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Q04721

- NOTC2_HUMAN

UniProt

Q04721 - NOTC2_HUMAN

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Protein

Neurogenic locus notch homolog protein 2

Gene

NOTCH2

Organism
Homo sapiens (Human)
Status
Reviewed - 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). Involved in bone remodeling and homeostasis. In collaboration with RELA/p65 enhances NFATc1 promoter activity and positively regulates RANKL-induced osteoclast differentiation.By similarity2 Publications

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sitei614 – 6141Essential for O-xylosylationBy similarity

GO - Molecular functioni

  1. calcium ion binding Source: InterPro
  2. ligand-activated RNA polymerase II transcription factor binding transcription factor activity Source: UniProtKB
  3. receptor activity Source: UniProtKB

GO - Biological processi

  1. apoptotic process Source: UniProtKB
  2. atrial septum morphogenesis Source: BHF-UCL
  3. bone remodeling Source: UniProtKB
  4. cell cycle arrest Source: UniProtKB
  5. cell fate determination Source: UniProtKB
  6. cell growth Source: UniProtKB
  7. ciliary body morphogenesis Source: Ensembl
  8. determination of left/right symmetry Source: Ensembl
  9. embryonic limb morphogenesis Source: Ensembl
  10. gene expression Source: Reactome
  11. hemopoiesis Source: UniProtKB
  12. humoral immune response Source: Ensembl
  13. inflammatory response to antigenic stimulus Source: Ensembl
  14. interleukin-4 secretion Source: Ensembl
  15. intracellular receptor signaling pathway Source: GOC
  16. in utero embryonic development Source: Ensembl
  17. morphogenesis of an epithelial sheet Source: Ensembl
  18. multicellular organismal development Source: UniProtKB
  19. negative regulation of apoptotic process Source: UniProtKB
  20. negative regulation of cell proliferation Source: UniProtKB
  21. negative regulation of transcription from RNA polymerase II promoter Source: Ensembl
  22. nervous system development Source: UniProtKB
  23. Notch receptor processing Source: Reactome
  24. Notch signaling involved in heart development Source: BHF-UCL
  25. Notch signaling pathway Source: Reactome
  26. organ morphogenesis Source: UniProtKB
  27. placenta blood vessel development Source: Ensembl
  28. positive regulation of apoptotic process Source: Ensembl
  29. positive regulation of BMP signaling pathway Source: Ensembl
  30. positive regulation of cell proliferation Source: Ensembl
  31. positive regulation of Ras protein signal transduction Source: UniProtKB
  32. pulmonary valve morphogenesis Source: BHF-UCL
  33. regulation of transcription, DNA-templated Source: UniProtKB
  34. stem cell maintenance Source: UniProtKB
  35. transcription initiation from RNA polymerase II promoter Source: Reactome
Complete GO annotation...

Keywords - Molecular functioni

Activator, Developmental protein, Receptor

Keywords - Biological processi

Differentiation, Notch signaling pathway, Transcription, Transcription regulation

Enzyme and pathway databases

ReactomeiREACT_118568. Pre-NOTCH Transcription and Translation.
REACT_118722. Pre-NOTCH Processing in the Endoplasmic Reticulum.
REACT_118798. Pre-NOTCH Processing in Golgi.
REACT_14835. Notch-HLH transcription pathway.
REACT_160205. NOTCH2 Activation and Transmission of Signal to the Nucleus.
REACT_163910. NOTCH2 intracellular domain regulates transcription.
SignaLinkiQ04721.

Names & Taxonomyi

Protein namesi
Recommended name:
Neurogenic locus notch homolog protein 2
Short name:
Notch 2
Short name:
hN2
Cleaved into the following 2 chains:
Gene namesi
Name:NOTCH2
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640: Chromosome 1

Organism-specific databases

HGNCiHGNC:7882. NOTCH2.

Subcellular locationi

Chain Notch 2 intracellular domain : Nucleus
Note: Following proteolytical processing NICD is translocated to the nucleus.

GO - Cellular componenti

  1. cell surface Source: UniProtKB
  2. cilium Source: Ensembl
  3. endoplasmic reticulum membrane Source: Reactome
  4. extracellular region Source: Reactome
  5. Golgi membrane Source: Reactome
  6. integral component of plasma membrane Source: UniProtKB
  7. membrane Source: UniProtKB
  8. nucleoplasm Source: Reactome
  9. nucleus Source: UniProtKB
  10. plasma membrane Source: Reactome
  11. receptor complex Source: MGI
Complete GO annotation...

Keywords - Cellular componenti

Cell membrane, Membrane, Nucleus

Pathology & Biotechi

Involvement in diseasei

Alagille syndrome 2 (ALGS2) [MIM:610205]: A form of Alagille syndrome, an autosomal dominant multisystem disorder. It is clinically defined by hepatic bile duct paucity and cholestasis in association with cardiac, skeletal, and ophthalmologic manifestations. There are characteristic facial features and less frequent clinical involvement of the renal and vascular systems.1 Publication
Note: The disease is caused by mutations affecting the gene represented in this entry.
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti444 – 4441C → Y in ALGS2. 1 Publication
VAR_029361
Hajdu-Cheney syndrome (HJCYS) [MIM:102500]: A rare skeletal disorder characterized by the association of facial anomalies, acro-osteolysis, general osteoporosis, insufficient ossification of the skull, and periodontal disease (premature loss of permanent teeth). Other features include cleft palate, congenital heart defects, polycystic kidneys, orthopedic problems and anomalies of the genitalia, intestines and eyes.2 Publications
Note: The disease is caused by mutations affecting the gene represented in this entry. NOTCH2 mutations associated with Hajdu-Cheney syndrome cluster to the last coding exon of the gene. This suggests that the mutant mRNA products may escape nonsense-mediated decay and the resulting truncated NOTCH2 proteins act in a gain-of-function manner.

