O35516 (NOTC2_MOUSE) Reviewed, UniProtKB/Swiss-Prot
Last modified
May 1, 2013.
Version 143.
History...
Clusters with 
Names·Attributes·General annotation·Ontologies·Alt products·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize orderNames·Attributes·General annotation·Ontologies·Alt products·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize orderNames and origin
| Protein names | Recommended name: Neurogenic locus notch homolog protein 2 Short name=Notch 2 Alternative name(s): Motch B Cleaved into the following 2 chains: | ||
| Gene names |
| ||
| Organism | Mus musculus (Mouse) [Reference proteome] | ||
| Taxonomic identifier | 10090 [NCBI] | ||
| Taxonomic lineage | Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Glires › Rodentia › Sciurognathi › Muroidea › Muridae › Murinae › Mus › Mus |
Protein attributes
| Sequence length | 2470 AA. |
| Sequence status | Complete. |
| Sequence processing | The displayed sequence is further processed into a mature form. |
| Protein existence | Evidence at protein level |
General annotation (Comments)
| Function | Functions as a receptor for membrane-bound ligands Jagged1, Jagged2 and Delta1 to regulate cell-fate determination. Upon ligand activation through the released notch intracellular domain (NICD) it forms a transcriptional activator complex with RBPJ/RBPSUH and activates genes of the enhancer of split locus. Affects the implementation of differentiation, proliferation and apoptotic programs By similarity. May play an essential role in postimplantation development, probably in some aspect of cell specification and/or differentiation. In collaboration with RELA/p65 enhances NFATc1 promoter activity and positively regulates RANKL-induced osteoclast differentiation. Ref.4 Ref.10 |
| Subunit structure | Heterodimer of a C-terminal fragment N(TM) and an N-terminal fragment N(EC) which are probably linked by disulfide bonds. Interacts with MAML1, MAML2 and MAML3 which act as transcriptional coactivators for NOTCH2. Interacts with RELA/p65. Interacts with HIF1AN. Ref.8 Ref.9 Ref.10 |
| Subcellular location | Cell membrane; Single-pass type I membrane protein. Notch 2 intracellular domain: Nucleus. Note: Following proteolytical processing NICD is translocated to the nucleus. |
| Tissue specificity | Expressed in the brain, liver, kidney, neuroepithelia, somites, optic vesicles and branchial arches, but not heart. |
| Developmental stage | Expressed in the embryonic ventricular zone, the postnatal ependymal cells, and the choroid plexus throughout embryonic and postnatal development. Ref.5 |
| Post-translational modification | 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 TNF-alpha converting enzyme (TACE) to yield a membrane-associated intermediate fragment called notch extracellular truncation (NEXT). This fragment is then cleaved by presenilin dependent gamma-secretase to release a notch-derived peptide containing the intracellular domain (NICD) from the membrane. Ref.6 Ref.7 Hydroxylated by HIF1AN. |
| Sequence similarities | Belongs to the NOTCH family. Contains 6 ANK repeats. Contains 35 EGF-like domains. Contains 3 LNR (Lin/Notch) repeats. |
Ontologies
Alternative products
| This entry describes 2 isoforms produced by alternative splicing. [Align] [Select] | ||||||
