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O35516

- NOTC2_MOUSE

UniProt

O35516 - NOTC2_MOUSE

Protein

Neurogenic locus notch homolog protein 2

Gene

Notch2

Organism
Mus musculus (Mouse)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 156 (01 Oct 2014)
      Sequence version 1 (01 Jan 1998)
      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. May play an essential role in postimplantation development, probably in some aspect of cell specification and/or differentiation. 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
    Sitei612 – 6121Essential for O-xylosylation

    GO - Molecular functioni

    1. calcium ion binding Source: InterPro
    2. enzyme binding Source: UniProtKB
    3. NF-kappaB binding Source: UniProtKB
    4. protein binding Source: UniProtKB

    GO - Biological processi

    1. atrial septum morphogenesis Source: BHF-UCL
    2. cell cycle arrest Source: UniProtKB
    3. cell fate determination Source: UniProtKB
    4. cell growth Source: UniProtKB
    5. ciliary body morphogenesis Source: MGI
    6. defense response to bacterium Source: MGI
    7. determination of left/right symmetry Source: MGI
    8. embryonic limb morphogenesis Source: MGI
    9. glomerular capillary formation Source: UniProtKB
    10. glomerular visceral epithelial cell development Source: UniProtKB
    11. heart looping Source: BHF-UCL
    12. humoral immune response Source: MGI
    13. inflammatory response to antigenic stimulus Source: MGI
    14. interleukin-4 secretion Source: MGI
    15. in utero embryonic development Source: MGI
    16. left/right axis specification Source: BHF-UCL
    17. morphogenesis of an epithelial sheet Source: MGI
    18. myeloid dendritic cell differentiation Source: MGI
    19. negative regulation of cell proliferation Source: UniProtKB
    20. negative regulation of transcription from RNA polymerase II promoter Source: MGI
    21. Notch signaling pathway Source: UniProtKB
    22. organ morphogenesis Source: UniProtKB
    23. placenta blood vessel development Source: MGI
    24. placenta development Source: MGI
    25. positive regulation of apoptotic process Source: MGI
    26. positive regulation of BMP signaling pathway Source: MGI
    27. positive regulation of cell proliferation Source: MGI
    28. positive regulation of osteoclast differentiation Source: UniProtKB
    29. positive regulation of Ras protein signal transduction Source: UniProtKB
    30. proximal tubule development Source: UniProtKB
    31. transcription, DNA-templated Source: UniProtKB-KW
    32. wound healing Source: UniProtKB

    Keywords - Molecular functioni

    Activator, Developmental protein, Receptor

    Keywords - Biological processi

    Differentiation, Notch signaling pathway, Transcription, Transcription regulation

    Enzyme and pathway databases

    ReactomeiREACT_196492. Pre-NOTCH Processing in the Endoplasmic Reticulum.
    REACT_196517. Pre-NOTCH Processing in Golgi.
    REACT_196593. NOTCH2 intracellular domain regulates transcription.
    REACT_199411. NOTCH2 Activation and Transmission of Signal to the Nucleus.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Neurogenic locus notch homolog protein 2
    Short name:
    Notch 2
    Alternative name(s):
    Motch B
    Cleaved into the following 2 chains:
    Gene namesi
    Name:Notch2
    OrganismiMus musculus (Mouse)
    Taxonomic identifieri10090 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
    ProteomesiUP000000589: Unplaced

    Organism-specific databases

    MGIiMGI:97364. 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: MGI
    3. cytosol Source: Reactome
    4. extracellular region Source: Reactome
    5. integral component of plasma membrane Source: UniProtKB
    6. nucleoplasm Source: Reactome
    7. nucleus Source: UniProtKB
    8. plasma membrane Source: Reactome
    9. receptor complex Source: MGI

    Keywords - Cellular componenti

    Cell membrane, Membrane, Nucleus

    Pathology & Biotechi

    Mutagenesis

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Mutagenesisi612 – 6121S → A: No effect on O-glycosylation by POGLUT1. Loss of O-xylosylation. 1 Publication
    Mutagenesisi1699 – 16991M → L: No effect on NICD processing. 2 Publications
    Mutagenesisi1699 – 16991M → V: Decreased NICD processing. 2 Publications

