P31695 (NOTC4_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Neurogenic locus notch homolog protein 4
Short name=Notch 4

Cleaved into the following 3 chains:

1. Transforming protein Int-3
2. Notch 4 extracellular truncation
3. Notch 4 intracellular domain

Gene names

Name:	Notch4
Synonyms:	Int-3, Int3

Organism

Mus musculus (Mouse) [Reference proteome]

Taxonomic identifier

10090 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Opisthokonta › Metazoa › Eumetazoa › Bilateria › Deuterostomia › Chordata › Craniata › Vertebrata › Gnathostomata › Teleostomi › Euteleostomi › Sarcopterygii › Tetrapoda › Amniota › Mammalia › Theria › Eutheria › Euarchontoglires › Glires › Rodentia › Sciurognathi › Muroidea › Muridae › Murinae › Mus › Mus

Protein attributes

Sequence length	1964 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Evidence 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 regulate branching morphogenesis in the developing vascular system. Ref.7
Subunit structure	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. Ref.9
Subcellular location	Cell membrane; Single-pass type I membrane protein. Notch 4 intracellular domain: Nucleus. Note: Following proteolytical processing NICD is translocated to the nucleus.
Tissue specificity	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 stage	Highly expressed in endothelial cells during embryonic development from 9.0 dpc.
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.8 Phosphorylated.
Involvement in disease	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.
Sequence similarities	Belongs to the NOTCH family. Contains 5 ANK repeats. Contains 29 EGF-like domains. Contains 3 LNR (Lin/Notch) repeats.
Sequence caution	The sequence BAA32281.1 differs from that shown. Reason: The sequence BAA32283.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally shortened. The sequence BAA32284.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally extended.

Ontologies

Keywords
Biological process	Differentiation Notch signaling pathway Transcription Transcription regulation
Cellular component	Cell membrane Membrane Nucleus
Disease	Proto-oncogene
Domain	ANK repeat EGF-like domain Repeat Signal Transmembrane Transmembrane helix
Molecular function	Activator Developmental protein Receptor
PTM	Disulfide bond Glycoprotein Phosphoprotein
Technical term	Complete proteome Direct protein sequencing Reference proteome
Gene Ontology (GO)
Biological_process	Notch signaling pathway Traceable author statement Ref.7. Source: UniProtKB cell differentiation Inferred from electronic annotation. Source: UniProtKB-KW embryo development Inferred from mutant phenotype Ref.7. Source: UniProtKB negative regulation of endothelial cell differentiation Inferred from mutant phenotype Ref.7. Source: UniProtKB patterning of blood vessels Inferred from mutant phenotype Ref.7. Source: UniProtKB regulation of transcription, DNA-dependent Inferred from electronic annotation. Source: UniProtKB-KW transcription, DNA-dependent Inferred from electronic annotation. Source: UniProtKB-KW
Cellular_component	cell surface Inferred from sequence or structural similarity. Source: UniProtKB integral to membrane Inferred from electronic annotation. Source: UniProtKB-KW nucleus Inferred from electronic annotation. Source: UniProtKB-SubCell plasma membrane Inferred from electronic annotation. Source: UniProtKB-SubCell
Molecular_function	calcium ion binding Inferred from electronic annotation. Source: InterPro
Complete GO annotation...

Binary interactions

With	Entry	#Exp.	IntAct	Notes
sel-10	Q93794	2	EBI-643670,EBI-323098	From a different organism.

