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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.2 Publications

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sitei612 – 6121Essential for O-xylosylation

GO - Molecular functioni

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

GO - Biological processi

  1. Notch signaling pathway Source: UniProtKB
  2. atrial septum morphogenesis Source: BHF-UCL
  3. cell cycle arrest Source: UniProtKB
  4. cell fate determination Source: UniProtKB
  5. cell growth Source: UniProtKB
  6. ciliary body morphogenesis 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. in utero embryonic development Source: MGI
  14. inflammatory response to antigenic stimulus Source: MGI
  15. interleukin-4 secretion Source: MGI
  16. left/right axis specification Source: BHF-UCL
  17. morphogenesis of an epithelial sheet Source: MGI
  18. negative regulation of cell proliferation Source: UniProtKB
  19. negative regulation of transcription from RNA polymerase II promoter Source: MGI
  20. organ morphogenesis Source: UniProtKB
  21. placenta blood vessel development Source: MGI
  22. placenta development Source: MGI
  23. positive regulation of BMP signaling pathway Source: MGI
  24. positive regulation of Ras protein signal transduction Source: UniProtKB
  25. positive regulation of apoptotic process Source: MGI
  26. positive regulation of cell proliferation Source: MGI
  27. positive regulation of osteoclast differentiation Source: UniProtKB
  28. proximal tubule development Source: UniProtKB
  29. transcription, DNA-templated Source: UniProtKB-KW
  30. 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 – 16771652Extracellular Reviewed prediction
Add
BLAST
Transmembranei1678 – 169821Helical; Reviewed prediction
Add
BLAST
Topological domaini1699 – 2470772Cytoplasmic Reviewed prediction
Add
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 – 2525 Reviewed prediction
Add
BLAST
Chaini26 – 24702445Neurogenic locus notch homolog protein 2
PRO_0000007686Add
BLAST
Chaini1666 – 2470805Notch 2 extracellular truncation
PRO_0000007687Add
BLAST
Chaini1697 – 2470774Notch 2 intracellular domain
PRO_0000007688Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Disulfide bondi28 ↔ 41 By similarity
Disulfide bondi35 ↔ 51 By similarity
Glycosylationi46 – 461N-linked (GlcNAc...) Reviewed prediction
Disulfide bondi53 ↔ 62 By similarity
Disulfide bondi68 ↔ 79 By similarity
Disulfide bondi73 ↔ 90 By similarity
Disulfide bondi92 ↔ 101 By similarity
Disulfide bondi109 ↔ 121 By similarity
Disulfide bondi115 ↔ 131 By similarity
Disulfide bondi133 ↔ 142 By similarity
Disulfide bondi148 ↔ 159 By similarity
Disulfide bondi153 ↔ 168 By similarity
Glycosylationi155 – 1551N-linked (GlcNAc...) Reviewed prediction
Disulfide bondi170 ↔ 179 By similarity
Disulfide bondi186 ↔ 198 By similarity
Disulfide bondi192 ↔ 207 By similarity
Disulfide bondi209 ↔ 218 By similarity
Disulfide bondi228 ↔ 244 By similarity
Disulfide bondi246 ↔ 255 By similarity
Disulfide bondi262 ↔ 273 By similarity
Disulfide bondi267 ↔ 282 By similarity
Disulfide bondi284 ↔ 293 By similarity
Disulfide bondi300 ↔ 313 By similarity
Disulfide bondi307 ↔ 322 By similarity
Disulfide bondi324 ↔ 333 By similarity
Disulfide bondi340 ↔ 351 By similarity
Disulfide bondi345 ↔ 360 By similarity
Disulfide bondi362 ↔ 371 By similarity
Disulfide bondi377 ↔ 388 By similarity
Disulfide bondi382 ↔ 399 By similarity
Disulfide bondi401 ↔ 410 By similarity
Disulfide bondi417 ↔ 431 By similarity
Disulfide bondi425 ↔ 440 By similarity
Disulfide bondi442 ↔ 451 By similarity
Disulfide bondi458 ↔ 469 By similarity
Disulfide bondi463 ↔ 478 By similarity
Disulfide bondi480 ↔ 489 By similarity
Disulfide bondi496 ↔ 507 By similarity
Disulfide bondi501 ↔ 516 By similarity
Disulfide bondi518 ↔ 527 By similarity
Disulfide bondi534 ↔ 545 By similarity
