CPLM 1.0 - Compendium of Protein Lysine Modification
TagContent
CPLM ID CPLM-011474
UniProt Accession
Genbank Protein ID
 X57405 
Genbank Nucleotide ID
Protein Name
 Neurogenic locus notch homolog protein 1 
Protein Synonyms/Alias
 Notch 1; Notch 1 extracellular truncation; Notch 1 intracellular domain; NICD 
Gene Name
 Notch1 
Gene Synonyms/Alias
  
Created Date
 July 27, 2013 
Organism
 Rattus norvegicus (Rat) 
NCBI Taxa ID
 10116 
Lysine Modification
Position
Peptide
Type
References
1764LWFPEGFKVSEASKKacetylation[1]
1770FKVSEASKKKRREPLacetylation[1]
1771KVSEASKKKRREPLGacetylation[1]
1772VSEASKKKRREPLGEacetylation[1]
1785GEDSVGLKPLKNASDacetylation[1]
1935YSRSDAAKRLLEASAacetylation[1]
2050NKDMQNNKEETPLFLacetylation[1]
2068EGSYETAKVLLDHFAacetylation[1]
2146LKSATQGKKARKPSTacetylation[1]
2147KSATQGKKARKPSTKacetylation[1]
2150TQGKKARKPSTKGLAacetylation[1]
2154KARKPSTKGLACSSKacetylation[1]
2161KGLACSSKEAKDLKAacetylation[1]
2164ACSSKEAKDLKARRKacetylation[1]
Reference
 [1] Acetylation-dependent regulation of endothelial Notch signalling by the SIRT1 deacetylase.
 Guarani V, Deflorian G, Franco CA, Krüger M, Phng LK, Bentley K, Toussaint L, Dequiedt F, Mostoslavsky R, Schmidt MH, Zimmermann B, Brandes RP, Mione M, Westphal CH, Braun T, Zeiher AM, Gerhardt H, Dimmeler S, Potente M.
 Nature. 2011 May 12;473(7346):234-8. [PMID: 21499261] 
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. May be important for follicular differentiation and possibly cell fate selection within the follicle. During cerebellar development, may function as a receptor for neuronal DNER and may be involved in the differentiation of Bergmann glia. Represses neuronal and myogenic differentiation. May enhance HIF1A function by sequestering HIF1AN away from HIF1A. Involved in angiogenesis; negatively regulates endothelial cell proliferation and migration and angiogenic sprouting (By similarity). Acts instructively to control the cell fate determination of CNS multipotent progenitor cells, resulting in astroglial induction and neuron/oligodendrocyte suppression. 
Sequence Annotation
 DOMAIN 20 58 EGF-like 1.
 DOMAIN 59 99 EGF-like 2.
 DOMAIN 102 139 EGF-like 3.
 DOMAIN 140 176 EGF-like 4.
 DOMAIN 178 216 EGF-like 5; calcium-binding (Potential).
 DOMAIN 218 255 EGF-like 6.
 DOMAIN 257 293 EGF-like 7; calcium-binding (Potential).
 DOMAIN 295 333 EGF-like 8; calcium-binding (Potential).
 DOMAIN 335 371 EGF-like 9; calcium-binding (Potential).
 DOMAIN 372 410 EGF-like 10.
 DOMAIN 412 450 EGF-like 11; calcium-binding (Potential).
 DOMAIN 452 488 EGF-like 12; calcium-binding (Potential).
 DOMAIN 490 526 EGF-like 13; calcium-binding (Potential).
 DOMAIN 528 564 EGF-like 14; calcium-binding (Potential).
 DOMAIN 566 601 EGF-like 15; calcium-binding (Potential).
 DOMAIN 603 639 EGF-like 16; calcium-binding (Potential).
 DOMAIN 641 676 EGF-like 17; calcium-binding (Potential).
 DOMAIN 678 714 EGF-like 18; calcium-binding (Potential).
 DOMAIN 716 751 EGF-like 19; calcium-binding (Potential).
 DOMAIN 753 789 EGF-like 20; calcium-binding (Potential).
 DOMAIN 791 827 EGF-like 21; calcium-binding (Potential).
 DOMAIN 829 867 EGF-like 22.
 DOMAIN 869 905 EGF-like 23; calcium-binding (Potential).
 DOMAIN 907 943 EGF-like 24.
 DOMAIN 945 981 EGF-like 25; calcium-binding (Potential).
 DOMAIN 983 1019 EGF-like 26.
 DOMAIN 1021 1057 EGF-like 27; calcium-binding (Potential).
 DOMAIN 1059 1095 EGF-like 28.