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Signal peptide	1 – 20	20	Potential
	Chain	21 – 1964	1944	Neurogenic locus notch homolog protein 4		PRO_0000007704
	Chain	1411 – 1964	554	Transforming protein Int-3		PRO_0000007705
	Chain	1428 – 1964	537	Notch 4 extracellular truncation		PRO_0000007706
	Chain	1463 – 1964	502	Notch 4 intracellular domain		PRO_0000007707
Regions
	Topological domain	21 – 1443	1423	Extracellular Potential
	Transmembrane	1444 – 1464	21	Helical; Potential
	Topological domain	1465 – 1964	500	Cytoplasmic Potential
	Domain	21 – 60	40	EGF-like 1
	Domain	61 – 112	52	EGF-like 2
	Domain	115 – 152	38	EGF-like 3
	Domain	153 – 189	37	EGF-like 4
	Domain	191 – 229	39	EGF-like 5; calcium-binding Potential
	Domain	231 – 271	41	EGF-like 6
	Domain	273 – 309	37	EGF-like 7; calcium-binding Potential
	Domain	311 – 350	40	EGF-like 8; calcium-binding Potential
	Domain	352 – 388	37	EGF-like 9; calcium-binding Potential
	Domain	389 – 427	39	EGF-like 10
	Domain	429 – 470	42	EGF-like 11; calcium-binding Potential
	Domain	472 – 508	37	EGF-like 12; calcium-binding Potential
	Domain	510 – 546	37	EGF-like 13; calcium-binding Potential
	Domain	548 – 584	37	EGF-like 14; calcium-binding Potential
	Domain	586 – 622	37	EGF-like 15; calcium-binding Potential
	Domain	623 – 656	34	EGF-like 16
	Domain	658 – 686	29	EGF-like 17
	Domain	688 – 724	37	EGF-like 18
	Domain	726 – 762	37	EGF-like 19
	Domain	764 – 800	37	EGF-like 20
	Domain	803 – 839	37	EGF-like 21
	Domain	841 – 877	37	EGF-like 22
	Domain	878 – 924	47	EGF-like 23
	Domain	926 – 962	37	EGF-like 24
	Domain	964 – 1000	37	EGF-like 25
	Domain	1002 – 1040	39	EGF-like 26
	Domain	1042 – 1081	40	EGF-like 27
	Domain	1083 – 1122	40	EGF-like 28
	Domain	1126 – 1167	42	EGF-like 29
	Repeat	1166 – 1209	44	LNR 1
	Repeat	1210 – 1241	32	LNR 2
	Repeat	1247 – 1287	41	LNR 3
	Repeat	1628 – 1657	30	ANK 1
	Repeat	1661 – 1691	31	ANK 2
	Repeat	1695 – 1724	30	ANK 3
	Repeat	1728 – 1757	30	ANK 4
	Repeat	1761 – 1790	30	ANK 5
Amino acid modifications
	Glycosylation	711	1	N-linked (GlcNAc...) Potential
	Glycosylation	960	1	N-linked (GlcNAc...) Potential
	Glycosylation	1139	1	N-linked (GlcNAc...) Potential
	Disulfide bond	25 ↔ 38		By similarity
	Disulfide bond	32 ↔ 48		By similarity
	Disulfide bond	50 ↔ 59		By similarity
	Disulfide bond	65 ↔ 77		By similarity
	Disulfide bond	71 ↔ 100		By similarity
	Disulfide bond	102 ↔ 111		By similarity
	Disulfide bond	119 ↔ 130		By similarity
	Disulfide bond	124 ↔ 140		By similarity
	Disulfide bond	142 ↔ 151		By similarity
	Disulfide bond	157 ↔ 168		By similarity
	Disulfide bond	162 ↔ 177		By similarity
