| Tag | Content |
|---|
| CPLM ID | CPLM-014389 |
UniProt Accession | |
Genbank Protein ID | |
Genbank Nucleotide ID | |
Protein Name | Neurogenic locus notch homolog protein 3 |
Protein Synonyms/Alias | Notch 3; Notch 3 extracellular truncation; Notch 3 intracellular domain |
Gene Name | Notch3 |
Gene Synonyms/Alias | |
Created Date | July 27, 2013 |
Organism | Mus musculus (Mouse) |
NCBI Taxa ID | 10090 |
Lysine Modification | Position | Peptide | Type | References |
|---|
| 1692 | KDIAAGHKGRREPVG | acetylation | [1] | | 1731 | DSECPEAKRLKVEEP | acetylation | [1] |
|
Reference | [1] Acetylation controls Notch3 stability and function in T-cell leukemia. Palermo R, Checquolo S, Giovenco A, Grazioli P, Kumar V, Campese AF, Giorgi A, Napolitano M, Canettieri G, Ferrara G, Schininà ME, Maroder M, Frati L, Gulino A, Vacca A, Screpanti I. Oncogene. 2012 Aug 16;31(33):3807-17. [ PMID: 22120716] |
Functional Description | 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. |
Sequence Annotation | DOMAIN 40 78 EGF-like 1.
DOMAIN 79 119 EGF-like 2.
DOMAIN 120 157 EGF-like 3.
DOMAIN 159 196 EGF-like 4; calcium-binding (Potential).
DOMAIN 198 235 EGF-like 5.
DOMAIN 237 273 EGF-like 6; calcium-binding (Potential).
DOMAIN 275 313 EGF-like 7.
DOMAIN 315 351 EGF-like 8; calcium-binding (Potential).
DOMAIN 352 390 EGF-like 9.
DOMAIN 392 430 EGF-like 10; calcium-binding (Potential).
DOMAIN 432 468 EGF-like 11; calcium-binding (Potential).
DOMAIN 470 506 EGF-like 12; calcium-binding (Potential).
DOMAIN 508 544 EGF-like 13; calcium-binding (Potential).
DOMAIN 546 581 EGF-like 14; calcium-binding (Potential).
DOMAIN 583 619 EGF-like 15; calcium-binding (Potential).
DOMAIN 621 656 EGF-like 16; calcium-binding (Potential).
DOMAIN 658 694 EGF-like 17; calcium-binding (Potential).
DOMAIN 696 731 EGF-like 18.
DOMAIN 735 771 EGF-like 19.
DOMAIN 772 809 EGF-like 20.
DOMAIN 811 848 EGF-like 21; calcium-binding (Potential).
DOMAIN 850 886 EGF-like 22; calcium-binding (Potential).
DOMAIN 888 923 EGF-like 23; calcium-binding (Potential).
DOMAIN 925 961 EGF-like 24.
DOMAIN 963 999 EGF-like 25.
DOMAIN 1001 1035 EGF-like 26.
DOMAIN 1037 1083 EGF-like 27.
DOMAIN 1085 1121 EGF-like 28.
DOMAIN 1123 1159 EGF-like 29; calcium-binding (Potential).
DOMAIN 1161 1204 EGF-like 30; calcium-binding (Potential).
DOMAIN 1206 1245 EGF-like 31.
DOMAIN 1247 1288 EGF-like 32.
DOMAIN 1290 1326 EGF-like 33.
DOMAIN 1336 1374 EGF-like 34.
REPEAT 1388 1428 LNR 1.
REPEAT 1429 1466 LNR 2.
REPEAT 1468 1506 LNR 3.
REPEAT 1839 1868 ANK 1.
REPEAT 1872 1902 ANK 2.
REPEAT 1906 1935 ANK 3.
REPEAT 1939 1968 ANK 4.
REPEAT 1972 2001 ANK 5.
REGION 2242 2261 PEST-like.
CARBOHYD 1180 1180 N-linked (GlcNAc...) (Potential).
CARBOHYD 1337 1337 N-linked (GlcNAc...) (Potential).
