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Protein

Neurogenic locus notch homolog protein 1

Gene

NOTCH1

Organism
Cricetulus griseus (Chinese hamster) (Cricetulus barabensis griseus)
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. May enhance HIF1A function by sequestering HIF1AN away from HIF1A (By similarity). Required for the THBS4 function in regulating protective astrogenesis from the subventricular zone (SVZ) niche after injury. 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 bindingi448Calcium 1; via carbonyl oxygenBy similarity1
Metal bindingi451Calcium 1; via amide nitrogenBy similarity1
Metal bindingi468Calcium 2By similarity1
Metal bindingi469Calcium 2; via carbonyl oxygenBy similarity1
Metal bindingi471Calcium 2By similarity1
Metal bindingi485Calcium 2By similarity1
Metal bindingi486Calcium 2; via carbonyl oxygenBy similarity1
Metal bindingi506Calcium 3By similarity1
Metal bindingi507Calcium 3; via carbonyl oxygenBy similarity1
Metal bindingi509Calcium 3By similarity1
Metal bindingi523Calcium 3By similarity1
Metal bindingi524Calcium 3; via carbonyl oxygenBy similarity1
Metal bindingi1473Calcium 4; via carbonyl oxygenPROSITE-ProRule annotation1
Metal bindingi1476Calcium 4PROSITE-ProRule annotation1
Metal bindingi1491Calcium 4PROSITE-ProRule annotation1
Metal bindingi1494Calcium 4PROSITE-ProRule annotation1

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
Cleaved into the following 2 chains:
Gene namesi
Name:NOTCH1
OrganismiCricetulus griseus (Chinese hamster) (Cricetulus barabensis griseus)
Taxonomic identifieri10029 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaMyomorphaMuroideaCricetidaeCricetinaeCricetulus
Proteomesi
  • UP000001075 Componenti: Unassembled WGS sequence

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 domaini37 – 1741ExtracellularSequence analysisAdd BLAST1705
Transmembranei1742 – 1762HelicalSequence analysisAdd BLAST21
Topological domaini1763 – 2527CytoplasmicSequence analysisAdd BLAST765

Keywords - Cellular componenti

Cell membrane, Membrane, Nucleus

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Signal peptidei1 – 36Sequence analysisAdd BLAST36
ChainiPRO_000042401337 – 2527Neurogenic locus notch homolog protein 1Add BLAST2491
ChainiPRO_00004240141727 – 2527Notch 1 extracellular truncationBy similarityAdd BLAST801
ChainiPRO_00004240151760 – 2527Notch 1 intracellular domainBy similarityAdd BLAST768

