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Entry version 178 (08 May 2019)
Sequence version 2 (27 Jul 2011)
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Protein

Delta-like protein 1

Gene

Dll1

Organism
Mus musculus (Mouse)
Status
Reviewed-Annotation score:

Annotation score:5 out of 5

<p>The annotation score provides a heuristic measure of the annotation content of a UniProtKB entry or proteome. This score <strong>cannot</strong> be used as a measure of the accuracy of the annotation as we cannot define the ‘correct annotation’ for any given protein.<p><a href='/help/annotation_score' target='_top'>More...</a></p>
-Experimental evidence at protein leveli <p>This indicates the type of evidence that supports the existence of the protein. Note that the ‘protein existence’ evidence does not give information on the accuracy or correctness of the sequence(s) displayed.<p><a href='/help/protein_existence' target='_top'>More...</a></p>

<p>This section provides any useful information about the protein, mostly biological knowledge.<p><a href='/help/function_section' target='_top'>More...</a></p>Functioni

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).By similarity27 Publications

<p>The <a href="http://www.geneontology.org/">Gene Ontology (GO)</a> project provides a set of hierarchical controlled vocabulary split into 3 categories:<p><a href='/help/gene_ontology' target='_top'>More...</a></p>GO - Molecular functioni

GO - Biological processi

<p>UniProtKB Keywords constitute a <a href="http://www.uniprot.org/keywords">controlled vocabulary</a> with a hierarchical structure. Keywords summarise the content of a UniProtKB entry and facilitate the search for proteins of interest.<p><a href='/help/keywords' target='_top'>More...</a></p>Keywordsi

Molecular functionDevelopmental protein
Biological processDifferentiation, Notch signaling pathway

Enzyme and pathway databases

Reactome - a knowledgebase of biological pathways and processes

More...
Reactomei
R-MMU-9013507 NOTCH3 Activation and Transmission of Signal to the Nucleus

<p>This section provides information about the protein and gene name(s) and synonym(s) and about the organism that is the source of the protein sequence.<p><a href='/help/names_and_taxonomy_section' target='_top'>More...</a></p>Names & Taxonomyi

<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section provides an exhaustive list of all names of the protein, from commonly used to obsolete, to allow unambiguous identification of a protein.<p><a href='/help/protein_names' target='_top'>More...</a></p>Protein namesi
Recommended name:
Delta-like protein 1Curated
Alternative name(s):
Drosophila Delta homolog 1
Short name:
Delta11 Publication
Cleaved into the following 3 chains:
Dll1-soluble form1 Publication
Short name:
Dll1-EC1 Publication
Short name:
Shed form1 Publication
Dll1-derived cell-associated form1 Publication
Short name:
Dll1-TMIC1 Publication
Short name:
Membrane-associated fragment1 Publication
Dll1-intracellular form1 Publication
Short name:
Dll1-IC1 Publication
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section indicates the name(s) of the gene(s) that code for the protein sequence(s) described in the entry. Four distinct tokens exist: ‘Name’, ‘Synonyms’, ‘Ordered locus names’ and ‘ORF names’.<p><a href='/help/gene_name' target='_top'>More...</a></p>Gene namesi
Name:Dll1
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section provides information on the name(s) of the organism that is the source of the protein sequence.<p><a href='/help/organism-name' target='_top'>More...</a></p>OrganismiMus musculus (Mouse)
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section shows the unique identifier assigned by the NCBI to the source organism of the protein. This is known as the ‘taxonomic identifier’ or ‘taxid’.<p><a href='/help/taxonomic_identifier' target='_top'>More...</a></p>Taxonomic identifieri10090 [NCBI]
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section contains the taxonomic hierarchical classification lineage of the source organism. It lists the nodes as they appear top-down in the taxonomic tree, with the more general grouping listed first.<p><a href='/help/taxonomic_lineage' target='_top'>More...</a></p>Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaMyomorphaMuroideaMuridaeMurinaeMusMus
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section is present for entries that are part of a <a href="http://www.uniprot.org/proteomes">proteome</a>, i.e. of a set of proteins thought to be expressed by organisms whose genomes have been completely sequenced.<p><a href='/help/proteomes_manual' target='_top'>More...</a></p>Proteomesi
  • UP000000589 <p>A UniProt <a href="http://www.uniprot.org/manual/proteomes_manual">proteome</a> can consist of several components. <br></br>The component name refers to the genomic component encoding a set of proteins.<p><a href='/help/proteome_component' target='_top'>More...</a></p> Componenti: Chromosome 17