CARBOHYD 1439 1439 N-linked (GlcNAc...) (Potential).
DISULFID 43 55 By similarity.
DISULFID 49 66 By similarity.
DISULFID 68 77 By similarity.
DISULFID 83 94 By similarity.
DISULFID 88 107 By similarity.
DISULFID 109 118 By similarity.
DISULFID 124 135 By similarity.
DISULFID 129 145 By similarity.
DISULFID 147 156 By similarity.
DISULFID 163 175 By similarity.
DISULFID 169 184 By similarity.
DISULFID 186 195 By similarity.
DISULFID 202 213 By similarity.
DISULFID 207 223 By similarity.
DISULFID 225 234 By similarity.
DISULFID 241 252 By similarity.
DISULFID 246 261 By similarity.
DISULFID 263 272 By similarity.
DISULFID 279 292 By similarity.
DISULFID 286 301 By similarity.
DISULFID 303 312 By similarity.
DISULFID 319 330 By similarity.
DISULFID 324 339 By similarity.
DISULFID 341 350 By similarity.
DISULFID 356 367 By similarity.
DISULFID 361 378 By similarity.
DISULFID 380 389 By similarity.
DISULFID 396 409 By similarity.
DISULFID 403 418 By similarity.
DISULFID 420 429 By similarity.
DISULFID 436 447 By similarity.
DISULFID 441 456 By similarity.
DISULFID 458 467 By similarity.
DISULFID 474 485 By similarity.
DISULFID 479 494 By similarity.
DISULFID 496 505 By similarity.
DISULFID 512 523 By similarity.
DISULFID 517 532 By similarity.
DISULFID 534 543 By similarity.
DISULFID 550 560 By similarity.
DISULFID 555 569 By similarity.
DISULFID 571 580 By similarity.
DISULFID 587 598 By similarity.
DISULFID 592 607 By similarity.
DISULFID 609 618 By similarity.
DISULFID 625 635 By similarity.
DISULFID 630 644 By similarity.
DISULFID 646 655 By similarity.
DISULFID 662 673 By similarity.
DISULFID 667 682 By similarity.
DISULFID 684 693 By similarity.
DISULFID 700 710 By similarity.
DISULFID 705 719 By similarity.
DISULFID 721 730 By similarity.
DISULFID 739 750 By similarity.
DISULFID 744 759 By similarity.
DISULFID 761 770 By similarity.
DISULFID 776 787 By similarity.
DISULFID 781 797 By similarity.
DISULFID 799 808 By similarity.
DISULFID 815 827 By similarity.
DISULFID 821 836 By similarity.
DISULFID 838 847 By similarity.
DISULFID 854 865 By similarity.
DISULFID 859 874 By similarity.
DISULFID 876 885 By similarity.
DISULFID 892 902 By similarity.
DISULFID 897 911 By similarity.
DISULFID 913 922 By similarity.
DISULFID 929 940 By similarity.
DISULFID 934 949 By similarity.
DISULFID 951 960 By similarity.
DISULFID 967 978 By similarity.
DISULFID 972 987 By similarity.
DISULFID 989 998 By similarity.
DISULFID 1005 1016 By similarity.
DISULFID 1010 1023 By similarity.
DISULFID 1025 1034 By similarity.
DISULFID 1041 1062 By similarity.
DISULFID 1056 1071 By similarity.
DISULFID 1073 1082 By similarity.
DISULFID 1089 1100 By similarity.
DISULFID 1094 1109 By similarity.
DISULFID 1111 1120 By similarity.
DISULFID 1127 1138 By similarity.
DISULFID 1132 1147 By similarity.
DISULFID 1149 1158 By similarity.
DISULFID 1165 1183 By similarity.
DISULFID 1177 1192 By similarity.
DISULFID 1194 1203 By similarity.
DISULFID 1210 1223 By similarity.
DISULFID 1215 1233 By similarity.
DISULFID 1235 1244 By similarity.
DISULFID 1251 1262 By similarity.
DISULFID 1256 1276 By similarity.
DISULFID 1278 1287 By similarity.
