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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

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.
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)LengthDescriptionGraphical viewFeature identifierActions
Topological domaini40 – 16431604ExtracellularSequence analysisAdd
BLAST
Transmembranei1644 – 166421HelicalSequence analysisAdd
BLAST
Topological domaini1665 – 2321657CytoplasmicSequence analysisAdd
BLAST

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)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti43 – 431C → G in CADASIL1. 2 Publications
VAR_044230
Natural varianti49 – 491C → F in CADASIL1. 2 Publications
VAR_044231
Natural varianti49 – 491C → Y in CADASIL1. 2 Publications
VAR_012871
Natural varianti54 – 541R → C in CADASIL1. 1 Publication
VAR_044232
Natural varianti60 – 601S → C in CADASIL1. 2 Publications
VAR_044233
Natural varianti65 – 651C → S in CADASIL1. 2 Publications
VAR_044234
Natural varianti67 – 671C → Y in CADASIL1. 1 Publication
VAR_044235
Natural varianti71 – 711W → C in CADASIL1. 1 Publication
Corresponds to variant rs28937321 [ dbSNP | Ensembl ].
VAR_012872
Natural varianti76 – 761C → R in CADASIL1. 2 Publications
VAR_044236
Natural varianti76 – 761C → W in CADASIL1. 2 Publications
VAR_044237
Natural varianti77 – 826Missing in CADASIL1. 1 Publication
VAR_044238
Natural varianti80 – 845Missing in CADASIL1. 3 Publications
VAR_044239
Natural varianti87 – 871C → R in CADASIL1. 2 Publications
VAR_044240
Natural varianti87 – 871C → Y in CADASIL1. 1 Publication
VAR_044241
Natural varianti90 – 901R → C in CADASIL1. 8 Publications
VAR_012873
Natural varianti93 – 931C → F in CADASIL1. 3 Publications
VAR_044242
Natural varianti93 – 931C → Y in CADASIL1. 1 Publication
VAR_044243
Natural varianti106 – 1061C → W in CADASIL1. 1 Publication
VAR_044244
Natural varianti108 – 1081C → W in CADASIL1. 1 Publication
VAR_044245
Natural varianti108 – 1081C → Y in CADASIL1. 2 Publications
VAR_044246
Natural varianti110 – 1101R → C in CADASIL1. 7 Publications
VAR_012874
Natural varianti114 – 1207Missing in CADASIL1. 2 Publications
VAR_012875
Natural varianti117 – 1171C → F in CADASIL1. 4 Publications
VAR_044247
Natural varianti118 – 1181S → C in CADASIL1. 1 Publication
VAR_044248
Natural varianti123 – 1231C → F in CADASIL1. 3 Publications
VAR_044249
Natural varianti123 – 1231C → Y in CADASIL1. 1 Publication
VAR_044250
Natural varianti128 – 1281C → Y in CADASIL1. 1 Publication
VAR_044251
Natural varianti133 – 1331R → C in CADASIL1. 10 Publications
VAR_012876
Natural varianti134 – 1341C → W in CADASIL1. 4 Publications
VAR_044252
Natural varianti141 – 1411R → C in CADASIL1. 9 Publications
VAR_012877
Natural varianti142 – 1421F → C in CADASIL1. 1 Publication
VAR_044253
Natural varianti144 – 1441C → F in CADASIL1. 1 Publication
VAR_044254
Natural varianti144 – 1441C → S in CADASIL1. 3 Publications
VAR_044255
Natural varianti144 – 1441C → Y in CADASIL1. 3 Publications
VAR_044256
Natural varianti145 – 1451S → C in CADASIL1. 1 Publication
VAR_044257
Natural varianti146 – 1461C → R in CADASIL1. 2 Publications
VAR_012878
Natural varianti149 – 1491G → C in CADASIL1. 2 Publications
VAR_044258
Natural varianti150 – 1501Y → C in CADASIL1. 3 Publications
VAR_044259
Natural varianti153 – 1553Missing in CADASIL1. 2 Publications
VAR_044260
Natural varianti153 – 1531R → C in CADASIL1. 8 Publications
VAR_012879
Natural varianti155 – 1551C → S in CADASIL1. 1 Publication
VAR_044261
Natural varianti162 – 1621C → S in CADASIL1. 1 Publication
VAR_044262
Natural varianti169 – 1691R → C in CADASIL1. 8 Publications
Corresponds to variant rs28933696 [ dbSNP | Ensembl ].
VAR_012880
Natural varianti171 – 1711G → C in CADASIL1. 1 Publication
VAR_012882
Natural varianti174 – 1741C → F in CADASIL1. 1 Publication
VAR_044263
Natural varianti174 – 1741C → R in CADASIL1. 3 Publications
VAR_044264
Natural varianti174 – 1741C → Y in CADASIL1. 5 Publications
VAR_044265
Natural varianti180 – 1801S → C in CADASIL1. 1 Publication
VAR_044266
Natural varianti182 – 1821R → C in CADASIL1. 9 Publications
Corresponds to variant rs28933697 [ dbSNP | Ensembl ].
VAR_012883
Natural varianti183 – 1831C → F in CADASIL1. 2 Publications
VAR_044267
Natural varianti183 – 1831C → R in CADASIL1. 4 Publications
VAR_044268
Natural varianti183 – 1831C → S in CADASIL1. 3 Publications
VAR_044269
Natural varianti185 – 1851C → G in CADASIL1. 1 Publication
VAR_044270
Natural varianti185 – 1851C → R in CADASIL1. 5 Publications
VAR_012884
Natural varianti189 – 1891Y → C in CADASIL1. 1 Publication
VAR_044271
Natural varianti194 – 1941C → F in CADASIL1. 3 Publications
VAR_044272