Keywords - Diseasei

Disease mutation

Organism-specific databases

MIMi102500. phenotype.
610205. phenotype.
Orphaneti955. Acroosteolysis dominant type.
261629. Alagille syndrome due to a NOTCH2 point mutation.
PharmGKBiPA31684.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Signal peptidei1 – 2525Sequence AnalysisAdd
BLAST
Chaini26 – 24712446Neurogenic locus notch homolog protein 2PRO_0000007683Add
BLAST
Chaini1666 – 2471806Notch 2 extracellular truncationBy similarityPRO_0000007684Add
BLAST
Chaini1697 – 2471775Notch 2 intracellular domainBy similarityPRO_0000007685Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Disulfide bondi28 ↔ 41By similarity
Disulfide bondi35 ↔ 51By similarity
Glycosylationi46 – 461N-linked (GlcNAc...)Sequence Analysis
Disulfide bondi53 ↔ 62By similarity
Disulfide bondi68 ↔ 79By similarity
Disulfide bondi73 ↔ 90By similarity
Disulfide bondi92 ↔ 101By similarity
Disulfide bondi109 ↔ 121By similarity
Disulfide bondi115 ↔ 131By similarity
Disulfide bondi133 ↔ 142By similarity
Disulfide bondi148 ↔ 159By similarity
Disulfide bondi153 ↔ 168By similarity
Glycosylationi155 – 1551N-linked (GlcNAc...)Sequence Analysis
Disulfide bondi170 ↔ 179By similarity
Disulfide bondi186 ↔ 198By similarity
Disulfide bondi192 ↔ 207By similarity
Disulfide bondi209 ↔ 218By similarity
Disulfide bondi225 ↔ 236By similarity
Disulfide bondi230 ↔ 246By similarity
Disulfide bondi248 ↔ 257By similarity
Disulfide bondi264 ↔ 275By similarity
Disulfide bondi269 ↔ 284By similarity
Disulfide bondi286 ↔ 295By similarity
Disulfide bondi302 ↔ 315By similarity
Disulfide bondi309 ↔ 324By similarity
Disulfide bondi326 ↔ 335By similarity
Disulfide bondi342 ↔ 353By similarity
Disulfide bondi347 ↔ 362By similarity
Disulfide bondi364 ↔ 373By similarity
Disulfide bondi379 ↔ 390By similarity
Disulfide bondi384 ↔ 401By similarity
Disulfide bondi403 ↔ 412By similarity
Disulfide bondi419 ↔ 433By similarity
Disulfide bondi427 ↔ 442By similarity
Disulfide bondi444 ↔ 453By similarity
Disulfide bondi460 ↔ 471By similarity
Disulfide bondi465 ↔ 480By similarity
Disulfide bondi482 ↔ 491By similarity
Disulfide bondi498 ↔ 509By similarity
Disulfide bondi503 ↔ 518By similarity
Disulfide bondi520 ↔ 529By similarity
Disulfide bondi536 ↔ 547By similarity
Disulfide bondi541 ↔ 556By similarity
Disulfide bondi558 ↔ 567By similarity
Disulfide bondi574 ↔ 584By similarity
Disulfide bondi579 ↔ 593By similarity
Disulfide bondi595 ↔ 604By similarity
Disulfide bondi611 ↔ 622By similarity
Glycosylationi613 – 6131O-linked (Glc...); alternateBy similarity
Glycosylationi613 – 6131O-linked (Xyl...); alternateBy similarity
Disulfide bondi616 ↔ 631By similarity
Disulfide bondi633 ↔ 642By similarity
Disulfide bondi649 ↔ 659By similarity
Disulfide bondi654 ↔ 668By similarity
Disulfide bondi670 ↔ 679By similarity
Disulfide bondi686 ↔ 697By similarity
Disulfide bondi691 ↔ 706By similarity
Disulfide bondi708 ↔ 717By similarity
Disulfide bondi724 ↔ 734By similarity
Disulfide bondi729 ↔ 743By similarity
Glycosylationi733 – 7331N-linked (GlcNAc...)Sequence Analysis
Disulfide bondi745 ↔ 754By similarity
Disulfide bondi761 ↔ 772By similarity
Disulfide bondi766 ↔ 781By similarity
Disulfide bondi783 ↔ 792By similarity
Disulfide bondi799 ↔ 810By similarity
Disulfide bondi804 ↔ 819By similarity
Disulfide bondi821 ↔ 830By similarity
Disulfide bondi837 ↔ 848By similarity
Disulfide bondi842 ↔ 859By similarity
Disulfide bondi861 ↔ 870By similarity
Disulfide bondi877 ↔ 888By similarity
Disulfide bondi882 ↔ 897By similarity
Disulfide bondi899 ↔ 908By similarity
Disulfide bondi915 ↔ 926By similarity
Disulfide bondi920 ↔ 935By similarity
Disulfide bondi937 ↔ 946By similarity
Disulfide bondi953 ↔ 964By similarity
Disulfide bondi958 ↔ 973By similarity
Disulfide bondi975 ↔ 984By similarity
Disulfide bondi991 ↔ 1002By similarity
Disulfide bondi996 ↔ 1011By similarity
Disulfide bondi1013 ↔ 1022By similarity
Disulfide bondi1029 ↔ 1040By similarity
Disulfide bondi1034 ↔ 1049By similarity
Disulfide bondi1051 ↔ 1060By similarity
Disulfide bondi1067 ↔ 1078By similarity
Disulfide bondi1072 ↔ 1087By similarity
Disulfide bondi1089 ↔ 1098By similarity
Glycosylationi1102 – 11021N-linked (GlcNAc...)Sequence Analysis
Disulfide bondi1105 ↔ 1126By similarity
Disulfide bondi1120 ↔ 1135By similarity
Disulfide bondi1137 ↔ 1146By similarity
Disulfide bondi1153 ↔ 1164By similarity
Disulfide bondi1158 ↔ 1173By similarity
Disulfide bondi1175 ↔ 1184By similarity
Disulfide bondi1191 ↔ 1202By similarity
Disulfide bondi1196 ↔ 1211By similarity
Disulfide bondi1213 ↔ 1222By similarity
Disulfide bondi1229 ↔ 1241By similarity
Disulfide bondi1235 ↔ 1250By similarity
Disulfide bondi1252 ↔ 1261By similarity
Disulfide bondi1268 ↔ 1281By similarity
Disulfide bondi1273 ↔ 1290By similarity
Disulfide bondi1292 ↔ 1301By similarity
Disulfide bondi1308 ↔ 1319By similarity
Disulfide bondi1313 ↔ 1331By similarity
Disulfide bondi1333 ↔ 1342By similarity
Disulfide bondi1378 ↔ 1389By similarity
Disulfide bondi1383 ↔ 1400By similarity
Disulfide bondi1402 ↔ 1411By similarity
Disulfide bondi1425 ↔ 14481 Publication
Disulfide bondi1430 ↔ 14431 Publication
Disulfide bondi1439 ↔ 14551 Publication
Glycosylationi1465 – 14651N-linked (GlcNAc...)Sequence Analysis
Disulfide bondi1466 ↔ 14891 Publication
Disulfide bondi1472 ↔ 14841 Publication
Disulfide bondi1480 ↔ 14961 Publication
Disulfide bondi1503 ↔ 15271 Publication
Disulfide bondi1509 ↔ 15221 Publication
Disulfide bondi1518 ↔ 15341 Publication
Disulfide bondi1632 ↔ 16391 Publication
Modified residuei1716 – 17161Phosphothreonine1 Publication
Modified residuei1778 – 17781Phosphoserine2 Publications
Modified residuei1802 – 18021Phosphothreonine1 Publication
Modified residuei1804 – 18041Phosphoserine1 Publication
Modified residuei1808 – 18081Phosphothreonine1 Publication
Modified residuei1842 – 18421PhosphoserineBy similarity
Modified residuei1845 – 18451Phosphoserine2 Publications
Modified residuei2070 – 20701Phosphoserine1 Publication
Modified residuei2078 – 20781PhosphoserineBy similarity
Modified residuei2081 – 20811Phosphoserine1 Publication
Modified residuei2097 – 20971Phosphothreonine1 Publication

