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Delta-like protein 1 (Drosophila Delta homolog 1) (Delta1) [Cleaved into: Dll1-soluble form (Dll1-EC) (Shed form); Dll1-derived cell-associated form (Dll1-TMIC) (Membrane-associated fragment); Dll1-intracellular form (Dll1-IC)]

 DLL1_MOUSE              Reviewed;         722 AA.
Q61483; Q6PFV7;
01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
27-JUL-2011, sequence version 2.
07-APR-2021, entry version 189.
RecName: Full=Delta-like protein 1 {ECO:0000305};
AltName: Full=Drosophila Delta homolog 1;
Short=Delta1 {ECO:0000303|PubMed:12794186};
Contains:
RecName: Full=Dll1-soluble form {ECO:0000303|PubMed:12794186};
Short=Dll1-EC {ECO:0000305|PubMed:12794186};
Short=Shed form {ECO:0000303|PubMed:12794186};
Contains:
RecName: Full=Dll1-derived cell-associated form {ECO:0000303|PubMed:12794186};
Short=Dll1-TMIC {ECO:0000305|PubMed:12794186};
Short=Membrane-associated fragment {ECO:0000303|PubMed:12794186};
Contains:
RecName: Full=Dll1-intracellular form {ECO:0000303|PubMed:12794186};
Short=Dll1-IC {ECO:0000305|PubMed:12794186};
Flags: Precursor;
Name=Dll1;
Mus musculus (Mouse).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
Murinae; Mus; Mus.
NCBI_TaxID=10090;
[1]
NUCLEOTIDE SEQUENCE [MRNA], DEVELOPMENTAL STAGE, TISSUE SPECIFICITY, AND
FUNCTION.
STRAIN=C57BL/6 X BALB/c; TISSUE=Embryo;
PubMed=7671806;
Bettenhausen B., de Angelis M.H., Simon D., Guenet J.-L., Gossler A.;
"Transient and restricted expression during mouse embryogenesis of Dll1, a
murine gene closely related to Drosophila Delta.";
Development 121:2407-2418(1995).
[2]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=C57BL/6J;
PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., She X.,
Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., Kapustin Y.,
Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., Zhou S.,
Teague B., Potamousis K., Churas C., Place M., Herschleb J., Runnheim R.,
Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., Lindblad-Toh K.,
Eichler E.E., Ponting C.P.;
"Lineage-specific biology revealed by a finished genome assembly of the
mouse.";
PLoS Biol. 7:E1000112-E1000112(2009).
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Mural R.J., Adams M.D., Myers E.W., Smith H.O., Venter J.C.;
Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
STRAIN=C57BL/6J; TISSUE=Embryonic brain;
PubMed=15489334; DOI=10.1101/gr.2596504;
The MGC Project Team;
"The status, quality, and expansion of the NIH full-length cDNA project:
the Mammalian Gene Collection (MGC).";
Genome Res. 14:2121-2127(2004).
[5]
PROTEIN SEQUENCE OF 527-534 AND 536-543, PROTEOLYTIC CLEAVAGE BY MMP14,
INTERACTION WITH MMP14, IDENTIFICATION BY MASS SPECTROMETRY, AND FUNCTION.
PubMed=21572390; DOI=10.1038/emboj.2011.136;
Jin G., Zhang F., Chan K.M., Xavier Wong H.L., Liu B., Cheah K.S., Liu X.,
Mauch C., Liu D., Zhou Z.;
"MT1-MMP cleaves Dll1 to negatively regulate Notch signalling to maintain
normal B-cell development.";
EMBO J. 30:2281-2293(2011).
[6]
PROTEIN SEQUENCE OF 536-554, PROTEOLYTIC CLEAVAGE, HOMODIMERIZATION,
INTERACTION WITH PSEN1, AND SUBCELLULAR LOCATION.
PubMed=12794186; DOI=10.1073/pnas.1230693100;
Six E., Ndiaye D., Laabi Y., Brou C., Gupta-Rossi N., Israel A., Logeat F.;
"The Notch ligand Delta1 is sequentially cleaved by an ADAM protease and
gamma-secretase.";
Proc. Natl. Acad. Sci. U.S.A. 100:7638-7643(2003).
[7]
FUNCTION.
PubMed=10958687; DOI=10.1128/mcb.20.18.6913-6922.2000;
Shimizu K., Chiba S., Hosoya N., Kumano K., Saito T., Kurokawa M.,
Kanda Y., Hamada Y., Hirai H.;
"Binding of Delta1, Jagged1, and Jagged2 to Notch2 rapidly induces
cleavage, nuclear translocation, and hyperphosphorylation of Notch2.";
Mol. Cell. Biol. 20:6913-6922(2000).
[8]
FUNCTION.
PubMed=15146182; DOI=10.1038/ni1075;
Hozumi K., Negishi N., Suzuki D., Abe N., Sotomaru Y., Tamaoki N.,
Mailhos C., Ish-Horowicz D., Habu S., Owen M.J.;
"Delta-like 1 is necessary for the generation of marginal zone B cells but
not T cells in vivo.";
Nat. Immunol. 5:638-644(2004).
[9]
INTERACTION WITH MFAP5.
PubMed=15788413; DOI=10.1074/jbc.m500273200;
Nehring L.C., Miyamoto A., Hein P.W., Weinmaster G., Shipley J.M.;
"The extracellular matrix protein MAGP-2 interacts with Jagged1 and induces
its shedding from the cell surface.";
J. Biol. Chem. 280:20349-20355(2005).
[10]
INTERACTION WITH MAGI1, AND SUBCELLULAR LOCATION.
PubMed=15908431; DOI=10.1074/jbc.m500375200;
Mizuhara E., Nakatani T., Minaki Y., Sakamoto Y., Ono Y., Takai Y.;
"MAGI1 recruits Dll1 to cadherin-based adherens junctions and stabilizes it
on the cell surface.";
J. Biol. Chem. 280:26499-26507(2005).
[11]
FUNCTION, AND DISRUPTION PHENOTYPE.
PubMed=16495313; DOI=10.1242/dev.02284;
Brooker R., Hozumi K., Lewis J.;
"Notch ligands with contrasting functions: Jagged1 and Delta1 in the mouse
inner ear.";
Development 133:1277-1286(2006).
[12]
INTERACTION WITH NEURL1B, AND UBIQUITINATION.
PubMed=17003037; DOI=10.1074/jbc.m606601200;
Song R., Koo B.-K., Yoon K.-J., Yoon M.-J., Yoo K.-W., Kim H.-T., Oh H.-J.,
Kim Y.-Y., Han J.-K., Kim C.-H., Kong Y.-Y.;
"Neuralized-2 regulates a Notch ligand in cooperation with Mind bomb-1.";
J. Biol. Chem. 281:36391-36400(2006).
[13]
DEVELOPMENTAL STAGE, DISRUPTION PHENOTYPE, AND FUNCTION.
PubMed=17194759; DOI=10.1073/pnas.0608281104;
Schuster-Gossler K., Cordes R., Gossler A.;
"Premature myogenic differentiation and depletion of progenitor cells cause
severe muscle hypotrophy in Delta1 mutants.";
Proc. Natl. Acad. Sci. U.S.A. 104:537-542(2007).
[14]
FUNCTION, DEVELOPMENTAL STAGE, AND DISRUPTION PHENOTYPE.
PubMed=18997111; DOI=10.1242/dev.024570;
Kawaguchi D., Yoshimatsu T., Hozumi K., Gotoh Y.;
"Selection of differentiating cells by different levels of delta-like 1
among neural precursor cells in the developing mouse telencephalon.";
Development 135:3849-3858(2008).
