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Entry version 191 (16 Oct 2019)
Sequence version 2 (05 May 2009)
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Protein

Dystroglycan

Gene

DAG1

Organism
Homo sapiens (Human)
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

The dystroglycan complex is involved in a number of processes including laminin and basement membrane assembly, sarcolemmal stability, cell survival, peripheral nerve myelination, nodal structure, cell migration, and epithelial polarization.
Alpha-dystroglycan is an extracellular peripheral glycoprotein that acts as a receptor for both extracellular matrix proteins containing laminin-G domains. Receptor for laminin-2 (LAMA2) and agrin in peripheral nerve Schwann cells.
Beta-dystroglycan is a transmembrane protein that plays important roles in connecting the extracellular matrix to the cytoskeleton. Acts as a cell adhesion receptor in both muscle and non-muscle tissues. Receptor for both DMD and UTRN and, through these interactions, scaffolds axin to the cytoskeleton. Also functions in cell adhesion-mediated signaling and implicated in cell polarity.
(Microbial infection) Alpha-dystroglycan acts as a receptor for lassa virus and lymphocytic choriomeningitis virus glycoprotein and class C new-world arenaviruses (PubMed:16254364, PubMed:19324387, PubMed:17360738). Alpha-dystroglycan acts as a Schwann cell receptor for Mycobacterium leprae, the causative organism of leprosy, but only in the presence of the G-domain of LAMA2 (PubMed:9851927).4 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 functionHost cell receptor for virus entry, Receptor
Biological processHost-virus interaction

Enzyme and pathway databases

Reactome - a knowledgebase of biological pathways and processes

More...
Reactomei
R-HSA-3000171 Non-integrin membrane-ECM interactions
R-HSA-3000178 ECM proteoglycans
R-HSA-5083628 Defective POMGNT1 causes MDDGA3, MDDGB3 and MDDGC3
R-HSA-5083629 Defective POMT2 causes MDDGA2, MDDGB2 and MDDGC2
R-HSA-5083633 Defective POMT1 causes MDDGA1, MDDGB1 and MDDGC1
R-HSA-5173105 O-linked glycosylation
R-HSA-9010553 Regulation of expression of SLITs and ROBOs

SIGNOR Signaling Network Open Resource

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SIGNORi
Q14118

Protein family/group databases

MEROPS protease database

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MEROPSi
S72.001

Transport Classification Database

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TCDBi
9.B.277.1.1 the dystroglycan (dg) family

<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:
Dystroglycan
Alternative name(s):
Dystrophin-associated glycoprotein 1
Cleaved into the following 2 chains:
Alpha-dystroglycan
Short name:
Alpha-DG
Beta-dystroglycan
Short name:
Beta-DG
<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:DAG1
<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>OrganismiHomo sapiens (Human)
<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 identifieri9606 [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 lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
<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
  • UP000005640 <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 3

Organism-specific databases

Human Gene Nomenclature Database

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HGNCi
HGNC:2666 DAG1

Online Mendelian Inheritance in Man (OMIM)

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MIMi
128239 gene

neXtProt; the human protein knowledge platform

More...
neXtProti
NX_Q14118

<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 domaini654 – 749ExtracellularSequence analysisAdd BLAST96
<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>Transmembranei750 – 775HelicalSequence analysisAdd BLAST26
Topological domaini776 – 895CytoplasmicSequence analysisAdd BLAST120

Keywords - Cellular componenti

Cell junction, Cell membrane, Cytoplasm, Cytoskeleton, Membrane, Nucleus, Postsynaptic cell membrane, Secreted, Synapse

<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 provides information on the disease(s) associated with genetic variations in a given protein. The information is extracted from the scientific literature and diseases that are also described in the <a href="http://www.ncbi.nlm.nih.gov/sites/entrez?db=omim">OMIM</a> database are represented with a <a href="http://www.uniprot.org/diseases">controlled vocabulary</a> in the following way:<p><a href='/help/involvement_in_disease' target='_top'>More...</a></p>Involvement in diseasei

