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Q04721

- NOTC2_HUMAN

UniProt

Q04721 - NOTC2_HUMAN

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
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    • History
      Entry version 173 (01 Oct 2014)
      Sequence version 3 (03 Apr 2007)
      Previous versions | rss
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    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. protein binding Source: UniProtKB
    4. 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. determination of left/right symmetry Source: Ensembl
    8. embryonic limb morphogenesis Source: Ensembl
    9. gene expression Source: Reactome
    10. hemopoiesis Source: UniProtKB
    11. humoral immune response Source: Ensembl
    12. inflammatory response to antigenic stimulus Source: Ensembl
    13. interleukin-4 secretion Source: Ensembl
    14. intracellular receptor signaling pathway Source: GOC
    15. in utero embryonic development Source: Ensembl
    16. morphogenesis of an epithelial sheet Source: Ensembl
    17. multicellular organismal development Source: UniProtKB
    18. negative regulation of apoptotic process Source: UniProtKB
    19. negative regulation of cell proliferation Source: UniProtKB
    20. nervous system development Source: UniProtKB
    21. Notch receptor processing Source: Reactome
    22. Notch signaling involved in heart development Source: BHF-UCL
    23. Notch signaling pathway Source: Reactome
    24. organ morphogenesis Source: UniProtKB
    25. placenta blood vessel development Source: Ensembl
    26. positive regulation of apoptotic process Source: Ensembl
    27. positive regulation of Ras protein signal transduction Source: UniProtKB
    28. pulmonary valve morphogenesis Source: BHF-UCL
    29. regulation of transcription, DNA-templated Source: UniProtKB
    30. stem cell maintenance Source: UniProtKB
    31. transcription initiation from RNA polymerase II promoter Source: Reactome

    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. endoplasmic reticulum membrane Source: Reactome
    3. extracellular region Source: Reactome
    4. Golgi membrane Source: Reactome
    5. integral component of plasma membrane Source: UniProtKB
    6. membrane Source: UniProtKB
    7. nucleoplasm Source: Reactome
    8. nucleus Source: UniProtKB
    9. plasma membrane Source: Reactome
    10. receptor complex Source: MGI

    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

    ArrayExpressiQ04721.
    BgeeiQ04721.
    CleanExiHS_NOTCH2.
    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. 25 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 34-1376, 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.
    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