	Disulfide bond	179 ↔ 188		By similarity
	Disulfide bond	195 ↔ 208		By similarity
	Disulfide bond	202 ↔ 217		By similarity
	Disulfide bond	219 ↔ 228		By similarity
	Disulfide bond	235 ↔ 246		By similarity
	Disulfide bond	240 ↔ 259		By similarity
	Disulfide bond	261 ↔ 270		By similarity
	Disulfide bond	277 ↔ 288		By similarity
	Disulfide bond	282 ↔ 297		By similarity
	Disulfide bond	299 ↔ 308		By similarity
	Disulfide bond	315 ↔ 329		By similarity
	Disulfide bond	323 ↔ 338		By similarity
	Disulfide bond	340 ↔ 349		By similarity
	Disulfide bond	356 ↔ 367		By similarity
	Disulfide bond	361 ↔ 376		By similarity
	Disulfide bond	378 ↔ 387		By similarity
	Disulfide bond	393 ↔ 404		By similarity
	Disulfide bond	398 ↔ 415		By similarity
	Disulfide bond	417 ↔ 426		By similarity
	Disulfide bond	433 ↔ 449		By similarity
	Disulfide bond	443 ↔ 458		By similarity
	Disulfide bond	460 ↔ 469		By similarity
	Disulfide bond	476 ↔ 487		By similarity
	Disulfide bond	481 ↔ 496		By similarity
	Disulfide bond	498 ↔ 507		By similarity
	Disulfide bond	514 ↔ 525		By similarity
	Disulfide bond	519 ↔ 534		By similarity
	Disulfide bond	536 ↔ 545		By similarity
	Disulfide bond	552 ↔ 563		By similarity
	Disulfide bond	557 ↔ 572		By similarity
	Disulfide bond	574 ↔ 583		By similarity
	Disulfide bond	590 ↔ 601		By similarity
	Disulfide bond	595 ↔ 610		By similarity
	Disulfide bond	612 ↔ 621		By similarity
	Disulfide bond	626 ↔ 637		By similarity
	Disulfide bond	631 ↔ 646		By similarity
	Disulfide bond	648 ↔ 655		By similarity
	Disulfide bond	662 ↔ 669		By similarity
	Disulfide bond	664 ↔ 674		By similarity
	Disulfide bond	676 ↔ 685		By similarity
	Disulfide bond	692 ↔ 703		By similarity
	Disulfide bond	697 ↔ 712		By similarity
	Disulfide bond	714 ↔ 723		By similarity
	Disulfide bond	730 ↔ 741		By similarity
	Disulfide bond	735 ↔ 750		By similarity
	Disulfide bond	752 ↔ 761		By similarity
	Disulfide bond	768 ↔ 779		By similarity
	Disulfide bond	773 ↔ 788		By similarity
	Disulfide bond	790 ↔ 799		By similarity
	Disulfide bond	807 ↔ 818		By similarity
	Disulfide bond	812 ↔ 827		By similarity
	Disulfide bond	829 ↔ 838		By similarity
	Disulfide bond	845 ↔ 856		By similarity
	Disulfide bond	850 ↔ 865		By similarity
	Disulfide bond	867 ↔ 876		By similarity
	Disulfide bond	882 ↔ 903		By similarity
	Disulfide bond	897 ↔ 912		By similarity
	Disulfide bond	914 ↔ 923		By similarity
	Disulfide bond	930 ↔ 941		By similarity
	Disulfide bond	935 ↔ 950		By similarity
	Disulfide bond	952 ↔ 961		By similarity
	Disulfide bond	968 ↔ 979		By similarity
	Disulfide bond	973 ↔ 988		By similarity
