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Protein

Neurogenic locus notch homolog protein 1

Gene

notch1

Organism
Xenopus laevis (African clawed frog)
Status
Reviewed-Annotation score: -Experimental evidence at protein leveli

Functioni

Functions as a receptor for membrane-bound ligands Jagged-1 (JAG1), Jagged-2 (JAG2) and Delta-1 (DLL1) 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. Involved in angiogenesis; negatively regulates endothelial cell proliferation and migration and angiogenic sprouting. Involved in the maturation of both CD4+ and CD8+ cells in the thymus. Important for follicular differentiation and possibly cell fate selection within the follicle. During cerebellar development, functions as a receptor for neuronal DNER and is involved in the differentiation of Bergmann glia. Represses neuronal and myogenic differentiation. May play an essential role in postimplantation development, probably in some aspect of cell specification and/or differentiation. May be involved in mesoderm development, somite formation and neurogenesis. Involved in determination of left/right symmetry by modulating the balance between motile and immotile (sensory) cilia at the left-right organiser (LRO) (By similarity).By similarity

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Metal bindingi431Calcium 1; via carbonyl oxygenBy similarity1
Metal bindingi434Calcium 1; via amide nitrogenBy similarity1
Metal bindingi451Calcium 2By similarity1
Metal bindingi452Calcium 2; via carbonyl oxygenBy similarity1
Metal bindingi454Calcium 2By similarity1
Metal bindingi468Calcium 2By similarity1
Metal bindingi469Calcium 2; via carbonyl oxygenBy similarity1
Metal bindingi489Calcium 3By similarity1
Metal bindingi490Calcium 3; via carbonyl oxygenBy similarity1
Metal bindingi492Calcium 3By similarity1
Metal bindingi506Calcium 3By similarity1
Metal bindingi507Calcium 3; via carbonyl oxygenBy similarity1

GO - Molecular functioni

GO - Biological processi

Keywordsi

Molecular functionActivator, Developmental protein, Receptor
Biological processAngiogenesis, Differentiation, Notch signaling pathway, Transcription, Transcription regulation
LigandCalcium, Metal-binding

Names & Taxonomyi

Protein namesi
Recommended name:
Neurogenic locus notch homolog protein 1
Short name:
Notch 1
Short name:
xOTCH
Cleaved into the following 2 chains:
Gene namesi
Name:notch1
Synonyms:xotch
OrganismiXenopus laevis (African clawed frog)
Taxonomic identifieri8355 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiAmphibiaBatrachiaAnuraPipoideaPipidaeXenopodinaeXenopusXenopus

Organism-specific databases

XenbaseiXB-GENE-865261 notch1

Subcellular locationi

Extracellular region or secreted Cytosol Plasma membrane Cytoskeleton Lysosome Endosome Peroxisome ER Golgi apparatus Nucleus Mitochondrion Manual annotation Automatic computational assertionGraphics by Christian Stolte; Source: COMPARTMENTS

Topology

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Topological domaini20 – 1728ExtracellularSequence analysisAdd BLAST1709
Transmembranei1729 – 1750HelicalSequence analysisAdd BLAST22
Topological domaini1751 – 2524CytoplasmicSequence analysisAdd BLAST774

Keywords - Cellular componenti

Cell membrane, Membrane, Nucleus

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Signal peptidei1 – 19Sequence analysisAdd BLAST19
ChainiPRO_000000770920 – 2524Neurogenic locus notch homolog protein 1Add BLAST2505
ChainiPRO_00004252021715 – 2524Notch 1 extracellular truncationBy similarityAdd BLAST810
ChainiPRO_00004252031748 – 2524Notch 1 intracellular domainBy similarityAdd BLAST777