Organism-specific databases

Mouse genome database (MGD) from Mouse Genome Informatics (MGI)

More...
MGIi
MGI:104659 Dll1

<p>This section provides information on the location and the topology of the mature protein in the cell.<p><a href='/help/subcellular_location_section' target='_top'>More...</a></p>Subcellular locationi

Extracellular region or secreted Cytosol Plasma membrane Cytoskeleton Lysosome Endosome Peroxisome ER Golgi apparatus Nucleus Mitochondrion Manual annotation Automatic computational assertionGraphics by Christian Stolte & Seán O’Donoghue; Source: COMPARTMENTS

Topology

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/help/subcellular_location_section">'Subcellular location'</a> section describes the subcellular compartment where each non-membrane region of a membrane-spanning protein is found.<p><a href='/help/topo_dom' target='_top'>More...</a></p>Topological domaini18 – 545ExtracellularSequence analysisAdd BLAST528
<p>This subsection of the <a href="http://www.uniprot.org/help/subcellular_location_section">'Subcellular location'</a> section describes the extent of a membrane-spanning region of the protein. It denotes the presence of both alpha-helical transmembrane regions and the membrane spanning regions of beta-barrel transmembrane proteins.<p><a href='/help/transmem' target='_top'>More...</a></p>Transmembranei546 – 568HelicalSequence analysisAdd BLAST23
Topological domaini569 – 722CytoplasmicSequence analysisAdd BLAST154

Keywords - Cellular componenti

Cell junction, Cell membrane, Membrane, Nucleus

<p>This section provides information on the disease(s) and phenotype(s) associated with a protein.<p><a href='/help/pathology_and_biotech_section' target='_top'>More...</a></p>Pathology & Biotechi

<p>This subsection of the ‘Pathology and Biotech’ section describes the in vivo effects caused by ablation of the gene (or one or more transcripts) coding for the protein described in the entry. This includes gene knockout and knockdown, provided experiments have been performed in the context of a whole organism or a specific tissue, and not at the single-cell level.<p><a href='/help/disruption_phenotype' target='_top'>More...</a></p>Disruption phenotypei

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).8 Publications

Mutagenesis

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/manual/pathology_and_biotech_section">'Pathology and Biotech'</a> section describes the effect of the experimental mutation of one or more amino acid(s) on the biological properties of the protein.<p><a href='/help/mutagen' target='_top'>More...</a></p>Mutagenesisi613 – 618KNTNKK → 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. 1 Publication6
Mutagenesisi613K → 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. 1 Publication1
Mutagenesisi638T → 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. 1 Publication1
Mutagenesisi689K → R: Decreases Notch signaling pathway. 1 Publication1
Mutagenesisi693S → 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. 1 Publication1
Mutagenesisi696S → 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. 1 Publication1
Mutagenesisi699K → R: Decreases Notch signaling pathway. 1 Publication1
Mutagenesisi713K → R: Decreases Notch signaling pathway. 1 Publication1

<p>This section describes post-translational modifications (PTMs) and/or processing events.<p><a href='/help/ptm_processing_section' target='_top'>More...</a></p>PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the ‘PTM / Processing’ section denotes the presence of an N-terminal signal peptide.<p><a href='/help/signal' target='_top'>More...</a></p>Signal peptidei1 – 17Sequence analysisAdd BLAST17
<p>This subsection of the ‘PTM / Processing’ section describes the extent of a polypeptide chain in the mature protein following processing.<p><a href='/help/chain' target='_top'>More...</a></p>ChainiPRO_000000750718 – 722Delta-like protein 1Add BLAST705
ChainiPRO_000043483018 – 535Dll1-soluble form1 PublicationAdd BLAST518
ChainiPRO_0000434831536 – 722Dll1-derived cell-associated form1 PublicationAdd BLAST187
ChainiPRO_0000434832? – 722Dll1-intracellular form1 Publication