	Disulfide bond	990 ↔ 999		By similarity
	Disulfide bond	1006 ↔ 1019		By similarity
	Disulfide bond	1011 ↔ 1028		By similarity
	Disulfide bond	1030 ↔ 1039		By similarity
	Disulfide bond	1046 ↔ 1057		By similarity
	Disulfide bond	1051 ↔ 1069		By similarity
	Disulfide bond	1071 ↔ 1080		By similarity
	Disulfide bond	1087 ↔ 1098		By similarity
	Disulfide bond	1092 ↔ 1110		By similarity
	Disulfide bond	1112 ↔ 1121		By similarity
	Disulfide bond	1130 ↔ 1142		By similarity
	Disulfide bond	1136 ↔ 1155		By similarity
	Disulfide bond	1157 ↔ 1166		By similarity
	Disulfide bond	1174 ↔ 1187		By similarity
	Disulfide bond	1183 ↔ 1199		By similarity
	Disulfide bond	1210 ↔ 1234		By similarity
	Disulfide bond	1216 ↔ 1229		By similarity
	Disulfide bond	1225 ↔ 1241		By similarity
	Disulfide bond	1247 ↔ 1273		By similarity
	Disulfide bond	1255 ↔ 1268		By similarity
	Disulfide bond	1264 ↔ 1280		By similarity
Experimental info
	Mutagenesis	1463	1	V → L: NICD processing severely reduced. Ref.6
	Sequence conflict	43	1	Q → R in AAC52630. Ref.3
	Sequence conflict	43	1	Q → R in AAB82004. Ref.4
	Sequence conflict	298	1	L → P in AAC52630. Ref.3
	Sequence conflict	884	1	M → K in AAC52630. Ref.3
	Sequence conflict	884	1	M → K in AAB82004. Ref.4
	Sequence conflict	927	1	M → V in AAC52630. Ref.3
	Sequence conflict	927	1	M → V in AAB82004. Ref.4
	Sequence conflict	966	1	E → D in AAC52630. Ref.3
	Sequence conflict	966	1	E → D in AAB82004. Ref.4
	Sequence conflict	1245	1	L → P in AAC52630. Ref.3
	Sequence conflict	1437	1	P → S in AAB82004. Ref.4
	Sequence conflict	1469	1	R → Q in BAA32283. Ref.5
	Sequence conflict	1469	1	R → Q in BAA32284. Ref.5
	Sequence conflict	1489	1	A → T in AAC52630. Ref.3
	Sequence conflict	1489	1	A → T in AAC52631. Ref.3
	Sequence conflict	1489	1	A → T in AAB82004. Ref.4
	Sequence conflict	1489	1	A → T in BAA32283. Ref.5
	Sequence conflict	1489	1	A → T in BAA32284. Ref.5
	Sequence conflict	1549	1	S → G in AAC52630. Ref.3
	Sequence conflict	1549	1	S → G in AAC52631. Ref.3
	Sequence conflict	1549	1	S → G in AAB82004. Ref.4
	Sequence conflict	1549	1	S → G in BAA32283. Ref.5
	Sequence conflict	1549	1	S → G in BAA32284. Ref.5
	Sequence conflict	1549	1	S → G in BAA32285. Ref.5
	Sequence conflict	1688	1	S → T in AAC52630. Ref.3
	Sequence conflict	1688	1	S → T in AAC52631. Ref.3
	Sequence conflict	1688	1	S → T in AAB82004. Ref.4
	Sequence conflict	1836	1	A → S in AAC52630. Ref.3
	Sequence conflict	1836	1	A → S in AAC52631. Ref.3
	Sequence conflict	1838	1	A → P in AAC52630. Ref.3
	Sequence conflict	1838	1	A → P in AAC52631. Ref.3
	Sequence conflict	1838	1	A → P in AAB82004. Ref.4

