UniProtKB - Q9QW30 (NOTC2_RAT)
Neurogenic locus notch homolog protein 2
Notch2
Functioni
Sites
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Sitei | 614 | Essential for O-xylosylationBy similarity | 1 |
GO - Molecular functioni
- calcium ion binding Source: InterPro
- enzyme binding Source: RGD
- NF-kappaB binding Source: RGD
- signaling receptor activity Source: RGD
GO - Biological processi
- animal organ morphogenesis Source: UniProtKB
- atrial septum morphogenesis Source: RGD
- bone remodeling Source: RGD
- cell cycle arrest Source: UniProtKB
- cell fate determination Source: RGD
- central nervous system development Source: GO_Central
- cholangiocyte proliferation Source: RGD
- ciliary body morphogenesis Source: RGD
- defense response to bacterium Source: RGD
- determination of left/right symmetry Source: RGD
- embryonic limb morphogenesis Source: RGD
- glomerular capillary formation Source: RGD
- glomerular visceral epithelial cell development Source: RGD
- heart looping Source: RGD
- hepatocyte proliferation Source: RGD
- humoral immune response Source: RGD
- inflammatory response to antigenic stimulus Source: RGD
- interleukin-4 production Source: RGD
- intrahepatic bile duct development Source: RGD
- in utero embryonic development Source: RGD
- left/right axis specification Source: RGD
- liver development Source: RGD
- liver morphogenesis Source: RGD
- marginal zone B cell differentiation Source: UniProtKB
- morphogenesis of an epithelial sheet Source: RGD
- multicellular organism growth Source: RGD
- myeloid dendritic cell differentiation Source: RGD
- negative regulation of gene expression Source: RGD
- negative regulation of growth rate Source: UniProtKB
- negative regulation of transcription by RNA polymerase II Source: RGD
- Notch signaling pathway Source: UniProtKB
- placenta blood vessel development Source: RGD
- placenta development Source: RGD
- positive regulation of apoptotic process Source: RGD
- positive regulation of BMP signaling pathway Source: RGD
- positive regulation of cell population proliferation Source: RGD
- positive regulation of ERK1 and ERK2 cascade Source: RGD
- positive regulation of keratinocyte proliferation Source: UniProtKB
- positive regulation of osteoclast differentiation Source: RGD
- positive regulation of Ras protein signal transduction Source: UniProtKB
- proximal tubule development Source: RGD
- pulmonary valve morphogenesis Source: RGD
- regulation of actin cytoskeleton reorganization Source: UniProtKB
- regulation of osteoclast development Source: UniProtKB
- regulation of transcription by RNA polymerase II Source: RGD
- skeletal system development Source: GO_Central
- tissue regeneration Source: RGD
- wound healing Source: UniProtKB
Keywordsi
Molecular function | Activator, Developmental protein, Receptor |
Biological process | Differentiation, Notch signaling pathway, Transcription, Transcription regulation |
Names & Taxonomyi
Protein namesi | Recommended name: Neurogenic locus notch homolog protein 2By similarityShort name: Notch 2 Cleaved into the following 2 chains: |
Gene namesi | Name:Notch2Imported |
Organismi | Rattus norvegicus (Rat) |
Taxonomic identifieri | 10116 [NCBI] |