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Disulfide bondi40 ↔ 53By similarity
Disulfide bondi47 ↔ 62By similarity
Glycosylationi57N-linked (GlcNAc...) asparagineSequence analysis1
Disulfide bondi64 ↔ 73By similarity
Disulfide bondi79 ↔ 90By similarity
Glycosylationi81O-linked (Glc...) serineBy similarity1
Disulfide bondi84 ↔ 103By similarity
Glycosylationi89O-linked (Fuc...) threonineBy similarity1
Disulfide bondi105 ↔ 114By similarity
Disulfide bondi122 ↔ 133By similarity
Disulfide bondi127 ↔ 143By similarity
Glycosylationi132O-linked (Fuc...) threonineBy similarity1
Disulfide bondi145 ↔ 154By similarity
Disulfide bondi160 ↔ 171By similarity
Glycosylationi162O-linked (Glc...) serineBy similarity1
Disulfide bondi165 ↔ 180By similarity
Disulfide bondi182 ↔ 191By similarity
Disulfide bondi198 ↔ 211By similarity
Disulfide bondi205 ↔ 220By similarity
Glycosylationi210O-linked (Fuc...) threonineBy similarity1
Disulfide bondi222 ↔ 231By similarity
Disulfide bondi238 ↔ 249By similarity
Disulfide bondi243 ↔ 259By similarity
Glycosylationi248O-linked (Fuc...) threonine; alternateBy similarity1
Glycosylationi248O-linked (GalNAc...) threonine; alternateBy similarity1
Disulfide bondi261 ↔ 270By similarity
Disulfide bondi277 ↔ 288By similarity
Disulfide bondi282 ↔ 297By similarity
Disulfide bondi299 ↔ 308By similarity
Disulfide bondi315 ↔ 328By similarity
Disulfide bondi322 ↔ 337By similarity
Glycosylationi327O-linked (Fuc...) threonineBy similarity1
Disulfide bondi339 ↔ 348By similarity
Disulfide bondi355 ↔ 366By similarity
Glycosylationi357O-linked (Glc...) serineBy similarity1
Disulfide bondi360 ↔ 375By similarity
Glycosylationi365O-linked (Fuc...) threonineBy similarity1
Disulfide bondi377 ↔ 386By similarity
Disulfide bondi392 ↔ 403By similarity
Glycosylationi394O-linked (Glc...) serineBy similarity1
Disulfide bondi397 ↔ 414By similarity
Disulfide bondi416 ↔ 425By similarity
Disulfide bondi432 ↔ 445By similarity
Disulfide bondi439 ↔ 454By similarity
Glycosylationi451O-linked (Glc...) serineBy similarity1
Disulfide bondi456 ↔ 465By similarity
Disulfide bondi472 ↔ 483By similarity
Glycosylationi474O-linked (Glc...) serineBy similarity1
Disulfide bondi477 ↔ 492By similarity
Glycosylationi482O-linked (Fuc...) threonineBy similarity1
Disulfide bondi494 ↔ 503By similarity
Disulfide bondi510 ↔ 521By similarity
Glycosylationi512O-linked (Glc...) serineBy similarity1
Disulfide bondi515 ↔ 530By similarity
Disulfide bondi532 ↔ 541By similarity
Disulfide bondi548 ↔ 559By similarity
Glycosylationi550O-linked (Glc...) serineBy similarity1
Disulfide bondi553 ↔ 568By similarity
Disulfide bondi570 ↔ 579By similarity
Disulfide bondi586 ↔ 596By similarity
Disulfide bondi591 ↔ 605By similarity
Disulfide bondi607 ↔ 616By similarity
Disulfide bondi623 ↔ 634By similarity
Glycosylationi625O-linked (Glc...) serineBy similarity1
Disulfide bondi628 ↔ 643By similarity
Glycosylationi633O-linked (Fuc...) threonineBy similarity1
Disulfide bondi645 ↔ 654By similarity
Disulfide bondi661 ↔ 671By similarity
Glycosylationi663O-linked (Glc...) serineBy similarity1
Disulfide bondi666 ↔ 680By similarity
Disulfide bondi682 ↔ 691By similarity
Disulfide bondi698 ↔ 709By similarity
Disulfide bondi703 ↔ 718By similarity
Glycosylationi708O-linked (Fuc...) threonineBy similarity1
Disulfide bondi720 ↔ 729By similarity
Disulfide bondi736 ↔ 746By similarity
Glycosylationi738O-linked (Glc...) serineBy similarity1
Disulfide bondi741 ↔ 755By similarity
Disulfide bondi757 ↔ 766By similarity
Disulfide bondi773 ↔ 784By similarity
Glycosylationi775O-linked (Glc...) serineBy similarity1
Disulfide bondi778 ↔ 793By similarity
Glycosylationi783O-linked (Fuc...) threonineBy similarity1
Disulfide bondi795 ↔ 804By similarity
Glycosylationi800O-linked (GlcNAc) serineBy similarity1
Disulfide bondi811 ↔ 822By similarity
Glycosylationi813O-linked (Glc...) serineBy similarity1
Disulfide bondi816 ↔ 831By similarity
Glycosylationi821O-linked (Fuc...) threonineBy similarity1
Disulfide bondi833 ↔ 842By similarity
Disulfide bondi849 ↔ 860By similarity
Glycosylationi904N-linked (GlcNAc...) asparagineSequence analysis1
Glycosylationi916O-linked (GlcNAc) threonineBy similarity1
Glycosylationi937O-linked (Fuc) serineBy similarity1
Glycosylationi967O-linked (Glc...) serineBy similarity1
Glycosylationi975N-linked (GlcNAc...) asparagineSequence analysis1
Glycosylationi1013O-linked (Fuc...) threonineBy similarity1
Glycosylationi1043O-linked (Glc...) serineBy similarity1
Glycosylationi1051O-linked (Fuc...) threonineBy similarity1
Glycosylationi1081O-linked (Glc...) serineBy similarity1
Glycosylationi1175O-linked (Fuc...) threonineBy similarity1
Glycosylationi1195N-linked (GlcNAc...) asparagineSequence analysis1
Glycosylationi1205O-linked (Glc...) serineBy similarity1
Glycosylationi1213O-linked (Fuc...) threonineBy similarity1
Glycosylationi1257N-linked (GlcNAc...) asparagineSequence analysis1
Glycosylationi1289O-linked (Glc...) serineBy similarity1
Glycosylationi1378O-linked (Fuc...) threonineBy similarity1
Glycosylationi1395O-linked (GlcNAc...) threonineBy similarity1
Glycosylationi1418O-linked (Fuc...) threonine; alternateBy similarity1
Glycosylationi1418O-linked (GalNAc...) threonine; alternateBy similarity1
Glycosylationi1505N-linked (GlcNAc...) asparagineSequence analysis1
Glycosylationi1603N-linked (GlcNAc...) asparagineSequence analysis1
Glycosylationi1731O-linked (GalNAc...) threonineBy similarity1
Cross-linki1765Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)By similarity
Modified residuei1867PhosphothreonineBy similarity1
Modified residuei1961(3S)-3-hydroxyasparagine; by HIF1AN; partialBy similarity1
Modified residuei2028(3S)-3-hydroxyasparagine; by HIF1ANBy similarity1

