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Protein

Neurogenic locus notch homolog protein 3

Gene

Notch3

Organism
Mus musculus (Mouse)
Status
Reviewed-Annotation score: 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 a role during CNS development.By similarity

GO - Molecular functioni

  • calcium ion binding Source: InterPro
  • enzyme binding Source: UniProtKB

GO - Biological processi

  • artery morphogenesis Source: MGI
  • forebrain development Source: MGI
  • glomerular capillary formation Source: UniProtKB
  • negative regulation of cell differentiation Source: MGI
  • negative regulation of neuron differentiation Source: MGI
  • negative regulation of transcription from RNA polymerase II promoter Source: MGI
  • neuron fate commitment Source: MGI
  • Notch signaling pathway Source: UniProtKB
  • positive regulation of smooth muscle cell proliferation Source: UniProtKB
  • positive regulation of transcription from RNA polymerase II promoter Source: MGI
  • transcription, DNA-templated Source: UniProtKB-KW
Complete GO annotation...

Keywords - Molecular functioni

Activator, Developmental protein, Receptor

Keywords - Biological processi

Differentiation, Notch signaling pathway, Transcription, Transcription regulation

Enzyme and pathway databases

ReactomeiR-MMU-1912420. Pre-NOTCH Processing in Golgi.
R-MMU-1980148. Signaling by NOTCH3.
R-MMU-350054. Notch-HLH transcription pathway.

Names & Taxonomyi

Protein namesi
Recommended name:
Neurogenic locus notch homolog protein 3
Short name:
Notch 3
Cleaved into the following 2 chains:
Gene namesi
Name:Notch3
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
Proteomesi
  • UP000000589 Componenti: Chromosome 17

Organism-specific databases

MGIiMGI:99460. Notch3.

Subcellular locationi

Notch 3 intracellular domain :
  • Nucleus

  • Note: Following proteolytical processing NICD is translocated to the nucleus.

Topology

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Topological domaini40 – 16431604ExtracellularAdd
BLAST
Transmembranei1644 – 166421HelicalSequence analysisAdd
BLAST
Topological domaini1665 – 2318654CytoplasmicAdd
BLAST

GO - Cellular componenti

  • actin cytoskeleton Source: MGI
  • cytoplasm Source: MGI
  • integral component of plasma membrane Source: UniProtKB
  • nucleoplasm Source: MGI
  • nucleus Source: AgBase
  • plasma membrane Source: MGI
  • receptor complex Source: MGI
Complete GO annotation...

Keywords - Cellular componenti

Cell membrane, Membrane, Nucleus

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi1664 – 16641M → L: No effect on NICD processing. 1 Publication