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Signal peptidei1 – 2525Sequence AnalysisAdd
    BLAST
    Chaini26 – 24702445Neurogenic locus notch homolog protein 2PRO_0000007686Add
    BLAST
    Chaini1666 – 2470805Notch 2 extracellular truncationPRO_0000007687Add
    BLAST
    Chaini1697 – 2470774Notch 2 intracellular domainPRO_0000007688Add
    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 bondi228 ↔ 244By similarity
    Disulfide bondi246 ↔ 255By similarity
    Disulfide bondi262 ↔ 273By similarity
    Disulfide bondi267 ↔ 282By similarity
    Disulfide bondi284 ↔ 293By similarity
    Disulfide bondi300 ↔ 313By similarity
    Disulfide bondi307 ↔ 322By similarity
    Disulfide bondi324 ↔ 333By similarity
    Disulfide bondi340 ↔ 351By similarity
    Disulfide bondi345 ↔ 360By similarity
    Disulfide bondi362 ↔ 371By similarity
    Disulfide bondi377 ↔ 388By similarity
    Disulfide bondi382 ↔ 399By similarity
    Disulfide bondi401 ↔ 410By similarity
    Disulfide bondi417 ↔ 431By similarity
    Disulfide bondi425 ↔ 440By similarity
    Disulfide bondi442 ↔ 451By similarity
    Disulfide bondi458 ↔ 469By similarity
    Disulfide bondi463 ↔ 478By similarity
    Disulfide bondi480 ↔ 489By similarity
    Disulfide bondi496 ↔ 507By similarity
    Disulfide bondi501 ↔ 516By similarity
    Disulfide bondi518 ↔ 527By similarity
    Disulfide bondi534 ↔ 545By similarity
    Disulfide bondi539 ↔ 554By similarity
    Disulfide bondi556 ↔ 565By similarity
    Disulfide bondi572 ↔ 582By similarity
    Disulfide bondi577 ↔ 591By similarity
    Disulfide bondi593 ↔ 602By similarity
    Disulfide bondi609 ↔ 620By similarity
    Glycosylationi611 – 6111O-linked (Glc...); alternate1 Publication
    Glycosylationi611 – 6111O-linked (Xyl...); alternate1 Publication
    Disulfide bondi614 ↔ 629By similarity
    Disulfide bondi631 ↔ 640By similarity
    Disulfide bondi647 ↔ 657By similarity
    Disulfide bondi652 ↔ 666By similarity
    Disulfide bondi668 ↔ 677By similarity
    Disulfide bondi684 ↔ 695By similarity
    Disulfide bondi689 ↔ 704By similarity
    Disulfide bondi706 ↔ 715By similarity
    Disulfide bondi722 ↔ 732By similarity
    Disulfide bondi727 ↔ 741By similarity
    Glycosylationi731 – 7311N-linked (GlcNAc...)Sequence Analysis
    Disulfide bondi743 ↔ 752By similarity
    Disulfide bondi759 ↔ 770By similarity
    Disulfide bondi764 ↔ 779By similarity
    Disulfide bondi781 ↔ 790By similarity
    Disulfide bondi797 ↔ 808By similarity
    Disulfide bondi802 ↔ 817By similarity
    Disulfide bondi819 ↔ 828By similarity
    Disulfide bondi835 ↔ 846By similarity
    Disulfide bondi840 ↔ 857By similarity
    Disulfide bondi859 ↔ 868By similarity
    Disulfide bondi875 ↔ 886By similarity
    Disulfide bondi880 ↔ 895By similarity
    Disulfide bondi897 ↔ 906By similarity
    Disulfide bondi913 ↔ 924By similarity
    Disulfide bondi918 ↔ 933By similarity