Taxonomic lineagei | Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Glires › Rodentia › Myomorpha › Muroidea › Muridae › Murinae › Rattus |
Proteomesi |
|
Organism-specific databases
RGDi | 3188, Notch2 |
Subcellular locationi
Plasma membrane
- Cell membrane By similarity; Single-pass type I membrane protein By similarity
Cytosol
- cytosol Source: Reactome
Extracellular region or secreted
- extracellular matrix Source: GO_Central
- extracellular region Source: Reactome
Nucleus
- nucleus Source: UniProtKB
Plasma Membrane
- integral component of plasma membrane Source: UniProtKB
- plasma membrane Source: Reactome
Other locations
- cell surface Source: UniProtKB
- cilium Source: RGD
- receptor complex Source: RGD
Topology
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Topological domaini | 26 – 1677 | ExtracellularSequence analysisAdd BLAST | 1652 | |
Transmembranei | 1678 – 1698 | HelicalSequence analysisAdd BLAST | 21 | |
Topological domaini | 1699 – 2471 | CytoplasmicSequence analysisAdd BLAST | 773 |
Keywords - Cellular componenti
Cell membrane, Cytoplasm, Membrane, NucleusPathology & Biotechi
Mutagenesis
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Mutagenesisi | 2078 | S → A: Permits Notch2 inhibitory activity upon G-CSF action on myeloid cells. 1 Publication | 1 | |
Mutagenesisi | 2090 | S → A: No effect. 1 Publication | 1 |
PTM / Processingi
Molecule processing
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Signal peptidei | 1 – 25 | Sequence analysisAdd BLAST | 25 | |
ChainiPRO_0000007689 | 26 – 2471 | Neurogenic locus notch homolog protein 2Add BLAST | 2446 | |
ChainiPRO_0000007690 | 1666 – 2471 | Notch 2 extracellular truncationBy similarityAdd BLAST | 806 | |
ChainiPRO_0000007691 | 1697 – 2471 | Notch 2 intracellular domainBy similarityAdd BLAST | 775 |
Amino acid modifications
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Disulfide bondi | 28 ↔ 41 | By similarity | ||
Disulfide bondi | 35 ↔ 51 | By similarity | ||
Glycosylationi | 46 | N-linked (GlcNAc...) asparagineSequence analysis | 1 | |
Disulfide bondi | 53 ↔ 62 | By similarity | ||
Disulfide bondi | 68 ↔ 79 | By similarity | ||
Disulfide bondi | 73 ↔ 90 | By similarity | ||
Disulfide bondi | 92 ↔ 101 | By similarity | ||
Disulfide bondi | 109 ↔ 121 | By similarity | ||
Disulfide bondi | 115 ↔ 131 | By similarity | ||
Disulfide bondi | 133 ↔ 142 | By similarity | ||
Disulfide bondi | 148 ↔ 159 | By similarity | ||
Disulfide bondi | 153 ↔ 168 | By similarity | ||
Glycosylationi | 155 | N-linked (GlcNAc...) asparagineSequence analysis | 1 | |
Disulfide bondi | 170 ↔ 179 | By similarity | ||
Disulfide bondi | 186 ↔ 198 | By similarity | ||
Disulfide bondi | 192 ↔ 207 | By similarity | ||
Disulfide bondi | 209 ↔ 218 | By similarity | ||
Disulfide bondi | 225 ↔ 236 | By similarity | ||
Disulfide bondi | 230 ↔ 246 | By similarity | ||
Disulfide bondi | 248 ↔ 257 | By similarity | ||
Disulfide bondi | 264 ↔ 275 | By similarity | ||
Disulfide bondi | 269 ↔ 284 | By similarity | ||
Disulfide bondi | 286 ↔ 295 | By similarity | ||
Disulfide bondi | 302 ↔ 315 | By similarity | ||
Disulfide bondi | 309 ↔ 324 | By similarity | ||
Disulfide bondi | 326 ↔ 335 | By similarity | ||