Natural varianti194 – 1941C → R in CADASIL1. 1 Publication
VAR_044273
Natural varianti194 – 1941C → S in CADASIL1. 1 Publication
VAR_044274
Natural varianti194 – 1941C → Y in CADASIL1. 1 Publication
VAR_044275
Natural varianti201 – 2011C → Y in CADASIL1. 1 Publication
VAR_044276
Natural varianti206 – 2061C → Y in CADASIL1. 1 Publication
VAR_044277
Natural varianti207 – 2071R → C in CADASIL1. 6 Publications
VAR_044278
Natural varianti212 – 2121C → S in CADASIL1. 3 Publications
VAR_012885
Natural varianti213 – 2131R → K in CADASIL1. 1 Publication
VAR_044279
Natural varianti222 – 2221C → G in CADASIL1. 3 Publications
VAR_012886
Natural varianti222 – 2221C → Y in CADASIL1. 1 Publication
VAR_044280
Natural varianti224 – 2241C → Y in CADASIL1. 2 Publications
VAR_012887
Natural varianti233 – 2331C → S in CADASIL1. 1 Publication
VAR_044281
Natural varianti233 – 2331C → Y in CADASIL1. 2 Publications
VAR_044282
Natural varianti239 – 25315Missing in CADASIL1. 2 Publications
VAR_044283Add
BLAST
Natural varianti240 – 2401C → S in CADASIL1. 2 Publications
VAR_044284
Natural varianti245 – 2451C → R in CADASIL1. 2 Publications
VAR_044285
Natural varianti251 – 2511C → R in CADASIL1. 2 Publications
VAR_044286
Natural varianti258 – 2581Y → C in CADASIL1. 2 Publications
VAR_012888
Natural varianti260 – 2601C → Y in CADASIL1. 2 Publications
VAR_044287
Natural varianti319 – 3191A → C in CADASIL1; requires 2 nucleotide substitutions. 1 Publication
VAR_044288
Natural varianti332 – 3321R → C in CADASIL1. 4 Publications
VAR_044289
Natural varianti335 – 3351S → C in CADASIL1. 2 Publications
VAR_044290
Natural varianti337 – 3371Y → C in CADASIL1. 2 Publications
VAR_044291
Natural varianti379 – 3791C → S in CADASIL1. 2 Publications
VAR_044292
Natural varianti395 – 3951C → R in CADASIL1. 2 Publications
VAR_044293
Natural varianti420 – 4201G → C in CADASIL1. 1 Publication
VAR_044294
Natural varianti421 – 4211R → C in CADASIL1. 2 Publications
VAR_044295
Natural varianti428 – 4281C → S in CADASIL1. 1 Publication
VAR_044296
Natural varianti428 – 4281C → Y in CADASIL1. 2 Publications
VAR_044297
Natural varianti440 – 4401C → G in CADASIL1. 2 Publications
VAR_044298
Natural varianti440 – 4401C → R in CADASIL1. 2 Publications
VAR_044299
Natural varianti446 – 4461C → S in CADASIL1. 1 Publication
VAR_044300
Natural varianti449 – 4491R → C in CADASIL1. 1 Publication
VAR_044301
Natural varianti455 – 4551C → R in CADASIL1. 1 Publication
Corresponds to variant rs28933698 [ dbSNP | Ensembl ].
VAR_044302
Natural varianti484 – 4841C → F in CADASIL1. 1 Publication
VAR_044303
Natural varianti484 – 4841C → Y in CADASIL1. 1 Publication
VAR_044304
Natural varianti495 – 4951C → Y in CADASIL1. 2 Publications
VAR_044305
Natural varianti511 – 5111C → R in CADASIL1. 2 Publications
VAR_044306
Natural varianti542 – 5421C → Y in CADASIL1. 2 Publications
VAR_012890
Natural varianti544 – 5441R → C in CADASIL1. 1 Publication
Corresponds to variant rs201118034 [ dbSNP | Ensembl ].
VAR_044307
Natural varianti549 – 5491C → Y in CADASIL1. 2 Publications
VAR_044308
Natural varianti558 – 5581R → C in CADASIL1. 5 Publications
VAR_012891
Natural varianti578 – 5781R → C in CADASIL1. 2 Publications
VAR_012892
Natural varianti607 – 6071R → C in CADASIL1. 2 Publications
VAR_044309
Natural varianti710 – 7101Y → C in CADASIL1; found in a compound heterozygote also carrying an intragenic frameshift deletion. 1 Publication
VAR_072080
Natural varianti728 – 7281R → C in CADASIL1. 3 Publications
VAR_012893
Natural varianti775 – 7751C → S in CADASIL1. 1 Publication
VAR_044310
Natural varianti953 – 9531G → C in CADASIL1. 2 Publications
VAR_044311
Natural varianti984 – 9841F → C in CADASIL1. 1 Publication
VAR_044312
Natural varianti985 – 9851R → C in CADASIL1. 5 Publications
VAR_012894
Natural varianti1006 – 10061R → C in CADASIL1. 2 Publications
VAR_012895
Natural varianti1015 – 10151C → R in CADASIL1. 1 Publication
VAR_044313
Natural varianti1021 – 10211Y → C in CADASIL1. 1 Publication
VAR_044315
Natural varianti1031 – 10311R → C in CADASIL1. 2 Publications
VAR_012896
Natural varianti1063 – 10631D → C in CADASIL1; requires 2 nucleotide substitutions. 1 Publication
VAR_044316
Natural varianti1231 – 12311R → C in CADASIL1. 3 Publications
Corresponds to variant rs201680145 [ dbSNP | Ensembl ].
VAR_012899
Natural varianti1261 – 12611C → R in CADASIL1. 2 Publications
VAR_012900
Natural varianti1261 – 12611C → Y in CADASIL1. 2 Publications
VAR_044317
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)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti1519 – 15191L → P in IMF2. 1 Publication
VAR_069927
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