Post-translational modificationi

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
Phosphorylated.By similarity
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). O-glycosylated on the EGF-like domains (PubMed:10734111). Contains both O-linked fucose and O-linked glucose in the EGF-like domains 11, 12 and 13, which are interacting with the residues on DLL4. MFNG-, RFNG- and LFNG-mediated modification of O-fucose residues at specific EGF-like domains results in inhibition of its activation by JAG1 and enhancement of its activation by DLL1 via an increased binding to DLL1 (By similarity).By similarity1 Publication
Ubiquitinated. Undergoes 'Lys-29'-linked polyubiquitination by ITCH; promotes the lysosomal degradation of non-activated internalized NOTCH1. Monoubiquitination at Lys-1765 is required for activation by gamma-secretase cleavage, it promotes interaction with AAK1, which stabilizes it. Deubiquitination by EIF3F is necessary for nuclear import of activated Notch.By similarity
Hydroxylated at Asn-1961 by HIF1AN. Hydroxylated at Asn-2028 by HIF1AN (By similarity). Hydroxylation reduces affinity for HI1AN and may thus indirectly modulate negative regulation of NICD (By similarity).By similarity

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sitei1670 – 1671Cleavage; by furin-like proteaseBy similarity2
Sitei1726 – 1727Cleavage; by ADAM17By similarity2

Keywords - PTMi

Disulfide bond, Glycoprotein, Hydroxylation, Isopeptide bond, Phosphoprotein, Ubl conjugation