Muscular dystrophy-dystroglycanopathy limb-girdle C9 (MDDGC9)2 Publications
The disease is caused by mutations affecting the gene represented in this entry. MDDGC7 is caused by DAG1 mutations that interfere with normal post-translational processing, resulting in defective DAG1 glycosylation and impaired interactions with extracellular-matrix components. Other muscular dystrophy-dystroglycanopathies are caused by defects in enzymes involved in protein O-glycosylation.
Disease descriptionAn autosomal recessive muscular dystrophy showing onset in early childhood, and associated with mental retardation without structural brain anomalies.
Related information in OMIM
Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the ‘Sequence’ section describes natural variant(s) of the protein sequence.<p><a href='/help/variant' target='_top'>More...</a></p>Natural variantiVAR_07580974V → I in MDDGC9; no effect on dystroglycan expression; impairs alpha-dystroglycan glycosylation. 1 PublicationCorresponds to variant dbSNP:rs189360006EnsemblClinVar.1
Natural variantiVAR_075810111D → N in MDDGC9; does not affect dystroglycan expression; impairs alpha-dystroglycan glycosylation. 1 PublicationCorresponds to variant dbSNP:rs117209107EnsemblClinVar.1
Natural variantiVAR_065266192T → M in MDDGC9; results in impaired interaction with LARGE1 and incomplete DAG1 glycosylation. 1 PublicationCorresponds to variant dbSNP:rs193922955EnsemblClinVar.1
Muscular dystrophy-dystroglycanopathy congenital with brain and eye anomalies A9 (MDDGA9)2 Publications
The disease is caused by mutations affecting the gene represented in this entry.
Disease descriptionAn autosomal recessive disorder characterized by congenital muscular dystrophy associated with cobblestone lissencephaly and other brain anomalies, eye malformations, profound mental retardation, and death usually in the first years of life. Included diseases are the more severe Walker-Warburg syndrome and the slightly less severe muscle-eye-brain disease.
Related information in OMIM
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Natural variantiVAR_075811669C → F in MDDGA9. 1 PublicationCorresponds to variant dbSNP:rs797045023EnsemblClinVar.1

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>Mutagenesisi317 – 319TPT → APA: Impaired laminin-binding. 2 Publications3
Mutagenesisi328 – 329TT → AA: Does not affect laminin-binding. 1 Publication2
Mutagenesisi654S → A: Abolishes autoproteolysis and enhances laminin-binding. 2 Publications1
Mutagenesisi663T → A: Reduced N-linked glycosylation. No change in nuclear translocation. 1 Publication1
Mutagenesisi776 – 782RKKRKGK → AKKRKGA: Moderate reduction in nuclear accumulation. 7
Mutagenesisi777 – 782KKRKGK → AARKGA: About 50% reduction in nuclear accumulation. 1 Publication6
Mutagenesisi777 – 782KKRKGK → RKKAAGA: Drastic reduction in nuclear accumulation. 1 Publication6
Mutagenesisi777 – 780KKRK → NPGE: Abolishes nuclear translocation. 1 Publication4
Mutagenesisi779R → A: Significant reduction in nuclear accumulation. 1
Mutagenesisi780K → A: Significant reduction in nuclear accumulation. 1
Mutagenesisi793 – 794KK → TA: Abolishes nuclear translocation. 1 Publication2
Mutagenesisi823K → A: No change in nuclear location. 1 Publication1
Mutagenesisi828 – 829PP → AA: No change in nuclear location. 1 Publication2
Mutagenesisi831Y → A: No change in nuclear location. 1 Publication1
Mutagenesisi892Y → A: Abolishes phosphorylation. No change in plasma membrane location. 2 Publications1
Mutagenesisi892Y → E: Redistributes to a vesicular internal membrane compartment. 2 Publications1
Mutagenesisi892Y → F: Abolishes phosphorylation. Increase in nuclear location. 2 Publications1

Keywords - Diseasei

Congenital muscular dystrophy, Disease mutation, Dystroglycanopathy, Limb-girdle muscular dystrophy, Lissencephaly

Organism-specific databases

DisGeNET

More...
DisGeNETi
1605

MalaCards human disease database

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MalaCardsi
DAG1
MIMi613818 phenotype
616538 phenotype

Open Targets

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OpenTargetsi
ENSG00000173402

Orphanet; a database dedicated to information on rare diseases and orphan drugs

More...
Orphaneti
280333 Autosomal recessive limb-girdle muscular dystrophy type 2P
370997 Muscle-eye-brain disease with bilateral multicystic leucodystrophy
899 Walker-Warburg syndrome

The Pharmacogenetics and Pharmacogenomics Knowledge Base

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PharmGKBi
PA27138

Miscellaneous databases

Pharos NIH Druggable Genome Knowledgebase

More...
Pharosi
Q14118

Chemistry databases

ChEMBL database of bioactive drug-like small molecules

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ChEMBLi
CHEMBL3714399

Polymorphism and mutation databases

BioMuta curated single-nucleotide variation and disease association database

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BioMutai
DAG1

Domain mapping of disease mutations (DMDM)