| Isoform 1 (identifier: O35516-1) This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry. | ||||||
| Isoform 2 (identifier: O35516-2) The sequence of this isoform differs from the canonical sequence as follows: 1302-1508: Missing. | ||||||
| Note: No experimental confirmation available. |
Sequence annotation (Features)
| Feature key | Position(s) | Length | Description | Graphical view | Feature identifier | ||||||
Molecule processing | |||||||||||
|---|---|---|---|---|---|---|---|---|---|---|---|
| Signal peptide | 1 – 25 | 25 | Potential | ||||||||
| Chain | 26 – 2470 | 2445 | Neurogenic locus notch homolog protein 2 | PRO_0000007686 | |||||||
| Chain | 1666 – 2470 | 805 | Notch 2 extracellular truncation | PRO_0000007687 | |||||||
| Chain | 1697 – 2470 | 774 | Notch 2 intracellular domain | PRO_0000007688 | |||||||
Regions | |||||||||||
| Topological domain | 26 – 1677 | 1652 | Extracellular Potential | ||||||||
| Transmembrane | 1678 – 1698 | 21 | Helical; Potential | ||||||||
| Topological domain | 1699 – 2470 | 772 | Cytoplasmic Potential | ||||||||
| Domain | 26 – 63 | 38 | EGF-like 1 | ||||||||
| Domain | 64 – 102 | 39 | EGF-like 2 | ||||||||
| Domain | 105 – 143 | 39 | EGF-like 3 | ||||||||
| Domain | 144 – 180 | 37 | EGF-like 4 | ||||||||
| Domain | 182 – 219 | 38 | EGF-like 5; calcium-binding Potential | ||||||||
| Domain | 221 – 256 | 36 | EGF-like 6; incomplete | ||||||||
| Domain | 258 – 294 | 37 | EGF-like 7; calcium-binding Potential | ||||||||
| Domain | 296 – 334 | 39 | EGF-like 8; calcium-binding Potential | ||||||||
| Domain | 336 – 372 | 37 | EGF-like 9; calcium-binding Potential | ||||||||
| Domain | 373 – 411 | 39 | EGF-like 10 | ||||||||
| Domain | 413 – 452 | 40 | EGF-like 11; calcium-binding Potential | ||||||||
| Domain | 454 – 490 | 37 | EGF-like 12; calcium-binding Potential | ||||||||
| Domain | 492 – 528 | 37 | EGF-like 13; calcium-binding Potential | ||||||||
| Domain | 530 – 566 | 37 | EGF-like 14; calcium-binding Potential | ||||||||
| Domain | 568 – 603 | 36 | EGF-like 15; calcium-binding Potential | ||||||||
| Domain | 605 – 641 | 37 | EGF-like 16; calcium-binding Potential | ||||||||
| Domain | 643 – 678 | 36 | EGF-like 17; calcium-binding Potential | ||||||||
| Domain | 680 – 716 | 37 | EGF-like 18; calcium-binding Potential | ||||||||
| Domain | 718 – 753 | 36 | EGF-like 19 | ||||||||
| Domain | 755 – 791 | 37 | EGF-like 20; calcium-binding Potential | ||||||||
| Domain | 793 – 829 | 37 | EGF-like 21; calcium-binding Potential | ||||||||
| Domain | 831 – 869 | 39 | EGF-like 22 | ||||||||
| Domain | 871 – 907 | 37 | EGF-like 23; calcium-binding Potential | ||||||||
| Domain | 909 – 945 | 37 | EGF-like 24; calcium-binding Potential | ||||||||
| Domain | 947 – 983 | 37 | EGF-like 25; calcium-binding Potential | ||||||||
| Domain | 985 – 1021 | 37 | EGF-like 26; calcium-binding Potential | ||||||||
| Domain | 1023 – 1059 | 37 | EGF-like 27; calcium-binding Potential | ||||||||
| Domain | 1061 – 1097 | 37 | EGF-like 28 | ||||||||
| Domain | 1099 – 1145 | 47 | EGF-like 29 | ||||||||
| Domain | 1147 – 1183 | 37 | EGF-like 30; calcium-binding Potential | ||||||||
| Domain | 1185 – 1221 | 37 | EGF-like 31; calcium-binding Potential | ||||||||
