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Protein

Neurogenic locus notch homolog protein 4

Gene

Notch4

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 regulate branching morphogenesis in the developing vascular system.By similarity1 Publication

GO - Molecular functioni

  • calcium ion binding Source: InterPro
  • Notch binding Source: MGI

GO - Biological processi

  • cell differentiation Source: UniProtKB-KW
  • embryo development Source: UniProtKB
  • mammary gland development Source: MGI
  • morphogenesis of a branching structure Source: UniProtKB
  • negative regulation of endothelial cell differentiation Source: UniProtKB
  • negative regulation of Notch signaling pathway Source: MGI
  • Notch signaling pathway Source: UniProtKB
  • patterning of blood vessels Source: UniProtKB
  • positive regulation of angiogenesis Source: MGI
  • positive regulation of aorta morphogenesis Source: MGI
  • regulation of Notch signaling pathway Source: MGI
  • regulation of protein localization Source: MGI
  • regulation of protein processing Source: MGI
  • regulation of transcription, DNA-templated Source: UniProtKB-KW
  • transcription, DNA-templated Source: UniProtKB-KW
  • venous blood vessel morphogenesis Source: MGI
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-1912399. Pre-NOTCH Processing in the Endoplasmic Reticulum.
R-MMU-1912420. Pre-NOTCH Processing in Golgi.

Names & Taxonomyi

Protein namesi
Recommended name:
Neurogenic locus notch homolog protein 4
Short name:
Notch 4
Cleaved into the following 3 chains:
Gene namesi
Name:Notch4
Synonyms:Int-3, Int3
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
Proteomesi
  • UP000000589 Componenti: Unplaced

Organism-specific databases

MGIiMGI:107471. Notch4.

Subcellular locationi

Notch 4 intracellular domain :
  • Nucleus

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

Topology

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Topological domaini21 – 14431423ExtracellularSequence analysisAdd
BLAST
Transmembranei1444 – 146421HelicalSequence analysisAdd
BLAST
Topological domaini1465 – 1964500CytoplasmicSequence analysisAdd
BLAST

GO - Cellular componenti

  • cell surface Source: UniProtKB
  • cytoplasmic vesicle Source: MGI
  • endoplasmic reticulum Source: MGI
  • integral component of membrane Source: UniProtKB-KW
  • nucleus Source: UniProtKB-SubCell
  • plasma membrane Source: UniProtKB-SubCell
Complete GO annotation...

Keywords - Cellular componenti

Cell membrane, Membrane, Nucleus

Pathology & Biotechi

Involvement in diseasei

Loss of the extracellular domain causes constitutive activation of the Notch protein, which leads to hyperproliferation of glandular epithelial tissues and development of mammary carcinomas.

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi1463 – 14631V → L: NICD processing severely reduced. 1 Publication

