GenomeNet

Database: UniProt
Entry: Q01705
LinkDB: Q01705
Original site: Q01705 
ID   NOTC1_MOUSE             Reviewed;        2531 AA.
AC   Q01705; Q06007; Q3TZW2; Q3U3Y2; Q61905; Q7TQ50; Q7TQ51; Q7TQ52;
AC   Q8K428; Q99JC2; Q9QW58; Q9R0X7;
DT   01-NOV-1995, integrated into UniProtKB/Swiss-Prot.
DT   18-APR-2012, sequence version 3.
DT   10-APR-2019, entry version 213.
DE   RecName: Full=Neurogenic locus notch homolog protein 1;
DE            Short=Notch 1;
DE   AltName: Full=Motch A {ECO:0000303|PubMed:8440332};
DE   AltName: Full=mT14;
DE   AltName: Full=p300;
DE   Contains:
DE     RecName: Full=Notch 1 extracellular truncation {ECO:0000303|PubMed:10882062};
DE              Short=NEXT {ECO:0000303|PubMed:10882062};
DE   Contains:
DE     RecName: Full=Notch 1 intracellular domain;
DE              Short=NICD;
DE   Flags: Precursor;
GN   Name=Notch1; Synonyms=Motch {ECO:0000303|PubMed:8440332};
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
RC   TISSUE=Embryo;
RX   PubMed=8449489; DOI=10.1006/geno.1993.1055;
RA   Franco del Amo F., Gendron-Maguire M., Swiatek P.J., Jenkins N.A.,
RA   Copeland N.G., Gridley T.;
RT   "Cloning, analysis, and chromosomal localization of Notch-1, a mouse
RT   homolog of Drosophila Notch.";
RL   Genomics 15:259-264(1993).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
RC   STRAIN=BALB/cJ; TISSUE=Thymus;
RX   PubMed=7956822;
RA   Nye J.S., Kopan R., Axel R.;
RT   "An activated Notch suppresses neurogenesis and myogenesis but not
RT   gliogenesis in mammalian cells.";
RL   Development 120:2421-2430(1994).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
RC   STRAIN=BALB/cJ; TISSUE=Thymus;
RX   PubMed=12123574; DOI=10.1016/S0960-9822(02)00888-6;
RA   Foltz D.R., Santiago M.C., Berechid B.E., Nye J.S.;
RT   "Glycogen synthase kinase-3beta modulates notch signaling and
RT   stability.";
RL   Curr. Biol. 12:1006-1011(2002).
RN   [4]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=CB-17/SCID; TISSUE=Thymus;
RX   PubMed=12807718; DOI=10.1093/carcin/bgg071;
RA   Tsuji H., Ishii-Ohba H., Ukai H., Katsube T., Ogiu T.;
RT   "Radiation-induced deletions in the 5' end region of Notch1 lead to
RT   the formation of truncated proteins and are involved in the
RT   development of mouse thymic lymphomas.";
RL   Carcinogenesis 24:1257-1268(2003).
RN   [5]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=C57BL/6J;
RX   PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA   Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S.,
RA   She X., Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W.,
RA   Kapustin Y., Meric P., Maglott D., Birtle Z., Marques A.C., Graves T.,
RA   Zhou S., Teague B., Potamousis K., Churas C., Place M., Herschleb J.,
RA   Runnheim R., Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z.,
RA   Lindblad-Toh K., Eichler E.E., Ponting C.P.;
RT   "Lineage-specific biology revealed by a finished genome assembly of
RT   the mouse.";
RL   PLoS Biol. 7:E1000112-E1000112(2009).
RN   [6]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA   Mural R.J., Adams M.D., Myers E.W., Smith H.O., Venter J.C.;
RL   Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN   [7]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC   TISSUE=Brain;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [8]
RP   NUCLEOTIDE SEQUENCE [MRNA] OF 731-1899 (ISOFORM 2), AND DEVELOPMENTAL
RP   STAGE.
RC   STRAIN=CD-1; TISSUE=Embryo;
RX   PubMed=1426644; DOI=10.1016/0012-1606(92)90076-S;
RA   Reaume A.G., Conlon R.A., Zirngibl R., Yamaguchi T.P., Rossant J.;
RT   "Expression analysis of a Notch homologue in the mouse embryo.";
RL   Dev. Biol. 154:377-387(1992).
RN   [9]
RP   NUCLEOTIDE SEQUENCE [MRNA] OF 1161-1547.
RC   STRAIN=C57BL/6 X CBA; TISSUE=Embryo;
RX   PubMed=8440332; DOI=10.1006/excr.1993.1044;
RA   Lardelli M., Lendahl U.;
RT   "Motch A and Motch B-two mouse Notch homologues coexpressed in a wide
RT   variety of tissues.";
RL   Exp. Cell Res. 204:364-372(1993).
RN   [10]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1373-2531.
RC   STRAIN=NOD;
RX   PubMed=16141072; DOI=10.1126/science.1112014;
RA   Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA   Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA   Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
RA   Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
RA   Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
RA   Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
RA   Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
RA   Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
RA   di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
RA   Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
RA   Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
RA   Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
RA   Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
RA   Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
RA   Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
RA   Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
RA   Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
RA   Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
RA   Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
RA   Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
RA   Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
RA   Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA   Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA   Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
RA   Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
RA   Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
RA   Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
RA   Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
RA   Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
RA   Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
RA   Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
RA   Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
RA   Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
RA   Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
RA   Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
RA   Hayashizaki Y.;
RT   "The transcriptional landscape of the mammalian genome.";
RL   Science 309:1559-1563(2005).
RN   [11]
RP   NUCLEOTIDE SEQUENCE [MRNA] OF 1551-1647 (ISOFORM 1), AND DEVELOPMENTAL
RP   STAGE.
RC   TISSUE=Embryo;
RX   PubMed=1425352;
RA   Franco del Amo F., Smith D.E., Swiatek P.J., Gendron-Maguire M.,
RA   Greenspan R.J., McMahon A.P., Gridley T.;
RT   "Expression pattern of Motch, a mouse homolog of Drosophila Notch,
RT   suggests an important role in early postimplantation mouse
RT   development.";
RL   Development 115:737-744(1992).
RN   [12]
RP   PROTEIN SEQUENCE OF 1655-1659, CLEAVAGE BY FURIN-LIKE CONVERTASE, AND
RP   MUTAGENESIS OF 1651-ARG--ARG-1654.
RX   PubMed=9653148; DOI=10.1073/pnas.95.14.8108;
RA   Logeat F., Bessia C., Brou C., LeBail O., Jarriault S., Seidah N.G.,
RA   Israel A.;
RT   "The Notch1 receptor is cleaved constitutively by a furin-like
RT   convertase.";
RL   Proc. Natl. Acad. Sci. U.S.A. 95:8108-8112(1998).
RN   [13]
RP   NUCLEOTIDE SEQUENCE [MRNA] OF 1659-1673.
RX   PubMed=10437788; DOI=10.1016/S0014-5793(99)00901-1;
RA   Lee J.S., Ishimoto A., Yanagawa S.;
RT   "Murine leukemia provirus-mediated activation of the Notch1 gene leads
RT   to induction of HES-1 in a mouse T lymphoma cell line, DL-3.";
RL   FEBS Lett. 455:276-280(1999).
RN   [14]
RP   NUCLEOTIDE SEQUENCE [MRNA] OF 1865-2076, AND DEVELOPMENTAL STAGE IN
RP   HAIR FOLLICLES.
RX   PubMed=8486742; DOI=10.1083/jcb.121.3.631;
RA   Kopan R., Weintraub H.;
RT   "Mouse notch: expression in hair follicles correlates with cell fate
RT   determination.";
RL   J. Cell Biol. 121:631-641(1993).
RN   [15]
RP   PROTEIN SEQUENCE OF 1937-1952 AND 1995-2019, FUNCTION, INTERACTION
RP   WITH HIF1AN, HYDROXYLATION AT ASN-1945 AND ASN-2012 BY HIF1AN,
RP   MUTAGENESIS OF ASN-1945 AND ASN-2012, AND IDENTIFICATION BY MASS
RP   SPECTROMETRY.
RX   PubMed=18299578; DOI=10.1073/pnas.0711591105;
RA   Zheng X., Linke S., Dias J.M., Zheng X., Gradin K., Wallis T.P.,
RA   Hamilton B.R., Gustafsson M., Ruas J.L., Wilkins S., Bilton R.L.,
RA   Brismar K., Whitelaw M.L., Pereira T., Gorman J.J., Ericson J.,
RA   Peet D.J., Lendahl U., Poellinger L.;
RT   "Interaction with factor inhibiting HIF-1 defines an additional mode
RT   of cross-coupling between the Notch and hypoxia signaling pathways.";
RL   Proc. Natl. Acad. Sci. U.S.A. 105:3368-3373(2008).
RN   [16]
RP   NUCLEOTIDE SEQUENCE [MRNA] OF 1951-2201.
RX   PubMed=9384671;
RA   Messerle M., Follo M., Nehls M., Eggert H., Boehm T.;
RT   "Dynamic changes in gene expression during in vitro differentiation of
RT   mouse embryonic stem cells.";
RL   Cytokines Cell. Mol. Ther. 1:139-143(1995).
RN   [17]
RP   SUBCELLULAR LOCATION, PROTEOLYTIC PROCESSING, AND MUTAGENESIS OF
RP   CYS-1675 AND CYS-1682.
RX   PubMed=10882062;
RA   Mumm J.S., Schroeter E.H., Saxena M.T., Griesemer A., Tian X.,
RA   Pan D.J., Ray W.J., Kopan R.;
RT   "A ligand-induced extracellular cleavage regulates gamma-secretase-
RT   like proteolytic activation of Notch1.";
RL   Mol. Cell 5:197-206(2000).
RN   [18]
RP   PROTEOLYTIC PROCESSING.
RX   PubMed=10882063; DOI=10.1016/S1097-2765(00)80417-7;
RA   Brou C., Logeat F., Gupta N., Bessia C., LeBail O., Doedens J.R.,
RA   Cumano A., Roux P., Black R.A., Israel A.;
RT   "A novel proteolytic cleavage involved in Notch signaling: the role of
RT   the disintegrin-metalloprotease TACE.";
RL   Mol. Cell 5:207-216(2000).
RN   [19]
RP   PARTIAL PROTEIN SEQUENCE, AND PROTEOLYTIC PROCESSING.
RX   PubMed=11518718; DOI=10.1074/jbc.M107234200;
RA   Saxena M.T., Schroeter E.H., Mumm J.S., Kopan R.;
RT   "Murine notch homologs (N1-4) undergo presenilin-dependent
RT   proteolysis.";
RL   J. Biol. Chem. 276:40268-40273(2001).
RN   [20]
RP   PROTEOLYTIC PROCESSING.
RX   PubMed=11459941; DOI=10.1073/pnas.161269998;
RA   Mizutani T., Taniguchi Y., Aoki T., Hashimoto N., Honjo T.;
RT   "Conservation of the biochemical mechanisms of signal transduction
RT   among mammalian Notch family members.";
RL   Proc. Natl. Acad. Sci. U.S.A. 98:9026-9031(2001).
RN   [21]
RP   INTERACTION WITH DTX1 AND DTX2.
RX   PubMed=11226752; DOI=10.1016/S0736-5748(00)00071-X;
RA   Kishi N., Tang Z., Maeda Y., Hirai A., Mo R., Ito M., Suzuki S.,
RA   Nakao K., Kinoshita T., Kadesch T., Hui C.-C., Artavanis-Tsakonas S.,
RA   Okano H., Matsuno K.;
RT   "Murine homologs of deltex define a novel gene family involved in
RT   vertebrate Notch signaling and neurogenesis.";
RL   Int. J. Dev. Neurosci. 19:21-35(2001).
RN   [22]
RP   INTERACTION WITH CCN3.
RX   PubMed=12050162; DOI=10.1074/jbc.M203727200;
RA   Sakamoto K., Yamaguchi S., Ando R., Miyawaki A., Kabasawa Y.,
RA   Takagi M., Li C.L., Perbal B., Katsube K.;
RT   "The nephroblastoma overexpressed gene (NOV/ccn3) protein associates
RT   with Notch1 extracellular domain and inhibits myoblast differentiation
RT   via Notch signaling pathway.";
RL   J. Biol. Chem. 277:29399-29405(2002).
RN   [23]
RP   INTERACTION WITH MAML1.
RX   PubMed=15019995; DOI=10.1016/j.gene.2003.12.007;
RA   Wu L., Kobayashi K., Sun T., Gao P., Liu J., Nakamura M., Weisberg E.,
RA   Mukhopadhyay N.K., Griffin J.D.;
RT   "Cloning and functional characterization of the murine mastermind-like
RT   1 (Maml1) gene.";
RL   Gene 328:153-165(2004).
RN   [24]
RP   UBIQUITINATION AT LYS-1749, AND ENDOCYTOSIS.
RX   PubMed=15240571; DOI=10.1083/jcb.200310098;
RA   Gupta-Rossi N., Six E., LeBail O., Logeat F., Chastagner P., Olry A.,
RA   Israel A., Brou C.;
RT   "Monoubiquitination and endocytosis direct gamma-secretase cleavage of
RT   activated Notch receptor.";
RL   J. Cell Biol. 166:73-83(2004).
RN   [25]
RP   INTERACTION WITH DNER, FUNCTION, AND TISSUE SPECIFICITY.
RX   PubMed=15965470; DOI=10.1038/nn1492;
RA   Eiraku M., Tohgo A., Ono K., Kaneko M., Fujishima K., Hirano T.,
RA   Kengaku M.;
RT   "DNER acts as a neuron-specific Notch ligand during Bergmann glial
RT   development.";
RL   Nat. Neurosci. 8:873-880(2005).