Disulfide bondi | 342 ↔ 353 | By similarity | ||
Disulfide bondi | 347 ↔ 362 | By similarity | ||
Disulfide bondi | 364 ↔ 373 | By similarity | ||
Disulfide bondi | 379 ↔ 390 | By similarity | ||
Disulfide bondi | 384 ↔ 401 | By similarity | ||
Disulfide bondi | 403 ↔ 412 | By similarity | ||
Disulfide bondi | 419 ↔ 433 | By similarity | ||
Disulfide bondi | 427 ↔ 442 | By similarity | ||
Disulfide bondi | 444 ↔ 453 | By similarity | ||
Disulfide bondi | 460 ↔ 471 | By similarity | ||
Disulfide bondi | 465 ↔ 480 | By similarity | ||
Disulfide bondi | 482 ↔ 491 | By similarity | ||
Disulfide bondi | 498 ↔ 509 | By similarity | ||
Disulfide bondi | 503 ↔ 518 | By similarity | ||
Disulfide bondi | 520 ↔ 529 | By similarity | ||
Disulfide bondi | 536 ↔ 547 | By similarity | ||
Disulfide bondi | 541 ↔ 556 | By similarity | ||
Disulfide bondi | 558 ↔ 567 | By similarity | ||
Disulfide bondi | 574 ↔ 584 | By similarity | ||
Disulfide bondi | 579 ↔ 593 | By similarity | ||
Disulfide bondi | 595 ↔ 604 | By similarity | ||
Disulfide bondi | 611 ↔ 622 | By similarity | ||
Glycosylationi | 613 | O-linked (Glc...) serine; alternateBy similarity | 1 | |
Glycosylationi | 613 | O-linked (Xyl...) serine; alternateBy similarity | 1 | |
Disulfide bondi | 616 ↔ 631 | By similarity | ||
Disulfide bondi | 633 ↔ 642 | By similarity | ||
Disulfide bondi | 649 ↔ 659 | By similarity | ||
Disulfide bondi | 654 ↔ 668 | By similarity | ||
Disulfide bondi | 670 ↔ 679 | By similarity | ||
Disulfide bondi | 686 ↔ 697 | By similarity | ||
Disulfide bondi | 691 ↔ 706 | By similarity | ||
Disulfide bondi | 708 ↔ 717 | By similarity | ||
Disulfide bondi | 724 ↔ 734 | By similarity | ||
Disulfide bondi | 729 ↔ 743 | By similarity | ||
Glycosylationi | 733 | N-linked (GlcNAc...) asparagineSequence analysis | 1 | |
Disulfide bondi | 745 ↔ 754 | By similarity | ||
Disulfide bondi | 761 ↔ 772 | By similarity | ||
Disulfide bondi | 766 ↔ 781 | By similarity | ||
Disulfide bondi | 783 ↔ 792 | By similarity | ||
Disulfide bondi | 799 ↔ 810 | By similarity | ||
Disulfide bondi | 804 ↔ 819 | By similarity | ||
Disulfide bondi | 821 ↔ 830 | By similarity | ||
Disulfide bondi | 837 ↔ 848 | By similarity | ||
Disulfide bondi | 842 ↔ 859 | By similarity | ||
Disulfide bondi | 861 ↔ 870 | By similarity | ||
Disulfide bondi | 877 ↔ 888 | By similarity | ||
Disulfide bondi | 882 ↔ 897 | By similarity | ||
Disulfide bondi | 899 ↔ 908 | By similarity | ||
Disulfide bondi | 915 ↔ 926 | By similarity | ||
Disulfide bondi | 920 ↔ 935 | By similarity | ||
Disulfide bondi | 937 ↔ 946 | By similarity | ||
Disulfide bondi | 953 ↔ 964 | By similarity | ||
Disulfide bondi | 958 ↔ 973 | By similarity | ||
Disulfide bondi | 975 ↔ 984 | By similarity | ||
Disulfide bondi | 991 ↔ 1002 | By similarity | ||
Disulfide bondi | 996 ↔ 1011 | By similarity | ||
Disulfide bondi | 1013 ↔ 1022 | By similarity | ||
Disulfide bondi | 1029 ↔ 1040 | By similarity | ||
Disulfide bondi | 1034 ↔ 1049 | By similarity | ||
Disulfide bondi | 1051 ↔ 1060 | By similarity | ||
Disulfide bondi | 1067 ↔ 1078 | By similarity | ||
Disulfide bondi | 1072 ↔ 1087 | By similarity | ||
Disulfide bondi | 1089 ↔ 1098 | By similarity | ||