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DMDMi
229462879

<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 – 29Sequence analysisAdd BLAST29
<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_000002106530 – 653Alpha-dystroglycanAdd BLAST624
ChainiPRO_0000021066654 – 895Beta-dystroglycanAdd BLAST242

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<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>Glycosylationi63O-linked (GalNAc...) threonine1 Publication1
Glycosylationi141N-linked (GlcNAc...) asparagineSequence analysis1
<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 bondi182 ↔ 264Combined sources1 Publication
Glycosylationi317O-linked (Man6P...) threonine2 Publications1
Glycosylationi319O-linked (Man6P...) threonine2 Publications1
Glycosylationi367O-linked (Hex...) threonine1 Publication1
Glycosylationi369O-linked (Hex...) threonine1 Publication1
Glycosylationi372O-linked (Hex...) threonine1 Publication1
Glycosylationi379O-linked (Man6P...) threonine1 Publication1
Glycosylationi381O-linked (Hex...) threonine1 Publication1
Glycosylationi388O-linked (Hex...) threonine1 Publication1
Glycosylationi455O-linked (GalNAc...) threonine1 Publication1
Glycosylationi641N-linked (GlcNAc...) asparagineSequence analysis1
Glycosylationi649N-linked (GlcNAc...) asparagineSequence analysis1
Glycosylationi661N-linked (GlcNAc...) asparagineSequence analysis1
Disulfide bondi669 ↔ 7131 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 residuei790PhosphothreonineCombined sources1
Modified residuei892Phosphotyrosine; by SRC3 Publications1

<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

O-glycosylated. POMGNT1 catalyzes the initial addition of N-acetylglucosamine, giving rise to the GlcNAc(beta1-2)Man(alpha1-)O-Ser/Thr moiety and thus providing the necessary basis for the addition of further carbohydrate moieties (PubMed:27493216). Alpha-dystroglycan is heavily O-glycosylated comprising of up to two thirds of its mass and the carbohydrate composition differs depending on tissue type. Mucin-type O-glycosylation is important for ligand binding activity. O-mannosylation of alpha-DAG1 is found in high abundance in both brain and muscle where the most abundant glycan is Sia-alpha-2-3-Gal-beta-1-4-Glc-NAc-beta-1-2-Man. In muscle, glycosylation on Thr-317, Thr-319 and Thr-379 by a phosphorylated O-mannosyl glycan with the structure 2-(N-acetylamido)-2-deoxygalactosyl-beta-1,3-2-(N-acetylamido)-2-deoxyglucosyl-beta-1,4-6-phosphomannose is mediated by like-acetylglucosaminyltransferase (LARGE1) protein and is required for laminin binding (PubMed:20044576, PubMed:21987822, PubMed:24256719). O-mannosylation is also required for binding lymphocytic choriomeningitis virus, Old World Lassa fever virus, and clade C New World arenaviruses. The O-glycosyl hexose on Thr-367, Thr-369, Thr-372, Thr-381 and Thr-388 is probably mannose. O-glycosylated in the N-terminal region with a core 1 or possibly core 8 glycan.11 Publications
The beta subunit is N-glycosylated.Sequence analysis
Autolytic cleavage produces the alpha and beta subunits. In cutaneous cells, as well as in certain pathological conditions, shedding of beta-dystroglcan can occur releasing a peptide of about 30 kDa.4 Publications
SRC-mediated phosphorylation of the PPXY motif of the beta subunit recruits SH2 domain-containing proteins, but inhibits binding to WWW domain-containing proteins, DMD and UTRN. This phosphorylation also inhibits nuclear entry.

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>Sitei653 – 654Cleavage; by autolysis1 Publication2
Sitei715 – 716Cleavage; by MMP91 Publication2