Keywords - Diseasei

Proto-oncogene

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Signal peptidei1 – 2020Sequence analysisAdd
BLAST
Chaini21 – 19641944Neurogenic locus notch homolog protein 4PRO_0000007704Add
BLAST
Chaini1411 – 1964554Transforming protein Int-3PRO_0000007705Add
BLAST
Chaini1428 – 1964537Notch 4 extracellular truncationPRO_0000007706Add
BLAST
Chaini1463 – 1964502Notch 4 intracellular domainPRO_0000007707Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Disulfide bondi25 ↔ 38By similarity
Disulfide bondi32 ↔ 48By similarity
Disulfide bondi50 ↔ 59By similarity
Disulfide bondi65 ↔ 77By similarity
Disulfide bondi71 ↔ 100By similarity
Disulfide bondi102 ↔ 111By similarity
Disulfide bondi119 ↔ 130By similarity
Disulfide bondi124 ↔ 140By similarity
Disulfide bondi142 ↔ 151By similarity
Disulfide bondi157 ↔ 168By similarity
Disulfide bondi162 ↔ 177By similarity
Disulfide bondi179 ↔ 188By similarity
Disulfide bondi195 ↔ 208By similarity
Disulfide bondi202 ↔ 217By similarity
Disulfide bondi219 ↔ 228By similarity
Disulfide bondi235 ↔ 246By similarity
Disulfide bondi240 ↔ 259By similarity
Disulfide bondi261 ↔ 270By similarity
Disulfide bondi277 ↔ 288By similarity
Disulfide bondi282 ↔ 297By similarity
Disulfide bondi299 ↔ 308By similarity
Disulfide bondi315 ↔ 329By similarity
Disulfide bondi323 ↔ 338By similarity
Disulfide bondi340 ↔ 349By similarity
Disulfide bondi356 ↔ 367By similarity
Disulfide bondi361 ↔ 376By similarity
Disulfide bondi378 ↔ 387By similarity
Disulfide bondi393 ↔ 404By similarity
Disulfide bondi398 ↔ 415By similarity
Disulfide bondi417 ↔ 426By similarity
Disulfide bondi433 ↔ 449By similarity
Disulfide bondi443 ↔ 458By similarity
Disulfide bondi460 ↔ 469By similarity
Disulfide bondi476 ↔ 487By similarity
Disulfide bondi481 ↔ 496By similarity
Disulfide bondi498 ↔ 507By similarity
Disulfide bondi514 ↔ 525By similarity
Disulfide bondi519 ↔ 534By similarity
Disulfide bondi536 ↔ 545By similarity
Disulfide bondi552 ↔ 563By similarity
Disulfide bondi557 ↔ 572By similarity
Disulfide bondi574 ↔ 583By similarity
Disulfide bondi590 ↔ 601By similarity
Disulfide bondi595 ↔ 610By similarity
Disulfide bondi612 ↔ 621By similarity
Disulfide bondi626 ↔ 637By similarity
Disulfide bondi631 ↔ 646By similarity
Disulfide bondi648 ↔ 655By similarity
Disulfide bondi662 ↔ 669By similarity
Disulfide bondi664 ↔ 674By similarity
Disulfide bondi676 ↔ 685By similarity
Disulfide bondi692 ↔ 703By similarity
Disulfide bondi697 ↔ 712By similarity
Glycosylationi711 – 7111N-linked (GlcNAc...)Sequence analysis
Disulfide bondi714 ↔ 723By similarity
Disulfide bondi730 ↔ 741By similarity
Disulfide bondi735 ↔ 750By similarity
Disulfide bondi752 ↔ 761By similarity
Disulfide bondi768 ↔ 779By similarity
Disulfide bondi773 ↔ 788By similarity
Disulfide bondi790 ↔ 799By similarity
Disulfide bondi807 ↔ 818By similarity
Disulfide bondi812 ↔ 827By similarity
Disulfide bondi829 ↔ 838By similarity
Disulfide bondi845 ↔ 856By similarity
Disulfide bondi850 ↔ 865By similarity
Disulfide bondi867 ↔ 876By similarity
Disulfide bondi882 ↔ 903By similarity
Disulfide bondi897 ↔ 912By similarity
Disulfide bondi914 ↔ 923By similarity
Disulfide bondi930 ↔ 941By similarity
Disulfide bondi935 ↔ 950By similarity
Disulfide bondi952 ↔ 961By similarity
Glycosylationi960 – 9601N-linked (GlcNAc...)Sequence analysis
Disulfide bondi968 ↔ 979By similarity
Disulfide bondi973 ↔ 988By similarity
Disulfide bondi990 ↔ 999By similarity
Disulfide bondi1006 ↔ 1019By similarity
Disulfide bondi1011 ↔ 1028By similarity
Disulfide bondi1030 ↔ 1039By similarity
Disulfide bondi1046 ↔ 1057By similarity
Disulfide bondi1051 ↔ 1069By similarity
Disulfide bondi1071 ↔ 1080By similarity
Disulfide bondi1087 ↔ 1098By similarity
Disulfide bondi1092 ↔ 1110By similarity
Disulfide bondi1112 ↔ 1121By similarity
Disulfide bondi1130 ↔ 1142By similarity
Disulfide bondi1136 ↔ 1155By similarity
Glycosylationi1139 – 11391N-linked (GlcNAc...)Sequence analysis
Disulfide bondi1157 ↔ 1166By similarity
Disulfide bondi1174 ↔ 1187By similarity
Disulfide bondi1183 ↔ 1199By similarity
Disulfide bondi1210 ↔ 1234By similarity
Disulfide bondi1216 ↔ 1229By similarity
Disulfide bondi1225 ↔ 1241By similarity
Disulfide bondi1247 ↔ 1273By similarity
Disulfide bondi1255 ↔ 1268By similarity
Disulfide bondi1264 ↔ 1280By 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.