Glycosylationi | 1102 | N-linked (GlcNAc...) asparagineSequence analysis | 1 | |
Disulfide bondi | 1105 ↔ 1126 | Curated | ||
Disulfide bondi | 1120 ↔ 1135 | By similarity | ||
Disulfide bondi | 1137 ↔ 1146 | By similarity | ||
Disulfide bondi | 1153 ↔ 1164 | By similarity | ||
Disulfide bondi | 1158 ↔ 1173 | By similarity | ||
Disulfide bondi | 1175 ↔ 1184 | By similarity | ||
Disulfide bondi | 1191 ↔ 1202 | By similarity | ||
Disulfide bondi | 1196 ↔ 1211 | By similarity | ||
Disulfide bondi | 1213 ↔ 1222 | By similarity | ||
Disulfide bondi | 1229 ↔ 1241 | By similarity | ||
Disulfide bondi | 1235 ↔ 1250 | By similarity | ||
Disulfide bondi | 1252 ↔ 1261 | By similarity | ||
Disulfide bondi | 1268 ↔ 1281 | By similarity | ||
Disulfide bondi | 1273 ↔ 1290 | By similarity | ||
Disulfide bondi | 1292 ↔ 1301 | By similarity | ||
Disulfide bondi | 1308 ↔ 1319 | By similarity | ||
Disulfide bondi | 1313 ↔ 1331 | By similarity | ||
Disulfide bondi | 1333 ↔ 1342 | By similarity | ||
Disulfide bondi | 1378 ↔ 1389 | By similarity | ||
Disulfide bondi | 1383 ↔ 1400 | By similarity | ||
Disulfide bondi | 1402 ↔ 1411 | By similarity | ||
Disulfide bondi | 1425 ↔ 1448 | By similarity | ||
Disulfide bondi | 1430 ↔ 1443 | By similarity | ||
Disulfide bondi | 1439 ↔ 1455 | By similarity | ||
Glycosylationi | 1465 | N-linked (GlcNAc...) asparagineSequence analysis | 1 | |
Disulfide bondi | 1466 ↔ 1489 | By similarity | ||
Disulfide bondi | 1472 ↔ 1484 | By similarity | ||
Disulfide bondi | 1480 ↔ 1496 | By similarity | ||
Disulfide bondi | 1503 ↔ 1527 | By similarity | ||
Disulfide bondi | 1509 ↔ 1522 | By similarity | ||
Disulfide bondi | 1518 ↔ 1534 | By similarity | ||
Disulfide bondi | 1632 ↔ 1639 | By similarity | ||
Modified residuei | 1716 | PhosphothreonineBy similarity | 1 | |
Modified residuei | 1779 | PhosphoserineBy similarity | 1 | |
Modified residuei | 1802 | PhosphothreonineBy similarity | 1 | |
Modified residuei | 1804 | PhosphoserineBy similarity | 1 | |
Modified residuei | 1808 | PhosphothreonineBy similarity | 1 | |
Modified residuei | 1842 | PhosphoserineBy similarity | 1 | |
Modified residuei | 1845 | PhosphoserineCombined sources | 1 | |
Modified residuei | 2070 | PhosphoserineBy similarity | 1 | |
Modified residuei | 2078 | Phosphoserine1 Publication | 1 | |
Modified residuei | 2081 | PhosphoserineBy similarity | 1 | |
Modified residuei | 2097 | PhosphothreonineBy similarity | 1 |
Post-translational modificationi
Keywords - PTMi
Disulfide bond, Glycoprotein, Phosphoprotein, Ubl conjugationProteomic databases
PaxDbi | Q9QW30 |
PRIDEi | Q9QW30 |
PTM databases
GlyGeni | Q9QW30, 6 sites |
iPTMneti | Q9QW30 |
PhosphoSitePlusi | Q9QW30 |
Expressioni
Tissue specificityi
Developmental stagei
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 (By similarity).
Interacts with MAML1, MAML2 and MAML3 which act as transcriptional coactivators for NOTCH2.
Interacts with RELA/p65 (By similarity).
Interacts with HIF1AN.
Interacts (via ANK repeats) with TCIM, the interaction inhibits the nuclear translocation of NOTCH2 N2ICD (By similarity).
Interacts with CUL1, RBX1, SKP1 and FBXW7 that are SCF(FBXW7) E3 ubiquitin-protein ligase complex components.