Keywords - PTMi

Autocatalytic cleavage, Disulfide bond, Glycoprotein, Phosphoprotein

Proteomic databases

Encyclopedia of Proteome Dynamics

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EPDi
Q14118

jPOST - Japan Proteome Standard Repository/Database

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jPOSTi
Q14118

MassIVE - Mass Spectrometry Interactive Virtual Environment

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MassIVEi
Q14118

MaxQB - The MaxQuant DataBase

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MaxQBi
Q14118

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

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PaxDbi
Q14118

PeptideAtlas

More...
PeptideAtlasi
Q14118

PRoteomics IDEntifications database

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PRIDEi
Q14118

ProteomicsDB: a multi-organism proteome resource

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ProteomicsDBi
59825

Consortium for Top Down Proteomics

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TopDownProteomicsi
Q14118

PTM databases

GlyConnect protein glycosylation platform

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GlyConnecti
715

iPTMnet integrated resource for PTMs in systems biology context

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iPTMneti
Q14118

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

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PhosphoSitePlusi
Q14118

SwissPalm database of S-palmitoylation events

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SwissPalmi
Q14118

UniCarbKB; an annotated and curated database of glycan structures

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UniCarbKBi
Q14118

<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

Expressed in a variety of fetal and adult tissues. In epidermal tissue, located to the basement membrane. Also expressed in keratinocytes and fibroblasts.2 Publications

Gene expression databases

Bgee dataBase for Gene Expression Evolution

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Bgeei
ENSG00000173402 Expressed in 246 organ(s), highest expression level in olfactory bulb

ExpressionAtlas, Differential and Baseline Expression

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ExpressionAtlasi
Q14118 baseline and differential

Genevisible search portal to normalized and curated expression data from Genevestigator

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Genevisiblei
Q14118 HS

Organism-specific databases

Human Protein Atlas

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HPAi
CAB001960
CAB016353

<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

Monomer. Heterodimer of alpha- and beta-dystroglycan subunits which are the central components of the dystrophin-glycoprotein complex. This complex then can form a dystrophin-associated glycoprotein complex (DGC) which is composed of three subcomplexes: a cytoplasmic complex comprised of DMD (or UTRN), DTNA and a number of syntrophins, such as SNTB1, SNTB2, SNTG1 and SNTG2, the transmembrane dystroglycan complex, and the sarcoglycan-sarcospan complex.

Interacts (via the N-terminal of alphaDAG1) with LARGE1; the interaction enhances laminin binding (By similarity).

Interacts with SGCD.

Interacts with AGR2 and AGR3.

Interacts (betaDAG1) with DMD; the interaction is inhibited by phosphorylation on the PPXY motif.

Interacts (betaDAG1, via its PPXY motif) with UTRN (via its WWW and ZZ domains); the interaction is inhibited by phosphorylation on the PPXY motif.

Interacts (betaDAG1, via its phosphorylated PPXY motif) with the SH2 domain-containing proteins, FYN, CSK, NCK and SHC.

Interacts (betaDAG1) with CAV3 (via a central WW-like domain); the interaction disrupts the binding of DMD. BetaDAG1 directly interacts with ANK3, but not with ANK2; this interaction does not interfere with DMD-binding and is required for retention at costameres (By similarity).

Identified in a dystroglycan complex that contains at least PRX, DRP2, UTRN, DMD and DAG1 (By similarity).

Interacts with POMGNT1 (PubMed:27493216).

By similarity8 Publications

(Microbial infection) Interacts with lassa virus and lymphocytic choriomeningitis virus glycoprotein (PubMed:16254364, PubMed:19324387).

2 Publications

(Microbial infection) Interacts with surface molecules of mycobacterium leprae.

1 Publication

<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

GO - Molecular functioni

Protein-protein interaction databases

The Biological General Repository for Interaction Datasets (BioGrid)

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BioGridi
107975, 67 interactors

CORUM comprehensive resource of mammalian protein complexes

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CORUMi
Q14118

Database of interacting proteins

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DIPi
DIP-40928N

Protein interaction database and analysis system

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IntActi
Q14118, 64 interactors

Molecular INTeraction database

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MINTi
Q14118

STRING: functional protein association networks

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STRINGi
9606.ENSP00000442600

<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

Secondary structure

1895
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details

3D structure databases

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

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SMRi
Q14118

Database of comparative protein structure models

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ModBasei
Search...

Protein Data Bank in Europe - Knowledge Base

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PDBe-KBi
Search...