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
Hydroxylated by HIF1AN.1 Publication
Can be either O-glucosylated or O-xylosylated at Ser-613 by POGLUT1.By similarity

Keywords - PTMi

Disulfide bond, Glycoprotein, Phosphoprotein

Proteomic databases

MaxQBiQ04721.
PaxDbiQ04721.
PRIDEiQ04721.

PTM databases

PhosphoSiteiQ04721.

Expressioni

Tissue specificityi

Expressed in the brain, heart, kidney, lung, skeletal muscle and liver. Ubiquitously expressed in the embryo.1 Publication

Gene expression databases

BgeeiQ04721.
CleanExiHS_NOTCH2.
ExpressionAtlasiQ04721. baseline and differential.
GenevestigatoriQ04721.

Organism-specific databases

HPAiHPA046392.

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 (By similarity). Interacts with MAML1, MAML2 and MAML3 which act as transcriptional coactivators for NOTCH2. Interacts with RELA/p65 (By similarity). Interacts with HIF1AN.By similarity3 Publications

Protein-protein interaction databases

BioGridi110915. 28 interactions.
IntActiQ04721. 5 interactions.
MINTiMINT-1187009.
STRINGi9606.ENSP00000256646.

Structurei

Secondary structure

1
2471
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi1428 – 14336
Beta strandi1436 – 14383
Helixi1441 – 14433
Turni1446 – 14483
Helixi1449 – 14524
Turni1453 – 14586
Turni1462 – 14654
Helixi1472 – 14743
Beta strandi1477 – 14793
Helixi1482 – 14843
Turni1487 – 14904
Helixi1491 – 14944
Helixi1506 – 15127
Beta strandi1515 – 15173
Helixi1520 – 15223
Helixi1525 – 15328
Beta strandi1544 – 155310
Helixi1555 – 15606
Helixi1562 – 157312
Beta strandi1575 – 15795
Beta strandi1589 – 15946
Beta strandi1617 – 162812
Helixi1632 – 16354
Helixi1643 – 165614
Beta strandi1663 – 16708

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
2OO4X-ray2.00A/B1423-1677[»]
ProteinModelPortaliQ04721.
SMRiQ04721. Positions 33-1343, 1425-1672, 1777-2063.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiQ04721.