Interacts with MINAR1; this interaction increases MINAR1 stability and function (By similarity).
Interacts with MDK; this interaction mediates a nuclear accumulation of NOTCH2 and therefore activation of NOTCH2 signaling leading to interaction between HES1 and STAT3 (By similarity).
By similarityGO - Molecular functioni
- enzyme binding Source: RGD
- NF-kappaB binding Source: RGD
Protein-protein interaction databases
STRINGi | 10116.ENSRNOP00000025718 |
Family & Domainsi
Domains and Repeats
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Domaini | 26 – 63 | EGF-like 1PROSITE-ProRule annotationAdd BLAST | 38 | |
Domaini | 64 – 102 | EGF-like 2PROSITE-ProRule annotationAdd BLAST | 39 | |
Domaini | 105 – 143 | EGF-like 3PROSITE-ProRule annotationAdd BLAST | 39 | |
Domaini | 144 – 180 | EGF-like 4PROSITE-ProRule annotationAdd BLAST | 37 | |
Domaini | 182 – 219 | EGF-like 5; calcium-bindingPROSITE-ProRule annotationAdd BLAST | 38 | |
Domaini | 221 – 258 | EGF-like 6PROSITE-ProRule annotationAdd BLAST | 38 | |
Domaini | 260 – 296 | EGF-like 7; calcium-bindingPROSITE-ProRule annotationAdd BLAST | 37 | |
Domaini | 298 – 336 | EGF-like 8; calcium-bindingPROSITE-ProRule annotationAdd BLAST | 39 | |
Domaini | 338 – 374 | EGF-like 9; calcium-bindingPROSITE-ProRule annotationAdd BLAST | 37 | |
Domaini | 375 – 413 | EGF-like 10PROSITE-ProRule annotationAdd BLAST | 39 | |
Domaini | 415 – 454 | EGF-like 11; calcium-bindingPROSITE-ProRule annotationAdd BLAST | 40 | |
Domaini | 456 – 492 | EGF-like 12; calcium-bindingPROSITE-ProRule annotationAdd BLAST | 37 | |
Domaini | 494 – 530 | EGF-like 13; calcium-bindingPROSITE-ProRule annotationAdd BLAST | 37 | |
Domaini | 532 – 568 | EGF-like 14; calcium-bindingPROSITE-ProRule annotationAdd BLAST | 37 | |
Domaini | 570 – 605 | EGF-like 15; calcium-bindingPROSITE-ProRule annotationAdd BLAST | 36 | |
Domaini | 607 – 643 | EGF-like 16; calcium-bindingPROSITE-ProRule annotationAdd BLAST | 37 | |
Domaini | 645 – 680 | EGF-like 17; calcium-bindingPROSITE-ProRule annotationAdd BLAST | 36 | |
Domaini | 682 – 718 | EGF-like 18; calcium-bindingPROSITE-ProRule annotationAdd BLAST | 37 | |
Domaini | 720 – 755 | EGF-like 19PROSITE-ProRule annotationAdd BLAST | 36 | |
Domaini | 757 – 793 | EGF-like 20; calcium-bindingPROSITE-ProRule annotationAdd BLAST | 37 | |
Domaini | 795 – 831 | EGF-like 21; calcium-bindingPROSITE-ProRule annotationAdd BLAST | 37 | |
Domaini | 833 – 871 | EGF-like 22PROSITE-ProRule annotationAdd BLAST | 39 | |
Domaini | 873 – 909 | EGF-like 23; calcium-bindingPROSITE-ProRule annotationAdd BLAST | 37 | |
Domaini | 911 – 947 | EGF-like 24; calcium-bindingPROSITE-ProRule annotationAdd BLAST | 37 | |
Domaini | 949 – 985 | EGF-like 25; calcium-bindingPROSITE-ProRule annotationAdd BLAST | 37 | |
Domaini | 987 – 1023 | EGF-like 26; calcium-bindingPROSITE-ProRule annotationAdd BLAST | 37 | |
Domaini | 1025 – 1061 | EGF-like 27; calcium-bindingPROSITE-ProRule annotationAdd BLAST | 37 | |
Domaini | 1063 – 1099 | EGF-like 28PROSITE-ProRule annotationAdd BLAST | 37 | |
Domaini | 1101 – 1147 | EGF-like 29CuratedAdd BLAST | 47 | |
Domaini | 1149 – 1185 | EGF-like 30; calcium-bindingPROSITE-ProRule annotationAdd BLAST | 37 | |