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Signal peptidei1 – 3939Sequence analysisAdd
BLAST
Chaini40 – 23182279Neurogenic locus notch homolog protein 3PRO_0000007695Add
BLAST
Chaini1630 – 2318689Notch 3 extracellular truncationPRO_0000007696Add
BLAST
Chaini1663 – 2318656Notch 3 intracellular domainPRO_0000007697Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Disulfide bondi43 ↔ 55By similarity
Disulfide bondi49 ↔ 66By similarity
Disulfide bondi68 ↔ 77By similarity
Disulfide bondi83 ↔ 94By similarity
Disulfide bondi88 ↔ 107By similarity
Disulfide bondi109 ↔ 118By similarity
Disulfide bondi124 ↔ 135By similarity
Disulfide bondi129 ↔ 145By similarity
Disulfide bondi147 ↔ 156By similarity
Disulfide bondi163 ↔ 175By similarity
Disulfide bondi169 ↔ 184By similarity
Disulfide bondi186 ↔ 195By similarity
Disulfide bondi202 ↔ 213By similarity
Disulfide bondi207 ↔ 223By similarity
Disulfide bondi225 ↔ 234By similarity
Disulfide bondi241 ↔ 252By similarity
Disulfide bondi246 ↔ 261By similarity
Disulfide bondi263 ↔ 272By similarity
Disulfide bondi279 ↔ 292By similarity
Disulfide bondi286 ↔ 301By similarity
Disulfide bondi303 ↔ 312By similarity
Disulfide bondi319 ↔ 330By similarity
Disulfide bondi324 ↔ 339By similarity
Disulfide bondi341 ↔ 350By similarity
Disulfide bondi356 ↔ 367By similarity
Disulfide bondi361 ↔ 378By similarity
Disulfide bondi380 ↔ 389By similarity
Disulfide bondi396 ↔ 409By similarity
Disulfide bondi403 ↔ 418By similarity
Disulfide bondi420 ↔ 429By similarity
Disulfide bondi436 ↔ 447By similarity
Disulfide bondi441 ↔ 456By similarity
Disulfide bondi458 ↔ 467By similarity
Disulfide bondi474 ↔ 485By similarity
Disulfide bondi479 ↔ 494By similarity
Disulfide bondi496 ↔ 505By similarity
Disulfide bondi512 ↔ 523By similarity
Disulfide bondi517 ↔ 532By similarity
Disulfide bondi534 ↔ 543By similarity
Disulfide bondi550 ↔ 560By similarity
Disulfide bondi555 ↔ 569By similarity
Disulfide bondi571 ↔ 580By similarity
Disulfide bondi587 ↔ 598By similarity
Disulfide bondi592 ↔ 607By similarity
Disulfide bondi609 ↔ 618By similarity
Disulfide bondi625 ↔ 635By similarity
Disulfide bondi630 ↔ 644By similarity
Disulfide bondi646 ↔ 655By similarity
Disulfide bondi662 ↔ 673By similarity
Disulfide bondi667 ↔ 682By similarity
Disulfide bondi684 ↔ 693By similarity
Disulfide bondi700 ↔ 710By similarity
Disulfide bondi705 ↔ 719By similarity
Disulfide bondi721 ↔ 730By similarity
Disulfide bondi739 ↔ 750By similarity
Disulfide bondi744 ↔ 759By similarity
Disulfide bondi761 ↔ 770By similarity
Disulfide bondi776 ↔ 787By similarity
Disulfide bondi781 ↔ 797By similarity
Disulfide bondi799 ↔ 808By similarity
Disulfide bondi815 ↔ 827By similarity
Disulfide bondi821 ↔ 836By similarity
Disulfide bondi838 ↔ 847By similarity
Disulfide bondi854 ↔ 865By similarity
Disulfide bondi859 ↔ 874By similarity
Disulfide bondi876 ↔ 885By similarity
Disulfide bondi892 ↔ 902By similarity
Disulfide bondi897 ↔ 911By similarity
Disulfide bondi913 ↔ 922By similarity
Disulfide bondi929 ↔ 940By similarity
Disulfide bondi934 ↔ 949By similarity
Disulfide bondi951 ↔ 960By similarity
Disulfide bondi967 ↔ 978By similarity
Disulfide bondi972 ↔ 987By similarity
Disulfide bondi989 ↔ 998By similarity
Disulfide bondi1005 ↔ 1016By similarity
Disulfide bondi1010 ↔ 1023By similarity
Disulfide bondi1025 ↔ 1034By similarity
Disulfide bondi1041 ↔ 1062By similarity
Disulfide bondi1056 ↔ 1071By similarity
Disulfide bondi1073 ↔ 1082By similarity
Disulfide bondi1089 ↔ 1100By similarity
Disulfide bondi1094 ↔ 1109By similarity
Disulfide bondi1111 ↔ 1120By similarity
Disulfide bondi1127 ↔ 1138By similarity
Disulfide bondi1132 ↔ 1147By similarity
Disulfide bondi1149 ↔ 1158By similarity
Disulfide bondi1165 ↔ 1183By similarity
Disulfide bondi1177 ↔ 1192By similarity
Glycosylationi1180 – 11801N-linked (GlcNAc...)Sequence analysis
Disulfide bondi1194 ↔ 1203By similarity
Disulfide bondi1210 ↔ 1223By similarity
Disulfide bondi1215 ↔ 1233By similarity
Disulfide bondi1235 ↔ 1244By similarity
Disulfide bondi1251 ↔ 1262By similarity
Disulfide bondi1256 ↔ 1276By similarity
Disulfide bondi1278 ↔ 1287By similarity
Disulfide bondi1294 ↔ 1305By similarity
Disulfide bondi1299 ↔ 1314By similarity
Disulfide bondi1316 ↔ 1325By similarity
Glycosylationi1337 – 13371N-linked (GlcNAc...)Sequence analysis
Disulfide bondi1340 ↔ 1351By similarity
Disulfide bondi1345 ↔ 1362By similarity
Disulfide bondi1364 ↔ 1373By similarity
Disulfide bondi1388 ↔ 1411By similarity
Disulfide bondi1393 ↔ 1406By similarity
Disulfide bondi1402 ↔ 1418By similarity
Disulfide bondi1429 ↔ 1452By similarity
Disulfide bondi1434 ↔ 1447By similarity
Glycosylationi1439 – 14391N-linked (GlcNAc...)Sequence analysis
Disulfide bondi1443 ↔ 1459By similarity
Disulfide bondi1468 ↔ 1494By similarity
Disulfide bondi1476 ↔ 1489By similarity
Disulfide bondi1485 ↔ 1501By 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
Phosphorylated.
Hydroxylated by HIF1AN.1 Publication