 DOMAIN 1097 1143 EGF-like 29.
 DOMAIN 1145 1181 EGF-like 30; calcium-binding (Potential).
 DOMAIN 1183 1219 EGF-like 31; calcium-binding (Potential).
 DOMAIN 1221 1265 EGF-like 32; calcium-binding (Potential).
 DOMAIN 1267 1305 EGF-like 33.
 DOMAIN 1307 1346 EGF-like 34.
 DOMAIN 1348 1384 EGF-like 35.
 DOMAIN 1387 1426 EGF-like 36.
 REPEAT 1449 1489 LNR 1.
 REPEAT 1490 1531 LNR 2.
 REPEAT 1532 1571 LNR 3.
 REPEAT 1917 1946 ANK 1.
 REPEAT 1950 1980 ANK 2.
 REPEAT 1984 2013 ANK 3.
 REPEAT 2017 2046 ANK 4.
 REPEAT 2050 2079 ANK 5.
 REGION 1937 1945 HIF1AN-binding (By similarity).
 REGION 2004 2012 HIF1AN-binding (By similarity).
 METAL 1457 1457 Calcium; via carbonyl oxygen (By
 METAL 1460 1460 Calcium (By similarity).
 METAL 1475 1475 Calcium (By similarity).
 METAL 1478 1478 Calcium (By similarity).
 MOD_RES 1945 1945 (3S)-3-hydroxyasparagine; by HIF1AN (By
 MOD_RES 2012 2012 (3S)-3-hydroxyasparagine; by HIF1AN (By
 CARBOHYD 41 41 N-linked (GlcNAc...) (Potential).
 CARBOHYD 888 888 N-linked (GlcNAc...) (Potential).
 CARBOHYD 959 959 N-linked (GlcNAc...) (Potential).
 CARBOHYD 1179 1179 N-linked (GlcNAc...) (Potential).
 CARBOHYD 1241 1241 N-linked (GlcNAc...) (Potential).
 CARBOHYD 1489 1489 N-linked (GlcNAc...) (Potential).
 CARBOHYD 1587 1587 N-linked (GlcNAc...) (Potential).
 DISULFID 24 37 By similarity.
 DISULFID 31 46 By similarity.
 DISULFID 48 57 By similarity.
 DISULFID 63 74 By similarity.
 DISULFID 68 87 By similarity.
 DISULFID 89 98 By similarity.
 DISULFID 106 117 By similarity.
 DISULFID 111 127 By similarity.
 DISULFID 129 138 By similarity.
 DISULFID 144 155 By similarity.
 DISULFID 149 164 By similarity.
 DISULFID 166 175 By similarity.
 DISULFID 182 195 By similarity.
 DISULFID 189 204 By similarity.
 DISULFID 206 215 By similarity.
 DISULFID 222 233 By similarity.
 DISULFID 227 243 By similarity.
 DISULFID 245 254 By similarity.
 DISULFID 261 272 By similarity.
 DISULFID 266 281 By similarity.
 DISULFID 283 292 By similarity.
 DISULFID 299 312 By similarity.
 DISULFID 306 321 By similarity.
 DISULFID 323 332 By similarity.
 DISULFID 339 350 By similarity.
 DISULFID 344 359 By similarity.
 DISULFID 361 370 By similarity.
 DISULFID 376 387 By similarity.
 DISULFID 381 398 By similarity.
 DISULFID 400 409 By similarity.
 DISULFID 416 429 By similarity.
 DISULFID 423 438 By similarity.
 DISULFID 440 449 By similarity.
 DISULFID 456 467 By similarity.
 DISULFID 461 476 By similarity.
 DISULFID 478 487 By similarity.
 DISULFID 494 505 By similarity.
 DISULFID 499 514 By similarity.
 DISULFID 516 525 By similarity.
 DISULFID 532 543 By similarity.
 DISULFID 537 552 By similarity.
 DISULFID 554 563 By similarity.
 DISULFID 570 580 By similarity.
 DISULFID 575 589 By similarity.
 DISULFID 591 600 By similarity.
 DISULFID 607 618 By similarity.
 DISULFID 612 627 By similarity.
 DISULFID 629 638 By similarity.
 DISULFID 645 655 By similarity.
 DISULFID 650 664 By similarity.
 DISULFID 666 675 By similarity.
 DISULFID 682 693 By similarity.
 DISULFID 687 702 By similarity.
 DISULFID 704 713 By similarity.
 DISULFID 720 730 By similarity.
 DISULFID 725 739 By similarity.
 DISULFID 741 750 By similarity.
 DISULFID 757 768 By similarity.