Keywords - PTMi

Disulfide bond, Glycoprotein, Phosphoprotein

Proteomic databases

MaxQBiP31695.
PaxDbiP31695.
PRIDEiP31695.

PTM databases

iPTMnetiP31695.
PhosphoSiteiP31695.

Expressioni

Tissue specificityi

Highly expressed in lung, moderately in heart kidney, and at lower levels in the ovary and skeletal muscle. A very low expression is seen in the brain, intestine, liver and testis.

Developmental stagei

Highly expressed in endothelial cells during embryonic development from 9.0 dpc.

Gene expression databases

CleanExiMM_NOTCH4.

Interactioni

Subunit structurei

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 NOTCH4.1 Publication

Binary interactionsi

WithEntry#Exp.IntActNotes
sel-10Q937942EBI-643670,EBI-323098From a different organism.

GO - Molecular functioni

  • Notch binding Source: MGI

Protein-protein interaction databases

BioGridi201812. 6 interactions.
IntActiP31695. 2 interactions.
MINTiMINT-1713714.
STRINGi10090.ENSMUSP00000015612.

Structurei

3D structure databases

ProteinModelPortaliP31695.
SMRiP31695. Positions 30-1121, 1183-1340, 1579-1882.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini21 – 6040EGF-like 1PROSITE-ProRule annotationAdd
BLAST
Domaini61 – 11252EGF-like 2PROSITE-ProRule annotationAdd
BLAST
Domaini115 – 15238EGF-like 3PROSITE-ProRule annotationAdd
BLAST
Domaini153 – 18937EGF-like 4PROSITE-ProRule annotationAdd
BLAST
Domaini191 – 22939EGF-like 5; calcium-bindingPROSITE-ProRule annotationAdd
BLAST
Domaini231 – 27141EGF-like 6PROSITE-ProRule annotationAdd
BLAST
Domaini273 – 30937EGF-like 7; calcium-bindingPROSITE-ProRule annotationAdd
BLAST
Domaini311 – 35040EGF-like 8; calcium-bindingPROSITE-ProRule annotationAdd
BLAST
Domaini352 – 38837EGF-like 9; calcium-bindingPROSITE-ProRule annotationAdd
BLAST
Domaini389 – 42739EGF-like 10PROSITE-ProRule annotationAdd
BLAST
Domaini429 – 47042EGF-like 11; calcium-bindingPROSITE-ProRule annotationAdd
BLAST
Domaini472 – 50837EGF-like 12; calcium-bindingPROSITE-ProRule annotationAdd
BLAST
Domaini510 – 54637EGF-like 13; calcium-bindingPROSITE-ProRule annotationAdd
BLAST
Domaini548 – 58437EGF-like 14; calcium-bindingPROSITE-ProRule annotationAdd
BLAST
Domaini586 – 62237EGF-like 15; calcium-bindingPROSITE-ProRule annotationAdd
BLAST
Domaini623 – 65634EGF-like 16PROSITE-ProRule annotationAdd
BLAST
Domaini658 – 68629EGF-like 17PROSITE-ProRule annotationAdd
BLAST
Domaini688 – 72437EGF-like 18PROSITE-ProRule annotationAdd
BLAST
Domaini726 – 76237EGF-like 19PROSITE-ProRule annotationAdd
BLAST
Domaini764 – 80037EGF-like 20PROSITE-ProRule annotationAdd
BLAST
Domaini803 – 83937EGF-like 21PROSITE-ProRule annotationAdd
BLAST
Domaini841 – 87737EGF-like 22PROSITE-ProRule annotationAdd
BLAST
Domaini878 – 92447EGF-like 23PROSITE-ProRule annotationAdd
BLAST
Domaini926 – 96237EGF-like 24PROSITE-ProRule annotationAdd
BLAST
Domaini964 – 100037EGF-like 25PROSITE-ProRule annotationAdd
BLAST
Domaini1002 – 104039EGF-like 26PROSITE-ProRule annotationAdd
BLAST
Domaini1042 – 108140EGF-like 27PROSITE-ProRule annotationAdd
BLAST
Domaini1083 – 112240EGF-like 28PROSITE-ProRule annotationAdd
BLAST
Domaini1126 – 116742EGF-like 29PROSITE-ProRule annotationAdd
BLAST
Repeati1166 – 120944LNR 1Add
BLAST
Repeati1210 – 124132LNR 2Add
BLAST
Repeati1247 – 128741LNR 3Add
BLAST
Repeati1628 – 165730ANK 1Add
BLAST
Repeati1661 – 169131ANK 2Add
BLAST
Repeati1695 – 172430ANK 3Add
BLAST
Repeati1728 – 175730ANK 4Add
BLAST
Repeati1761 – 179030ANK 5Add
BLAST