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the PTM / Processing":/help/ptm_processing_section section describes the positions of cysteine residues participating in disulfide bonds.<p><a href='/help/disulfid' target='_top'>More...</a></p>Disulfide bondi178 ↔ 187By similarity
Disulfide bondi191 ↔ 203By similarity
Disulfide bondi211 ↔ 220By similarity
Disulfide bondi225 ↔ 236By similarity
Disulfide bondi229 ↔ 242By similarity
Disulfide bondi244 ↔ 253By similarity
Disulfide bondi256 ↔ 267By similarity
Disulfide bondi262 ↔ 273By similarity
Disulfide bondi275 ↔ 284By similarity
Disulfide bondi291 ↔ 303By similarity
Disulfide bondi297 ↔ 313By similarity
Disulfide bondi315 ↔ 324By similarity
Disulfide bondi331 ↔ 342By similarity
Disulfide bondi336 ↔ 351By similarity
Disulfide bondi353 ↔ 362By similarity
Disulfide bondi369 ↔ 380By similarity
Disulfide bondi374 ↔ 390By similarity
Disulfide bondi392 ↔ 401By similarity
Disulfide bondi408 ↔ 419By similarity
Disulfide bondi413 ↔ 428By similarity
Disulfide bondi430 ↔ 439By similarity
Disulfide bondi446 ↔ 457By similarity
Disulfide bondi451 ↔ 466By similarity
Disulfide bondi468 ↔ 477By similarity
<p>This subsection of the <a href="http://www.uniprot.org/help/ptm_processing_section">PTM / Processing</a> section specifies the position and type of each covalently attached glycan group (mono-, di-, or polysaccharide).<p><a href='/help/carbohyd' target='_top'>More...</a></p>Glycosylationi476N-linked (GlcNAc...) asparagineSequence analysis1
Disulfide bondi484 ↔ 495By similarity
Disulfide bondi489 ↔ 504By similarity
Disulfide bondi506 ↔ 515By similarity
<p>This subsection of the <a href="http://www.uniprot.org/help/ptm_processing_section">PTM / Processing</a> section describes <strong>covalent linkages</strong> of various types formed <strong>between two proteins (interchain cross-links)</strong> or <strong>between two parts of the same protein (intrachain cross-links)</strong>, except the disulfide bonds that are annotated in the <a href="http://www.uniprot.org/manual/disulfid">'Disulfide bond'</a> subsection.<p><a href='/help/crosslnk' target='_top'>More...</a></p>Cross-linki613Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)1 Publication
<p>This subsection of the ‘PTM / Processing’ section specifies the position and type of each modified residue excluding <a href="http://www.uniprot.org/manual/lipid">lipids</a>, <a href="http://www.uniprot.org/manual/carbohyd">glycans</a> and <a href="http://www.uniprot.org/manual/crosslnk">protein cross-links</a>.<p><a href='/help/mod_res' target='_top'>More...</a></p>Modified residuei638Phosphothreonine1 Publication1
Modified residuei693Phosphoserine; by PKB1 Publication1
Modified residuei696Phosphoserine1 Publication1

<p>This subsection of the <a href="http://www.uniprot.org/help/ptm_processing_section">PTM/processing</a> section describes post-translational modifications (PTMs). This subsection <strong>complements</strong> the information provided at the sequence level or describes modifications for which <strong>position-specific data is not yet available</strong>.<p><a href='/help/post-translational_modification' target='_top'>More...</a></p>Post-translational modificationi

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).By similarity3 Publications
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.1 Publication
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).2 Publications
O-fucosylated. Can be elongated to a disaccharide by MFNG.By similarity

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection describes interesting single amino acid sites on the sequence that are not defined in any other subsection. This subsection can be displayed in different sections (‘Function’, ‘PTM / Processing’, ‘Pathology and Biotech’) according to its content.<p><a href='/help/site' target='_top'>More...</a></p>Sitei527 – 528Cleavage; by MMP141 Publication2
Sitei535 – 536Cleavage; by ADAM protease1 Publication2

Keywords - PTMi

Disulfide bond, Glycoprotein, Isopeptide bond, Phosphoprotein, Ubl conjugation

Proteomic databases

PaxDb, a database of protein abundance averages across all three domains of life

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PaxDbi
Q61483

PRoteomics IDEntifications database

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PRIDEi
Q61483

PTM databases

iPTMnet integrated resource for PTMs in systems biology context

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iPTMneti
Q61483

Comprehensive resource for the study of protein post-translational modifications (PTMs) in human, mouse and rat.