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Disulfide bondi22 ↔ 35By similarity
Disulfide bondi29 ↔ 45By similarity
Disulfide bondi47 ↔ 56By similarity
Disulfide bondi62 ↔ 74By similarity
Disulfide bondi68 ↔ 87By similarity
Disulfide bondi89 ↔ 98By similarity
Disulfide bondi106 ↔ 117By similarity
Disulfide bondi111 ↔ 128By similarity
Disulfide bondi130 ↔ 139By similarity
Disulfide bondi145 ↔ 156By similarity
Disulfide bondi150 ↔ 165By similarity
Disulfide bondi167 ↔ 176By similarity
Disulfide bondi183 ↔ 194By similarity
Disulfide bondi188 ↔ 203By similarity
Disulfide bondi205 ↔ 214By similarity
Disulfide bondi221 ↔ 232By similarity
Disulfide bondi226 ↔ 242By similarity
Glycosylationi231O-linked (Fuc...) threonine; alternateBy similarity1
Glycosylationi231O-linked (GalNAc...) threonine; alternateBy similarity1
Disulfide bondi244 ↔ 253By similarity
Disulfide bondi260 ↔ 271By similarity
Disulfide bondi265 ↔ 280By similarity
Disulfide bondi282 ↔ 291By similarity
Disulfide bondi298 ↔ 311By similarity
Disulfide bondi305 ↔ 320By similarity
Disulfide bondi322 ↔ 331By similarity
Disulfide bondi338 ↔ 349By similarity
Disulfide bondi343 ↔ 358By similarity
Disulfide bondi360 ↔ 369By similarity
Disulfide bondi375 ↔ 386By similarity
Disulfide bondi380 ↔ 397By similarity
Disulfide bondi399 ↔ 408By similarity
Disulfide bondi415 ↔ 428By similarity
Disulfide bondi422 ↔ 437By similarity
Glycosylationi434O-linked (Glc...) serineBy similarity1
Disulfide bondi439 ↔ 448By similarity
Disulfide bondi455 ↔ 466By similarity
Glycosylationi457O-linked (Glc...) serineBy similarity1
Disulfide bondi460 ↔ 475By similarity
Glycosylationi462N-linked (GlcNAc...) asparagineSequence analysis1
Glycosylationi465O-linked (Fuc...) threonineBy similarity1
Disulfide bondi477 ↔ 486By similarity
Disulfide bondi493 ↔ 504By similarity
Glycosylationi495O-linked (Glc...) serineBy similarity1
Disulfide bondi498 ↔ 513By similarity
Disulfide bondi515 ↔ 524By similarity
Disulfide bondi531 ↔ 542By similarity
Disulfide bondi536 ↔ 551By similarity
Disulfide bondi553 ↔ 562By similarity
Disulfide bondi569 ↔ 579By similarity
Disulfide bondi574 ↔ 588By similarity
Disulfide bondi590 ↔ 599By similarity
Disulfide bondi606 ↔ 617By similarity
Disulfide bondi611 ↔ 626By similarity
Disulfide bondi628 ↔ 637By similarity
Disulfide bondi644 ↔ 654By similarity
Disulfide bondi649 ↔ 663By similarity
Disulfide bondi665 ↔ 674By similarity
Disulfide bondi681 ↔ 692By similarity
Disulfide bondi686 ↔ 701By similarity
Disulfide bondi703 ↔ 712By similarity
Disulfide bondi719 ↔ 729By similarity
Disulfide bondi724 ↔ 738By similarity
Disulfide bondi740 ↔ 749By similarity
Disulfide bondi756 ↔ 767By similarity
Disulfide bondi761 ↔ 776By similarity
Disulfide bondi778 ↔ 787By similarity
Disulfide bondi794 ↔ 805By similarity
Disulfide bondi799 ↔ 814By similarity
Disulfide bondi816 ↔ 825By similarity
Disulfide bondi832 ↔ 843By similarity
Disulfide bondi837 ↔ 854By similarity
Disulfide bondi856 ↔ 865By similarity
Disulfide bondi872 ↔ 883By similarity
Disulfide bondi877 ↔ 892By similarity
Glycosylationi887N-linked (GlcNAc...) asparagineSequence analysis1
Disulfide bondi894 ↔ 903By similarity
Disulfide bondi910 ↔ 921By similarity
Disulfide bondi915 ↔ 930By similarity
Disulfide bondi932 ↔ 941By similarity
Disulfide bondi948 ↔ 959By similarity
Disulfide bondi953 ↔ 968By similarity
Glycosylationi958N-linked (GlcNAc...) asparagineSequence analysis1
Disulfide bondi970 ↔ 979By similarity
Disulfide bondi986 ↔ 997By similarity
Disulfide bondi991 ↔ 1006By similarity
Disulfide bondi1008 ↔ 1017By similarity
Disulfide bondi1024 ↔ 1035By similarity
Disulfide bondi1029 ↔ 1044By similarity
Disulfide bondi1046 ↔ 1055By similarity
Disulfide bondi1062 ↔ 1073By similarity
Disulfide bondi1067 ↔ 1082By similarity
Disulfide bondi1084 ↔ 1093By similarity
Disulfide bondi1100 ↔ 1121By similarity
Disulfide bondi1115 ↔ 1130By similarity
Disulfide bondi1132 ↔ 1141By similarity
Disulfide bondi1148 ↔ 1159By similarity
Disulfide bondi1153 ↔ 1168By similarity
Disulfide bondi1170 ↔ 1179By similarity
Glycosylationi1178N-linked (GlcNAc...) asparagineSequence analysis1
Disulfide bondi1186 ↔ 1197By similarity
Disulfide bondi1191 ↔ 1206By similarity
Disulfide bondi1208 ↔ 1217By similarity
Disulfide bondi1224 ↔ 1243By similarity
Disulfide bondi1237 ↔ 1252By similarity
Disulfide bondi1254 ↔ 1263By similarity
Disulfide bondi1270 ↔ 1283By similarity
Disulfide bondi1275 ↔ 1292By similarity
Disulfide bondi1294 ↔ 1303By similarity
Disulfide bondi1310 ↔ 1321By similarity
Disulfide bondi1315 ↔ 1333By similarity
Disulfide bondi1335 ↔ 1344By similarity
Disulfide bondi1351 ↔ 1362By similarity
Disulfide bondi1356 ↔ 1371By similarity
Disulfide bondi1373 ↔ 1382By similarity
Disulfide bondi1390 ↔ 1401By similarity
Disulfide bondi1395 ↔ 1412By similarity
Glycosylationi1400O-linked (Fuc...) threonine; alternateBy similarity1
Glycosylationi1400O-linked (GalNAc...) threonine; alternateBy similarity1
Disulfide bondi1414 ↔ 1423By similarity
Disulfide bondi1447 ↔ 1470By similarity
Disulfide bondi1452 ↔ 1465By similarity
Disulfide bondi1461 ↔ 1477By similarity
Glycosylationi1487N-linked (GlcNAc...) asparagineSequence analysis1
Disulfide bondi1488 ↔ 1512By similarity
Disulfide bondi1494 ↔ 1507By similarity
Disulfide bondi1503 ↔ 1519By similarity
Glycosylationi1508N-linked (GlcNAc...) asparagineSequence analysis1
Disulfide bondi1534 ↔ 1547By similarity
Disulfide bondi1543 ↔ 1559By similarity
Glycosylationi1584N-linked (GlcNAc...) asparagineSequence analysis1