Domaini | 1187 – 1223 | EGF-like 31; calcium-bindingPROSITE-ProRule annotationAdd BLAST | 37 | |
Domaini | 1225 – 1262 | EGF-like 32; calcium-bindingPROSITE-ProRule annotationAdd BLAST | 38 | |
Domaini | 1264 – 1302 | EGF-like 33PROSITE-ProRule annotationAdd BLAST | 39 | |
Domaini | 1304 – 1343 | EGF-like 34PROSITE-ProRule annotationAdd BLAST | 40 | |
Domaini | 1374 – 1412 | EGF-like 35PROSITE-ProRule annotationAdd BLAST | 39 | |
Repeati | 1425 – 1465 | LNR 1Add BLAST | 41 | |
Repeati | 1466 – 1502 | LNR 2Add BLAST | 37 | |
Repeati | 1503 – 1544 | LNR 3Add BLAST | 42 | |
Repeati | 1827 – 1871 | ANK 1Add BLAST | 45 | |
Repeati | 1876 – 1905 | ANK 2Add BLAST | 30 | |
Repeati | 1909 – 1939 | ANK 3Add BLAST | 31 | |
Repeati | 1943 – 1972 | ANK 4Add BLAST | 30 | |
Repeati | 1976 – 2005 | ANK 5Add BLAST | 30 | |
Repeati | 2009 – 2038 | ANK 6Add BLAST | 30 |
Region
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Regioni | 1425 – 1677 | Negative regulatory region (NRR)By similarityAdd BLAST | 253 |
Compositional bias
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Compositional biasi | 1645 – 1648 | Poly-Ala | 4 | |
Compositional biasi | 1994 – 1997 | Poly-Leu | 4 | |
Compositional biasi | 2426 – 2429 | Poly-Ser | 4 | |
Compositional biasi | 2446 – 2451 | Poly-Gly | 6 |
Sequence similaritiesi
Keywords - Domaini
ANK repeat, EGF-like domain, Repeat, Signal, Transmembrane, Transmembrane helixPhylogenomic databases
eggNOGi | KOG1217, Eukaryota |
InParanoidi | Q9QW30 |
PhylomeDBi | Q9QW30 |
Family and domain databases
Gene3Di | 1.25.40.20, 1 hit |
InterProi | View 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 IPR022336, Notch_2 IPR000800, Notch_dom IPR010660, Notch_NOD_dom IPR011656, Notch_NODP_dom |
Pfami | View protein in Pfam PF12796, Ank_2, 1 hit PF11936, DUF3454, 1 hit PF00008, EGF, 22 hits PF07645, EGF_CA, 5 hits PF12661, hEGF, 3 hits PF06816, NOD, 1 hit PF07684, NODP, 1 hit PF00066, Notch, 3 hits |
PIRSFi | PIRSF002279, Notch, 1 hit |
PRINTSi | PR01452, LNOTCHREPEAT PR01985, NOTCH2 |
SMARTi | View protein in SMART SM00248, ANK, 6 hits SM01334, DUF3454, 1 hit SM00181, EGF, 35 hits SM00179, EGF_CA, 33 hits SM00004, NL, 3 hits SM01338, NOD, 1 hit SM01339, NODP, 1 hit |
SUPFAMi | SSF48403, SSF48403, 1 hit SSF57184, SSF57184, 6 hits SSF90193, SSF90193, 2 hits |
PROSITEi | View protein in PROSITE PS50297, ANK_REP_REGION, 1 hit PS50088, ANK_REPEAT, 4 hits PS00010, ASX_HYDROXYL, 22 hits PS00022, EGF_1, 34 hits PS01186, EGF_2, 26 hits PS50026, EGF_3, 35 hits PS01187, EGF_CA, 22 hits PS50258, LNR, 3 hits |
(1+)i Sequence
Sequence statusi: Complete.
: The displayed sequence is further processed into a mature form. Sequence processingi
This entry has 1 described isoform and 2 potential isoforms that are computationally mapped.Show allAlign All
10 20 30 40 50
MPALRPAALR ALLWLWLCGA GPAHALQCRG GQEPCVNEGT CVTYHNGTGY
60 70 80 90 100
CRCPEGFLGE YCQHRDPCEK NRCQNGGTCV TQAMLGKATC RCAPGFTGED
110 120 130 140 150
CQYSTSHPCF VSRPCQNGGT CHMLSWDTYE CTCQVGFTGK QCQWTDVCLS
160 170 180 190 200
HPCENGSTCS SVANQFSCRC PAGITGQKCD ADINECDIPG RCQHGGTCLN
210 220 230 240 250
LPGSYRCQCP QRFTGQHCDS PYVPCAPSPC VNGGTCRQTG DFTSECHCLP
260 270 280 290 300