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sitei1572 – 15732Cleavage; by furin-like proteaseBy similarity

Keywords - PTMi

Disulfide bond, Glycoprotein, Phosphoprotein

Proteomic databases

MaxQBiQ61982.
PaxDbiQ61982.
PRIDEiQ61982.

PTM databases

iPTMnetiQ61982.
PhosphoSiteiQ61982.

Expressioni

Tissue specificityi

Proliferating neuroepithelium.

Developmental stagei

CNS development.

Gene expression databases

BgeeiQ61982.
CleanExiMM_NOTCH3.
GenevisibleiQ61982. MM.

Interactioni

Subunit structurei

Interacts with PSMA1 (By similarity). Heterodimer of a C-terminal fragment N(TM) and a N-terminal fragment N(EC) which are probably linked by disulfide bonds. Interacts with MAML1, MAML2 and MAML3 which act as transcriptional coactivators for NOTCH3. Interacts with HIF1AN.By similarity2 Publications

Binary interactionsi

WithEntry#Exp.IntActNotes
LRORF2Q77CA83EBI-11292908,EBI-11292862From a different organism.

GO - Molecular functioni

  • enzyme binding Source: UniProtKB

Protein-protein interaction databases

BioGridi201811. 5 interactions.
IntActiQ61982. 4 interactions.
MINTiMINT-1955915.
STRINGi10090.ENSMUSP00000085016.

Structurei

3D structure databases

ProteinModelPortaliQ61982.
SMRiQ61982. Positions 392-506, 1792-2027.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini40 – 7839EGF-like 1PROSITE-ProRule annotationAdd
BLAST
Domaini79 – 11941EGF-like 2PROSITE-ProRule annotationAdd
BLAST
Domaini120 – 15738EGF-like 3PROSITE-ProRule annotationAdd
BLAST
Domaini159 – 19638EGF-like 4; calcium-bindingPROSITE-ProRule annotationAdd
BLAST
Domaini198 – 23538EGF-like 5PROSITE-ProRule annotationAdd
BLAST
Domaini237 – 27337EGF-like 6; calcium-bindingPROSITE-ProRule annotationAdd
BLAST
Domaini275 – 31339EGF-like 7PROSITE-ProRule annotationAdd
BLAST
Domaini315 – 35137EGF-like 8; calcium-bindingPROSITE-ProRule annotationAdd
BLAST
Domaini352 – 39039EGF-like 9PROSITE-ProRule annotationAdd
BLAST
Domaini392 – 43039EGF-like 10; calcium-bindingPROSITE-ProRule annotationAdd
BLAST
Domaini432 – 46837EGF-like 11; calcium-bindingPROSITE-ProRule annotationAdd
BLAST
Domaini470 – 50637EGF-like 12; calcium-bindingPROSITE-ProRule annotationAdd
BLAST
Domaini508 – 54437EGF-like 13; calcium-bindingPROSITE-ProRule annotationAdd
BLAST
Domaini546 – 58136EGF-like 14; calcium-bindingPROSITE-ProRule annotationAdd
BLAST
Domaini583 – 61937EGF-like 15; calcium-bindingPROSITE-ProRule annotationAdd
BLAST
Domaini621 – 65636EGF-like 16; calcium-bindingPROSITE-ProRule annotationAdd
BLAST
Domaini658 – 69437EGF-like 17; calcium-bindingPROSITE-ProRule annotationAdd
BLAST
Domaini696 – 73136EGF-like 18PROSITE-ProRule annotationAdd
BLAST
Domaini735 – 77137EGF-like 19PROSITE-ProRule annotationAdd
BLAST
Domaini772 – 80938EGF-like 20PROSITE-ProRule annotationAdd
BLAST
Domaini811 – 84838EGF-like 21; calcium-bindingPROSITE-ProRule annotationAdd
BLAST
Domaini850 – 88637EGF-like 22; calcium-bindingPROSITE-ProRule annotationAdd
BLAST
Domaini888 – 92336EGF-like 23; calcium-bindingPROSITE-ProRule annotationAdd
BLAST
Domaini925 – 96137EGF-like 24PROSITE-ProRule annotationAdd
BLAST
Domaini963 – 99937EGF-like 25PROSITE-ProRule annotationAdd
BLAST
Domaini1001 – 103535EGF-like 26PROSITE-ProRule annotationAdd
BLAST
Domaini1037 – 108347EGF-like 27PROSITE-ProRule annotationAdd
BLAST
Domaini1085 – 112137EGF-like 28PROSITE-ProRule annotationAdd
BLAST
Domaini1123 – 115937EGF-like 29; calcium-bindingPROSITE-ProRule annotationAdd
BLAST
Domaini1161 – 120444EGF-like 30; calcium-bindingPROSITE-ProRule annotationAdd
BLAST
Domaini1206 – 124540EGF-like 31PROSITE-ProRule annotationAdd
BLAST
Domaini1247 – 128842EGF-like 32PROSITE-ProRule annotationAdd
BLAST
Domaini1290 – 132637EGF-like 33PROSITE-ProRule annotationAdd
BLAST
Domaini1336 – 137439EGF-like 34PROSITE-ProRule annotationAdd
BLAST
Repeati1388 – 142841LNR 1Add
BLAST
Repeati1429 – 146638LNR 2Add
BLAST
Repeati1468 – 150639LNR 3Add
BLAST
Repeati1839 – 186830ANK 1Add
BLAST
Repeati1872 – 190231ANK 2Add
BLAST
Repeati1906 – 193530ANK 3Add
BLAST
Repeati1939 – 196830ANK 4Add
BLAST
Repeati1972 – 200130ANK 5Add
BLAST