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

Chemistry

ChEMBLiCHEMBL3407319.
GuidetoPHARMACOLOGYi2860.

Polymorphism and mutation databases

BioMutaiNOTCH3.
DMDMi322510053.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Signal peptidei1 – 3939Sequence analysisAdd
BLAST
Chaini40 – 23212282Neurogenic locus notch homolog protein 3PRO_0000007692Add
BLAST
Chaini1629 – 2321693Notch 3 extracellular truncationBy similarityPRO_0000007693Add
BLAST
Chaini1662 – 2321660Notch 3 intracellular domainBy similarityPRO_0000007694Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
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
Glycosylationi1179 – 11791N-linked (GlcNAc...)Sequence analysis
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
Glycosylationi1336 – 13361N-linked (GlcNAc...)Sequence analysis
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
Glycosylationi1438 – 14381N-linked (GlcNAc...)Sequence analysis
Disulfide bondi1442 ↔ 1458By similarity
Disulfide bondi1467 ↔ 1493By similarity
Disulfide bondi1475 ↔ 1488By similarity
Disulfide bondi1484 ↔ 1500By 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 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)LengthDescriptionGraphical viewFeature identifierActions
Sitei1571 – 15722Cleavage; by furin-like proteaseBy similarity

Keywords - PTMi

Disulfide bond, Glycoprotein, Phosphoprotein

Proteomic databases

MaxQBiQ9UM47.
PaxDbiQ9UM47.
PRIDEiQ9UM47.

PTM databases

iPTMnetiQ9UM47.
PhosphoSiteiQ9UM47.

Expressioni

Tissue specificityi

Ubiquitously expressed in fetal and adult tissues.

Gene expression databases

BgeeiQ9UM47.
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.

Protein-protein interaction databases

BioGridi110916. 60 interactions.
DIPiDIP-39827N.
IntActiQ9UM47. 14 interactions.
MINTiMINT-2822317.
STRINGi9606.ENSP00000263388.

