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P07207 (NOTCH_DROME) Reviewed, UniProtKB/Swiss-Prot

Last modified May 1, 2013. Version 172. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Interactions·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order
to top of pageNames·Attributes·General annotation·Ontologies·Interactions·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Neurogenic locus Notch protein

Cleaved into the following chain:

  1. Processed neurogenic locus Notch protein
Gene names
Name:N
ORF Names:CG3936
OrganismDrosophila melanogaster (Fruit fly) [Reference proteome]
Taxonomic identifier7227 [NCBI]
Taxonomic lineageEukaryota › Metazoa › Ecdysozoa › Arthropoda › Hexapoda › Insecta › Pterygota › Neoptera › Endopterygota › Diptera › Brachycera › Muscomorpha › Ephydroidea › Drosophilidae › Drosophila › Sophophora ›

Protein attributes

Sequence length2703 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Signaling protein, which regulates, with both positive and negative signals, the differentiation of at least central and peripheral nervous system and eye, wing disk, oogenesis, segmental appendages such as antennae and legs, and muscles, through lateral inhibition or induction. Functions as a receptor for membrane-bound ligands Delta and Serrate to regulate cell-fate determination. Upon ligand activation, and releasing from the cell membrane, the Notch intracellular domain (NICD) forms a transcriptional activator complex with Su(H) (Suppressor of hairless) and activates genes of the E(spl) complex. Essential for proper differentiation of ectoderm. Fringe (fng) acts in the Golgi to determine the type of O-linked fucose on the EGF modules in N, altering the ability of N to bind with Delta (Dl). O-fut1 also has a role in modulating the interaction. Rumi acts in the endoplasmic reticulum to glucosylate the EGF modules in N, this is required for correct folding and cleavage of N. Ref.13 Ref.21

Subunit structure

Homomer. Interacts with Su(H) when activated. Interacts with Dx via its ANK repeats. Interacts with Dl via the EGF repeats and the Dl EGF repeats. Interacts with Nedd4 and Su(dx). Interacts with O-fut1; the interaction glycosylates N and transports N to early endosomes. Ref.9 Ref.10 Ref.13 Ref.18 Ref.19 Ref.20 Ref.23

Subcellular location

Cell membrane; Single-pass type I membrane protein. Endosome. Note: Transported to early endosomes by O-fut1. Ref.20

Processed neurogenic locus Notch protein: Nucleus. Note: Upon activation and S3 cleavage, it is released from the cell membrane and enters into the nucleus in conjunction with Su(H). Ref.20

Domain

Crystal structure of the ANK repeat domain shows that there are 7 repeats and the stabilizing C-terminal repeat enhances the protein stability by extending the ankyrin domain. Ref.23

Post-translational modification

Upon binding its ligands such as Delta or Serrate, it is cleaved (S2 cleavage) in its extracellular domain, close to the transmembrane domain. S2 cleavage is probably mediated by Kuz. It is then cleaved (S3 cleavage) downstream of its transmembrane domain, releasing it from the cell membrane. S3 cleavage requires Psn. Ref.11 Ref.12 Ref.15

O-glycosylated. O-fucosylated by O-fut1 in the EGF repeat doamin which inhibits both Serrate/Ser- and Delta/Dl-binding. Ref.17

Ubiquitinated by Nedd4; which promotes ligand-independent endocytosis and proteasomal degradation. May also be ubiquitinated by Su(dx). Ref.18

Sequence similarities

Belongs to the NOTCH family.

Contains 7 ANK repeats.

Contains 36 EGF-like domains.

Contains 3 LNR (Lin/Notch) repeats.

Ontologies

Keywords
   Biological processDifferentiation
Neurogenesis
Notch signaling pathway
Oogenesis
Transcription
Transcription regulation
   Cellular componentCell membrane
Endosome
Membrane
Nucleus
   Coding sequence diversityPolymorphism
   DomainANK repeat
EGF-like domain
Repeat
Signal
Transmembrane
Transmembrane helix
   Molecular functionActivator
Developmental protein
Receptor
   PTMDisulfide bond
Glycoprotein
Phosphoprotein
Ubl conjugation
   Technical term3D-structure
Complete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processMalpighian tubule tip cell differentiation

