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O35516 (NOTC2_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Last modified June 11, 2014. Version 154. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Alt products·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Neurogenic locus notch homolog protein 2

Short name=Notch 2
Alternative name(s):
Motch B
Gene names
Name:Notch2
OrganismMus musculus (Mouse) [Reference proteome]
Taxonomic identifier10090 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus

Protein attributes

Sequence length2470 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

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. Ref.4 Ref.10

Subunit structure

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. Ref.8 Ref.9 Ref.10

Subcellular location

Cell membrane; Single-pass type I membrane protein.

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

Tissue specificity

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

Developmental stage

Expressed in the embryonic ventricular zone, the postnatal ependymal cells, and the choroid plexus throughout embryonic and postnatal development. Ref.5

Post-translational modification

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. Ref.6 Ref.7

Hydroxylated by HIF1AN.

Can be either O-glucosylated or O-xylosylated at Ser-611 by POGLUT1.

Sequence similarities

Belongs to the NOTCH family.

Contains 6 ANK repeats.

Contains 35 EGF-like domains.

Contains 3 LNR (Lin/Notch) repeats.

Ontologies

Keywords
   Biological processDifferentiation
Notch signaling pathway
Transcription
Transcription regulation
   Cellular componentCell membrane
Membrane
Nucleus
   Coding sequence diversityAlternative splicing
   DomainANK repeat
EGF-like domain
Repeat
Signal
Transmembrane
Transmembrane helix
   Molecular functionActivator
Developmental protein
Receptor
   PTMDisulfide bond
Glycoprotein
Phosphoprotein
   Technical termComplete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processNotch signaling pathway