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PhosphoSitePlusi
Q61483

<p>This section provides information on the expression of a gene at the mRNA or protein level in cells or in tissues of multicellular organisms.<p><a href='/help/expression_section' target='_top'>More...</a></p>Expressioni

<p>This subsection of the ‘Expression’ section provides information on the expression of a gene at the mRNA or protein level in cells or in tissues of multicellular organisms. By default, the information is derived from experiments at the mRNA level, unless specified ‘at protein level’. <br></br>Examples: <a href="http://www.uniprot.org/uniprot/P92958#expression">P92958</a>, <a href="http://www.uniprot.org/uniprot/Q8TDN4#expression">Q8TDN4</a>, <a href="http://www.uniprot.org/uniprot/O14734#expression">O14734</a><p><a href='/help/tissue_specificity' target='_top'>More...</a></p>Tissue specificityi

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).2 Publications

<p>This subsection of the ‘Expression’ section provides information on the expression of the gene product at various stages of a cell, tissue or organism development. By default, the information is derived from experiments at the mRNA level, unless specified ‘at the protein level’.<p><a href='/help/developmental_stage' target='_top'>More...</a></p>Developmental stagei

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).6 Publications

<p>This subsection of the ‘Expression’ section reports the experimentally proven effects of inducers and repressors (usually chemical compounds or environmental factors) on the level of protein (or mRNA) expression (up-regulation, down-regulation, constitutive expression).<p><a href='/help/induction' target='_top'>More...</a></p>Inductioni

Induced by PTF1A in multipotent pancreatic progenitor cells (PubMed:22096075). Induced by CDX1 and CDX2 during somitogenesis and goblet cell differentiation (PubMed:22015720).2 Publications

Gene expression databases

Bgee dataBase for Gene Expression Evolution

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Bgeei
ENSMUSG00000014773 Expressed in 315 organ(s), highest expression level in presomitic mesoderm

Genevisible search portal to normalized and curated expression data from Genevestigator

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Genevisiblei
Q61483 MM

<p>This section provides information on the quaternary structure of a protein and on interaction(s) with other proteins or protein complexes.<p><a href='/help/interaction_section' target='_top'>More...</a></p>Interactioni

<p>This subsection of the <a href="http://www.uniprot.org/help/interaction_section">'Interaction'</a> section provides information about the protein quaternary structure and interaction(s) with other proteins or protein complexes (with the exception of physiological receptor-ligand interactions which are annotated in the <a href="http://www.uniprot.org/help/function_section">'Function'</a> section).<p><a href='/help/subunit_structure' target='_top'>More...</a></p>Subunit structurei

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).By similarity8 Publications

<p>This subsection of the '<a href="http://www.uniprot.org/help/interaction_section%27">Interaction</a> section provides information about binary protein-protein interactions. The data presented in this section are a quality-filtered subset of binary interactions automatically derived from the <a href="http://www.ebi.ac.uk/intact/">IntAct database</a>. It is updated on a monthly basis. Each binary interaction is displayed on a separate line.<p><a href='/help/binary_interactions' target='_top'>More...</a></p>Binary interactionsi

WithEntry#Exp.IntActNotes
Magi2Q9WVQ13EBI-297125,EBI-297151

GO - Molecular functioni

Protein-protein interaction databases

The Biological General Repository for Interaction Datasets (BioGrid)

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BioGridi
199232, 7 interactors

Database of interacting proteins

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DIPi
DIP-32600N

Protein interaction database and analysis system

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IntActi
Q61483, 8 interactors

Molecular INTeraction database

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MINTi
Q61483

STRING: functional protein association networks

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STRINGi
10090.ENSMUSP00000014917

<p>This section provides information on the tertiary and secondary structure of a protein.<p><a href='/help/structure_section' target='_top'>More...</a></p>Structurei

3D structure databases

SWISS-MODEL Repository - a database of annotated 3D protein structure models

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SMRi
Q61483

Database of comparative protein structure models

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ModBasei
Search...