    Disulfide bondi935 ↔ 944By similarity
    Disulfide bondi951 ↔ 962By similarity
    Disulfide bondi956 ↔ 971By similarity
    Disulfide bondi973 ↔ 982By similarity
    Disulfide bondi989 ↔ 1000By similarity
    Disulfide bondi994 ↔ 1009By similarity
    Disulfide bondi1011 ↔ 1020By similarity
    Disulfide bondi1027 ↔ 1038By similarity
    Disulfide bondi1032 ↔ 1047By similarity
    Disulfide bondi1049 ↔ 1058By similarity
    Disulfide bondi1065 ↔ 1076By similarity
    Disulfide bondi1070 ↔ 1085By similarity
    Disulfide bondi1087 ↔ 1096By similarity
    Glycosylationi1100 – 11001N-linked (GlcNAc...)Sequence Analysis
    Disulfide bondi1103 ↔ 1124By similarity
    Disulfide bondi1118 ↔ 1133By similarity
    Disulfide bondi1135 ↔ 1144By similarity
    Disulfide bondi1151 ↔ 1162By similarity
    Disulfide bondi1156 ↔ 1171By similarity
    Disulfide bondi1173 ↔ 1182By similarity
    Disulfide bondi1189 ↔ 1200By similarity
    Disulfide bondi1194 ↔ 1209By similarity
    Disulfide bondi1211 ↔ 1220By similarity
    Disulfide bondi1227 ↔ 1239By similarity
    Disulfide bondi1233 ↔ 1248By similarity
    Disulfide bondi1250 ↔ 1259By similarity
    Disulfide bondi1266 ↔ 1279By similarity
    Disulfide bondi1271 ↔ 1288By similarity
    Disulfide bondi1290 ↔ 1299By similarity
    Disulfide bondi1306 ↔ 1317By similarity
    Disulfide bondi1311 ↔ 1329By similarity
    Disulfide bondi1331 ↔ 1344By similarity
    Disulfide bondi1376 ↔ 1387By similarity
    Disulfide bondi1381 ↔ 1398By similarity
    Disulfide bondi1400 ↔ 1409By similarity
    Disulfide bondi1423 ↔ 1446By similarity
    Disulfide bondi1428 ↔ 1441By similarity
    Disulfide bondi1437 ↔ 1453By similarity
    Glycosylationi1463 – 14631N-linked (GlcNAc...)Sequence Analysis
    Disulfide bondi1464 ↔ 1487By similarity
    Disulfide bondi1470 ↔ 1482By similarity
    Disulfide bondi1478 ↔ 1494By similarity
    Disulfide bondi1501 ↔ 1525By similarity
    Disulfide bondi1507 ↔ 1520By similarity
    Disulfide bondi1516 ↔ 1532By similarity
    Disulfide bondi1632 ↔ 1639By similarity
    Modified residuei1715 – 17151PhosphothreonineBy similarity
    Modified residuei1777 – 17771Phosphoserine1 Publication
    Modified residuei1800 – 18001PhosphothreonineBy similarity
    Modified residuei1802 – 18021PhosphoserineBy similarity
    Modified residuei1806 – 18061PhosphothreonineBy similarity
    Modified residuei1840 – 18401Phosphoserine1 Publication
    Modified residuei1843 – 18431Phosphoserine1 Publication
    Modified residuei2068 – 20681PhosphoserineBy similarity
    Modified residuei2076 – 20761PhosphoserineBy similarity
    Modified residuei2079 – 20791PhosphoserineBy similarity
    Modified residuei2095 – 20951PhosphothreonineBy 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.2 Publications
    Hydroxylated by HIF1AN.1 Publication
    Can be either O-glucosylated or O-xylosylated at Ser-611 by POGLUT1.