Inferred from mutant phenotype PubMed 10625542. Source: FlyBase

Notch signaling pathway

Inferred from electronic annotation. Source: UniProtKB-KW

R1/R6 cell differentiation

Inferred from mutant phenotype PubMed 19118542. Source: FlyBase

R3/R4 cell fate commitment

Non-traceable author statement PubMed 12414186. Source: FlyBase

R7 cell differentiation

Inferred from mutant phenotype PubMed 19118542. Source: FlyBase

R8 cell development

Traceable author statement PubMed 10929403. Source: FlyBase

R8 cell fate commitment

Traceable author statement PubMed 10929403. Source: FlyBase

actin filament organization

Inferred from mutant phenotype PubMed 16049109. Source: FlyBase

asymmetric cell division

Traceable author statement PubMed 12593977PubMed 15018932. Source: FlyBase

border follicle cell migration

Inferred from mutant phenotype PubMed 16014514PubMed 17010965. Source: FlyBase

chaeta morphogenesis

Inferred from mutant phenotype PubMed 16168983. Source: FlyBase

compound eye cone cell fate commitment

Traceable author statement PubMed 12419199. Source: FlyBase

compound eye retinal cell programmed cell death

Traceable author statement PubMed 11735386. Source: FlyBase

dorsal appendage formation

Inferred from mutant phenotype PubMed 16223477. Source: FlyBase

dorsal closure

Traceable author statement PubMed 12147138. Source: FlyBase

dorsal/ventral lineage restriction, imaginal disc

Traceable author statement PubMed 11253649. Source: FlyBase

ectoderm development

Traceable author statement PubMed 1913825. Source: FlyBase

embryonic crystal cell differentiation

Traceable author statement PubMed 14602069. Source: FlyBase

epithelial cell proliferation involved in Malpighian tubule morphogenesis

Inferred from mutant phenotype PubMed 11861476. Source: FlyBase

epithelial cell type specification, open tracheal system

Inferred from mutant phenotype PubMed 16760977. Source: FlyBase

eye-antennal disc development

Inferred from mutant phenotype PubMed 18639538. Source: FlyBase

foregut morphogenesis

Inferred from mutant phenotype PubMed 14975725. Source: FlyBase

formation of a compartment boundary

Inferred from mutant phenotype PubMed 21795284. Source: FlyBase

germ-line stem cell maintenance

Inferred from mutant phenotype PubMed 17287246. Source: FlyBase

germarium-derived female germ-line cyst encapsulation

Traceable author statement PubMed 11591336. Source: FlyBase

glial cell fate determination

Inferred from mutant phenotype PubMed 11262238PubMed 11262244PubMed 11973271. Source: FlyBase

glial cell migration

Inferred from mutant phenotype PubMed 17157832. Source: FlyBase

hemocyte proliferation

Inferred from mutant phenotype PubMed 12569125. Source: FlyBase

heterophilic cell-cell adhesion

Inferred from mutant phenotype PubMed 15611340. Source: FlyBase

imaginal disc growth

Traceable author statement PubMed 10679387. Source: FlyBase

imaginal disc-derived leg joint morphogenesis

Inferred from mutant phenotype PubMed 21527259. Source: FlyBase

imaginal disc-derived male genitalia morphogenesis

Inferred from mutant phenotype PubMed 21729695. Source: FlyBase

imaginal disc-derived wing margin morphogenesis

Inferred from mutant phenotype PubMed 12897132PubMed 15452147PubMed 16326033PubMed 19027066. Source: FlyBase

imaginal disc-derived wing vein specification

Inferred from mutant phenotype PubMed 15452147. Source: FlyBase

lamellocyte differentiation

Inferred from mutant phenotype PubMed 12445385. Source: FlyBase

lateral inhibition

Inferred from mutant phenotype PubMed 19363474. Source: FlyBase

long-term memory

Inferred from mutant phenotype PubMed 15220476. Source: FlyBase

lymph gland crystal cell differentiation

Traceable author statement PubMed 14734104. Source: FlyBase

mesoderm development

Inferred from mutant phenotype PubMed 1913825. Source: FlyBase

motor neuron axon guidance

Inferred from mutant phenotype PubMed 21246649. Source: FlyBase

muscle cell fate determination

Inferred from mutant phenotype PubMed 12756185. Source: FlyBase

negative regulation of JNK cascade

Non-traceable author statement PubMed 12147138. Source: FlyBase

negative regulation of compound eye photoreceptor development

Inferred from mutant phenotype PubMed 16039641. Source: FlyBase

negative regulation of fusion cell fate specification

Traceable author statement PubMed 10684581. Source: FlyBase

negative regulation of neurogenesis

Inferred from mutant phenotype PubMed 15452147. Source: FlyBase

negative regulation of terminal cell fate specification, open tracheal system

Traceable author statement PubMed 10684581. Source: FlyBase

negative regulation of transcription from RNA polymerase II promoter

Traceable author statement PubMed 10929403. Source: FlyBase

neuroblast fate determination

Inferred from direct assay PubMed 19782677. Source: FlyBase

oocyte anterior/posterior axis specification

Traceable author statement PubMed 11591336PubMed 12879448. Source: FlyBase

oocyte localization involved in germarium-derived egg chamber formation

Inferred from mutant phenotype PubMed 14536057. Source: FlyBase

ovarian follicle cell stalk formation

Inferred from mutant phenotype PubMed 14536057PubMed 9012507. Source: FlyBase

peripheral nervous system development

Inferred from mutant phenotype PubMed 11262238. Source: FlyBase

positive regulation of Notch signaling pathway

Inferred from mutant phenotype PubMed 15611340. Source: FlyBase

positive regulation of S phase of mitotic cell cycle

Inferred from mutant phenotype PubMed 15809036. Source: FlyBase

positive regulation of cell proliferation

Inferred from mutant phenotype PubMed 16039641. Source: FlyBase

positive regulation of transcription from RNA polymerase II promoter

Inferred from direct assay PubMed 12556495. Source: FlyBase

regulation of R8 cell spacing in compound eye

Non-traceable author statement PubMed 11880339. Source: FlyBase

regulation of cardioblast cell fate specification

Inferred from mutant phenotype PubMed 12756185. Source: FlyBase

regulation of crystal cell differentiation

Traceable author statement PubMed 12732186. Source: FlyBase

regulation of filopodium assembly

Inferred from mutant phenotype PubMed 21447553. Source: FlyBase

regulation of growth

Inferred from mutant phenotype PubMed 14592975. Source: FlyBase

response to symbiont

Inferred from mutant phenotype PubMed 12445385. Source: FlyBase

second mitotic wave involved in compound eye morphogenesis

Non-traceable author statement PubMed 11735386. Source: FlyBase

skeletal muscle tissue development

Inferred from mutant phenotype PubMed 10859168. Source: FlyBase

transcription, DNA-dependent

Inferred from electronic annotation. Source: UniProtKB-KW

ventral cord development

Non-traceable author statement PubMed 12593977. Source: FlyBase

wing disc dorsal/ventral pattern formation

Inferred from mutant phenotype PubMed 16049109. Source: FlyBase

wing disc proximal/distal pattern formation

Traceable author statement PubMed 12717815. Source: FlyBase

   Cellular_componentGolgi lumen

Traceable author statement. Source: Reactome

adherens junction

Inferred from direct assay PubMed 17212657. Source: FlyBase

cell surface

Inferred from direct assay PubMed 21771811. Source: FlyBase

cytosol

Traceable author statement. Source: Reactome

endoplasmic reticulum lumen

Traceable author statement. Source: Reactome

endosome

Inferred from electronic annotation. Source: UniProtKB-SubCell

integral to membrane

Traceable author statement PubMed 10929403. Source: FlyBase

nucleoplasm

Traceable author statement. Source: Reactome

protein complex

Inferred from physical interaction PubMed 17535912. Source: FlyBase

subapical complex

Inferred from direct assay PubMed 17212657. Source: FlyBase

   Molecular_functioncalcium ion binding

Inferred from electronic annotation. Source: InterPro

chromatin binding

Inferred from direct assay PubMed 16763555. Source: FlyBase

transmembrane signaling receptor activity

Non-traceable author statement PubMed 11880339. Source: FlyBase

Complete GO annotation...