Sequence similaritiesi

Belongs to the NOTCH family.Curated
Contains 5 ANK repeats.PROSITE-ProRule annotation
Contains 29 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

eggNOGiENOG410IR7G. Eukaryota.
COG0666. LUCA.
HOVERGENiHBG052650.
InParanoidiP31695.
KOiK02599.
PhylomeDBiP31695.

Family and domain databases

Gene3Di1.25.40.20. 1 hit.
InterProiIPR002110. Ankyrin_rpt.
IPR020683. Ankyrin_rpt-contain_dom.
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_.
IPR022355. Notch_4.
IPR000800. Notch_dom.
IPR010660. Notch_NOD_dom.
IPR011656. Notch_NODP_dom.
[Graphical view]
PfamiPF12796. Ank_2. 1 hit.
PF00008. EGF. 17 hits.
PF07645. EGF_CA. 4 hits.
PF12661. hEGF. 2 hits.
PF07684. NODP. 1 hit.
PF00066. Notch. 3 hits.
[Graphical view]
PRINTSiPR01452. LNOTCHREPEAT.
PR01987. NOTCH4.
SMARTiSM00248. ANK. 6 hits.
SM00181. EGF. 28 hits.
SM00179. EGF_CA. 21 hits.
SM00004. NL. 3 hits.
SM01338. NOD. 1 hit.
SM01339. NODP. 1 hit.
[Graphical view]
SUPFAMiSSF48403. SSF48403. 1 hit.
SSF57184. SSF57184. 4 hits.
SSF90193. SSF90193. 2 hits.
PROSITEiPS50297. ANK_REP_REGION. 1 hit.
PS50088. ANK_REPEAT. 5 hits.
PS00010. ASX_HYDROXYL. 11 hits.
PS00022. EGF_1. 28 hits.
PS01186. EGF_2. 21 hits.
PS50026. EGF_3. 27 hits.
PS01187. EGF_CA. 9 hits.
PS50258. LNR. 3 hits.
[Graphical view]

Sequencei

Sequence statusi: Complete.