Proteomic databases

PRIDEiG3I6Z6

Interactioni

Subunit structurei

Heterodimer of a C-terminal fragment N(TM) and an N-terminal fragment N(EC) which are probably linked by disulfide bonds. Interacts with DNER, DTX1, DTX2 and RBPJ/RBPSUH. Also interacts with MAML1, MAML2 and MAML3 which act as transcriptional coactivators for NOTCH1. Notch 1 intracellular domain interacts with SNW1; the interaction involves multimerized NOTCH1 NICD and is implicated in a formation of an intermediate preactivation complex which associates with DNA-bound CBF-1/RBPJ. The activated membrane-bound form interacts with AAK1 which promotes NOTCH1 stabilization. Forms a trimeric complex with FBXW7 and SGK1. Interacts with HIF1AN. HIF1AN negatively regulates the function of notch intracellular domain (NICD), accelerating myogenic differentiation. Interacts (via NICD) with SNAI1 (via zinc fingers); the interaction induces SNAI1 degradation via MDM2-mediated ubiquitination and inhibits SNAI1-induced cell invasion. Interacts (via NICD) with MDM2A. Interacts (via NICD) with BCL6; the interaction decreases MAML1 recruitment by NOTCH1 NICD on target genes DNA and inhibits NOTCH1 transcractivation activity (By similarity). Interacts with THBS4 (By similarity). Interacts (via the EGF-like repeat region) with NOV (via CTCK domain). Interacts (via EGF-like domains) with DLL4 (via N-terminal DSL and MNNL domains). Interacts with ZMIZ1. Interacts (via NICD domain) with MEGF10 (via the cytoplasmic domain). Interacts with DLL1 and JAG1 (By similarity). Interacts (via NICD domain) with PRAG1 (By similarity). Forms a complex with PRAG1, N1ICD and MAML1, in a MAML1-dependent manner (By similarity).By similarity

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sitei485Interaction with DLL4By similarity1

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Domaini75 – 115EGF-like 1PROSITE-ProRule annotationAdd BLAST41
Domaini118 – 155EGF-like 2PROSITE-ProRule annotationAdd BLAST38
Domaini156 – 192EGF-like 3PROSITE-ProRule annotationAdd BLAST37
Domaini194 – 232EGF-like 4; calcium-bindingPROSITE-ProRule annotationAdd BLAST39
Domaini234 – 271EGF-like 5PROSITE-ProRule annotationAdd BLAST38
Domaini273 – 309EGF-like 6; calcium-bindingPROSITE-ProRule annotationAdd BLAST37
Domaini311 – 349EGF-like 7; calcium-bindingPROSITE-ProRule annotationAdd BLAST39
Domaini351 – 387EGF-like 8; calcium-bindingPROSITE-ProRule annotationAdd BLAST37
Domaini388 – 426EGF-like 9PROSITE-ProRule annotationAdd BLAST39
Domaini428 – 466EGF-like 10; calcium-bindingPROSITE-ProRule annotationAdd BLAST39
Domaini468 – 504EGF-like 11; calcium-bindingPROSITE-ProRule annotationAdd BLAST37
Domaini506 – 542EGF-like 12; calcium-bindingPROSITE-ProRule annotationAdd BLAST37
Domaini544 – 580EGF-like 13; calcium-bindingPROSITE-ProRule annotationAdd BLAST37
Domaini582 – 617EGF-like 14; calcium-bindingPROSITE-ProRule annotationAdd BLAST36
Domaini619 – 655EGF-like 15; calcium-bindingPROSITE-ProRule annotationAdd BLAST37
Domaini657 – 692EGF-like 16; calcium-bindingPROSITE-ProRule annotationAdd BLAST36
Domaini694 – 730EGF-like 17; calcium-bindingPROSITE-ProRule annotationAdd BLAST37
Domaini732 – 767EGF-like 18; calcium-bindingPROSITE-ProRule annotationAdd BLAST36
Domaini769 – 805EGF-like 19PROSITE-ProRule annotationAdd BLAST37
Domaini807 – 843EGF-like 20; calcium-bindingPROSITE-ProRule annotationAdd BLAST37
Domaini845 – 883EGF-like 21PROSITE-ProRule annotationAdd BLAST39
Domaini885 – 921EGF-like 22; calcium-bindingPROSITE-ProRule annotationAdd BLAST37
Domaini923 – 959EGF-like 23PROSITE-ProRule annotationAdd BLAST37
Domaini961 – 997EGF-like 24; calcium-bindingPROSITE-ProRule annotationAdd BLAST37
Domaini999 – 1035EGF-like 25PROSITE-ProRule annotationAdd BLAST37
Domaini1037 – 1073EGF-like 26PROSITE-ProRule annotationAdd BLAST37
Domaini1075 – 1111EGF-like 27PROSITE-ProRule annotationAdd BLAST37
Domaini1113 – 1159EGF-like 28PROSITE-ProRule annotationAdd BLAST47
Domaini1161 – 1197EGF-like 29PROSITE-ProRule annotationAdd BLAST37
Domaini1199 – 1235EGF-like 30; calcium-bindingPROSITE-ProRule annotationAdd BLAST37
Domaini1237 – 1281EGF-like 31; calcium-bindingPROSITE-ProRule annotationAdd BLAST45
Domaini1283 – 1321EGF-like 32PROSITE-ProRule annotationAdd BLAST39
Domaini1323 – 1362EGF-like 33PROSITE-ProRule annotationAdd BLAST40
Domaini1364 – 1400EGF-like 34PROSITE-ProRule annotationAdd BLAST37
Domaini1403 – 1442EGF-like 35PROSITE-ProRule annotationAdd BLAST40
Repeati1465 – 1505LNR 1Add BLAST41
Repeati1506 – 1547LNR 2Add BLAST42
Repeati1548 – 1587LNR 3Add BLAST40
Repeati1933 – 1962ANK 1Add BLAST30
Repeati1966 – 1996ANK 2Add BLAST31
Repeati2000 – 2029ANK 3Add BLAST30
Repeati2033 – 2062ANK 4Add BLAST30
Repeati2066 – 2095ANK 5Add BLAST30