Binary interactions

With

Entry

#Exp.

IntAct

Notes

cnoQ242793EBI-103438,EBI-868783
DlP100412EBI-103438,EBI-115346

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Signal peptide1 – 5252 Potential
Chain53 – 27032651Neurogenic locus Notch protein
PRO_0000007673
Chain? – 2703Processed neurogenic locus Notch proteinPRO_0000296234

Regions

Topological domain53 – 17451693Extracellular Potential
Transmembrane1746 – 176621Helical; Potential
Topological domain1767 – 2703937Cytoplasmic Potential
Domain58 – 9538EGF-like 1
Domain96 – 13641EGF-like 2
Domain139 – 17638EGF-like 3
Domain177 – 21539EGF-like 4
Domain217 – 25337EGF-like 5; calcium-binding Potential
Domain255 – 29137EGF-like 6
Domain293 – 32937EGF-like 7; calcium-binding Potential
Domain331 – 37040EGF-like 8; calcium-binding Potential
Domain372 – 40837EGF-like 9; calcium-binding Potential
Domain409 – 44739EGF-like 10
Domain449 – 48638EGF-like 11; calcium-binding Potential
Domain488 – 52437EGF-like 12; calcium-binding Potential
Domain526 – 56237EGF-like 13; calcium-binding Potential
Domain564 – 60037EGF-like 14; calcium-binding Potential
Domain602 – 63736EGF-like 15; calcium-binding Potential
Domain639 – 67537EGF-like 16; calcium-binding Potential
Domain677 – 71337EGF-like 17; calcium-binding Potential
Domain715 – 75137EGF-like 18; calcium-binding Potential
Domain753 – 78937EGF-like 19; calcium-binding Potential
Domain791 – 82737EGF-like 20; calcium-binding Potential
Domain829 – 86537EGF-like 21; calcium-binding Potential
Domain867 – 90539EGF-like 22
Domain907 – 94438EGF-like 23; calcium-binding Potential
Domain946 – 98237EGF-like 24; calcium-binding Potential
Domain984 – 102037EGF-like 25
Domain1022 – 105837EGF-like 26; calcium-binding Potential
Domain1060 – 109637EGF-like 27
Domain1098 – 113437EGF-like 28
Domain1136 – 118146EGF-like 29
Domain1183 – 121937EGF-like 30; calcium-binding Potential
Domain1221 – 125737EGF-like 31; calcium-binding Potential
Domain1259 – 129537EGF-like 32; calcium-binding Potential
Domain1297 – 133539EGF-like 33
Domain1337 – 137337EGF-like 34
Domain1375 – 141238EGF-like 35
Domain1415 – 145137EGF-like 36
Repeat1482 – 152140LNR 1
Repeat1522 – 155736LNR 2
Repeat1559 – 159941LNR 3
Repeat1901 – 194545ANK 1
Repeat1950 – 197930ANK 2
Repeat1983 – 201331ANK 3
Repeat2017 – 204630ANK 4
Repeat2050 – 207930ANK 5
Repeat2083 – 211230ANK 6
Repeat2116 – 213924ANK 7
Region2325 – 23284Interaction with Nedd4
Compositional bias2486 – 249813Poly-Gly
Compositional bias2538 – 256831Poly-Gln (OPA repeat)
Compositional bias2664 – 26674Poly-Ser