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

P31695-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MQPQLLLLLL LPLNFPVILT RELLCGGSPE PCANGGTCLR LSQGQGICQC
60 70 80 90 100
APGFLGETCQ FPDPCRDTQL CKNGGSCQAL LPTPPSSRSP TSPLTPHFSC
110 120 130 140 150
TCPSGFTGDR CQTHLEELCP PSFCSNGGHC YVQASGRPQC SCEPGWTGEQ
160 170 180 190 200
CQLRDFCSAN PCANGGVCLA TYPQIQCRCP PGFEGHTCER DINECFLEPG
210 220 230 240 250
PCPQGTSCHN TLGSYQCLCP VGQEGPQCKL RKGACPPGSC LNGGTCQLVP
260 270 280 290 300
EGHSTFHLCL CPPGFTGLDC EMNPDDCVRH QCQNGATCLD GLDTYTCLCP
310 320 330 340 350
KTWKGWDCSE DIDECEARGP PRCRNGGTCQ NTAGSFHCVC VSGWGGAGCE
360 370 380 390 400
ENLDDCAAAT CAPGSTCIDR VGSFSCLCPP GRTGLLCHLE DMCLSQPCHV
410 420 430 440 450
NAQCSTNPLT GSTLCICQPG YSGSTCHQDL DECQMAQQGP SPCEHGGSCI
460 470 480 490 500
NTPGSFNCLC LPGYTGSRCE ADHNECLSQP CHPGSTCLDL LATFHCLCPP
510 520 530 540 550
GLEGRLCEVE VNECTSNPCL NQAACHDLLN GFQCLCLPGF TGARCEKDMD
560 570 580 590 600
ECSSTPCANG GRCRDQPGAF YCECLPGFEG PHCEKEVDEC LSDPCPVGAS
610 620 630 640 650
CLDLPGAFFC LCRPGFTGQL CEVPLCTPNM CQPGQQCQGQ EHRAPCLCPD
660 670 680 690 700
GSPGCVPAED NCPCHHGHCQ RSLCVCDEGW TGPECETELG GCISTPCAHG
710 720 730 740 750
GTCHPQPSGY NCTCPAGYMG LTCSEEVTAC HSGPCLNGGS CSIRPEGYSC
760 770 780 790 800
TCLPSHTGRH CQTAVDHCVS ASCLNGGTCV NKPGTFFCLC ATGFQGLHCE
810 820 830 840 850
EKTNPSCADS PCRNKATCQD TPRGARCLCS PGYTGSSCQT LIDLCARKPC
860 870 880 890 900
PHTARCLQSG PSFQCLCLQG WTGALCDFPL SCQMAAMSQG IEISGLCQNG
910 920 930 940 950
GLCIDTGSSY FCRCPPGFQG KLCQDNMNPC EPNPCHHGST CVPQPSGYVC
960 970 980 990 1000
QCAPGYEGQN CSKVLEACQS QPCHNHGTCT SRPGGFHCAC PPGFVGLRCE
1010 1020 1030 1040 1050