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni436 – 437Interaction with DLL4By similarity2
Regioni464 – 468Interaction with DLL4By similarity5
Regioni1953 – 1961HIF1AN-bindingBy similarity9
Regioni2020 – 2028HIF1AN-bindingBy similarity9

Sequence similaritiesi

Belongs to the NOTCH family.Curated

Keywords - Domaini

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

Phylogenomic databases

InParanoidiG3I6Z6
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, 20 hits
PF07645 EGF_CA, 5 hits
PF12661 hEGF, 3 hits
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, 33 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, 22 hits
PS00022 EGF_1, 35 hits
PS01186 EGF_2, 28 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.

G3I6Z6-1 [UniParc]FASTAAdd to basket
« Hide
        10         20         30         40         50
MGRSDSRAGA LLEGGCEQNI DPRRAAHCHH PRLATSSLRC SQPSGTCLNG
60 70 80 90 100
GRCEVANGTE ACVCSGPFVG QRCQDPNPCL STPCKNAGTC HVVEHGGTVN
110 120 130 140 150
YACSCPLGFS GPLCLTPLDN ACLANPCRNG GTCDLLTLTE YKCRCPPGWS
160 170 180 190 200
GKSCQQADPC ASNPCANGGQ CLPFESSYIC GCPPGFHGPT CRQDVNECSQ
210 220 230 240 250
NPGLCRHGGT CHNEIGSYRC VCRATHTGPH CELPYVPCSP SPCQNGGTCR
260 270 280 290 300
PTGDTTHECA CLPGFAGQNC EENVDDCPGN NCKNGGACVD GVNTYNCRCP
310 320 330 340 350
PEWTGQYCTE DVDECQLMPN ACQNGGTCHN THGGYNCVCV NGWTGEDCSE
360 370 380 390 400
NIDDCASAAC FQGATCHDRV ASFYCECPHG RTGLLCHLND ACISNPCNEG
410 420 430 440 450
SNCDTNPVNG KAICTCPSGY TGPACSQDVD ECALGANPCE HAGKCLNTLG
460 470 480 490 500
SFECQCLQGY TGPRCEIDVN ECISNPCQND ATCLDQIGEF QCICMPGYEG
510 520 530 540 550
VYCEINTDEC ASSPCLHNGH CMDKINEFLC QCPKGFSGHL CQYDVDECAS
560 570 580 590 600
TPCKNGAKCL DGPNTYTCVC TEGYTGTHCE VDIDECDPDP CHYGFCKDGV
610 620 630 640 650
ATFTCLCQPG YTGHHCETNI NECHSQPCRH GGTCQDRDNS YLCLCLKGTT
660 670 680 690 700
GPNCEINLDD CASNPCDSGT CLDKIDGYEC ACEPGYTGSM CNVNIDECAG
710 720 730 740 750
SPCHNGGTCE DGIAGFTCRC PEGYHDPTCL SEVNECNSNP CIHGACRDGL
760 770 780 790 800
NGYKCDCAPG WSGTNCDINN NECESNPCVN GGTCKDMTSG YVCTCREGFS
810 820 830 840 850
GPNCQTNINE CASNPCLNQG TCIDDVAGYK CNCPLPYTGA TCEVVLAPCA
860 870 880 890 900
TSPCKNSGVC KESEDYESFS CVCPTGWQGQ TCEIDINECV KSPCRHGASC
910 920 930 940 950
QNTNGSYRCL CQAGYTGRNC ESDIDDCRPN PCHNGGSCTD GINMAFCDCL
960 970 980 990 1000
PGFQGAFCEE DINECASNPC RNGANCTDCV DSYTCTCPAG FNGIHCENNT
1010 1020 1030 1040 1050
PDCTESSCFN GGTCVDGINS FTCLCPPGFT GSYCQYDVNE CDSRPCLHGG
1060 1070 1080 1090 1100
TCQDSYGTYK CTCPQGYTGL NCQNLVHWCD SAPCKNGGKC WQTNTQYHCE
1110 1120 1130 1140 1150
