CPLM 1.0 - Compendium of Protein Lysine Modification
TagContent
CPLM ID CPLM-023206
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
 Homo sapiens (Human) 
NCBI Taxa ID
 9606 
Lysine Modification
Position
Peptide
Type
References
1684PEGFSLHKDVASGHKubiquitination[1]
1989EGSYEAAKLLLDHFAubiquitination[2]
Reference
 [1] A proteome-wide, quantitative survey of in vivo ubiquitylation sites reveals widespread regulatory roles.
 Wagner SA, Beli P, Weinert BT, Nielsen ML, Cox J, Mann M, Choudhary C.
 Mol Cell Proteomics. 2011 Oct;10(10):M111.013284. [PMID: 21890473]
 [2] Refined preparation and use of anti-diglycine remnant (K-ε-GG) antibody enables routine quantification of 10,000s of ubiquitination sites in single proteomics experiments.
 Udeshi ND, Svinkina T, Mertins P, Kuhn E, Mani DR, Qiao JW, Carr SA.
 Mol Cell Proteomics. 2013 Mar;12(3):825-31. [PMID: 23266961
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). 
Sequence Annotation
 DOMAIN 40 77 EGF-like 1.
 DOMAIN 78 118 EGF-like 2.
 DOMAIN 119 156 EGF-like 3.
 DOMAIN 158 195 EGF-like 4; calcium-binding (Potential).
 DOMAIN 197 234 EGF-like 5.
 DOMAIN 236 272 EGF-like 6; calcium-binding (Potential).
 DOMAIN 274 312 EGF-like 7.
 DOMAIN 314 350 EGF-like 8; calcium-binding (Potential).
 DOMAIN 351 389 EGF-like 9.
 DOMAIN 391 429 EGF-like 10; calcium-binding (Potential).
 DOMAIN 431 467 EGF-like 11; calcium-binding (Potential).
 DOMAIN 469 505 EGF-like 12; calcium-binding (Potential).
 DOMAIN 507 543 EGF-like 13; calcium-binding (Potential).
 DOMAIN 545 580 EGF-like 14; calcium-binding (Potential).
 DOMAIN 582 618 EGF-like 15; calcium-binding (Potential).
 DOMAIN 620 655 EGF-like 16; calcium-binding (Potential).
 DOMAIN 657 693 EGF-like 17; calcium-binding (Potential).
 DOMAIN 695 730 EGF-like 18.
 DOMAIN 734 770 EGF-like 19.
 DOMAIN 771 808 EGF-like 20.
 DOMAIN 810 847 EGF-like 21; calcium-binding (Potential).
 DOMAIN 849 885 EGF-like 22; calcium-binding (Potential).
 DOMAIN 887 922 EGF-like 23; calcium-binding (Potential).
 DOMAIN 924 960 EGF-like 24.
 DOMAIN 962 998 EGF-like 25.
 DOMAIN 1000 1034 EGF-like 26.
 DOMAIN 1047 1082 EGF-like 27.
 DOMAIN 1084 1120 EGF-like 28.
 DOMAIN 1122 1158 EGF-like 29; calcium-binding (Potential).
 DOMAIN 1160 1203 EGF-like 30; calcium-binding (Potential).
 DOMAIN 1205 1244 EGF-like 31.
 DOMAIN 1246 1287 EGF-like 32.
 DOMAIN 1289 1325 EGF-like 33.
 DOMAIN 1335 1373 EGF-like 34.
 REPEAT 1387 1427 LNR 1.
 REPEAT 1428 1458 LNR 2.
 REPEAT 1467 1505 LNR 3.
 REPEAT 1838 1867 ANK 1.
 REPEAT 1871 1901 ANK 2.
 REPEAT 1905 1934 ANK 3.
 REPEAT 1938 1967 ANK 4.
 REPEAT 1971 2000 ANK 5.
 CARBOHYD 1179 1179 N-linked (GlcNAc...) (Potential).
 CARBOHYD 1336 1336 N-linked (GlcNAc...) (Potential).
 CARBOHYD 1438 1438 N-linked (GlcNAc...) (Potential).
 DISULFID 43 55 By similarity.
 DISULFID 49 65 By similarity.
 DISULFID 67 76 By similarity.
 DISULFID 82 93 By similarity.
 DISULFID 87 106 By similarity.
 DISULFID 108 117 By similarity.
 DISULFID 123 134 By similarity.
 DISULFID 128 144 By similarity.
 DISULFID 146 155 By similarity.
