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O35516

- NOTC2_MOUSE

UniProt

O35516 - NOTC2_MOUSE

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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

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

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
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_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.

Topology

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Topological domaini26 – 16771652ExtracellularSequence AnalysisAdd
BLAST
Transmembranei1678 – 169821HelicalSequence AnalysisAdd
BLAST
Topological domaini1699 – 2470772CytoplasmicSequence AnalysisAdd
BLAST

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
Complete GO annotation...

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

MaxQBiO35516.
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, 1423-1669, 1777-2061.
ModBaseiSearch...
MobiDBiSearch...

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.

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        10         20         30         40         50
MPDLRPAALR ALLWLWLCGA GPAHALQCRG GQEPCVNEGT CVTYHNGTGF
60 70 80 90 100
CRCPEGFLGE YCQHRDPCEK NRCQNGGTCV PQGMLGKATC RCAPGFTGED
110 120 130 140 150
CQYSTSHPCF VSRPCQNGGT CHMLSRDTYE CTCQVGFTGK QCQWTDACLS
160 170 180 190 200
HPCENGSTCT SVASQFSCKC PAGLTGQKCE ADINECDIPG RCQHGGTCLN
210 220 230 240 250
LPGSYRCQCG QGFTGQHCDS PYVRGLPCVN GGTCRQTGDF TLECNCLPGF
260 270 280 290 300
EGSTCERNID DCPNHKCQNG GVCVDGVNTY NCRCPPQWTG QFCTEDVDEC
310 320 330 340 350
LLQPNACQNG GTCTNRNGGY GCVCVNGWSG DDCSENIDDC AYASCTPGST
360 370 380 390 400
CIDRVASFSC LCPEGKAGLL CHLDDACISN PCHKGALCDT NPLNGQYICT
410 420 430 440 450
CPQGYKGADC TEDVDECAMA NSNPCEHAGK CVNTDGAFHC ECLKGYAGPR
460 470 480 490 500
CEMDINECHS DPCQNDATCL DKIGGFTCLC MPGFKGVHCE LEVNECQSNP
510 520 530 540 550
CVNNGQCVDK VNRFQCLCPP GFTGPVCQID IDDCSSTPCL NGAKCIDHPN
560 570 580 590 600
GYECQCATGF TGILCDENID NCDPDPCHHG QCQDGIDSYT CICNPGYMGA
610 620 630 640 650
ICSDQIDECY SSPCLNDGRC IDLVNGYQCN CQPGTSGLNC EINFDDCASN
660 670 680 690 700
PCMHGVCVDG INRYSCVCSP GFTGQRCNID IDECASNPCR KGATCINDVN
710 720 730 740 750
GFRCICPEGP HHPSCYSQVN ECLSNPCIHG NCTGGLSGYK CLCDAGWVGV
760 770 780 790 800
NCEVDKNECL SNPCQNGGTC NNLVNGYRCT CKKGFKGYNC QVNIDECASN
810 820 830 840 850
PCLNQGTCFD DVSGYTCHCM LPYTGKNCQT VLAPCSPNPC ENAAVCKEAP
860 870 880 890 900
NFESFSCLCA PGWQGKRCTV DVDECISKPC MNNGVCHNTQ GSYVCECPPG
910 920 930 940 950
FSGMDCEEDI NDCLANPCQN GGSCVDHVNT FSCQCHPGFI GDKCQTDMNE
960 970 980 990 1000
CLSEPCKNGG TCSDYVNSYT CTCPAGFHGV HCENNIDECT ESSCFNGGTC
1010 1020 1030 1040 1050
VDGINSFSCL CPVGFTGPFC LHDINECSSN PCLNAGTCVD GLGTYRCICP
1060 1070 1080 1090 1100