CRSGWTGFNC DVLSVSCEVA AQKRGIDVTL LCQHGGLCVD EEDKHYCHCQ
1160 1170 1180 1190 1200
AGYTGSYCED EVDECSPNPC QNGATCTDYL GGFSCKCVAG YHGSNCSEEI
1210 1220 1230 1240 1250
NECLSQPCQN GGTCIDLTNT YKCSCPRGTQ GVHCEINVDD CHPHLDPASR
1260 1270 1280 1290 1300
SPKCFNNGTC VDQVGGYSCT CPPGFVGERC EGDINECLSN PCDPRGTQDC
1310 1320 1330 1340 1350
VQRVNDFHCE CRAGHTGRRC ESVINGCRGK PCKNGGVCAV ASNTARGFIC
1360 1370 1380 1390 1400
RCPAGFEGAT CENDARTCGS LRCLNGGTCI SGPRSPTCLC LGSFTGPECQ
1410 1420 1430 1440 1450
FPASSPCVGS NPCYNQGTCE PTSESPFYRC LCPAKFNGLL CHILDYSFTG
1460 1470 1480 1490 1500
GAGRDIPPPQ IEEACELPEC QEDAGNKVCN LQCNNHACGW DGGDCSLNFN
1510 1520 1530 1540 1550
DPWKNCTQSL QCWKYFSDGH CDSQCNSASC LFDGFDCQRT EGQCNPLYDQ
1560 1570 1580 1590 1600
YCKDHFSDGH CDQGCNSAEC DWDGLDCADH VPERLAAGTL VLVVLLPPEQ
1610 1620 1630 1640 1650
LRNNSFHFLR ELSHVLHTNV VFKRDAEGQQ MIFPYYGHEE ELRKHPIKRS
1660 1670 1680 1690 1700
AVGWTTSSLL PSTNGGRQRR ELDPMDIRGS IVYLEIDNRQ CVQSSSQCFQ
1710 1720 1730 1740 1750
SATDVAAFLG ALASLGNLNI PYKIEAVKSE TVEPPLPSQL HLMYLAAAAF
1760 1770 1780 1790 1800
VLLFFVGCGV LLSRKRRRQH GQLWFPEGFK VSEASKKKRR EPLGEDSVGL
1810 1820 1830 1840 1850
KPLKNASDGA LMDDNQNEWG DEDLETKKFR FEEPVVVPDL DDQTDHRQWT
1860 1870 1880 1890 1900
QQHLDAADLR MSAMAPTPPQ GEVDADCMDV NVRGPDGFTP LMIASCSGGG
1910 1920 1930 1940 1950
LETGNSEEEE DAPAVISDFI YQGASLHNQT DRTGETALHL AARYSRSDAA
1960 1970 1980 1990 2000
KRLLEASADA NIQDNMGRTP LHAAVSADAQ GVFQILLRNR ATDLDARMHD
2010 2020 2030 2040 2050
GTTPLILAAR LAVEGMLEDL INSHADVNAV DDLGKSALHW AAAVNNVDAA
2060 2070 2080 2090 2100
VVLLKNGANK DMQNNKEETP LFLAAREGSY ETAKVLLDHF ANRDITDHMD
2110 2120 2130 2140 2150
RLPRDIAQER MHHDIVRLLD EYNLVRSPQL HGTALGGTPT LSPTLCSPNG
2160 2170 2180 2190 2200
YLGNLKSATQ GKKARKPSTK GLACGSKEAK DLKARRKKSQ DGKGCLLDSS
2210 2220 2230 2240 2250
SMLSPVDSLE SPHGYLSDVA SPPLLPSPFQ QSPSMPLSHL PGMPDTHLGI
2260 2270 2280 2290 2300
SHLNVAAKPE MAALAGSSRL AFEPPPPRLP HLPVASSAST VLSTNGSXGE
2310 2320 2330 2340 2350
EEWLAPSQYN PLRPGVASGT LSTQAAGLQH GMMGPLHSSL STNTLSPMIY
2360 2370 2380 2390 2400
QGLPNTRLAT QPHLVQTQQV QPQNLQIQPQ NLQPPSQPHL SVSSAANGHL
2410 2420 2430 2440 2450
GRSFLGGEHS QADVQPLGPS SLPVHTILPQ ESQALPTSLP SSMVPPMTTT
2460 2470 2480 2490 2500
QFLTPPSQHS YSSSPVDNTP SHQLQVPEHP FLTPSPESPD QWSSSSPHSN
2510 2520
ISDWSEGISS PPTSMPSQIT HIPEAFK
Length:2,527
Mass (Da):270,858
Last modified:October 16, 2013 - v2
Checksum:i5E20EC5287850426
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
JH001398 Genomic DNA Translation: EGW12778.1
RefSeqiXP_003510910.1, XM_003510862.3