    Keywords - PTMi

    Disulfide bond, Glycoprotein, Phosphoprotein

    Proteomic databases

    PaxDbiO35516.
    PRIDEiO35516.

    PTM databases

    PhosphoSiteiO35516.

    Expressioni

    Tissue specificityi

    Expressed in the brain, liver, kidney, neuroepithelia, somites, optic vesicles and branchial arches, but not heart.

    Developmental stagei

    Expressed in the embryonic ventricular zone, the postnatal ependymal cells, and the choroid plexus throughout embryonic and postnatal development.1 Publication

    Gene expression databases

    CleanExiMM_NOTCH2.
    GenevestigatoriO35516.

    Interactioni

    Subunit structurei

    Heterodimer of a C-terminal fragment N(TM) and an N-terminal fragment N(EC) which are probably linked by disulfide bonds. Interacts with MAML1, MAML2 and MAML3 which act as transcriptional coactivators for NOTCH2. Interacts with RELA/p65. Interacts with HIF1AN.3 Publications

    Protein-protein interaction databases

    BioGridi201809. 5 interactions.
    DIPiDIP-6008N.
    IntActiO35516. 1 interaction.

    Structurei

    3D structure databases

    ProteinModelPortaliO35516.
    SMRiO35516. Positions 27-1341, 1381-1410, 1423-1669, 1777-2061.
    ModBaseiSearch...
    MobiDBiSearch...

    Topological domain

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Topological domaini26 – 16771652ExtracellularSequence AnalysisAdd
    BLAST
    Topological domaini1699 – 2470772CytoplasmicSequence 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 – 25636EGF-like 6; incompletePROSITE-ProRule annotationAdd
    BLAST
    Domaini258 – 29437EGF-like 7; calcium-bindingPROSITE-ProRule annotationAdd
    BLAST
    Domaini296 – 33439EGF-like 8; calcium-bindingPROSITE-ProRule annotationAdd
    BLAST
    Domaini336 – 37237EGF-like 9; calcium-bindingPROSITE-ProRule annotationAdd
    BLAST
    Domaini373 – 41139EGF-like 10PROSITE-ProRule annotationAdd
    BLAST
    Domaini413 – 45240EGF-like 11; calcium-bindingPROSITE-ProRule annotationAdd
    BLAST
    Domaini454 – 49037EGF-like 12; calcium-bindingPROSITE-ProRule annotationAdd
    BLAST
    Domaini492 – 52837EGF-like 13; calcium-bindingPROSITE-ProRule annotationAdd
    BLAST
    Domaini530 – 56637EGF-like 14; calcium-bindingPROSITE-ProRule annotationAdd
    BLAST
    Domaini568 – 60336EGF-like 15; calcium-bindingPROSITE-ProRule annotationAdd
    BLAST
    Domaini605 – 64137EGF-like 16; calcium-bindingPROSITE-ProRule annotationAdd
    BLAST
    Domaini643 – 67836EGF-like 17; calcium-bindingPROSITE-ProRule annotationAdd
    BLAST
    Domaini680 – 71637EGF-like 18; calcium-bindingPROSITE-ProRule annotationAdd
    BLAST
    Domaini718 – 75336EGF-like 19PROSITE-ProRule annotationAdd
    BLAST
    Domaini755 – 79137EGF-like 20; calcium-bindingPROSITE-ProRule annotationAdd
    BLAST
    Domaini793 – 82937EGF-like 21; calcium-bindingPROSITE-ProRule annotationAdd
    BLAST
    Domaini831 – 86939EGF-like 22PROSITE-ProRule annotationAdd
    BLAST
    Domaini871 – 90737EGF-like 23; calcium-bindingPROSITE-ProRule annotationAdd
    BLAST
    Domaini909 – 94537EGF-like 24; calcium-bindingPROSITE-ProRule annotationAdd
    BLAST
    Domaini947 – 98337EGF-like 25; calcium-bindingPROSITE-ProRule annotationAdd
    BLAST
    Domaini985 – 102137EGF-like 26; calcium-bindingPROSITE-ProRule annotationAdd
    BLAST
    Domaini1023 – 105937EGF-like 27; calcium-bindingPROSITE-ProRule annotationAdd
    BLAST
    Domaini1061 – 109737EGF-like 28PROSITE-ProRule annotationAdd
    BLAST
    Domaini1099 – 114547EGF-like 29PROSITE-ProRule annotationAdd
    BLAST
    Domaini1147 – 118337EGF-like 30; calcium-bindingPROSITE-ProRule annotationAdd
    BLAST
    Domaini1185 – 122137EGF-like 31; calcium-bindingPROSITE-ProRule annotationAdd
    BLAST
    Domaini1223 – 126038EGF-like 32; calcium-bindingPROSITE-ProRule annotationAdd
    BLAST
    Domaini1262 – 130039EGF-like 33PROSITE-ProRule annotationAdd
    BLAST
    Domaini1302 – 134544EGF-like 34PROSITE-ProRule annotationAdd
    BLAST
    Domaini1372 – 141039EGF-like 35PROSITE-ProRule annotationAdd
    BLAST
    Repeati1423 – 146341LNR 1Add
    BLAST
    Repeati1464 – 150037LNR 2Add
    BLAST
    Repeati1501 – 154242LNR 3Add
    BLAST
    Repeati1825 – 186945ANK 1Add
    BLAST
    Repeati1874 – 190330ANK 2Add
    BLAST
    Repeati1907 – 193731ANK 3Add
    BLAST
    Repeati1941 – 197030ANK 4Add
    BLAST
    Repeati1974 – 200330ANK 5Add
    BLAST
    Repeati2007 – 203630ANK 6Add
    BLAST