MobiDB: a database of protein disorder and mobility annotations

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MobiDBi
Search...

<p>This section provides information on sequence similarities with other proteins and the domain(s) present in a protein.<p><a href='/help/family_and_domains_section' target='_top'>More...</a></p>Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/help/family_and_domains_section">Family and Domains</a> section describes the position and type of a domain, which is defined as a specific combination of secondary structures organized into a characteristic three-dimensional structure or fold.<p><a href='/help/domain' target='_top'>More...</a></p>Domaini176 – 220DSLPROSITE-ProRule annotationAdd BLAST45
Domaini225 – 253EGF-like 1PROSITE-ProRule annotationAdd BLAST29
Domaini256 – 284EGF-like 2PROSITE-ProRule annotationAdd BLAST29
Domaini291 – 324EGF-like 3PROSITE-ProRule annotationAdd BLAST34
Domaini331 – 362EGF-like 4; calcium-bindingPROSITE-ProRule annotationAdd BLAST32
Domaini369 – 401EGF-like 5PROSITE-ProRule annotationAdd BLAST33
Domaini408 – 439EGF-like 6PROSITE-ProRule annotationAdd BLAST32
Domaini446 – 477EGF-like 7; calcium-bindingPROSITE-ProRule annotationAdd BLAST32
Domaini484 – 515EGF-like 8PROSITE-ProRule annotationAdd BLAST32

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the ‘Family and Domains’ section describes a region of interest that cannot be described in other subsections.<p><a href='/help/region' target='_top'>More...</a></p>Regioni719 – 722Interaction with MAGI11 Publication4

Keywords - Domaini

EGF-like domain, Repeat, Signal, Transmembrane, Transmembrane helix

Phylogenomic databases

evolutionary genealogy of genes: Non-supervised Orthologous Groups

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eggNOGi
ENOG410IR7B Eukaryota
ENOG410XUNS LUCA

Ensembl GeneTree

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GeneTreei
ENSGT00940000159781

The HOGENOM Database of Homologous Genes from Fully Sequenced Organisms

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HOGENOMi
HOG000267024

InParanoid: Eukaryotic Ortholog Groups

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InParanoidi
Q61483

KEGG Orthology (KO)

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KOi
K06051

Identification of Orthologs from Complete Genome Data

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OMAi
DKPCHQG

Database of Orthologous Groups

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OrthoDBi
406049at2759

TreeFam database of animal gene trees

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TreeFami
TF351835

Family and domain databases

Integrated resource of protein families, domains and functional sites

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InterProi
View protein in InterPro
IPR001774 DSL
IPR001881 EGF-like_Ca-bd_dom
IPR013032 EGF-like_CS
IPR000742 EGF-like_dom
IPR000152 EGF-type_Asp/Asn_hydroxyl_site
IPR018097 EGF_Ca-bd_CS
IPR009030 Growth_fac_rcpt_cys_sf
IPR011651 Notch_ligand_N

Pfam protein domain database

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Pfami
View protein in Pfam
PF01414 DSL, 1 hit
PF00008 EGF, 4 hits
PF07645 EGF_CA, 1 hit
PF12661 hEGF, 1 hit
PF07657 MNNL, 1 hit

Simple Modular Architecture Research Tool; a protein domain database

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SMARTi
View protein in SMART
SM00051 DSL, 1 hit
SM00181 EGF, 8 hits
SM00179 EGF_CA, 6 hits

Superfamily database of structural and functional annotation

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SUPFAMi
SSF57184 SSF57184, 1 hit

PROSITE; a protein domain and family database

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PROSITEi
View protein in PROSITE
PS00010 ASX_HYDROXYL, 3 hits
PS51051 DSL, 1 hit
PS00022 EGF_1, 8 hits
PS01186 EGF_2, 8 hits
PS50026 EGF_3, 7 hits
PS01187 EGF_CA, 2 hits

<p>This section displays by default the canonical protein sequence and upon request all isoforms described in the entry. It also includes information pertinent to the sequence(s), including <a href="http://www.uniprot.org/help/sequence_length">length</a> and <a href="http://www.uniprot.org/help/sequences">molecular weight</a>. The information is filed in different subsections. The current subsections and their content are listed below:<p><a href='/help/sequences_section' target='_top'>More...</a></p>Sequence (1+)i

<p>This subsection of the <a href="http://www.uniprot.org/help/sequences_section">Sequence</a> section indicates if the <a href="http://www.uniprot.org/help/canonical_and_isoforms">canonical sequence</a> displayed by default in the entry is complete or not.<p><a href='/help/sequence_status' target='_top'>More...</a></p>Sequence statusi: Complete.