GDVDECLDRP CHPSGTAACH SLANAFYCQC LPGHTGQRCE VEMDLCQSQP
1060 1070 1080 1090 1100
CSNGGSCEIT TGPPPGFTCH CPKGFEGPTC SHKALSCGIH HCHNGGLCLP
1110 1120 1130 1140 1150
SPKPGSPPLC ACLSGFGGPD CLTPPAPPGC GPPSPCLHNG TCTETPGLGN
1160 1170 1180 1190 1200
PGFQCTCPPD SPGPRCQRPG ASGCEGRGGD GTCDAGCSGP GGDWDGGDCS
1210 1220 1230 1240 1250
LGVPDPWKGC PPHSQCWLLF RDGRCHPQCD SEECLFDGYD CEIPLTCIPA
1260 1270 1280 1290 1300
YDQYCRDHFH NGHCEKGCNN AECGWDGGDC RPEGEDSEGR PSLALLVVLR
1310 1320 1330 1340 1350
PPALDQQLLA LARVLSLTLR VGLWVRKDSE GRNMVFPYPG TRAKEELSGA
1360 1370 1380 1390 1400
RDSSSWERQA PPTQPLGKET ESLGAGFVVV MGVDLSRCGP EHPASRCPWD
1410 1420 1430 1440 1450
SGLLLRFLAA MAAVGALEPL LPGPLLAAHP QAGTRPPANQ LPWPILCSPV
1460 1470 1480 1490 1500
VGVLLLALGA LLVLQLIRRR RREHGALWLP PGFIRRPQAQ QAPHRRRPPL
1510 1520 1530 1540 1550
GEDNIGLKAL KPEAEVDEDG VAMCSGPEEG EAEETASASR CQLWPLNSSC
1560 1570 1580 1590 1600
GELPQAAMLT PPQECESEVL DVDTCGPDGV TPLMSAVFCG GVQSTTGASP
1610 1620 1630 1640 1650
QRLGLGNLEP WEPLLDRGAC PQAHTVGTGE TPLHLAARFS RPTAARRLLE
1660 1670 1680 1690 1700
AGANPNQPDR AGRTPLHTAV AADAREVCQL LLASRQTSVD ARTEDGTTPL
1710 1720 1730 1740 1750
MLAARLAVED LVEELIAARA DVGARDKRGK TALHWAAAVN NARAARSLLQ
1760 1770 1780 1790 1800
AGADKDAQDS REQTPLFLAA REGAVEVAQL LLELGAARGL RDQAGLAPGD
1810 1820 1830 1840 1850
VARQRSHWDL LTLLEGAGPT TQEARAHART TPGGGAAARC RTLSAGARPR
1860 1870 1880 1890 1900
GGGACLQART WSVDLGARGG KVYARCRSRS GSCGGPTTRG RRFSAGSRGR
1910 1920 1930 1940 1950
RGARASQDDW PRDWVALEAC GSACSAPIPP PSLTPSPERG SPQVAWGLPV
1960
HQEIPLNSVV RNLN
Length:1,964
Mass (Da):206,693
Last modified:November 1, 1997 - v2
Checksum:i213B65D11BF489BE
GO