[15]
FUNCTION, AND DISRUPTION PHENOTYPE.
PubMed=17960184; DOI=10.1038/sj.jid.5701113;
Estrach S., Cordes R., Hozumi K., Gossler A., Watt F.M.;
"Role of the Notch ligand Delta1 in embryonic and adult mouse epidermis.";
J. Invest. Dermatol. 128:825-832(2008).
[16]
UBIQUITINATION, FUNCTION, AND SUBCELLULAR LOCATION.
PubMed=18676613; DOI=10.1073/pnas.0800695105;
Heuss S.F., Ndiaye-Lobry D., Six E.M., Israel A., Logeat F.;
"The intracellular region of Notch ligands Dll1 and Dll3 regulates their
trafficking and signaling activity.";
Proc. Natl. Acad. Sci. U.S.A. 105:11212-11217(2008).
[17]
INTERACTION WITH NEURL1 AND NEURL1B.
PubMed=19723503; DOI=10.1016/j.bbrc.2009.08.147;
Rullinkov G., Tamme R., Sarapuu A., Lauren J., Sepp M., Palm K.,
Timmusk T.;
"Neuralized-2: Expression in human and rodents and interaction with Delta-
like ligands.";
Biochem. Biophys. Res. Commun. 389:420-425(2009).
[18]
DEVELOPMENTAL STAGE, DISRUPTION PHENOTYPE, AND FUNCTION.
PubMed=19144989; DOI=10.1182/blood-2008-08-174508;
Soerensen I., Adams R.H., Gossler A.;
"DLL1-mediated Notch activation regulates endothelial identity in mouse
fetal arteries.";
Blood 113:5680-5688(2009).
[19]
FUNCTION, AND DEVELOPMENTAL STAGE.
PubMed=19389377; DOI=10.1016/j.ydbio.2009.01.011;
Rocha S.F., Lopes S.S., Gossler A., Henrique D.;
"Dll1 and Dll4 function sequentially in the retina and pV2 domain of the
spinal cord to regulate neurogenesis and create cell diversity.";
Dev. Biol. 328:54-65(2009).
[20]
FUNCTION.
PubMed=19217325; DOI=10.1016/j.immuni.2008.12.016;
Tan J.B., Xu K., Cretegny K., Visan I., Yuan J.S., Egan S.E., Guidos C.J.;
"Lunatic and manic fringe cooperatively enhance marginal zone B cell
precursor competition for delta-like 1 in splenic endothelial niches.";
Immunity 30:254-263(2009).
[21]
DISRUPTION PHENOTYPE, AND FUNCTION.
PubMed=19562077; DOI=10.1371/journal.pone.0006054;
Rubio-Aliaga I., Przemeck G.K., Fuchs H., Gailus-Durner V., Adler T.,
Hans W., Horsch M., Rathkolb B., Rozman J., Schrewe A., Wagner S.,
Hoelter S.M., Becker L., Klopstock T., Wurst W., Wolf E., Klingenspor M.,
Ivandic B.T., Busch D.H., Beckers J., Hrabe de Angelis M.;
"Dll1 haploinsufficiency in adult mice leads to a complex phenotype
affecting metabolic and immunological processes.";
PLoS ONE 4:E6054-E6054(2009).
[22]
FUNCTION.
PubMed=20081190; DOI=10.1242/dev.036806;
Marklund U., Hansson E.M., Sundstroem E., de Angelis M.H., Przemeck G.K.,
Lendahl U., Muhr J., Ericson J.;
"Domain-specific control of neurogenesis achieved through patterned
regulation of Notch ligand expression.";
Development 137:437-445(2010).
[23]
MUTAGENESIS OF 613-LYS--LYS-618; LYS-613; LYS-689; LYS-699 AND LYS-713,
INTERACTION WITH MIB1, SUBCELLULAR LOCATION, FUNCTION, AND UBIQUITINATION
AT LYS-613.
PubMed=21985982; DOI=10.1016/j.bbamcr.2011.08.019;
Zhang L., Widau R.C., Herring B.P., Gallagher P.J.;
"Delta-like 1-Lysine613 regulates notch signaling.";
Biochim. Biophys. Acta 1813:2036-2043(2011).
[24]
FUNCTION.
PubMed=21238454; DOI=10.1053/j.gastro.2011.01.005;
Pellegrinet L., Rodilla V., Liu Z., Chen S., Koch U., Espinosa L.,
Kaestner K.H., Kopan R., Lewis J., Radtke F.;
"Dll1- and dll4-mediated notch signaling are required for homeostasis of
intestinal stem cells.";
Gastroenterology 140:1230-1240(2011).
[25]
FUNCTION.
PubMed=21915337; DOI=10.1371/journal.pone.0024484;
Stamataki D., Holder M., Hodgetts C., Jeffery R., Nye E., Spencer-Dene B.,
Winton D.J., Lewis J.;
"Delta1 expression, cell cycle exit, and commitment to a specific secretory
fate coincide within a few hours in the mouse intestinal stem cell
system.";
PLoS ONE 6:E24484-E24484(2011).
[26]
FUNCTION.
PubMed=22282195; DOI=10.1161/circresaha.111.263319;
Napp L.C., Augustynik M., Paesler F., Krishnasamy K., Woiterski J.,
Limbourg A., Bauersachs J., Drexler H., Le Noble F., Limbourg F.P.;
"Extrinsic Notch ligand Delta-like 1 regulates tip cell selection and
vascular branching morphogenesis.";
Circ. Res. 110:530-535(2012).
[27]
FUNCTION, AND INDUCTION.
PubMed=22096075; DOI=10.1242/dev.071761;
Ahnfelt-Roenne J., Joergensen M.C., Klinck R., Jensen J.N.,
Fuechtbauer E.M., Deering T., MacDonald R.J., Wright C.V., Madsen O.D.,
Serup P.;
"Ptf1a-mediated control of Dll1 reveals an alternative to the lateral
inhibition mechanism.";
Development 139:33-45(2012).
[28]
INDUCTION.
PubMed=22015720; DOI=10.1016/j.ydbio.2011.09.034;
Grainger S., Lam J., Savory J.G., Mears A.J., Rijli F.M., Lohnes D.;
"Cdx regulates Dll1 in multiple lineages.";
Dev. Biol. 361:1-11(2012).
[29]
FUNCTION.
PubMed=22940113; DOI=10.1016/j.devcel.2012.07.014;
Broehl D., Vasyutina E., Czajkowski M.T., Griger J., Rassek C., Rahn H.P.,
Purfuerst B., Wende H., Birchmeier C.;
"Colonization of the satellite cell niche by skeletal muscle progenitor
cells depends on Notch signals.";
Dev. Cell 23:469-481(2012).
[30]
FUNCTION.
PubMed=22529374; DOI=10.1073/pnas.1203605109;
Horn S., Kobberup S., Joergensen M.C., Kalisz M., Klein T., Kageyama R.,
Gegg M., Lickert H., Lindner J., Magnuson M.A., Kong Y.Y., Serup P.,
Ahnfelt-Roenne J., Jensen J.N.;
"Mind bomb 1 is required for pancreatic beta-cell formation.";
Proc. Natl. Acad. Sci. U.S.A. 109:7356-7361(2012).
[31]
FUNCTION.
PubMed=23806616; DOI=10.1016/j.devcel.2013.05.022;
Liu Z., Chen S., Boyle S., Zhu Y., Zhang A., Piwnica-Worms D.R.,
Ilagan M.X., Kopan R.;
"The extracellular domain of Notch2 increases its cell-surface abundance
and ligand responsiveness during kidney development.";
Dev. Cell 25:585-598(2013).