Post-translational modificationi

O-glycosylated on the EGF-like domains. Contains both O-linked fucose and O-linked glucose. O-linked glycosylation by galnt11 is involved in determination of left/right symmetry: glycosylation promotes activation of notch1, possibly by promoting cleavage by adam17, modulating the balance between motile and immotile (sensory) cilia at the left-right organiser (LRO) (By similarity).By similarity
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 adam17 to yield a membrane-associated intermediate fragment called notch extracellular truncation (NEXT). Following endocytosis, this fragment is then cleaved by presenilin dependent gamma-secretase to release a notch-derived peptide containing the intracellular domain (NICD) from the membrane (By similarity).By similarity

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sitei1657 – 1658Cleavage; by furin-like proteaseBy similarity2
Sitei1714 – 1715Cleavage; by adam17By similarity2

Keywords - PTMi

Disulfide bond, Glycoprotein

Proteomic databases

PRIDEiP21783

Expressioni

Developmental stagei

Expressed almost uniformly in early embryos.

Interactioni

Subunit structurei

Forms a ternary complex with nrarp and rbpj/suh.1 Publication

Structurei

3D structure databases

ProteinModelPortaliP21783
SMRiP21783
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Domaini20 – 57EGF-like 1PROSITE-ProRule annotationAdd BLAST38
Domaini58 – 99EGF-like 2PROSITE-ProRule annotationAdd BLAST42
Domaini102 – 140EGF-like 3PROSITE-ProRule annotationAdd BLAST39
Domaini141 – 177EGF-like 4PROSITE-ProRule annotationAdd BLAST37
Domaini179 – 215EGF-like 5; calcium-bindingPROSITE-ProRule annotationAdd BLAST37
Domaini217 – 254EGF-like 6PROSITE-ProRule annotationAdd BLAST38
Domaini256 – 292EGF-like 7; calcium-bindingPROSITE-ProRule annotationAdd BLAST37
Domaini294 – 332EGF-like 8; calcium-bindingPROSITE-ProRule annotationAdd BLAST39
Domaini334 – 370EGF-like 9; calcium-bindingPROSITE-ProRule annotationAdd BLAST37
Domaini371 – 409EGF-like 10PROSITE-ProRule annotationAdd BLAST39
Domaini411 – 449EGF-like 11; calcium-bindingPROSITE-ProRule annotationAdd BLAST39
Domaini451 – 487EGF-like 12; calcium-bindingPROSITE-ProRule annotationAdd BLAST37
Domaini489 – 525EGF-like 13; calcium-bindingPROSITE-ProRule annotationAdd BLAST37
Domaini527 – 563EGF-like 14; calcium-bindingPROSITE-ProRule annotationAdd BLAST37
Domaini565 – 600EGF-like 15; calcium-bindingPROSITE-ProRule annotationAdd BLAST36
Domaini602 – 638EGF-like 16; calcium-bindingPROSITE-ProRule annotationAdd BLAST37
Domaini640 – 675EGF-like 17PROSITE-ProRule annotationAdd BLAST36
Domaini677 – 713EGF-like 18; calcium-bindingPROSITE-ProRule annotationAdd BLAST37
Domaini715 – 750EGF-like 19; calcium-bindingPROSITE-ProRule annotationAdd BLAST36
Domaini752 – 788EGF-like 20; calcium-bindingPROSITE-ProRule annotationAdd BLAST37
Domaini790 – 826EGF-like 21; calcium-bindingPROSITE-ProRule annotationAdd BLAST37
Domaini828 – 866EGF-like 22PROSITE-ProRule annotationAdd BLAST39
Domaini868 – 904EGF-like 23; calcium-bindingPROSITE-ProRule annotationAdd BLAST37
Domaini906 – 942EGF-like 24; calcium-bindingPROSITE-ProRule annotationAdd BLAST37
Domaini944 – 980EGF-like 25; calcium-bindingPROSITE-ProRule annotationAdd BLAST37
Domaini982 – 1018EGF-like 26PROSITE-ProRule annotationAdd BLAST37
Domaini1020 – 1056EGF-like 27; calcium-bindingPROSITE-ProRule annotationAdd BLAST37
Domaini1058 – 1094EGF-like 28PROSITE-ProRule annotationAdd BLAST37
Domaini1096 – 1142EGF-like 29PROSITE-ProRule annotationAdd BLAST47
Domaini1144 – 1180EGF-like 30; calcium-bindingPROSITE-ProRule annotationAdd BLAST37
Domaini1182 – 1218EGF-like 31; calcium-bindingPROSITE-ProRule annotationAdd BLAST37
Domaini1220 – 1264EGF-like 32; calcium-bindingPROSITE-ProRule annotationAdd BLAST45
Domaini1266 – 1304EGF-like 33PROSITE-ProRule annotationAdd BLAST39
Domaini1306 – 1346EGF-like 34PROSITE-ProRule annotationAdd BLAST41
Domaini1347 – 1383EGF-like 35PROSITE-ProRule annotationAdd BLAST37
Domaini1386 – 1424EGF-like 36PROSITE-ProRule annotationAdd BLAST39
Repeati1447 – 1487LNR 1Add BLAST41
Repeati1488 – 1529LNR 2Add BLAST42
Repeati1530 – 1564LNR 3Add BLAST35
Repeati1876 – 1919ANK 1Add BLAST44
Repeati1924 – 1953ANK 2Add BLAST30
Repeati1957 – 1987ANK 3Add BLAST31
Repeati1991 – 2020ANK 4Add BLAST30
Repeati2024 – 2053ANK 5Add BLAST30
Repeati2057 – 2086ANK 6Add BLAST30