| Domain | 1223 – 1260 | 38 | EGF-like 32; calcium-binding Potential | ||||||||
| Domain | 1262 – 1300 | 39 | EGF-like 33 | ||||||||
| Domain | 1302 – 1345 | 44 | EGF-like 34 | ||||||||
| Domain | 1372 – 1410 | 39 | EGF-like 35 | ||||||||
| Repeat | 1423 – 1463 | 41 | LNR 1 | ||||||||
| Repeat | 1464 – 1500 | 37 | LNR 2 | ||||||||
| Repeat | 1501 – 1542 | 42 | LNR 3 | ||||||||
| Repeat | 1825 – 1869 | 45 | ANK 1 | ||||||||
| Repeat | 1874 – 1903 | 30 | ANK 2 | ||||||||
| Repeat | 1907 – 1937 | 31 | ANK 3 | ||||||||
| Repeat | 1941 – 1970 | 30 | ANK 4 | ||||||||
| Repeat | 1974 – 2003 | 30 | ANK 5 | ||||||||
| Repeat | 2007 – 2036 | 30 | ANK 6 | ||||||||
| Region | 1423 – 1677 | 255 | Negative regulatory region (NRR) By similarity | ||||||||
| Compositional bias | 1645 – 1648 | 4 | Poly-Ala | ||||||||
| Compositional bias | 1992 – 1995 | 4 | Poly-Leu | ||||||||
| Compositional bias | 2183 – 2189 | 7 | Poly-Ala | ||||||||
| Compositional bias | 2425 – 2428 | 4 | Poly-Ser | ||||||||
| Compositional bias | 2445 – 2450 | 6 | Poly-Gly | ||||||||
Amino acid modifications | |||||||||||
| Modified residue | 1715 | 1 | Phosphothreonine By similarity | ||||||||
| Modified residue | 1777 | 1 | Phosphoserine Ref.12 | ||||||||
| Modified residue | 1800 | 1 | Phosphothreonine By similarity | ||||||||
| Modified residue | 1802 | 1 | Phosphoserine By similarity | ||||||||
| Modified residue | 1806 | 1 | Phosphothreonine By similarity | ||||||||
| Modified residue | 1843 | 1 | Phosphoserine By similarity | ||||||||
| Modified residue | 2068 | 1 | Phosphoserine By similarity | ||||||||
| Modified residue | 2076 | 1 | Phosphoserine By similarity | ||||||||
| Modified residue | 2079 | 1 | Phosphoserine By similarity | ||||||||
| Modified residue | 2095 | 1 | Phosphothreonine By similarity | ||||||||
| Glycosylation | 46 | 1 | N-linked (GlcNAc...) Potential | ||||||||
| Glycosylation | 155 | 1 | N-linked (GlcNAc...) Potential | ||||||||
| Glycosylation | 731 | 1 | N-linked (GlcNAc...) Potential | ||||||||
| Glycosylation | 1100 | 1 | N-linked (GlcNAc...) Potential | ||||||||
| Glycosylation | 1463 | 1 | N-linked (GlcNAc...) Potential | ||||||||
| Disulfide bond | 28 ↔ 41 | By similarity | |||||||||
| Disulfide bond | 35 ↔ 51 | By similarity | |||||||||
| Disulfide bond | 53 ↔ 62 | By similarity | |||||||||
| Disulfide bond | 68 ↔ 79 | By similarity | |||||||||
| Disulfide bond | 73 ↔ 90 | By similarity | |||||||||
| Disulfide bond | 92 ↔ 101 | By similarity | |||||||||
| Disulfide bond | 109 ↔ 121 | By similarity | |||||||||
| Disulfide bond | 115 ↔ 131 | By similarity | |||||||||
| Disulfide bond | 133 ↔ 142 | By similarity | |||||||||
| Disulfide bond | 148 ↔ 159 | By similarity | |||||||||
| Disulfide bond | 153 ↔ 168 | By similarity | |||||||||
| Disulfide bond | 170 ↔ 179 | By similarity | |||||||||
| Disulfide bond | 186 ↔ 198 | By similarity | |||||||||
| Disulfide bond | 192 ↔ 207 | By similarity | |||||||||
| Disulfide bond | 209 ↔ 218 | By similarity | |||||||||
| Disulfide bond | 228 ↔ 244 | By similarity | |||||||||
| Disulfide bond | 246 ↔ 255 | By similarity | |||||||||
| Disulfide bond | 262 ↔ 273 | By similarity | |||||||||
| Disulfide bond | 267 ↔ 282 | By similarity | |||||||||
| Disulfide bond | 284 ↔ 293 | By similarity | |||||||||