[32]
FUNCTION.
PubMed=23699523; DOI=10.1523/jneurosci.0791-13.2013;
Nelson B.R., Hodge R.D., Bedogni F., Hevner R.F.;
"Dynamic interactions between intermediate neurogenic progenitors and
radial glia in embryonic mouse neocortex: potential role in Dll1-Notch
signaling.";
J. Neurosci. 33:9122-9139(2013).
[33]
DISRUPTION PHENOTYPE, AND FUNCTION.
PubMed=23688253; DOI=10.1186/1756-6606-6-25;
Hiraoka Y., Komine O., Nagaoka M., Bai N., Hozumi K., Tanaka K.;
"Delta-like 1 regulates Bergmann glial monolayer formation during
cerebellar development.";
Mol. Brain 6:25-25(2013).
[34]
FUNCTION.
PubMed=23695674; DOI=10.1038/ncomms2895;
Kawaguchi D., Furutachi S., Kawai H., Hozumi K., Gotoh Y.;
"Dll1 maintains quiescence of adult neural stem cells and segregates
asymmetrically during mitosis.";
Nat. Commun. 4:1880-1880(2013).
[35]
INTERACTION WITH TJP1, AND SUBCELLULAR LOCATION.
PubMed=24715457; DOI=10.1242/dev.102988;
Hatakeyama J., Wakamatsu Y., Nagafuchi A., Kageyama R., Shigemoto R.,
Shimamura K.;
"Cadherin-based adhesions in the apical endfoot are required for active
Notch signaling to control neurogenesis in vertebrates.";
Development 141:1671-1682(2014).
[36]
FUNCTION, DEVELOPMENTAL STAGE, DISRUPTION PHENOTYPE, AND TISSUE
SPECIFICITY.
PubMed=25220152; DOI=10.1016/j.ydbio.2014.09.005;
Czajkowski M.T., Rassek C., Lenhard D.C., Broehl D., Birchmeier C.;
"Divergent and conserved roles of Dll1 signaling in development of
craniofacial and trunk muscle.";
Dev. Biol. 395:307-316(2014).
[37]
IDENTIFICATION BY MASS SPECTROMETRY, PHOSPHORYLATION AT THR-638; SER-693
AND SER-696, AND MUTAGENESIS OF THR-638; SER-693 AND SER-696.
PubMed=24449764; DOI=10.1128/mcb.00965-13;
Braune E.B., Schuster-Gossler K., Lyszkiewicz M., Serth K., Preusse K.,
Madlung J., Macek B., Krueger A., Gossler A.;
"S/T phosphorylation of DLL1 is required for full ligand activity in vitro
but dispensable for DLL1 function in vivo during embryonic patterning and
marginal zone B cell development.";
Mol. Cell. Biol. 34:1221-1233(2014).
[38]
FUNCTION.
PubMed=26114479; DOI=10.1371/journal.pgen.1005328;
Preusse K., Tveriakhina L., Schuster-Gossler K., Gaspar C., Rosa A.I.,
Henrique D., Gossler A., Stauber M.;
"Context-dependent functional divergence of the Notch ligands DLL1 and DLL4
in vivo.";
PLoS Genet. 11:E1005328-E1005328(2015).
-!- FUNCTION: Transmembrane ligand protein of NOTCH1, NOTCH2 and NOTCH3
receptors that binds the extracellular domain (ECD) of Notch receptor
in a cis and trans fashion manner (PubMed:21985982, PubMed:10958687).
Following transinteraction, ligand cells produce mechanical force that
depends of a clathrin-mediated endocytosis, requiring ligand
ubiquitination, EPN1 interaction, and actin polymerisation; these
events promote Notch receptor extracellular domain (NECD)
transendocytosis and triggers Notch signaling through induction of
cleavage, hyperphosphorylation, and nuclear accumulation of the
intracellular domain of Notch receptors (NICD) (PubMed:10958687,
PubMed:18676613). Is required for embryonic development and maintenance
of adult stem cells in many different tissues and immune systeme; the
DLL1-induced Notch signaling is mediated through an intercellular
communication that regulates cell lineage, cell specification, cell
patterning and morphogenesis through effects on differentiation and
proliferation (PubMed:17194759, PubMed:19562077, PubMed:18997111,
PubMed:23695674, PubMed:16495313, PubMed:21238454, PubMed:22282195,
PubMed:7671806, PubMed:17960184, PubMed:22529374, PubMed:19389377,
PubMed:23699523, PubMed:19144989, PubMed:23688253, PubMed:23806616,
PubMed:26114479, PubMed:22940113, PubMed:25220152, PubMed:20081190,
PubMed:21572390, PubMed:22096075). Plays a role in brain development at
different level, namely by regulating neuronal differentiation of
neural precursor cells via cell-cell interaction, most likely through
the lateral inhibitory system in an endogenous level dependent-manner
(PubMed:7671806, PubMed:18997111). During neocortex development, Dll1-
Notch signaling transmission is mediated by dynamic interactions
between intermediate neurogenic progenitors and radial glia; the cell-
cell interactions are mediated via dynamic and transient elongation
processes, likely to reactivate/maintain Notch activity in neighboring
progenitors, and coordinate progenitor cell division and
differentiation across radial and zonal boundaries (PubMed:23699523).
During cerebellar development, regulates Bergmann glial monolayer
formation and its morphological maturation through a Notch signaling
pathway (PubMed:23688253). At the retina and spinal cord level,
regulates neurogenesis by preventing the premature differentiation of
neural progenitors and also by maintaining progenitors in spinal cord
through Notch signaling pathway (PubMed:19389377, PubMed:26114479).
Also controls neurogenesis of the neural tube in a progenitor domain-
specific fashion along the dorsoventral axis (PubMed:20081190).
Maintains quiescence of neural stem cells and plays a role as a fate
determinant that segregates asymmetrically to one daughter cell during
neural stem cells mitosis, resulting in neuronal differentiation in
Dll1-inheriting cell (PubMed:23695674). Plays a role in immune systeme
development, namely the development of all T-cells and marginal zone
(MZ) B cells (PubMed:15146182, PubMed:19217325). Blocks the
differentiation of progenitor cells into the B-cell lineage while
promoting the emergence of a population of cells with the
characteristics of a T-cell/NK-cell precursor (By similarity). Upon
MMP14 cleavage, negatively regulates Notch signaling in haematopoietic
progenitor cells to specifically maintain normal B-cell development in
bone marrow (PubMed:21572390). Also plays a role during muscle
development. During early development, inhibits myoblasts
differentiation from the medial dermomyotomal lip and later regulates
progenitor cell differentiation (PubMed:17194759). Directly modulates
cell adhesion and basal lamina formation in satellite cells through
Notch signaling. Maintains myogenic progenitors pool by suppressing
differentiation through down-regulation of MYOD1 and is required for
satellite cell homing and PAX7 expression (PubMed:22940113). During
craniofacial and trunk myogenesis suppresses differentiation of cranial
mesoderm-derived and somite-derived muscle via MYOD1 regulation but in
cranial mesoderm-derived progenitors, is neither required for satellite
cell homing nor for PAX7 expression (PubMed:25220152). Also plays a
role during pancreatic cell development. During type B pancreatic cell
development, may be involved in the initiation of proximodistal
patterning in the early pancreatic epithelium (PubMed:22529374).