<p>This subsection of the <a href="http://www.uniprot.org/help/sequences_section">Sequence</a> section indicates if the <a href="http://www.uniprot.org/help/canonical_and_isoforms">canonical sequence</a> displayed by default in the entry is in its mature form or if it represents the precursor.<p><a href='/help/sequence_processing' target='_top'>More...</a></p>Sequence processingi: The displayed sequence is further processed into a mature form.

This entry has 1 described isoform and 1 potential isoform that is computationally mapped.Show allAlign All

Q61483-1 [UniParc]FASTAAdd to basket
« Hide
        10         20         30         40         50
MGRRSALALA VVSALLCQVW SSGVFELKLQ EFVNKKGLLG NRNCCRGGSG
60 70 80 90 100
PPCACRTFFR VCLKHYQASV SPEPPCTYGS AVTPVLGVDS FSLPDGAGID
110 120 130 140 150
PAFSNPIRFP FGFTWPGTFS LIIEALHTDS PDDLATENPE RLISRLTTQR
160 170 180 190 200
HLTVGEEWSQ DLHSSGRTDL RYSYRFVCDE HYYGEGCSVF CRPRDDAFGH
210 220 230 240 250
FTCGDRGEKM CDPGWKGQYC TDPICLPGCD DQHGYCDKPG ECKCRVGWQG
260 270 280 290 300
RYCDECIRYP GCLHGTCQQP WQCNCQEGWG GLFCNQDLNY CTHHKPCRNG
310 320 330 340 350
ATCTNTGQGS YTCSCRPGYT GANCELEVDE CAPSPCKNGA SCTDLEDSFS
360 370 380 390 400
CTCPPGFYGK VCELSAMTCA DGPCFNGGRC SDNPDGGYTC HCPLGFSGFN
410 420 430 440 450
CEKKMDLCGS SPCSNGAKCV DLGNSYLCRC QAGFSGRYCE DNVDDCASSP
460 470 480 490 500
CANGGTCRDS VNDFSCTCPP GYTGKNCSAP VSRCEHAPCH NGATCHQRGQ
510 520 530 540 550
RYMCECAQGY GGPNCQFLLP EPPPGPMVVD LSERHMESQG GPFPWVAVCA
560 570 580 590 600
GVVLVLLLLL GCAAVVVCVR LKLQKHQPPP EPCGGETETM NNLANCQREK
610 620 630 640 650
DVSVSIIGAT QIKNTNKKAD FHGDHGAEKS SFKVRYPTVD YNLVRDLKGD
660 670 680 690 700
EATVRDTHSK RDTKCQSQSS AGEEKIAPTL RGGEIPDRKR PESVYSTSKD
710 720
TKYQSVYVLS AEKDECVIAT EV
Length:722
Mass (Da):78,449
Last modified:July 27, 2011 - v2
<p>The checksum is a form of redundancy check that is calculated from the sequence. It is useful for tracking sequence updates.</p> <p>It should be noted that while, in theory, two different sequences could have the same checksum value, the likelihood that this would happen is extremely low.</p> <p>However UniProtKB may contain entries with identical sequences in case of multiple genes (paralogs).</p> <p>The checksum is computed as the sequence 64-bit Cyclic Redundancy Check value (CRC64) using the generator polynomial: x<sup>64</sup> + x<sup>4</sup> + x<sup>3</sup> + x + 1. The algorithm is described in the ISO 3309 standard. </p> <p class="publication">Press W.H., Flannery B.P., Teukolsky S.A. and Vetterling W.T.<br /> <strong>Cyclic redundancy and other checksums</strong><br /> <a href="http://www.nrbook.com/b/bookcpdf.php">Numerical recipes in C 2nd ed., pp896-902, Cambridge University Press (1993)</a>)</p> Checksum:i9D570B9DC7EEC75E
GO