 DISULFID 162 174 By similarity.
 DISULFID 168 183 By similarity.
 DISULFID 185 194 By similarity.
 DISULFID 201 212 By similarity.
 DISULFID 206 222 By similarity.
 DISULFID 224 233 By similarity.
 DISULFID 240 251 By similarity.
 DISULFID 245 260 By similarity.
 DISULFID 262 271 By similarity.
 DISULFID 278 291 By similarity.
 DISULFID 285 300 By similarity.
 DISULFID 302 311 By similarity.
 DISULFID 318 329 By similarity.
 DISULFID 323 338 By similarity.
 DISULFID 340 349 By similarity.
 DISULFID 355 366 By similarity.
 DISULFID 360 377 By similarity.
 DISULFID 379 388 By similarity.
 DISULFID 395 408 By similarity.
 DISULFID 402 417 By similarity.
 DISULFID 419 428 By similarity.
 DISULFID 435 446 By similarity.
 DISULFID 440 455 By similarity.
 DISULFID 457 466 By similarity.
 DISULFID 473 484 By similarity.
 DISULFID 478 493 By similarity.
 DISULFID 495 504 By similarity.
 DISULFID 511 522 By similarity.
 DISULFID 516 531 By similarity.
 DISULFID 533 542 By similarity.
 DISULFID 549 559 By similarity.
 DISULFID 554 568 By similarity.
 DISULFID 570 579 By similarity.
 DISULFID 586 597 By similarity.
 DISULFID 591 606 By similarity.
 DISULFID 608 617 By similarity.
 DISULFID 624 634 By similarity.
 DISULFID 629 643 By similarity.
 DISULFID 645 654 By similarity.
 DISULFID 661 672 By similarity.
 DISULFID 666 681 By similarity.
 DISULFID 683 692 By similarity.
 DISULFID 699 709 By similarity.
 DISULFID 704 718 By similarity.
 DISULFID 720 729 By similarity.
 DISULFID 738 749 By similarity.
 DISULFID 743 758 By similarity.
 DISULFID 760 769 By similarity.
 DISULFID 775 786 By similarity.
 DISULFID 780 796 By similarity.
 DISULFID 798 807 By similarity.
 DISULFID 814 826 By similarity.
 DISULFID 820 835 By similarity.
 DISULFID 837 846 By similarity.
 DISULFID 853 864 By similarity.
 DISULFID 858 873 By similarity.
 DISULFID 875 884 By similarity.
 DISULFID 891 901 By similarity.
 DISULFID 896 910 By similarity.
 DISULFID 912 921 By similarity.
 DISULFID 928 939 By similarity.
 DISULFID 933 948 By similarity.
 DISULFID 950 959 By similarity.
 DISULFID 966 977 By similarity.
 DISULFID 971 986 By similarity.
 DISULFID 988 997 By similarity.
 DISULFID 1004 1015 By similarity.
 DISULFID 1009 1022 By similarity.
 DISULFID 1024 1033 By similarity.
 DISULFID 1040 1061 By similarity.
 DISULFID 1055 1070 By similarity.
 DISULFID 1072 1081 By similarity.
 DISULFID 1088 1099 By similarity.
 DISULFID 1093 1108 By similarity.
 DISULFID 1110 1119 By similarity.
 DISULFID 1126 1137 By similarity.
 DISULFID 1131 1146 By similarity.
 DISULFID 1148 1157 By similarity.
 DISULFID 1164 1182 By similarity.
 DISULFID 1176 1191 By similarity.
 DISULFID 1193 1202 By similarity.
 DISULFID 1209 1222 By similarity.
 DISULFID 1214 1232 By similarity.
 DISULFID 1234 1243 By similarity.
 DISULFID 1250 1261 By similarity.
 DISULFID 1255 1275 By similarity.
 DISULFID 1277 1286 By similarity.
 DISULFID 1293 1304 By similarity.
 DISULFID 1298 1313 By similarity.
 DISULFID 1315 1324 By similarity.
 DISULFID 1339 1350 By similarity.
 DISULFID 1344 1361 By similarity.
 DISULFID 1363 1372 By similarity.
 DISULFID 1387 1410 By similarity.
 DISULFID 1392 1405 By similarity.
 DISULFID 1401 1417 By similarity.
 DISULFID 1428 1451 By similarity.
 DISULFID 1433 1446 By similarity.
 DISULFID 1442 1458 By similarity.
 DISULFID 1467 1493 By similarity.
 DISULFID 1475 1488 By similarity.