GFEGSNCERN IDDCPNHKCQ NGGVCVDGVN TYNCRCPPQW TGQFCTEDVD
310 320 330 340 350
ECLLQPNACQ NGGTCTNRNG GYGCVCVNGW SGDDCSENID DCAFASCTPG
360 370 380 390 400
STCIDRVASF SCLCPEGKAG LLCHLDDACI SNPCHKGALC DTNPLNGQYI
410 420 430 440 450
CTCPQAYKGA DCTEDVDECA MANSNPCEHA GKCVNTDGAF HCECLKGYAG
460 470 480 490 500
PRCEMDINEC HSDPCQNDAT CLDKIGGFTC LCMPGFKGVH CELEVNECQS
510 520 530 540 550
NPCVNNGQCV DKVNRFQCLC PPGFTGPVCQ IDIDDCSSTP CLNGAKCIDH
560 570 580 590 600
PNGYECQCAT GFTGTLCDEN IDNCDPDPCH HGQCQDGIDS YTCICNPGYM
610 620 630 640 650
GAICSDQIDE CYSSPCLNDG RCIDLVNGYQ CNCQPGTSGL NCEINFDDCA
660 670 680 690 700
SNPCLHGACV DGINRYSCVC SPGFTGQRCN IDIDECASNP CRKDATCIND
710 720 730 740 750
VNGFRCMCPE GPHHPSCYSQ VNECLSSPCI HGNCTGGLSG YKCLCDAGWV
760 770 780 790 800
GINCEVDKNE CLSNPCQNGG TCNNLVNGYR CTCKKGFKGY NCQVNIDECA
810 820 830 840 850
SNPCLNQGTC LDDVSGYTCH CMLPYTGKNC QTVLAPCSPN PCENAAVCKE
860 870 880 890 900
APNFESFTCL CAPGWQGQRC TVDVDECVSK PCMNNGICHN TQGSYMCECP
910 920 930 940 950
PGFSGMDCEE DINDCLANPC QNGGSCVDKV NTFSCLCLPG FVGDKCQTDM
960 970 980 990 1000
NECLSEPCKN GGTCSDYVNS YTCTCPAGFH GVHCENNIDE CTESSCFNGG
1010 1020 1030 1040 1050
TCVDGINSFS CLCPVGFTGP FCLHDINECS SNPCLNSGTC VDGLGTYRCT
1060 1070 1080 1090 1100
CPLGYTGKNC QTLVNLCSPS PCKNKGTCAQ EKARPRCLCP PGWDGAYCDV
1110 1120 1130 1140 1150
LNVSCKAAAL QKGVPVEHLC QHSGICINAG NTHHCQCPLG YTGSYCEEQL
1160 1170 1180 1190 1200
DECASNPCQH GATCSDFIGG YRCECVPGYQ GVNCEYEVDE CQNQPCQNGG
1210 1220 1230 1240 1250
TCIDLVNHFK CSCPPGTRGL LCEENIDDCA GAPHCLNGGQ CVDRIGGYSC
1260 1270 1280 1290 1300
RCLPGFAGER CEGDINECLS NPCSSEGSLD CIQLKNNYQC VCRSAFTGRH
1310 1320 1330 1340 1350
CETFLDVCPQ KPCLNGGTCA VASNVPDGFI CRCPPGFSGA RCQSSCGQVK
1360 1370 1380 1390 1400
CRRGEQCVHT ASGPHCFCPN HKDCESGCAS NPCQHGGTCY PQRQPPYYSC
1410 1420 1430 1440 1450
RCSPPFWGSH CESYTAPTST PPATCLSQYC ADKARDGICD EACNSHACQW
1460 1470 1480 1490 1500
DGGDCSLTME DPWANCTSSL RCWEYINNQC DELCNTAECL FDNFECQRNS
1510 1520 1530 1540 1550
KTCKYDKYCA DHFKDNHCDK GCNNEECGWD GLDCAADQPE NLAEGILVIV
1560 1570 1580 1590 1600
VLLPPEQLLQ DSRSFLRALG TLLHTNLRIK QDSQGALMVY PYYGEKSAAM
1610 1620 1630 1640 1650
KKQKVARRSL PDEQEQEIIG SKVFLEIDNR QCVQDSDQCF KNTDAAAALL
1660 1670 1680 1690 1700
ASHAIQGTLS YPLVSVVSES EDPRNTPLLY LLAVAVVIIL FLILLGVIMA
1710 1720 1730 1740 1750
KRKRKHGFLW LPEGFTLRRD SSNHKRREPV GQDAVGLKNL SVQVSEANLI
1760 1770 1780 1790 1800
GSTTSEHWGD DEGPQPKKAK AEDDEALLSE DDPVDRRPWT QQHLEAADIR
1810 1820 1830 1840 1850
RTPSLALTPP QAEQEVDVLD VNVRGPDGCT PLMLASLRGG SSDLSDEDED
1860 1870 1880 1890 1900
AEDSSANIIT DLVYQGASLQ AQTDRTGEMA LHLAARYSRA DAAKRLLDAG
1910 1920 1930 1940 1950
ADANAQDNMG RCPLHAAVAA DAQGVFQILI RNRVTDLDAR MNDGTTPLIL
1960 1970 1980 1990 2000
AARLAVEGMV AELINCQADV NAVDDHGKSA LHWAAAVNNV EATLLLLKNG
2010 2020 2030 2040 2050
ANRDMQDNKE ETPLFLAARE GSYEAAKILL DHFANRDITD HMDRLPRDVA
2060 2070 2080 2090 2100
RDRMHHDIVR LLDEYNVTPS PPGTVLTSAL SPVLCGPNRS FLSLKHTPMG
2110 2120 2130 2140 2150
KKARRPNTKS TMPTSLPNLA KEAKDVKGSR RKKCLNEKVQ LSESSVTLSP
2160 2170 2180 2190 2200
VDSLESPHTY VSDATSSPMI TSPGILQASP TPLLAAAPAA PVHAQHALSF
2210 2220 2230 2240 2250
SNLHEMQPLR PGASTVLPSV SQLLSHHHIV PPGSGSAGSL GRLHSVPVPS
2260 2270 2280 2290 2300
DWMNRVEMSE TQYSEMFGMV LAPAEGTHPG MAAPQSRAPE GKPIPTQREP