Topological domain

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Topological domaini26 – 16771652ExtracellularSequence AnalysisAdd
BLAST
Topological domaini1699 – 2471773CytoplasmicSequence AnalysisAdd
BLAST

Transmembrane

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Transmembranei1678 – 169821HelicalSequence AnalysisAdd
BLAST

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini26 – 6338EGF-like 1PROSITE-ProRule annotationAdd
BLAST
Domaini64 – 10239EGF-like 2PROSITE-ProRule annotationAdd
BLAST
Domaini105 – 14339EGF-like 3PROSITE-ProRule annotationAdd
BLAST
Domaini144 – 18037EGF-like 4PROSITE-ProRule annotationAdd
BLAST
Domaini182 – 21938EGF-like 5; calcium-bindingPROSITE-ProRule annotationAdd
BLAST
Domaini221 – 25838EGF-like 6PROSITE-ProRule annotationAdd
BLAST
Domaini260 – 29637EGF-like 7; calcium-bindingPROSITE-ProRule annotationAdd
BLAST
Domaini298 – 33639EGF-like 8; calcium-bindingPROSITE-ProRule annotationAdd
BLAST
Domaini338 – 37437EGF-like 9; calcium-bindingPROSITE-ProRule annotationAdd
BLAST
Domaini375 – 41339EGF-like 10PROSITE-ProRule annotationAdd
BLAST
Domaini415 – 45440EGF-like 11; calcium-bindingPROSITE-ProRule annotationAdd
BLAST
Domaini456 – 49237EGF-like 12; calcium-bindingPROSITE-ProRule annotationAdd
BLAST
Domaini494 – 53037EGF-like 13; calcium-bindingPROSITE-ProRule annotationAdd
BLAST
Domaini532 – 56837EGF-like 14; calcium-bindingPROSITE-ProRule annotationAdd
BLAST
Domaini570 – 60536EGF-like 15; calcium-bindingPROSITE-ProRule annotationAdd
BLAST
Domaini607 – 64337EGF-like 16; calcium-bindingPROSITE-ProRule annotationAdd
BLAST
Domaini645 – 68036EGF-like 17; calcium-bindingPROSITE-ProRule annotationAdd
BLAST
Domaini682 – 71837EGF-like 18; calcium-bindingPROSITE-ProRule annotationAdd
BLAST
Domaini720 – 75536EGF-like 19PROSITE-ProRule annotationAdd
BLAST
Domaini757 – 79337EGF-like 20; calcium-bindingPROSITE-ProRule annotationAdd
BLAST
Domaini795 – 83137EGF-like 21; calcium-bindingPROSITE-ProRule annotationAdd
BLAST
Domaini833 – 87139EGF-like 22PROSITE-ProRule annotationAdd
BLAST
Domaini873 – 90937EGF-like 23; calcium-bindingPROSITE-ProRule annotationAdd
BLAST
Domaini911 – 94737EGF-like 24; calcium-bindingPROSITE-ProRule annotationAdd
BLAST
Domaini949 – 98537EGF-like 25; calcium-bindingPROSITE-ProRule annotationAdd
BLAST
Domaini987 – 102337EGF-like 26; calcium-bindingPROSITE-ProRule annotationAdd
BLAST
Domaini1025 – 106137EGF-like 27; calcium-bindingPROSITE-ProRule annotationAdd
BLAST
Domaini1063 – 109937EGF-like 28PROSITE-ProRule annotationAdd
BLAST
Domaini1101 – 114747EGF-like 29PROSITE-ProRule annotationAdd
BLAST
Domaini1149 – 118537EGF-like 30; calcium-bindingPROSITE-ProRule annotationAdd
BLAST
Domaini1187 – 122337EGF-like 31; calcium-bindingPROSITE-ProRule annotationAdd
BLAST
Domaini1225 – 126238EGF-like 32; calcium-bindingPROSITE-ProRule annotationAdd
BLAST
Domaini1264 – 130239EGF-like 33PROSITE-ProRule annotationAdd
BLAST
Domaini1304 – 134340EGF-like 34PROSITE-ProRule annotationAdd
BLAST
Domaini1374 – 141239EGF-like 35PROSITE-ProRule annotationAdd
BLAST
Repeati1425 – 146541LNR 1Add
BLAST
Repeati1466 – 150237LNR 2Add
BLAST
Repeati1503 – 154442LNR 3Add
BLAST
Repeati1827 – 187145ANK 1Add
BLAST
Repeati1876 – 190530ANK 2Add
BLAST
Repeati1909 – 193931ANK 3Add
BLAST
Repeati1943 – 197230ANK 4Add
BLAST
Repeati1976 – 200530ANK 5Add
BLAST
Repeati2009 – 203830ANK 6Add
BLAST

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni1425 – 1677253Negative regulatory region (NRR)Add
BLAST

Compositional bias

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Compositional biasi1645 – 16484Poly-Ala
Compositional biasi1994 – 19974Poly-Leu
Compositional biasi2426 – 24294Poly-Ser

Sequence similaritiesi

Belongs to the NOTCH family.Curated
Contains 6 ANK repeats.PROSITE-ProRule annotation
Contains 35 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.
InParanoidiQ04721.
KOiK02599.
OMAiMEDPWAN.
OrthoDBiEOG7992RD.
PhylomeDBiQ04721.
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.
IPR022336. Notch_2.
IPR000800. Notch_dom.
IPR010660. Notch_NOD_dom.
IPR011656. Notch_NODP_dom.
[Graphical view]
PfamiPF00023. Ank. 1 hit.
PF12796. Ank_2. 2 hits.
PF11936. DUF3454. 1 hit.
PF00008. EGF. 23 hits.
PF07645. EGF_CA. 5 hits.
PF06816. NOD. 1 hit.
PF07684. NODP. 1 hit.
PF00066. Notch. 3 hits.
[Graphical view]
PIRSFiPIRSF002279. Notch. 1 hit.
PRINTSiPR01452. LNOTCHREPEAT.
PR01985. NOTCH2.
SMARTiSM00248. ANK. 6 hits.
SM00181. EGF. 12 hits.
SM00179. EGF_CA. 23 hits.
SM00004. NL. 3 hits.
[Graphical view]
SUPFAMiSSF48403. SSF48403. 1 hit.
SSF57184. SSF57184. 6 hits.
SSF90193. SSF90193. 2 hits.
PROSITEiPS50297. ANK_REP_REGION. 1 hit.
PS50088. ANK_REPEAT. 4 hits.
PS00010. ASX_HYDROXYL. 22 hits.
PS00022. EGF_1. 34 hits.
PS01186. EGF_2. 29 hits.
PS50026. EGF_3. 35 hits.
PS01187. EGF_CA. 22 hits.
PS50258. LNR. 3 hits.
[Graphical view]

Sequencei

Sequence statusi: Complete.