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni2242 – 226120PEST-likeAdd
BLAST

Sequence similaritiesi

Belongs to the NOTCH family.Curated
Contains 5 ANK repeats.PROSITE-ProRule annotation
Contains 34 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

eggNOGiENOG410KD9W. Eukaryota.
COG0666. LUCA.
GeneTreeiENSGT00810000125346.
HOGENOMiHOG000234369.
HOVERGENiHBG052650.
InParanoidiQ61982.
KOiK02599.
OMAiADHFADG.
OrthoDBiEOG7992RD.
PhylomeDBiQ61982.
TreeFamiTF351641.

Family and domain databases

Gene3Di1.25.40.20. 1 hit.
InterProiIPR002110. Ankyrin_rpt.
IPR020683. Ankyrin_rpt-contain_dom.
IPR024600. DUF3454_notch.
IPR001881. EGF-like_Ca-bd_dom.
IPR013032. EGF-like_CS.
IPR000742. EGF-like_dom.
IPR000152. EGF-type_Asp/Asn_hydroxyl_site.
IPR018097. EGF_Ca-bd_CS.
IPR009030. Growth_fac_rcpt_.
IPR022331. Notch_3.
IPR000800. Notch_dom.
IPR010660. Notch_NOD_dom.
IPR011656. Notch_NODP_dom.
[Graphical view]
PfamiPF12796. Ank_2. 2 hits.
PF11936. DUF3454. 1 hit.
PF00008. EGF. 18 hits.
PF07645. EGF_CA. 7 hits.
PF12661. hEGF. 4 hits.
PF06816. NOD. 1 hit.
PF07684. NODP. 1 hit.
PF00066. Notch. 3 hits.
[Graphical view]
PRINTSiPR01452. LNOTCHREPEAT.
PR01986. NOTCH3.
SMARTiSM00248. ANK. 6 hits.
SM01334. DUF3454. 1 hit.
SM00181. EGF. 34 hits.
SM00179. EGF_CA. 30 hits.
SM00004. NL. 3 hits.
SM01338. NOD. 1 hit.
SM01339. NODP. 1 hit.
[Graphical view]
SUPFAMiSSF48403. SSF48403. 1 hit.
SSF57184. SSF57184. 5 hits.
SSF90193. SSF90193. 3 hits.
PROSITEiPS50297. ANK_REP_REGION. 1 hit.
PS50088. ANK_REPEAT. 4 hits.
PS00010. ASX_HYDROXYL. 18 hits.
PS00022. EGF_1. 33 hits.
PS01186. EGF_2. 27 hits.
PS50026. EGF_3. 34 hits.
PS01187. EGF_CA. 16 hits.
PS50258. LNR. 3 hits.
[Graphical view]

Sequencei

Sequence statusi: Complete.