RN   [26]
RP   UBIQUITINATION BY ITCH.
RX   PubMed=18628966; DOI=10.1371/journal.pone.0002735;
RA   Chastagner P., Israel A., Brou C.;
RT   "AIP4/Itch regulates Notch receptor degradation in the absence of
RT   ligand.";
RL   PLoS ONE 3:E2735-E2735(2008).
RN   [27]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-1851, AND IDENTIFICATION
RP   BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   TISSUE=Pancreas;
RX   PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA   Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA   Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT   "A tissue-specific atlas of mouse protein phosphorylation and
RT   expression.";
RL   Cell 143:1174-1189(2010).
RN   [28]
RP   INTERACTION WITH AAK1.
RX   PubMed=21464124; DOI=10.1074/jbc.M110.190769;
RA   Gupta-Rossi N., Ortica S., Meas-Yedid V., Heuss S., Moretti J.,
RA   Olivo-Marin J.C., Israel A.;
RT   "The adaptor-associated kinase 1, AAK1, is a positive regulator of the
RT   Notch pathway.";
RL   J. Biol. Chem. 286:18720-18730(2011).
RN   [29]
RP   GLYCOSYLATION AT SER-65; THR-73; THR-116; SER-146; THR-194; SER-341;
RP   SER-378; SER-458; THR-466; SER-496; SER-534; SER-609; SER-647;
RP   SER-722; SER-759; THR-767; SER-797; THR-805; SER-951; SER-1027;
RP   THR-1035; SER-1065; SER-1189; THR-1197; SER-1273 AND THR-1362, AND
RP   MUTAGENESIS OF SER-65; SER-146; SER-341; SER-378; SER-458; SER-496;
RP   SER-534; SER-609; SER-647; SER-722; SER-759; SER-797; SER-951;
RP   SER-1027; SER-1065; SER-1189 AND SER-1273.
RX   PubMed=21757702; DOI=10.1074/jbc.M111.268243;
RA   Rana N.A., Nita-Lazar A., Takeuchi H., Kakuda S., Luther K.B.,
RA   Haltiwanger R.S.;
RT   "O-glucose trisaccharide is present at high but variable stoichiometry
RT   at multiple sites on mouse Notch1.";
RL   J. Biol. Chem. 286:31623-31637(2011).
RN   [30]
RP   FUNCTION AS NEUROGENESIS REPRESSOR, AND INTERACTION WITH BCL6.
RX   PubMed=23160044; DOI=10.1038/nn.3264;
RA   Tiberi L., van den Ameele J., Dimidschstein J., Piccirilli J.,
RA   Gall D., Herpoel A., Bilheu A., Bonnefont J., Iacovino M., Kyba M.,
RA   Bouschet T., Vanderhaeghen P.;
RT   "BCL6 controls neurogenesis through Sirt1-dependent epigenetic
RT   repression of selective Notch targets.";
RL   Nat. Neurosci. 15:1627-1635(2012).
RN   [31]
RP   UBIQUITINATION BY ITCH.
RX   PubMed=23886940; DOI=10.1242/jcs.130500;
RA   Puca L., Chastagner P., Meas-Yedid V., Israel A., Brou C.;
RT   "Alpha-arrestin 1 (ARRDC1) and beta-arrestins cooperate to mediate
RT   Notch degradation in mammals.";
RL   J. Cell Sci. 126:4457-4468(2013).
RN   [32]
RP   FUNCTION, AND INTERACTION WITH THBS4.
RX   PubMed=23615612; DOI=10.1038/nature12069;
RA   Benner E.J., Luciano D., Jo R., Abdi K., Paez-Gonzalez P., Sheng H.,
RA   Warner D.S., Liu C., Eroglu C., Kuo C.T.;
RT   "Protective astrogenesis from the SVZ niche after injury is controlled
RT   by Notch modulator Thbs4.";
RL   Nature 497:369-373(2013).
RN   [33]
RP   INTERACTION WITH PRAG1, AND INTERACTION WITH PRAG1 AND MAML1.
RX   PubMed=25038227; DOI=10.1158/0008-5472.CAN-14-1547;
RA   Weaver K.L., Alves-Guerra M.C., Jin K., Wang Z., Han X.,
RA   Ranganathan P., Zhu X., DaSilva T., Liu W., Ratti F., Demarest R.M.,
RA   Tzimas C., Rice M., Vasquez-Del Carpio R., Dahmane N., Robbins D.J.,
RA   Capobianco A.J.;
RT   "NACK is an integral component of the Notch transcriptional activation
RT   complex and is critical for development and tumorigenesis.";
RL   Cancer Res. 74:4741-4751(2014).
RN   [34]
RP   GLYCOSYLATION AT THR-73; THR-116; THR-194; THR-232; THR-311; THR-349;
RP   SER-458; THR-466; THR-617; THR-692; SER-759; THR-767; SER-784;
RP   SER-797; THR-805; THR-900; SER-921; THR-997; THR-1035; THR-1159;
RP   THR-1197; THR-1362; THR-1379 AND THR-1402, MUTAGENESIS OF THR-232;
RP   THR-311; THR-349; THR-466; THR-997; THR-1035; THR-1159; THR-1362 AND
RP   THR-1402, AND INTERACTION WITH DLL1 AND JAG1.
RX   PubMed=28089369; DOI=10.1016/j.devcel.2016.12.013;
RA   Kakuda S., Haltiwanger R.S.;
RT   "Deciphering the fringe-mediated notch code: identification of
RT   activating and inhibiting sites allowing discrimination between
RT   ligands.";
RL   Dev. Cell 40:193-201(2017).
RN   [35]
RP   SUBCELLULAR LOCATION, AND INTERACTION WITH MEGF10.
RX   PubMed=28498977; DOI=10.1093/hmg/ddx189;
RA   Saha M., Mitsuhashi S., Jones M.D., Manko K., Reddy H.M., Bruels C.,
RA   Cho K.A., Pacak C.A., Draper I., Kang P.B.;
RT   "Consequences of MEGF10 deficiency on myoblast function and Notch1
RT   interactions.";
RL   Hum. Mol. Genet. 26:2984-3000(2017).
RN   [36]
RP   GLYCOSYLATION AT SER-435, AND MUTAGENESIS OF THR-311 AND SER-435.
RX   PubMed=30127001; DOI=10.1073/pnas.1804005115;
RA   Takeuchi H., Schneider M., Williamson D.B., Ito A., Takeuchi M.,
RA   Handford P.A., Haltiwanger R.S.;
RT   "Two novel protein O-glucosyltransferases that modify sites distinct
RT   from POGLUT1 and affect Notch trafficking and signaling.";
RL   Proc. Natl. Acad. Sci. U.S.A. 115:E8395-E8402(2018).
RN   [37]
RP   X-RAY CRYSTALLOGRAPHY (2.2 ANGSTROMS) OF 1971-2104.
RX   PubMed=15802643; DOI=10.1110/ps.041184105;
RA   Lubman O.Y., Kopan R., Waksman G., Korolev S.;
RT   "The crystal structure of a partial mouse Notch-1 ankyrin domain:
RT   repeats 4 through 7 preserve an ankyrin fold.";
RL   Protein Sci. 14:1274-1281(2005).
RN   [38]
RP   X-RAY CRYSTALLOGRAPHY (2.35 ANGSTROMS) OF 1899-2106 IN COMPLEX WITH
RP   HIF1AN; IRON AND 2-OXOGLUTARATE, HYDROXYLATION AT ASN-1945 AND
RP   ASN-2012, MUTAGENESIS OF ASN-1945 AND ASN-2012, AND IDENTIFICATION BY
RP   MASS SPECTROMETRY.
RX   PubMed=17573339; DOI=10.1074/jbc.M704102200;
RA   Coleman M.L., McDonough M.A., Hewitson K.S., Coles C., Mecinovic J.,
RA   Edelmann M., Cook K.M., Cockman M.E., Lancaster D.E., Kessler B.M.,
RA   Oldham N.J., Ratcliffe P.J., Schofield C.J.;
RT   "Asparaginyl hydroxylation of the Notch ankyrin repeat domain by
RT   factor inhibiting hypoxia-inducible factor.";
RL   J. Biol. Chem. 282:24027-24038(2007).
CC   -!- FUNCTION: Functions as a receptor for membrane-bound ligands
CC       Jagged-1 (JAG1), Jagged-2 (JAG2) and Delta-1 (DLL1) to regulate
CC       cell-fate determination. Upon ligand activation through the
CC       released notch intracellular domain (NICD) it forms a
CC       transcriptional activator complex with RBPJ/RBPSUH and activates
CC       genes of the enhancer of split locus. Affects the implementation
CC       of differentiation, proliferation and apoptotic programs. Involved
CC       in angiogenesis; negatively regulates endothelial cell
CC       proliferation and migration and angiogenic sprouting. Involved in
CC       the maturation of both CD4(+) and CD8(+) cells in the thymus.
CC       Important for follicular differentiation and possibly cell fate
CC       selection within the follicle. During cerebellar development,
CC       functions as a receptor for neuronal DNER and is involved in the
CC       differentiation of Bergmann glia. Represses neuronal and myogenic
CC       differentiation. May play an essential role in postimplantation
CC       development, probably in some aspect of cell specification and/or
CC       differentiation. May be involved in mesoderm development, somite
CC       formation and neurogenesis. May enhance HIF1A function by
CC       sequestering HIF1AN away from HIF1A. Required for the THBS4
CC       function in regulating protective astrogenesis from the
CC       subventricular zone (SVZ) niche after injury. Involved in
CC       determination of left/right symmetry by modulating the balance
CC       between motile and immotile (sensory) cilia at the left-right
CC       organiser (LRO). {ECO:0000269|PubMed:15965470,
CC       ECO:0000269|PubMed:18299578, ECO:0000269|PubMed:23160044,
CC       ECO:0000269|PubMed:23615612}.
CC   -!- SUBUNIT: Heterodimer of a C-terminal fragment N(TM) and an N-
CC       terminal fragment N(EC) which are probably linked by disulfide
CC       bonds. Interacts with DNER, DTX1, DTX2 and RBPJ/RBPSUH. Also
CC       interacts with MAML1, MAML2 and MAML3 which act as transcriptional
CC       coactivators for NOTCH1. Notch 1 intracellular domain interacts
CC       with SNW1; the interaction involves multimerized NOTCH1 NICD and
CC       is implicated in a formation of an intermediate preactivation
CC       complex which associates with DNA-bound CBF-1/RBPJ. The activated
CC       membrane-bound form interacts with AAK1 which promotes NOTCH1
CC       stabilization. Forms a trimeric complex with FBXW7 and SGK1.
CC       Interacts with HIF1AN. HIF1AN negatively regulates the function of
CC       notch intracellular domain (NICD), accelerating myogenic
CC       differentiation. Interacts (via NICD) with SNAI1 (via zinc
CC       fingers); the interaction induces SNAI1 degradation via MDM2-
CC       mediated ubiquitination and inhibits SNAI1-induced cell invasion.
CC       Interacts (via NICD) with MDM2A. Interacts (via NICD) with BCL6;
CC       the interaction decreases MAML1 recruitment by NOTCH1 NICD on
CC       target genes DNA and inhibits NOTCH1 transcractivation activity.
CC       Interacts with THBS4. Interacts (via the EGF-like repeat region)
CC       with CCN3 (via CTCK domain) (PubMed:12050162). Interacts (via EGF-
CC       like domains) with DLL4 (via N-terminal DSL and MNNL domains) (By
CC       similarity). Interacts with ZMIZ1. Interacts (via NICD domain)
CC       with MEGF10 (via the cytoplasmic domain) (PubMed:28498977).
CC       Interacts with DLL1 and JAG1 (PubMed:28089369). Interacts (via
CC       NICD domain) with PRAG1 (PubMed:25038227). Forms a complex with
CC       PRAG1, N1ICD and MAML1, in a MAML1-dependent manner
CC       (PubMed:25038227). Interacts (via transmembrane region) with
CC       PSEN1; the interaction is direct (By similarity).
CC       {ECO:0000250|UniProtKB:P46531, ECO:0000250|UniProtKB:Q07008,
CC       ECO:0000269|PubMed:11226752, ECO:0000269|PubMed:12050162,
CC       ECO:0000269|PubMed:15019995, ECO:0000269|PubMed:15965470,
CC       ECO:0000269|PubMed:17573339, ECO:0000269|PubMed:18299578,
CC       ECO:0000269|PubMed:21464124, ECO:0000269|PubMed:23160044,
CC       ECO:0000269|PubMed:23615612, ECO:0000269|PubMed:25038227,
CC       ECO:0000269|PubMed:28089369, ECO:0000269|PubMed:28498977}.
CC   -!- INTERACTION:
CC       Q77CA8:LRORF2 (xeno); NbExp=3; IntAct=EBI-11292892, EBI-11292862;
CC       Q06330:RBPJ (xeno); NbExp=3; IntAct=EBI-1392707, EBI-632552;
CC       P31266:Rbpj; NbExp=8; IntAct=EBI-1392707, EBI-1392666;
CC       Q3TKT4:Smarca4; NbExp=2; IntAct=EBI-1392707, EBI-1210244;
CC       Q6P9Z1:Smarcd3; NbExp=2; IntAct=EBI-1392707, EBI-7525857;
CC       P28159:Su(H) (xeno); NbExp=3; IntAct=EBI-1392707, EBI-92180;
CC       P62991:Ubc; NbExp=3; IntAct=EBI-1392707, EBI-413074;
CC   -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:10882062,
CC       ECO:0000269|PubMed:28498977}; Single-pass type I membrane protein.
