similarity
Disulfide bondi440 ↔ 455By similarity
Disulfide bondi457 ↔ 466By similarity
Disulfide bondi473 ↔ 484By similarity
Disulfide bondi478 ↔ 493By similarity
Disulfide bondi495 ↔ 504By similarity
Disulfide bondi511 ↔ 522By similarity
Disulfide bondi516 ↔ 531By similarity
Disulfide bondi533 ↔ 542By similarity
Disulfide bondi549 ↔ 559By similarity
Disulfide bondi554 ↔ 568By similarity
Disulfide bondi570 ↔ 579By similarity
Disulfide bondi586 ↔ 597By similarity
Disulfide bondi591 ↔ 606By similarity
Disulfide bondi608 ↔ 617By similarity
Disulfide bondi624 ↔ 634By similarity
Disulfide bondi629 ↔ 643By similarity
Disulfide bondi645 ↔ 654By similarity
Disulfide bondi661 ↔ 672By similarity
Disulfide bondi666 ↔ 681By similarity
Disulfide bondi683 ↔ 692By similarity
Disulfide bondi699 ↔ 709By similarity
Disulfide bondi704 ↔ 718By similarity
Disulfide bondi720 ↔ 729By similarity
Disulfide bondi738 ↔ 749By similarity
Disulfide bondi743 ↔ 758By similarity
Disulfide bondi760 ↔ 769By similarity
Disulfide bondi775 ↔ 786By similarity
Disulfide bondi780 ↔ 796By similarity
Disulfide bondi798 ↔ 807By similarity
Disulfide bondi814 ↔ 826By similarity
Disulfide bondi820 ↔ 835By similarity
Disulfide bondi837 ↔ 846By similarity
Disulfide bondi853 ↔ 864By similarity
Disulfide bondi858 ↔ 873By similarity
Disulfide bondi875 ↔ 884By similarity
Disulfide bondi891 ↔ 901By similarity
Disulfide bondi896 ↔ 910By similarity
Disulfide bondi912 ↔ 921By similarity
Disulfide bondi928 ↔ 939By similarity
Disulfide bondi933 ↔ 948By similarity
Disulfide bondi950 ↔ 959By similarity
Disulfide bondi966 ↔ 977By similarity
Disulfide bondi971 ↔ 986By similarity
Disulfide bondi988 ↔ 997By similarity
Disulfide bondi1004 ↔ 1015By similarity
Disulfide bondi1009 ↔ 1022By similarity
Disulfide bondi1024 ↔ 1033By similarity
Disulfide bondi1040 ↔ 1061By similarity
Disulfide bondi1055 ↔ 1070By similarity
Disulfide bondi1072 ↔ 1081By similarity
Disulfide bondi1088 ↔ 1099By similarity
Disulfide bondi1093 ↔ 1108By similarity
Disulfide bondi1110 ↔ 1119By similarity
Disulfide bondi1126 ↔ 1137By similarity
Disulfide bondi1131 ↔ 1146By similarity
Disulfide bondi1148 ↔ 1157By similarity
Disulfide bondi1164 ↔ 1182By similarity
Disulfide bondi1176 ↔ 1191By similarity
Glycosylationi1179N-linked (GlcNAc...)Sequence analysis1
Disulfide bondi1193 ↔ 1202By similarity
Disulfide bondi1209 ↔ 1222By similarity
Disulfide bondi1214 ↔ 1232By similarity
Disulfide bondi1234 ↔ 1243By similarity
Disulfide bondi1250 ↔ 1261By similarity
Disulfide bondi1255 ↔ 1275By similarity
Disulfide bondi1277 ↔ 1286By similarity
Disulfide bondi1293 ↔ 1304By similarity
Disulfide bondi1298 ↔ 1313By similarity
Disulfide bondi1315 ↔ 1324By similarity
Glycosylationi1336N-linked (GlcNAc...)Sequence analysis1
Disulfide bondi1339 ↔ 1350By similarity
Disulfide bondi1344 ↔ 1361By similarity
Disulfide bondi1363 ↔ 1372By similarity
Disulfide bondi1387 ↔ 1410By similarity
Disulfide bondi1392 ↔ 1405By similarity
Disulfide bondi1401 ↔ 1417By similarity
Disulfide bondi1428 ↔ 1451By similarity
Disulfide bondi1433 ↔ 1446By similarity
Glycosylationi1438N-linked (GlcNAc...)Sequence analysis1
Disulfide bondi1442 ↔ 1458By similarity
Disulfide bondi1467 ↔ 1493By similarity
Disulfide bondi1475 ↔ 1488By similarity
Disulfide bondi1484 ↔ 1500By similarity
Modified residuei2174Omega-N-methylarginineCombined sources1