Miscellaneous databases

Relative evolutionary importance of amino acids within a protein sequence

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EvolutionaryTracei
Q14118

<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>Domaini603 – 712Peptidase S72Add BLAST110

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>Regioni30 – 408Required for laminin recognitionAdd BLAST379
Regioni169 – 200O-glycosylated at one siteAdd BLAST32
Regioni316 – 485Mucin-like domainAdd BLAST170
Regioni463 – 485O-glycosylated at seven sites with GalNAcAdd BLAST23
Regioni819 – 895Required for interaction with CAV31 PublicationAdd BLAST77
Regioni880 – 895Required for binding DMD and UTRNAdd BLAST16

Motif

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the ‘Family and Domains’ section describes a short (usually not more than 20 amino acids) conserved sequence motif of biological significance.<p><a href='/help/motif' target='_top'>More...</a></p>Motifi776 – 782Nuclear localization signal1 Publication7
Motifi889 – 892PPXY motif4

Compositional bias

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the ‘Family and Domains’ section describes the position of regions of compositional bias within the protein and the particular amino acids that are over-represented within those regions.<p><a href='/help/compbias' target='_top'>More...</a></p>Compositional biasi317 – 484Thr-richAdd BLAST168
Compositional biasi809 – 895Pro-richAdd BLAST87

Keywords - Domaini

Signal, Transmembrane, Transmembrane helix

Phylogenomic databases

evolutionary genealogy of genes: Non-supervised Orthologous Groups

More...
eggNOGi
KOG3781 Eukaryota
ENOG410XQTU LUCA

Ensembl GeneTree

More...
GeneTreei
ENSGT00390000008429

The HOGENOM Database of Homologous Genes from Fully Sequenced Organisms

More...
HOGENOMi
HOG000072580

InParanoid: Eukaryotic Ortholog Groups

More...
InParanoidi
Q14118

KEGG Orthology (KO)

More...
KOi
K06265

Identification of Orthologs from Complete Genome Data

More...
OMAi
YDKEDTT

Database of Orthologous Groups

More...
OrthoDBi
156878at2759

Database for complete collections of gene phylogenies

More...
PhylomeDBi
Q14118

TreeFam database of animal gene trees

More...
TreeFami
TF328370

Family and domain databases

Gene3D Structural and Functional Annotation of Protein Families

More...
Gene3Di
2.60.40.10, 2 hits
3.30.70.1040, 1 hit

Integrated resource of protein families, domains and functional sites

More...
InterProi
View protein in InterPro
IPR027468 Alpha-dystroglycan_domain_2
IPR041631 Alpha_DG1_N2
IPR006644 Cadg
IPR015919 Cadherin-like_sf
IPR008465 DAG1_C
IPR013783 Ig-like_fold
IPR030398 SEA_DG_dom

Pfam protein domain database

More...
Pfami
View protein in Pfam
PF18424 a_DG1_N2, 1 hit
PF05454 DAG1, 1 hit

Simple Modular Architecture Research Tool; a protein domain database

More...
SMARTi
View protein in SMART
SM00736 CADG, 2 hits

Superfamily database of structural and functional annotation

More...
SUPFAMi
SSF111006 SSF111006, 1 hit
SSF49313 SSF49313, 2 hits

PROSITE; a protein domain and family database

More...
PROSITEi
View protein in PROSITE
PS51699 SEA_DG, 1 hit

<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 9 potential isoforms that are computationally mapped.Show allAlign All