Stimulates multipotent pancreatic progenitor cells proliferation and
pancreatic growth by maintaining HES1 expression and PTF1A protein
levels (PubMed:22096075). During fetal stages of development, is
required to maintain arterial identity and the responsiveness of
arterial endothelial cells for VEGFA through regulation of KDR
activation and NRP1 expression (PubMed:19144989). Controls sprouting
angiogenesis and subsequent vertical branch formation througth
regulation on tip cell differentiation (PubMed:22282195). Negatively
regulates goblet cell differentiation in intestine and controls
secretory fat commitment through lateral inhibition in small intestine
(PubMed:21238454, PubMed:21915337). Plays a role during inner ear
development; negatively regulates auditory hair cell differentiation
(PubMed:16495313). Plays a role during nephron development through
Notch signaling pathway (PubMed:23806616). Regulates growth, blood
pressure and energy homeostasis (PubMed:19562077).
{ECO:0000250|UniProtKB:O00548, ECO:0000250|UniProtKB:P97677,
ECO:0000269|PubMed:10958687, ECO:0000269|PubMed:15146182,
ECO:0000269|PubMed:16495313, ECO:0000269|PubMed:17194759,
ECO:0000269|PubMed:17960184, ECO:0000269|PubMed:18676613,
ECO:0000269|PubMed:18997111, ECO:0000269|PubMed:19144989,
ECO:0000269|PubMed:19217325, ECO:0000269|PubMed:19389377,
ECO:0000269|PubMed:19562077, ECO:0000269|PubMed:20081190,
ECO:0000269|PubMed:21238454, ECO:0000269|PubMed:21572390,
ECO:0000269|PubMed:21915337, ECO:0000269|PubMed:21985982,
ECO:0000269|PubMed:22096075, ECO:0000269|PubMed:22282195,
ECO:0000269|PubMed:22529374, ECO:0000269|PubMed:22940113,
ECO:0000269|PubMed:23688253, ECO:0000269|PubMed:23695674,
ECO:0000269|PubMed:23699523, ECO:0000269|PubMed:23806616,
ECO:0000269|PubMed:25220152, ECO:0000269|PubMed:26114479,
ECO:0000269|PubMed:7671806}.
-!- SUBUNIT: Homodimer (PubMed:12794186). Interacts with TJP1
(PubMed:24715457). Interacts with MMP14; inhibits DLL1-induced Notch
signaling (PubMed:21572390). Interacts with MAGI1 (via PDZ domain);
forms a complex with CTNNB1 and CDH2 and promotes recruitment to the
adherens junction and stabilization on the cell surface
(PubMed:15908431). Interacts with PSEN1; undergoes a presenilin-
dependent gamma-secretase cleavage that releases a Dll1-intracellular
form (PubMed:12794186). Interacts with MFAP5 (PubMed:15788413).
Interacts with MIB1 (PubMed:21985982). Interacts with NEURL1B; leads to
ubiquitination (PubMed:17003037, PubMed:19723503). Interacts with
NEURL1 (PubMed:19723503). Interacts with SYNJ2BP; enhances DLL1 protein
stability, and promotes Notch signaling in endothelial cells (By
similarity). Interacts with MAGI1, MAGI2, MAGI3 and MPDZ (By
similarity). Interacts (via ubiquitin) with EPN1 (via IUM domain);
binding with NOTCH1 attached to neighboring cell, promotes ligand
ubiquitination and EPN1 interaction, leading to NECD transendocytosis
and Notch signaling. Interacts with NOTCH1 (By similarity).
{ECO:0000250|UniProtKB:O00548, ECO:0000250|UniProtKB:P97677,
ECO:0000269|PubMed:12794186, ECO:0000269|PubMed:15788413,
ECO:0000269|PubMed:15908431, ECO:0000269|PubMed:17003037,
ECO:0000269|PubMed:19723503, ECO:0000269|PubMed:21572390,
ECO:0000269|PubMed:21985982, ECO:0000269|PubMed:24715457}.
-!- INTERACTION:
Q61483; Q9WVQ1: Magi2; NbExp=3; IntAct=EBI-297125, EBI-297151;
-!- SUBCELLULAR LOCATION: Apical cell membrane
{ECO:0000269|PubMed:24715457}; Single-pass type I membrane protein
{ECO:0000269|PubMed:24715457}. Cell junction, adherens junction
{ECO:0000269|PubMed:15908431, ECO:0000269|PubMed:24715457}. Membrane
raft {ECO:0000269|PubMed:18676613, ECO:0000269|PubMed:21985982}.
Note=Distributed around adherens junction in the apical endfeet through
interactions with MAGI1. {ECO:0000269|PubMed:15908431,
ECO:0000269|PubMed:24715457}.
-!- SUBCELLULAR LOCATION: [Dll1-derived cell-associated form]: Cell
membrane {ECO:0000269|PubMed:12794186}.
-!- SUBCELLULAR LOCATION: [Dll1-intracellular form]: Nucleus
{ECO:0000269|PubMed:12794186}.
-!- TISSUE SPECIFICITY: In the embryo, expressed in the paraxial mesoderm
and nervous system. Expressed at high levels in adult heart and at
lower levels, in adult lung. Highly expressed in satellite cells from
masseter and tongue than in satellite cells from leg and extraocular
muscle.? (PubMed:25220152). {ECO:0000269|PubMed:25220152,
ECO:0000269|PubMed:7671806}.
-!- DEVELOPMENTAL STAGE: Expressed until 15 dpc. Expression then decreases
and increases again in the adult. In differentiating somites, is
expressed at low levels in cells emerging from the dorsomedial lip and
subsequently throughout myotomes. In the limb buds, is found in
myoblasts and myocytes but not in the progenitor cells
(PubMed:17194759). Highly expressed in the endothelium and in the
smooth muscle layer starting at 13.5 dpc in arterial vessels, but not
in veins. At 12.5 dpc, there is no detectable expression in arteries or
veins. This pattern persists until 18.5 dpc (PubMed:19144989). Strongly
expressed in developing muscle of tongue, cheek, and in extraocular
muscle at 11.5 dpc. Found at 18 dpc and P21 in head muscle
(PubMed:25220152). Detected in a subset of cells in the ventricular
zone (VZ), the intermediate zone (IZ) and the cortical plate (CP) of
neocortex and in the ganglionic eminences at 13.5 dpc. At later stages,
such as at 16.5 dpc, found in the VZ and IZ, but at very low levels in
the CP of the neocortex (PubMed:18997111). Highly expressed in
embryonic cells located in the ventricular zone (VZ) of the retinal
neuroepithelium that form clusters; is first detected in cells located
in the central retina. As the retina grows, expression spreads
peripherally along the expanding neurogenic region, being always absent
from the ciliary margin zone (CMZ) (PubMed:19389377).
{ECO:0000269|PubMed:17194759, ECO:0000269|PubMed:18997111,
ECO:0000269|PubMed:19144989, ECO:0000269|PubMed:19389377,
ECO:0000269|PubMed:25220152, ECO:0000269|PubMed:7671806}.
-!- INDUCTION: Induced by PTF1A in multipotent pancreatic progenitor cells
(PubMed:22096075). Induced by CDX1 and CDX2 during somitogenesis and
goblet cell differentiation (PubMed:22015720).
{ECO:0000269|PubMed:22015720, ECO:0000269|PubMed:22096075}.
-!- PTM: Ubiquitinated by MIB (MIB1 or MIB2), leading to its endocytosis
and subsequent degradation. Ubiquitinated; promotes recycling back to
the plasma membrane and confers a strong affinity for NOTCH1
(PubMed:18676613). Multi-ubiquitination of LYS-613 by MIB1 promotes
both cis and trans-interaction with NOTCH1, as well as activation of
Notch signaling (PubMed:21985982). Ubiquitinated by NEURL1B
(PubMed:17003037). {ECO:0000250|UniProtKB:P10041,
ECO:0000269|PubMed:17003037, ECO:0000269|PubMed:18676613,
ECO:0000269|PubMed:21985982}.