Amino acid modifications

Modified residue24471Phosphoserine Ref.22
Glycosylation3221N-linked (GlcNAc...) Potential
Glycosylation3711N-linked (GlcNAc...) Potential
Glycosylation4301N-linked (GlcNAc...) Potential
Glycosylation4751N-linked (GlcNAc...) Potential
Glycosylation10451N-linked (GlcNAc...) Potential
Glycosylation11571N-linked (GlcNAc...) Potential
Glycosylation12421N-linked (GlcNAc...) Potential
Glycosylation12711N-linked (GlcNAc...) Potential
Glycosylation15211N-linked (GlcNAc...) Potential
Glycosylation15941N-linked (GlcNAc...) Potential
Glycosylation16271N-linked (GlcNAc...) Potential
Disulfide bond62 ↔ 73 By similarity
Disulfide bond67 ↔ 83 By similarity
Disulfide bond85 ↔ 94 By similarity
Disulfide bond100 ↔ 111 By similarity
Disulfide bond105 ↔ 124 By similarity
Disulfide bond126 ↔ 135 By similarity
Disulfide bond143 ↔ 154 By similarity
Disulfide bond148 ↔ 164 By similarity
Disulfide bond166 ↔ 175 By similarity
Disulfide bond181 ↔ 192 By similarity
Disulfide bond186 ↔ 203 By similarity
Disulfide bond205 ↔ 214 By similarity
Disulfide bond221 ↔ 232 By similarity
Disulfide bond226 ↔ 241 By similarity
Disulfide bond243 ↔ 252 By similarity
Disulfide bond259 ↔ 270 By similarity
Disulfide bond264 ↔ 279 By similarity
Disulfide bond281 ↔ 290 By similarity
Disulfide bond297 ↔ 308 By similarity
Disulfide bond302 ↔ 317 By similarity
Disulfide bond319 ↔ 328 By similarity
Disulfide bond335 ↔ 349 By similarity
Disulfide bond343 ↔ 358 By similarity
Disulfide bond360 ↔ 369 By similarity
Disulfide bond376 ↔ 387 By similarity
Disulfide bond381 ↔ 396 By similarity
Disulfide bond398 ↔ 407 By similarity
Disulfide bond413 ↔ 424 By similarity
Disulfide bond418 ↔ 435 By similarity
Disulfide bond437 ↔ 446 By similarity
Disulfide bond453 ↔ 465 By similarity
Disulfide bond459 ↔ 474 By similarity
Disulfide bond476 ↔ 485 By similarity
Disulfide bond492 ↔ 503 By similarity
Disulfide bond497 ↔ 512 By similarity
Disulfide bond514 ↔ 523 By similarity
Disulfide bond530 ↔ 541 By similarity
Disulfide bond535 ↔ 550 By similarity
Disulfide bond552 ↔ 561 By similarity
Disulfide bond568 ↔ 579 By similarity
Disulfide bond573 ↔ 588 By similarity
Disulfide bond590 ↔ 599 By similarity
Disulfide bond606 ↔ 616 By similarity
Disulfide bond611 ↔ 625 By similarity
Disulfide bond627 ↔ 636 By similarity
Disulfide bond643 ↔ 654 By similarity
Disulfide bond648 ↔ 663 By similarity
Disulfide bond665 ↔ 674 By similarity
Disulfide bond681 ↔ 692 By similarity
Disulfide bond686 ↔ 701 By similarity
Disulfide bond703 ↔ 712 By similarity
Disulfide bond719 ↔ 730 By similarity
Disulfide bond724 ↔ 739 By similarity
Disulfide bond741 ↔ 750 By similarity
Disulfide bond757 ↔ 768 By similarity
Disulfide bond762 ↔ 777 By similarity
Disulfide bond779 ↔ 788 By similarity
Disulfide bond795 ↔ 806 By similarity
Disulfide bond800 ↔ 815 By similarity
Disulfide bond817 ↔ 826 By similarity
Disulfide bond833 ↔ 844 By similarity
Disulfide bond838 ↔ 853 By similarity
Disulfide bond855 ↔ 864 By similarity
Disulfide bond871 ↔ 882 By similarity
Disulfide bond876 ↔ 893 By similarity
Disulfide bond895 ↔ 904 By similarity
Disulfide bond911 ↔ 923 By similarity
Disulfide bond917 ↔ 932 By similarity
Disulfide bond934 ↔ 943 By similarity
Disulfide bond950 ↔ 961 By similarity
Disulfide bond955 ↔ 970 By similarity
Disulfide bond972 ↔ 981 By similarity
Disulfide bond988 ↔ 999 By similarity
Disulfide bond993 ↔ 1008 By similarity
Disulfide bond1010 ↔ 1019 By similarity
Disulfide bond1026 ↔ 1037 By similarity
Disulfide bond1031 ↔ 1046 By similarity
Disulfide bond1048 ↔ 1057 By similarity
Disulfide bond1064 ↔ 1075 By similarity
Disulfide bond1069 ↔ 1084 By similarity
Disulfide bond1086 ↔ 1095 By similarity
Disulfide bond1102 ↔ 1113 By similarity
Disulfide bond1107 ↔ 1122 By similarity
Disulfide bond1124 ↔ 1133 By similarity
Disulfide bond1140 ↔ 1160 By similarity
Disulfide bond1155 ↔ 1169 By similarity
Disulfide bond1171 ↔ 1180 By similarity
Disulfide bond1187 ↔ 1198 By similarity
Disulfide bond1192 ↔ 1207 By similarity
Disulfide bond1209 ↔ 1218 By similarity
Disulfide bond1225 ↔ 1236 By similarity
Disulfide bond1230 ↔ 1245 By similarity
Disulfide bond1247 ↔ 1256 By similarity
Disulfide bond1263 ↔ 1274 By similarity
Disulfide bond1268 ↔ 1283 By similarity
Disulfide bond1285 ↔ 1294 By similarity
Disulfide bond1301 ↔ 1314 By similarity
Disulfide bond1306 ↔ 1323 By similarity
Disulfide bond1325 ↔ 1334 By similarity
Disulfide bond1341 ↔ 1352 By similarity
Disulfide bond1346 ↔ 1361 By similarity
Disulfide bond1363 ↔ 1372 By similarity
Disulfide bond1379 ↔ 1389 By similarity
Disulfide bond1384 ↔ 1400 By similarity
Disulfide bond1402 ↔ 1411 By similarity
Disulfide bond1419 ↔ 1430 By similarity
Disulfide bond1424 ↔ 1439 By similarity
Disulfide bond1441 ↔ 1450 By similarity
Disulfide bond1482 ↔ 1505 By similarity
Disulfide bond1487 ↔ 1500 By similarity
Disulfide bond1496 ↔ 1512 By similarity
Disulfide bond1522 ↔ 1545 By similarity
Disulfide bond1527 ↔ 1540 By similarity
Disulfide bond1536 ↔ 1552 By similarity
Disulfide bond1559 ↔ 1585 By similarity
Disulfide bond1567 ↔ 1580 By similarity
Disulfide bond1576 ↔ 1592 By similarity

Natural variations

Natural variant5781I → T.
Natural variant20441I → R.
Natural variant22651A → V.
Natural variant24071H → R.
Natural variant24451R → L.
Natural variant25681Q → QQQQQ.