Traceable author statement PubMed 15821257. Source: UniProtKB

atrial septum morphogenesis

Inferred from sequence or structural similarity. Source: BHF-UCL

cell cycle arrest

Inferred from sequence or structural similarity. Source: UniProtKB

cell fate determination

Traceable author statement PubMed 12496659. Source: UniProtKB

cell growth

Inferred from sequence or structural similarity. Source: UniProtKB

ciliary body morphogenesis

Inferred from mutant phenotype PubMed 23676271. Source: MGI

determination of left/right symmetry

Inferred from mutant phenotype PubMed 12730124. Source: MGI

embryonic limb morphogenesis

Inferred from genetic interaction PubMed 16169548. Source: MGI

glomerular capillary formation

Inferred from expression pattern PubMed 15821257. Source: UniProtKB

glomerular visceral epithelial cell development

Inferred from expression pattern PubMed 15821257. Source: UniProtKB

heart looping

Inferred from genetic interaction PubMed 12730124. Source: BHF-UCL

humoral immune response

Inferred from genetic interaction PubMed 17658279. Source: MGI

in utero embryonic development

Inferred from mutant phenotype PubMed 17359302. Source: MGI

inflammatory response to antigenic stimulus

Inferred from genetic interaction PubMed 17658279. Source: MGI

interleukin-4 secretion

Inferred from genetic interaction PubMed 17658279. Source: MGI

left/right axis specification

Inferred from genetic interaction PubMed 12730124. Source: BHF-UCL

morphogenesis of an epithelial sheet

Inferred from mutant phenotype PubMed 11861489. Source: MGI

negative regulation of cell proliferation

Inferred from sequence or structural similarity. Source: UniProtKB

negative regulation of transcription from RNA polymerase II promoter

Inferred from mutant phenotype PubMed 23676271. Source: MGI

organ morphogenesis

Traceable author statement PubMed 12496659. Source: UniProtKB

placenta blood vessel development

Inferred from mutant phenotype PubMed 17359302. Source: MGI

placenta development

Inferred from mutant phenotype PubMed 17359302. Source: MGI

positive regulation of BMP signaling pathway

Inferred from mutant phenotype PubMed 23676271. Source: MGI

positive regulation of Ras protein signal transduction

Inferred from sequence or structural similarity. Source: UniProtKB

positive regulation of apoptotic process

Inferred from genetic interaction PubMed 16169548. Source: MGI

positive regulation of cell proliferation

Inferred from mutant phenotype PubMed 23676271. Source: MGI

positive regulation of osteoclast differentiation

Inferred from direct assay Ref.10. Source: UniProtKB

proximal tubule development

Inferred from expression pattern PubMed 15821257. Source: UniProtKB

transcription, DNA-templated

Inferred from electronic annotation. Source: UniProtKB-KW

wound healing

Inferred from direct assay PubMed 12496659. Source: UniProtKB

   Cellular_componentcell surface

Inferred from sequence or structural similarity. Source: UniProtKB

cilium

Inferred from direct assay PubMed 21703454. Source: MGI

cytosol

Traceable author statement. Source: Reactome

extracellular region

Traceable author statement. Source: Reactome

integral component of plasma membrane

Inferred by curator PubMed 10551863. Source: UniProtKB

nucleoplasm

Traceable author statement. Source: Reactome

nucleus

Inferred from direct assay PubMed 12496659. Source: UniProtKB

plasma membrane

Traceable author statement. Source: Reactome

receptor complex

Inferred from sequence orthology PubMed 23382219. Source: MGI

   Molecular_functionNF-kappaB binding

Inferred from physical interaction Ref.10. Source: UniProtKB

calcium ion binding

Inferred from electronic annotation. Source: InterPro

enzyme binding

Inferred from physical interaction Ref.9. Source: UniProtKB

protein binding

Inferred from physical interaction PubMed 10551863PubMed 12496659. Source: UniProtKB

Complete GO annotation...

Alternative products

This entry describes 2 isoforms produced by alternative splicing. [Align] [Select]
Isoform 1 (identifier: O35516-1)

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.
Isoform 2 (identifier: O35516-2)

The sequence of this isoform differs from the canonical sequence as follows:
     1302-1508: Missing.
Note: No experimental confirmation available.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Signal peptide1 – 2525 Potential
Chain26 – 24702445Neurogenic locus notch homolog protein 2
PRO_0000007686
Chain1666 – 2470805Notch 2 extracellular truncation
PRO_0000007687
Chain1697 – 2470774Notch 2 intracellular domain
PRO_0000007688

Regions

Topological domain26 – 16771652Extracellular Potential
Transmembrane1678 – 169821Helical; Potential
Topological domain1699 – 2470772Cytoplasmic Potential
Domain26 – 6338EGF-like 1
Domain64 – 10239EGF-like 2
Domain105 – 14339EGF-like 3
Domain144 – 18037EGF-like 4
Domain182 – 21938EGF-like 5; calcium-binding Potential
Domain221 – 25636EGF-like 6; incomplete
Domain258 – 29437EGF-like 7; calcium-binding Potential
Domain296 – 33439EGF-like 8; calcium-binding Potential
Domain336 – 37237EGF-like 9; calcium-binding Potential
Domain373 – 41139EGF-like 10
Domain413 – 45240EGF-like 11; calcium-binding Potential
Domain454 – 49037EGF-like 12; calcium-binding Potential
Domain492 – 52837EGF-like 13; calcium-binding Potential
Domain530 – 56637EGF-like 14; calcium-binding Potential
Domain568 – 60336EGF-like 15; calcium-binding Potential
Domain605 – 64137EGF-like 16; calcium-binding Potential
Domain643 – 67836EGF-like 17; calcium-binding Potential
Domain680 – 71637EGF-like 18; calcium-binding Potential
Domain718 – 75336EGF-like 19
Domain755 – 79137EGF-like 20; calcium-binding Potential
Domain793 – 82937EGF-like 21; calcium-binding Potential
Domain831 – 86939EGF-like 22
Domain871 – 90737EGF-like 23; calcium-binding Potential
Domain909 – 94537EGF-like 24; calcium-binding Potential
Domain947 – 98337EGF-like 25; calcium-binding Potential
Domain985 – 102137EGF-like 26; calcium-binding Potential
Domain1023 – 105937EGF-like 27; calcium-binding Potential
Domain1061 – 109737EGF-like 28
Domain1099 – 114547EGF-like 29
Domain1147 – 118337EGF-like 30; calcium-binding Potential
Domain1185 – 122137EGF-like 31; calcium-binding Potential
Domain1223 – 126038EGF-like 32; calcium-binding Potential
Domain1262 – 130039EGF-like 33
Domain1302 – 134544EGF-like 34
Domain1372 – 141039EGF-like 35
Repeat1423 – 146341LNR 1
Repeat1464 – 150037LNR 2
Repeat1501 – 154242LNR 3
Repeat1825 – 186945ANK 1
Repeat1874 – 190330ANK 2
Repeat1907 – 193731ANK 3
Repeat1941 – 197030ANK 4
Repeat1974 – 200330ANK 5
Repeat2007 – 203630ANK 6
Region1423 – 1677255Negative regulatory region (NRR) By similarity
Compositional bias1645 – 16484Poly-Ala
Compositional bias1992 – 19954Poly-Leu
Compositional bias2183 – 21897Poly-Ala
Compositional bias2425 – 24284Poly-Ser
Compositional bias2445 – 24506Poly-Gly