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

Q04721-1 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
MPALRPALLW ALLALWLCCA APAHALQCRD GYEPCVNEGM CVTYHNGTGY
60 70 80 90 100
CKCPEGFLGE YCQHRDPCEK NRCQNGGTCV AQAMLGKATC RCASGFTGED
110 120 130 140 150
CQYSTSHPCF VSRPCLNGGT CHMLSRDTYE CTCQVGFTGK ECQWTDACLS
160 170 180 190 200
HPCANGSTCT TVANQFSCKC LTGFTGQKCE TDVNECDIPG HCQHGGTCLN
210 220 230 240 250
LPGSYQCQCP QGFTGQYCDS LYVPCAPSPC VNGGTCRQTG DFTFECNCLP
260 270 280 290 300
GFEGSTCERN IDDCPNHRCQ NGGVCVDGVN TYNCRCPPQW TGQFCTEDVD
310 320 330 340 350
ECLLQPNACQ NGGTCANRNG GYGCVCVNGW SGDDCSENID DCAFASCTPG
360 370 380 390 400
STCIDRVASF SCMCPEGKAG LLCHLDDACI SNPCHKGALC DTNPLNGQYI
410 420 430 440 450
CTCPQGYKGA DCTEDVDECA MANSNPCEHA GKCVNTDGAF HCECLKGYAG
460 470 480 490 500
PRCEMDINEC HSDPCQNDAT CLDKIGGFTC LCMPGFKGVH CELEINECQS
510 520 530 540 550
NPCVNNGQCV DKVNRFQCLC PPGFTGPVCQ IDIDDCSSTP CLNGAKCIDH
560 570 580 590 600
PNGYECQCAT GFTGVLCEEN IDNCDPDPCH HGQCQDGIDS YTCICNPGYM
610 620 630 640 650
GAICSDQIDE CYSSPCLNDG RCIDLVNGYQ CNCQPGTSGV NCEINFDDCA
660 670 680 690 700
SNPCIHGICM DGINRYSCVC SPGFTGQRCN IDIDECASNP CRKGATCING
710 720 730 740 750
VNGFRCICPE GPHHPSCYSQ VNECLSNPCI HGNCTGGLSG YKCLCDAGWV
760 770 780 790 800
GINCEVDKNE CLSNPCQNGG TCDNLVNGYR CTCKKGFKGY NCQVNIDECA
810 820 830 840 850
SNPCLNQGTC FDDISGYTCH CVLPYTGKNC QTVLAPCSPN PCENAAVCKE
860 870 880 890 900
SPNFESYTCL CAPGWQGQRC TIDIDECISK PCMNHGLCHN TQGSYMCECP
910 920 930 940 950
PGFSGMDCEE DIDDCLANPC QNGGSCMDGV NTFSCLCLPG FTGDKCQTDM
960 970 980 990 1000
NECLSEPCKN GGTCSDYVNS YTCKCQAGFD GVHCENNINE CTESSCFNGG
1010 1020 1030 1040 1050
TCVDGINSFS CLCPVGFTGS FCLHEINECS SHPCLNEGTC VDGLGTYRCS
1060 1070 1080 1090 1100
CPLGYTGKNC QTLVNLCSRS PCKNKGTCVQ KKAESQCLCP SGWAGAYCDV
1110 1120 1130 1140 1150
PNVSCDIAAS RRGVLVEHLC QHSGVCINAG NTHYCQCPLG YTGSYCEEQL
1160 1170 1180 1190 1200
DECASNPCQH GATCSDFIGG YRCECVPGYQ GVNCEYEVDE CQNQPCQNGG
1210 1220 1230 1240 1250
TCIDLVNHFK CSCPPGTRGL LCEENIDDCA RGPHCLNGGQ CMDRIGGYSC
1260 1270 1280 1290 1300
RCLPGFAGER CEGDINECLS NPCSSEGSLD CIQLTNDYLC VCRSAFTGRH
1310 1320 1330 1340 1350
CETFVDVCPQ MPCLNGGTCA VASNMPDGFI CRCPPGFSGA RCQSSCGQVK
1360 1370 1380 1390 1400
CRKGEQCVHT ASGPRCFCPS PRDCESGCAS SPCQHGGSCH PQRQPPYYSC
1410 1420 1430 1440 1450
QCAPPFSGSR CELYTAPPST PPATCLSQYC ADKARDGVCD EACNSHACQW
1460 1470 1480 1490 1500
DGGDCSLTME NPWANCSSPL PCWDYINNQC DELCNTVECL FDNFECQGNS
1510 1520 1530 1540 1550
KTCKYDKYCA DHFKDNHCDQ GCNSEECGWD GLDCAADQPE NLAEGTLVIV
1560 1570 1580 1590 1600
VLMPPEQLLQ DARSFLRALG TLLHTNLRIK RDSQGELMVY PYYGEKSAAM
1610 1620 1630 1640 1650
KKQRMTRRSL PGEQEQEVAG SKVFLEIDNR QCVQDSDHCF KNTDAAAALL
1660 1670 1680 1690 1700
ASHAIQGTLS YPLVSVVSES LTPERTQLLY LLAVAVVIIL FIILLGVIMA
1710 1720 1730 1740 1750
KRKRKHGSLW LPEGFTLRRD ASNHKRREPV GQDAVGLKNL SVQVSEANLI
1760 1770 1780 1790 1800
GTGTSEHWVD DEGPQPKKVK AEDEALLSEE DDPIDRRPWT QQHLEAADIR
1810 1820 1830 1840 1850
RTPSLALTPP QAEQEVDVLD VNVRGPDGCT PLMLASLRGG SSDLSDEDED
1860 1870 1880 1890 1900
AEDSSANIIT DLVYQGASLQ AQTDRTGEMA LHLAARYSRA DAAKRLLDAG
1910 1920 1930 1940 1950
ADANAQDNMG RCPLHAAVAA DAQGVFQILI RNRVTDLDAR MNDGTTPLIL
1960 1970 1980 1990 2000
AARLAVEGMV AELINCQADV NAVDDHGKSA LHWAAAVNNV EATLLLLKNG
2010 2020 2030 2040 2050
ANRDMQDNKE ETPLFLAARE GSYEAAKILL DHFANRDITD HMDRLPRDVA
2060 2070 2080 2090 2100
RDRMHHDIVR LLDEYNVTPS PPGTVLTSAL SPVICGPNRS FLSLKHTPMG
2110 2120 2130 2140 2150
KKSRRPSAKS TMPTSLPNLA KEAKDAKGSR RKKSLSEKVQ LSESSVTLSP
2160 2170 2180 2190 2200
VDSLESPHTY VSDTTSSPMI TSPGILQASP NPMLATAAPP APVHAQHALS
2210 2220 2230 2240 2250
FSNLHEMQPL AHGASTVLPS VSQLLSHHHI VSPGSGSAGS LSRLHPVPVP
2260 2270 2280 2290 2300
ADWMNRMEVN ETQYNEMFGM VLAPAEGTHP GIAPQSRPPE GKHITTPREP
2310 2320 2330 2340 2350
LPPIVTFQLI PKGSIAQPAG APQPQSTCPP AVAGPLPTMY QIPEMARLPS
2360 2370 2380 2390 2400
VAFPTAMMPQ QDGQVAQTIL PAYHPFPASV GKYPTPPSQH SYASSNAAER
2410 2420 2430 2440 2450
TPSHSGHLQG EHPYLTPSPE SPDQWSSSSP HSASDWSDVT TSPTPGGAGG
2460 2470
GQRGPGTHMS EPPHNNMQVY A
Length:2,471
Mass (Da):265,405
Last modified:April 3, 2007 - v3
Checksum:i605B1B963C812BE1
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti21 – 211A → T in AAG37073. 1 PublicationCurated
Sequence conflicti210 – 2101P → L in AAG37073. 1 PublicationCurated
Sequence conflicti1037 – 10371E → D in AAB19224. 1 PublicationCurated
Sequence conflicti1084 – 10852ES → SP in AAB19224. 1 PublicationCurated
Sequence conflicti1094 – 10941A → V in AAB19224. 1 PublicationCurated
Sequence conflicti1139 – 11391L → V in AAB19224. 1 PublicationCurated
Sequence conflicti1519 – 15191D → N in AAA36377. 1 PublicationCurated
Sequence conflicti2053 – 20531R → H in AAG37073. 1 PublicationCurated