Experimental info

Mutagenesis7391C → Y in mcd5; induces loss of microchaetae sensory precursors.
Mutagenesis20601A → V in su42c; deltex-like mutation that induces outstreched wings and variability-fused ocelli.
Mutagenesis23281Y → F: Abolishes interaction with Nedd4 and reduces ubiquitination. Ref.18
Sequence conflict91R → G in CAB37610. Ref.5
Sequence conflict841A → G in CAB37610. Ref.5
Sequence conflict1031M → I in AAB59220. Ref.1
Sequence conflict1191R → H in AAA28725. Ref.2
Sequence conflict2311T → I in AAB59220. Ref.1
Sequence conflict2401Q → R in CAB37610. Ref.5
Sequence conflict2671G → A in AAB59220. Ref.1
Sequence conflict15611S → T in AAB59220. Ref.1
Sequence conflict15611S → T in AAA28725. Ref.2
Sequence conflict22571G → S in AAA28725. Ref.2
Sequence conflict25771A → E in AAA74496. Ref.7

Secondary structure

1 ............................. 2703
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
P07207 [UniParc].

Last modified November 2, 2001. Version 3.
Checksum: 0EAE23F426FECD7B

FASTA2,703288,853
        10         20         30         40         50         60 
MQSQRSRRRS RAPNTWICFW INKMHAVASL PASLPLLLLT LAFANLPNTV RGTDTALVAA 

        70         80         90        100        110        120 
SCTSVGCQNG GTCVTQLNGK TYCACDSHYV GDYCEHRNPC NSMRCQNGGT CQVTFRNGRP 

       130        140        150        160        170        180 
GISCKCPLGF DESLCEIAVP NACDHVTCLN GGTCQLKTLE EYTCACANGY TGERCETKNL 

       190        200        210        220        230        240 
CASSPCRNGA TCTALAGSSS FTCSCPPGFT GDTCSYDIEE CQSNPCKYGG TCVNTHGSYQ 

       250        260        270        280        290        300 
CMCPTGYTGK DCDTKYKPCS PSPCQNGGIC RSNGLSYECK CPKGFEGKNC EQNYDDCLGH 

       310        320        330        340        350        360 
LCQNGGTCID GISDYTCRCP PNFTGRFCQD DVDECAQRDH PVCQNGATCT NTHGSYSCIC 

       370        380        390        400        410        420 
VNGWAGLDCS NNTDDCKQAA CFYGATCIDG VGSFYCQCTK GKTGLLCHLD DACTSNPCHA 

       430        440        450        460        470        480 
DAICDTSPIN GSYACSCATG YKGVDCSEDI DECDQGSPCE HNGICVNTPG SYRCNCSQGF 

       490        500        510        520        530        540 
TGPRCETNIN ECESHPCQNE GSCLDDPGTF RCVCMPGFTG TQCEIDIDEC QSNPCLNDGT 

       550        560        570        580        590        600 
CHDKINGFKC SCALGFTGAR CQINIDDCQS QPCRNRGICH DSIAGYSCEC PPGYTGTSCE 

       610        620        630        640        650        660 
ININDCDSNP CHRGKCIDDV NSFKCLCDPG YTGYICQKQI NECESNPCQF DGHCQDRVGS 

       670        680        690        700        710        720 
YYCQCQAGTS GKNCEVNVNE CHSNPCNNGA TCIDGINSYK CQCVPGFTGQ HCEKNVDECI 

       730        740        750        760        770        780 
SSPCANNGVC IDQVNGYKCE CPRGFYDAHC LSDVDECASN PCVNEGRCED GINEFICHCP 

       790        800        810        820        830        840 
PGYTGKRCEL DIDECSSNPC QHGGTCYDKL NAFSCQCMPG YTGQKCETNI DDCVTNPCGN 

       850        860        870        880        890        900 
GGTCIDKVNG YKCVCKVPFT GRDCESKMDP CASNRCKNEA KCTPSSNFLD FSCTCKLGYT 

       910        920        930        940        950        960 
GRYCDEDIDE CSLSSPCRNG ASCLNVPGSY RCLCTKGYEG RDCAINTDDC ASFPCQNGGT 

       970        980        990       1000       1010       1020 
CLDGIGDYSC LCVDGFDGKH CETDINECLS QPCQNGATCS QYVNSYTCTC PLGFSGINCQ 

      1030       1040       1050       1060       1070       1080 
TNDEDCTESS CLNGGSCIDG INGYNCSCLA GYSGANCQYK LNKCDSNPCL NGATCHEQNN 

      1090       1100       1110       1120       1130       1140 
EYTCHCPSGF TGKQCSEYVD WCGQSPCENG ATCSQMKHQF SCKCSAGWTG KLCDVQTISC 

      1150       1160       1170       1180       1190       1200 
QDAADRKGLS LRQLCNNGTC KDYGNSHVCY CSQGYAGSYC QKEIDECQSQ PCQNGGTCRD 

      1210       1220       1230       1240       1250       1260 
LIGAYECQCR QGFQGQNCEL NIDDCAPNPC QNGGTCHDRV MNFSCSCPPG TMGIICEINK 

      1270       1280       1290       1300       1310       1320 
DDCKPGACHN NGSCIDRVGG FECVCQPGFV GARCEGDINE CLSNPCSNAG TLDCVQLVNN 

      1330       1340       1350       1360       1370       1380 
YHCNCRPGHM GRHCEHKVDF CAQSPCQNGG NCNIRQSGHH CICNNGFYGK NCELSGQDCD 

      1390       1400       1410       1420       1430       1440 
SNPCRVGNCV VADEGFGYRC ECPRGTLGEH CEIDTLDECS PNPCAQGAAC EDLLGDYECL 

      1450       1460       1470       1480       1490       1500 
CPSKWKGKRC DIYDANYPGW NGGSGSGNDR YAADLEQQRA MCDKRGCTEK QGNGICDSDC 

      1510       1520       1530       1540       1550       1560 
NTYACNFDGN DCSLGINPWA NCTANECWNK FKNGKCNEEC NNAACHYDGH DCERKLKSCD 

      1570       1580       1590       1600       1610       1620 
SLFDAYCQKH YGDGFCDYGC NNAECSWDGL DCENKTQSPV LAEGAMSVVM LMNVEAFREI 