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

Q61982-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MGLGARGRRR RRRLMALPPP PPPMRALPLL LLLAGLGAAA PPCLDGSPCA
60 70 80 90 100
NGGRCTHQQP SLEAACLCLP GWVGERCQLE DPCHSGPCAG RGVCQSSVVA
110 120 130 140 150
GTARFSCRCL RGFQGPDCSQ PDPCVSRPCV HGAPCSVGPD GRFACACPPG
160 170 180 190 200
YQGQSCQSDI DECRSGTTCR HGGTCLNTPG SFRCQCPLGY TGLLCENPVV
210 220 230 240 250
PCAPSPCRNG GTCRQSSDVT YDCACLPGFE GQNCEVNVDD CPGHRCLNGG
260 270 280 290 300
TCVDGVNTYN CQCPPEWTGQ FCTEDVDECQ LQPNACHNGG TCFNLLGGHS
310 320 330 340 350
CVCVNGWTGE SCSQNIDDCA TAVCFHGATC HDRVASFYCA CPMGKTGLLC
360 370 380 390 400
HLDDACVSNP CHEDAICDTN PVSGRAICTC PPGFTGGACD QDVDECSIGA
410 420 430 440 450
NPCEHLGRCV NTQGSFLCQC GRGYTGPRCE TDVNECLSGP CRNQATCLDR
460 470 480 490 500
IGQFTCICMA GFTGTYCEVD IDECQSSPCV NGGVCKDRVN GFSCTCPSGF
510 520 530 540 550
SGSMCQLDVD ECASTPCRNG AKCVDQPDGY ECRCAEGFEG TLCERNVDDC
560 570 580 590 600
SPDPCHHGRC VDGIASFSCA CAPGYTGIRC ESQVDECRSQ PCRYGGKCLD
610 620 630 640 650
LVDKYLCRCP PGTTGVNCEV NIDDCASNPC TFGVCRDGIN RYDCVCQPGF
660 670 680 690 700
TGPLCNVEIN ECASSPCGEG GSCVDGENGF HCLCPPGSLP PLCLPANHPC
710 720 730 740 750
AHKPCSHGVC HDAPGGFRCV CEPGWSGPRC SQSLAPDACE SQPCQAGGTC
760 770 780 790 800
TSDGIGFRCT CAPGFQGHQC EVLSPCTPSL CEHGGHCESD PDRLTVCSCP
810 820 830 840 850
PGWQGPRCQQ DVDECAGASP CGPHGTCTNL PGNFRCICHR GYTGPFCDQD
860 870 880 890 900
IDDCDPNPCL HGGSCQDGVG SFSCSCLDGF AGPRCARDVD ECLSSPCGPG
910 920 930 940 950
TCTDHVASFT CACPPGYGGF HCEIDLPDCS PSSCFNGGTC VDGVSSFSCL
960 970 980 990 1000
CRPGYTGTHC QYEADPCFSR PCLHGGICNP THPGFECTCR EGFTGSQCQN
1010 1020 1030 1040 1050
PVDWCSQAPC QNGGRCVQTG AYCICPPGWS GRLCDIQSLP CTEAAAQMGV
1060 1070 1080 1090 1100
RLEQLCQEGG KCIDKGRSHY CVCPEGRTGS HCEHEVDPCT AQPCQHGGTC
1110 1120 1130 1140 1150
RGYMGGYVCE CPAGYAGDSC EDNIDECASQ PCQNGGSCID LVARYLCSCP
1160 1170 1180 1190 1200
PGTLGVLCEI NEDDCDLGPS LDSGVQCLHN GTCVDLVGGF RCNCPPGYTG
1210 1220 1230 1240 1250
LHCEADINEC RPGACHAAHT RDCLQDPGGH FRCVCHPGFT GPRCQIALSP