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti444 – 4441C → Y in ALGS2. 1 Publication
VAR_029361
Natural varianti1667 – 16671V → F.
Corresponds to variant rs17024517 [ dbSNP | Ensembl ].
VAR_031463

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AF308601 mRNA. Translation: AAA36377.2.
AF315356 mRNA. Translation: AAG37073.1.
AL359752, AL512503, AL596222 Genomic DNA. Translation: CAI18974.1.
AL512503, AL359752, AL596222 Genomic DNA. Translation: CAH72483.1.
AL596222, AL359752, AL512503 Genomic DNA. Translation: CAH70182.1.
U77493 mRNA. Translation: AAB19224.1.
CCDSiCCDS908.1.
RefSeqiNP_001186930.1. NM_001200001.1.
NP_077719.2. NM_024408.3.
UniGeneiHs.487360.

Genome annotation databases

EnsembliENST00000256646; ENSP00000256646; ENSG00000134250.
GeneIDi4853.
KEGGihsa:4853.
UCSCiuc001eik.3. human.

Polymorphism databases

DMDMi143811429.

Cross-referencesi

Web resourcesi

Atlas of Genetics and Cytogenetics in Oncology and Haematology

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AF308601 mRNA. Translation: AAA36377.2 .
AF315356 mRNA. Translation: AAG37073.1 .
AL359752 , AL512503 , AL596222 Genomic DNA. Translation: CAI18974.1 .
AL512503 , AL359752 , AL596222 Genomic DNA. Translation: CAH72483.1 .
AL596222 , AL359752 , AL512503 Genomic DNA. Translation: CAH70182.1 .
U77493 mRNA. Translation: AAB19224.1 .
CCDSi CCDS908.1.
RefSeqi NP_001186930.1. NM_001200001.1.
NP_077719.2. NM_024408.3.
UniGenei Hs.487360.

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
2OO4 X-ray 2.00 A/B 1423-1677 [» ]
ProteinModelPortali Q04721.
SMRi Q04721. Positions 33-1343, 1425-1672, 1777-2063.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 110915. 28 interactions.
IntActi Q04721. 5 interactions.
MINTi MINT-1187009.
STRINGi 9606.ENSP00000256646.