Genome annotation databases

GeneIDi100761880
KEGGicge:100761880

Similar proteinsi

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
JH001398 Genomic DNA Translation: EGW12778.1
RefSeqiXP_003510910.1, XM_003510862.3

3D structure databases

ModBaseiSearch...
MobiDBiSearch...

Proteomic databases

PRIDEiG3I6Z6

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

GeneIDi100761880
KEGGicge:100761880

Organism-specific databases

CTDi4851

Phylogenomic databases

InParanoidiG3I6Z6
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, 20 hits
PF07645 EGF_CA, 5 hits
PF12661 hEGF, 3 hits
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, 33 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, 22 hits
PS00022 EGF_1, 35 hits
PS01186 EGF_2, 28 hits
PS50026 EGF_3, 36 hits
PS01187 EGF_CA, 21 hits
PS50258 LNR, 3 hits
ProtoNetiSearch...

Entry informationi

Entry nameiNOTC1_CRIGR
AccessioniPrimary (citable) accession number: G3I6Z6
Entry historyiIntegrated into UniProtKB/Swiss-Prot: October 16, 2013
Last sequence update: October 16, 2013
Last modified: September 12, 2018
This is version 43 of the entry and version 2 of the sequence. See complete history.
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. SIMILARITY comments
    Index of protein domains and families
UniProt is an ELIXIR core data resource
Main funding by: National Institutes of Health

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