DISULFID 1294 1305 By similarity.
DISULFID 1299 1314 By similarity.
DISULFID 1316 1325 By similarity.
DISULFID 1340 1351 By similarity.
DISULFID 1345 1362 By similarity.
DISULFID 1364 1373 By similarity.
DISULFID 1388 1411 By similarity.
DISULFID 1393 1406 By similarity.
DISULFID 1402 1418 By similarity.
DISULFID 1429 1452 By similarity.
DISULFID 1434 1447 By similarity.
DISULFID 1443 1459 By similarity.
DISULFID 1468 1494 By similarity.
DISULFID 1476 1489 By similarity.
DISULFID 1485 1501 By similarity. |
Keyword | Activator; ANK repeat; Cell membrane; Complete proteome; Developmental protein; Differentiation; Disulfide bond; EGF-like domain; Glycoprotein; Membrane; Notch signaling pathway; Nucleus; Phosphoprotein; Receptor; Reference proteome; Repeat; Signal; Transcription; Transcription regulation; Transmembrane; Transmembrane helix. |
Sequence Source | UniProt (SWISSPROT/TrEMBL); GenBank; EMBL |
Protein Length | 2318 AA |
Protein Sequence | MGLGARGRRR RRRLMALPPP PPPMRALPLL LLLAGLGAAA PPCLDGSPCA NGGRCTHQQP 60
SLEAACLCLP GWVGERCQLE DPCHSGPCAG RGVCQSSVVA GTARFSCRCL RGFQGPDCSQ 120
PDPCVSRPCV HGAPCSVGPD GRFACACPPG YQGQSCQSDI DECRSGTTCR HGGTCLNTPG 180
SFRCQCPLGY TGLLCENPVV PCAPSPCRNG GTCRQSSDVT YDCACLPGFE GQNCEVNVDD 240
CPGHRCLNGG TCVDGVNTYN CQCPPEWTGQ FCTEDVDECQ LQPNACHNGG TCFNLLGGHS 300
CVCVNGWTGE SCSQNIDDCA TAVCFHGATC HDRVASFYCA CPMGKTGLLC HLDDACVSNP 360
CHEDAICDTN PVSGRAICTC PPGFTGGACD QDVDECSIGA NPCEHLGRCV NTQGSFLCQC 420
GRGYTGPRCE TDVNECLSGP CRNQATCLDR IGQFTCICMA GFTGTYCEVD IDECQSSPCV 480
NGGVCKDRVN GFSCTCPSGF SGSMCQLDVD ECASTPCRNG AKCVDQPDGY ECRCAEGFEG 540
TLCERNVDDC SPDPCHHGRC VDGIASFSCA CAPGYTGIRC ESQVDECRSQ PCRYGGKCLD 600
LVDKYLCRCP PGTTGVNCEV NIDDCASNPC TFGVCRDGIN RYDCVCQPGF TGPLCNVEIN 660
ECASSPCGEG GSCVDGENGF HCLCPPGSLP PLCLPANHPC AHKPCSHGVC HDAPGGFRCV 720
CEPGWSGPRC SQSLAPDACE SQPCQAGGTC TSDGIGFRCT CAPGFQGHQC EVLSPCTPSL 780
CEHGGHCESD PDRLTVCSCP PGWQGPRCQQ DVDECAGASP CGPHGTCTNL PGNFRCICHR 840
GYTGPFCDQD IDDCDPNPCL HGGSCQDGVG SFSCSCLDGF AGPRCARDVD ECLSSPCGPG 900
TCTDHVASFT CACPPGYGGF HCEIDLPDCS PSSCFNGGTC VDGVSSFSCL CRPGYTGTHC 960
QYEADPCFSR PCLHGGICNP THPGFECTCR EGFTGSQCQN PVDWCSQAPC QNGGRCVQTG 1020
AYCICPPGWS GRLCDIQSLP CTEAAAQMGV RLEQLCQEGG KCIDKGRSHY CVCPEGRTGS 1080