CC   -!- SUBCELLULAR LOCATION: Notch 1 intracellular domain: Nucleus
CC       {ECO:0000269|PubMed:28498977}. Note=Following proteolytical
CC       processing NICD is translocated to the nucleus. Nuclear location
CC       may require MEGF10. {ECO:0000269|PubMed:28498977}.
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=4;
CC       Name=1;
CC         IsoId=Q01705-1; Sequence=Displayed;
CC       Name=2;
CC         IsoId=Q01705-2; Sequence=VSP_001402, VSP_001403, VSP_001404;
CC         Note=No experimental confirmation available.;
CC       Name=3;
CC         IsoId=Q01705-3; Sequence=VSP_043064;
CC         Note=No experimental confirmation available.;
CC       Name=4;
CC         IsoId=Q01705-4; Sequence=VSP_043065;
CC         Note=No experimental confirmation available.;
CC   -!- TISSUE SPECIFICITY: Highly expressed in the brain, lung and
CC       thymus. Expressed at lower levels in the spleen, bone-marrow,
CC       spinal cord, eyes, mammary gland, liver, intestine, skeletal
CC       muscle, kidney and heart. In the hair follicle, highly expressed
CC       exclusively in the epithelial compartment.
CC       {ECO:0000269|PubMed:15965470}.
CC   -!- DEVELOPMENTAL STAGE: First detected in the mesoderm at 7.5 dpc By
CC       8.5 dpc highly expressed in presomitic mesoderm, mesenchyme and
CC       endothelial cells, while much lower levels are seen in the
CC       neuroepithelium. Between 9.5-10.5 dpc expressed at high levels in
CC       the neuroepithelium. At 13.5 dpc expressed in the surface
CC       ectoderm, eye and developing whisker follicles. Hair follicle
CC       matrix cells expression starts as different cell types become
CC       distinguishable in the developing follicle. Expression persists
CC       throughout the growth phase of the follicle and maintains the same
CC       expression profile in the second hair cycle. The cells in the
CC       follicle that undergo a phase of high level expression are in
CC       transition from mitotic precursors to several discrete,
CC       differentiating cell types. Specifically expressed in cerebellar
CC       Bergmann glial cells during postnatal development.
CC       {ECO:0000269|PubMed:1425352, ECO:0000269|PubMed:1426644,
CC       ECO:0000269|PubMed:8486742}.
CC   -!- DOMAIN: Interaction with PSEN1 causes partial unwinding of the
CC       transmembrane helix, facilitating access to the scissile peptide
CC       bond. {ECO:0000250|UniProtKB:P46531}.
CC   -!- PTM: Synthesized in the endoplasmic reticulum as an inactive form
CC       which is proteolytically cleaved by a furin-like convertase in the
CC       trans-Golgi network before it reaches the plasma membrane to yield
CC       an active, ligand-accessible form (PubMed:10882062,
CC       PubMed:10882063). Cleavage results in a C-terminal fragment N(TM)
CC       and a N-terminal fragment N(EC). Following ligand binding, it is
CC       cleaved by ADAM17 to yield a membrane-associated intermediate
CC       fragment called notch extracellular truncation (NEXT)
CC       (PubMed:10882062, PubMed:10882063). Following endocytosis, this
CC       fragment is then cleaved by one of the catalytic subunits of
CC       gamma-secretase (PSEN1 or PSEN2) to release a Notch-derived
CC       peptide containing the intracellular domain (NICD) from the
CC       membrane (PubMed:10882062, PubMed:11518718, PubMed:11459941).
CC       {ECO:0000269|PubMed:10882062, ECO:0000269|PubMed:10882063,
CC       ECO:0000269|PubMed:11459941, ECO:0000269|PubMed:11518718}.
CC   -!- PTM: Phosphorylated.
CC   -!- PTM: O-linked glycosylation by GALNT11 is involved in
CC       determination of left/right symmetry: glycosylation promotes
CC       activation of NOTCH1, possibly by promoting cleavage by ADAM17,
CC       modulating the balance between motile and immotile (sensory) cilia
CC       at the left-right organiser (LRO) (By similarity). O-glycosylated
CC       on the EGF-like domains (PubMed:21757702). O-glucosylated at Ser-
CC       435 by KDELC1 and KDELC2 (PubMed:30127001). Contains both O-linked
CC       fucose and O-linked glucose in the EGF-like domains 11, 12 and 13,
CC       which are interacting with the residues on DLL4 (By similarity).
CC       O-glycosylation at Ser-1027 is only partial (PubMed:21757702).
CC       MFNG-, RFNG- and LFNG-mediated modification of O-fucose residues
CC       at specific EGF-like domains results in inhibition of its
CC       activation by JAG1 and enhancement of its activation by DLL1 via
CC       an increased binding to DLL1 (PubMed:28089369).
CC       {ECO:0000250|UniProtKB:P46531, ECO:0000250|UniProtKB:Q07008,
CC       ECO:0000269|PubMed:21757702, ECO:0000269|PubMed:28089369,
CC       ECO:0000269|PubMed:30127001}.
CC   -!- PTM: Ubiquitinated. Undergoes 'Lys-29'-linked polyubiquitination
CC       by ITCH; promotes the lysosomal degradation of non-activated
CC       internalized NOTCH1 (PubMed:18628966, PubMed:23886940).
CC       Monoubiquitination at Lys-1749 is required for activation by
CC       gamma-secretase cleavage, it promotes interaction with AAK1, which
CC       stabilizes it. Deubiquitination by EIF3F is necessary for nuclear
CC       import of activated Notch (PubMed:15240571).
CC       {ECO:0000269|PubMed:15240571, ECO:0000269|PubMed:18628966,
CC       ECO:0000269|PubMed:23886940}.
CC   -!- PTM: Hydroxylated at Asn-1945 and Asn-2012 by HIF1AN.
CC       Hydroxylation reduces affinity for HI1AN and may thus indirectly
CC       modulate negative regulation of NICD.
CC       {ECO:0000269|PubMed:17573339, ECO:0000269|PubMed:18299578}.
CC   -!- SIMILARITY: Belongs to the NOTCH family. {ECO:0000305}.
DR   EMBL; Z11886; CAA77941.1; -; mRNA.
DR   EMBL; AF508809; AAM28905.1; -; mRNA.
DR   EMBL; AB100603; BAC77038.1; -; Genomic_DNA.
DR   EMBL; AB100603; BAC77039.1; -; Genomic_DNA.
DR   EMBL; AB100603; BAC77040.1; -; Genomic_DNA.
DR   EMBL; AL732541; CAM20304.1; -; Genomic_DNA.
DR   EMBL; CH466542; EDL08321.1; -; Genomic_DNA.
DR   EMBL; BC138441; AAI38442.1; -; mRNA.
DR   EMBL; BC138442; AAI38443.1; -; mRNA.
DR   EMBL; L02613; AAK14898.1; -; mRNA.
DR   EMBL; X68278; CAA48339.1; -; mRNA.
DR   EMBL; AK154528; BAE32653.1; -; mRNA.
DR   EMBL; AK157475; BAE34095.1; -; mRNA.
DR   EMBL; AJ238029; CAB40733.1; -; mRNA.
DR   EMBL; X82562; CAA57909.1; -; mRNA.
DR   CCDS; CCDS15806.1; -. [Q01705-1]
DR   PIR; A46438; A46438.
DR   PIR; B49175; B49175.
DR   RefSeq; NP_032740.3; NM_008714.3. [Q01705-1]
DR   UniGene; Mm.290610; -.
DR   PDB; 1YMP; X-ray; 2.20 A; A/B=1971-2105.
DR   PDB; 2QC9; X-ray; 2.35 A; A/B=1899-2106.
DR   PDB; 2RQZ; NMR; -; A=452-489.
DR   PDB; 2RR0; NMR; -; A=452-489.
DR   PDB; 2RR2; NMR; -; A=452-489.
DR   PDB; 3P3N; X-ray; 2.40 A; B=1930-1949.
DR   PDB; 3P3P; X-ray; 2.60 A; B=1999-2016.
DR   PDB; 5KY0; X-ray; 1.53 A; B=452-491.
DR   PDB; 5KY4; X-ray; 1.47 A; B=983-1022.
DR   PDB; 5KY8; X-ray; 1.65 A; B=452-491.
DR   PDB; 5KY9; X-ray; 1.83 A; B=452-491.
DR   PDBsum; 1YMP; -.
DR   PDBsum; 2QC9; -.
DR   PDBsum; 2RQZ; -.
DR   PDBsum; 2RR0; -.
DR   PDBsum; 2RR2; -.
DR   PDBsum; 3P3N; -.
DR   PDBsum; 3P3P; -.
DR   PDBsum; 5KY0; -.
DR   PDBsum; 5KY4; -.
DR   PDBsum; 5KY8; -.
DR   PDBsum; 5KY9; -.
DR   ProteinModelPortal; Q01705; -.
DR   SMR; Q01705; -.
DR   BioGrid; 201808; 20.
DR   CORUM; Q01705; -.
DR   DIP; DIP-214N; -.
DR   IntAct; Q01705; 11.
DR   MINT; Q01705; -.
DR   STRING; 10090.ENSMUSP00000028288; -.
DR   iPTMnet; Q01705; -.
DR   PhosphoSitePlus; Q01705; -.
DR   PaxDb; Q01705; -.
DR   PeptideAtlas; Q01705; -.
DR   PRIDE; Q01705; -.
DR   Ensembl; ENSMUST00000028288; ENSMUSP00000028288; ENSMUSG00000026923. [Q01705-1]
DR   GeneID; 18128; -.
DR   KEGG; mmu:18128; -.
DR   UCSC; uc008ivl.2; mouse. [Q01705-1]
DR   CTD; 4851; -.
DR   MGI; MGI:97363; Notch1.
DR   eggNOG; ENOG410IR7G; Eukaryota.
DR   eggNOG; COG0666; LUCA.
DR   GeneTree; ENSGT00940000157157; -.
DR   HOGENOM; HOG000234369; -.
DR   HOVERGEN; HBG052650; -.
DR   InParanoid; Q01705; -.
DR   KO; K02599; -.
DR   OMA; GRDCESK; -.
DR   OrthoDB; 7525at2759; -.
DR   TreeFam; TF351641; -.
DR   Reactome; R-MMU-1912420; Pre-NOTCH Processing in Golgi.
DR   Reactome; R-MMU-2122947; NOTCH1 Intracellular Domain Regulates Transcription.
DR   Reactome; R-MMU-2122948; Activated NOTCH1 Transmits Signal to the Nucleus.
DR   Reactome; R-MMU-350054; Notch-HLH transcription pathway.
DR   Reactome; R-MMU-8941856; RUNX3 regulates NOTCH signaling.
DR   ChiTaRS; Notch1; mouse.
DR   EvolutionaryTrace; Q01705; -.
DR   PRO; PR:Q01705; -.
DR   Proteomes; UP000000589; Chromosome 2.
DR   Bgee; ENSMUSG00000026923; Expressed in 376 organ(s), highest expression level in hair follicle.
DR   ExpressionAtlas; Q01705; baseline and differential.
DR   Genevisible; Q01705; MM.
DR   GO; GO:0001669; C:acrosomal vesicle; ISO:MGI.
DR   GO; GO:0005912; C:adherens junction; IDA:UniProtKB.
DR   GO; GO:0016324; C:apical plasma membrane; IDA:UniProtKB.
DR   GO; GO:0071944; C:cell periphery; IDA:MGI.
DR   GO; GO:0009986; C:cell surface; IDA:MGI.
DR   GO; GO:0005737; C:cytoplasm; IDA:MGI.
DR   GO; GO:0031410; C:cytoplasmic vesicle; IDA:MGI.
DR   GO; GO:0005856; C:cytoskeleton; ISS:UniProtKB.
DR   GO; GO:0005829; C:cytosol; TAS:Reactome.
DR   GO; GO:0005783; C:endoplasmic reticulum; IDA:MGI.
DR   GO; GO:0005789; C:endoplasmic reticulum membrane; TAS:Reactome.
DR   GO; GO:0005576; C:extracellular region; TAS:Reactome.
DR   GO; GO:0005794; C:Golgi apparatus; ISO:MGI.
DR   GO; GO:0000139; C:Golgi membrane; TAS:Reactome.
DR   GO; GO:0005887; C:integral component of plasma membrane; IC:UniProtKB.
DR   GO; GO:0030027; C:lamellipodium; ISS:UniProtKB.
DR   GO; GO:0002193; C:MAML1-RBP-Jkappa- ICN1 complex; ISO:MGI.
DR   GO; GO:0005654; C:nucleoplasm; TAS:Reactome.
DR   GO; GO:0005634; C:nucleus; IDA:AgBase.
DR   GO; GO:0005886; C:plasma membrane; IDA:BHF-UCL.
DR   GO; GO:0043235; C:receptor complex; ISO:MGI.
DR   GO; GO:0001726; C:ruffle; ISS:UniProtKB.
DR   GO; GO:0005509; F:calcium ion binding; IEA:InterPro.
DR   GO; GO:0003682; F:chromatin binding; IDA:MGI.
DR   GO; GO:0031490; F:chromatin DNA binding; IDA:MGI.
DR   GO; GO:0001228; F:DNA-binding transcription activator activity, RNA polymerase II-specific; IDA:BHF-UCL.
DR   GO; GO:0003700; F:DNA-binding transcription factor activity; IDA:MGI.
DR   GO; GO:0019899; F:enzyme binding; IPI:UniProtKB.
DR   GO; GO:0004857; F:enzyme inhibitor activity; IDA:UniProtKB.
DR   GO; GO:0005112; F:Notch binding; IPI:MGI.