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni1423 – 1677255Negative regulatory region (NRR)By similarityAdd
    BLAST

    Compositional bias

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Compositional biasi1645 – 16484Poly-Ala
    Compositional biasi1992 – 19954Poly-Leu
    Compositional biasi2183 – 21897Poly-Ala
    Compositional biasi2425 – 24284Poly-Ser
    Compositional biasi2445 – 24506Poly-Gly

    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.
    InParanoidiO35516.
    KOiK02599.
    PhylomeDBiO35516.

    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. 3 hits.
    PF12796. Ank_2. 1 hit.
    PF11936. DUF3454. 1 hit.
    PF00008. EGF. 23 hits.
    PF07645. EGF_CA. 6 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. 5 hits.
    SSF90193. SSF90193. 2 hits.
    PROSITEiPS50297. ANK_REP_REGION. 1 hit.
    PS50088. ANK_REPEAT. 4 hits.
    PS00010. ASX_HYDROXYL. 22 hits.
    PS00022. EGF_1. 33 hits.
    PS01186. EGF_2. 27 hits.
    PS50026. EGF_3. 35 hits.
    PS01187. EGF_CA. 22 hits.
    PS50258. LNR. 3 hits.
    [Graphical view]

    Sequences (2)i

    Sequence statusi: Complete.