Disulfide bondi539 ↔ 554 By similarity
Disulfide bondi556 ↔ 565 By similarity
Disulfide bondi572 ↔ 582 By similarity
Disulfide bondi577 ↔ 591 By similarity
Disulfide bondi593 ↔ 602 By similarity
Disulfide bondi609 ↔ 620 By similarity
Glycosylationi611 – 6111O-linked (Glc...); alternate1 Publication
Glycosylationi611 – 6111O-linked (Xyl...); alternate1 Publication
Disulfide bondi614 ↔ 629 By similarity
Disulfide bondi631 ↔ 640 By similarity
Disulfide bondi647 ↔ 657 By similarity
Disulfide bondi652 ↔ 666 By similarity
Disulfide bondi668 ↔ 677 By similarity
Disulfide bondi684 ↔ 695 By similarity
Disulfide bondi689 ↔ 704 By similarity
Disulfide bondi706 ↔ 715 By similarity
Disulfide bondi722 ↔ 732 By similarity
Disulfide bondi727 ↔ 741 By similarity
Glycosylationi731 – 7311N-linked (GlcNAc...) Reviewed prediction
Disulfide bondi743 ↔ 752 By similarity
Disulfide bondi759 ↔ 770 By similarity
Disulfide bondi764 ↔ 779 By similarity
Disulfide bondi781 ↔ 790 By similarity
Disulfide bondi797 ↔ 808 By similarity
Disulfide bondi802 ↔ 817 By similarity
Disulfide bondi819 ↔ 828 By similarity
Disulfide bondi835 ↔ 846 By similarity
Disulfide bondi840 ↔ 857 By similarity
Disulfide bondi859 ↔ 868 By similarity
Disulfide bondi875 ↔ 886 By similarity
Disulfide bondi880 ↔ 895 By similarity
Disulfide bondi897 ↔ 906 By similarity
Disulfide bondi913 ↔ 924 By similarity
Disulfide bondi918 ↔ 933 By similarity
Disulfide bondi935 ↔ 944 By similarity
Disulfide bondi951 ↔ 962 By similarity
Disulfide bondi956 ↔ 971 By similarity
Disulfide bondi973 ↔ 982 By similarity
Disulfide bondi989 ↔ 1000 By similarity
Disulfide bondi994 ↔ 1009 By similarity
Disulfide bondi1011 ↔ 1020 By similarity
Disulfide bondi1027 ↔ 1038 By similarity
Disulfide bondi1032 ↔ 1047 By similarity
Disulfide bondi1049 ↔ 1058 By similarity
Disulfide bondi1065 ↔ 1076 By similarity
Disulfide bondi1070 ↔ 1085 By similarity
Disulfide bondi1087 ↔ 1096 By similarity
Glycosylationi1100 – 11001N-linked (GlcNAc...) Reviewed prediction
Disulfide bondi1103 ↔ 1124 By similarity
Disulfide bondi1118 ↔ 1133 By similarity
Disulfide bondi1135 ↔ 1144 By similarity
Disulfide bondi1151 ↔ 1162 By similarity
Disulfide bondi1156 ↔ 1171 By similarity
Disulfide bondi1173 ↔ 1182 By similarity
Disulfide bondi1189 ↔ 1200 By similarity
Disulfide bondi1194 ↔ 1209 By similarity
Disulfide bondi1211 ↔ 1220 By similarity
Disulfide bondi1227 ↔ 1239 By similarity
Disulfide bondi1233 ↔ 1248 By similarity
Disulfide bondi1250 ↔ 1259 By similarity
Disulfide bondi1266 ↔ 1279 By similarity
Disulfide bondi1271 ↔ 1288 By similarity
Disulfide bondi1290 ↔ 1299 By similarity
Disulfide bondi1306 ↔ 1317 By similarity
Disulfide bondi1311 ↔ 1329 By similarity
Disulfide bondi1331 ↔ 1344 By similarity
Disulfide bondi1376 ↔ 1387 By similarity
Disulfide bondi1381 ↔ 1398 By similarity
Disulfide bondi1400 ↔ 1409 By similarity
Disulfide bondi1423 ↔ 1446 By similarity
Disulfide bondi1428 ↔ 1441 By similarity
Disulfide bondi1437 ↔ 1453 By similarity
Glycosylationi1463 – 14631N-linked (GlcNAc...) Reviewed prediction
Disulfide bondi1464 ↔ 1487 By similarity
Disulfide bondi1470 ↔ 1482 By similarity
Disulfide bondi1478 ↔ 1494 By similarity
Disulfide bondi1501 ↔ 1525 By similarity
Disulfide bondi1507 ↔ 1520 By similarity
Disulfide bondi1516 ↔ 1532 By similarity
Disulfide bondi1632 ↔ 1639 By similarity
Modified residuei1715 – 17151Phosphothreonine By similarity
Modified residuei1777 – 17771Phosphoserine1 Publication
Modified residuei1800 – 18001Phosphothreonine By similarity
Modified residuei1802 – 18021Phosphoserine By similarity
Modified residuei1806 – 18061Phosphothreonine By similarity
Modified residuei1840 – 18401Phosphoserine1 Publication
Modified residuei1843 – 18431Phosphoserine1 Publication
Modified residuei2068 – 20681Phosphoserine By similarity
Modified residuei2076 – 20761Phosphoserine By similarity