PTM databases

PhosphoSitei Q04721.

Polymorphism databases

DMDMi 143811429.

Proteomic databases

MaxQBi Q04721.
PaxDbi Q04721.
PRIDEi Q04721.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENST00000256646 ; ENSP00000256646 ; ENSG00000134250 .
GeneIDi 4853.
KEGGi hsa:4853.
UCSCi uc001eik.3. human.

Organism-specific databases

CTDi 4853.
GeneCardsi GC01M120454.
GeneReviewsi NOTCH2.
HGNCi HGNC:7882. NOTCH2.
HPAi HPA046392.
MIMi 102500. phenotype.
600275. gene.
610205. phenotype.
neXtProti NX_Q04721.
Orphaneti 955. Acroosteolysis dominant type.
261629. Alagille syndrome due to a NOTCH2 point mutation.
PharmGKBi PA31684.
GenAtlasi Search...

Phylogenomic databases

eggNOGi COG0666.
GeneTreei ENSGT00760000118786.
HOGENOMi HOG000234369.
HOVERGENi HBG052650.
InParanoidi Q04721.
KOi K02599.
OMAi MEDPWAN.
OrthoDBi EOG7992RD.
PhylomeDBi Q04721.
TreeFami TF351641.

Enzyme and pathway databases

Reactomei REACT_118568. Pre-NOTCH Transcription and Translation.
REACT_118722. Pre-NOTCH Processing in the Endoplasmic Reticulum.
REACT_118798. Pre-NOTCH Processing in Golgi.
REACT_14835. Notch-HLH transcription pathway.
REACT_160205. NOTCH2 Activation and Transmission of Signal to the Nucleus.
REACT_163910. NOTCH2 intracellular domain regulates transcription.
SignaLinki Q04721.

Miscellaneous databases

ChiTaRSi NOTCH2. human.
EvolutionaryTracei Q04721.
GeneWikii Notch-2.
GenomeRNAii 4853.
NextBioi 18692.
PROi Q04721.
SOURCEi Search...

Gene expression databases

Bgeei Q04721.
CleanExi HS_NOTCH2.
ExpressionAtlasi Q04721. baseline and differential.
Genevestigatori Q04721.