Sequence cautioni

The sequence BAA32281.1 differs from that shown.Curated
The sequence BAA32283.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally shortened.Curated
The sequence BAA32284.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally extended.Curated

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti43 – 431Q → R in AAC52630 (PubMed:8681805).Curated
Sequence conflicti43 – 431Q → R in AAB82004 (PubMed:14656967).Curated
Sequence conflicti298 – 2981L → P in AAC52630 (PubMed:8681805).Curated
Sequence conflicti884 – 8841M → K in AAC52630 (PubMed:8681805).Curated
Sequence conflicti884 – 8841M → K in AAB82004 (PubMed:14656967).Curated
Sequence conflicti927 – 9271M → V in AAC52630 (PubMed:8681805).Curated
Sequence conflicti927 – 9271M → V in AAB82004 (PubMed:14656967).Curated
Sequence conflicti966 – 9661E → D in AAC52630 (PubMed:8681805).Curated
Sequence conflicti966 – 9661E → D in AAB82004 (PubMed:14656967).Curated
Sequence conflicti1245 – 12451L → P in AAC52630 (PubMed:8681805).Curated
Sequence conflicti1437 – 14371P → S in AAB82004 (PubMed:14656967).Curated
Sequence conflicti1469 – 14691R → Q in BAA32283 (PubMed:10233982).Curated
Sequence conflicti1469 – 14691R → Q in BAA32284 (PubMed:10233982).Curated
Sequence conflicti1489 – 14891A → T in AAC52630 (PubMed:8681805).Curated
Sequence conflicti1489 – 14891A → T in AAC52631 (PubMed:8681805).Curated
Sequence conflicti1489 – 14891A → T in AAB82004 (PubMed:14656967).Curated
Sequence conflicti1489 – 14891A → T in BAA32283 (PubMed:10233982).Curated
Sequence conflicti1489 – 14891A → T in BAA32284 (PubMed:10233982).Curated
Sequence conflicti1549 – 15491S → G in AAC52630 (PubMed:8681805).Curated
Sequence conflicti1549 – 15491S → G in AAC52631 (PubMed:8681805).Curated
Sequence conflicti1549 – 15491S → G in AAB82004 (PubMed:14656967).Curated
Sequence conflicti1549 – 15491S → G in BAA32283 (PubMed:10233982).Curated
Sequence conflicti1549 – 15491S → G in BAA32284 (PubMed:10233982).Curated
Sequence conflicti1549 – 15491S → G in BAA32285 (PubMed:10233982).Curated
Sequence conflicti1688 – 16881S → T in AAC52630 (PubMed:8681805).Curated
Sequence conflicti1688 – 16881S → T in AAC52631 (PubMed:8681805).Curated
Sequence conflicti1688 – 16881S → T in AAB82004 (PubMed:14656967).Curated
Sequence conflicti1836 – 18361A → S in AAC52630 (PubMed:8681805).Curated
Sequence conflicti1836 – 18361A → S in AAC52631 (PubMed:8681805).Curated
Sequence conflicti1838 – 18381A → P in AAC52630 (PubMed:8681805).Curated
Sequence conflicti1838 – 18381A → P in AAC52631 (PubMed:8681805).Curated
Sequence conflicti1838 – 18381A → P in AAB82004 (PubMed:14656967).Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M80456 mRNA. Translation: AAB38377.1.
U43691 mRNA. Translation: AAC52630.1.
U43691 mRNA. Translation: AAC52631.1.
AF030001 Genomic DNA. Translation: AAB82004.1.
AB016771 Genomic DNA. Translation: BAA32281.1. Sequence problems.
AB016772 mRNA. Translation: BAA32283.1. Different initiation.
AB016773 mRNA. Translation: BAA32284.1. Different initiation.
AB016774 mRNA. Translation: BAA32285.1.
CCDSiCCDS28647.1.
PIRiA38072. TVMVT3.
T09059.
RefSeqiNP_035059.2. NM_010929.2.
UniGeneiMm.173813.

Genome annotation databases

GeneIDi18132.
KEGGimmu:18132.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M80456 mRNA. Translation: AAB38377.1.
U43691 mRNA. Translation: AAC52630.1.
U43691 mRNA. Translation: AAC52631.1.
AF030001 Genomic DNA. Translation: AAB82004.1.
AB016771 Genomic DNA. Translation: BAA32281.1. Sequence problems.
AB016772 mRNA. Translation: BAA32283.1. Different initiation.
AB016773 mRNA. Translation: BAA32284.1. Different initiation.
AB016774 mRNA. Translation: BAA32285.1.
CCDSiCCDS28647.1.
PIRiA38072. TVMVT3.
T09059.
RefSeqiNP_035059.2. NM_010929.2.
UniGeneiMm.173813.

3D structure databases

ProteinModelPortaliP31695.
SMRiP31695. Positions 30-1121, 1183-1340, 1579-1882.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi201812. 6 interactions.
IntActiP31695. 2 interactions.
MINTiMINT-1713714.
STRINGi10090.ENSMUSP00000015612.

PTM databases

iPTMnetiP31695.
PhosphoSiteiP31695.

Proteomic databases

MaxQBiP31695.
PaxDbiP31695.
PRIDEiP31695.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

GeneIDi18132.
KEGGimmu:18132.

Organism-specific databases

CTDi4855.
MGIiMGI:107471. Notch4.

Phylogenomic databases

eggNOGiENOG410IR7G. Eukaryota.
COG0666. LUCA.
HOVERGENiHBG052650.
InParanoidiP31695.
KOiK02599.
PhylomeDBiP31695.

Enzyme and pathway databases

ReactomeiR-MMU-1912399. Pre-NOTCH Processing in the Endoplasmic Reticulum.
R-MMU-1912420. Pre-NOTCH Processing in Golgi.

Miscellaneous databases

PROiP31695.
SOURCEiSearch...

Gene expression databases

CleanExiMM_NOTCH4.