Sites

Site6121Essential for O-xylosylation

Amino acid modifications

Modified residue17151Phosphothreonine By similarity
Modified residue17771Phosphoserine Ref.12
Modified residue18001Phosphothreonine By similarity
Modified residue18021Phosphoserine By similarity
Modified residue18061Phosphothreonine By similarity
Modified residue18401Phosphoserine Ref.12
Modified residue18431Phosphoserine Ref.12
Modified residue20681Phosphoserine By similarity
Modified residue20761Phosphoserine By similarity
Modified residue20791Phosphoserine By similarity
Modified residue20951Phosphothreonine By similarity
Glycosylation461N-linked (GlcNAc...) Potential
Glycosylation1551N-linked (GlcNAc...) Potential
Glycosylation6111O-linked (Glc...); alternate Ref.13
Glycosylation6111O-linked (Xyl...); alternate Ref.13
Glycosylation7311N-linked (GlcNAc...) Potential
Glycosylation11001N-linked (GlcNAc...) Potential
Glycosylation14631N-linked (GlcNAc...) Potential
Disulfide bond28 ↔ 41 By similarity
Disulfide bond35 ↔ 51 By similarity
Disulfide bond53 ↔ 62 By similarity
Disulfide bond68 ↔ 79 By similarity
Disulfide bond73 ↔ 90 By similarity
Disulfide bond92 ↔ 101 By similarity
Disulfide bond109 ↔ 121 By similarity
Disulfide bond115 ↔ 131 By similarity
Disulfide bond133 ↔ 142 By similarity
Disulfide bond148 ↔ 159 By similarity
Disulfide bond153 ↔ 168 By similarity
Disulfide bond170 ↔ 179 By similarity
Disulfide bond186 ↔ 198 By similarity
Disulfide bond192 ↔ 207 By similarity
Disulfide bond209 ↔ 218 By similarity
Disulfide bond228 ↔ 244 By similarity
Disulfide bond246 ↔ 255 By similarity
Disulfide bond262 ↔ 273 By similarity
Disulfide bond267 ↔ 282 By similarity
Disulfide bond284 ↔ 293 By similarity
Disulfide bond300 ↔ 313 By similarity
Disulfide bond307 ↔ 322 By similarity
Disulfide bond324 ↔ 333 By similarity
Disulfide bond340 ↔ 351 By similarity
Disulfide bond345 ↔ 360 By similarity
Disulfide bond362 ↔ 371 By similarity
Disulfide bond377 ↔ 388 By similarity
Disulfide bond382 ↔ 399 By similarity
Disulfide bond401 ↔ 410 By similarity
Disulfide bond417 ↔ 431 By similarity
Disulfide bond425 ↔ 440 By similarity
Disulfide bond442 ↔ 451 By similarity
Disulfide bond458 ↔ 469 By similarity
Disulfide bond463 ↔ 478 By similarity
Disulfide bond480 ↔ 489 By similarity
Disulfide bond496 ↔ 507 By similarity
Disulfide bond501 ↔ 516 By similarity
Disulfide bond518 ↔ 527 By similarity
Disulfide bond534 ↔ 545 By similarity
Disulfide bond539 ↔ 554 By similarity
Disulfide bond556 ↔ 565 By similarity
Disulfide bond572 ↔ 582 By similarity
Disulfide bond577 ↔ 591 By similarity
Disulfide bond593 ↔ 602 By similarity
Disulfide bond609 ↔ 620 By similarity
Disulfide bond614 ↔ 629 By similarity
Disulfide bond631 ↔ 640 By similarity
Disulfide bond647 ↔ 657 By similarity
Disulfide bond652 ↔ 666 By similarity
Disulfide bond668 ↔ 677 By similarity
Disulfide bond684 ↔ 695 By similarity
Disulfide bond689 ↔ 704 By similarity
Disulfide bond706 ↔ 715 By similarity