 DISULFID 762 777 By similarity.
 DISULFID 779 788 By similarity.
 DISULFID 795 806 By similarity.
 DISULFID 800 815 By similarity.
 DISULFID 817 826 By similarity.
 DISULFID 833 844 By similarity.
 DISULFID 838 855 By similarity.
 DISULFID 857 866 By similarity.
 DISULFID 873 884 By similarity.
 DISULFID 878 893 By similarity.
 DISULFID 895 904 By similarity.
 DISULFID 911 922 By similarity.
 DISULFID 916 931 By similarity.
 DISULFID 933 942 By similarity.
 DISULFID 949 960 By similarity.
 DISULFID 954 969 By similarity.
 DISULFID 971 980 By similarity.
 DISULFID 987 998 By similarity.
 DISULFID 992 1007 By similarity.
 DISULFID 1009 1018 By similarity.
 DISULFID 1025 1036 By similarity.
 DISULFID 1030 1045 By similarity.
 DISULFID 1047 1056 By similarity.
 DISULFID 1063 1074 By similarity.
 DISULFID 1068 1083 By similarity.
 DISULFID 1085 1094 By similarity.
 DISULFID 1101 1122 By similarity.
 DISULFID 1116 1131 By similarity.
 DISULFID 1133 1142 By similarity.
 DISULFID 1149 1160 By similarity.
 DISULFID 1154 1169 By similarity.
 DISULFID 1171 1180 By similarity.
 DISULFID 1187 1198 By similarity.
 DISULFID 1192 1207 By similarity.
 DISULFID 1209 1218 By similarity.
 DISULFID 1225 1244 By similarity.
 DISULFID 1238 1253 By similarity.
 DISULFID 1255 1264 By similarity.
 DISULFID 1271 1284 By similarity.
 DISULFID 1276 1293 By similarity.
 DISULFID 1295 1304 By similarity.
 DISULFID 1311 1322 By similarity.
 DISULFID 1316 1334 By similarity.
 DISULFID 1336 1345 By similarity.
 DISULFID 1352 1363 By similarity.
 DISULFID 1357 1372 By similarity.
 DISULFID 1374 1383 By similarity.
 DISULFID 1391 1403 By similarity.
 DISULFID 1397 1414 By similarity.
 DISULFID 1416 1425 By similarity.
 DISULFID 1449 1472 By similarity.
 DISULFID 1454 1467 By similarity.
 DISULFID 1463 1479 By similarity.
 DISULFID 1490 1514 By similarity.
 DISULFID 1496 1509 By similarity.
 DISULFID 1505 1521 By similarity.
 DISULFID 1536 1549 By similarity.
 DISULFID 1545 1561 By similarity.
 CROSSLNK 1749 1749 Glycyl lysine isopeptide (Lys-Gly)  
Keyword
 Activator; Angiogenesis; ANK repeat; Calcium; Cell membrane; Complete proteome; Developmental protein; Differentiation; Disulfide bond; EGF-like domain; Glycoprotein; Hydroxylation; Isopeptide bond; Membrane; Metal-binding; Notch signaling pathway; Nucleus; Phosphoprotein; Receptor; Reference proteome; Repeat; Signal; Transcription; Transcription regulation; Transmembrane; Transmembrane helix; Ubl conjugation. 