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 TNF-alpha converting enzyme (TACE) to yield a membrane-associated intermediate fragment called notch extracellular truncation (NEXT). 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
Hydroxylated by HIF1AN.1 Publication

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sitei1571 – 1572Cleavage; by furin-like proteaseBy similarity2

Keywords - PTMi

Disulfide bond, Glycoprotein, Methylation, Phosphoprotein

Proteomic databases

EPDiQ9UM47.
MaxQBiQ9UM47.
PaxDbiQ9UM47.
PeptideAtlasiQ9UM47.
PRIDEiQ9UM47.

PTM databases

iPTMnetiQ9UM47.
PhosphoSitePlusiQ9UM47.

Expressioni

Tissue specificityi

Ubiquitously expressed in fetal and adult tissues.

Gene expression databases

BgeeiENSG00000074181.
CleanExiHS_NOTCH3.
ExpressionAtlasiQ9UM47. baseline and differential.
GenevisibleiQ9UM47. HS.

Organism-specific databases

HPAiCAB005393.
HPA044392.

Interactioni

Subunit structurei

Heterodimer of a C-terminal fragment N(TM) and a N-terminal fragment N(EC) which are probably linked by disulfide bonds (By similarity). Interacts with MAML1, MAML2 and MAML3 which act as transcriptional coactivators for NOTCH3. Interacts with PSMA1. Interacts with HIF1AN.By similarity4 Publications

Binary interactionsi

WithEntry#Exp.IntActNotes
Psma1Q9R1P42EBI-1236377,EBI-991653From a different organism.

GO - Molecular functioni

  • cadherin binding involved in cell-cell adhesion Source: BHF-UCL

Protein-protein interaction databases

BioGridi110916. 60 interactors.
DIPiDIP-39827N.
IntActiQ9UM47. 17 interactors.
MINTiMINT-2822317.
STRINGi9606.ENSP00000263388.

Chemistry databases

BindingDBiQ9UM47.

Structurei

Secondary structure

12321
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Beta strandi1389 – 1391Combined sources3
Helixi1393 – 1395Combined sources3
Beta strandi1398 – 1400Combined sources3
Helixi1403 – 1405Combined sources3
Turni1408 – 1410Combined sources3
Helixi1411 – 1414Combined sources4
Turni1415 – 1420Combined sources6
Turni1424 – 1427Combined sources4
Turni1431 – 1433Combined sources3
Helixi1434 – 1437Combined sources4
Beta strandi1439 – 1441Combined sources3
Helixi1444 – 1446Combined sources3
Turni1449 – 1451Combined sources3
Helixi1452 – 1456Combined sources5
Turni1457 – 1459Combined sources3
Helixi1463 – 1465Combined sources3
Helixi1469 – 1471Combined sources3
Helixi1472 – 1478Combined sources7
Beta strandi1481 – 1483Combined sources3
Helixi1486 – 1488Combined sources3
Helixi1491 – 1493Combined sources3
Helixi1495 – 1498Combined sources4
Beta strandi1510 – 1519Combined sources10
Helixi1521 – 1526Combined sources6
Helixi1528 – 1539Combined sources12
Beta strandi1541 – 1545Combined sources5
Beta strandi1555 – 1558Combined sources4
Beta strandi1579 – 1587Combined sources9
Turni1589 – 1592Combined sources4
Turni1595 – 1597Combined sources3
Beta strandi1598 – 1600Combined sources3
Helixi1604 – 1616Combined sources13
Beta strandi1626 – 1632Combined sources7