| Disulfide bond | 300 ↔ 313 | By similarity | |||||||||
| Disulfide bond | 307 ↔ 322 | By similarity | |||||||||
| Disulfide bond | 324 ↔ 333 | By similarity | |||||||||
| Disulfide bond | 340 ↔ 351 | By similarity | |||||||||
| Disulfide bond | 345 ↔ 360 | By similarity | |||||||||
| Disulfide bond | 362 ↔ 371 | By similarity | |||||||||
| Disulfide bond | 377 ↔ 388 | By similarity | |||||||||
| Disulfide bond | 382 ↔ 399 | By similarity | |||||||||
| Disulfide bond | 401 ↔ 410 | By similarity | |||||||||
| Disulfide bond | 417 ↔ 431 | By similarity | |||||||||
| Disulfide bond | 425 ↔ 440 | By similarity | |||||||||
| Disulfide bond | 442 ↔ 451 | By similarity | |||||||||
| Disulfide bond | 458 ↔ 469 | By similarity | |||||||||
| Disulfide bond | 463 ↔ 478 | By similarity | |||||||||
| Disulfide bond | 480 ↔ 489 | By similarity | |||||||||
| Disulfide bond | 496 ↔ 507 | By similarity | |||||||||
| Disulfide bond | 501 ↔ 516 | By similarity | |||||||||
| Disulfide bond | 518 ↔ 527 | By similarity | |||||||||
| Disulfide bond | 534 ↔ 545 | By similarity | |||||||||
| Disulfide bond | 539 ↔ 554 | By similarity | |||||||||
| Disulfide bond | 556 ↔ 565 | By similarity | |||||||||
| Disulfide bond | 572 ↔ 582 | By similarity | |||||||||
| Disulfide bond | 577 ↔ 591 | By similarity | |||||||||
| Disulfide bond | 593 ↔ 602 | By similarity | |||||||||
| Disulfide bond | 609 ↔ 620 | By similarity | |||||||||
| Disulfide bond | 614 ↔ 629 | By similarity | |||||||||
| Disulfide bond | 631 ↔ 640 | By similarity | |||||||||
| Disulfide bond | 647 ↔ 657 | By similarity | |||||||||
| Disulfide bond | 652 ↔ 666 | By similarity | |||||||||
| Disulfide bond | 668 ↔ 677 | By similarity | |||||||||
| Disulfide bond | 684 ↔ 695 | By similarity | |||||||||
| Disulfide bond | 689 ↔ 704 | By similarity | |||||||||
| Disulfide bond | 706 ↔ 715 | By similarity | |||||||||
| Disulfide bond | 722 ↔ 732 | By similarity | |||||||||
| Disulfide bond | 727 ↔ 741 | By similarity | |||||||||
| Disulfide bond | 743 ↔ 752 | By similarity | |||||||||
| Disulfide bond | 759 ↔ 770 | By similarity | |||||||||
| Disulfide bond | 764 ↔ 779 | By similarity | |||||||||
| Disulfide bond | 781 ↔ 790 | By similarity | |||||||||
| Disulfide bond | 797 ↔ 808 | By similarity | |||||||||
| Disulfide bond | 802 ↔ 817 | By similarity | |||||||||
| Disulfide bond | 819 ↔ 828 | By similarity | |||||||||
| Disulfide bond | 835 ↔ 846 | By similarity | |||||||||
| Disulfide bond | 840 ↔ 857 | By similarity | |||||||||
| Disulfide bond | 859 ↔ 868 | By similarity | |||||||||
| Disulfide bond | 875 ↔ 886 | By similarity | |||||||||
| Disulfide bond | 880 ↔ 895 | By similarity | |||||||||
| Disulfide bond | 897 ↔ 906 | By similarity | |||||||||
| Disulfide bond | 913 ↔ 924 | By similarity | |||||||||
| Disulfide bond | 918 ↔ 933 | By similarity | |||||||||
| Disulfide bond | 935 ↔ 944 | By similarity | |||||||||
| Disulfide bond | 951 ↔ 962 | By similarity | |||||||||
| Disulfide bond | 956 ↔ 971 | By similarity | |||||||||
| Disulfide bond | 973 ↔ 982 | By similarity | |||||||||
| Disulfide bond | 989 ↔ 1000 | By similarity | |||||||||
| Disulfide bond | 994 ↔ 1009 | By similarity | |||||||||
| Disulfide bond | 1011 ↔ 1020 | By similarity | |||||||||
| Disulfide bond | 1027 ↔ 1038 | By similarity | |||||||||