Modified residuei2079 – 20791Phosphoserine By similarity
Modified residuei2095 – 20951Phosphothreonine By 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.
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.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini26 – 6338EGF-like 1
Add
BLAST
Domaini64 – 10239EGF-like 2
Add
BLAST
Domaini105 – 14339EGF-like 3
Add
BLAST
Domaini144 – 18037EGF-like 4
Add
BLAST
Domaini182 – 21938EGF-like 5; calcium-binding Reviewed prediction
Add
BLAST
Domaini221 – 25636EGF-like 6; incomplete
Add
BLAST
Domaini258 – 29437EGF-like 7; calcium-binding Reviewed prediction
Add
BLAST
Domaini296 – 33439EGF-like 8; calcium-binding Reviewed prediction
Add
BLAST
Domaini336 – 37237EGF-like 9; calcium-binding Reviewed prediction
Add
BLAST
Domaini373 – 41139EGF-like 10
Add
BLAST
Domaini413 – 45240EGF-like 11; calcium-binding Reviewed prediction
Add
BLAST
Domaini454 – 49037EGF-like 12; calcium-binding Reviewed prediction
Add
BLAST
Domaini492 – 52837EGF-like 13; calcium-binding Reviewed prediction
Add
BLAST
Domaini530 – 56637EGF-like 14; calcium-binding Reviewed prediction
Add
BLAST
Domaini568 – 60336EGF-like 15; calcium-binding Reviewed prediction
Add
BLAST
Domaini605 – 64137EGF-like 16; calcium-binding Reviewed prediction
Add
BLAST
Domaini643 – 67836EGF-like 17; calcium-binding Reviewed prediction
Add
BLAST
Domaini680 – 71637EGF-like 18; calcium-binding Reviewed prediction
Add
BLAST
Domaini718 – 75336EGF-like 19
Add
BLAST
Domaini755 – 79137EGF-like 20; calcium-binding Reviewed prediction
Add
BLAST
Domaini793 – 82937EGF-like 21; calcium-binding Reviewed prediction
Add
BLAST
Domaini831 – 86939EGF-like 22
Add
BLAST
Domaini871 – 90737EGF-like 23; calcium-binding Reviewed prediction
Add
BLAST
Domaini909 – 94537EGF-like 24; calcium-binding Reviewed prediction
Add
BLAST
Domaini947 – 98337EGF-like 25; calcium-binding Reviewed prediction
Add
BLAST
Domaini985 – 102137EGF-like 26; calcium-binding Reviewed prediction
Add
BLAST
Domaini1023 – 105937EGF-like 27; calcium-binding Reviewed prediction
Add
BLAST
Domaini1061 – 109737EGF-like 28
Add
BLAST
Domaini1099 – 114547EGF-like 29
Add
BLAST
Domaini1147 – 118337EGF-like 30; calcium-binding Reviewed prediction
Add
BLAST
Domaini1185 – 122137EGF-like 31; calcium-binding Reviewed prediction
Add
BLAST
Domaini1223 – 126038EGF-like 32; calcium-binding Reviewed prediction
Add
BLAST
Domaini1262 – 130039EGF-like 33
Add
BLAST
Domaini1302 – 134544EGF-like 34
Add
BLAST
Domaini1372 – 141039EGF-like 35
Add
BLAST
Repeati1423 – 146341LNR 1
Add
BLAST
Repeati1464 – 150037LNR 2
Add
BLAST
Repeati1501 – 154242LNR 3
Add
BLAST
Repeati1825 – 186945ANK 1
Add
BLAST
Repeati1874 – 190330ANK 2
Add
BLAST
Repeati1907 – 193731ANK 3
Add
BLAST
Repeati1941 – 197030ANK 4
Add
BLAST
Repeati1974 – 200330ANK 5
Add
BLAST
Repeati2007 – 203630ANK 6
Add
BLAST

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni1423 – 1677255Negative regulatory region (NRR) By similarity
Add
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.
Contains 6 ANK repeats.
Contains 35 EGF-like domains.

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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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

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei1302 – 1508207Missing in isoform 2.
VSP_001405Add
BLAST

Sequence conflict

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti1340 – 13401L → C in CAA48340. 1 Publication
Sequence conflicti1798 – 17981S → R in AAC52924. 1 Publication
Sequence conflicti1901 – 19011R → A in AAC52924. 1 Publication
Sequence conflicti1918 – 19181G → A in AAC52924. 1 Publication

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

« 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: September 3, 2014
This is version 155 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

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