-!- PTM: Phosphorylated in a membrane association-dependent manner.
Phosphorylation at Ser-696 requires the presence of Ser-693, whereas
phosphorylation at Thr-638 and Ser-693 occurs independently of the
other sites. Phosphorylation is required for full ligand activity in
vitro and affects surface presentation, ectodomain shedding, and
endocytosis. {ECO:0000269|PubMed:24449764}.
-!- PTM: Cleaved by MMP14; negatively regulates DLL1-induced Notch
signaling in HPCs, modulating B-lymphocyte differentiation in bone
marrow (PubMed:21572390). Undergoes two consecutive processing events:
a shedding event, partially by ADAM10, that generates a soluble
extracellular form and an intracellular membrane-anchored form,
followed by a gamma-secretase cleavage releasing an intracellular
fragment (PubMed:12794186). {ECO:0000269|PubMed:12794186,
ECO:0000269|PubMed:21572390}.
-!- PTM: O-fucosylated. Can be elongated to a disaccharide by MFNG.
{ECO:0000250|UniProtKB:P97677}.
-!- DISRUPTION PHENOTYPE: Heterozygous Dll1 mice mutants are lighter and
smaller, with altered fat to lean ratio and have increased blood
pressure and a slight bradycardia. The animals have reduced cholesterol
and triglyceride levels in blood (PubMed:19562077). Heterozygous Dll1
mice mutants and hypomorphic Dll1 mice mutants survive until birth,
despite significantly reduced Notch activity (PubMed:17194759).
Conditional knockout in inner ear leads to an early and excessive
production of hair cells and have vestibular defects (PubMed:16495313).
Conditional knockout in a small proportion of neural precursor cells
reduces neurogenesis, whereas conditional knockout in a large
proportion promotes premature neurogenesis (PubMed:18997111). Hypomorph
Dll1 pups mutant survive until birth but are smaller. Conditional
knockout Dll1 mice mutant in epidermis, survive and have no gross
abnormalities (PubMed:17960184). Hypomorph Dll1 mice mutant survive
until birth and have severe skeletal muscle defects (PubMed:19144989).
Heterozygous Dll1 mutant embryos show disrupted muscle growth
(PubMed:25220152). Conditional knockout Dll1 mice mutant show
disorganization of Bergmann fibers, ectopic localization of Bergmann
glia in the molecular layer and a reduction in the number of Bergmann
glia (PubMed:23688253). {ECO:0000269|PubMed:16495313,
ECO:0000269|PubMed:17194759, ECO:0000269|PubMed:17960184,
ECO:0000269|PubMed:18997111, ECO:0000269|PubMed:19144989,
ECO:0000269|PubMed:19562077, ECO:0000269|PubMed:23688253,
ECO:0000269|PubMed:25220152}.
---------------------------------------------------------------------------
Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
Distributed under the Creative Commons Attribution (CC BY 4.0) License
---------------------------------------------------------------------------
EMBL; X80903; CAA56865.1; -; mRNA.
EMBL; AY497019; AAR30869.1; -; Genomic_DNA.
EMBL; CH466630; EDL20466.1; -; Genomic_DNA.
EMBL; BC057400; AAH57400.1; -; mRNA.
EMBL; BC065063; AAH65063.1; -; mRNA.
CCDS; CCDS37452.1; -.
PIR; I48324; I48324.
RefSeq; NP_031891.2; NM_007865.3.
SMR; Q61483; -.
BioGRID; 199232; 7.
DIP; DIP-32600N; -.
IntAct; Q61483; 8.
MINT; Q61483; -.
STRING; 10090.ENSMUSP00000014917; -.
GlyGen; Q61483; 1 site.
iPTMnet; Q61483; -.
PhosphoSitePlus; Q61483; -.
PaxDb; Q61483; -.
PRIDE; Q61483; -.
ProteomicsDB; 279687; -.
Antibodypedia; 20091; 559 antibodies.
Ensembl; ENSMUST00000014917; ENSMUSP00000014917; ENSMUSG00000014773.
GeneID; 13388; -.
KEGG; mmu:13388; -.
UCSC; uc008aoi.2; mouse.
CTD; 28514; -.
MGI; MGI:104659; Dll1.
eggNOG; KOG1217; Eukaryota.
GeneTree; ENSGT00940000159781; -.
HOGENOM; CLU_012574_1_0_1; -.
InParanoid; Q61483; -.
OMA; DKPCHQG; -.
OrthoDB; 406049at2759; -.
TreeFam; TF351835; -.
Reactome; R-MMU-9013507; NOTCH3 Activation and Transmission of Signal to the Nucleus.
BioGRID-ORCS; 13388; 3 hits in 52 CRISPR screens.
ChiTaRS; Dll1; mouse.
PRO; PR:Q61483; -.
Proteomes; UP000000589; Chromosome 17.
RNAct; Q61483; protein.
Bgee; ENSMUSG00000014773; Expressed in presomitic mesoderm and 336 other tissues.
ExpressionAtlas; Q61483; baseline and differential.
Genevisible; Q61483; MM.
GO; GO:0005912; C:adherens junction; IDA:UniProtKB.
GO; GO:0016324; C:apical plasma membrane; IDA:UniProtKB.
GO; GO:0031410; C:cytoplasmic vesicle; IDA:MGI.
GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
GO; GO:0045121; C:membrane raft; IDA:UniProtKB.
GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
GO; GO:0005886; C:plasma membrane; IDA:MGI.
GO; GO:0005509; F:calcium ion binding; IEA:InterPro.
GO; GO:0005112; F:Notch binding; IPI:UniProtKB.
GO; GO:0097110; F:scaffold protein binding; IPI:UniProtKB.
GO; GO:0030957; F:Tat protein binding; ISO:MGI.
GO; GO:0009887; P:animal organ morphogenesis; NAS:UniProtKB.
GO; GO:0014002; P:astrocyte development; IMP:UniProtKB.
GO; GO:0009912; P:auditory receptor cell fate commitment; NAS:UniProtKB.
GO; GO:0007267; P:cell-cell signaling; IDA:MGI.
GO; GO:0021688; P:cerebellar molecular layer formation; IMP:UniProtKB.
GO; GO:0021693; P:cerebellar Purkinje cell layer structural organization; IMP:UniProtKB.
GO; GO:0072583; P:clathrin-dependent endocytosis; ISS:UniProtKB.
GO; GO:0007386; P:compartment pattern specification; IMP:MGI.
GO; GO:0007368; P:determination of left/right symmetry; IMP:MGI.
GO; GO:0097102; P:endothelial tip cell fate specification; IMP:UniProtKB.
GO; GO:0097009; P:energy homeostasis; IMP:UniProtKB.
GO; GO:0001947; P:heart looping; IMP:BHF-UCL.
GO; GO:0001701; P:in utero embryonic development; NAS:UniProtKB.
GO; GO:0042491; P:inner ear auditory receptor cell differentiation; NAS:UniProtKB.
GO; GO:0048839; P:inner ear development; IMP:MGI.
GO; GO:0042472; P:inner ear morphogenesis; NAS:UniProtKB.
GO; GO:0046331; P:lateral inhibition; IDA:UniProtKB.
GO; GO:0070986; P:left/right axis specification; IMP:BHF-UCL.
GO; GO:0072070; P:loop of Henle development; IEP:UniProtKB.
GO; GO:0002315; P:marginal zone B cell differentiation; IMP:UniProtKB.