 DISULFID 1484 1500 By similarity.  
Keyword
 Activator; ANK repeat; Cell membrane; Complete proteome; Developmental protein; Differentiation; Disease mutation; Disulfide bond; EGF-like domain; Glycoprotein; Membrane; Notch signaling pathway; Nucleus; Phosphoprotein; Polymorphism; Receptor; Reference proteome; Repeat; Signal; Transcription; Transcription regulation; Transmembrane; Transmembrane helix. 
Sequence Source
 UniProt (SWISSPROT/TrEMBL); GenBank; EMBL 
Protein Length
 2321 AA 
Protein Sequence
MGPGARGRRR RRRPMSPPPP PPPVRALPLL LLLAGPGAAA PPCLDGSPCA NGGRCTQLPS 60
REAACLCPPG WVGERCQLED PCHSGPCAGR GVCQSSVVAG TARFSCRCPR GFRGPDCSLP 120
DPCLSSPCAH GARCSVGPDG RFLCSCPPGY QGRSCRSDVD ECRVGEPCRH GGTCLNTPGS 180
FRCQCPAGYT GPLCENPAVP CAPSPCRNGG TCRQSGDLTY DCACLPGFEG QNCEVNVDDC 240
PGHRCLNGGT CVDGVNTYNC QCPPEWTGQF CTEDVDECQL QPNACHNGGT CFNTLGGHSC 300
VCVNGWTGES CSQNIDDCAT AVCFHGATCH DRVASFYCAC PMGKTGLLCH LDDACVSNPC 360
HEDAICDTNP VNGRAICTCP PGFTGGACDQ DVDECSIGAN PCEHLGRCVN TQGSFLCQCG 420
RGYTGPRCET DVNECLSGPC RNQATCLDRI GQFTCICMAG FTGTYCEVDI DECQSSPCVN 480
GGVCKDRVNG FSCTCPSGFS GSTCQLDVDE CASTPCRNGA KCVDQPDGYE CRCAEGFEGT 540
LCDRNVDDCS PDPCHHGRCV DGIASFSCAC APGYTGTRCE SQVDECRSQP CRHGGKCLDL 600
VDKYLCRCPS GTTGVNCEVN IDDCASNPCT FGVCRDGINR YDCVCQPGFT GPLCNVEINE 660
CASSPCGEGG SCVDGENGFR CLCPPGSLPP LCLPPSHPCA HEPCSHGICY DAPGGFRCVC 720
EPGWSGPRCS QSLARDACES QPCRAGGTCS SDGMGFHCTC PPGVQGRQCE LLSPCTPNPC 780
EHGGRCESAP GQLPVCSCPQ GWQGPRCQQD VDECAGPAPC GPHGICTNLA GSFSCTCHGG 840
YTGPSCDQDI NDCDPNPCLN GGSCQDGVGS FSCSCLPGFA GPRCARDVDE CLSNPCGPGT 900
CTDHVASFTC TCPPGYGGFH CEQDLPDCSP SSCFNGGTCV DGVNSFSCLC RPGYTGAHCQ 960
HEADPCLSRP CLHGGVCSAA HPGFRCTCLE SFTGPQCQTL VDWCSRQPCQ NGGRCVQTGA 1020
YCLCPPGWSG RLCDIRSLPC REAAAQIGVR LEQLCQAGGQ CVDEDSSHYC VCPEGRTGSH 1080
CEQEVDPCLA QPCQHGGTCR GYMGGYMCEC LPGYNGDNCE DDVDECASQP CQHGGSCIDL 1140
VARYLCSCPP GTLGVLCEIN EDDCGPGPPL DSGPRCLHNG TCVDLVGGFR CTCPPGYTGL 1200
RCEADINECR SGACHAAHTR DCLQDPGGGF RCLCHAGFSG PRCQTVLSPC ESQPCQHGGQ 1260
CRPSPGPGGG LTFTCHCAQP FWGPRCERVA RSCRELQCPV GVPCQQTPRG PRCACPPGLS 1320
GPSCRSFPGS PPGASNASCA AAPCLHGGSC RPAPLAPFFR CACAQGWTGP RCEAPAAAPE 1380
VSEEPRCPRA ACQAKRGDQR CDRECNSPGC GWDGGDCSLS VGDPWRQCEA LQCWRLFNNS 1440
RCDPACSSPA CLYDNFDCHA GGRERTCNPV YEKYCADHFA DGRCDQGCNT EECGWDGLDC 1500
ASEVPALLAR GVLVLTVLLP PEELLRSSAD FLQRLSAILR TSLRFRLDAH GQAMVFPYHR 1560
PSPGSEPRAR RELAPEVIGS VVMLEIDNRL CLQSPENDHC FPDAQSAADY LGALSAVERL 1620
DFPYPLRDVR GEPLEPPEPS VPLLPLLVAG AVLLLVILVL GVMVARRKRE HSTLWFPEGF 1680