Disulfide bond722 ↔ 732 By similarity
Disulfide bond727 ↔ 741 By similarity
Disulfide bond743 ↔ 752 By similarity
Disulfide bond759 ↔ 770 By similarity
Disulfide bond764 ↔ 779 By similarity
Disulfide bond781 ↔ 790 By similarity
Disulfide bond797 ↔ 808 By similarity
Disulfide bond802 ↔ 817 By similarity
Disulfide bond819 ↔ 828 By similarity
Disulfide bond835 ↔ 846 By similarity
Disulfide bond840 ↔ 857 By similarity
Disulfide bond859 ↔ 868 By similarity
Disulfide bond875 ↔ 886 By similarity
Disulfide bond880 ↔ 895 By similarity
Disulfide bond897 ↔ 906 By similarity
Disulfide bond913 ↔ 924 By similarity
Disulfide bond918 ↔ 933 By similarity
Disulfide bond935 ↔ 944 By similarity
Disulfide bond951 ↔ 962 By similarity
Disulfide bond956 ↔ 971 By similarity
Disulfide bond973 ↔ 982 By similarity
Disulfide bond989 ↔ 1000 By similarity
Disulfide bond994 ↔ 1009 By similarity
Disulfide bond1011 ↔ 1020 By similarity
Disulfide bond1027 ↔ 1038 By similarity
Disulfide bond1032 ↔ 1047 By similarity
Disulfide bond1049 ↔ 1058 By similarity
Disulfide bond1065 ↔ 1076 By similarity
Disulfide bond1070 ↔ 1085 By similarity
Disulfide bond1087 ↔ 1096 By similarity
Disulfide bond1103 ↔ 1124 By similarity
Disulfide bond1118 ↔ 1133 By similarity
Disulfide bond1135 ↔ 1144 By similarity
Disulfide bond1151 ↔ 1162 By similarity
Disulfide bond1156 ↔ 1171 By similarity
Disulfide bond1173 ↔ 1182 By similarity
Disulfide bond1189 ↔ 1200 By similarity
Disulfide bond1194 ↔ 1209 By similarity
Disulfide bond1211 ↔ 1220 By similarity
Disulfide bond1227 ↔ 1239 By similarity
Disulfide bond1233 ↔ 1248 By similarity
Disulfide bond1250 ↔ 1259 By similarity
Disulfide bond1266 ↔ 1279 By similarity
Disulfide bond1271 ↔ 1288 By similarity
Disulfide bond1290 ↔ 1299 By similarity
Disulfide bond1306 ↔ 1317 By similarity
Disulfide bond1311 ↔ 1329 By similarity
Disulfide bond1331 ↔ 1344 By similarity
Disulfide bond1376 ↔ 1387 By similarity
Disulfide bond1381 ↔ 1398 By similarity
Disulfide bond1400 ↔ 1409 By similarity
Disulfide bond1423 ↔ 1446 By similarity
Disulfide bond1428 ↔ 1441 By similarity
Disulfide bond1437 ↔ 1453 By similarity
Disulfide bond1464 ↔ 1487 By similarity
Disulfide bond1470 ↔ 1482 By similarity
Disulfide bond1478 ↔ 1494 By similarity
Disulfide bond1501 ↔ 1525 By similarity
Disulfide bond1507 ↔ 1520 By similarity
Disulfide bond1516 ↔ 1532 By similarity
Disulfide bond1632 ↔ 1639 By similarity

Natural variations

Alternative sequence1302 – 1508207Missing in isoform 2.
VSP_001405

Experimental info

Mutagenesis6121S → A: No effect on O-glycosylation by POGLUT1. Loss of O-xylosylation. Ref.13
Mutagenesis16991M → L: No effect on NICD processing. Ref.6 Ref.7
Mutagenesis16991M → V: Decreased NICD processing. Ref.6 Ref.7
Sequence conflict13401L → C in CAA48340. Ref.2
Sequence conflict17981S → R in AAC52924. Ref.3
Sequence conflict19011R → A in AAC52924. Ref.3
Sequence conflict19181G → A in AAC52924. Ref.3

Sequences

Sequence LengthMass (Da)Tools
Isoform 1 [UniParc].