Sequences

	Sequence		Length	Mass (Da)
	P31695 [UniParc]. Last modified November 1, 1997. Version 2. Checksum: 213B65D11BF489BE	FASTA	1,964	206,693
	10 20 30 40 50 60 MQPQLLLLLL LPLNFPVILT RELLCGGSPE PCANGGTCLR LSQGQGICQC APGFLGETCQ 70 80 90 100 110 120 FPDPCRDTQL CKNGGSCQAL LPTPPSSRSP TSPLTPHFSC TCPSGFTGDR CQTHLEELCP 130 140 150 160 170 180 PSFCSNGGHC YVQASGRPQC SCEPGWTGEQ CQLRDFCSAN PCANGGVCLA TYPQIQCRCP 190 200 210 220 230 240 PGFEGHTCER DINECFLEPG PCPQGTSCHN TLGSYQCLCP VGQEGPQCKL RKGACPPGSC 250 260 270 280 290 300 LNGGTCQLVP EGHSTFHLCL CPPGFTGLDC EMNPDDCVRH QCQNGATCLD GLDTYTCLCP 310 320 330 340 350 360 KTWKGWDCSE DIDECEARGP PRCRNGGTCQ NTAGSFHCVC VSGWGGAGCE ENLDDCAAAT 370 380 390 400 410 420 CAPGSTCIDR VGSFSCLCPP GRTGLLCHLE DMCLSQPCHV NAQCSTNPLT GSTLCICQPG 430 440 450 460 470 480 YSGSTCHQDL DECQMAQQGP SPCEHGGSCI NTPGSFNCLC LPGYTGSRCE ADHNECLSQP 490 500 510 520 530 540 CHPGSTCLDL LATFHCLCPP GLEGRLCEVE VNECTSNPCL NQAACHDLLN GFQCLCLPGF 550 560 570 580 590 600 TGARCEKDMD ECSSTPCANG GRCRDQPGAF YCECLPGFEG PHCEKEVDEC LSDPCPVGAS 610 620 630 640 650 660 CLDLPGAFFC LCRPGFTGQL CEVPLCTPNM CQPGQQCQGQ EHRAPCLCPD GSPGCVPAED 670 680 690 700 710 720 NCPCHHGHCQ RSLCVCDEGW TGPECETELG GCISTPCAHG GTCHPQPSGY NCTCPAGYMG 730 740 750 760 770 780 LTCSEEVTAC HSGPCLNGGS CSIRPEGYSC TCLPSHTGRH CQTAVDHCVS ASCLNGGTCV 790 800 810 820 830 840 NKPGTFFCLC ATGFQGLHCE EKTNPSCADS PCRNKATCQD TPRGARCLCS PGYTGSSCQT 850 860 870 880 890 900 LIDLCARKPC PHTARCLQSG PSFQCLCLQG WTGALCDFPL SCQMAAMSQG IEISGLCQNG 910 920 930 940 950 960 GLCIDTGSSY FCRCPPGFQG KLCQDNMNPC EPNPCHHGST CVPQPSGYVC QCAPGYEGQN 970 980 990 1000 1010 1020 CSKVLEACQS QPCHNHGTCT SRPGGFHCAC PPGFVGLRCE GDVDECLDRP CHPSGTAACH 1030 1040 1050 1060 1070 1080 SLANAFYCQC LPGHTGQRCE VEMDLCQSQP CSNGGSCEIT TGPPPGFTCH CPKGFEGPTC 1090 1100 1110 1120 1130 1140 SHKALSCGIH HCHNGGLCLP SPKPGSPPLC ACLSGFGGPD CLTPPAPPGC GPPSPCLHNG 1150 1160 1170 1180 1190 1200 TCTETPGLGN PGFQCTCPPD SPGPRCQRPG ASGCEGRGGD GTCDAGCSGP GGDWDGGDCS 1210 1220 1230 1240 1250 1260 LGVPDPWKGC PPHSQCWLLF RDGRCHPQCD SEECLFDGYD CEIPLTCIPA YDQYCRDHFH 1270 1280 1290 1300 1310 1320 NGHCEKGCNN AECGWDGGDC RPEGEDSEGR PSLALLVVLR PPALDQQLLA LARVLSLTLR 1330 1340 1350 1360 1370 1380 VGLWVRKDSE GRNMVFPYPG TRAKEELSGA RDSSSWERQA PPTQPLGKET ESLGAGFVVV 1390 1400 1410 1420 1430 1440 MGVDLSRCGP EHPASRCPWD SGLLLRFLAA MAAVGALEPL LPGPLLAAHP QAGTRPPANQ 1450 1460 1470 1480 1490 1500 LPWPILCSPV VGVLLLALGA LLVLQLIRRR RREHGALWLP PGFIRRPQAQ QAPHRRRPPL 1510 1520 1530 1540 1550 1560 GEDNIGLKAL KPEAEVDEDG VAMCSGPEEG EAEETASASR CQLWPLNSSC GELPQAAMLT 1570 1580 1590 1600 1610 1620 PPQECESEVL DVDTCGPDGV TPLMSAVFCG GVQSTTGASP QRLGLGNLEP WEPLLDRGAC 1630 1640 1650 1660 1670 1680 PQAHTVGTGE TPLHLAARFS RPTAARRLLE AGANPNQPDR AGRTPLHTAV AADAREVCQL 1690 1700 1710 1720 1730 1740 LLASRQTSVD ARTEDGTTPL MLAARLAVED LVEELIAARA DVGARDKRGK TALHWAAAVN 1750 1760 1770 1780 1790 1800 NARAARSLLQ AGADKDAQDS REQTPLFLAA REGAVEVAQL LLELGAARGL RDQAGLAPGD 1810 1820 1830 1840 1850 1860 VARQRSHWDL LTLLEGAGPT TQEARAHART TPGGGAAARC RTLSAGARPR GGGACLQART 1870 1880 1890 1900 1910 1920 WSVDLGARGG KVYARCRSRS GSCGGPTTRG RRFSAGSRGR RGARASQDDW PRDWVALEAC 1930 1940 1950 1960 GSACSAPIPP PSLTPSPERG SPQVAWGLPV HQEIPLNSVV RNLN