2310 2320 2330 2340 2350
LPPIVTFQLI PKGSLAQAAG APQTQSGCPP AVAGPLPSMY QIPEMARLPS
2360 2370 2380 2390 2400
VAFPPTMMPQ QEGQVAQTIV PTYHPFPASV GKYPTPPSQH SYASSNAAER
2410 2420 2430 2440 2450
TPNHGGHLQG EHPYLTPSPE SPDQWSSSSP HSASDWSDVT TSPTPGGGGG
2460 2470
GQRGPGTHMS EPPHSNMQVY A
Computationally mapped potential isoform sequencesi
There are 2 potential isoforms mapped to this entry.BLASTAlignShow allAdd to basketG3V8G9 | G3V8G9_RAT | Neurogenic locus notch homolog prot... | Notch2 rCG_52042 | 2,471 | Annotation score: | ||
A0A1W2Q619 | A0A1W2Q619_RAT | Neurogenic locus notch homolog prot... | Notch2 | 79 | Annotation score: |
Sequence databases
Select the link destinations: EMBLi GenBanki DDBJi Links Updated | M93661 mRNA Translation: AAK13558.1 |
PIRi | A49128 |
Genome annotation databases
UCSCi | RGD:3188, rat |
Similar proteinsi
Cross-referencesi
Sequence databases
Select the link destinations: EMBLi GenBanki DDBJi Links Updated | M93661 mRNA Translation: AAK13558.1 |
PIRi | A49128 |
3D structure databases
SMRi | Q9QW30 |
ModBasei | Search... |
Protein-protein interaction databases
STRINGi | 10116.ENSRNOP00000025718 |
PTM databases
GlyGeni | Q9QW30, 6 sites |
iPTMneti | Q9QW30 |
PhosphoSitePlusi | Q9QW30 |
Proteomic databases
PaxDbi | Q9QW30 |
PRIDEi | Q9QW30 |
Genome annotation databases
UCSCi | RGD:3188, rat |
Organism-specific databases
RGDi | 3188, Notch2 |
Phylogenomic databases
eggNOGi | KOG1217, Eukaryota |
InParanoidi | Q9QW30 |
PhylomeDBi | Q9QW30 |
Miscellaneous databases
PROi | PR:Q9QW30 |
Family and domain databases
Gene3Di | 1.25.40.20, 1 hit |
InterProi | View 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 IPR022336, Notch_2 IPR000800, Notch_dom IPR010660, Notch_NOD_dom IPR011656, Notch_NODP_dom |
Pfami | View protein in Pfam PF12796, Ank_2, 1 hit PF11936, DUF3454, 1 hit PF00008, EGF, 22 hits PF07645, EGF_CA, 5 hits PF12661, hEGF, 3 hits PF06816, NOD, 1 hit PF07684, NODP, 1 hit PF00066, Notch, 3 hits |
PIRSFi | PIRSF002279, Notch, 1 hit |
PRINTSi | PR01452, LNOTCHREPEAT PR01985, NOTCH2 |
SMARTi | View protein in SMART SM00248, ANK, 6 hits SM01334, DUF3454, 1 hit SM00181, EGF, 35 hits SM00179, EGF_CA, 33 hits SM00004, NL, 3 hits SM01338, NOD, 1 hit SM01339, NODP, 1 hit |
SUPFAMi | SSF48403, SSF48403, 1 hit SSF57184, SSF57184, 6 hits SSF90193, SSF90193, 2 hits |
PROSITEi | View protein in PROSITE PS50297, ANK_REP_REGION, 1 hit PS50088, ANK_REPEAT, 4 hits PS00010, ASX_HYDROXYL, 22 hits PS00022, EGF_1, 34 hits PS01186, EGF_2, 26 hits PS50026, EGF_3, 35 hits PS01187, EGF_CA, 22 hits PS50258, LNR, 3 hits |
ProtoNeti | Search... |
MobiDBi | Search... |
Entry informationi
Entry namei | NOTC2_RAT | |
Accessioni | Q9QW30Primary (citable) accession number: Q9QW30 | |
Entry historyi | Integrated into UniProtKB/Swiss-Prot: | March 27, 2002 |
Last sequence update: | May 1, 2000 | |
Last modified: | December 2, 2020 | |
This is version 175 of the entry and version 1 of the sequence. See complete history. | ||
Entry statusi | Reviewed (UniProtKB/Swiss-Prot) | |
Annotation program | Chordata Protein Annotation Program |
Miscellaneousi
Keywords - Technical termi
Reference proteomeDocuments
- SIMILARITY comments
Index of protein domains and families