Sequence similaritiesi

Belongs to the NOTCH family.Curated

Keywords - Domaini

ANK repeat, EGF-like domain, Repeat, Signal, Transmembrane, Transmembrane helix

Phylogenomic databases

HOVERGENiHBG052650
KOiK02599

Family and domain databases

CDDicd00204 ANK, 2 hits
Gene3Di1.25.40.20, 1 hit
InterProiView protein in InterPro
IPR002110 Ankyrin_rpt
IPR020683 Ankyrin_rpt-contain_dom
IPR036770 Ankyrin_rpt-contain_sf
IPR024600 DUF3454_notch
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_cys_sf
IPR008297 Notch
IPR035993 Notch-like_dom_sf
IPR022362 Notch_1
IPR000800 Notch_dom
IPR010660 Notch_NOD_dom
IPR011656 Notch_NODP_dom
PfamiView protein in Pfam
PF12796 Ank_2, 2 hits
PF11936 DUF3454, 1 hit
PF00008 EGF, 28 hits
PF07645 EGF_CA, 4 hits
PF12661 hEGF, 1 hit
PF06816 NOD, 1 hit
PF07684 NODP, 1 hit
PF00066 Notch, 3 hits
PIRSFiPIRSF002279 Notch, 1 hit
PRINTSiPR01452 LNOTCHREPEAT
PR01984 NOTCH1
SMARTiView protein in SMART
SM00248 ANK, 6 hits
SM01334 DUF3454, 1 hit
SM00181 EGF, 36 hits
SM00179 EGF_CA, 32 hits
SM00004 NL, 3 hits
SM01338 NOD, 1 hit
SM01339 NODP, 1 hit
SUPFAMiSSF48403 SSF48403, 1 hit
SSF57184 SSF57184, 5 hits
SSF90193 SSF90193, 3 hits
PROSITEiView protein in PROSITE
PS50297 ANK_REP_REGION, 1 hit
PS50088 ANK_REPEAT, 4 hits
PS00010 ASX_HYDROXYL, 23 hits
PS00022 EGF_1, 34 hits
PS01186 EGF_2, 29 hits
PS50026 EGF_3, 36 hits
PS01187 EGF_CA, 21 hits
PS50258 LNR, 3 hits

Sequencei

Sequence statusi: Complete.