DR   GO; GO:0046982; F:protein heterodimerization activity; IDA:MGI.
DR   GO; GO:0000978; F:RNA polymerase II proximal promoter sequence-specific DNA binding; IDA:UniProtKB.
DR   GO; GO:0043565; F:sequence-specific DNA binding; IDA:MGI.
DR   GO; GO:0004888; F:transmembrane signaling receptor activity; ISO:MGI.
DR   GO; GO:0031100; P:animal organ regeneration; IEA:Ensembl.
DR   GO; GO:0003180; P:aortic valve morphogenesis; IMP:BHF-UCL.
DR   GO; GO:1902263; P:apoptotic process involved in embryonic digit morphogenesis; IMP:MGI.
DR   GO; GO:0060842; P:arterial endothelial cell differentiation; IMP:BHF-UCL.
DR   GO; GO:0048708; P:astrocyte differentiation; ISO:MGI.
DR   GO; GO:0003162; P:atrioventricular node development; IMP:BHF-UCL.
DR   GO; GO:0003181; P:atrioventricular valve morphogenesis; IMP:BHF-UCL.
DR   GO; GO:0009912; P:auditory receptor cell fate commitment; IMP:MGI.
DR   GO; GO:0007409; P:axonogenesis; IDA:MGI.
DR   GO; GO:0048754; P:branching morphogenesis of an epithelial tube; IMP:MGI.
DR   GO; GO:0003209; P:cardiac atrium morphogenesis; IMP:BHF-UCL.
DR   GO; GO:0003207; P:cardiac chamber formation; IMP:BHF-UCL.
DR   GO; GO:0060317; P:cardiac epithelial to mesenchymal transition; IMP:BHF-UCL.
DR   GO; GO:0003214; P:cardiac left ventricle morphogenesis; IMP:BHF-UCL.
DR   GO; GO:0060038; P:cardiac muscle cell proliferation; IMP:BHF-UCL.
DR   GO; GO:0055008; P:cardiac muscle tissue morphogenesis; IMP:BHF-UCL.
DR   GO; GO:0003213; P:cardiac right atrium morphogenesis; IMP:BHF-UCL.
DR   GO; GO:0003219; P:cardiac right ventricle formation; IMP:MGI.
DR   GO; GO:0060411; P:cardiac septum morphogenesis; IMP:BHF-UCL.
DR   GO; GO:0060948; P:cardiac vascular smooth muscle cell development; IMP:BHF-UCL.
DR   GO; GO:0003208; P:cardiac ventricle morphogenesis; IMP:BHF-UCL.
DR   GO; GO:0007050; P:cell cycle arrest; ISO:MGI.
DR   GO; GO:0030154; P:cell differentiation; IMP:MGI.
DR   GO; GO:0021515; P:cell differentiation in spinal cord; IEA:Ensembl.
DR   GO; GO:0045165; P:cell fate commitment; IMP:MGI.
DR   GO; GO:0001708; P:cell fate specification; IMP:MGI.
DR   GO; GO:0003273; P:cell migration involved in endocardial cushion formation; IMP:BHF-UCL.
DR   GO; GO:0071372; P:cellular response to follicle-stimulating hormone stimulus; ISO:MGI.
DR   GO; GO:0035924; P:cellular response to vascular endothelial growth factor stimulus; ISS:UniProtKB.
DR   GO; GO:0060271; P:cilium assembly; ISS:UniProtKB.
DR   GO; GO:0072044; P:collecting duct development; IEP:UniProtKB.
DR   GO; GO:0007386; P:compartment pattern specification; IMP:MGI.
DR   GO; GO:0060982; P:coronary artery morphogenesis; IMP:BHF-UCL.
DR   GO; GO:0003182; P:coronary sinus valve morphogenesis; IMP:BHF-UCL.
DR   GO; GO:0003169; P:coronary vein morphogenesis; IMP:BHF-UCL.
DR   GO; GO:0007368; P:determination of left/right symmetry; IMP:MGI.
DR   GO; GO:0072017; P:distal tubule development; IEP:UniProtKB.
DR   GO; GO:0035116; P:embryonic hindlimb morphogenesis; IMP:MGI.
DR   GO; GO:0030326; P:embryonic limb morphogenesis; IGI:MGI.
DR   GO; GO:0060956; P:endocardial cell differentiation; IMP:BHF-UCL.
DR   GO; GO:0003197; P:endocardial cushion development; IMP:MGI.
DR   GO; GO:0003203; P:endocardial cushion morphogenesis; IMP:BHF-UCL.
DR   GO; GO:0003157; P:endocardium development; IMP:BHF-UCL.
DR   GO; GO:0003160; P:endocardium morphogenesis; IMP:BHF-UCL.
DR   GO; GO:0007492; P:endoderm development; IMP:MGI.
DR   GO; GO:0008544; P:epidermis development; IGI:MGI.
DR   GO; GO:0001837; P:epithelial to mesenchymal transition; IMP:MGI.
DR   GO; GO:0003198; P:epithelial to mesenchymal transition involved in endocardial cushion formation; IMP:BHF-UCL.
DR   GO; GO:0030900; P:forebrain development; IMP:MGI.
DR   GO; GO:0007440; P:foregut morphogenesis; IMP:MGI.
DR   GO; GO:0010001; P:glial cell differentiation; IMP:MGI.
DR   GO; GO:0072144; P:glomerular mesangial cell development; IEP:UniProtKB.
DR   GO; GO:0003241; P:growth involved in heart morphogenesis; IMP:BHF-UCL.
DR   GO; GO:0031069; P:hair follicle morphogenesis; IMP:MGI.
DR   GO; GO:0007507; P:heart development; ISO:MGI.
DR   GO; GO:0001947; P:heart looping; IGI:BHF-UCL.
DR   GO; GO:0061384; P:heart trabecula morphogenesis; IMP:BHF-UCL.
DR   GO; GO:0048873; P:homeostasis of number of cells within a tissue; IGI:BHF-UCL.
DR   GO; GO:0006959; P:humoral immune response; IGI:MGI.
DR   GO; GO:0001701; P:in utero embryonic development; IMP:MGI.
DR   GO; GO:0002437; P:inflammatory response to antigenic stimulus; IGI:MGI.
DR   GO; GO:0072602; P:interleukin-4 secretion; IGI:MGI.
DR   GO; GO:0030216; P:keratinocyte differentiation; IMP:MGI.
DR   GO; GO:0070986; P:left/right axis specification; IGI:BHF-UCL.
DR   GO; GO:0001889; P:liver development; IMP:MGI.
DR   GO; GO:0030324; P:lung development; IMP:MGI.
DR   GO; GO:0014031; P:mesenchymal cell development; IMP:BHF-UCL.
DR   GO; GO:0003192; P:mitral valve formation; ISO:MGI.
DR   GO; GO:2000811; P:negative regulation of anoikis; ISO:MGI.
DR   GO; GO:0070168; P:negative regulation of biomineral tissue development; IDA:BHF-UCL.
DR   GO; GO:0030514; P:negative regulation of BMP signaling pathway; IMP:BHF-UCL.
DR   GO; GO:0045955; P:negative regulation of calcium ion-dependent exocytosis; IMP:MGI.
DR   GO; GO:0090090; P:negative regulation of canonical Wnt signaling pathway; IMP:MGI.
DR   GO; GO:0010614; P:negative regulation of cardiac muscle hypertrophy; IMP:BHF-UCL.
DR   GO; GO:0043086; P:negative regulation of catalytic activity; IDA:UniProtKB.
DR   GO; GO:0060548; P:negative regulation of cell death; IMP:MGI.
DR   GO; GO:0045596; P:negative regulation of cell differentiation; IMP:MGI.
DR   GO; GO:0090051; P:negative regulation of cell migration involved in sprouting angiogenesis; ISS:UniProtKB.
DR   GO; GO:0008285; P:negative regulation of cell population proliferation; IMP:MGI.
DR   GO; GO:0003252; P:negative regulation of cell proliferation involved in heart valve morphogenesis; IDA:BHF-UCL.
DR   GO; GO:0010812; P:negative regulation of cell-substrate adhesion; ISO:MGI.
DR   GO; GO:0120163; P:negative regulation of cold-induced thermogenesis; IMP:YuBioLab.
DR   GO; GO:2001027; P:negative regulation of endothelial cell chemotaxis; ISS:UniProtKB.
DR   GO; GO:0003332; P:negative regulation of extracellular matrix constituent secretion; IMP:BHF-UCL.
DR   GO; GO:0010629; P:negative regulation of gene expression; ISO:MGI.
DR   GO; GO:0060253; P:negative regulation of glial cell proliferation; IDA:UniProtKB.
DR   GO; GO:0045967; P:negative regulation of growth rate; ISO:MGI.
DR   GO; GO:0045608; P:negative regulation of inner ear auditory receptor cell differentiation; IMP:MGI.
DR   GO; GO:0045662; P:negative regulation of myoblast differentiation; ISO:MGI.
DR   GO; GO:0010832; P:negative regulation of myotube differentiation; IDA:UniProtKB.
DR   GO; GO:0050768; P:negative regulation of neurogenesis; IDA:UniProtKB.
DR   GO; GO:0045665; P:negative regulation of neuron differentiation; IMP:MGI.
DR   GO; GO:0048715; P:negative regulation of oligodendrocyte differentiation; IDA:UniProtKB.
DR   GO; GO:0030279; P:negative regulation of ossification; IMP:BHF-UCL.
DR   GO; GO:0045668; P:negative regulation of osteoblast differentiation; IMP:BHF-UCL.
DR   GO; GO:0046533; P:negative regulation of photoreceptor cell differentiation; IMP:MGI.
DR   GO; GO:2000974; P:negative regulation of pro-B cell differentiation; IMP:UniProtKB.
DR   GO; GO:2000737; P:negative regulation of stem cell differentiation; ISO:MGI.
DR   GO; GO:0000122; P:negative regulation of transcription by RNA polymerase II; IDA:UniProtKB.
DR   GO; GO:0045892; P:negative regulation of transcription, DNA-templated; IDA:BHF-UCL.
DR   GO; GO:0021915; P:neural tube development; IMP:MGI.
DR   GO; GO:0030182; P:neuron differentiation; IMP:MGI.
DR   GO; GO:0048663; P:neuron fate commitment; IGI:MGI.
DR   GO; GO:0097150; P:neuronal stem cell population maintenance; IEA:Ensembl.
DR   GO; GO:0061314; P:Notch signaling involved in heart development; IMP:BHF-UCL.
DR   GO; GO:0007219; P:Notch signaling pathway; IDA:MGI.
DR   GO; GO:0003270; P:Notch signaling pathway involved in regulation of secondary heart field cardioblast proliferation; IMP:MGI.
DR   GO; GO:0048709; P:oligodendrocyte differentiation; IEA:Ensembl.
DR   GO; GO:0002051; P:osteoblast fate commitment; NAS:BHF-UCL.
DR   GO; GO:0003151; P:outflow tract morphogenesis; ISO:MGI.
DR   GO; GO:0003344; P:pericardium morphogenesis; IMP:BHF-UCL.
DR   GO; GO:1903849; P:positive regulation of aorta morphogenesis; IMP:MGI.
DR   GO; GO:0043065; P:positive regulation of apoptotic process; IDA:MGI.
DR   GO; GO:1902339; P:positive regulation of apoptotic process involved in morphogenesis; IDA:BHF-UCL.
DR   GO; GO:0048711; P:positive regulation of astrocyte differentiation; IDA:UniProtKB.
DR   GO; GO:0030513; P:positive regulation of BMP signaling pathway; IDA:UniProtKB.
DR   GO; GO:0062043; P:positive regulation of cardiac epithelial to mesenchymal transition; ISO:MGI.
DR   GO; GO:0060045; P:positive regulation of cardiac muscle cell proliferation; IMP:BHF-UCL.
DR   GO; GO:0030335; P:positive regulation of cell migration; IMP:BHF-UCL.
DR   GO; GO:0008284; P:positive regulation of cell population proliferation; IGI:MGI.
DR   GO; GO:0045603; P:positive regulation of endothelial cell differentiation; ISO:MGI.
DR   GO; GO:1901189; P:positive regulation of ephrin receptor signaling pathway; IC:BHF-UCL.
DR   GO; GO:0050679; P:positive regulation of epithelial cell proliferation; IGI:MGI.
DR   GO; GO:0010718; P:positive regulation of epithelial to mesenchymal transition; IMP:BHF-UCL.
DR   GO; GO:0070374; P:positive regulation of ERK1 and ERK2 cascade; ISO:MGI.
DR   GO; GO:0010628; P:positive regulation of gene expression; IDA:BHF-UCL.
DR   GO; GO:0045687; P:positive regulation of glial cell differentiation; ISO:MGI.
DR   GO; GO:0045618; P:positive regulation of keratinocyte differentiation; IDA:MGI.
DR   GO; GO:0002052; P:positive regulation of neuroblast proliferation; ISO:MGI.
DR   GO; GO:0045747; P:positive regulation of Notch signaling pathway; IDA:MGI.
DR   GO; GO:0046579; P:positive regulation of Ras protein signal transduction; ISO:MGI.
DR   GO; GO:0046427; P:positive regulation of receptor signaling pathway via JAK-STAT; IDA:UniProtKB.
DR   GO; GO:0045944; P:positive regulation of transcription by RNA polymerase II; IDA:UniProtKB.
DR   GO; GO:0061419; P:positive regulation of transcription from RNA polymerase II promoter in response to hypoxia; IDA:UniProtKB.
DR   GO; GO:0007221; P:positive regulation of transcription of Notch receptor target; IGI:MGI.