| Disulfide bond | 1032 ↔ 1047 | By similarity | |||||||||
| Disulfide bond | 1049 ↔ 1058 | By similarity | |||||||||
| Disulfide bond | 1065 ↔ 1076 | By similarity | |||||||||
| Disulfide bond | 1070 ↔ 1085 | By similarity | |||||||||
| Disulfide bond | 1087 ↔ 1096 | By similarity | |||||||||
| Disulfide bond | 1103 ↔ 1124 | By similarity | |||||||||
| Disulfide bond | 1118 ↔ 1133 | By similarity | |||||||||
| Disulfide bond | 1135 ↔ 1144 | By similarity | |||||||||
| Disulfide bond | 1151 ↔ 1162 | By similarity | |||||||||
| Disulfide bond | 1156 ↔ 1171 | By similarity | |||||||||
| Disulfide bond | 1173 ↔ 1182 | By similarity | |||||||||
| Disulfide bond | 1189 ↔ 1200 | By similarity | |||||||||
| Disulfide bond | 1194 ↔ 1209 | By similarity | |||||||||
| Disulfide bond | 1211 ↔ 1220 | By similarity | |||||||||
| Disulfide bond | 1227 ↔ 1239 | By similarity | |||||||||
| Disulfide bond | 1233 ↔ 1248 | By similarity | |||||||||
| Disulfide bond | 1250 ↔ 1259 | By similarity | |||||||||
| Disulfide bond | 1266 ↔ 1279 | By similarity | |||||||||
| Disulfide bond | 1271 ↔ 1288 | By similarity | |||||||||
| Disulfide bond | 1290 ↔ 1299 | By similarity | |||||||||
| Disulfide bond | 1306 ↔ 1317 | By similarity | |||||||||
| Disulfide bond | 1311 ↔ 1329 | By similarity | |||||||||
| Disulfide bond | 1331 ↔ 1344 | By similarity | |||||||||
| Disulfide bond | 1376 ↔ 1387 | By similarity | |||||||||
| Disulfide bond | 1381 ↔ 1398 | By similarity | |||||||||
| Disulfide bond | 1400 ↔ 1409 | By similarity | |||||||||
| Disulfide bond | 1423 ↔ 1446 | By similarity | |||||||||
| Disulfide bond | 1428 ↔ 1441 | By similarity | |||||||||
| Disulfide bond | 1437 ↔ 1453 | By similarity | |||||||||
| Disulfide bond | 1464 ↔ 1487 | By similarity | |||||||||
| Disulfide bond | 1470 ↔ 1482 | By similarity | |||||||||
| Disulfide bond | 1478 ↔ 1494 | By similarity | |||||||||
| Disulfide bond | 1501 ↔ 1525 | By similarity | |||||||||
| Disulfide bond | 1507 ↔ 1520 | By similarity | |||||||||
| Disulfide bond | 1516 ↔ 1532 | By similarity | |||||||||
| Disulfide bond | 1632 ↔ 1639 | By similarity | |||||||||
Natural variations | |||||||||||
| Alternative sequence | 1302 – 1508 | 207 | Missing in isoform 2. | VSP_001405 | |||||||
Experimental info | |||||||||||
| Mutagenesis | 1699 | 1 | M → L: No effect on NICD processing. Ref.6 Ref.7 | ||||||||
| Mutagenesis | 1699 | 1 | M → V: Decreased NICD processing. Ref.6 Ref.7 | ||||||||
| Sequence conflict | 1340 | 1 | L → C in CAA48340. Ref.2 | ||||||||
| Sequence conflict | 1798 | 1 | S → R in AAC52924. Ref.3 | ||||||||
| Sequence conflict | 1901 | 1 | R → A in AAC52924. Ref.3 | ||||||||
| Sequence conflict | 1918 | 1 | G → A in AAC52924. Ref.3 | ||||||||
Sequences
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References
| « Hide 'large scale' references | |
| [1] | "Complete amino acid sequence and mutliform transcripts encoded by a single copy of mouse Notch2 gene." Hamada Y., Higuchi M., Tsujimoto Y. Submitted (JUL-1994) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [MRNA]. Strain: C57BL/6. Tissue: Thymus. |
| [2] | "Motch A and Motch B-two mouse Notch homologues coexpressed in a wide variety of tissues." Lardelli M., Lendahl U. Exp. Cell Res. 204:364-372(1993) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 316-1518. Strain: C57BL/6 X CBA. Tissue: Embryo. |