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

P21783-1 [UniParc]FASTAAdd to basket
« Hide
        10         20         30         40         50
MDRIGLAVLL CSLPVLTQGL RCTQTAEMCL NGGRCEMTPG GTGVCLCGNL
60 70 80 90 100
YFGERCQFPN PCTIKNQCMN FGTCEPVLQG NAIDFICHCP VGFTDKVCLT
110 120 130 140 150
PVDNACVNNP CRNGGTCELL NSVTEYKCRC PPGWTGDSCQ QADPCASNPC
160 170 180 190 200
ANGGKCLPFE IQYICKCPPG FHGATCKQDI NECSQNPCKN GGQCINEFGS
210 220 230 240 250
YRCTCQNRFT GRNCDEPYVP CNPSPCLNGG TCRQTDDTSY DCTCLPGFSG
260 270 280 290 300
QNCEENIDDC PSNNCRNGGT CVDGVNTYNC QCPPDWTGQY CTEDVDECQL
310 320 330 340 350
MPNACQNGGT CHNTYGGYNC VCVNGWTGED CSENIDDCAN AACHSGATCH
360 370 380 390 400
DRVASFYCEC PHGRTGLLCH LDNACISNPC NEGSNCDTNP VNGKAICTCP
410 420 430 440 450
PGYTGPACNN DVDECSLGAN PCEHGGRCTN TLGSFQCNCP QGYAGPRCEI
460 470 480 490 500
DVNECLSNPC QNDSTCLDQI GEFQCICMPG YEGLYCETNI DECASNPCLH
510 520 530 540 550
NGKCIDKINE FRCDCPTGFS GNLCQHDFDE CTSTPCKNGA KCLDGPNSYT
560 570 580 590 600
CQCTEGFTGR HCEQDINECI PDPCHYGTCK DGIATFTCLC RPGYTGRLCD
610 620 630 640 650
NDINECLSKP CLNGGQCTDR ENGYICTCPK GTTGVNCETK IDDCASNLCD
660 670 680 690 700
NGKCIDKIDG YECTCEPGYT GKLCNININE CDSNPCRNGG TCKDQINGFT
710 720 730 740 750
CVCPDGYHDH MCLSEVNECN SNPCIHGACH DGVNGYKCDC EAGWSGSNCD
760 770 780 790 800
INNNECESNP CMNGGTCKDM TGAYICTCKA GFSGPNCQTN INECSSNPCL
810 820 830 840 850
NHGTCIDDVA GYKCNCMLPY TGAICEAVLA PCAGSPCKNG GRCKESEDFE
860 870 880 890 900
TFSCECPPGW QGQTCEIDMN ECVNRPCRNG ATCQNTNGSY KCNCKPGYTG
910 920 930 940 950
RNCEMDIDDC QPNPCHNGGS CSDGINMFFC NCPAGFRGPK CEEDINECAS
960 970 980 990 1000
NPCKNGANCT DCVNSYTCTC QPGFSGIHCE SNTPDCTESS CFNGGTCIDG
1010 1020 1030 1040 1050
INTFTCQCPP GFTGSYCQHD INECDSKPCL NGGTCQDSYG TYKCTCPQGY
1060 1070 1080 1090 1100
TGLNCQNLVR WCDSSPCKNG GKCWQTNNFY RCECKSGWTG VYCDVPSVSC
1110 1120 1130 1140 1150
EVAAKQQGVD IVHLCRNSGM CVDTGNTHFC RCQAGYTGSY CEEQVDECSP
1160 1170 1180 1190 1200
NPCQNGATCT DYLGGYSCEC VAGYHGVNCS EEINECLSHP CQNGGTCIDL
1210 1220 1230 1240 1250
INTYKCSCPR GTQGVHCEIN VDDCTPFYDS FTLEPKCFNN GKCIDRVGGY
1260 1270 1280 1290 1300
NCICPPGFVG ERCEGDVNEC LSNPCDSRGT QNCIQLVNDY RCECRQGFTG
1310 1320 1330 1340 1350