DR   GO; GO:0045893; P:positive regulation of transcription, DNA-templated; IDA:UniProtKB.
DR   GO; GO:0045070; P:positive regulation of viral genome replication; IMP:AgBase.
DR   GO; GO:0050434; P:positive regulation of viral transcription; IMP:AgBase.
DR   GO; GO:0060740; P:prostate gland epithelium morphogenesis; IMP:MGI.
DR   GO; GO:0003184; P:pulmonary valve morphogenesis; IMP:BHF-UCL.
DR   GO; GO:0003264; P:regulation of cardioblast proliferation; ISO:MGI.
DR   GO; GO:0061344; P:regulation of cell adhesion involved in heart morphogenesis; IC:BHF-UCL.
DR   GO; GO:0030334; P:regulation of cell migration; IMP:BHF-UCL.
DR   GO; GO:0042127; P:regulation of cell population proliferation; IGI:MGI.
DR   GO; GO:0050678; P:regulation of epithelial cell proliferation; IMP:MGI.
DR   GO; GO:0060768; P:regulation of epithelial cell proliferation involved in prostate gland development; IMP:MGI.
DR   GO; GO:1901201; P:regulation of extracellular matrix assembly; IMP:BHF-UCL.
DR   GO; GO:0010468; P:regulation of gene expression; IMP:MGI.
DR   GO; GO:0045607; P:regulation of inner ear auditory receptor cell differentiation; IMP:MGI.
DR   GO; GO:0050767; P:regulation of neurogenesis; IMP:MGI.
DR   GO; GO:0008593; P:regulation of Notch signaling pathway; IGI:MGI.
DR   GO; GO:0014807; P:regulation of somitogenesis; IMP:MGI.
DR   GO; GO:0006357; P:regulation of transcription by RNA polymerase II; IMP:MGI.
DR   GO; GO:0003256; P:regulation of transcription from RNA polymerase II promoter involved in myocardial precursor cell differentiation; IMP:BHF-UCL.
DR   GO; GO:0031960; P:response to corticosteroid; IEA:Ensembl.
DR   GO; GO:0032496; P:response to lipopolysaccharide; IEA:Ensembl.
DR   GO; GO:0032495; P:response to muramyl dipeptide; IDA:BHF-UCL.
DR   GO; GO:0060528; P:secretory columnal luminar epithelial cell differentiation involved in prostate glandular acinus development; IMP:MGI.
DR   GO; GO:0035914; P:skeletal muscle cell differentiation; IMP:MGI.
DR   GO; GO:0048103; P:somatic stem cell division; IDA:MGI.
DR   GO; GO:0007283; P:spermatogenesis; ISO:MGI.
DR   GO; GO:0002040; P:sprouting angiogenesis; IMP:MGI.
DR   GO; GO:0042246; P:tissue regeneration; IEA:Ensembl.
DR   GO; GO:0035148; P:tube formation; ISS:UniProtKB.
DR   GO; GO:0060979; P:vasculogenesis involved in coronary vascular morphogenesis; IMP:BHF-UCL.
DR   GO; GO:0048845; P:venous blood vessel morphogenesis; IMP:MGI.
DR   GO; GO:0060843; P:venous endothelial cell differentiation; IMP:BHF-UCL.
DR   GO; GO:0060412; P:ventricular septum morphogenesis; IMP:BHF-UCL.
DR   GO; GO:0003222; P:ventricular trabecula myocardium morphogenesis; IMP:BHF-UCL.
DR   CDD; cd00204; ANK; 2.
DR   Gene3D; 1.25.40.20; -; 1.
DR   InterPro; IPR002110; Ankyrin_rpt.
DR   InterPro; IPR020683; Ankyrin_rpt-contain_dom.
DR   InterPro; IPR036770; Ankyrin_rpt-contain_sf.
DR   InterPro; IPR024600; DUF3454_notch.
DR   InterPro; IPR001881; EGF-like_Ca-bd_dom.
DR   InterPro; IPR013032; EGF-like_CS.
DR   InterPro; IPR000742; EGF-like_dom.
DR   InterPro; IPR000152; EGF-type_Asp/Asn_hydroxyl_site.
DR   InterPro; IPR018097; EGF_Ca-bd_CS.
DR   InterPro; IPR009030; Growth_fac_rcpt_cys_sf.
DR   InterPro; IPR008297; Notch.
DR   InterPro; IPR035993; Notch-like_dom_sf.
DR   InterPro; IPR022362; Notch_1.
DR   InterPro; IPR000800; Notch_dom.
DR   InterPro; IPR010660; Notch_NOD_dom.
DR   InterPro; IPR011656; Notch_NODP_dom.
DR   Pfam; PF12796; Ank_2; 2.
DR   Pfam; PF11936; DUF3454; 1.
DR   Pfam; PF00008; EGF; 21.
DR   Pfam; PF07645; EGF_CA; 5.
DR   Pfam; PF12661; hEGF; 3.
DR   Pfam; PF06816; NOD; 1.
DR   Pfam; PF07684; NODP; 1.
DR   Pfam; PF00066; Notch; 3.
DR   PIRSF; PIRSF002279; Notch; 1.
DR   PRINTS; PR01452; LNOTCHREPEAT.
DR   PRINTS; PR01984; NOTCH1.
DR   SMART; SM00248; ANK; 6.
DR   SMART; SM01334; DUF3454; 1.
DR   SMART; SM00181; EGF; 36.
DR   SMART; SM00179; EGF_CA; 33.
DR   SMART; SM00004; NL; 3.
DR   SMART; SM01338; NOD; 1.
DR   SMART; SM01339; NODP; 1.
DR   SUPFAM; SSF48403; SSF48403; 1.
DR   SUPFAM; SSF57184; SSF57184; 6.
DR   SUPFAM; SSF90193; SSF90193; 3.
DR   PROSITE; PS50297; ANK_REP_REGION; 1.
DR   PROSITE; PS50088; ANK_REPEAT; 4.
DR   PROSITE; PS00010; ASX_HYDROXYL; 22.
DR   PROSITE; PS00022; EGF_1; 35.
DR   PROSITE; PS01186; EGF_2; 27.
DR   PROSITE; PS50026; EGF_3; 36.
DR   PROSITE; PS01187; EGF_CA; 21.
DR   PROSITE; PS50258; LNR; 3.
PE   1: Evidence at protein level;
KW   3D-structure; Activator; Alternative splicing; Angiogenesis;
KW   ANK repeat; Calcium; Cell membrane; Complete proteome;
KW   Developmental protein; Differentiation; Direct protein sequencing;
KW   Disulfide bond; EGF-like domain; Glycoprotein; Hydroxylation;
KW   Isopeptide bond; Membrane; Metal-binding; Notch signaling pathway;
KW   Nucleus; Phosphoprotein; Receptor; Reference proteome; Repeat; Signal;
KW   Transcription; Transcription regulation; Transmembrane;
KW   Transmembrane helix; Ubl conjugation.
FT   SIGNAL        1     18       {ECO:0000255}.
FT   CHAIN        19   2531       Neurogenic locus notch homolog protein 1.
FT                                /FTId=PRO_0000007677.
FT   CHAIN      1711   2531       Notch 1 extracellular truncation.
FT                                {ECO:0000305|PubMed:10882062,
FT                                ECO:0000305|PubMed:10882063}.
FT                                /FTId=PRO_0000007678.
FT   CHAIN      1744   2531       Notch 1 intracellular domain.
FT                                {ECO:0000305|PubMed:10882062,
FT                                ECO:0000305|PubMed:11459941,
FT                                ECO:0000305|PubMed:11518718}.
FT                                /FTId=PRO_0000007679.
FT   TOPO_DOM     19   1725       Extracellular. {ECO:0000305}.
FT   TRANSMEM   1726   1746       Helical. {ECO:0000250|UniProtKB:P46531}.
FT   TOPO_DOM   1747   2531       Cytoplasmic. {ECO:0000305}.
FT   DOMAIN       20     58       EGF-like 1. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00076}.
FT   DOMAIN       59     99       EGF-like 2. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00076}.
FT   DOMAIN      102    139       EGF-like 3. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00076}.
FT   DOMAIN      140    176       EGF-like 4. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00076}.
FT   DOMAIN      178    216       EGF-like 5; calcium-binding.
FT                                {ECO:0000255|PROSITE-ProRule:PRU00076}.
FT   DOMAIN      218    255       EGF-like 6. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00076}.
FT   DOMAIN      257    293       EGF-like 7; calcium-binding.
FT                                {ECO:0000255|PROSITE-ProRule:PRU00076}.
FT   DOMAIN      295    333       EGF-like 8; calcium-binding.
FT                                {ECO:0000255|PROSITE-ProRule:PRU00076}.
FT   DOMAIN      335    371       EGF-like 9; calcium-binding.
FT                                {ECO:0000255|PROSITE-ProRule:PRU00076}.
FT   DOMAIN      372    410       EGF-like 10; calcium-binding.
FT                                {ECO:0000255|PROSITE-ProRule:PRU00076}.
FT   DOMAIN      412    450       EGF-like 11; calcium-binding.
FT                                {ECO:0000255|PROSITE-ProRule:PRU00076}.
FT   DOMAIN      452    488       EGF-like 12; calcium-binding.
FT                                {ECO:0000255|PROSITE-ProRule:PRU00076}.
FT   DOMAIN      490    526       EGF-like 13; calcium-binding.
FT                                {ECO:0000255|PROSITE-ProRule:PRU00076}.
FT   DOMAIN      528    564       EGF-like 14; calcium-binding.
FT                                {ECO:0000255|PROSITE-ProRule:PRU00076}.
FT   DOMAIN      566    601       EGF-like 15; calcium-binding.
FT                                {ECO:0000255|PROSITE-ProRule:PRU00076}.
FT   DOMAIN      603    639       EGF-like 16; calcium-binding.
FT                                {ECO:0000255|PROSITE-ProRule:PRU00076}.
FT   DOMAIN      641    676       EGF-like 17; calcium-binding.
FT                                {ECO:0000255|PROSITE-ProRule:PRU00076}.
FT   DOMAIN      678    714       EGF-like 18; calcium-binding.
FT                                {ECO:0000255|PROSITE-ProRule:PRU00076}.
FT   DOMAIN      716    751       EGF-like 19; calcium-binding.
FT                                {ECO:0000255|PROSITE-ProRule:PRU00076}.
FT   DOMAIN      753    789       EGF-like 20; calcium-binding.
FT                                {ECO:0000255|PROSITE-ProRule:PRU00076}.
FT   DOMAIN      791    827       EGF-like 21; calcium-binding.
FT                                {ECO:0000255|PROSITE-ProRule:PRU00076}.
FT   DOMAIN      829    867       EGF-like 22. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00076}.
FT   DOMAIN      869    905       EGF-like 23; calcium-binding.
FT                                {ECO:0000255|PROSITE-ProRule:PRU00076}.
FT   DOMAIN      907    943       EGF-like 24. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00076}.
FT   DOMAIN      945    981       EGF-like 25; calcium-binding.
FT                                {ECO:0000255|PROSITE-ProRule:PRU00076}.
FT   DOMAIN      983   1019       EGF-like 26. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00076}.
FT   DOMAIN     1021   1057       EGF-like 27; calcium-binding.
FT                                {ECO:0000255|PROSITE-ProRule:PRU00076}.
FT   DOMAIN     1059   1095       EGF-like 28. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00076}.
FT   DOMAIN     1097   1143       EGF-like 29. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00076}.
FT   DOMAIN     1145   1181       EGF-like 30; calcium-binding.
FT                                {ECO:0000255|PROSITE-ProRule:PRU00076}.
FT   DOMAIN     1183   1219       EGF-like 31; calcium-binding.
FT                                {ECO:0000255|PROSITE-ProRule:PRU00076}.
FT   DOMAIN     1221   1265       EGF-like 32; calcium-binding.
FT                                {ECO:0000255|PROSITE-ProRule:PRU00076}.
FT   DOMAIN     1267   1305       EGF-like 33. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00076}.
FT   DOMAIN     1307   1346       EGF-like 34. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00076}.
FT   DOMAIN     1348   1384       EGF-like 35. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00076}.
FT   DOMAIN     1387   1426       EGF-like 36. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00076}.
FT   REPEAT     1449   1489       LNR 1.
FT   REPEAT     1490   1531       LNR 2.
FT   REPEAT     1532   1571       LNR 3.
FT   REPEAT     1917   1946       ANK 1.
FT   REPEAT     1950   1980       ANK 2.
FT   REPEAT     1984   2013       ANK 3.
FT   REPEAT     2017   2046       ANK 4.
FT   REPEAT     2050   2079       ANK 5.
FT   REGION      420    421       Interaction with DLL4.
FT                                {ECO:0000250|UniProtKB:Q07008}.
FT   REGION      448    452       Interaction with DLL4.
FT                                {ECO:0000250|UniProtKB:Q07008}.
FT   REGION     1718   1750       Interaction with PSEN1.
FT                                {ECO:0000250|UniProtKB:P46531}.
FT   REGION     1937   1945       HIF1AN-binding.
FT   REGION     2004   2012       HIF1AN-binding.
FT   METAL       432    432       Calcium 1; via carbonyl oxygen.
FT                                {ECO:0000250|UniProtKB:Q07008}.
FT   METAL       435    435       Calcium 1; via amide nitrogen.
FT                                {ECO:0000250|UniProtKB:Q07008}.
FT   METAL       452    452       Calcium 2.
FT                                {ECO:0000250|UniProtKB:Q07008}.
FT   METAL       453    453       Calcium 2; via carbonyl oxygen.
FT                                {ECO:0000250|UniProtKB:Q07008}.