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

    This entry describes 2 isoformsi produced by alternative splicing. Align

    Isoform 1 (identifier: O35516-1) [UniParc]FASTAAdd to Basket

    This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

    « Hide

    MPDLRPAALR ALLWLWLCGA GPAHALQCRG GQEPCVNEGT CVTYHNGTGF     50
    CRCPEGFLGE YCQHRDPCEK NRCQNGGTCV PQGMLGKATC RCAPGFTGED 100
    CQYSTSHPCF VSRPCQNGGT CHMLSRDTYE CTCQVGFTGK QCQWTDACLS 150
    HPCENGSTCT SVASQFSCKC PAGLTGQKCE ADINECDIPG RCQHGGTCLN 200
    LPGSYRCQCG QGFTGQHCDS PYVRGLPCVN GGTCRQTGDF TLECNCLPGF 250
    EGSTCERNID DCPNHKCQNG GVCVDGVNTY NCRCPPQWTG QFCTEDVDEC 300
    LLQPNACQNG GTCTNRNGGY GCVCVNGWSG DDCSENIDDC AYASCTPGST 350
    CIDRVASFSC LCPEGKAGLL CHLDDACISN PCHKGALCDT NPLNGQYICT 400
    CPQGYKGADC TEDVDECAMA NSNPCEHAGK CVNTDGAFHC ECLKGYAGPR 450
    CEMDINECHS DPCQNDATCL DKIGGFTCLC MPGFKGVHCE LEVNECQSNP 500
    CVNNGQCVDK VNRFQCLCPP GFTGPVCQID IDDCSSTPCL NGAKCIDHPN 550
    GYECQCATGF TGILCDENID NCDPDPCHHG QCQDGIDSYT CICNPGYMGA 600
    ICSDQIDECY SSPCLNDGRC IDLVNGYQCN CQPGTSGLNC EINFDDCASN 650
    PCMHGVCVDG INRYSCVCSP GFTGQRCNID IDECASNPCR KGATCINDVN 700
    GFRCICPEGP HHPSCYSQVN ECLSNPCIHG NCTGGLSGYK CLCDAGWVGV 750
    NCEVDKNECL SNPCQNGGTC NNLVNGYRCT CKKGFKGYNC QVNIDECASN 800
    PCLNQGTCFD DVSGYTCHCM LPYTGKNCQT VLAPCSPNPC ENAAVCKEAP 850
    NFESFSCLCA PGWQGKRCTV DVDECISKPC MNNGVCHNTQ GSYVCECPPG 900
    FSGMDCEEDI NDCLANPCQN GGSCVDHVNT FSCQCHPGFI GDKCQTDMNE 950
    CLSEPCKNGG TCSDYVNSYT CTCPAGFHGV HCENNIDECT ESSCFNGGTC 1000
    VDGINSFSCL CPVGFTGPFC LHDINECSSN PCLNAGTCVD GLGTYRCICP 1050
    LGYTGKNCQT LVNLCSRSPC KNKGTCVQEK ARPHCLCPPG WDGAYCDVLN 1100
    VSCKAAALQK GVPVEHLCQH SGICINAGNT HHCQCPLGYT GSYCEEQLDE 1150
    CASNPCQHGA TCNDFIGGYR CECVPGYQGV NCEYEVDECQ NQPCQNGGTC 1200
    IDLVNHFKCS CPPGTRGLLC EENIDECAGG PHCLNGGQCV DRIGGYTCRC 1250
    LPGFAGERCE GDINECLSNP CSSEGSLDCV QLKNNYNCIC RSAFTGRHCE 1300
    TFLDVCPQKP CLNGGTCAVA SNMPDGFICR CPPGFSGARL QSSCGQVKCR 1350
    RGEQCIHTDS GPRCFCLNPK DCESGCASNP CQHGGTCYPQ RQPPHYSCRC 1400
    PPSFGGSHCE LYTAPTSTPP ATCQSQYCAD KARDGICDEA CNSHACQWDG 1450
    GDCSLTMEDP WANCTSTLRC WEYINNQCDE QCNTAECLFD NFECQRNSKT 1500
    CKYDKYCADH FKDNHCDQGC NSEECGWDGL DCASDQPENL AEGTLIIVVL 1550
    LPPEQLLQDS RSFLRALGTL LHTNLRIKQD SQGALMVYPY FGEKSAAMKK 1600
    QKMTRRSLPE EQEQEQEVIG SKIFLEIDNR QCVQDSDQCF KNTDAAAALL 1650
    ASHAIQGTLS YPLVSVFSEL ESPRNAQLLY LLAVAVVIIL FFILLGVIMA 1700
    KRKQAWLPLA AGRFTLRRDS SNHKRREPVG QDAVGLKNLS VQVSEANLIG 1750
    SGTSEHWVDD EGPQPKKAKA EDEALLSEDD PIDRRPWTQQ HLEAADISHT 1800
    PSLALTPPQA EQEVDVLDVN VRGPDGCTPL MLASLRGGSS DLSDEDEDAE 1850
    DSSANIITDL VYQGASLQAQ TDRTGEMALH LAARYSRADA AKRLLDAGAD 1900
    RNAQDNMGRC PLHAAVAGDA QGVFQILIRN RVTDLDARMN DGTTPLILAA 1950
    RLAVEGMVAE LINCQADVNA VDDHGKSALH WAAAVNNVEA TLLLLKNGAN 2000
    RDMQDNKEET PLFLAAREGS YEAAKILLDH FANRDITDHM DRLPRDVARD 2050
    RMHHDIVRLL DEYNVTPSPP GTVLTSALSP VLCGPNRSFL SLKHTPMGKK 2100
    ARRPNTKSTM PTSLPNLAKE AKDAKGSRRK KCLNEKVQLS ESSVTLSPVD 2150
    SLESPHTYVS DATSSPMITS PGILQASPTP LLAAAAPAAP VHTQHALSFS 2200
    NLHDMQPLAP GASTVLPSVS QLLSHHHIAP PGSSSAGSLG RLHPVPVPAD 2250
    WMNRVEMNET QYSEMFGMVL APAEGAHPGI AAPQSRPPEG KHMSTQREPL 2300
    PPIVTFQLIP KRSIAQAAGA PQTQSSCPPA VAGPLPSMYQ IPEMPRLPSV 2350
    AFPPTMMPQQ EGQVAQTIVP TYHPFPASVG KYPTPPSQHS YASSNAAERT 2400
    PSHGGHLQGE HPYLTPSPES PDQWSSSSPH SASDWSDVTT SPTPGGGGGG 2450
    QRGPGTHMSE PPHSNMQVYA 2470
    Length:2,470
    Mass (Da):265,327
    Last modified:January 1, 1998 - v1
    Checksum:iB55A31B35242716D
    GO
    Isoform 2 (identifier: O35516-2) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         1302-1508: Missing.