RRCESVVDGC KGMPCRNGGT CAVASNTERG FICKCPPGFD GATCEYDSRT
1360 1370 1380 1390 1400
CSNLRCQNGG TCISVLTSSK CVCSEGYTGA TCQYPVISPC ASHPCYNGGT
1410 1420 1430 1440 1450
CQFFAEEPFF QCFCPKNFNG LFCHILDYEF PGGLGKNITP PDNDDICENE
1460 1470 1480 1490 1500
QCSELADNKV CNANCNNHAC GWDGGDCSLN FNDPWKNCTQ SLQCWKYFND
1510 1520 1530 1540 1550
GKCDSQCNNT GCLYDGFDCQ KVEVQCNPLY DQYCKDHFQD GHCDQGCNNA
1560 1570 1580 1590 1600
ECEWDGLDCA NMPENLAEGT LVLVVLMPPE RLKNNSVNFL RELSRVLHTN
1610 1620 1630 1640 1650
VVFKKDSKGE YKIYPYYGNE EELKKHHIKR STDYWSDAPS AIFSTMKESI
1660 1670 1680 1690 1700
LLGRHRRELD EMEVRGSIVY LEIDNRQCYK SSSQCFNSAT DVAAFLGALA
1710 1720 1730 1740 1750
SLGSLDTLSY KIEAVKSENM ETPKPSTLYP MLSMLVIPLL IIFVFMMVIV
1760 1770 1780 1790 1800
NKKRRREHGQ LWFPDGFIPK EPSKKKRRDR LGEDSVGLKP IKNMTDGSFM
1810 1820 1830 1840 1850
DDNQNEWGDE ETLENKRFRF EEQVILPELV DDKTDPRQWT RQHLDAADLR
1860 1870 1880 1890 1900
ISSMAPTPPQ GEIEADCMDV NVRGPDGFTP LMIASCSGGG LETGNSEEEE
1910 1920 1930 1940 1950
DASANMISDF IGQGAQLHNQ TDRTGETALH LAARYARADA AKRLLESSAD
1960 1970 1980 1990 2000
ANVQDNMGRT PLHAAVAADA QGVFQILIRN RATDLDARMF DGTTPLILAA
2010 2020 2030 2040 2050
RLAVEGMVEE LINAHADVNA VDEFGKSALH WAAAVNNVDA AAVLLKNSAN
2060 2070 2080 2090 2100
KDMQNNKEET SLFLAAREGS YETAKVLLDH YANRDITDHM DRLPRDIAQE
2110 2120 2130 2140 2150
RMHHDIVHLL DEYNLVKSPT LHNGPLGATT LSPPICSPNG YMGNMKPSVQ
2160 2170 2180 2190 2200
SKKARKPSIK GNGCKEAKEL KARRKKSQDG KTTLLDSGSS GVLSPVDSLE
2210 2220 2230 2240 2250
STHGYLSDVS SPPLMTSPFQ QSPSMPLNHL TSMPESQLGM NHINMATKQE
2260 2270 2280 2290 2300
MAAGSNRMAF DAMVPRLTHL NASSPNTIMS NGSMHFTVGG APTMNSQCDW
2310 2320 2330 2340 2350
LARLQNGMVQ NQYDPIRNGI QQGNAQQAQA LQHGLMTSLH NGLPATTLSQ
2360 2370 2380 2390 2400
MMTYQAMPNT RLANQPHLMQ AQQMQQQQNL QLHQSMQQQH HNSSTTSTHI
2410 2420 2430 2440 2450
NSPFCSSDIS QTDLQQMSSN NIHSVMPQDT QIFAASLPSN LTQSMTTAQF
2460 2470 2480 2490 2500
LTPPSQHSYS SPMDNTPSHQ LQVPDHPFLT PSPESPDQWS SSSPHSNMSD
2510 2520
WSEGISSPPT SMQPQRTHIP EAFK
Length:2,524
Mass (Da):275,125
Last modified:October 1, 1996 - v3
Checksum:i19556183AFCB7F48
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M33874 mRNA Translation: AAB02039.1
PIRiA35844
RefSeqiNP_001081074.1, NM_001087605.1
UniGeneiXl.1057