SLHKDVASGH KGRREPVGQD ALGMKNMAKG ESLMGEVATD WMDTECPEAK RLKVEEPGMG 1740
AEEAVDCRQW TQHHLVAADI RVAPAMALTP PQGDADADGM DVNVRGPDGF TPLMLASFCG 1800
GALEPMPTEE DEADDTSASI ISDLICQGAQ LGARTDRTGE TALHLAARYA RADAAKRLLD 1860
AGADTNAQDH SGRTPLHTAV TADAQGVFQI LIRNRSTDLD ARMADGSTAL ILAARLAVEG 1920
MVEELIASHA DVNAVDELGK SALHWAAAVN NVEATLALLK NGANKDMQDS KEETPLFLAA 1980
REGSYEAAKL LLDHFANREI TDHLDRLPRD VAQERLHQDI VRLLDQPSGP RSPPGPHGLG 2040
PLLCPPGAFL PGLKAAQSGS KKSRRPPGKA GLGPQGPRGR GKKLTLACPG PLADSSVTLS 2100
PVDSLDSPRP FGGPPASPGG FPLEGPYAAA TATAVSLAQL GGPGRAGLGR QPPGGCVLSL 2160
GLLNPVAVPL DWARLPPPAP PGPSFLLPLA PGPQLLNPGT PVSPQERPPP YLAVPGHGEE 2220
YPAAGAHSSP PKARFLRVPS EHPYLTPSPE SPEHWASPSP PSLSDWSEST PSPATATGAM 2280
ATTTGALPAQ PLPLSVPSSL AQAQTQLGPQ PEVTPKRQVL A 2321 
Gene Ontology
 GO:0005829; C:cytosol; TAS:Reactome.
 GO:0005789; C:endoplasmic reticulum membrane; TAS:Reactome.
 GO:0005576; C:extracellular region; TAS:Reactome.
 GO:0000139; C:Golgi membrane; TAS:Reactome.
 GO:0016021; C:integral to membrane; IEA:UniProtKB-KW.
 GO:0005654; C:nucleoplasm; TAS:Reactome.
 GO:0005886; C:plasma membrane; TAS:Reactome.
 GO:0005509; F:calcium ion binding; IEA:InterPro.
 GO:0030900; P:forebrain development; IEA:Compara.
 GO:0072104; P:glomerular capillary formation; IEA:Compara.
 GO:0045665; P:negative regulation of neuron differentiation; IEA:Compara.
 GO:0048663; P:neuron fate commitment; IEA:Compara.
 GO:0007220; P:Notch receptor processing; TAS:Reactome.
 GO:0007219; P:Notch signaling pathway; TAS:Reactome.
 GO:0048661; P:positive regulation of smooth muscle cell proliferation; IEA:Compara.
 GO:0006355; P:regulation of transcription, DNA-dependent; IEA:UniProtKB-KW.
 GO:0006367; P:transcription initiation from RNA polymerase II promoter; TAS:Reactome. 
Interpro
 IPR002110; Ankyrin_rpt.
 IPR020683; Ankyrin_rpt-contain_dom.
 IPR024600; DUF3454_notch.
 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.
 IPR022331; Notch_3.
 IPR000800; Notch_dom.
 IPR010660; Notch_NOD_dom.
 IPR011656; Notch_NODP_dom. 
Pfam
 PF12796; Ank_2
 PF11936; DUF3454
 PF00008; EGF
 PF07645; EGF_CA
 PF12661; hEGF
 PF06816; NOD
 PF07684; NODP
 PF00066; Notch 
SMART
 SM00248; ANK
 SM00181; EGF
 SM00179; EGF_CA
 SM00004; NL 
PROSITE
 PS50297; ANK_REP_REGION
 PS50088; ANK_REPEAT
 PS00010; ASX_HYDROXYL
 PS00022; EGF_1
 PS01186; EGF_2
 PS50026; EGF_3
 PS01187; EGF_CA
 PS50258; LNR 
PRINTS
 PR01452; LNOTCHREPEAT.
 PR01986; NOTCH3.