GO; GO:2000726; P:negative regulation of cardiac muscle cell differentiation; IMP:BHF-UCL.
GO; GO:0045596; P:negative regulation of cell differentiation; IMP:UniProtKB.
GO; GO:0008285; P:negative regulation of cell population proliferation; IMP:UniProtKB.
GO; GO:0045605; P:negative regulation of epidermal cell differentiation; IMP:UniProtKB.
GO; GO:0030857; P:negative regulation of epithelial cell differentiation; IMP:UniProtKB.
GO; GO:0034351; P:negative regulation of glial cell apoptotic process; IMP:UniProtKB.
GO; GO:0045608; P:negative regulation of inner ear auditory receptor cell differentiation; IMP:MGI.
GO; GO:0032693; P:negative regulation of interleukin-10 production; ISO:MGI.
GO; GO:0045638; P:negative regulation of myeloid cell differentiation; IDA:MGI.
GO; GO:0045662; P:negative regulation of myoblast differentiation; IMP:UniProtKB.
GO; GO:0045665; P:negative regulation of neuron differentiation; IMP:UniProtKB.
GO; GO:0045746; P:negative regulation of Notch signaling pathway; IBA:GO_Central.
GO; GO:0072006; P:nephron development; IMP:UniProtKB.
GO; GO:0007399; P:nervous system development; NAS:UniProtKB.
GO; GO:0048665; P:neuron fate specification; IDA:UniProtKB.
GO; GO:0097150; P:neuronal stem cell population maintenance; IMP:UniProtKB.
GO; GO:0061314; P:Notch signaling involved in heart development; IC:BHF-UCL.
GO; GO:0007219; P:Notch signaling pathway; IMP:UniProtKB.
GO; GO:0060853; P:Notch signaling pathway involved in arterial endothelial cell fate commitment; IMP:UniProtKB.
GO; GO:0042475; P:odontogenesis of dentin-containing tooth; NAS:UniProtKB.
GO; GO:0035265; P:organ growth; IMP:UniProtKB.
GO; GO:0008284; P:positive regulation of cell population proliferation; IMP:UniProtKB.
GO; GO:0045807; P:positive regulation of endocytosis; IDA:UniProtKB.
GO; GO:0010628; P:positive regulation of gene expression; IMP:MGI.
GO; GO:0045747; P:positive regulation of Notch signaling pathway; IDA:UniProtKB.
GO; GO:0048633; P:positive regulation of skeletal muscle tissue growth; IMP:UniProtKB.
GO; GO:1903672; P:positive regulation of sprouting angiogenesis; IMP:UniProtKB.
GO; GO:0045944; P:positive regulation of transcription by RNA polymerase II; IMP:BHF-UCL.
GO; GO:0072014; P:proximal tubule development; IEP:UniProtKB.
GO; GO:0009954; P:proximal/distal pattern formation; IMP:UniProtKB.
GO; GO:0008217; P:regulation of blood pressure; IMP:UniProtKB.
GO; GO:0030155; P:regulation of cell adhesion; IMP:UniProtKB.
GO; GO:0051302; P:regulation of cell division; IMP:UniProtKB.
GO; GO:0040008; P:regulation of growth; IMP:UniProtKB.
GO; GO:0050767; P:regulation of neurogenesis; IMP:UniProtKB.
GO; GO:0048631; P:regulation of skeletal muscle tissue growth; IMP:UniProtKB.
GO; GO:0014807; P:regulation of somitogenesis; IMP:UniProtKB.
GO; GO:1900746; P:regulation of vascular endothelial growth factor signaling pathway; IMP:UniProtKB.
GO; GO:0060041; P:retina development in camera-type eye; IMP:UniProtKB.
GO; GO:0060042; P:retina morphogenesis in camera-type eye; IMP:UniProtKB.
GO; GO:0048630; P:skeletal muscle tissue growth; IMP:UniProtKB.
GO; GO:0098773; P:skin epidermis development; IMP:UniProtKB.
GO; GO:0001757; P:somite specification; IMP:MGI.
GO; GO:0001756; P:somitogenesis; IMP:UniProtKB.
GO; GO:0021510; P:spinal cord development; IMP:UniProtKB.
GO; GO:0003323; P:type B pancreatic cell development; IMP:UniProtKB.
InterPro; IPR001774; DSL.
InterPro; IPR001881; EGF-like_Ca-bd_dom.
InterPro; IPR013032; EGF-like_CS.
InterPro; IPR000742; EGF-like_dom.
InterPro; IPR000152; EGF-type_Asp/Asn_hydroxyl_site.
InterPro; IPR018097; EGF_Ca-bd_CS.
InterPro; IPR009030; Growth_fac_rcpt_cys_sf.
InterPro; IPR011651; Notch_ligand_N.
Pfam; PF01414; DSL; 1.
Pfam; PF00008; EGF; 4.
Pfam; PF07645; EGF_CA; 1.
Pfam; PF12661; hEGF; 1.
Pfam; PF07657; MNNL; 1.
SMART; SM00051; DSL; 1.
SMART; SM00181; EGF; 8.
SMART; SM00179; EGF_CA; 6.
SUPFAM; SSF57184; SSF57184; 1.
PROSITE; PS00010; ASX_HYDROXYL; 3.
PROSITE; PS51051; DSL; 1.
PROSITE; PS00022; EGF_1; 8.
PROSITE; PS01186; EGF_2; 8.
PROSITE; PS50026; EGF_3; 7.
PROSITE; PS01187; EGF_CA; 2.
1: Evidence at protein level;
Cell junction; Cell membrane; Developmental protein; Differentiation;
Direct protein sequencing; Disulfide bond; EGF-like domain; Glycoprotein;
Isopeptide bond; Membrane; Notch signaling pathway; Nucleus;
Phosphoprotein; Reference proteome; Repeat; Signal; Transmembrane;
Transmembrane helix; Ubl conjugation.