References

	« Hide 'large scale' referencesShow 'large scale' references »
[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]. 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.
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBL GenBank DDBJ	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.
IPI	IPI00136971.
PIR	TVMVT3. A38072. T09059.
RefSeq	NP_035059.2. NM_010929.2.
UniGene	Mm.173813.
3D structure databases
ProteinModelPortal	P31695.
SMR	P31695. Positions 32-654, 663-1169, 1183-1340, 1573-1849.
ModBase	Search...
Protein-protein interaction databases
IntAct	P31695. 2 interactions.
PTM databases
PhosphoSite	P31695.
Proteomic databases
PaxDb	P31695.
PRIDE	P31695.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
GeneID	18132.
KEGG	mmu:18132.
Organism-specific databases
CTD	4855.
MGI	MGI:107471. Notch4.
Phylogenomic databases
eggNOG	COG0666.
HOVERGEN	HBG052650.
InParanoid	P31695.
KO	K02599.
OrthoDB	EOG437RD0.
Enzyme and pathway databases
Reactome	REACT_115202. Signal Transduction.
Gene expression databases
CleanEx	MM_NOTCH4.
Genevestigator	P31695.
GermOnline	ENSMUSG00000015468. Mus musculus.
Family and domain databases
Gene3D	1.25.40.20. 1 hit.
InterPro	IPR002110. Ankyrin_rpt. IPR020683. Ankyrin_rpt-contain_dom. IPR000742. EG-like_dom. IPR001881. EGF-like_Ca-bd. IPR013032. EGF-like_CS. IPR000152. EGF-type_Asp/Asn_hydroxyl_site. IPR018097. EGF_Ca-bd_CS. IPR008297. Notch. IPR022355. Notch_4. IPR000800. Notch_dom. IPR011656. Notch_NODP_dom. [Graphical view]
Pfam	PF00023. Ank. 6 hits. PF00008. EGF. 11 hits. PF07645. EGF_CA. 3 hits. PF12661. hEGF. 4 hits. PF07684. NODP. 1 hit. PF00066. Notch. 3 hits. [Graphical view]
PIRSF	PIRSF002279. Notch. 1 hit.
PRINTS	PR01452. LNOTCHREPEAT. PR01987. NOTCH4.
SMART	SM00248. ANK. 6 hits. SM00181. EGF. 16 hits. SM00179. EGF_CA. 11 hits. SM00004. NL. 3 hits. [Graphical view]
SUPFAM	SSF48403. ANK. 1 hit. SSF90193. Notch_region. 2 hits.
PROSITE	PS50297. 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]
ProtoNet	Search...
Other
NextBio	293372.
SOURCE	Search...

Entry information

Entry name

NOTC4_MOUSE

Accession

Primary (citable) accession number: P31695
Secondary accession number(s): O35442 , O88314, O88316, Q62389, Q62390, Q9R1W9, Q9R1X0

Entry history

Integrated into UniProtKB/Swiss-Prot:	July 1, 1993
Last sequence update:	November 1, 1997
Last modified:	May 1, 2013
This is version 138 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program