    Note: No experimental confirmation available.

    Show »
    Length:2,263
    Mass (Da):242,663
    Checksum:i4EF13A99DB3647BC
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti1340 – 13401L → C in CAA48340. (PubMed:8440332)Curated
    Sequence conflicti1798 – 17981S → R in AAC52924. (PubMed:8917536)Curated
    Sequence conflicti1901 – 19011R → A in AAC52924. (PubMed:8917536)Curated
    Sequence conflicti1918 – 19181G → A in AAC52924. (PubMed:8917536)Curated

    Alternative sequence

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Alternative sequencei1302 – 1508207Missing in isoform 2. CuratedVSP_001405Add
    BLAST

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    D32210 mRNA. Translation: BAA22094.1.
    X68279 mRNA. Translation: CAA48340.1.
    U31881 mRNA. Translation: AAC52924.1.
    PIRiA49175.
    RefSeqiNP_035058.2. NM_010928.2.
    UniGeneiMm.485843.

    Genome annotation databases

    GeneIDi18129.
    KEGGimmu:18129.

    Keywords - Coding sequence diversityi

    Alternative splicing

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    D32210 mRNA. Translation: BAA22094.1 .
    X68279 mRNA. Translation: CAA48340.1 .
    U31881 mRNA. Translation: AAC52924.1 .
    PIRi A49175.
    RefSeqi NP_035058.2. NM_010928.2.
    UniGenei Mm.485843.

    3D structure databases

    ProteinModelPortali O35516.
    SMRi O35516. Positions 27-1341, 1381-1410, 1423-1669, 1777-2061.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 201809. 5 interactions.
    DIPi DIP-6008N.
    IntActi O35516. 1 interaction.

    PTM databases

    PhosphoSitei O35516.

    Proteomic databases

    PaxDbi O35516.
    PRIDEi O35516.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    GeneIDi 18129.
    KEGGi mmu:18129.

    Organism-specific databases

    CTDi 4853.
    MGIi MGI:97364. Notch2.

    Phylogenomic databases

    eggNOGi COG0666.
    HOGENOMi HOG000234369.
    HOVERGENi HBG052650.
    InParanoidi O35516.
    KOi K02599.
    PhylomeDBi O35516.

    Enzyme and pathway databases

    Reactomei REACT_196492. Pre-NOTCH Processing in the Endoplasmic Reticulum.
    REACT_196517. Pre-NOTCH Processing in Golgi.
    REACT_196593. NOTCH2 intracellular domain regulates transcription.
    REACT_199411. NOTCH2 Activation and Transmission of Signal to the Nucleus.

    Miscellaneous databases

    ChiTaRSi NOTCH2. mouse.
    NextBioi 293360.
    PROi O35516.
    SOURCEi Search...

    Gene expression databases

    CleanExi MM_NOTCH2.
    Genevestigatori O35516.