Q14118-1 [UniParc]FASTAAdd to basket
« Hide
        10         20         30         40         50
MRMSVGLSLL LPLSGRTFLL LLSVVMAQSH WPSEPSEAVR DWENQLEASM
60 70 80 90 100
HSVLSDLHEA VPTVVGIPDG TAVVGRSFRV TIPTDLIASS GDIIKVSAAG
110 120 130 140 150
KEALPSWLHW DSQSHTLEGL PLDTDKGVHY ISVSATRLGA NGSHIPQTSS
160 170 180 190 200
VFSIEVYPED HSELQSVRTA SPDPGEVVSS ACAADEPVTV LTVILDADLT
210 220 230 240 250
KMTPKQRIDL LHRMRSFSEV ELHNMKLVPV VNNRLFDMSA FMAGPGNAKK
260 270 280 290 300
VVENGALLSW KLGCSLNQNS VPDIHGVEAP AREGAMSAQL GYPVVGWHIA
310 320 330 340 350
NKKPPLPKRV RRQIHATPTP VTAIGPPTTA IQEPPSRIVP TPTSPAIAPP
360 370 380 390 400
TETMAPPVRD PVPGKPTVTI RTRGAIIQTP TLGPIQPTRV SEAGTTVPGQ
410 420 430 440 450
IRPTMTIPGY VEPTAVATPP TTTTKKPRVS TPKPATPSTD STTTTTRRPT
460 470 480 490 500
KKPRTPRPVP RVTTKVSITR LETASPPTRI RTTTSGVPRG GEPNQRPELK
510 520 530 540 550
NHIDRVDAWV GTYFEVKIPS DTFYDHEDTT TDKLKLTLKL REQQLVGEKS
560 570 580 590 600
WVQFNSNSQL MYGLPDSSHV GKHEYFMHAT DKGGLSAVDA FEIHVHRRPQ
610 620 630 640 650
GDRAPARFKA KFVGDPALVL NDIHKKIALV KKLAFAFGDR NCSTITLQNI
660 670 680 690 700
TRGSIVVEWT NNTLPLEPCP KEQIAGLSRR IAEDDGKPRP AFSNALEPDF
710 720 730 740 750
KATSITVTGS GSCRHLQFIP VVPPRRVPSE APPTEVPDRD PEKSSEDDVY
760 770 780 790 800
LHTVIPAVVV AAILLIAGII AMICYRKKRK GKLTLEDQAT FIKKGVPIIF
810 820 830 840 850
ADELDDSKPP PSSSMPLILQ EEKAPLPPPE YPNQSVPETT PLNQDTMGEY
860 870 880 890
TPLRDEDPNA PPYQPPPPFT APMEGKGSRP KNMTPYRSPP PYVPP
Length:895
Mass (Da):97,441
Last modified:May 5, 2009 - 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:i3AF6CBB0DCF91962
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 are 9 potential isoforms mapped to this entry.BLASTAlignShow allAdd to basket
EntryEntry nameProtein names
Gene namesLengthAnnotation
C9JQL4C9JQL4_HUMAN
Dystroglycan
DAG1
117Annotation 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>
C9J196C9J196_HUMAN
Dystroglycan
DAG1
106Annotation 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>
C9JYS1C9JYS1_HUMAN
Dystroglycan
DAG1
95Annotation 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>
C9J6Z6C9J6Z6_HUMAN
Dystroglycan
DAG1
88Annotation 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>
C9JEN1C9JEN1_HUMAN
Dystroglycan
DAG1
86Annotation 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>
C9JEH2C9JEH2_HUMAN
Dystroglycan
DAG1
52Annotation 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>
C9JY76C9JY76_HUMAN
Dystroglycan
DAG1
41Annotation 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>
C9JLH6C9JLH6_HUMAN
Dystroglycan
DAG1
15Annotation 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>
A0A1D5RMP6A0A1D5RMP6_HUMAN
Dystroglycan
DAG1
8Annotation 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 conflicti163E → D in AAA81779 (PubMed:8268918).Curated1
Sequence conflicti248A → P in AAA81779 (PubMed:8268918).Curated1
Sequence conflicti319T → A in BAF84381 (PubMed:14702039).Curated1
Sequence conflicti871A → V in AAA81779 (PubMed:8268918).Curated1

Natural variant

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Natural variantiVAR_02433514S → W4 PublicationsCorresponds to variant dbSNP:rs2131107Ensembl.1
Natural variantiVAR_07580974V → I in MDDGC9; no effect on dystroglycan expression; impairs alpha-dystroglycan glycosylation. 1 PublicationCorresponds to variant dbSNP:rs189360006EnsemblClinVar.1
Natural variantiVAR_075810111D → N in MDDGC9; does not affect dystroglycan expression; impairs alpha-dystroglycan glycosylation. 1 PublicationCorresponds to variant dbSNP:rs117209107EnsemblClinVar.1
Natural variantiVAR_065266192T → M in MDDGC9; results in impaired interaction with LARGE1 and incomplete DAG1 glycosylation. 1 PublicationCorresponds to variant dbSNP:rs193922955EnsemblClinVar.1
Natural variantiVAR_075811669C → F in MDDGA9. 1 PublicationCorresponds to variant dbSNP:rs797045023EnsemblClinVar.1

Sequence databases

Select the link destinations:

EMBL nucleotide sequence database

More...
EMBLi

GenBank nucleotide sequence database

More...
GenBanki

DNA Data Bank of Japan; a nucleotide sequence database

More...
DDBJi
Links Updated
L19711 mRNA Translation: AAA81779.1
AK291692 mRNA Translation: BAF84381.1
AC104452 Genomic DNA No translation available.
CH471055 Genomic DNA Translation: EAW64989.1
BC012740 mRNA Translation: AAH12740.1
BC014616 mRNA Translation: AAH14616.1