Family and domain databases

Gene3Di1.25.40.20. 1 hit.
InterProiIPR002110. Ankyrin_rpt.
IPR020683. Ankyrin_rpt-contain_dom.
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_.
IPR022355. Notch_4.
IPR000800. Notch_dom.
IPR010660. Notch_NOD_dom.
IPR011656. Notch_NODP_dom.
[Graphical view]
PfamiPF12796. Ank_2. 1 hit.
PF00008. EGF. 17 hits.
PF07645. EGF_CA. 4 hits.
PF12661. hEGF. 2 hits.
PF07684. NODP. 1 hit.
PF00066. Notch. 3 hits.
[Graphical view]
PRINTSiPR01452. LNOTCHREPEAT.
PR01987. NOTCH4.
SMARTiSM00248. ANK. 6 hits.
SM00181. EGF. 28 hits.
SM00179. EGF_CA. 21 hits.
SM00004. NL. 3 hits.
SM01338. NOD. 1 hit.
SM01339. NODP. 1 hit.
[Graphical view]
SUPFAMiSSF48403. SSF48403. 1 hit.
SSF57184. SSF57184. 4 hits.
SSF90193. SSF90193. 2 hits.
PROSITEiPS50297. ANK_REP_REGION. 1 hit.
PS50088. ANK_REPEAT. 5 hits.
PS00010. ASX_HYDROXYL. 11 hits.
PS00022. EGF_1. 28 hits.
PS01186. EGF_2. 21 hits.
PS50026. EGF_3. 27 hits.
PS01187. EGF_CA. 9 hits.
PS50258. LNR. 3 hits.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "Mouse mammary tumor gene int-3: a member of the notch gene family transforms mammary epithelial cells."
    Robbins J., Blondel B.J., Gallahan D., Callahan R.
    J. Virol. 66:2594-2599(1992) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
  2. "The mouse mammary tumor associated gene INT3 is a unique member of the NOTCH gene family (NOTCH4)."
    Gallahan D., Callahan R.
    Oncogene 14:1883-1890(1997) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA], SEQUENCE REVISION.
  3. "Notch4/int-3, a mammary proto-oncogene, is an endothelial cell-specific mammalian Notch gene."
    Uyttendaele H., Marazzi G., Wu G., Yan Q., Sassoon D., Kitajewski J.
    Development 122:2251-2259(1996) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA], INVOLVEMENT IN MAMMARY CARCINOMA.
    Tissue: Lung and Testis.
  4. "Analysis of the gene-dense major histocompatibility complex class III region and its comparison to mouse."
    Xie T., Rowen L., Aguado B., Ahearn M.E., Madan A., Qin S., Campbell R.D., Hood L.
    Genome Res. 13:2621-2636(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: 129.
  5. "Intracisternal type A particle-mediated activation of the Notch4/int3 gene in a mouse mammary tumor: generation of truncated Notch4/int3 mRNAs by retroviral splicing events."
    Lee J.-S., Haruna T., Ishimoto A., Honjo T., Yanagawa S.
    J. Virol. 73:5166-5171(1999) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA] OF 1436-1600.
  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: PROTEIN SEQUENCE OF 1463-1964, PROTEOLYTIC PROCESSING, MUTAGENESIS OF VAL-1463.
  7. "Vascular patterning defects associated with expression of activated Notch4 in embryonic endothelium."
    Uyttendaele H., Ho J., Rossant J., Kitajewski J.
    Proc. Natl. Acad. Sci. U.S.A. 98:5643-5648(2001) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION.
  8. "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.
  9. "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.
  10. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Lung.

Entry informationi

Entry nameiNOTC4_MOUSE
AccessioniPrimary (citable) accession number: P31695
Secondary accession number(s): O35442
, O88314, O88316, Q62389, Q62390, Q9R1W9, Q9R1X0
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 1, 1993
Last sequence update: November 1, 1997
Last modified: June 8, 2016
This is version 166 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Direct protein sequencing, 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.