<p>In eukaryotic reference proteomes, unreviewed entries that are likely to belong to the same gene are computationally mapped, based on gene identifiers from Ensembl, EnsemblGenomes and model organism databases.<p><a href='/help/gene_centric_isoform_mapping' target='_top'>More...</a></p>Computationally mapped potential isoform sequencesi

There is 1 potential isoform mapped to this entry.BLASTAlignShow allAdd to basket
EntryEntry nameProtein names
Gene namesLengthAnnotation
A0A338P7A6A0A338P7A6_MOUSE
Delta-like protein 1
Dll1
73Annotation score:

Annotation score:1 out of 5

<p>The annotation score provides a heuristic measure of the annotation content of a UniProtKB entry or proteome. This score <strong>cannot</strong> be used as a measure of the accuracy of the annotation as we cannot define the ‘correct annotation’ for any given protein.<p><a href='/help/annotation_score' target='_top'>More...</a></p>

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the ‘Sequence’ section reports difference(s) between the canonical sequence (displayed by default in the entry) and the different sequence submissions merged in the entry. These various submissions may originate from different sequencing projects, different types of experiments, or different biological samples. Sequence conflicts are usually of unknown origin.<p><a href='/help/conflict' target='_top'>More...</a></p>Sequence conflicti628E → K in CAA56865 (PubMed:7671806).Curated1

Sequence databases

Select the link destinations:

EMBL nucleotide sequence database

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EMBLi

GenBank nucleotide sequence database

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GenBanki

DNA Data Bank of Japan; a nucleotide sequence database

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DDBJi
Links Updated
X80903 mRNA Translation: CAA56865.1
AY497019 Genomic DNA Translation: AAR30869.1
CH466630 Genomic DNA Translation: EDL20466.1
BC057400 mRNA Translation: AAH57400.1
BC065063 mRNA Translation: AAH65063.1

The Consensus CDS (CCDS) project

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CCDSi
CCDS37452.1

Protein sequence database of the Protein Information Resource

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PIRi
I48324

NCBI Reference Sequences

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RefSeqi
NP_031891.2, NM_007865.3

Genome annotation databases

Ensembl eukaryotic genome annotation project

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Ensembli
ENSMUST00000014917; ENSMUSP00000014917; ENSMUSG00000014773

Database of genes from NCBI RefSeq genomes

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GeneIDi
13388

KEGG: Kyoto Encyclopedia of Genes and Genomes

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KEGGi
mmu:13388

UCSC genome browser

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UCSCi
uc008aoi.2 mouse

<p>This section provides links to proteins that are similar to the protein sequence(s) described in this entry at different levels of sequence identity thresholds (100%, 90% and 50%) based on their membership in UniProt Reference Clusters (<a href="http://www.uniprot.org/help/uniref">UniRef</a>).<p><a href='/help/similar_proteins_section' target='_top'>More...</a></p>Similar proteinsi

<p>This section is used to point to information related to entries and found in data collections other than UniProtKB.<p><a href='/help/cross_references_section' target='_top'>More...</a></p>Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X80903 mRNA Translation: CAA56865.1
AY497019 Genomic DNA Translation: AAR30869.1
CH466630 Genomic DNA Translation: EDL20466.1
BC057400 mRNA Translation: AAH57400.1
BC065063 mRNA Translation: AAH65063.1
CCDSiCCDS37452.1
PIRiI48324
RefSeqiNP_031891.2, NM_007865.3

3D structure databases

SMRiQ61483
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi199232, 7 interactors
DIPiDIP-32600N
IntActiQ61483, 8 interactors
MINTiQ61483
STRINGi10090.ENSMUSP00000014917

PTM databases

iPTMnetiQ61483
PhosphoSitePlusiQ61483

Proteomic databases

PaxDbiQ61483
PRIDEiQ61483

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSMUST00000014917; ENSMUSP00000014917; ENSMUSG00000014773
GeneIDi13388
KEGGimmu:13388
UCSCiuc008aoi.2 mouse