The Consensus CDS (CCDS) project

More...
CCDSi
CCDS2799.1

Protein sequence database of the Protein Information Resource

More...
PIRi
I54343

NCBI Reference Sequences

More...
RefSeqi
NP_001159400.2, NM_001165928.3
NP_001171105.1, NM_001177634.2
NP_001171106.1, NM_001177635.2
NP_001171107.1, NM_001177636.2
NP_001171108.1, NM_001177637.2
NP_001171109.1, NM_001177638.2
NP_001171110.1, NM_001177639.2
NP_001171111.1, NM_001177640.2
NP_001171112.1, NM_001177641.2
NP_001171113.1, NM_001177642.2
NP_001171114.1, NM_001177643.2
NP_001171115.1, NM_001177644.2
NP_004384.4, NM_004393.5

Genome annotation databases

Ensembl eukaryotic genome annotation project

More...
Ensembli
ENST00000308775; ENSP00000312435; ENSG00000173402
ENST00000515359; ENSP00000440705; ENSG00000173402
ENST00000538711; ENSP00000438421; ENSG00000173402
ENST00000539901; ENSP00000439334; ENSG00000173402
ENST00000541308; ENSP00000440590; ENSG00000173402
ENST00000545947; ENSP00000442600; ENSG00000173402

Database of genes from NCBI RefSeq genomes

More...
GeneIDi
1605

KEGG: Kyoto Encyclopedia of Genes and Genomes

More...
KEGGi
hsa:1605

UCSC genome browser

More...
UCSCi
uc003cxc.5 human

Keywords - Coding sequence diversityi

Polymorphism

<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

<p>This subsection of the <a href="http://www.uniprot.org/manual/cross_references_section">Cross-references</a> section provides links to various web resources that are relevant for a specific protein.<p><a href='/help/web_resource' target='_top'>More...</a></p>Web resourcesi

Wikipedia

Dystroglycan entry

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
L19711 mRNA Translation: AAA81779.1
AK291692 mRNA Translation: BAF84381.1
AC104452 Genomic DNA No translation available.
CH471055 Genomic DNA Translation: EAW64989.1
BC012740 mRNA Translation: AAH12740.1
BC014616 mRNA Translation: AAH14616.1
CCDSiCCDS2799.1
PIRiI54343
RefSeqiNP_001159400.2, NM_001165928.3
NP_001171105.1, NM_001177634.2
NP_001171106.1, NM_001177635.2
NP_001171107.1, NM_001177636.2
NP_001171108.1, NM_001177637.2
NP_001171109.1, NM_001177638.2
NP_001171110.1, NM_001177639.2
NP_001171111.1, NM_001177640.2
NP_001171112.1, NM_001177641.2
NP_001171113.1, NM_001177642.2
NP_001171114.1, NM_001177643.2
NP_001171115.1, NM_001177644.2
NP_004384.4, NM_004393.5

3D structure databases

Select the link destinations:

Protein Data Bank Europe

More...
PDBei

Protein Data Bank RCSB

More...
RCSB PDBi

Protein Data Bank Japan

More...
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1EG4X-ray2.00P881-895[»]
2MK7NMR-A419-427[»]
5GGPX-ray1.60C/D316-325[»]
5LLKX-ray1.80A52-315[»]
SMRiQ14118
ModBaseiSearch...
PDBe-KBiSearch...

Protein-protein interaction databases

BioGridi107975, 67 interactors
CORUMiQ14118
DIPiDIP-40928N
IntActiQ14118, 64 interactors
MINTiQ14118
STRINGi9606.ENSP00000442600

Chemistry databases

ChEMBLiCHEMBL3714399

Protein family/group databases

MEROPSiS72.001
TCDBi9.B.277.1.1 the dystroglycan (dg) family

PTM databases

GlyConnecti715
iPTMnetiQ14118
PhosphoSitePlusiQ14118
SwissPalmiQ14118
UniCarbKBiQ14118

Polymorphism and mutation databases

BioMutaiDAG1
DMDMi229462879

Proteomic databases

EPDiQ14118
jPOSTiQ14118
MassIVEiQ14118
MaxQBiQ14118
PaxDbiQ14118
PeptideAtlasiQ14118
PRIDEiQ14118
ProteomicsDBi59825
TopDownProteomicsiQ14118