      1630       1640       1650       1660       1670       1680 
QAQFLRNMSH MLRTTVRLKK DALGHDIIIN WKDNVRVPEI EDTDFARKNK ILYTQQVHQT 

      1690       1700       1710       1720       1730       1740 
GIQIYLEIDN RKCTECFTHA VEAAEFLAAT AAKHQLRNDF QIHSVRGIKN PGDEDNGEPP 

      1750       1760       1770       1780       1790       1800 
ANVKYVITGI ILVIIALAFF GMVLSTQRKR AHGVTWFPEG FRAPAAVMSR RRRDPHGQEM 

      1810       1820       1830       1840       1850       1860 
RNLNKQVAMQ SQGVGQPGAH WSDDESDMPL PKRQRSDPVS GVGLGNNGGY ASDHTMVSEY 

      1870       1880       1890       1900       1910       1920 
EEADQRVWSQ AHLDVVDVRA IMTPPAHQDG GKHDVDARGP CGLTPLMIAA VRGGGLDTGE 

      1930       1940       1950       1960       1970       1980 
DIENNEDSTA QVISDLLAQG AELNATMDKT GETSLHLAAR FARADAAKRL LDAGADANCQ 

      1990       2000       2010       2020       2030       2040 
DNTGRTPLHA AVAADAMGVF QILLRNRATN LNARMHDGTT PLILAARLAI EGMVEDLITA 

      2050       2060       2070       2080       2090       2100 
DADINAADNS GKTALHWAAA VNNTEAVNIL LMHHANRDAQ DDKDETPLFL AAREGSYEAC 

      2110       2120       2130       2140       2150       2160 
KALLDNFANR EITDHMDRLP RDVASERLHH DIVRLLDEHV PRSPQMLSMT PQAMIGSPPP 

      2170       2180       2190       2200       2210       2220 
GQQQPQLITQ PTVISAGNGG NNGNGNASGK QSNQTAKQKA AKKAKLIEGS PDNGLDATGS 

      2230       2240       2250       2260       2270       2280 
LRRKASSKKT SAASKKAANL NGLNPGQLTG GVSGVPGVPP TNSAAQAAAA AAAAVAAMSH 

      2290       2300       2310       2320       2330       2340 
ELEGSPVGVG MGGNLPSPYD TSSMYSNAMA APLANGNPNT GAKQPPSYED CIKNAQSMQS 

      2350       2360       2370       2380       2390       2400 
LQGNGLDMIK LDNYAYSMGS PFQQELLNGQ GLGMNGNGQR NGVGPGVLPG GLCGMGGLSG 

      2410       2420       2430       2440       2450       2460 
AGNGNSHEQG LSPPYSNQSP PHSVQSSLAL SPHAYLGSPS PAKSRPSLPT SPTHIQAMRH 

      2470       2480       2490       2500       2510       2520 
ATQQKQFGGS NLNSLLGGAN GGGVVGGGGG GGGGVGQGPQ NSPVSLGIIS PTGSDMGIML 

      2530       2540       2550       2560       2570       2580 
APPQSSKNSA IMQTISPQQQ QQQQQQQQQQ HQQQQQQQQQ QQQQQQQQLG GLEFGSAGLD 

      2590       2600       2610       2620       2630       2640 
LNGFCGSPDS FHSGQMNPPS IQSSMSGSSP STNMLSPSSQ HNQQAFYQYL TPSSQHSGGH 

      2650       2660       2670       2680       2690       2700 
TPQHLVQTLD SYPTPSPESP GHWSSSSPRS NSDWSEGVQS PAANNLYISG GHQANKGSEA 