FT   METAL       455    455       Calcium 2.
FT                                {ECO:0000250|UniProtKB:Q07008}.
FT   METAL       469    469       Calcium 2.
FT                                {ECO:0000250|UniProtKB:Q07008}.
FT   METAL       470    470       Calcium 2; via carbonyl oxygen.
FT                                {ECO:0000250|UniProtKB:Q07008}.
FT   METAL       490    490       Calcium 3.
FT                                {ECO:0000250|UniProtKB:Q07008}.
FT   METAL       491    491       Calcium 3; via carbonyl oxygen.
FT                                {ECO:0000250|UniProtKB:Q07008}.
FT   METAL       493    493       Calcium 3.
FT                                {ECO:0000250|UniProtKB:Q07008}.
FT   METAL       507    507       Calcium 3.
FT                                {ECO:0000250|UniProtKB:Q07008}.
FT   METAL       508    508       Calcium 3; via carbonyl oxygen.
FT                                {ECO:0000250|UniProtKB:Q07008}.
FT   METAL      1457   1457       Calcium 4; via carbonyl oxygen.
FT                                {ECO:0000255|PROSITE-ProRule:PRU00525}.
FT   METAL      1460   1460       Calcium 4. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00525}.
FT   METAL      1475   1475       Calcium 4. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00525}.
FT   METAL      1478   1478       Calcium 4. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00525}.
FT   SITE        469    469       Interaction with DLL4.
FT                                {ECO:0000250|UniProtKB:Q07008}.
FT   SITE       1654   1655       Cleavage; by furin-like protease.
FT                                {ECO:0000269|PubMed:9653148}.
FT   SITE       1710   1711       Cleavage; by ADAM17.
FT                                {ECO:0000269|PubMed:10882062,
FT                                ECO:0000269|PubMed:10882063}.
FT   MOD_RES    1851   1851       Phosphothreonine.
FT                                {ECO:0000244|PubMed:21183079}.
FT   MOD_RES    1945   1945       (3S)-3-hydroxyasparagine; by HIF1AN;
FT                                partial. {ECO:0000269|PubMed:17573339,
FT                                ECO:0000269|PubMed:18299578}.
FT   MOD_RES    2012   2012       (3S)-3-hydroxyasparagine; by HIF1AN;
FT                                partial. {ECO:0000269|PubMed:17573339,
FT                                ECO:0000269|PubMed:18299578}.
FT   CARBOHYD     65     65       O-linked (Glc...) serine.
FT                                {ECO:0000269|PubMed:21757702}.
FT   CARBOHYD     73     73       O-linked (Fuc...) threonine.
FT                                {ECO:0000269|PubMed:21757702,
FT                                ECO:0000269|PubMed:28089369}.
FT   CARBOHYD    116    116       O-linked (Fuc...) threonine.
FT                                {ECO:0000269|PubMed:21757702,
FT                                ECO:0000269|PubMed:28089369}.
FT   CARBOHYD    146    146       O-linked (Glc...) serine.
FT                                {ECO:0000269|PubMed:21757702}.
FT   CARBOHYD    194    194       O-linked (Fuc...) threonine.
FT                                {ECO:0000269|PubMed:21757702,
FT                                ECO:0000269|PubMed:28089369}.
FT   CARBOHYD    232    232       O-linked (Fuc...) threonine; alternate.
FT                                {ECO:0000269|PubMed:28089369}.
FT   CARBOHYD    232    232       O-linked (GalNAc...) threonine;
FT                                alternate.
FT                                {ECO:0000250|UniProtKB:P46531}.
FT   CARBOHYD    311    311       O-linked (Fuc...) threonine.
FT                                {ECO:0000269|PubMed:28089369}.
FT   CARBOHYD    341    341       O-linked (Glc...) serine.
FT                                {ECO:0000269|PubMed:21757702}.
FT   CARBOHYD    349    349       O-linked (Fuc...) threonine.
FT                                {ECO:0000269|PubMed:28089369}.
FT   CARBOHYD    378    378       O-linked (Glc...) serine.
FT                                {ECO:0000269|PubMed:21757702}.
FT   CARBOHYD    435    435       O-linked (Glc...) serine.
FT                                {ECO:0000269|PubMed:30127001}.
FT   CARBOHYD    458    458       O-linked (Glc...) serine.
FT                                {ECO:0000269|PubMed:21757702,
FT                                ECO:0000269|PubMed:28089369}.
FT   CARBOHYD    466    466       O-linked (Fuc...) threonine.
FT                                {ECO:0000269|PubMed:21757702,
FT                                ECO:0000269|PubMed:28089369}.
FT   CARBOHYD    496    496       O-linked (Glc...) serine.
FT                                {ECO:0000269|PubMed:21757702}.
FT   CARBOHYD    534    534       O-linked (Glc...) serine.
FT                                {ECO:0000269|PubMed:21757702}.
FT   CARBOHYD    609    609       O-linked (Glc...) serine.
FT                                {ECO:0000269|PubMed:21757702}.
FT   CARBOHYD    617    617       O-linked (Fuc...) threonine.
FT                                {ECO:0000269|PubMed:28089369}.
FT   CARBOHYD    647    647       O-linked (Glc...) serine.
FT                                {ECO:0000269|PubMed:21757702}.
FT   CARBOHYD    692    692       O-linked (Fuc...) threonine.
FT                                {ECO:0000269|PubMed:28089369}.
FT   CARBOHYD    722    722       O-linked (Glc...) serine.
FT                                {ECO:0000269|PubMed:21757702}.
FT   CARBOHYD    759    759       O-linked (Glc...) serine.
FT                                {ECO:0000269|PubMed:21757702,
FT                                ECO:0000269|PubMed:28089369}.
FT   CARBOHYD    767    767       O-linked (Fuc...) threonine.
FT                                {ECO:0000269|PubMed:21757702,
FT                                ECO:0000269|PubMed:28089369}.
FT   CARBOHYD    784    784       O-linked (GlcNAc) serine.
FT                                {ECO:0000269|PubMed:28089369}.
FT   CARBOHYD    797    797       O-linked (Glc...) serine.
FT                                {ECO:0000269|PubMed:21757702,
FT                                ECO:0000269|PubMed:28089369}.
FT   CARBOHYD    805    805       O-linked (Fuc...) threonine.
FT                                {ECO:0000269|PubMed:21757702,
FT                                ECO:0000269|PubMed:28089369}.
FT   CARBOHYD    888    888       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   CARBOHYD    900    900       O-linked (GlcNAc) threonine.
FT                                {ECO:0000269|PubMed:28089369}.
FT   CARBOHYD    921    921       O-linked (Fuc) serine.
FT                                {ECO:0000269|PubMed:28089369}.
FT   CARBOHYD    951    951       O-linked (Glc...) serine.
FT                                {ECO:0000269|PubMed:21757702}.
FT   CARBOHYD    959    959       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   CARBOHYD    997    997       O-linked (Fuc...) threonine.
FT                                {ECO:0000269|PubMed:28089369}.
FT   CARBOHYD   1027   1027       O-linked (Glc...) serine.
FT                                {ECO:0000269|PubMed:21757702}.
FT   CARBOHYD   1035   1035       O-linked (Fuc...) threonine.
FT                                {ECO:0000269|PubMed:21757702,
FT                                ECO:0000269|PubMed:28089369}.
FT   CARBOHYD   1065   1065       O-linked (Glc...) serine.
FT                                {ECO:0000269|PubMed:21757702}.
FT   CARBOHYD   1159   1159       O-linked (Fuc...) threonine.
FT                                {ECO:0000269|PubMed:28089369}.
FT   CARBOHYD   1179   1179       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   CARBOHYD   1189   1189       O-linked (Glc...) serine.
FT                                {ECO:0000269|PubMed:21757702}.
FT   CARBOHYD   1197   1197       O-linked (Fuc...) threonine.
FT                                {ECO:0000269|PubMed:21757702,
FT                                ECO:0000269|PubMed:28089369}.
FT   CARBOHYD   1241   1241       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   CARBOHYD   1273   1273       O-linked (Glc...) serine.
FT                                {ECO:0000269|PubMed:21757702}.
FT   CARBOHYD   1362   1362       O-linked (Fuc...) threonine.
FT                                {ECO:0000269|PubMed:21757702,
FT                                ECO:0000269|PubMed:28089369}.
FT   CARBOHYD   1379   1379       O-linked (GlcNAc...) threonine.
FT                                {ECO:0000269|PubMed:28089369}.
FT   CARBOHYD   1402   1402       O-linked (Fuc...) threonine; alternate.
FT                                {ECO:0000269|PubMed:28089369}.
FT   CARBOHYD   1402   1402       O-linked (GalNAc...) threonine;
FT                                alternate. {ECO:0000269|PubMed:28089369}.
FT   CARBOHYD   1489   1489       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   CARBOHYD   1587   1587       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   DISULFID     24     37       {ECO:0000250}.
FT   DISULFID     31     46       {ECO:0000250}.
FT   DISULFID     63     74       {ECO:0000250}.
FT   DISULFID     68     87       {ECO:0000250}.
FT   DISULFID     89     98       {ECO:0000250}.
FT   DISULFID    106    117       {ECO:0000250}.
FT   DISULFID    111    127       {ECO:0000250}.
FT   DISULFID    129    138       {ECO:0000250}.
FT   DISULFID    144    155       {ECO:0000250}.
FT   DISULFID    149    164       {ECO:0000250}.
FT   DISULFID    166    175       {ECO:0000250}.
FT   DISULFID    182    195       {ECO:0000250}.
FT   DISULFID    189    204       {ECO:0000250}.
FT   DISULFID    206    215       {ECO:0000250}.
FT   DISULFID    222    233       {ECO:0000250}.
FT   DISULFID    227    243       {ECO:0000250}.
FT   DISULFID    245    254       {ECO:0000250}.
FT   DISULFID    261    272       {ECO:0000250}.
FT   DISULFID    266    281       {ECO:0000250}.
FT   DISULFID    283    292       {ECO:0000250}.
FT   DISULFID    299    312       {ECO:0000250}.
FT   DISULFID    306    321       {ECO:0000250}.
FT   DISULFID    323    332       {ECO:0000250}.
FT   DISULFID    339    350       {ECO:0000250}.
FT   DISULFID    344    359       {ECO:0000250}.
FT   DISULFID    361    370       {ECO:0000250}.
FT   DISULFID    376    387       {ECO:0000250}.
FT   DISULFID    381    398       {ECO:0000250}.
FT   DISULFID    400    409       {ECO:0000250}.
FT   DISULFID    416    429       {ECO:0000250|UniProtKB:Q07008}.
FT   DISULFID    423    438       {ECO:0000250|UniProtKB:Q07008}.
FT   DISULFID    440    449       {ECO:0000250|UniProtKB:Q07008}.
FT   DISULFID    456    467       {ECO:0000250|UniProtKB:Q07008}.
FT   DISULFID    461    476       {ECO:0000250|UniProtKB:Q07008}.
FT   DISULFID    478    487       {ECO:0000250|UniProtKB:Q07008}.
FT   DISULFID    494    505       {ECO:0000250|UniProtKB:Q07008}.
FT   DISULFID    499    514       {ECO:0000250|UniProtKB:Q07008}.
FT   DISULFID    516    525       {ECO:0000250|UniProtKB:Q07008}.
FT   DISULFID    532    543       {ECO:0000250}.
FT   DISULFID    537    552       {ECO:0000250}.
FT   DISULFID    554    563       {ECO:0000250}.
FT   DISULFID    570    580       {ECO:0000250}.
FT   DISULFID    575    589       {ECO:0000250}.
FT   DISULFID    591    600       {ECO:0000250}.
FT   DISULFID    607    618       {ECO:0000250}.
FT   DISULFID    612    627       {ECO:0000250}.
FT   DISULFID    629    638       {ECO:0000250}.
FT   DISULFID    645    655       {ECO:0000250}.
FT   DISULFID    650    664       {ECO:0000250}.
FT   DISULFID    666    675       {ECO:0000250}.
FT   DISULFID    682    693       {ECO:0000250}.
FT   DISULFID    687    702       {ECO:0000250}.
FT   DISULFID    704    713       {ECO:0000250}.
FT   DISULFID    720    730       {ECO:0000250}.
FT   DISULFID    725    739       {ECO:0000250}.
FT   DISULFID    741    750       {ECO:0000250}.
FT   DISULFID    757    768       {ECO:0000250}.
FT   DISULFID    762    777       {ECO:0000250}.
FT   DISULFID    779    788       {ECO:0000250}.
FT   DISULFID    795    806       {ECO:0000250}.
FT   DISULFID    800    815       {ECO:0000250}.
FT   DISULFID    817    826       {ECO:0000250}.
FT   DISULFID    833    844       {ECO:0000250}.
FT   DISULFID    838    855       {ECO:0000250}.
FT   DISULFID    857    866       {ECO:0000250}.
FT   DISULFID    873    884       {ECO:0000250}.
FT   DISULFID    878    893       {ECO:0000250}.
FT   DISULFID    895    904       {ECO:0000250}.
FT   DISULFID    911    922       {ECO:0000250}.
FT   DISULFID    916    931       {ECO:0000250}.
FT   DISULFID    933    942       {ECO:0000250}.
FT   DISULFID    949    960       {ECO:0000250}.
FT   DISULFID    954    969       {ECO:0000250}.
FT   DISULFID    971    980       {ECO:0000250}.
FT   DISULFID    987    998       {ECO:0000250}.
FT   DISULFID    992   1007       {ECO:0000250}.
FT   DISULFID   1009   1018       {ECO:0000250}.
FT   DISULFID   1025   1036       {ECO:0000250}.