Sequence Source
 UniProt (SWISSPROT/TrEMBL); GenBank; EMBL 
Protein Length
 2531 AA 
Protein Sequence
MPRLLAPLLC LTLLPALAAR GLRCSQPSGT CLNGGRCEVA NGTEACVCSG AFVGQRCQDP 60
SPCLSTPCKN AGTCYVVDHG GIVDYACSCP LGFSGPLCLT PLANACLANP CRNGGTCDLL 120
TLTEYKCRCP PGWSGKSCQQ ADPCASNPCA NGGQCLPFES SYICGCPPGF HGPTCRQDVN 180
ECSQNPGLCR HGGTCHNEIG SYRCACRATH TGPHCELPYV PCSPSPCQNG GTCRPTGDTT 240
HECACLPGFA GQNCEENVDD CPGNNCKNGG ACVDGVNTYN CRCPPEWTGQ YCTEDVDECQ 300
LMPNACQNAG TCHNSHGGYN CVCVNGWTGE DCSDNIDDCA SAACFQGATC HDRVASFYCE 360
CPHGRTGLLC HLNDACISNP CNEGSNCDTN PVNGKAICTC PRGYTGPACS QDVDECALGA 420
NPCEHAGKCL NTLGSFECQC LQGYTGPRCE IDVNECISNP CQNDATCLDQ IGEFQCICMP 480
GYEGVYCEIN TDECASSPCL HNGRCVDKIN EFLCQCPKGF SGHLCQYDVD ECASTPCKNG 540
AKCLDGPNTY TCVCTEGYTG THCEVDIDEC DPDPCHIGLC KDGVATFTCL CQPGYTGHHC 600
ETNINECHSQ PCRHGGTCQD RDNYYLCLCL KGTTGPNCEI NLDDCASNPC DSGTCLDKID 660
GYECACEPGY TGSMCNVNID ECAGSPCHNG GTCEDGIAGF TCRCPEGYHD PTCLSEVNEC 720
NSNPCIHGAC RDGLNGYKCD CAPGWSGTNC DINNNECESN PCVNGGTCKD MTSGYVCTCR 780
EGFSGPNCQT NINECASNPC LNQGTCIDDV AGYKCNCPLP YTGATCEVVL APCATSPCKN 840
SGVCKESEDY ESFSCVCPTG WQGQTCEIDI NECVKSPCRH GASCQNTNGS YRCLCQAGYT 900
GRNCESDIDD CRPNPCHNGG SCTDGVNAAF CDCLPGFQGA FCEEDINECA TNPCQNGANC 960
TDCVDSYTCT CPTGFNGIHC ENNTPDCTES SCFNGGTCVD GINSFTCLCP PGFTGSYCQY 1020
DVNECDSRPC LHGGTCQDSY GTYKCTCPQG YTGLNCQNLV RWCDSAPCKN GGKCWQTNTQ 1080
YHCECRSGWT GFNCDVLSVS CEVAAQKRGI DVTLLCQHGG LCVDEEDKHY CHCQAGYTGS 1140
YCEDEVDECS PNPCQNGATC TDYLGGFSCK CVAGYHGSNC SEEINECLSQ PCQNGGTCID 1200
LTNTYKCSCP RGTQGVHCEI NVDDCHPPLD PASRSPKCFN NGTCVDQVGG YTCTCPPGFV 1260
GERCEGDVNE CLSNPCDPRG TQNCVQRVND FHCECRAGHT GRRCESVING CRGKPCRNGG 1320
VCAVASNTAR GFICRCPARF EGATCENDAR TCGSLRCLNG GTCISGPRSP TCLCLGSFTG 1380
PECQFPASSP CVGSNPCYNQ GTCEPTSESP FYRCLCPAKF NGLLCHILDY SFTGAAGRDI 1440
PPPQIEEACE LPECQEDAGN KVCNLQCNNH ACGWDGGDCS LNFNDPWKNC TQSLQCWKYF 1500
SDGHCDSQCN SAGCLFDGFD CQLTEGQCNP LYDQYCKDHF SDGHCDQGCN SAECEWDGLD 1560
CAEHVPERLA AGTLVLVVLL PPDQLRNNSF HFLRDVSHVL HTNVVFKRDA QGQQMIFPYY 1620
GREEELRKHP IKRSAVGWAT TSLLPGTNGG RQRRELDPMD IHGSIVYLEI DNRQCVQSSS 1680
QCFQSATDVA AFLGALASLG SLNIPYKIEA VKSETVEPPL PSQLHLMYVA AAAFVLLFFV 1740
GCGVLLSRKR RRQHGQLWFP EGFKVSEASK KKRREPLGED SVGLKPLKNA SDGALMDDNQ 1800
NEWGDEDLET KKFRFEEPVV LPDLDDQTDH RQWTQQHLDA ADLRVSAMAP TPPQGEVDAD 1860
CMDVNVRGPD GFTPLMIASC SGGGLETGNS EEEEDAPAVI SDFIYQGASL HNQTDRTGET 1920
ALHLAARYSR SDAAKRLLEA SADANIQDNM GRTPLHAAVS ADAQGVFQIL LRNRATDLDA 1980
RMHDGTTPLI LAARLAVEGM LEDLINSHAD VNAVDDLGKS ALHWAAAVNN VDAAVVLLKN 2040
GANKDMQNNK EETPLFLAAR EGSYETAKVL LDHFANRDIT DHMDRLPRDI AQERMHHDIV 2100
RLLDEYNLVR SPQLHGTALG GTPTLSPTLC SPNGYLGNLK SATQGKKARK PSTKGLACSS 2160
KEAKDLKARR KKSQDGKGCL LDSSSMLSPV DSLESPHGYL SDVASPPLLP SPFQQSPSMP 2220
LSHLPGMPDT HLGISHLNVA AKPEMAALAG GSRLAFEPPP PRLSHLPVAS SASTVLSTNG 2280
TGAMNFTVGA PASLNGQCEW LPRLQNGMVP SQYNPLRPGV TPGTLSTQAA GLQHGMMGPI 2340
HSSLSTNTLS PIIYQGLPNT RLATQPHLVQ TQQVQPQNLQ IQPQNLQPPS QPHLSVSSAA 2400
NGHLGRSFLS GEPSQADVQP LGPSSLPVHT ILPQESQALP TSLPSSMVPP MTTTQFLTPP 2460
SQHSYSSSPV DNTPSHQLQV PEHPFLTPSP ESPDQWSSSS RHSNISDWSE GISSPPTSMP 2520
SQITHIPEAF K 2531 
Gene Ontology
 GO:0001669; C:acrosomal vesicle; IDA:RGD.