LGYTGKNCQT LVNLCSRSPC KNKGTCVQEK ARPHCLCPPG WDGAYCDVLN
1110 1120 1130 1140 1150
VSCKAAALQK GVPVEHLCQH SGICINAGNT HHCQCPLGYT GSYCEEQLDE
1160 1170 1180 1190 1200
CASNPCQHGA TCNDFIGGYR CECVPGYQGV NCEYEVDECQ NQPCQNGGTC
1210 1220 1230 1240 1250
IDLVNHFKCS CPPGTRGLLC EENIDECAGG PHCLNGGQCV DRIGGYTCRC
1260 1270 1280 1290 1300
LPGFAGERCE GDINECLSNP CSSEGSLDCV QLKNNYNCIC RSAFTGRHCE
1310 1320 1330 1340 1350
TFLDVCPQKP CLNGGTCAVA SNMPDGFICR CPPGFSGARL QSSCGQVKCR
1360 1370 1380 1390 1400
RGEQCIHTDS GPRCFCLNPK DCESGCASNP CQHGGTCYPQ RQPPHYSCRC
1410 1420 1430 1440 1450
PPSFGGSHCE LYTAPTSTPP ATCQSQYCAD KARDGICDEA CNSHACQWDG
1460 1470 1480 1490 1500
GDCSLTMEDP WANCTSTLRC WEYINNQCDE QCNTAECLFD NFECQRNSKT
1510 1520 1530 1540 1550
CKYDKYCADH FKDNHCDQGC NSEECGWDGL DCASDQPENL AEGTLIIVVL
1560 1570 1580 1590 1600
LPPEQLLQDS RSFLRALGTL LHTNLRIKQD SQGALMVYPY FGEKSAAMKK
1610 1620 1630 1640 1650
QKMTRRSLPE EQEQEQEVIG SKIFLEIDNR QCVQDSDQCF KNTDAAAALL
1660 1670 1680 1690 1700
ASHAIQGTLS YPLVSVFSEL ESPRNAQLLY LLAVAVVIIL FFILLGVIMA
1710 1720 1730 1740 1750
KRKQAWLPLA AGRFTLRRDS SNHKRREPVG QDAVGLKNLS VQVSEANLIG
1760 1770 1780 1790 1800
SGTSEHWVDD EGPQPKKAKA EDEALLSEDD PIDRRPWTQQ HLEAADISHT
1810 1820 1830 1840 1850
PSLALTPPQA EQEVDVLDVN VRGPDGCTPL MLASLRGGSS DLSDEDEDAE
1860 1870 1880 1890 1900
DSSANIITDL VYQGASLQAQ TDRTGEMALH LAARYSRADA AKRLLDAGAD
1910 1920 1930 1940 1950
RNAQDNMGRC PLHAAVAGDA QGVFQILIRN RVTDLDARMN DGTTPLILAA
1960 1970 1980 1990 2000
RLAVEGMVAE LINCQADVNA VDDHGKSALH WAAAVNNVEA TLLLLKNGAN
2010 2020 2030 2040 2050
RDMQDNKEET PLFLAAREGS YEAAKILLDH FANRDITDHM DRLPRDVARD
2060 2070 2080 2090 2100
RMHHDIVRLL DEYNVTPSPP GTVLTSALSP VLCGPNRSFL SLKHTPMGKK
2110 2120 2130 2140 2150
ARRPNTKSTM PTSLPNLAKE AKDAKGSRRK KCLNEKVQLS ESSVTLSPVD
2160 2170 2180 2190 2200
SLESPHTYVS DATSSPMITS PGILQASPTP LLAAAAPAAP VHTQHALSFS
2210 2220 2230 2240 2250
NLHDMQPLAP GASTVLPSVS QLLSHHHIAP PGSSSAGSLG RLHPVPVPAD
2260 2270 2280 2290 2300
WMNRVEMNET QYSEMFGMVL APAEGAHPGI AAPQSRPPEG KHMSTQREPL
2310 2320 2330 2340 2350
PPIVTFQLIP KRSIAQAAGA PQTQSSCPPA VAGPLPSMYQ IPEMPRLPSV
2360 2370 2380 2390 2400
AFPPTMMPQQ EGQVAQTIVP TYHPFPASVG KYPTPPSQHS YASSNAAERT
2410 2420 2430 2440 2450
PSHGGHLQGE HPYLTPSPES PDQWSSSSPH SASDWSDVTT SPTPGGGGGG
2460 2470
QRGPGTHMSE PPHSNMQVYA
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:
EMBLi
GenBanki
DDBJi
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:
EMBLi
GenBanki
DDBJi
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, 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

MaxQBi O35516.
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

« Hide 'large scale' publications
  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: November 26, 2014
This is version 158 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