    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. 3 hits.
    PF12796. Ank_2. 1 hit.
    PF11936. DUF3454. 1 hit.
    PF00008. EGF. 23 hits.
    PF07645. EGF_CA. 6 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. 5 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. 33 hits.
    PS01186. EGF_2. 27 hits.
    PS50026. EGF_3. 35 hits.
    PS01187. EGF_CA. 22 hits.
    PS50258. LNR. 3 hits.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "Complete amino acid sequence and mutliform transcripts encoded by a single copy of mouse Notch2 gene."
      Hamada Y., Higuchi M., Tsujimoto Y.
      Submitted (JUL-1994) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [MRNA].
      Strain: C57BL/6.
      Tissue: Thymus.
    2. "Motch A and Motch B-two mouse Notch homologues coexpressed in a wide variety of tissues."
      Lardelli M., Lendahl U.
      Exp. Cell Res. 204:364-372(1993) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 316-1518.
      Strain: C57BL/6 X CBA.
      Tissue: Embryo.
    3. Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 1765-2153.
    4. "Mutation in ankyrin repeats of the mouse Notch2 gene induces early embryonic lethality."
      Hamada Y., Kadokawa Y., Okabe M., Ikawa M., Coleman J.R., Tsujimoto Y.
      Development 126:3415-3424(1999) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION.
    5. "Differential expression of Notch1 and Notch2 in developing and adult mouse brain."
      Higuchi M., Kiyama H., Hayakawa T., Hamada Y., Tsujimoto Y.
      Brain Res. Mol. Brain Res. 29:263-272(1995) [PubMed] [Europe PMC] [Abstract]
      Cited for: DEVELOPMENTAL STAGE, ALTERNATIVE SPLICING.
    6. "Murine notch homologs (N1-4) undergo presenilin-dependent proteolysis."
      Saxena M.T., Schroeter E.H., Mumm J.S., Kopan R.
      J. Biol. Chem. 276:40268-40273(2001) [PubMed] [Europe PMC] [Abstract]
      Cited for: PROTEOLYTIC PROCESSING, MUTAGENESIS OF MET-1699.
    7. "Conservation of the biochemical mechanisms of signal transduction among mammalian Notch family members."
      Mizutani T., Taniguchi Y., Aoki T., Hashimoto N., Honjo T.
      Proc. Natl. Acad. Sci. U.S.A. 98:9026-9031(2001) [PubMed] [Europe PMC] [Abstract]
      Cited for: PROTEOLYTIC PROCESSING, MUTAGENESIS OF MET-1699.
    8. "Cloning and functional characterization of the murine mastermind-like 1 (Maml1) gene."
      Wu L., Kobayashi K., Sun T., Gao P., Liu J., Nakamura M., Weisberg E., Mukhopadhyay N.K., Griffin J.D.
      Gene 328:153-165(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH MAML1.
    9. Cited for: INTERACTION WITH HIF1AN.
    10. "The association of Notch2 and NF-kappaB accelerates RANKL-induced osteoclastogenesis."
      Fukushima H., Nakao A., Okamoto F., Shin M., Kajiya H., Sakano S., Bigas A., Jimi E., Okabe K.
      Mol. Cell. Biol. 28:6402-6412(2008) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION AS POSITIVE REGULATOR OF OSTEOCLASTOGENESIS, INTERACTION WITH RELA.
    11. "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.
    12. "The phagosomal proteome in interferon-gamma-activated macrophages."
      Trost M., English L., Lemieux S., Courcelles M., Desjardins M., Thibault P.
      Immunity 30:143-154(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1777; SER-1840 AND SER-1843, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    13. Cited for: GLYCOSYLATION AT SER-611, MUTAGENESIS OF SER-612.

    Entry informationi

    Entry nameiNOTC2_MOUSE
    AccessioniPrimary (citable) accession number: O35516
    Secondary accession number(s): Q06008, Q60941
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: March 27, 2002
    Last sequence update: January 1, 1998
    Last modified: October 1, 2014
    This is version 156 of the entry and version 1 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programChordata Protein Annotation Program

    Miscellaneousi

    Keywords - Technical termi

    Complete proteome, Reference proteome

    Documents

    1. MGD cross-references
      Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
    2. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3