1260 1270 1280 1290 1300
CESQPCQHGG QCRHSLGRGG GLTFTCHCVP PFWGLRCERV ARSCRELQCP
1310 1320 1330 1340 1350
VGIPCQQTAR GPRCACPPGL SGPSCRVSRA SPSGATNASC ASAPCLHGGS
1360 1370 1380 1390 1400
CLPVQSVPFF RCVCAPGWGG PRCETPSAAP EVPEEPRCPR AACQAKRGDQ
1410 1420 1430 1440 1450
NCDRECNTPG CGWDGGDCSL NVDDPWRQCE ALQCWRLFNN SRCDPACSSP
1460 1470 1480 1490 1500
ACLYDNFDCY SGGRDRTCNP VYEKYCADHF ADGRCDQGCN TEECGWDGLD
1510 1520 1530 1540 1550
CASEVPALLA RGVLVLTVLL PPEELLRSSA DFLQRLSAIL RTSLRFRLDA
1560 1570 1580 1590 1600
RGQAMVFPYH RPSPGSESRV RRELGPEVIG SVVMLEIDNR LCLQSAENDH
1610 1620 1630 1640 1650
CFPDAQSAAD YLGALSAVER LDFPYPLRDV RGEPLEAPEQ SVPLLPLLVA
1660 1670 1680 1690 1700
GAVFLLIIFI LGVMVARRKR EHSTLWFPEG FALHKDIAAG HKGRREPVGQ
1710 1720 1730 1740 1750
DALGMKNMAK GESLMGEVVT DLNDSECPEA KRLKVEEPGM GAEEPEDCRQ
1760 1770 1780 1790 1800
WTQHHLVAAD IRVAPATALT PPQGDADADG VDVNVRGPDG FTPLMLASFC
1810 1820 1830 1840 1850
GGALEPMPAE EDEADDTSAS IISDLICQGA QLGARTDRTG ETALHLAARY
1860 1870 1880 1890 1900
ARADAAKRLL DAGADTNAQD HSGRTPLHTA VTADAQGVFQ ILIRNRSTDL
1910 1920 1930 1940 1950
DARMADGSTA LILAARLAVE GMVEELIASH ADVNAVDELG KSALHWAAAV
1960 1970 1980 1990 2000
NNVEATLALL KNGANKDMQD SKEETPLFLA AREGSYEAAK LLLDHLANRE
2010 2020 2030 2040 2050
ITDHLDRLPR DVAQERLHQD IVRLLDQPSG PRSPSGPHGL GPLLCPPGAF
2060 2070 2080 2090 2100
LPGLKAVQSG TKKSRRPPGK TGLGPQGTRG RGKKLTLACP GPLADSSVTL
2110 2120 2130 2140 2150
SPVDSLDSPR PFSGPPASPG GFPLEGPYAT TATAVSLAQL GASRAGPLGR
2160 2170 2180 2190 2200
QPPGGCVLSF GLLNPVAVPL DWARLPPPAP PGPSFLLPLA PGPQLLNPGA
2210 2220 2230 2240 2250
PVSPQERPPP YLAAPGHGEE YPAAGTRSSP TKARFLRVPS EHPYLTPSPE
2260 2270 2280 2290 2300
SPEHWASPSP PSLSDWSDST PSPATATNAT ASGALPAQPH PISVPSLPQS
2310
QTQLGPQPEV TPKRQVMA
Length:2,318
Mass (Da):244,248
Last modified:November 1, 1997 - v1
Checksum:iA80D1F75AFF0185A
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X74760 mRNA. Translation: CAA52776.1.
CCDSiCCDS28614.1.
PIRiS45306.
RefSeqiNP_032742.1. NM_008716.2.
UniGeneiMm.439741.