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    MPALRPALLW ALLALWLCCA APAHALQCRD GYEPCVNEGM CVTYHNGTGY     50
    CKCPEGFLGE YCQHRDPCEK NRCQNGGTCV AQAMLGKATC RCASGFTGED 100
    CQYSTSHPCF VSRPCLNGGT CHMLSRDTYE CTCQVGFTGK ECQWTDACLS 150
    HPCANGSTCT TVANQFSCKC LTGFTGQKCE TDVNECDIPG HCQHGGTCLN 200
    LPGSYQCQCP QGFTGQYCDS LYVPCAPSPC VNGGTCRQTG DFTFECNCLP 250
    GFEGSTCERN IDDCPNHRCQ NGGVCVDGVN TYNCRCPPQW TGQFCTEDVD 300
    ECLLQPNACQ NGGTCANRNG GYGCVCVNGW SGDDCSENID DCAFASCTPG 350
    STCIDRVASF SCMCPEGKAG LLCHLDDACI SNPCHKGALC DTNPLNGQYI 400
    CTCPQGYKGA DCTEDVDECA MANSNPCEHA GKCVNTDGAF HCECLKGYAG 450
    PRCEMDINEC HSDPCQNDAT CLDKIGGFTC LCMPGFKGVH CELEINECQS 500
    NPCVNNGQCV DKVNRFQCLC PPGFTGPVCQ IDIDDCSSTP CLNGAKCIDH 550
    PNGYECQCAT GFTGVLCEEN IDNCDPDPCH HGQCQDGIDS YTCICNPGYM 600
    GAICSDQIDE CYSSPCLNDG RCIDLVNGYQ CNCQPGTSGV NCEINFDDCA 650
    SNPCIHGICM DGINRYSCVC SPGFTGQRCN IDIDECASNP CRKGATCING 700
    VNGFRCICPE GPHHPSCYSQ VNECLSNPCI HGNCTGGLSG YKCLCDAGWV 750
    GINCEVDKNE CLSNPCQNGG TCDNLVNGYR CTCKKGFKGY NCQVNIDECA 800
    SNPCLNQGTC FDDISGYTCH CVLPYTGKNC QTVLAPCSPN PCENAAVCKE 850
    SPNFESYTCL CAPGWQGQRC TIDIDECISK PCMNHGLCHN TQGSYMCECP 900
    PGFSGMDCEE DIDDCLANPC QNGGSCMDGV NTFSCLCLPG FTGDKCQTDM 950
    NECLSEPCKN GGTCSDYVNS YTCKCQAGFD GVHCENNINE CTESSCFNGG 1000
    TCVDGINSFS CLCPVGFTGS FCLHEINECS SHPCLNEGTC VDGLGTYRCS 1050
    CPLGYTGKNC QTLVNLCSRS PCKNKGTCVQ KKAESQCLCP SGWAGAYCDV 1100
    PNVSCDIAAS RRGVLVEHLC QHSGVCINAG NTHYCQCPLG YTGSYCEEQL 1150
    DECASNPCQH GATCSDFIGG YRCECVPGYQ GVNCEYEVDE CQNQPCQNGG 1200
    TCIDLVNHFK CSCPPGTRGL LCEENIDDCA RGPHCLNGGQ CMDRIGGYSC 1250
    RCLPGFAGER CEGDINECLS NPCSSEGSLD CIQLTNDYLC VCRSAFTGRH 1300
    CETFVDVCPQ MPCLNGGTCA VASNMPDGFI CRCPPGFSGA RCQSSCGQVK 1350
    CRKGEQCVHT ASGPRCFCPS PRDCESGCAS SPCQHGGSCH PQRQPPYYSC 1400
    QCAPPFSGSR CELYTAPPST PPATCLSQYC ADKARDGVCD EACNSHACQW 1450
    DGGDCSLTME NPWANCSSPL PCWDYINNQC DELCNTVECL FDNFECQGNS 1500
    KTCKYDKYCA DHFKDNHCDQ GCNSEECGWD GLDCAADQPE NLAEGTLVIV 1550
    VLMPPEQLLQ DARSFLRALG TLLHTNLRIK RDSQGELMVY PYYGEKSAAM 1600
    KKQRMTRRSL PGEQEQEVAG SKVFLEIDNR QCVQDSDHCF KNTDAAAALL 1650
    ASHAIQGTLS YPLVSVVSES LTPERTQLLY LLAVAVVIIL FIILLGVIMA 1700
    KRKRKHGSLW LPEGFTLRRD ASNHKRREPV GQDAVGLKNL SVQVSEANLI 1750
    GTGTSEHWVD DEGPQPKKVK AEDEALLSEE DDPIDRRPWT QQHLEAADIR 1800
    RTPSLALTPP QAEQEVDVLD VNVRGPDGCT PLMLASLRGG SSDLSDEDED 1850
    AEDSSANIIT DLVYQGASLQ AQTDRTGEMA LHLAARYSRA DAAKRLLDAG 1900
    ADANAQDNMG RCPLHAAVAA DAQGVFQILI RNRVTDLDAR MNDGTTPLIL 1950
    AARLAVEGMV AELINCQADV NAVDDHGKSA LHWAAAVNNV EATLLLLKNG 2000
    ANRDMQDNKE ETPLFLAARE GSYEAAKILL DHFANRDITD HMDRLPRDVA 2050
    RDRMHHDIVR LLDEYNVTPS PPGTVLTSAL SPVICGPNRS FLSLKHTPMG 2100
    KKSRRPSAKS TMPTSLPNLA KEAKDAKGSR RKKSLSEKVQ LSESSVTLSP 2150
    VDSLESPHTY VSDTTSSPMI TSPGILQASP NPMLATAAPP APVHAQHALS 2200
    FSNLHEMQPL AHGASTVLPS VSQLLSHHHI VSPGSGSAGS LSRLHPVPVP 2250
    ADWMNRMEVN ETQYNEMFGM VLAPAEGTHP GIAPQSRPPE GKHITTPREP 2300
    LPPIVTFQLI PKGSIAQPAG APQPQSTCPP AVAGPLPTMY QIPEMARLPS 2350
    VAFPTAMMPQ QDGQVAQTIL PAYHPFPASV GKYPTPPSQH SYASSNAAER 2400
    TPSHSGHLQG EHPYLTPSPE SPDQWSSSSP HSASDWSDVT TSPTPGGAGG 2450
    GQRGPGTHMS EPPHNNMQVY A 2471
    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 34-1376, 1425-1672, 1777-2063.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 110915. 25 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.
    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

    ArrayExpressi Q04721.
    Bgeei Q04721.
    CleanExi HS_NOTCH2.
    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

    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 1, 2014
    This is version 173 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