Family and domain databases

Gene3Di 1.25.40.20. 1 hit.
InterProi IPR002110. Ankyrin_rpt.
IPR020683. Ankyrin_rpt-contain_dom.
IPR024600. DUF3454_notch.
IPR000742. EG-like_dom.
IPR001881. EGF-like_Ca-bd_dom.
IPR013032. EGF-like_CS.
IPR000152. EGF-type_Asp/Asn_hydroxyl_site.
IPR018097. EGF_Ca-bd_CS.
IPR009030. Growth_fac_rcpt_N_dom.
IPR008297. Notch.
IPR022336. Notch_2.
IPR000800. Notch_dom.
IPR010660. Notch_NOD_dom.
IPR011656. Notch_NODP_dom.
[Graphical view ]
Pfami PF00023. Ank. 1 hit.
PF12796. Ank_2. 2 hits.
PF11936. DUF3454. 1 hit.
PF00008. EGF. 23 hits.
PF07645. EGF_CA. 5 hits.
PF06816. NOD. 1 hit.
PF07684. NODP. 1 hit.
PF00066. Notch. 3 hits.
[Graphical view ]
PIRSFi PIRSF002279. Notch. 1 hit.
PRINTSi PR01452. LNOTCHREPEAT.
PR01985. NOTCH2.
SMARTi SM00248. ANK. 6 hits.
SM00181. EGF. 12 hits.
SM00179. EGF_CA. 23 hits.
SM00004. NL. 3 hits.
[Graphical view ]
SUPFAMi SSF48403. SSF48403. 1 hit.
SSF57184. SSF57184. 6 hits.
SSF90193. SSF90193. 2 hits.
PROSITEi PS50297. ANK_REP_REGION. 1 hit.
PS50088. ANK_REPEAT. 4 hits.
PS00010. ASX_HYDROXYL. 22 hits.
PS00022. EGF_1. 34 hits.
PS01186. EGF_2. 29 hits.
PS50026. EGF_3. 35 hits.
PS01187. EGF_CA. 22 hits.
PS50258. LNR. 3 hits.
[Graphical view ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  1. "Complete human notch 2 (hN2) cDNA sequence."
    Blaumueller C.M., Mann R.S.
    Submitted (NOV-2000) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
    Tissue: Brain.
  2. "Human Notch2, a novel member of cell-fate determining NOTCH family."
    Correa R.G., Camargo A.A., Moreira E.S., Simpson A.J.G.
    Submitted (OCT-2000) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
    Tissue: Mammary tumor.
  3. "The DNA sequence and biological annotation of human chromosome 1."
    Gregory S.G., Barlow K.F., McLay K.E., Kaul R., Swarbreck D., Dunham A., Scott C.E., Howe K.L., Woodfine K., Spencer C.C.A., Jones M.C., Gillson C., Searle S., Zhou Y., Kokocinski F., McDonald L., Evans R., Phillips K.
    , Atkinson A., Cooper R., Jones C., Hall R.E., Andrews T.D., Lloyd C., Ainscough R., Almeida J.P., Ambrose K.D., Anderson F., Andrew R.W., Ashwell R.I.S., Aubin K., Babbage A.K., Bagguley C.L., Bailey J., Beasley H., Bethel G., Bird C.P., Bray-Allen S., Brown J.Y., Brown A.J., Buckley D., Burton J., Bye J., Carder C., Chapman J.C., Clark S.Y., Clarke G., Clee C., Cobley V., Collier R.E., Corby N., Coville G.J., Davies J., Deadman R., Dunn M., Earthrowl M., Ellington A.G., Errington H., Frankish A., Frankland J., French L., Garner P., Garnett J., Gay L., Ghori M.R.J., Gibson R., Gilby L.M., Gillett W., Glithero R.J., Grafham D.V., Griffiths C., Griffiths-Jones S., Grocock R., Hammond S., Harrison E.S.I., Hart E., Haugen E., Heath P.D., Holmes S., Holt K., Howden P.J., Hunt A.R., Hunt S.E., Hunter G., Isherwood J., James R., Johnson C., Johnson D., Joy A., Kay M., Kershaw J.K., Kibukawa M., Kimberley A.M., King A., Knights A.J., Lad H., Laird G., Lawlor S., Leongamornlert D.A., Lloyd D.M., Loveland J., Lovell J., Lush M.J., Lyne R., Martin S., Mashreghi-Mohammadi M., Matthews L., Matthews N.S.W., McLaren S., Milne S., Mistry S., Moore M.J.F., Nickerson T., O'Dell C.N., Oliver K., Palmeiri A., Palmer S.A., Parker A., Patel D., Pearce A.V., Peck A.I., Pelan S., Phelps K., Phillimore B.J., Plumb R., Rajan J., Raymond C., Rouse G., Saenphimmachak C., Sehra H.K., Sheridan E., Shownkeen R., Sims S., Skuce C.D., Smith M., Steward C., Subramanian S., Sycamore N., Tracey A., Tromans A., Van Helmond Z., Wall M., Wallis J.M., White S., Whitehead S.L., Wilkinson J.E., Willey D.L., Williams H., Wilming L., Wray P.W., Wu Z., Coulson A., Vaudin M., Sulston J.E., Durbin R.M., Hubbard T., Wooster R., Dunham I., Carter N.P., McVean G., Ross M.T., Harrow J., Olson M.V., Beck S., Rogers J., Bentley D.R.
    Nature 441:315-321(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  4. "Partial sequence of EGF-like repeat domain of human Notch2 mRNA."
    Lemasson I., Devaux C., Mesnard J.-M.
    Submitted (NOV-1996) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 967-1229.
    Tissue: T-cell.
  5. "Human homologs of a Drosophila enhancer of split gene product define a novel family of nuclear proteins."
    Stifani S., Blaumueller C.M., Redhead N.J., Hill R.E., Artavanis-Tsakonas S.
    Nat. Genet. 2:119-127(1992) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 1810-2447.
    Tissue: Brain.
  6. "Intracellular cleavage of Notch leads to a heterodimeric receptor on the plasma membrane."
    Blaumueller C.M., Qi H., Zagouras P., Artavanis-Tsakonas S.
    Cell 90:281-291(1997) [PubMed] [Europe PMC] [Abstract]
    Cited for: PROTEOLYTIC PROCESSING.
  7. Cited for: IDENTIFICATION OF LIGANDS.
  8. "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.
  9. "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.
  10. "Global, in vivo, and site-specific phosphorylation dynamics in signaling networks."
    Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P., Mann M.
    Cell 127:635-648(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  11. Cited for: INTERACTION WITH HIF1AN.
  12. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-1716; THR-1802; SER-1804; THR-1808; SER-1845; SER-2070; SER-2081 AND THR-2097, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  13. "Interaction with factor inhibiting HIF-1 defines an additional mode of cross-coupling between the Notch and hypoxia signaling pathways."
    Zheng X., Linke S., Dias J.M., Zheng X., Gradin K., Wallis T.P., Hamilton B.R., Gustafsson M., Ruas J.L., Wilkins S., Bilton R.L., Brismar K., Whitelaw M.L., Pereira T., Gorman J.J., Ericson J., Peet D.J., Lendahl U., Poellinger L.
    Proc. Natl. Acad. Sci. U.S.A. 105:3368-3373(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: HYDROXYLATION BY HIF1AN.
  14. "Quantitative phosphoproteomic analysis of T cell receptor signaling reveals system-wide modulation of protein-protein interactions."
    Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K., Rodionov V., Han D.K.
    Sci. Signal. 2:RA46-RA46(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1778 AND SER-1845, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Leukemic T-cell.
  15. "Quantitative phosphoproteomics reveals widespread full phosphorylation site occupancy during mitosis."
    Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L., Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S., Mann M.
    Sci. Signal. 3:RA3-RA3(2010) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1778, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  16. Cited for: FUNCTION, INVOLVEMENT IN HJCYS.
  17. Cited for: FUNCTION, INVOLVEMENT IN HJCYS, TISSUE SPECIFICITY.
  18. Cited for: X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS) OF 1426-1677, DISULFIDE BONDS.
  19. "NOTCH2 mutations cause Alagille syndrome, a heterogeneous disorder of the notch signaling pathway."
    McDaniell R., Warthen D.M., Sanchez-Lara P.A., Pai A., Krantz I.D., Piccoli D.A., Spinner N.B.
    Am. J. Hum. Genet. 79:169-173(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: VARIANT ALGS2 TYR-444.

Entry informationi

Entry nameiNOTC2_HUMAN
AccessioniPrimary (citable) accession number: Q04721
Secondary accession number(s): Q5T3X7, Q99734, Q9H240
Entry historyi
Integrated into UniProtKB/Swiss-Prot: March 27, 2002
Last sequence update: April 3, 2007
Last modified: October 29, 2014
This is version 174 of the entry and version 3 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, Reference proteome

Documents

  1. Human chromosome 1
    Human chromosome 1: 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