Protocols and materials databases

The DNASU plasmid repository

More...
DNASUi
1605

Genome annotation databases

EnsembliENST00000308775; ENSP00000312435; ENSG00000173402
ENST00000515359; ENSP00000440705; ENSG00000173402
ENST00000538711; ENSP00000438421; ENSG00000173402
ENST00000539901; ENSP00000439334; ENSG00000173402
ENST00000541308; ENSP00000440590; ENSG00000173402
ENST00000545947; ENSP00000442600; ENSG00000173402
GeneIDi1605
KEGGihsa:1605
UCSCiuc003cxc.5 human

Organism-specific databases

Comparative Toxicogenomics Database

More...
CTDi
1605
DisGeNETi1605

GeneCards: human genes, protein and diseases

More...
GeneCardsi
DAG1
HGNCiHGNC:2666 DAG1
HPAiCAB001960
CAB016353
MalaCardsiDAG1
MIMi128239 gene
613818 phenotype
616538 phenotype
neXtProtiNX_Q14118
OpenTargetsiENSG00000173402
Orphaneti280333 Autosomal recessive limb-girdle muscular dystrophy type 2P
370997 Muscle-eye-brain disease with bilateral multicystic leucodystrophy
899 Walker-Warburg syndrome
PharmGKBiPA27138

GenAtlas: human gene database

More...
GenAtlasi
Search...

Phylogenomic databases

eggNOGiKOG3781 Eukaryota
ENOG410XQTU LUCA
GeneTreeiENSGT00390000008429
HOGENOMiHOG000072580
InParanoidiQ14118
KOiK06265
OMAiYDKEDTT
OrthoDBi156878at2759
PhylomeDBiQ14118
TreeFamiTF328370

Enzyme and pathway databases

ReactomeiR-HSA-3000171 Non-integrin membrane-ECM interactions
R-HSA-3000178 ECM proteoglycans
R-HSA-5083628 Defective POMGNT1 causes MDDGA3, MDDGB3 and MDDGC3
R-HSA-5083629 Defective POMT2 causes MDDGA2, MDDGB2 and MDDGC2
R-HSA-5083633 Defective POMT1 causes MDDGA1, MDDGB1 and MDDGC1
R-HSA-5173105 O-linked glycosylation
R-HSA-9010553 Regulation of expression of SLITs and ROBOs
SIGNORiQ14118

Miscellaneous databases

ChiTaRS: a database of human, mouse and fruit fly chimeric transcripts and RNA-sequencing data

More...
ChiTaRSi
DAG1 human
EvolutionaryTraceiQ14118

The Gene Wiki collection of pages on human genes and proteins

More...
GeneWikii
Dystroglycan

Database of phenotypes from RNA interference screens in Drosophila and Homo sapiens

More...
GenomeRNAii
1605
PharosiQ14118

Protein Ontology

More...
PROi
PR:Q14118

The Stanford Online Universal Resource for Clones and ESTs

More...
SOURCEi
Search...

Gene expression databases

BgeeiENSG00000173402 Expressed in 246 organ(s), highest expression level in olfactory bulb
ExpressionAtlasiQ14118 baseline and differential
GenevisibleiQ14118 HS

Family and domain databases

Gene3Di2.60.40.10, 2 hits
3.30.70.1040, 1 hit
InterProiView protein in InterPro
IPR027468 Alpha-dystroglycan_domain_2
IPR041631 Alpha_DG1_N2
IPR006644 Cadg
IPR015919 Cadherin-like_sf
IPR008465 DAG1_C
IPR013783 Ig-like_fold
IPR030398 SEA_DG_dom
PfamiView protein in Pfam
PF18424 a_DG1_N2, 1 hit
PF05454 DAG1, 1 hit
SMARTiView protein in SMART
SM00736 CADG, 2 hits
SUPFAMiSSF111006 SSF111006, 1 hit
SSF49313 SSF49313, 2 hits
PROSITEiView protein in PROSITE
PS51699 SEA_DG, 1 hit

ProtoNet; Automatic hierarchical classification of proteins

More...
ProtoNeti
Search...

MobiDB: a database of protein disorder and mobility annotations

More...
MobiDBi
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 nameiDAG1_HUMAN
<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: Q14118
Secondary accession number(s): A8K6M7, Q969J9
<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: May 5, 2009
Last modified: October 16, 2019
This is version 191 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
DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

<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

3D-structure, Complete proteome, Reference proteome

Documents

  1. Human chromosome 3
    Human chromosome 3: entries, gene names and cross-references to MIM
  2. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  3. Human polymorphisms and disease mutations
    Index of human polymorphisms and disease mutations
  4. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  5. Human entries with polymorphisms or disease mutations
    List of human entries with polymorphisms or disease mutations
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