| [3] | "Inhibition of granulocytic differentiation by mNotch1." Milner L.A., Bigas A., Kopan R., Brashem-Stein C., Bernstein I.D., Martin D.I. Proc. Natl. Acad. Sci. U.S.A. 93:13014-13019(1996) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 1765-2153. |
| [4] | "Mutation in ankyrin repeats of the mouse Notch2 gene induces early embryonic lethality." Hamada Y., Kadokawa Y., Okabe M., Ikawa M., Coleman J.R., Tsujimoto Y. Development 126:3415-3424(1999) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION. |
| [5] | "Differential expression of Notch1 and Notch2 in developing and adult mouse brain." Higuchi M., Kiyama H., Hayakawa T., Hamada Y., Tsujimoto Y. Brain Res. Mol. Brain Res. 29:263-272(1995) [PubMed] [Europe PMC] [Abstract] Cited for: DEVELOPMENTAL STAGE, ALTERNATIVE SPLICING. |
| [6] | "Murine notch homologs (N1-4) undergo presenilin-dependent proteolysis." Saxena M.T., Schroeter E.H., Mumm J.S., Kopan R. J. Biol. Chem. 276:40268-40273(2001) [PubMed] [Europe PMC] [Abstract] Cited for: PROTEOLYTIC PROCESSING, MUTAGENESIS OF MET-1699. |
| [7] | "Conservation of the biochemical mechanisms of signal transduction among mammalian Notch family members." Mizutani T., Taniguchi Y., Aoki T., Hashimoto N., Honjo T. Proc. Natl. Acad. Sci. U.S.A. 98:9026-9031(2001) [PubMed] [Europe PMC] [Abstract] Cited for: PROTEOLYTIC PROCESSING, MUTAGENESIS OF MET-1699. |
| [8] | "Cloning and functional characterization of the murine mastermind-like 1 (Maml1) gene." Wu L., Kobayashi K., Sun T., Gao P., Liu J., Nakamura M., Weisberg E., Mukhopadhyay N.K., Griffin J.D. Gene 328:153-165(2004) [PubMed] [Europe PMC] [Abstract] Cited for: INTERACTION WITH MAML1. |
| [9] | "Asparaginyl hydroxylation of the Notch ankyrin repeat domain by factor inhibiting hypoxia-inducible factor." Coleman M.L., McDonough M.A., Hewitson K.S., Coles C., Mecinovic J., Edelmann M., Cook K.M., Cockman M.E., Lancaster D.E., Kessler B.M., Oldham N.J., Ratcliffe P.J., Schofield C.J. J. Biol. Chem. 282:24027-24038(2007) [PubMed] [Europe PMC] [Abstract] Cited for: INTERACTION WITH HIF1AN. |
| [10] | "The association of Notch2 and NF-kappaB accelerates RANKL-induced osteoclastogenesis." Fukushima H., Nakao A., Okamoto F., Shin M., Kajiya H., Sakano S., Bigas A., Jimi E., Okabe K. Mol. Cell. Biol. 28:6402-6412(2008) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION AS POSITIVE REGULATOR OF OSTEOCLASTOGENESIS, INTERACTION WITH RELA. |
| [11] | "Interaction with factor inhibiting HIF-1 defines an additional mode of cross-coupling between the Notch and hypoxia signaling pathways." Zheng X., Linke S., Dias J.M., Zheng X., Gradin K., Wallis T.P., Hamilton B.R., Gustafsson M., Ruas J.L., Wilkins S., Bilton R.L., Brismar K., Whitelaw M.L., Pereira T., Gorman J.J., Ericson J., Peet D.J., Lendahl U., Poellinger L. Proc. Natl. Acad. Sci. U.S.A. 105:3368-3373(2008) [PubMed] [Europe PMC] [Abstract] Cited for: HYDROXYLATION BY HIF1AN. |
| [12] | "The phagosomal proteome in interferon-gamma-activated macrophages." Trost M., English L., Lemieux S., Courcelles M., Desjardins M., Thibault P. Immunity 30:143-154(2009) [PubMed] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1777, MASS SPECTROMETRY. Tissue: Macrophage. |