FT   DISULFID   1030   1045       {ECO:0000250}.
FT   DISULFID   1047   1056       {ECO:0000250}.
FT   DISULFID   1063   1074       {ECO:0000250}.
FT   DISULFID   1068   1083       {ECO:0000250}.
FT   DISULFID   1085   1094       {ECO:0000250}.
FT   DISULFID   1101   1122       {ECO:0000250}.
FT   DISULFID   1116   1131       {ECO:0000250}.
FT   DISULFID   1133   1142       {ECO:0000250}.
FT   DISULFID   1149   1160       {ECO:0000250}.
FT   DISULFID   1154   1169       {ECO:0000250}.
FT   DISULFID   1171   1180       {ECO:0000250}.
FT   DISULFID   1187   1198       {ECO:0000250}.
FT   DISULFID   1192   1207       {ECO:0000250}.
FT   DISULFID   1209   1218       {ECO:0000250}.
FT   DISULFID   1225   1244       {ECO:0000250}.
FT   DISULFID   1238   1253       {ECO:0000250}.
FT   DISULFID   1255   1264       {ECO:0000250}.
FT   DISULFID   1271   1284       {ECO:0000250}.
FT   DISULFID   1276   1293       {ECO:0000250}.
FT   DISULFID   1295   1304       {ECO:0000250}.
FT   DISULFID   1311   1322       {ECO:0000250}.
FT   DISULFID   1316   1334       {ECO:0000250}.
FT   DISULFID   1336   1345       {ECO:0000250}.
FT   DISULFID   1352   1363       {ECO:0000250}.
FT   DISULFID   1357   1372       {ECO:0000250}.
FT   DISULFID   1374   1383       {ECO:0000250}.
FT   DISULFID   1391   1403       {ECO:0000250}.
FT   DISULFID   1397   1414       {ECO:0000250}.
FT   DISULFID   1416   1425       {ECO:0000250}.
FT   DISULFID   1449   1472       {ECO:0000250}.
FT   DISULFID   1454   1467       {ECO:0000250}.
FT   DISULFID   1463   1479       {ECO:0000250}.
FT   DISULFID   1490   1514       {ECO:0000250}.
FT   DISULFID   1496   1509       {ECO:0000250}.
FT   DISULFID   1505   1521       {ECO:0000250}.
FT   DISULFID   1536   1549       {ECO:0000250}.
FT   DISULFID   1545   1561       {ECO:0000250}.
FT   CROSSLNK   1749   1749       Glycyl lysine isopeptide (Lys-Gly)
FT                                (interchain with G-Cter in ubiquitin).
FT                                {ECO:0000269|PubMed:15240571}.
FT   VAR_SEQ       1     47       MPRLLTPLLCLTLLPALAARGLRCSQPSGTCLNGGRCEVAN
FT                                GTEACV -> MQTPLLSLAGATTELCFLPASVLASSLPGPS
FT                                L (in isoform 4). {ECO:0000305}.
FT                                /FTId=VSP_043065.
FT   VAR_SEQ       1     21       MPRLLTPLLCLTLLPALAARG -> MKNSNTLTNKWRMEQC
FT                                (in isoform 3). {ECO:0000305}.
FT                                /FTId=VSP_043064.
FT   VAR_SEQ     857    914       Missing (in isoform 2).
FT                                {ECO:0000303|PubMed:1426644}.
FT                                /FTId=VSP_001402.
FT   VAR_SEQ    1329   1355       Missing (in isoform 2).
FT                                {ECO:0000303|PubMed:1426644}.
FT                                /FTId=VSP_001403.
FT   VAR_SEQ    1636   1854       Missing (in isoform 2).
FT                                {ECO:0000303|PubMed:1426644}.
FT                                /FTId=VSP_001404.
FT   MUTAGEN      65     65       S->A: No effect.
FT                                {ECO:0000269|PubMed:21757702}.
FT   MUTAGEN     146    146       S->A: No effect.
FT                                {ECO:0000269|PubMed:21757702}.
FT   MUTAGEN     232    232       T->V: No significant effect on its
FT                                binding and activation by DLL1 or JAG1.
FT                                No significant effect on RFNG-, LFNG- and
FT                                MFNG-mediated enhancement of its
FT                                activation by DLL1. Decrease in LFNG- and
FT                                MFNG-mediated inhibition of its
FT                                activation by JAG1. Significant decrease
FT                                in LFNG- and MFNG-mediated inhibition of
FT                                its activation by JAG1; when associated
FT                                with V-1402.
FT                                {ECO:0000269|PubMed:28089369}.
FT   MUTAGEN     311    311       T->V: Significant loss of binding and
FT                                activation by DLL1 or JAG1. Decrease in
FT                                RFNG-, LFNG- and MFNG-mediated
FT                                enhancement of its activation by DLL1.
FT                                Decrease in LFNG-mediated inhibition of
FT                                its activation by JAG1. Significant loss
FT                                of binding and activation by DLL1 or JAG1
FT                                and complete loss of RFNG- and LFNG-
FT                                mediated enhancement of its activation by
FT                                DLL1; when associated with V-466.
FT                                Decreased localization to the plasma
FT                                membrane; when associated with A-435.
FT                                {ECO:0000269|PubMed:28089369,
FT                                ECO:0000269|PubMed:30127001}.
FT   MUTAGEN     341    341       S->A: No effect.
FT                                {ECO:0000269|PubMed:21757702}.
FT   MUTAGEN     349    349       T->V: Reduced binding and activation by
FT                                JAG1 but not DLL1. Decrease in MFNG-
FT                                mediated enhancement of its activation by
FT                                DLL1. {ECO:0000269|PubMed:28089369}.
FT   MUTAGEN     378    378       S->A: No effect.
FT                                {ECO:0000269|PubMed:21757702}.
FT   MUTAGEN     435    435       S->A: No effect on localization to the
FT                                plasma membrane. No effect on binding and
FT                                activation by DLL1. Decreased
FT                                localization to the plasma membrane; when
FT                                associated with V-311.
FT                                {ECO:0000269|PubMed:30127001}.
FT   MUTAGEN     458    458       S->A: No effect.
FT                                {ECO:0000269|PubMed:21757702}.
FT   MUTAGEN     466    466       T->V: Reduced binding and activation by
FT                                DLL1 but not JAG1. Decrease in RFNG- and
FT                                LFNG-mediated enhancement of its
FT                                activation by DLL1. Loss of RFNG-mediated
FT                                enhancement of its activation by JAG1.
FT                                Significant loss of binding and
FT                                activation by DLL1 or JAG1 and complete
FT                                loss of RFNG- and LFNG-mediated
FT                                enhancement of its activation by DLL1;
FT                                when associated with V-311.
FT                                {ECO:0000269|PubMed:28089369}.
FT   MUTAGEN     496    496       S->A: No effect.
FT                                {ECO:0000269|PubMed:21757702}.
FT   MUTAGEN     534    534       S->A: No effect.
FT                                {ECO:0000269|PubMed:21757702}.
FT   MUTAGEN     609    609       S->A: No effect.
FT                                {ECO:0000269|PubMed:21757702}.
FT   MUTAGEN     647    647       S->A: No effect.
FT                                {ECO:0000269|PubMed:21757702}.
FT   MUTAGEN     722    722       S->A: No effect.
FT                                {ECO:0000269|PubMed:21757702}.
FT   MUTAGEN     759    759       S->A: No effect.
FT                                {ECO:0000269|PubMed:21757702}.
FT   MUTAGEN     797    797       S->A: No effect.
FT                                {ECO:0000269|PubMed:21757702}.
FT   MUTAGEN     951    951       S->A: No effect.
FT                                {ECO:0000269|PubMed:21757702}.
FT   MUTAGEN     997    997       T->V: Reduced binding and activation by
FT                                DLL1 but not JAG1. No effect on RFNG-,
FT                                LFNG- and MFNG-mediated enhancement of
FT                                its activation by DLL1. No effect on
FT                                LFNG- and MFNG-mediated inhibition of its
FT                                activation by JAG1.
FT                                {ECO:0000269|PubMed:28089369}.
FT   MUTAGEN    1027   1027       S->A: No effect.
FT                                {ECO:0000269|PubMed:21757702}.
FT   MUTAGEN    1035   1035       T->V: Reduced binding and activation by
FT                                JAG1 but not DLL1. No effect on RFNG-,
FT                                LFNG- and MFNG-mediated enhancement of
FT                                its activation by DLL1. No effect on
FT                                LFNG- and MFNG-mediated inhibition of its
FT                                activation by JAG1.
FT                                {ECO:0000269|PubMed:28089369}.
FT   MUTAGEN    1065   1065       S->A: Reduced activity.
FT                                {ECO:0000269|PubMed:21757702}.
FT   MUTAGEN    1159   1159       T->V: No significant effect on its
FT                                binding and activation by DLL1 or JAG1.
FT                                No effect on RFNG-, LFNG- and MFNG-
FT                                mediated enhancement of its activation by
FT                                DLL1. No effect on LFNG- and MFNG-
FT                                mediated inhibition of its activation by
FT                                JAG1. {ECO:0000269|PubMed:28089369}.
FT   MUTAGEN    1189   1189       S->A: No effect.
FT                                {ECO:0000269|PubMed:21757702}.
FT   MUTAGEN    1273   1273       S->A: No effect.
FT                                {ECO:0000269|PubMed:21757702}.
FT   MUTAGEN    1362   1362       T->V: No significant effect on its
FT                                binding and activation by DLL1 or JAG1.
FT                                No effect on RFNG-, LFNG- and MFNG-
FT                                mediated enhancement of its activation by
FT                                DLL1. No effect on LFNG- and MFNG-
FT                                mediated inhibition of its activation by
FT                                JAG1. {ECO:0000269|PubMed:28089369}.
FT   MUTAGEN    1402   1402       T->V: No significant effect on its
FT                                binding and activation by DLL1 or JAG1.
FT                                No effect on RFNG-, LFNG- and MFNG-
FT                                mediated enhancement of its activation by
FT                                DLL1. Decrease in LFNG- and MFNG-mediated
FT                                inhibition of its activation by JAG1.
FT                                Significant decrease in LFNG- and MFNG-
FT                                mediated inhibition of its activation by
FT                                JAG1; when associated with V-232.
FT                                {ECO:0000269|PubMed:28089369}.
FT   MUTAGEN    1651   1654       RQRR->AAAA: Processing by furin-like
FT                                convertase abolished.
FT                                {ECO:0000269|PubMed:9653148}.
FT   MUTAGEN    1675   1675       C->S: Produces an activated, ligand-
FT                                independent molecule; when associated
FT                                with S-1682.
FT                                {ECO:0000269|PubMed:10882062}.
FT   MUTAGEN    1682   1682       C->S: Produces an activated, ligand-
FT                                independent molecule; when associated
FT                                with S-1675.
FT                                {ECO:0000269|PubMed:10882062}.
FT   MUTAGEN    1744   1744       V->L: NICD processing severely reduced.
FT   MUTAGEN    1945   1945       N->A: Reduced ability to promote HIF1AN-
FT                                dependent 2-oxoglutarate decarboxylation
FT                                and greatly reduced transactivation
FT                                capacity. Abolished ability to promote
FT                                HIF1AN-dependent 2-oxoglutarate
FT                                decarboxylation; when associated with G-
FT                                2012. Almost abolished transactivation
FT                                capacity; when associated with A-2012.
FT                                {ECO:0000269|PubMed:17573339,
FT                                ECO:0000269|PubMed:18299578}.
FT   MUTAGEN    2012   2012       N->A: Slightly reduced ability to promote
FT                                HIF1AN-dependent 2-oxoglutarate
FT                                decarboxylation. Abolished ability to
FT                                promote HIF1AN-dependent 2-oxoglutarate
FT                                decarboxylation and almost abolished
FT                                transactivation capacity; when associated
FT                                with A-1945.
FT                                {ECO:0000269|PubMed:17573339,
FT                                ECO:0000269|PubMed:18299578}.
FT   MUTAGEN    2012   2012       N->G: Reduced ability to promote HIF1AN-
FT                                dependent 2-oxoglutarate decarboxylation.
FT                                Abolished ability to promote HIF1AN-
FT                                dependent 2-oxoglutarate decarboxylation;
FT                                when associated with A-1945.
FT                                {ECO:0000269|PubMed:17573339,
FT                                ECO:0000269|PubMed:18299578}.
FT   CONFLICT     17     17       L -> R (in Ref. 1; CAA77941).
FT                                {ECO:0000305}.
FT   CONFLICT     41     41       N -> S (in Ref. 1; CAA77941 and 3;
FT                                AAM28905). {ECO:0000305}.
FT   CONFLICT     48     48       C -> A (in Ref. 1; CAA77941).
FT                                {ECO:0000305}.
FT   CONFLICT     51     51       A -> S (in Ref. 1; CAA77941).
FT                                {ECO:0000305}.
FT   CONFLICT     60     60       S -> P (in Ref. 1; CAA77941).
FT                                {ECO:0000305}.
FT   CONFLICT     67     67       P -> R (in Ref. 1; CAA77941).
FT                                {ECO:0000305}.
FT   CONFLICT     75     75       H -> Y (in Ref. 1; CAA77941).
FT                                {ECO:0000305}.
FT   CONFLICT     82     82       T -> I (in Ref. 1; CAA77941).
FT                                {ECO:0000305}.
FT   CONFLICT    104    105       NA -> KP (in Ref. 1; CAA77941).
FT                                {ECO:0000305}.
FT   CONFLICT    130    130       P -> S (in Ref. 1; CAA77941).
FT                                {ECO:0000305}.