 GO:0005856; C:cytoskeleton; ISS:UniProtKB.
 GO:0005794; C:Golgi apparatus; IDA:RGD.
 GO:0016021; C:integral to membrane; IEA:UniProtKB-KW.
 GO:0030027; C:lamellipodium; ISS:UniProtKB.
 GO:0005634; C:nucleus; IDA:RGD.
 GO:0005886; C:plasma membrane; IDA:RGD.
 GO:0001726; C:ruffle; ISS:UniProtKB.
 GO:0005509; F:calcium ion binding; IEA:InterPro.
 GO:0001047; F:core promoter binding; ISS:UniProtKB.
 GO:0019899; F:enzyme binding; ISS:UniProtKB.
 GO:0004857; F:enzyme inhibitor activity; ISS:UniProtKB.
 GO:0004872; F:receptor activity; IEA:InterPro.
 GO:0001525; P:angiogenesis; IEA:UniProtKB-KW.
 GO:0048708; P:astrocyte differentiation; IDA:RGD.
 GO:0021515; P:cell differentiation in spinal cord; IEP:RGD.
 GO:0035924; P:cellular response to vascular endothelial growth factor stimulus; ISS:UniProtKB.
 GO:0009790; P:embryo development; IDA:RGD.
 GO:0090051; P:negative regulation of cell migration involved in sprouting angiogenesis; ISS:UniProtKB.
 GO:2001027; P:negative regulation of endothelial cell chemotaxis; ISS:UniProtKB.
 GO:0060253; P:negative regulation of glial cell proliferation; ISS:UniProtKB.
 GO:0010832; P:negative regulation of myotube differentiation; ISS:UniProtKB.
 GO:0045665; P:negative regulation of neuron differentiation; IMP:RGD.
 GO:0048715; P:negative regulation of oligodendrocyte differentiation; ISS:UniProtKB.
 GO:2000974; P:negative regulation of pro-B cell differentiation; ISS:UniProtKB.
 GO:0000122; P:negative regulation of transcription from RNA polymerase II promoter; ISS:UniProtKB.
 GO:0048709; P:oligodendrocyte differentiation; IEP:RGD.
 GO:0031100; P:organ regeneration; IEP:RGD.
 GO:0048711; P:positive regulation of astrocyte differentiation; ISS:UniProtKB.
 GO:0030513; P:positive regulation of BMP signaling pathway; ISS:UniProtKB.
 GO:0045603; P:positive regulation of endothelial cell differentiation; IMP:RGD.
 GO:0046427; P:positive regulation of JAK-STAT cascade; ISS:UniProtKB.
 GO:0002052; P:positive regulation of neuroblast proliferation; IMP:RGD.
 GO:0061419; P:positive regulation of transcription from RNA polymerase II promoter in response to hypoxia; ISS:UniProtKB.
 GO:0007221; P:positive regulation of transcription of Notch receptor target; IMP:RGD.
 GO:0003264; P:regulation of cardioblast proliferation; IMP:RGD.
 GO:0031960; P:response to corticosteroid stimulus; IEP:RGD.
 GO:0032496; P:response to lipopolysaccharide; IEP:RGD.
 GO:0007283; P:spermatogenesis; IMP:RGD.
 GO:0042246; P:tissue regeneration; IEP:RGD.
 GO:0006351; P:transcription, DNA-dependent; IEA:UniProtKB-KW.
 GO:0035148; P:tube formation; ISS:UniProtKB. 
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.
 IPR022362; Notch_1.
 IPR000800; Notch_dom.
 IPR010660; Notch_NOD_dom.
 IPR011656; Notch_NODP_dom. 
Pfam
 PF00023; Ank
 PF12796; Ank_2
 PF11936; DUF3454
 PF00008; EGF
 PF07645; EGF_CA
 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.
 PR01984; NOTCH1.