| + | Additional computationally mapped references. |
Cross-references
Sequence databases | |
|---|---|
| EMBL GenBank DDBJ | D32210 mRNA. Translation: BAA22094.1. X68279 mRNA. Translation: CAA48340.1. U31881 mRNA. Translation: AAC52924.1. |
| IPI | IPI00467908. IPI00621767. |
| PIR | A49175. |
| RefSeq | NP_035058.2. NM_010928.2. |
| UniGene | Mm.485843. |
3D structure databases | |
| ProteinModelPortal | O35516. |
| SMR | O35516. Positions 27-1341, 1381-1410, 1423-1669, 1777-2061. |
| ModBase | Search... |
Protein-protein interaction databases | |
| DIP | DIP-6008N. |
| IntAct | O35516. 1 interaction. |
PTM databases | |
| PhosphoSite | O35516. |
Proteomic databases | |
| PaxDb | O35516. |
| PRIDE | O35516. |
Protocols and materials databases | |
| StructuralBiologyKnowledgebase | Search... |
Genome annotation databases | |
| GeneID | 18129. |
| KEGG | mmu:18129. |
| UCSC | uc008qpo.1. mouse. |
Organism-specific databases | |
| CTD | 4853. |
| MGI | MGI:97364. Notch2. |
Phylogenomic databases | |
| eggNOG | COG0666. |
| HOGENOM | HOG000234369. |
| HOVERGEN | HBG052650. |
| InParanoid | O35516. |
| KO | K02599. |
| OrthoDB | EOG4Q58NH. |
Enzyme and pathway databases | |
| Reactome | REACT_115202. Signal Transduction. REACT_81380. Receptor-ligand binding initiates the second proteolytic cleavage of Notch receptor. |
Gene expression databases | |
| CleanEx | MM_NOTCH2. |
| Genevestigator | O35516. |
| GermOnline | ENSMUSG00000027878. Mus musculus. |
Family and domain databases | |
| Gene3D | 1.25.40.20. 1 hit. |
| InterPro | IPR002110. Ankyrin_rpt. IPR020683. Ankyrin_rpt-contain_dom. IPR024600. DUF3454_notch. IPR000742. EG-like_dom. IPR001881. EGF-like_Ca-bd. IPR013032. EGF-like_CS. IPR000152. EGF-type_Asp/Asn_hydroxyl_site. IPR018097. EGF_Ca-bd_CS. IPR008297. Notch. IPR022336. Notch_2. IPR000800. Notch_dom. IPR010660. Notch_NOD_dom. IPR011656. Notch_NODP_dom. [Graphical view] |
| Pfam | PF00023. Ank. 3 hits. PF12796. Ank_2. 1 hit. PF11936. DUF3454. 1 hit. PF00008. EGF. 23 hits. PF07645. EGF_CA. 6 hits. PF06816. NOD. 1 hit. PF07684. NODP. 1 hit. PF00066. Notch. 3 hits. [Graphical view] |
| PIRSF | PIRSF002279. Notch. 1 hit. |
| PRINTS | PR01452. LNOTCHREPEAT. PR01985. NOTCH2. |
| SMART | SM00248. ANK. 6 hits. SM00181. EGF. 12 hits. SM00179. EGF_CA. 23 hits. SM00004. NL. 3 hits. [Graphical view] |
| SUPFAM | SSF48403. ANK. 1 hit. SSF90193. Notch_region. 3 hits. |
| PROSITE | PS50297. ANK_REP_REGION. 1 hit. PS50088. ANK_REPEAT. 4 hits. PS00010. ASX_HYDROXYL. 22 hits. PS00022. EGF_1. 33 hits. PS01186. EGF_2. 27 hits. PS50026. EGF_3. 35 hits. PS01187. EGF_CA. 22 hits. PS50258. LNR. 3 hits. [Graphical view] |
| ProtoNet | Search... |
Other | |
| ChiTaRS | NOTCH2. mouse. |
| NextBio | 293360. |
| SOURCE | Search... |
Entry information
| Entry name | NOTC2_MOUSE | ||||||||
| Accession | Primary (citable) accession number: O35516 Secondary accession number(s): Q06008, Q60941 | ||||||||
| Entry history |
| ||||||||
| Entry status | Reviewed (UniProtKB/Swiss-Prot) | ||||||||
| Annotation program | Chordata Protein Annotation Program | ||||||||
Relevant documents
| MGD cross-references Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot |
| SIMILARITY comments Index of protein domains and families |