FT   CONFLICT    194    194       T -> H (in Ref. 1; CAA77941).
FT                                {ECO:0000305}.
FT   CONFLICT    207    207       R -> C (in Ref. 1; CAA77941).
FT                                {ECO:0000305}.
FT   CONFLICT    231    231       G -> A (in Ref. 1; CAA77941).
FT                                {ECO:0000305}.
FT   CONFLICT    287    287       W -> V (in Ref. 1; CAA77941).
FT                                {ECO:0000305}.
FT   CONFLICT    309    309       G -> A (in Ref. 1; CAA77941).
FT                                {ECO:0000305}.
FT   CONFLICT    373    374       ND -> KH (in Ref. 1; CAA77941).
FT                                {ECO:0000305}.
FT   CONFLICT    396    396       A -> R (in Ref. 1; CAA77941).
FT                                {ECO:0000305}.
FT   CONFLICT    417    417       A -> D (in Ref. 1; CAA77941).
FT                                {ECO:0000305}.
FT   CONFLICT    422    422       P -> R (in Ref. 1; CAA77941).
FT                                {ECO:0000305}.
FT   CONFLICT    448    448       R -> G (in Ref. 1; CAA77941).
FT                                {ECO:0000305}.
FT   CONFLICT    510    510       N -> H (in Ref. 1; CAA77941).
FT                                {ECO:0000305}.
FT   CONFLICT    835    835       T -> I (in Ref. 8; AAK14898).
FT                                {ECO:0000305}.
FT   CONFLICT    933    934       CL -> SV (in Ref. 8; AAK14898).
FT                                {ECO:0000305}.
FT   CONFLICT   1050   1050       G -> R (in Ref. 8; AAK14898).
FT                                {ECO:0000305}.
FT   CONFLICT   1104   1106       Missing (in Ref. 8; AAK14898).
FT                                {ECO:0000305}.
FT   CONFLICT   1155   1155       Q -> L (in Ref. 8; AAK14898).
FT                                {ECO:0000305}.
FT   CONFLICT   1209   1209       C -> W (in Ref. 8; AAK14898).
FT                                {ECO:0000305}.
FT   CONFLICT   1438   1438       R -> P (in Ref. 1; CAA77941).
FT                                {ECO:0000305}.
FT   CONFLICT   1545   1545       C -> S (in Ref. 8; AAK14898).
FT                                {ECO:0000305}.
FT   CONFLICT   1556   1556       W -> R (in Ref. 8; AAK14898).
FT                                {ECO:0000305}.
FT   CONFLICT   1572   1572       G -> R (in Ref. 8; AAK14898).
FT                                {ECO:0000305}.
FT   CONFLICT   1576   1576       L -> V (in Ref. 8; AAK14898).
FT                                {ECO:0000305}.
FT   CONFLICT   1609   1609       D -> H (in Ref. 8; AAK14898).
FT                                {ECO:0000305}.
FT   CONFLICT   1661   1661       I -> T (in Ref. 10; BAE32653).
FT                                {ECO:0000305}.
FT   CONFLICT   1864   1864       V -> D (in Ref. 8; AAK14898).
FT                                {ECO:0000305}.
FT   CONFLICT   1890   1890       S -> R (in Ref. 8; AAK14898).
FT                                {ECO:0000305}.
FT   CONFLICT   1896   1898       APA -> RPG (in Ref. 8; AAK14898).
FT                                {ECO:0000305}.
FT   CONFLICT   1933   1934       AA -> RR (in Ref. 1; CAA77941).
FT                                {ECO:0000305}.
FT   CONFLICT   1938   1938       Missing (in Ref. 1; CAA77941).
FT                                {ECO:0000305}.
FT   CONFLICT   1997   1997       V -> L (in Ref. 3; AAM28905).
FT                                {ECO:0000305}.
FT   CONFLICT   2046   2047       MQ -> IE (in Ref. 1; CAA77941).
FT                                {ECO:0000305}.
FT   CONFLICT   2054   2054       P -> S (in Ref. 1; CAA77941).
FT                                {ECO:0000305}.
FT   CONFLICT   2058   2062       AAREG -> SIRRE (in Ref. 1; CAA77941).
FT                                {ECO:0000305}.
FT   CONFLICT   2075   2075       A -> G (in Ref. 16; CAA57909).
FT                                {ECO:0000305}.
FT   CONFLICT   2086   2086       L -> M (in Ref. 10; BAE34095).
FT                                {ECO:0000305}.
FT   CONFLICT   2136   2136       L -> P (in Ref. 1; CAA77941).
FT                                {ECO:0000305}.
FT   CONFLICT   2172   2172       K -> S (in Ref. 1; CAA77941).
FT                                {ECO:0000305}.
FT   CONFLICT   2179   2179       C -> W (in Ref. 1; CAA77941).
FT                                {ECO:0000305}.
FT   CONFLICT   2185   2185       S -> SS (in Ref. 1; CAA77941).
FT                                {ECO:0000305}.
FT   CONFLICT   2206   2206       P -> H (in Ref. 1; CAA77941).
FT                                {ECO:0000305}.
FT   CONFLICT   2258   2258       P -> H (in Ref. 1; CAA77941).
FT                                {ECO:0000305}.
FT   CONFLICT   2273   2273       S -> C (in Ref. 1; CAA77941).
FT                                {ECO:0000305}.
FT   CONFLICT   2347   2347       N -> S (in Ref. 10; BAE34095).
FT                                {ECO:0000305}.
FT   CONFLICT   2380   2380       Q -> P (in Ref. 1; CAA77941).
FT                                {ECO:0000305}.
FT   CONFLICT   2483   2484       HP -> PT (in Ref. 1; CAA77941).
FT                                {ECO:0000305}.
FT   HELIX       456    458       {ECO:0000244|PDB:5KY0}.
FT   STRAND      462    464       {ECO:0000244|PDB:2RQZ}.
FT   STRAND      466    469       {ECO:0000244|PDB:5KY0}.
FT   STRAND      470    472       {ECO:0000244|PDB:2RR0}.
FT   STRAND      474    477       {ECO:0000244|PDB:5KY0}.
FT   STRAND      482    484       {ECO:0000244|PDB:5KY0}.
FT   STRAND      997   1000       {ECO:0000244|PDB:5KY4}.
FT   STRAND     1005   1008       {ECO:0000244|PDB:5KY4}.
FT   STRAND     1013   1015       {ECO:0000244|PDB:5KY4}.
FT   HELIX      1921   1927       {ECO:0000244|PDB:2QC9}.
FT   HELIX      1931   1939       {ECO:0000244|PDB:2QC9}.
FT   HELIX      1954   1961       {ECO:0000244|PDB:2QC9}.
FT   HELIX      1964   1972       {ECO:0000244|PDB:2QC9}.
FT   HELIX      1975   1977       {ECO:0000244|PDB:1YMP}.
FT   HELIX      1988   1995       {ECO:0000244|PDB:1YMP}.
FT   HELIX      2000   2006       {ECO:0000244|PDB:1YMP}.
FT   HELIX      2021   2027       {ECO:0000244|PDB:1YMP}.
FT   HELIX      2031   2039       {ECO:0000244|PDB:1YMP}.
FT   HELIX      2054   2061       {ECO:0000244|PDB:1YMP}.
FT   HELIX      2064   2072       {ECO:0000244|PDB:1YMP}.
FT   HELIX      2087   2093       {ECO:0000244|PDB:1YMP}.
FT   HELIX      2097   2103       {ECO:0000244|PDB:1YMP}.
SQ   SEQUENCE   2531 AA;  270835 MW;  97C91F69BABF02BF CRC64;
     MPRLLTPLLC LTLLPALAAR GLRCSQPSGT CLNGGRCEVA NGTEACVCSG AFVGQRCQDS
     NPCLSTPCKN AGTCHVVDHG GTVDYACSCP LGFSGPLCLT PLDNACLANP CRNGGTCDLL
     TLTEYKCRCP PGWSGKSCQQ ADPCASNPCA NGGQCLPFES SYICRCPPGF HGPTCRQDVN
     ECSQNPGLCR HGGTCHNEIG SYRCACRATH TGPHCELPYV PCSPSPCQNG GTCRPTGDTT
     HECACLPGFA GQNCEENVDD CPGNNCKNGG ACVDGVNTYN CRCPPEWTGQ YCTEDVDECQ
     LMPNACQNGG TCHNTHGGYN CVCVNGWTGE DCSENIDDCA SAACFQGATC HDRVASFYCE
     CPHGRTGLLC HLNDACISNP CNEGSNCDTN PVNGKAICTC PSGYTGPACS QDVDECALGA
     NPCEHAGKCL NTLGSFECQC LQGYTGPRCE IDVNECISNP CQNDATCLDQ IGEFQCICMP
     GYEGVYCEIN TDECASSPCL HNGHCMDKIN EFQCQCPKGF NGHLCQYDVD ECASTPCKNG
     AKCLDGPNTY TCVCTEGYTG THCEVDIDEC DPDPCHYGSC KDGVATFTCL CQPGYTGHHC
     ETNINECHSQ PCRHGGTCQD RDNSYLCLCL KGTTGPNCEI NLDDCASNPC DSGTCLDKID
     GYECACEPGY TGSMCNVNID ECAGSPCHNG GTCEDGIAGF TCRCPEGYHD PTCLSEVNEC
     NSNPCIHGAC RDGLNGYKCD CAPGWSGTNC DINNNECESN PCVNGGTCKD MTSGYVCTCR
     EGFSGPNCQT NINECASNPC LNQGTCIDDV AGYKCNCPLP YTGATCEVVL APCATSPCKN
     SGVCKESEDY ESFSCVCPTG WQGQTCEVDI NECVKSPCRH GASCQNTNGS YRCLCQAGYT
     GRNCESDIDD CRPNPCHNGG SCTDGINTAF CDCLPGFQGA FCEEDINECA SNPCQNGANC
     TDCVDSYTCT CPVGFNGIHC ENNTPDCTES SCFNGGTCVD GINSFTCLCP PGFTGSYCQY
     DVNECDSRPC LHGGTCQDSY GTYKCTCPQG YTGLNCQNLV RWCDSAPCKN GGRCWQTNTQ
     YHCECRSGWT GVNCDVLSVS CEVAAQKRGI DVTLLCQHGG LCVDEGDKHY CHCQAGYTGS
     YCEDEVDECS PNPCQNGATC TDYLGGFSCK CVAGYHGSNC SEEINECLSQ PCQNGGTCID
     LTNSYKCSCP RGTQGVHCEI NVDDCHPPLD PASRSPKCFN NGTCVDQVGG YTCTCPPGFV
     GERCEGDVNE CLSNPCDPRG TQNCVQRVND FHCECRAGHT GRRCESVING CRGKPCKNGG
     VCAVASNTAR GFICRCPAGF EGATCENDAR TCGSLRCLNG GTCISGPRSP TCLCLGSFTG
     PECQFPASSP CVGSNPCYNQ GTCEPTSENP FYRCLCPAKF NGLLCHILDY SFTGGAGRDI
     PPPQIEEACE LPECQVDAGN KVCNLQCNNH ACGWDGGDCS LNFNDPWKNC TQSLQCWKYF
     SDGHCDSQCN SAGCLFDGFD CQLTEGQCNP LYDQYCKDHF SDGHCDQGCN SAECEWDGLD
     CAEHVPERLA AGTLVLVVLL PPDQLRNNSF HFLRELSHVL HTNVVFKRDA QGQQMIFPYY
     GHEEELRKHP IKRSTVGWAT SSLLPGTSGG RQRRELDPMD IRGSIVYLEI DNRQCVQSSS
     QCFQSATDVA AFLGALASLG SLNIPYKIEA VKSEPVEPPL PSQLHLMYVA AAAFVLLFFV
     GCGVLLSRKR RRQHGQLWFP EGFKVSEASK KKRREPLGED SVGLKPLKNA SDGALMDDNQ
     NEWGDEDLET KKFRFEEPVV LPDLSDQTDH RQWTQQHLDA ADLRMSAMAP TPPQGEVDAD
     CMDVNVRGPD GFTPLMIASC SGGGLETGNS EEEEDAPAVI SDFIYQGASL HNQTDRTGET
     ALHLAARYSR SDAAKRLLEA SADANIQDNM GRTPLHAAVS ADAQGVFQIL LRNRATDLDA
     RMHDGTTPLI LAARLAVEGM LEDLINSHAD VNAVDDLGKS ALHWAAAVNN VDAAVVLLKN
     GANKDMQNNK EETPLFLAAR EGSYETAKVL LDHFANRDIT DHMDRLPRDI AQERMHHDIV
     RLLDEYNLVR SPQLHGTALG GTPTLSPTLC SPNGYLGNLK SATQGKKARK PSTKGLACGS
     KEAKDLKARR KKSQDGKGCL LDSSSMLSPV DSLESPHGYL SDVASPPLLP SPFQQSPSMP
     LSHLPGMPDT HLGISHLNVA AKPEMAALAG GSRLAFEPPP PRLSHLPVAS SASTVLSTNG
     TGAMNFTVGA PASLNGQCEW LPRLQNGMVP SQYNPLRPGV TPGTLSTQAA GLQHSMMGPL
     HSSLSTNTLS PIIYQGLPNT RLATQPHLVQ TQQVQPQNLQ LQPQNLQPPS QPHLSVSSAA
     NGHLGRSFLS GEPSQADVQP LGPSSLPVHT ILPQESQALP TSLPSSMVPP MTTTQFLTPP
     SQHSYSSSPV DNTPSHQLQV PEHPFLTPSP ESPDQWSSSS PHSNISDWSE GISSPPTTMP
     SQITHIPEAF K
//
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