Organism-specific databases

Comparative Toxicogenomics Database

More...
CTDi
28514
MGIiMGI:104659 Dll1

Phylogenomic databases

eggNOGiENOG410IR7B Eukaryota
ENOG410XUNS LUCA
GeneTreeiENSGT00940000159781
HOGENOMiHOG000267024
InParanoidiQ61483
KOiK06051
OMAiDKPCHQG
OrthoDBi406049at2759
TreeFamiTF351835

Enzyme and pathway databases

ReactomeiR-MMU-9013507 NOTCH3 Activation and Transmission of Signal to the Nucleus

Miscellaneous databases

Protein Ontology

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PROi
PR:Q61483

The Stanford Online Universal Resource for Clones and ESTs

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SOURCEi
Search...

Gene expression databases

BgeeiENSMUSG00000014773 Expressed in 315 organ(s), highest expression level in presomitic mesoderm
GenevisibleiQ61483 MM

Family and domain databases

InterProiView protein in InterPro
IPR001774 DSL
IPR001881 EGF-like_Ca-bd_dom
IPR013032 EGF-like_CS
IPR000742 EGF-like_dom
IPR000152 EGF-type_Asp/Asn_hydroxyl_site
IPR018097 EGF_Ca-bd_CS
IPR009030 Growth_fac_rcpt_cys_sf
IPR011651 Notch_ligand_N
PfamiView protein in Pfam
PF01414 DSL, 1 hit
PF00008 EGF, 4 hits
PF07645 EGF_CA, 1 hit
PF12661 hEGF, 1 hit
PF07657 MNNL, 1 hit
SMARTiView protein in SMART
SM00051 DSL, 1 hit
SM00181 EGF, 8 hits
SM00179 EGF_CA, 6 hits
SUPFAMiSSF57184 SSF57184, 1 hit
PROSITEiView protein in PROSITE
PS00010 ASX_HYDROXYL, 3 hits
PS51051 DSL, 1 hit
PS00022 EGF_1, 8 hits
PS01186 EGF_2, 8 hits
PS50026 EGF_3, 7 hits
PS01187 EGF_CA, 2 hits

ProtoNet; Automatic hierarchical classification of proteins

More...
ProtoNeti
Search...

<p>This section provides general information on the entry.<p><a href='/help/entry_information_section' target='_top'>More...</a></p>Entry informationi

<p>This subsection of the ‘Entry information’ section provides a mnemonic identifier for a UniProtKB entry, but it is not a stable identifier. Each reviewed entry is assigned a unique entry name upon integration into UniProtKB/Swiss-Prot.<p><a href='/help/entry_name' target='_top'>More...</a></p>Entry nameiDLL1_MOUSE
<p>This subsection of the ‘Entry information’ section provides one or more accession number(s). These are stable identifiers and should be used to cite UniProtKB entries. Upon integration into UniProtKB, each entry is assigned a unique accession number, which is called ‘Primary (citable) accession number’.<p><a href='/help/accession_numbers' target='_top'>More...</a></p>AccessioniPrimary (citable) accession number: Q61483
Secondary accession number(s): Q6PFV7
<p>This subsection of the ‘Entry information’ section shows the date of integration of the entry into UniProtKB, the date of the last sequence update and the date of the last annotation modification (‘Last modified’). The version number for both the entry and the <a href="http://www.uniprot.org/help/canonical_and_isoforms">canonical sequence</a> are also displayed.<p><a href='/help/entry_history' target='_top'>More...</a></p>Entry historyiIntegrated into UniProtKB/Swiss-Prot: November 1, 1997
Last sequence update: July 27, 2011
Last modified: May 8, 2019
This is version 178 of the entry and version 2 of the sequence. See complete history.
<p>This subsection of the ‘Entry information’ section indicates whether the entry has been manually annotated and reviewed by UniProtKB curators or not, in other words, if the entry belongs to the Swiss-Prot section of UniProtKB (<strong>reviewed</strong>) or to the computer-annotated TrEMBL section (<strong>unreviewed</strong>).<p><a href='/help/entry_status' target='_top'>More...</a></p>Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

<p>This section contains any relevant information that doesn’t fit in any other defined sections<p><a href='/help/miscellaneous_section' target='_top'>More...</a></p>Miscellaneousi

Keywords - Technical termi

Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. MGD cross-references
    Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
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