IYI

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References

« Hide 'large scale' references
[1]"Nucleotide sequence from the neurogenic locus notch implies a gene product that shares homology with proteins containing EGF-like repeats."
Wharton K.A., Johansen K.M., Xu T., Artavanis-Tsakonas S.
Cell 43:567-581(1985) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
Strain: Oregon-R.
Tissue: Embryo.
[2]"Sequence of the notch locus of Drosophila melanogaster: relationship of the encoded protein to mammalian clotting and growth factors."
Kidd S., Kelley M.R., Young M.W.
Mol. Cell. Biol. 6:3094-3108(1986) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
Strain: Canton-S and Oregon-R.
Tissue: Embryo.
[3]"The genome sequence of Drosophila melanogaster."
Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D., Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F., George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N., Sutton G.G., Wortman J.R., Yandell M.D. expand/collapse author list , Zhang Q., Chen L.X., Brandon R.C., Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D., Wan K.H., Doyle C., Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G., Abril J.F., Agbayani A., An H.-J., Andrews-Pfannkoch C., Baldwin D., Ballew R.M., Basu A., Baxendale J., Bayraktaroglu L., Beasley E.M., Beeson K.Y., Benos P.V., Berman B.P., Bhandari D., Bolshakov S., Borkova D., Botchan M.R., Bouck J., Brokstein P., Brottier P., Burtis K.C., Busam D.A., Butler H., Cadieu E., Center A., Chandra I., Cherry J.M., Cawley S., Dahlke C., Davenport L.B., Davies P., de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I., Dietz S.M., Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C., Dunn P., Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S., Fleischmann W., Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M., Glasser K., Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M., Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J., Hostin D., Houston K.A., Howland T.J., Wei M.-H., Ibegwam C., Jalali M., Kalush F., Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A., Kimmel B.E., Kodira C.D., Kraft C.L., Kravitz S., Kulp D., Lai Z., Lasko P., Lei Y., Levitsky A.A., Li J.H., Li Z., Liang Y., Lin X., Liu X., Mattei B., McIntosh T.C., McLeod M.P., McPherson D., Merkulov G., Milshina N.V., Mobarry C., Morris J., Moshrefi A., Mount S.M., Moy M., Murphy B., Murphy L., Muzny D.M., Nelson D.L., Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R., Pacleb J.M., Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V., Reese M.G., Reinert K., Remington K., Saunders R.D.C., Scheeler F., Shen H., Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T.J., Spier E., Spradling A.C., Stapleton M., Strong R., Sun E., Svirskas R., Tector C., Turner R., Venter E., Wang A.H., Wang X., Wang Z.-Y., Wassarman D.A., Weinstock G.M., Weissenbach J., Williams S.M., Woodage T., Worley K.C., Wu D., Yang S., Yao Q.A., Ye J., Yeh R.-F., Zaveri J.S., Zhan M., Zhang G., Zhao Q., Zheng L., Zheng X.H., Zhong F.N., Zhong W., Zhou X., Zhu S.C., Zhu X., Smith H.O., Gibbs R.A., Myers E.W., Rubin G.M., Venter J.C.
Science 287:2185-2195(2000) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: Berkeley.
[4]"Annotation of the Drosophila melanogaster euchromatic genome: a systematic review."
Misra S., Crosby M.A., Mungall C.J., Matthews B.B., Campbell K.S., Hradecky P., Huang Y., Kaminker J.S., Millburn G.H., Prochnik S.E., Smith C.D., Tupy J.L., Whitfield E.J., Bayraktaroglu L., Berman B.P., Bettencourt B.R., Celniker S.E., de Grey A.D.N.J. expand/collapse author list , Drysdale R.A., Harris N.L., Richter J., Russo S., Schroeder A.J., Shu S.Q., Stapleton M., Yamada C., Ashburner M., Gelbart W.M., Rubin G.M., Lewis S.E.
Genome Biol. 3:RESEARCH0083.1-RESEARCH0083.22(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: GENOME REANNOTATION.
Strain: Berkeley.
[5]"From sequence to chromosome: the tip of the X chromosome of D. melanogaster."
Benos P.V., Gatt M.K., Ashburner M., Murphy L., Harris D., Barrell B.G., Ferraz C., Vidal S., Brun C., Demailles J., Cadieu E., Dreano S., Gloux S., Lelaure V., Mottier S., Galibert F., Borkova D., Minana B. expand/collapse author list , Kafatos F.C., Louis C., Siden-Kiamos I., Bolshakov S., Papagiannakis G., Spanos L., Cox S., Madueno E., de Pablos B., Modolell J., Peter A., Schoettler P., Werner M., Mourkioti F., Beinert N., Dowe G., Schaefer U., Jaeckle H., Bucheton A., Callister D.M., Campbell L.A., Darlamitsou A., Henderson N.S., McMillan P.J., Salles C., Tait E.A., Valenti P., Saunders R.D.C., Glover D.M.
Science 287:2220-2222(2000) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: Oregon-R.
[6]"Restriction of P-element insertions at the Notch locus of Drosophila melanogaster."
Kelley M.R., Kidd S., Berg R.L., Young M.W.
Mol. Cell. Biol. 7:1545-1548(1987) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-8.
[7]"opa: a novel family of transcribed repeats shared by the Notch locus and other developmentally regulated loci in D. melanogaster."
Wharton K.A., Yedvobnick B., Finnerty V.G., Artavanis-Tsakonas S.
Cell 40:55-62(1985) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 2505-2611.
Strain: Oregon-R.
Tissue: Embryo.
[8]"Hypervariability of simple sequences as a general source for polymorphic DNA markers."
Tautz D.
Nucleic Acids Res. 17:6463-6471(1989) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 2505-2604.
[9]"Cytosolic interaction between deltex and Notch ankyrin repeats implicates deltex in the Notch signaling pathway."
Diederich R.J., Matsuno K., Hing H., Artavanis-Tsakonas S.
Development 120:473-481(1994) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH DX, MUTANT SU42C.
[10]"Deltex acts as a positive regulator of Notch signaling through interactions with the Notch ankyrin repeats."
Matsuno K., Diederich R.J., Go M.J., Blaumueller C.M., Artavanis-Tsakonas S.
Development 121:2633-2644(1995) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH DX.
[11]"Presenilin is required for activity and nuclear access of Notch in Drosophila."
Struhl G., Greenwald I.
Nature 398:522-525(1999) [PubMed] [Europe PMC] [Abstract]
Cited for: S3 CLEAVAGE BY PSN.
[12]"Neurogenic phenotypes and altered Notch processing in Drosophila Presenilin mutants."
Ye Y., Lukinova N., Fortini M.E.
Nature 398:525-529(1999) [PubMed] [Europe PMC] [Abstract]
Cited for: S3 CLEAVAGE BY PSN.
[13]"Glycosyltransferase activity of Fringe modulates Notch-Delta interactions."
Bruckner K., Perez L., Clausen H., Cohen S.
Nature 406:411-415(2000) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, INTERACTION WITH DL.
[14]"Novel Notch alleles reveal a Deltex-dependent pathway repressing neural fate."
Ramain P., Khechumian K., Seugnet L., Arbogast N., Ackermann C., Heitzler P.
Curr. Biol. 11:1729-1738(2001) [PubMed] [Europe PMC] [Abstract]
Cited for: MUTANT MCD5.
[15]"Kuzbanian-mediated cleavage of Drosophila Notch."
Lieber T., Kidd S., Young M.W.
Genes Dev. 16:209-221(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: S2 CLEAVAGE BY KUZ.
[16]"General outlines of the molecular genetics of the Notch signalling pathway in Drosophila melanogaster: a review."
Portin P.
Hereditas 136:89-96(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: REVIEW.
[17]"Modulation of notch-ligand binding by protein O-fucosyltransferase 1 and fringe."
Okajima T., Xu A., Irvine K.D.
J. Biol. Chem. 278:42340-42345(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: GLYCOSYLATION, LIGAND-BINDING.
[18]"Drosophila Nedd4 regulates endocytosis of notch and suppresses its ligand-independent activation."
Sakata T., Sakaguchi H., Tsuda L., Higashitani A., Aigaki T., Matsuno K., Hayashi S.
Curr. Biol. 14:2228-2236(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH NEDD4, UBIQUITINATION, MUTAGENESIS OF TYR-2328.
[19]"Regulation of notch endosomal sorting and signaling by Drosophila Nedd4 family proteins."
Wilkin M.B., Carbery A.-M., Fostier M., Aslam H., Mazaleyrat S.L., Higgs J., Myat A., Evans D.A.P., Cornell M., Baron M.
Curr. Biol. 14:2237-2244(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH SU(DX).
[20]"The O-fucosyltransferase O-fut1 is an extracellular component that is essential for the constitutive endocytic trafficking of Notch in Drosophila."
Sasamura T., Ishikawa H.O., Sasaki N., Higashi S., Kanai M., Nakao S., Ayukawa T., Aigaki T., Noda K., Miyoshi E., Taniguchi N., Matsuno K.
Development 134:1347-1356(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: SUBCELLULAR LOCATION, INTERACTION WITH O-FUT1.
[21]"Rumi is a CAP10 domain glycosyltransferase that modifies Notch and is required for Notch signaling."
Acar M., Jafar-Nejad H., Takeuchi H., Rajan A., Ibrani D., Rana N.A., Pan H., Haltiwanger R.S., Bellen H.J.
Cell 132:247-258(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION.
[22]"Phosphoproteome analysis of Drosophila melanogaster embryos."
Zhai B., Villen J., Beausoleil S.A., Mintseris J., Gygi S.P.
J. Proteome Res. 7:1675-1682(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-2447, MASS SPECTROMETRY.
Tissue: Embryo.
[23]"Structure and stability of the ankyrin domain of the Drosophila Notch receptor."
Zweifel M.E., Leahy D.J., Hughson F.M., Barrick D.
Protein Sci. 12:2622-2632(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS) OF 1901-2139, DOMAIN ANK REPEATS, SUBUNIT.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		M16152 expand/collapse EMBL AC list , M16153, M16149, M16150, M16151 Genomic DNA. Translation: AAB59220.1.
K03508, M13689, K03507 Genomic DNA. Translation: AAA28725.1.
AE014298 Genomic DNA. Translation: AAF45848.2.
AL035436, AL035395 Genomic DNA. Translation: CAB37610.1.
M16025 Genomic DNA. Translation: AAA28726.1.
M12175 Genomic DNA. Translation: AAA74496.1.
PIRA24420.
RefSeqNP_001245510.1. NM_001258581.1.
NP_476859.2. NM_057511.3.
UniGeneDm.4702.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
1OT8X-ray2.00A/B/C1902-2139[»]
2JMFNMR-B2318-2333[»]
ProteinModelPortalP07207.
SMRP07207. Positions 105-1452, 1482-1726, 1864-2198.
ModBaseSearch...