Genome annotation databases

EnsembliENSMUST00000087723; ENSMUSP00000085016; ENSMUSG00000038146.
GeneIDi18131.
KEGGimmu:18131.
UCSCiuc008bvx.1. mouse.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X74760 mRNA. Translation: CAA52776.1.
CCDSiCCDS28614.1.
PIRiS45306.
RefSeqiNP_032742.1. NM_008716.2.
UniGeneiMm.439741.

3D structure databases

ProteinModelPortaliQ61982.
SMRiQ61982. Positions 392-506, 1792-2027.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi201811. 5 interactions.
IntActiQ61982. 4 interactions.
MINTiMINT-1955915.
STRINGi10090.ENSMUSP00000085016.

PTM databases

iPTMnetiQ61982.
PhosphoSiteiQ61982.

Proteomic databases

MaxQBiQ61982.
PaxDbiQ61982.
PRIDEiQ61982.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSMUST00000087723; ENSMUSP00000085016; ENSMUSG00000038146.
GeneIDi18131.
KEGGimmu:18131.
UCSCiuc008bvx.1. mouse.

Organism-specific databases

CTDi4854.
MGIiMGI:99460. Notch3.

Phylogenomic databases

eggNOGiENOG410KD9W. Eukaryota.
COG0666. LUCA.
GeneTreeiENSGT00810000125346.
HOGENOMiHOG000234369.
HOVERGENiHBG052650.
InParanoidiQ61982.
KOiK02599.
OMAiADHFADG.
OrthoDBiEOG7992RD.
PhylomeDBiQ61982.
TreeFamiTF351641.

Enzyme and pathway databases

ReactomeiR-MMU-1912420. Pre-NOTCH Processing in Golgi.
R-MMU-1980148. Signaling by NOTCH3.
R-MMU-350054. Notch-HLH transcription pathway.

Miscellaneous databases

NextBioi293368.
PROiQ61982.
SOURCEiSearch...

Gene expression databases

BgeeiQ61982.
CleanExiMM_NOTCH3.
GenevisibleiQ61982. MM.

Family and domain databases

Gene3Di1.25.40.20. 1 hit.
InterProiIPR002110. Ankyrin_rpt.
IPR020683. Ankyrin_rpt-contain_dom.
IPR024600. DUF3454_notch.
IPR001881. EGF-like_Ca-bd_dom.
IPR013032. EGF-like_CS.
IPR000742. EGF-like_dom.
IPR000152. EGF-type_Asp/Asn_hydroxyl_site.
IPR018097. EGF_Ca-bd_CS.
IPR009030. Growth_fac_rcpt_.
IPR022331. Notch_3.
IPR000800. Notch_dom.
IPR010660. Notch_NOD_dom.
IPR011656. Notch_NODP_dom.
[Graphical view]
PfamiPF12796. Ank_2. 2 hits.
PF11936. DUF3454. 1 hit.
PF00008. EGF. 18 hits.
PF07645. EGF_CA. 7 hits.
PF12661. hEGF. 4 hits.
PF06816. NOD. 1 hit.
PF07684. NODP. 1 hit.
PF00066. Notch. 3 hits.
[Graphical view]
PRINTSiPR01452. LNOTCHREPEAT.
PR01986. NOTCH3.
SMARTiSM00248. ANK. 6 hits.
SM01334. DUF3454. 1 hit.
SM00181. EGF. 34 hits.
SM00179. EGF_CA. 30 hits.
SM00004. NL. 3 hits.
SM01338. NOD. 1 hit.
SM01339. NODP. 1 hit.
[Graphical view]
SUPFAMiSSF48403. SSF48403. 1 hit.
SSF57184. SSF57184. 5 hits.
SSF90193. SSF90193. 3 hits.
PROSITEiPS50297. ANK_REP_REGION. 1 hit.
PS50088. ANK_REPEAT. 4 hits.
PS00010. ASX_HYDROXYL. 18 hits.
PS00022. EGF_1. 33 hits.
PS01186. EGF_2. 27 hits.
PS50026. EGF_3. 34 hits.
PS01187. EGF_CA. 16 hits.
PS50258. LNR. 3 hits.
[Graphical view]
ProtoNetiSearch...

Publicationsi

  1. "The novel Notch homologue mouse Notch 3 lacks specific epidermal growth factor-repeats and is expressed in proliferating neuroepithelium."
    Lardelli M., Dalstrand J., Lendahl U.
    Mech. Dev. 46:123-136(1994) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
    Strain: ICR X Swiss Webster.
  2. "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-1664.
  3. "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.
  4. "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.
  5. Cited for: INTERACTION WITH HIF1AN.
  6. "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.

Entry informationi

Entry nameiNOTC3_MOUSE
AccessioniPrimary (citable) accession number: Q61982
Entry historyi
Integrated into UniProtKB/Swiss-Prot: November 1, 1997
Last sequence update: November 1, 1997
Last modified: May 11, 2016
This is version 163 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

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.