SIGNAL 1..17
/evidence="ECO:0000255"
CHAIN 18..722
/note="Delta-like protein 1"
/id="PRO_0000007507"
CHAIN 18..535
/note="Dll1-soluble form"
/evidence="ECO:0000269|PubMed:12794186"
/id="PRO_0000434830"
CHAIN 536..722
/note="Dll1-derived cell-associated form"
/evidence="ECO:0000269|PubMed:12794186"
/id="PRO_0000434831"
CHAIN ?..722
/note="Dll1-intracellular form"
/evidence="ECO:0000269|PubMed:12794186"
/id="PRO_0000434832"
TOPO_DOM 18..545
/note="Extracellular"
/evidence="ECO:0000255"
TRANSMEM 546..568
/note="Helical"
/evidence="ECO:0000255"
TOPO_DOM 569..722
/note="Cytoplasmic"
/evidence="ECO:0000255"
DOMAIN 176..220
/note="DSL"
/evidence="ECO:0000255|PROSITE-ProRule:PRU00377"
DOMAIN 225..253
/note="EGF-like 1"
/evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
DOMAIN 256..284
/note="EGF-like 2"
/evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
DOMAIN 291..324
/note="EGF-like 3"
/evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
DOMAIN 331..362
/note="EGF-like 4; calcium-binding"
/evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
DOMAIN 369..401
/note="EGF-like 5"
/evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
DOMAIN 408..439
/note="EGF-like 6"
/evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
DOMAIN 446..477
/note="EGF-like 7; calcium-binding"
/evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
DOMAIN 484..515
/note="EGF-like 8"
/evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
REGION 719..722
/note="Interaction with MAGI1"
/evidence="ECO:0000269|PubMed:15908431"
SITE 527..528
/note="Cleavage; by MMP14"
/evidence="ECO:0000269|PubMed:21572390"
SITE 535..536
/note="Cleavage; by ADAM protease"
/evidence="ECO:0000269|PubMed:12794186"
MOD_RES 638
/note="Phosphothreonine"
/evidence="ECO:0000269|PubMed:24449764"
MOD_RES 693
/note="Phosphoserine; by PKB"
/evidence="ECO:0000269|PubMed:24449764"
MOD_RES 696
/note="Phosphoserine"
/evidence="ECO:0000269|PubMed:24449764"
CARBOHYD 476
/note="N-linked (GlcNAc...) asparagine"
/evidence="ECO:0000255"
DISULFID 178..187
/evidence="ECO:0000250"
DISULFID 191..203
/evidence="ECO:0000250"
DISULFID 211..220
/evidence="ECO:0000250"
DISULFID 225..236
/evidence="ECO:0000250"
DISULFID 229..242
/evidence="ECO:0000250"
DISULFID 244..253
/evidence="ECO:0000250"
DISULFID 256..267
/evidence="ECO:0000250"
DISULFID 262..273
/evidence="ECO:0000250"
DISULFID 275..284
/evidence="ECO:0000250"
DISULFID 291..303
/evidence="ECO:0000250"
DISULFID 297..313
/evidence="ECO:0000250"
DISULFID 315..324
/evidence="ECO:0000250"
DISULFID 331..342
/evidence="ECO:0000250"
DISULFID 336..351
/evidence="ECO:0000250"
DISULFID 353..362
/evidence="ECO:0000250"
DISULFID 369..380
/evidence="ECO:0000250"
DISULFID 374..390
/evidence="ECO:0000250"
DISULFID 392..401
/evidence="ECO:0000250"
DISULFID 408..419
/evidence="ECO:0000250"
DISULFID 413..428
/evidence="ECO:0000250"
DISULFID 430..439
/evidence="ECO:0000250"
DISULFID 446..457
/evidence="ECO:0000250"
DISULFID 451..466
/evidence="ECO:0000250"
DISULFID 468..477
/evidence="ECO:0000250"
DISULFID 484..495
/evidence="ECO:0000250"
DISULFID 489..504
/evidence="ECO:0000250"
DISULFID 506..515
/evidence="ECO:0000250"
CROSSLNK 613
/note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
G-Cter in ubiquitin)"
/evidence="ECO:0000269|PubMed:21985982"
MUTAGEN 613..618
/note="KNTNKK->RNTNRR: Highly decreases Notch signaling
pathway. Multi-ubiquitination pattern is reduced, although
it does appear to be mono-ubiquitinated. Interacts with
MIB1. Loss of cis interaction with NOTCH1."
/evidence="ECO:0000269|PubMed:21985982"
MUTAGEN 613
/note="K->R: Highly decreases Notch signaling pathway.
Multi-ubiquitination pattern is reduced, although it does
appear to be mono-ubiquitinated. Interacts with MIB1. Loss
of cis and trans interaction with NOTCH1. Increases its
association with lipid raft microdomains."
/evidence="ECO:0000269|PubMed:21985982"
MUTAGEN 638
/note="T->V: Not phosphorylated; when associated with A-693
and A-696. Not phosphorylated and doesn't prevent
phosphorylation at S-693 and S-696. Reduces NOTCH1
transactivation; when associated with A-693 and A-696.
Reduces cell surface levels of proteins; when associated
with A-693 and A-696. Increases ectodomain shedding; when
associated with A-693 and A-696."
/evidence="ECO:0000269|PubMed:24449764"
MUTAGEN 689
/note="K->R: Decreases Notch signaling pathway."
/evidence="ECO:0000269|PubMed:21985982"
MUTAGEN 693
/note="S->A: Not phosphorylated; when associated with V-638
and A-696. Not phosphorylated and prevents phosphorylation
at S-696. Reduces NOTCH1 transactivation; when associated
with V-638 and A-696. Reduces cell surface levels of
proteins; when associated with V-638 and A-696. Increases
ectodomain shedding; when associated with V-638 and A-696."
/evidence="ECO:0000269|PubMed:24449764"
MUTAGEN 696
/note="S->A: Not phosphorylated; when associated with V-638
and A-693. Not phosphorylated and doesn't prevent
phosphorylation at T-638 and S-693, Reduces NOTCH1
transactivation; when associated with V-638 and A-693.
Reduces cell surface levels of proteins; when associated
with V-638 and A-693. Increases ectodomain shedding; when
associated with V-638 and A-693."
/evidence="ECO:0000269|PubMed:24449764"
MUTAGEN 699
/note="K->R: Decreases Notch signaling pathway."
/evidence="ECO:0000269|PubMed:21985982"
MUTAGEN 713
/note="K->R: Decreases Notch signaling pathway."
/evidence="ECO:0000269|PubMed:21985982"
CONFLICT 628
/note="E -> K (in Ref. 1; CAA56865)"
/evidence="ECO:0000305"
SEQUENCE 722 AA; 78449 MW; 9D570B9DC7EEC75E CRC64;
MGRRSALALA VVSALLCQVW SSGVFELKLQ EFVNKKGLLG NRNCCRGGSG PPCACRTFFR
VCLKHYQASV SPEPPCTYGS AVTPVLGVDS FSLPDGAGID PAFSNPIRFP FGFTWPGTFS
LIIEALHTDS PDDLATENPE RLISRLTTQR HLTVGEEWSQ DLHSSGRTDL RYSYRFVCDE
HYYGEGCSVF CRPRDDAFGH FTCGDRGEKM CDPGWKGQYC TDPICLPGCD DQHGYCDKPG
ECKCRVGWQG RYCDECIRYP GCLHGTCQQP WQCNCQEGWG GLFCNQDLNY CTHHKPCRNG
ATCTNTGQGS YTCSCRPGYT GANCELEVDE CAPSPCKNGA SCTDLEDSFS CTCPPGFYGK
VCELSAMTCA DGPCFNGGRC SDNPDGGYTC HCPLGFSGFN CEKKMDLCGS SPCSNGAKCV
DLGNSYLCRC QAGFSGRYCE DNVDDCASSP CANGGTCRDS VNDFSCTCPP GYTGKNCSAP
VSRCEHAPCH NGATCHQRGQ RYMCECAQGY GGPNCQFLLP EPPPGPMVVD LSERHMESQG
GPFPWVAVCA GVVLVLLLLL GCAAVVVCVR LKLQKHQPPP EPCGGETETM NNLANCQREK
DVSVSIIGAT QIKNTNKKAD FHGDHGAEKS SFKVRYPTVD YNLVRDLKGD EATVRDTHSK
RDTKCQSQSS AGEEKIAPTL RGGEIPDRKR PESVYSTSKD TKYQSVYVLS AEKDECVIAT
EV