Protein-protein interaction databases

DIPDIP-5N.
IntActP07207. 7 interactions.
MINTMINT-133064.

Proteomic databases

PaxDbP07207.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblMetazoaFBtr0070507; FBpp0070483; FBgn0004647.
FBtr0304659; FBpp0293201; FBgn0004647.
GeneID31293.
KEGGdme:Dmel_CG3936.

Organism-specific databases

CTD109544.
FlyBaseFBgn0004647. N.

Phylogenomic databases

eggNOGCOG0666.
GeneTreeENSGT00700000104305.
InParanoidP07207.
KOK02599.
OMAVCMPGFT.
OrthoDBEOG43N5TG.

Enzyme and pathway databases

ReactomeREACT_118588. Endoplasmic reticulum calcium ATPases positively regulate Notch precursor trafficking.
REACT_84305. NICD traffics to nucleus.
REACT_97910. Signal Transduction.

Gene expression databases

BgeeP07207.
GermOnlineCG3936. Drosophila melanogaster.

Family and domain databases

Gene3D1.25.40.20. 1 hit.
InterProIPR002110. 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.
IPR000800. Notch_dom.
IPR010660. Notch_NOD_dom.
IPR011656. Notch_NODP_dom.
[Graphical view]
PfamPF00023. Ank. 5 hits.
PF11936. DUF3454. 1 hit.
PF00008. EGF. 24 hits.
PF07645. EGF_CA. 4 hits.
PF06816. NOD. 1 hit.
PF07684. NODP. 1 hit.
PF00066. Notch. 3 hits.
[Graphical view]
PIRSFPIRSF002279. Notch. 1 hit.
PRINTSPR01452. LNOTCHREPEAT.
SMARTSM00248. ANK. 7 hits.
SM00181. EGF. 12 hits.
SM00179. EGF_CA. 24 hits.
SM00004. NL. 3 hits.
[Graphical view]
SUPFAMSSF48403. ANK. 1 hit.
SSF90193. Notch_region. 3 hits.
PROSITEPS50297. ANK_REP_REGION. 1 hit.
PS50088. ANK_REPEAT. 5 hits.
PS00010. ASX_HYDROXYL. 22 hits.
PS00022. EGF_1. 34 hits.
PS01186. EGF_2. 28 hits.
PS50026. EGF_3. 36 hits.
PS01187. EGF_CA. 21 hits.
PS50258. LNR. 3 hits.
[Graphical view]
ProtoNetSearch...

Other

EvolutionaryTraceP07207.
GenomeRNAi31293.
NextBio772898.

Entry information

Entry nameNOTCH_DROME
AccessionPrimary (citable) accession number: P07207
Secondary accession number(s): O97458, P04154, Q9W4T8
Entry history
Integrated into UniProtKB/Swiss-Prot: November 1, 1986
Last sequence update: November 2, 2001
Last modified: May 1, 2013
This is version 172 of the entry and version 3 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programDrosophila annotation project

Relevant documents

Drosophila

Drosophila: entries, gene names and cross-references to FlyBase

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

SIMILARITY comments

Index of protein domains and families

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