Genome annotation databases

GeneIDi394367
KEGGixla:394367

Similar proteinsi

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M33874 mRNA Translation: AAB02039.1
PIRiA35844
RefSeqiNP_001081074.1, NM_001087605.1
UniGeneiXl.1057

3D structure databases

ProteinModelPortaliP21783
SMRiP21783
ModBaseiSearch...
MobiDBiSearch...

Proteomic databases

PRIDEiP21783

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

GeneIDi394367
KEGGixla:394367

Organism-specific databases

CTDi394367
XenbaseiXB-GENE-865261 notch1

Phylogenomic databases

HOVERGENiHBG052650
KOiK02599

Family and domain databases

CDDicd00204 ANK, 2 hits
Gene3Di1.25.40.20, 1 hit
InterProiView protein in InterPro
IPR002110 Ankyrin_rpt
IPR020683 Ankyrin_rpt-contain_dom
IPR036770 Ankyrin_rpt-contain_sf
IPR024600 DUF3454_notch
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_cys_sf
IPR008297 Notch
IPR035993 Notch-like_dom_sf
IPR022362 Notch_1
IPR000800 Notch_dom
IPR010660 Notch_NOD_dom
IPR011656 Notch_NODP_dom
PfamiView protein in Pfam
PF12796 Ank_2, 2 hits
PF11936 DUF3454, 1 hit
PF00008 EGF, 28 hits
PF07645 EGF_CA, 4 hits
PF12661 hEGF, 1 hit
PF06816 NOD, 1 hit
PF07684 NODP, 1 hit
PF00066 Notch, 3 hits
PIRSFiPIRSF002279 Notch, 1 hit
PRINTSiPR01452 LNOTCHREPEAT
PR01984 NOTCH1
SMARTiView protein in SMART
SM00248 ANK, 6 hits
SM01334 DUF3454, 1 hit
SM00181 EGF, 36 hits
SM00179 EGF_CA, 32 hits
SM00004 NL, 3 hits
SM01338 NOD, 1 hit
SM01339 NODP, 1 hit
SUPFAMiSSF48403 SSF48403, 1 hit
SSF57184 SSF57184, 5 hits
SSF90193 SSF90193, 3 hits
PROSITEiView protein in PROSITE
PS50297 ANK_REP_REGION, 1 hit
PS50088 ANK_REPEAT, 4 hits
PS00010 ASX_HYDROXYL, 23 hits
PS00022 EGF_1, 34 hits
PS01186 EGF_2, 29 hits
PS50026 EGF_3, 36 hits
PS01187 EGF_CA, 21 hits
PS50258 LNR, 3 hits
ProtoNetiSearch...

Entry informationi

Entry nameiNOTC1_XENLA
AccessioniPrimary (citable) accession number: P21783
Entry historyiIntegrated into UniProtKB/Swiss-Prot: May 1, 1991
Last sequence update: October 1, 1996
Last modified: November 7, 2018
This is version 146 of the entry and version 3 of the sequence. See complete history.
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Documents

  1. SIMILARITY comments
    Index of protein domains and families
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