Last modified January 1, 1998. Version 1.
Checksum: B55A31B35242716D

FASTA2,470265,327
        10         20         30         40         50         60 
MPDLRPAALR ALLWLWLCGA GPAHALQCRG GQEPCVNEGT CVTYHNGTGF CRCPEGFLGE 

        70         80         90        100        110        120 
YCQHRDPCEK NRCQNGGTCV PQGMLGKATC RCAPGFTGED CQYSTSHPCF VSRPCQNGGT 

       130        140        150        160        170        180 
CHMLSRDTYE CTCQVGFTGK QCQWTDACLS HPCENGSTCT SVASQFSCKC PAGLTGQKCE 

       190        200        210        220        230        240 
ADINECDIPG RCQHGGTCLN LPGSYRCQCG QGFTGQHCDS PYVRGLPCVN GGTCRQTGDF 

       250        260        270        280        290        300 
TLECNCLPGF EGSTCERNID DCPNHKCQNG GVCVDGVNTY NCRCPPQWTG QFCTEDVDEC 

       310        320        330        340        350        360 
LLQPNACQNG GTCTNRNGGY GCVCVNGWSG DDCSENIDDC AYASCTPGST CIDRVASFSC 

       370        380        390        400        410        420 
LCPEGKAGLL CHLDDACISN PCHKGALCDT NPLNGQYICT CPQGYKGADC TEDVDECAMA 

       430        440        450        460        470        480 
NSNPCEHAGK CVNTDGAFHC ECLKGYAGPR CEMDINECHS DPCQNDATCL DKIGGFTCLC 

       490        500        510        520        530        540 
MPGFKGVHCE LEVNECQSNP CVNNGQCVDK VNRFQCLCPP GFTGPVCQID IDDCSSTPCL 

       550        560        570        580        590        600 
NGAKCIDHPN GYECQCATGF TGILCDENID NCDPDPCHHG QCQDGIDSYT CICNPGYMGA 

       610        620        630        640        650        660 
ICSDQIDECY SSPCLNDGRC IDLVNGYQCN CQPGTSGLNC EINFDDCASN PCMHGVCVDG 

       670        680        690        700        710        720 
INRYSCVCSP GFTGQRCNID IDECASNPCR KGATCINDVN GFRCICPEGP HHPSCYSQVN 

       730        740        750        760        770        780 
ECLSNPCIHG NCTGGLSGYK CLCDAGWVGV NCEVDKNECL SNPCQNGGTC NNLVNGYRCT 

       790        800        810        820        830        840 
CKKGFKGYNC QVNIDECASN PCLNQGTCFD DVSGYTCHCM LPYTGKNCQT VLAPCSPNPC 

       850        860        870        880        890        900 
ENAAVCKEAP NFESFSCLCA PGWQGKRCTV DVDECISKPC MNNGVCHNTQ GSYVCECPPG 

       910        920        930        940        950        960 
FSGMDCEEDI NDCLANPCQN GGSCVDHVNT FSCQCHPGFI GDKCQTDMNE CLSEPCKNGG 

       970        980        990       1000       1010       1020 
TCSDYVNSYT CTCPAGFHGV HCENNIDECT ESSCFNGGTC VDGINSFSCL CPVGFTGPFC 

      1030       1040       1050       1060       1070       1080 
LHDINECSSN PCLNAGTCVD GLGTYRCICP LGYTGKNCQT LVNLCSRSPC KNKGTCVQEK 

      1090       1100       1110       1120       1130       1140 
ARPHCLCPPG WDGAYCDVLN VSCKAAALQK GVPVEHLCQH SGICINAGNT HHCQCPLGYT 