HCEHEVDPCT AQPCQHGGTC RGYMGGYVCE CPAGYAGDSC EDNIDECASQ PCQNGGSCID 1140
LVARYLCSCP PGTLGVLCEI NEDDCDLGPS LDSGVQCLHN GTCVDLVGGF RCNCPPGYTG 1200
LHCEADINEC RPGACHAAHT RDCLQDPGGH FRCVCHPGFT GPRCQIALSP CESQPCQHGG 1260
QCRHSLGRGG GLTFTCHCVP PFWGLRCERV ARSCRELQCP VGIPCQQTAR GPRCACPPGL 1320
SGPSCRVSRA SPSGATNASC ASAPCLHGGS CLPVQSVPFF RCVCAPGWGG PRCETPSAAP 1380
EVPEEPRCPR AACQAKRGDQ NCDRECNTPG CGWDGGDCSL NVDDPWRQCE ALQCWRLFNN 1440
SRCDPACSSP ACLYDNFDCY SGGRDRTCNP VYEKYCADHF ADGRCDQGCN TEECGWDGLD 1500
CASEVPALLA RGVLVLTVLL PPEELLRSSA DFLQRLSAIL RTSLRFRLDA RGQAMVFPYH 1560
RPSPGSESRV RRELGPEVIG SVVMLEIDNR LCLQSAENDH CFPDAQSAAD YLGALSAVER 1620
LDFPYPLRDV RGEPLEAPEQ SVPLLPLLVA GAVFLLIIFI LGVMVARRKR EHSTLWFPEG 1680
FALHKDIAAG HKGRREPVGQ DALGMKNMAK GESLMGEVVT DLNDSECPEA KRLKVEEPGM 1740
GAEEPEDCRQ WTQHHLVAAD IRVAPATALT PPQGDADADG VDVNVRGPDG FTPLMLASFC 1800
GGALEPMPAE EDEADDTSAS IISDLICQGA QLGARTDRTG ETALHLAARY ARADAAKRLL 1860
DAGADTNAQD HSGRTPLHTA VTADAQGVFQ ILIRNRSTDL DARMADGSTA LILAARLAVE 1920
GMVEELIASH ADVNAVDELG KSALHWAAAV NNVEATLALL KNGANKDMQD SKEETPLFLA 1980
AREGSYEAAK LLLDHLANRE ITDHLDRLPR DVAQERLHQD IVRLLDQPSG PRSPSGPHGL 2040
GPLLCPPGAF LPGLKAVQSG TKKSRRPPGK TGLGPQGTRG RGKKLTLACP GPLADSSVTL 2100
SPVDSLDSPR PFSGPPASPG GFPLEGPYAT TATAVSLAQL GASRAGPLGR QPPGGCVLSF 2160
GLLNPVAVPL DWARLPPPAP PGPSFLLPLA PGPQLLNPGA PVSPQERPPP YLAAPGHGEE 2220
YPAAGTRSSP TKARFLRVPS EHPYLTPSPE SPEHWASPSP PSLSDWSDST PSPATATNAT 2280
ASGALPAQPH PISVPSLPQS QTQLGPQPEV TPKRQVMA 2318 |
Gene Ontology | GO:0005887; C:integral to plasma membrane; IC:UniProtKB. GO:0005634; C:nucleus; IEA:UniProtKB-SubCell. GO:0005509; F:calcium ion binding; IEA:InterPro. GO:0030900; P:forebrain development; IGI:MGI. GO:0072104; P:glomerular capillary formation; IEP:UniProtKB. GO:0045665; P:negative regulation of neuron differentiation; IMP:MGI. GO:0048663; P:neuron fate commitment; IGI:MGI. GO:0007219; P:Notch signaling pathway; IDA:UniProtKB. GO:0048661; P:positive regulation of smooth muscle cell proliferation; IDA:UniProtKB. GO:0006355; P:regulation of transcription, DNA-dependent; IEA:UniProtKB-KW. GO:0006351; P:transcription, DNA-dependent; IEA:UniProtKB-KW. |
Interpro | |
Pfam | |
SMART | |
PROSITE | |
PRINTS | |