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
4ZLPX-ray2.48A/B1378-1640[»]
5CZVX-ray3.19A1378-1640[»]
5CZXX-ray2.10A/B1378-1640[»]
ProteinModelPortaliQ9UM47.
SMRiQ9UM47.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Domaini40 – 77EGF-like 1PROSITE-ProRule annotationAdd BLAST38
Domaini78 – 118EGF-like 2PROSITE-ProRule annotationAdd BLAST41
Domaini119 – 156EGF-like 3PROSITE-ProRule annotationAdd BLAST38
Domaini158 – 195EGF-like 4; calcium-bindingPROSITE-ProRule annotationAdd BLAST38
Domaini197 – 234EGF-like 5PROSITE-ProRule annotationAdd BLAST38
Domaini236 – 272EGF-like 6; calcium-bindingPROSITE-ProRule annotationAdd BLAST37
Domaini274 – 312EGF-like 7PROSITE-ProRule annotationAdd BLAST39
Domaini314 – 350EGF-like 8; calcium-bindingPROSITE-ProRule annotationAdd BLAST37
Domaini351 – 389EGF-like 9PROSITE-ProRule annotationAdd BLAST39
Domaini391 – 429EGF-like 10; calcium-bindingPROSITE-ProRule annotationAdd BLAST39
Domaini431 – 467EGF-like 11; calcium-bindingPROSITE-ProRule annotationAdd BLAST37
Domaini469 – 505EGF-like 12; calcium-bindingPROSITE-ProRule annotationAdd BLAST37
Domaini507 – 543EGF-like 13; calcium-bindingPROSITE-ProRule annotationAdd BLAST37
Domaini545 – 580EGF-like 14; calcium-bindingPROSITE-ProRule annotationAdd BLAST36
Domaini582 – 618EGF-like 15; calcium-bindingPROSITE-ProRule annotationAdd BLAST37
Domaini620 – 655EGF-like 16; calcium-bindingPROSITE-ProRule annotationAdd BLAST36
Domaini657 – 693EGF-like 17; calcium-bindingPROSITE-ProRule annotationAdd BLAST37
Domaini695 – 730EGF-like 18PROSITE-ProRule annotationAdd BLAST36
Domaini734 – 770EGF-like 19PROSITE-ProRule annotationAdd BLAST37
Domaini771 – 808EGF-like 20PROSITE-ProRule annotationAdd BLAST38
Domaini810 – 847EGF-like 21; calcium-bindingPROSITE-ProRule annotationAdd BLAST38
Domaini849 – 885EGF-like 22; calcium-bindingPROSITE-ProRule annotationAdd BLAST37
Domaini887 – 922EGF-like 23; calcium-bindingPROSITE-ProRule annotationAdd BLAST36
Domaini924 – 960EGF-like 24PROSITE-ProRule annotationAdd BLAST37
Domaini962 – 998EGF-like 25PROSITE-ProRule annotationAdd BLAST37
Domaini1000 – 1034EGF-like 26PROSITE-ProRule annotationAdd BLAST35
Domaini1047 – 1082EGF-like 27PROSITE-ProRule annotationAdd BLAST36
Domaini1084 – 1120EGF-like 28PROSITE-ProRule annotationAdd BLAST37
Domaini1122 – 1158EGF-like 29; calcium-bindingPROSITE-ProRule annotationAdd BLAST37
Domaini1160 – 1203EGF-like 30; calcium-bindingPROSITE-ProRule annotationAdd BLAST44
Domaini1205 – 1244EGF-like 31PROSITE-ProRule annotationAdd BLAST40
Domaini1246 – 1287EGF-like 32PROSITE-ProRule annotationAdd BLAST42
Domaini1289 – 1325EGF-like 33PROSITE-ProRule annotationAdd BLAST37