      1150       1160       1170       1180       1190       1200 
GSYCEEQLDE CASNPCQHGA TCNDFIGGYR CECVPGYQGV NCEYEVDECQ NQPCQNGGTC 

      1210       1220       1230       1240       1250       1260 
IDLVNHFKCS CPPGTRGLLC EENIDECAGG PHCLNGGQCV DRIGGYTCRC LPGFAGERCE 

      1270       1280       1290       1300       1310       1320 
GDINECLSNP CSSEGSLDCV QLKNNYNCIC RSAFTGRHCE TFLDVCPQKP CLNGGTCAVA 

      1330       1340       1350       1360       1370       1380 
SNMPDGFICR CPPGFSGARL QSSCGQVKCR RGEQCIHTDS GPRCFCLNPK DCESGCASNP 

      1390       1400       1410       1420       1430       1440 
CQHGGTCYPQ RQPPHYSCRC PPSFGGSHCE LYTAPTSTPP ATCQSQYCAD KARDGICDEA 

      1450       1460       1470       1480       1490       1500 
CNSHACQWDG GDCSLTMEDP WANCTSTLRC WEYINNQCDE QCNTAECLFD NFECQRNSKT 

      1510       1520       1530       1540       1550       1560 
CKYDKYCADH FKDNHCDQGC NSEECGWDGL DCASDQPENL AEGTLIIVVL LPPEQLLQDS 

      1570       1580       1590       1600       1610       1620 
RSFLRALGTL LHTNLRIKQD SQGALMVYPY FGEKSAAMKK QKMTRRSLPE EQEQEQEVIG 

      1630       1640       1650       1660       1670       1680 
SKIFLEIDNR QCVQDSDQCF KNTDAAAALL ASHAIQGTLS YPLVSVFSEL ESPRNAQLLY 

      1690       1700       1710       1720       1730       1740 
LLAVAVVIIL FFILLGVIMA KRKQAWLPLA AGRFTLRRDS SNHKRREPVG QDAVGLKNLS 

      1750       1760       1770       1780       1790       1800 
VQVSEANLIG SGTSEHWVDD EGPQPKKAKA EDEALLSEDD PIDRRPWTQQ HLEAADISHT 

      1810       1820       1830       1840       1850       1860 
PSLALTPPQA EQEVDVLDVN VRGPDGCTPL MLASLRGGSS DLSDEDEDAE DSSANIITDL 

      1870       1880       1890       1900       1910       1920 
VYQGASLQAQ TDRTGEMALH LAARYSRADA AKRLLDAGAD RNAQDNMGRC PLHAAVAGDA 

      1930       1940       1950       1960       1970       1980 
QGVFQILIRN RVTDLDARMN DGTTPLILAA RLAVEGMVAE LINCQADVNA VDDHGKSALH 

      1990       2000       2010       2020       2030       2040 
WAAAVNNVEA TLLLLKNGAN RDMQDNKEET PLFLAAREGS YEAAKILLDH FANRDITDHM 

      2050       2060       2070       2080       2090       2100 
DRLPRDVARD RMHHDIVRLL DEYNVTPSPP GTVLTSALSP VLCGPNRSFL SLKHTPMGKK 

      2110       2120       2130       2140       2150       2160 
ARRPNTKSTM PTSLPNLAKE AKDAKGSRRK KCLNEKVQLS ESSVTLSPVD SLESPHTYVS 

      2170       2180       2190       2200       2210       2220 
DATSSPMITS PGILQASPTP LLAAAAPAAP VHTQHALSFS NLHDMQPLAP GASTVLPSVS 

      2230       2240       2250       2260       2270       2280 
QLLSHHHIAP PGSSSAGSLG RLHPVPVPAD WMNRVEMNET QYSEMFGMVL APAEGAHPGI 

      2290       2300       2310       2320       2330       2340 
AAPQSRPPEG KHMSTQREPL PPIVTFQLIP KRSIAQAAGA PQTQSSCPPA VAGPLPSMYQ 

      2350       2360       2370       2380       2390       2400 
IPEMPRLPSV AFPPTMMPQQ EGQVAQTIVP TYHPFPASVG KYPTPPSQHS YASSNAAERT 

      2410       2420       2430       2440       2450       2460 
PSHGGHLQGE HPYLTPSPES PDQWSSSSPH SASDWSDVTT SPTPGGGGGG QRGPGTHMSE 

      2470 
PPHSNMQVYA 

« Hide

Isoform 2 [UniParc].