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YHB0334Ra Rat Delta Like Protein 1(DLL1)ELISA Kit 48T
E1104Ra Rat Delta Like Protein 1(DLL1)ELISA Kit 48T
E1104Ra Rat Delta Like Protein 1(DLL1)ELISA Kit 96T
YHB0334Ra Rat Delta Like Protein 1(DLL1)ELISA Kit 96T
E1103Ra Rat Delta Like Protein 1(DLL1)ELISA Kit 48T
CSB-EL006947RA Rat Delta-like protein 1(DLL1) ELISA kit 96T
Pathways :
WP827: Delta-Notch Signaling Pathway
WP1064: Delta-Notch Signaling Pathway
WP199: Delta-Notch Signaling Pathway
WP946: Delta-Notch Signaling Pathway
WP265: Delta-Notch Signaling Pathway
WP1180: Delta-Notch Signaling Pathway
WP2074: Neural Crest Differentiation
WP517: Notch Signaling Pathway
WP2064: Neural Crest Differentiation
WP268: Notch Signaling Pathway
WP1029: Notch Signaling Pathway
WP29: Notch Signaling Pathway
WP912: Notch Signaling Pathway
WP1148: Notch Signaling Pathway
WP1232: Notch Signaling Pathway
WP1357: Notch Signaling Pathway
WP1694: Pyrimidine metabolism
WP1693: Purine metabolism
WP1663: Homologous recombination
WP32: Translation Factors
WP1644: DNA replication
WP1672: Mismatch repair
WP1205: Homologous recombination
WP1665: Limonene and pinene degradation
WP1714: Tyrosine metabolism

Related Genes :
[Dll1] Delta-like protein 1 (Drosophila Delta homolog 1) (Delta1) [Cleaved into: Dll1-soluble form (Dll1-EC) (Shed form); Dll1-derived cell-associated form (Dll1-TMIC) (Membrane-associated fragment); Dll1-intracellular form (Dll1-IC)]
[DLL1 UNQ146/PRO172] Delta-like protein 1 (Drosophila Delta homolog 1) (Delta1) (H-Delta-1)
[Dll1] Delta-like protein 1 (Drosophila Delta homolog 1) (Delta1)
[Notch1 Motch] Neurogenic locus notch homolog protein 1 (Notch 1) (Motch A) (mT14) (p300) [Cleaved into: Notch 1 extracellular truncation (NEXT); Notch 1 intracellular domain (NICD)]
[NOTCH1 TAN1] Neurogenic locus notch homolog protein 1 (Notch 1) (hN1) (Translocation-associated notch protein TAN-1) [Cleaved into: Notch 1 extracellular truncation (NEXT); Notch 1 intracellular domain (NICD)]
[Notch1] Neurogenic locus notch homolog protein 1 (Notch 1) [Cleaved into: Notch 1 extracellular truncation (NEXT); Notch 1 intracellular domain (NICD)]
[NOTCH1] Neurogenic locus notch homolog protein 1 (Notch 1) [Cleaved into: Notch 1 extracellular truncation (NEXT); Notch 1 intracellular domain (NICD)]
[notch1a notch] Neurogenic locus notch homolog protein 1 (Notch 1) [Cleaved into: Notch 1 extracellular truncation (NEXT); Notch 1 intracellular domain (NICD)]
[NOTCH3] Neurogenic locus notch homolog protein 3 (Notch 3) [Cleaved into: Notch 3 extracellular truncation; Notch 3 intracellular domain]
[NOTCH2] Neurogenic locus notch homolog protein 2 (Notch 2) (hN2) [Cleaved into: Notch 2 extracellular truncation (N2ECD); Notch 2 intracellular domain (N2ICD)]
[Notch2] Neurogenic locus notch homolog protein 2 (Notch 2) (Motch B) [Cleaved into: Notch 2 extracellular truncation; Notch 2 intracellular domain]
[Notch2] Neurogenic locus notch homolog protein 2 (Notch 2) [Cleaved into: Notch 2 extracellular truncation; Notch 2 intracellular domain]
[notch1] Neurogenic locus notch homolog protein 1 (Notch 1) [Cleaved into: Notch 1 extracellular truncation (NEXT); Notch 1 intracellular domain (NICD)]
[notch1 xotch] Neurogenic locus notch homolog protein 1 (Notch 1) (xOTCH) [Cleaved into: Notch 1 extracellular truncation (NEXT); Notch 1 intracellular domain (NICD)]
[leuB] 3-isopropylmalate dehydrogenase (EC 1.1.1.85) (3-IPM-DH) (Beta-IPM dehydrogenase) (IMDH)
[hes4-b hairy2 hairy2b] Transcription factor HES-4-B (Hairy and enhancer of split 4-B) (Protein hairy-2) (Xhairy2) (Protein hairy-2a) (Xhairy2b)
[Magi2 Acvrinp1 Aip1 Arip1] Membrane-associated guanylate kinase, WW and PDZ domain-containing protein 2 (Activin receptor-interacting protein 1) (Acvrip1) (Atrophin-1-interacting protein 1) (AIP-1) (Membrane-associated guanylate kinase inverted 2) (MAGI-2)
[NOTCH2NLC] Notch homolog 2 N-terminal-like protein C
[stat3.1 stat3] Signal transducer and activator of transcription 3.1 (Protein Stat3) (Xstat3)
[Synj2bp Omp25] Synaptojanin-2-binding protein (Mitochondrial outer membrane protein 25) (NPW16)
[MAGI2 ACVRINP1 AIP1 KIAA0705] Membrane-associated guanylate kinase, WW and PDZ domain-containing protein 2 (Atrophin-1-interacting protein 1) (AIP-1) (Atrophin-1-interacting protein A) (Membrane-associated guanylate kinase inverted 2) (MAGI-2)
[TNFSF13B BAFF BLYS TALL1 TNFSF20 ZTNF4 UNQ401/PRO738] Tumor necrosis factor ligand superfamily member 13B (B lymphocyte stimulator) (BLyS) (B-cell-activating factor) (BAFF) (Dendritic cell-derived TNF-like molecule) (TNF- and APOL-related leukocyte expressed ligand 1) (TALL-1) (CD antigen CD257) [Cleaved into: Tumor necrosis factor ligand superfamily member 13b, membrane form; Tumor necrosis factor ligand superfamily member 13b, soluble form]
[NOTCH2NLA N2N NOTCH2NL] Notch homolog 2 N-terminal-like protein A (Notch homolog 2 N-terminal-like protein)
[MPDZ MUPP1] Multiple PDZ domain protein (Multi-PDZ domain protein 1)
[Magi2 Acvrinp1 Aip1 Sscam] Membrane-associated guanylate kinase, WW and PDZ domain-containing protein 2 (Atrophin-1-interacting protein 1) (AIP-1) (Membrane-associated guanylate kinase inverted 2) (MAGI-2) (Synaptic-scaffolding molecule) (S-SCAM)
[NOTCH2NLB] Notch homolog 2 N-terminal-like protein B
[SYNJ2BP OMP25] Synaptojanin-2-binding protein (Mitochondrial outer membrane protein 25)
[Tnf Tnfa Tnfsf2] Tumor necrosis factor (Cachectin) (TNF-alpha) (Tumor necrosis factor ligand superfamily member 2) (TNF-a) [Cleaved into: Tumor necrosis factor, membrane form (N-terminal fragment) (NTF); Intracellular domain 1 (ICD1); Intracellular domain 2 (ICD2); C-domain 1; C-domain 2; Tumor necrosis factor, soluble form]
[Tnf Tnfa Tnfsf2] Tumor necrosis factor (Cachectin) (TNF-alpha) (Tumor necrosis factor ligand superfamily member 2) (TNF-a) [Cleaved into: Tumor necrosis factor, membrane form (N-terminal fragment) (NTF); Intracellular domain 1 (ICD1); Intracellular domain 2 (ICD2); C-domain 1; C-domain 2; Tumor necrosis factor, soluble form]
[TNF TNFA TNFSF2] Tumor necrosis factor (Cachectin) (TNF-alpha) (Tumor necrosis factor ligand superfamily member 2) (TNF-a) [Cleaved into: Tumor necrosis factor, membrane form (N-terminal fragment) (NTF); Intracellular domain 1 (ICD1); Intracellular domain 2 (ICD2); C-domain 1; C-domain 2; Tumor necrosis factor, soluble form]

Bibliography :
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