Structurei

Secondary structure

1
2321
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi1390 – 13956Combined sources
Beta strandi1398 – 14003Combined sources
Helixi1403 – 14053Combined sources
Helixi1408 – 14103Combined sources
Helixi1411 – 14144Combined sources
Turni1415 – 14206Combined sources
Turni1424 – 14274Combined sources
Helixi1433 – 14364Combined sources
Beta strandi1439 – 14413Combined sources
Helixi1444 – 14463Combined sources
Helixi1449 – 14568Combined sources
Turni1457 – 14593Combined sources
Helixi1462 – 14643Combined sources
Helixi1469 – 147810Combined sources
Beta strandi1481 – 14833Combined sources
Helixi1486 – 14883Combined sources
Turni1491 – 14944Combined sources
Helixi1495 – 14984Combined sources
Beta strandi1510 – 151910Combined sources
Helixi1521 – 15255Combined sources
Helixi1528 – 153912Combined sources
Beta strandi1541 – 15455Combined sources
Beta strandi1555 – 15595Combined sources
Beta strandi1577 – 158711Combined sources
Turni1595 – 15973Combined sources
Helixi1604 – 161613Combined sources
Beta strandi1626 – 16327Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
4ZLPX-ray2.48A/B1378-1640[»]
ProteinModelPortaliQ9UM47.
SMRiQ9UM47. Positions 391-505, 1385-1637, 1791-2026.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini40 – 7738EGF-like 1PROSITE-ProRule annotationAdd
BLAST
Domaini78 – 11841EGF-like 2PROSITE-ProRule annotationAdd
BLAST
Domaini119 – 15638EGF-like 3PROSITE-ProRule annotationAdd
BLAST
Domaini158 – 19538EGF-like 4; calcium-bindingPROSITE-ProRule annotationAdd
BLAST
Domaini197 – 23438EGF-like 5PROSITE-ProRule annotationAdd
BLAST
Domaini236 – 27237EGF-like 6; calcium-bindingPROSITE-ProRule annotationAdd
BLAST
Domaini274 – 31239EGF-like 7PROSITE-ProRule annotationAdd
BLAST
Domaini314 – 35037EGF-like 8; calcium-bindingPROSITE-ProRule annotationAdd
BLAST
Domaini351 – 38939EGF-like 9PROSITE-ProRule annotationAdd
BLAST
Domaini391 – 42939EGF-like 10; calcium-bindingPROSITE-ProRule annotationAdd
BLAST
Domaini431 – 46737EGF-like 11; calcium-bindingPROSITE-ProRule annotationAdd
BLAST
Domaini469 – 50537EGF-like 12; calcium-bindingPROSITE-ProRule annotationAdd
BLAST
Domaini507 – 54337EGF-like 13; calcium-bindingPROSITE-ProRule annotationAdd
BLAST
Domaini545 – 58036EGF-like 14; calcium-bindingPROSITE-ProRule annotationAdd
BLAST
Domaini582 – 61837EGF-like 15; calcium-bindingPROSITE-ProRule annotationAdd
BLAST
Domaini620 – 65536EGF-like 16; calcium-bindingPROSITE-ProRule annotationAdd
BLAST
Domaini657 – 69337EGF-like 17; calcium-bindingPROSITE-ProRule annotationAdd
BLAST
Domaini695 – 73036EGF-like 18PROSITE-ProRule annotationAdd
BLAST
Domaini734 – 77037EGF-like 19PROSITE-ProRule annotationAdd
BLAST
Domaini771 – 80838EGF-like 20PROSITE-ProRule annotationAdd
BLAST
Domaini810 – 84738EGF-like 21; calcium-bindingPROSITE-ProRule annotationAdd
BLAST
Domaini849 – 88537EGF-like 22; calcium-bindingPROSITE-ProRule annotationAdd
BLAST
Domaini887 – 92236EGF-like 23; calcium-bindingPROSITE-ProRule annotationAdd
BLAST
Domaini924 – 96037EGF-like 24PROSITE-ProRule annotationAdd
BLAST
Domaini962 – 99837EGF-like 25PROSITE-ProRule annotationAdd
BLAST
Domaini1000 – 103435EGF-like 26PROSITE-ProRule annotationAdd
BLAST
Domaini1047 – 108236EGF-like 27PROSITE-ProRule annotationAdd
BLAST
Domaini1084 – 112037EGF-like 28PROSITE-ProRule annotationAdd
BLAST
Domaini1122 – 115837EGF-like 29; calcium-bindingPROSITE-ProRule annotationAdd
BLAST
Domaini1160 – 120344EGF-like 30; calcium-bindingPROSITE-ProRule annotationAdd
BLAST
Domaini1205 – 124440EGF-like 31PROSITE-ProRule annotationAdd
BLAST
Domaini