Checksum: 4EF13A99DB3647BC
Show »

FASTA2,263242,663

References

« Hide 'large scale' references
[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]"Inhibition of granulocytic differentiation by mNotch1."
Milner L.A., Bigas A., Kopan R., Brashem-Stein C., Bernstein I.D., Martin D.I.
Proc. Natl. Acad. Sci. U.S.A. 93:13014-13019(1996) [PubMed] [Europe PMC] [Abstract]
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]"Asparaginyl hydroxylation of the Notch ankyrin repeat domain by factor inhibiting hypoxia-inducible factor."
Coleman M.L., McDonough M.A., Hewitson K.S., Coles C., Mecinovic J., Edelmann M., Cook K.M., Cockman M.E., Lancaster D.E., Kessler B.M., Oldham N.J., Ratcliffe P.J., Schofield C.J.
J. Biol. Chem. 282:24027-24038(2007) [PubMed] [Europe PMC] [Abstract]
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]"Rumi functions as both a protein O-glucosyltransferase and a protein O-xylosyltransferase."
Takeuchi H., Fernandez-Valdivia R.C., Caswell D.S., Nita-Lazar A., Rana N.A., Garner T.P., Weldeghiorghis T.K., Macnaughtan M.A., Jafar-Nejad H., Haltiwanger R.S.
Proc. Natl. Acad. Sci. U.S.A. 108:16600-16605(2011) [PubMed] [Europe PMC] [Abstract]
Cited for: GLYCOSYLATION AT SER-611, MUTAGENESIS OF SER-612.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
D32210 mRNA. Translation: BAA22094.1.
X68279 mRNA. Translation: CAA48340.1.
U31881 mRNA. Translation: AAC52924.1.
PIRA49175.
RefSeqNP_035058.2. NM_010928.2.
UniGeneMm.485843.

3D structure databases

ProteinModelPortalO35516.
SMRO35516. Positions 27-1341, 1381-1410, 1423-1669, 1777-2061.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid201809. 5 interactions.
DIPDIP-6008N.
IntActO35516. 1 interaction.

PTM databases

PhosphoSiteO35516.

Proteomic databases

PaxDbO35516.
PRIDEO35516.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

GeneID18129.
KEGGmmu:18129.

Organism-specific databases

CTD4853.
MGIMGI:97364. Notch2.

Phylogenomic databases

eggNOGCOG0666.
HOGENOMHOG000234369.
HOVERGENHBG052650.
InParanoidO35516.
KOK02599.
PhylomeDBO35516.

Enzyme and pathway databases

ReactomeREACT_188257. Signal Transduction.

Gene expression databases

CleanExMM_NOTCH2.
GenevestigatorO35516.

Family and domain databases

Gene3D1.25.40.20. 1 hit.
InterProIPR002110. 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]
PfamPF00023. 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]
PIRSFPIRSF002279. Notch. 1 hit.
PRINTSPR01452. LNOTCHREPEAT.
PR01985. NOTCH2.
SMARTSM00248. ANK. 6 hits.
SM00181. EGF. 12 hits.
SM00179. EGF_CA. 23 hits.
SM00004. NL. 3 hits.
[Graphical view]
SUPFAMSSF48403. SSF48403. 1 hit.
SSF57184. SSF57184. 5 hits.
SSF90193. SSF90193. 2 hits.
PROSITEPS50297. 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]
ProtoNetSearch...

Other

ChiTaRSNOTCH2. mouse.
NextBio293360.
PROO35516.
SOURCESearch...

Entry information

Entry nameNOTC2_MOUSE
AccessionPrimary (citable) accession number: O35516
Secondary accession number(s): Q06008, Q60941
Entry history
Integrated into UniProtKB/Swiss-Prot: March 27, 2002
Last sequence update: January 1, 1998
Last modified: June 11, 2014
This is version 154 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

MGD cross-references

Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot