DAG1 | ENSG00000173402 | NCBI 1605

Details for: DAG1

Gene ID: 1605

Symbol: DAG1

Ensembl ID: ENSG00000173402

Description: dystroglycan 1

Associated with

Defective pomgnt1 causes mddga3, mddgb3 and mddgc3
(R-HSA-5083628)
Defective pomt1 causes mddga1, mddgb1 and mddgc1
(R-HSA-5083633)
Defective pomt2 causes mddga2, mddgb2 and mddgc2
(R-HSA-5083629)
Developmental biology
(R-HSA-1266738)
Disease
(R-HSA-1643685)
Diseases associated with o-glycosylation of proteins
(R-HSA-3906995)
Diseases of glycosylation
(R-HSA-3781865)
Diseases of metabolism
(R-HSA-5668914)
Ecm proteoglycans
(R-HSA-3000178)
Egr2 and sox10-mediated initiation of schwann cell myelination
(R-HSA-9619665)
Extracellular matrix organization
(R-HSA-1474244)
Metabolism of proteins
(R-HSA-392499)
Nervous system development
(R-HSA-9675108)
Non-integrin membrane-ecm interactions
(R-HSA-3000171)
O-linked glycosylation
(R-HSA-5173105)
Post-translational protein modification
(R-HSA-597592)
Regulation of expression of slits and robos
(R-HSA-9010553)
Signaling by robo receptors
(R-HSA-376176)
Actin binding
(GO:0003779)
Adherens junction
(GO:0005912)
Alpha-actinin binding
(GO:0051393)
Angiogenesis involved in wound healing
(GO:0060055)
Axon guidance
(GO:0007411)
Axon regeneration
(GO:0031103)
Basement membrane
(GO:0005604)
Basement membrane organization
(GO:0071711)
Basolateral plasma membrane
(GO:0016323)
Branching involved in salivary gland morphogenesis
(GO:0060445)
Calcium-dependent cell-matrix adhesion
(GO:0016340)
Calcium ion binding
(GO:0005509)
Cellular response to cholesterol
(GO:0071397)
Cellular response to mechanical stimulus
(GO:0071260)
Commissural neuron axon guidance
(GO:0071679)
Costamere
(GO:0043034)
Cytoplasm
(GO:0005737)
Cytoskeleton
(GO:0005856)
Cytosol
(GO:0005829)
Dystroglycan binding
(GO:0002162)
Dystroglycan complex
(GO:0016011)
Dystrophin-associated glycoprotein complex
(GO:0016010)
Endoplasmic reticulum lumen
(GO:0005788)
Epithelial tube branching involved in lung morphogenesis
(GO:0060441)
External side of plasma membrane
(GO:0009897)
Extracellular region
(GO:0005576)
Extracellular space
(GO:0005615)
Filopodium
(GO:0030175)
Focal adhesion
(GO:0005925)
Golgi lumen
(GO:0005796)
Heart morphogenesis
(GO:0003007)
Lamellipodium
(GO:0030027)
Laminin-1 binding
(GO:0043237)
Laminin binding
(GO:0043236)
Membrane
(GO:0016020)
Membrane protein ectodomain proteolysis
(GO:0006509)
Microtubule anchoring
(GO:0034453)
Morphogenesis of an epithelial sheet
(GO:0002011)
Morphogenesis of an epithelium
(GO:0002009)
Muscle attachment
(GO:0016203)
Myelination in peripheral nervous system
(GO:0022011)
Negative regulation of cell migration
(GO:0030336)
Negative regulation of mapk cascade
(GO:0043409)
Negative regulation of phosphatidylinositol 3-kinase/protein kinase b signal transduction
(GO:0051898)
Nerve development
(GO:0021675)
Nerve maturation
(GO:0021682)
Node of ranvier
(GO:0033268)
Nuclear periphery
(GO:0034399)
Nucleoplasm
(GO:0005654)
Plasma membrane
(GO:0005886)
Positive regulation of basement membrane assembly involved in embryonic body morphogenesis
(GO:1904261)
Positive regulation of cell-matrix adhesion
(GO:0001954)
Positive regulation of myelination
(GO:0031643)
Positive regulation of oligodendrocyte differentiation
(GO:0048714)
Protein-containing complex binding
(GO:0044877)
Protein binding
(GO:0005515)
Protein transport
(GO:0015031)
Regulation of embryonic cell shape
(GO:0016476)
Regulation of epithelial to mesenchymal transition
(GO:0010717)
Regulation of gastrulation
(GO:0010470)
Regulation of neurotransmitter receptor localization to postsynaptic specialization membrane
(GO:0098696)
Regulation of synapse organization
(GO:0050807)
Regulation of synaptic plasticity
(GO:0048167)
Response to denervation involved in regulation of muscle adaptation
(GO:0014894)
Response to muscle activity
(GO:0014850)
Response to peptide hormone
(GO:0043434)
Retrograde trans-synaptic signaling by trans-synaptic protein complex
(GO:0098942)
Sarcolemma
(GO:0042383)
Sh2 domain binding
(GO:0042169)
Skeletal muscle tissue regeneration
(GO:0043403)
Structural constituent of muscle
(GO:0008307)
Symbiont entry into host cell
(GO:0046718)
Tubulin binding
(GO:0015631)
Vinculin binding
(GO:0017166)
Virus receptor activity
(GO:0001618)

Cells (max top 100)

(Cell Significance Index and respective Thresholds are uniquely calculated using our advanced thresholding algorithms to reveal cell-specific gene markers)

Cell Name: polychromatophilic erythroblast (CL0000550)
Fold Change: 192.0985
Cell Significance Index: -29.8800
Cell Name: hematopoietic oligopotent progenitor cell (CL0002032)
Fold Change: 121.8246
Cell Significance Index: -30.9000
Cell Name: smooth muscle fiber of ileum (CL1000278)
Fold Change: 66.4870
Cell Significance Index: -31.3900
Cell Name: mucosal type mast cell (CL0000485)
Fold Change: 62.4728
Cell Significance Index: -25.3800
Cell Name: ileal goblet cell (CL1000326)
Fold Change: 46.9433
Cell Significance Index: -31.5000
Cell Name: ciliated cell of the bronchus (CL0002332)
Fold Change: 26.5988
Cell Significance Index: -25.4000
Cell Name: orthochromatic erythroblast (CL0000552)
Fold Change: 24.8833
Cell Significance Index: -30.6800
Cell Name: CD8-alpha-beta-positive, alpha-beta intraepithelial T cell (CL0000796)
Fold Change: 11.2511
Cell Significance Index: -30.1400
Cell Name: stromal cell of bone marrow (CL0010001)
Fold Change: 7.8484
Cell Significance Index: -30.9700
Cell Name: CD8-positive, alpha-beta regulatory T cell (CL0000795)
Fold Change: 6.4823
Cell Significance Index: -19.9100
Cell Name: epidermal Langerhans cell (CL0002457)
Fold Change: 6.2735
Cell Significance Index: -13.7300
Cell Name: colon goblet cell (CL0009039)
Fold Change: 4.1648
Cell Significance Index: 412.0000
Cell Name: skeletal muscle fiber (CL0008002)
Fold Change: 3.8693
Cell Significance Index: 99.4600
Cell Name: placental villous trophoblast (CL2000060)
Fold Change: 2.9339
Cell Significance Index: 78.3400
Cell Name: skeletal muscle satellite stem cell (CL0008011)
Fold Change: 2.0355
Cell Significance Index: 21.2500
Cell Name: type I muscle cell (CL0002211)
Fold Change: 1.6787
Cell Significance Index: 40.9600
Cell Name: gut absorptive cell (CL0000677)
Fold Change: 1.4335
Cell Significance Index: 86.0600
Cell Name: intestinal crypt stem cell of colon (CL0009043)
Fold Change: 1.3935
Cell Significance Index: 151.5800
Cell Name: Sertoli cell (CL0000216)
Fold Change: 1.0430
Cell Significance Index: 14.6300
Cell Name: lung endothelial cell (CL1001567)
Fold Change: 0.9732
Cell Significance Index: 50.7000
Cell Name: cardiac muscle myoblast (CL0000513)
Fold Change: 0.9122
Cell Significance Index: 70.0000
Cell Name: granulosa cell (CL0000501)
Fold Change: 0.9074
Cell Significance Index: 23.8600
Cell Name: L2/3-6 intratelencephalic projecting glutamatergic neuron (CL4023040)
Fold Change: 0.8746
Cell Significance Index: 175.4500
Cell Name: neoplastic cell (CL0001063)
Fold Change: 0.7623
Cell Significance Index: 151.2800
Cell Name: intermediate cell of urothelium (CL4030055)
Fold Change: 0.7418
Cell Significance Index: 133.7200
Cell Name: epithelial cell of small intestine (CL0002254)
Fold Change: 0.7167
Cell Significance Index: 116.5600
Cell Name: basal cell of urothelium (CL1000486)
Fold Change: 0.7098
Cell Significance Index: 87.2800
Cell Name: tuft cell of colon (CL0009041)
Fold Change: 0.6942
Cell Significance Index: 626.8400
Cell Name: bladder urothelial cell (CL1001428)
Fold Change: 0.6626
Cell Significance Index: 34.4200
Cell Name: umbrella cell of urothelium (CL4030056)
Fold Change: 0.5804
Cell Significance Index: 5.3500
Cell Name: enterocyte of epithelium of small intestine (CL1000334)
Fold Change: 0.5631
Cell Significance Index: 16.2300
Cell Name: obsolete caudal ganglionic eminence derived GABAergic cortical interneuron (CL4023070)
Fold Change: 0.5305
Cell Significance Index: 190.2800
Cell Name: pancreatic acinar cell (CL0002064)
Fold Change: 0.5298
Cell Significance Index: 90.4700
Cell Name: cell in vitro (CL0001034)
Fold Change: 0.5188
Cell Significance Index: 283.3500
Cell Name: retinal progenitor cell (CL0002672)
Fold Change: 0.5005
Cell Significance Index: 28.0900
Cell Name: GABAergic interneuron (CL0011005)
Fold Change: 0.4911
Cell Significance Index: 339.6700
Cell Name: acinar cell of salivary gland (CL0002623)
Fold Change: 0.4180
Cell Significance Index: 19.4900
Cell Name: hair follicular keratinocyte (CL2000092)
Fold Change: 0.3651
Cell Significance Index: 161.4000
Cell Name: enteroendocrine cell of colon (CL0009042)
Fold Change: 0.3548
Cell Significance Index: 67.5200
Cell Name: enteroendocrine cell of small intestine (CL0009006)
Fold Change: 0.3320
Cell Significance Index: 8.3000
Cell Name: type II muscle cell (CL0002212)
Fold Change: 0.2842
Cell Significance Index: 4.5900
Cell Name: enterocyte of epithelium of large intestine (CL0002071)
Fold Change: 0.2771
Cell Significance Index: 12.5600
Cell Name: sebum secreting cell (CL0000317)
Fold Change: 0.2517
Cell Significance Index: 17.8000
Cell Name: stromal cell of ovary (CL0002132)
Fold Change: 0.2236
Cell Significance Index: 30.7000
Cell Name: leptomeningeal cell (CL0000708)
Fold Change: 0.1712
Cell Significance Index: 3.6600
Cell Name: small intestine goblet cell (CL1000495)
Fold Change: 0.1460
Cell Significance Index: 5.1300
Cell Name: luminal adaptive secretory precursor cell of mammary gland (CL4033057)
Fold Change: 0.1117
Cell Significance Index: 5.2500
Cell Name: odontoblast (CL0000060)
Fold Change: 0.1034
Cell Significance Index: 13.2500
Cell Name: cardiac muscle cell (CL0000746)
Fold Change: 0.0942
Cell Significance Index: 1.3900
Cell Name: microcirculation associated smooth muscle cell (CL0008035)
Fold Change: 0.0560
Cell Significance Index: 0.4700
Cell Name: basal epithelial cell of tracheobronchial tree (CL0002329)
Fold Change: 0.0444
Cell Significance Index: 1.2400
Cell Name: lactocyte (CL0002325)
Fold Change: 0.0336
Cell Significance Index: 4.3400
Cell Name: extravillous trophoblast (CL0008036)
Fold Change: 0.0209
Cell Significance Index: 0.1300
Cell Name: pigmented epithelial cell (CL0000529)
Fold Change: 0.0142
Cell Significance Index: 26.8300
Cell Name: kidney loop of Henle cortical thick ascending limb epithelial cell (CL1001109)
Fold Change: 0.0115
Cell Significance Index: 8.4400
Cell Name: pancreatic A cell (CL0000171)
Fold Change: -0.0055
Cell Significance Index: -4.0700
Cell Name: anterior lens cell (CL0002223)
Fold Change: -0.0075
Cell Significance Index: -13.7700
Cell Name: pancreatic PP cell (CL0002275)
Fold Change: -0.0081
Cell Significance Index: -5.0400
Cell Name: lens epithelial cell (CL0002224)
Fold Change: -0.0086
Cell Significance Index: -13.2700
Cell Name: ciliary muscle cell (CL1000443)
Fold Change: -0.0095
Cell Significance Index: -4.2900
Cell Name: non-pigmented ciliary epithelial cell (CL0002304)
Fold Change: -0.0124
Cell Significance Index: -7.8600
Cell Name: secondary lens fiber (CL0002225)
Fold Change: -0.0151
Cell Significance Index: -20.5300
Cell Name: pulmonary alveolar epithelial cell (CL0000322)
Fold Change: -0.0183
Cell Significance Index: -13.8800
Cell Name: type B pancreatic cell (CL0000169)
Fold Change: -0.0295
Cell Significance Index: -16.6400
Cell Name: intestinal crypt stem cell of small intestine (CL0009017)
Fold Change: -0.0455
Cell Significance Index: -0.9700
Cell Name: pancreatic D cell (CL0000173)
Fold Change: -0.0703
Cell Significance Index: -14.8100
Cell Name: progenitor cell of mammary luminal epithelium (CL0009116)
Fold Change: -0.0876
Cell Significance Index: -6.5300
Cell Name: dopaminergic neuron (CL0000700)
Fold Change: -0.0900
Cell Significance Index: -25.9000
Cell Name: abnormal cell (CL0001061)
Fold Change: -0.0974
Cell Significance Index: -9.9500
Cell Name: pancreatic endocrine cell (CL0008024)
Fold Change: -0.1060
Cell Significance Index: -12.1000
Cell Name: pancreatic ductal cell (CL0002079)
Fold Change: -0.1246
Cell Significance Index: -14.2700
Cell Name: epithelial cell of stomach (CL0002178)
Fold Change: -0.1437
Cell Significance Index: -16.7500
Cell Name: pigmented ciliary epithelial cell (CL0002303)
Fold Change: -0.1447
Cell Significance Index: -21.0400
Cell Name: forebrain neuroblast (CL1000042)
Fold Change: -0.1547
Cell Significance Index: -9.5100
Cell Name: hippocampal granule cell (CL0001033)
Fold Change: -0.1649
Cell Significance Index: -11.0900
Cell Name: transit amplifying cell of colon (CL0009011)
Fold Change: -0.1826
Cell Significance Index: -5.8500
Cell Name: tonsil germinal center B cell (CL2000006)
Fold Change: -0.1896
Cell Significance Index: -22.3600
Cell Name: eye photoreceptor cell (CL0000287)
Fold Change: -0.2098
Cell Significance Index: -13.2200
Cell Name: basal cell of prostate epithelium (CL0002341)
Fold Change: -0.2120
Cell Significance Index: -5.7700
Cell Name: paneth cell of epithelium of small intestine (CL1000343)
Fold Change: -0.2151
Cell Significance Index: -4.6600
Cell Name: mesonephric nephron tubule epithelial cell (CL1000022)
Fold Change: -0.2283
Cell Significance Index: -7.9400
Cell Name: indirect pathway medium spiny neuron (CL4023029)
Fold Change: -0.2478
Cell Significance Index: -10.9600
Cell Name: smooth muscle cell of sphincter of pupil (CL0002243)
Fold Change: -0.2635
Cell Significance Index: -27.4400
Cell Name: cerebellar granule cell (CL0001031)
Fold Change: -0.2690
Cell Significance Index: -4.6100
Cell Name: cortical cell of adrenal gland (CL0002097)
Fold Change: -0.2853
Cell Significance Index: -7.6500
Cell Name: direct pathway medium spiny neuron (CL4023026)
Fold Change: -0.3058
Cell Significance Index: -11.5800
Cell Name: peg cell (CL4033014)
Fold Change: -0.3268
Cell Significance Index: -7.5500
Cell Name: kidney loop of Henle descending limb epithelial cell (CL1001021)
Fold Change: -0.3280
Cell Significance Index: -25.9800
Cell Name: early pro-B cell (CL0002046)
Fold Change: -0.3413
Cell Significance Index: -22.0200
Cell Name: intestinal tuft cell (CL0019032)
Fold Change: -0.4167
Cell Significance Index: -25.5500
Cell Name: conjunctival epithelial cell (CL1000432)
Fold Change: -0.4170
Cell Significance Index: -5.6900
Cell Name: centrilobular region hepatocyte (CL0019029)
Fold Change: -0.4343
Cell Significance Index: -7.3200
Cell Name: proerythroblast (CL0000547)
Fold Change: -0.4501
Cell Significance Index: -6.4500
Cell Name: glycinergic neuron (CL1001509)
Fold Change: -0.4697
Cell Significance Index: -24.6600
Cell Name: preadipocyte (CL0002334)
Fold Change: -0.4704
Cell Significance Index: -9.1800
Cell Name: Purkinje cell (CL0000121)
Fold Change: -0.4722
Cell Significance Index: -10.3400
Cell Name: mesenchymal cell (CL0008019)
Fold Change: -0.4877
Cell Significance Index: -8.1600
Cell Name: kidney epithelial cell (CL0002518)
Fold Change: -0.4984
Cell Significance Index: -14.6800
Cell Name: BEST4+ enteroycte (CL4030026)
Fold Change: -0.5030
Cell Significance Index: -7.5800
Cell Name: kidney cell (CL1000497)
Fold Change: -0.6012
Cell Significance Index: -4.8000

Cell ID: Standard Cell Ontology term used for mapping and comparing cells across experiments. Ensures consistency in analyzing cellular functions across tissues.
Fold Change: Represents the ratio of the current Cell Significance Index to the Cell Significance Index Threshold, indicating how much the gene expression has changed compared to a baseline.
Cell Significance Index: Reflects how strongly a gene is expressed in this specific cell.

**Key Characteristics:** 1. **Structural Integrity:** DAG1 is a transmembrane protein composed of two subunits: alpha-dystroglycan (α-DG) and beta-dystroglycan (β-DG). The α-DG subunit is the ligand for laminin-211, a key component of the extracellular matrix. 2. **Cellular Adhesion:** DAG1 mediates adhesion between muscle fibers and the extracellular matrix, ensuring muscle stability and preventing muscle damage. 3. **Muscle Function:** DAG1 is essential for muscle contraction, relaxation, and signaling pathways that regulate muscle growth and differentiation. 4. **Signal Transduction:** DAG1 interacts with various signaling molecules, including integrins, laminins, and growth factors, to regulate cell migration, proliferation, and differentiation. **Pathways and Functions:** 1. **Muscle Signaling:** DAG1 regulates muscle function through interaction with the dystrophin-associated glycoprotein complex (DAG), which transduces signals from the extracellular matrix to the cytoskeleton. 2. **Cell Migration:** DAG1 mediates adhesion and migration of muscle cells, including satellite cells, during muscle development and repair. 3. **Synaptic Plasticity:** DAG1 regulates synaptic plasticity by interacting with neurotransmitter receptors and modulating the activity of signaling molecules, such as MAPK and PI3K. 4. **Glycosylation:** DAG1 is a substrate for O-glycosylation, a post-translational modification that regulates protein function and cellular signaling. **Clinical Significance:** Dysregulation of DAG1 has been implicated in various diseases, including: 1. **Muscular Dystrophy:** Mutations in the DAG1 gene have been associated with muscular dystrophy, a group of genetic disorders characterized by progressive muscle weakness and degeneration. 2. **Cancer:** Alterations in DAG1 expression and function have been linked to cancer progression, metastasis, and resistance to therapy. 3. **Neurological Disorders:** DAG1 dysregulation has been implicated in neurological disorders, such as epilepsy, Parkinson's disease, and amyotrophic lateral sclerosis (ALS). In conclusion, DAG1 is a critical gene that plays a central role in maintaining muscle integrity and cellular adhesion. Its dysregulation has far-reaching consequences for muscle function, cell migration, and synaptic plasticity, making it a promising target for the development of novel therapeutic strategies for various diseases.

Disclaimer: This summary is generated by an AI language model and may contain inaccuracies or hallucinations. However, it is cross-referenced with curated gene expression data from major biological sources. Please verify the information before use.

Alpha-dystroglycan

Genular Protein ID: 1478942946

Symbol: DAG1_HUMAN

Name: Alpha-dystroglycan

UniProtKB Accession Codes:

Q14118 A8K6M7 Q969J9

Database IDs:

Citations:

PubMed ID: 8268918

Title: Human dystroglycan: skeletal muscle cDNA, genomic structure, origin of tissue specific isoforms and chromosomal localization.

PubMed ID: 8268918

DOI: 10.1093/hmg/2.10.1651

PubMed ID: 14702039

Title: Complete sequencing and characterization of 21,243 full-length human cDNAs.

PubMed ID: 14702039

DOI: 10.1038/ng1285

PubMed ID: 16641997

Title: The DNA sequence, annotation and analysis of human chromosome 3.

PubMed ID: 16641997

DOI: 10.1038/nature04728

PubMed ID: 15489334

Title: The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC).

PubMed ID: 15489334

DOI: 10.1101/gr.2596504

PubMed ID: 7592992

Title: Identification and characterization of the dystrophin anchoring site on beta-dystroglycan.

PubMed ID: 7592992

DOI: 10.1074/jbc.270.45.27305

PubMed ID: 9851927

Title: Role of alpha-dystroglycan as a Schwann cell receptor for Mycobacterium leprae.

PubMed ID: 9851927

DOI: 10.1126/science.282.5396.2076

PubMed ID: 10767429

Title: Contribution of the different modules in the utrophin carboxy-terminal region to the formation and regulation of the DAP complex.

PubMed ID: 10767429

DOI: 10.1016/s0014-5793(00)01400-9

PubMed ID: 10988290

Title: Caveolin-3 directly interacts with the C-terminal tail of beta -dystroglycan. Identification of a central WW-like domain within caveolin family members.

PubMed ID: 10988290

DOI: 10.1074/jbc.m005321200

PubMed ID: 10769203

Title: Adhesion-dependent tyrosine phosphorylation of (beta)-dystroglycan regulates its interaction with utrophin.

PubMed ID: 10769203

DOI: 10.1242/jcs.113.10.1717

PubMed ID: 11724572

Title: Tyrosine phosphorylation of beta-dystroglycan at its WW domain binding motif, PPxY, recruits SH2 domain containing proteins.

PubMed ID: 11724572

DOI: 10.1021/bi011247r

PubMed ID: 11495720

Title: The interaction of dystrophin with beta-dystroglycan is regulated by tyrosine phosphorylation.

PubMed ID: 11495720

DOI: 10.1016/s0898-6568(01)00188-7

PubMed ID: 12140558

Title: Post-translational disruption of dystroglycan-ligand interactions in congenital muscular dystrophies.

PubMed ID: 12140558

DOI: 10.1038/nature00837

PubMed ID: 12795607

Title: Localization of phospho-beta-dystroglycan (pY892) to an intracellular vesicular compartment in cultured cells and skeletal muscle fibers in vivo.

PubMed ID: 12795607

DOI: 10.1021/bi0271289

PubMed ID: 12592373

Title: hAG-2 and hAG-3, human homologues of genes involved in differentiation, are associated with oestrogen receptor-positive breast tumours and interact with metastasis gene C4.4a and dystroglycan.

PubMed ID: 12592373

DOI: 10.1038/sj.bjc.6600740

PubMed ID: 15175026

Title: Dystroglycan in skin and cutaneous cells: beta-subunit is shed from the cell surface.

PubMed ID: 15175026

DOI: 10.1111/j.0022-202x.2004.22605.x

PubMed ID: 16254364

Title: O Mannosylation of alpha-dystroglycan is essential for lymphocytic choriomeningitis virus receptor function.

PubMed ID: 16254364

DOI: 10.1128/jvi.79.22.14297-14308.2005

PubMed ID: 17212656

Title: Cys669-Cys713 disulfide bridge formation is a key to dystroglycan cleavage and subunit association.

PubMed ID: 17212656

DOI: 10.1111/j.1365-2443.2006.01033.x

PubMed ID: 17360738

Title: Old World and clade C New World arenaviruses mimic the molecular mechanism of receptor recognition used by alpha-dystroglycan's host-derived ligands.

PubMed ID: 17360738

DOI: 10.1128/jvi.02574-06

PubMed ID: 17905726

Title: SEA domain proteolysis determines the functional composition of dystroglycan.

PubMed ID: 17905726

DOI: 10.1096/fj.07-8354com

PubMed ID: 18764929

Title: Nuclear translocation of beta-dystroglycan reveals a distinctive trafficking pattern of autoproteolyzed mucins.

PubMed ID: 18764929

DOI: 10.1111/j.1600-0854.2008.00822.x

PubMed ID: 19946898

Title: Enzymatic processing of beta-dystroglycan recombinant ectodomain by MMP-9: identification of the main cleavage site.

PubMed ID: 19946898

DOI: 10.1002/iub.273

PubMed ID: 19838169

Title: Enrichment of glycopeptides for glycan structure and attachment site identification.

PubMed ID: 19838169

DOI: 10.1038/nmeth.1392

PubMed ID: 19324387

Title: Receptor binding and cell entry of Old World arenaviruses reveal novel aspects of virus-host interaction.

PubMed ID: 19324387

DOI: 10.1016/j.virol.2009.02.042

PubMed ID: 20507882

Title: Characterization of site-specific O-glycan structures within the mucin-like domain of {alpha}-dystroglycan from human skeletal muscle.

PubMed ID: 20507882

DOI: 10.1093/glycob/cwq082

PubMed ID: 20512930

Title: Characterization of an Importin alpha/beta-recognized nuclear localization signal in beta-dystroglycan.

PubMed ID: 20512930

DOI: 10.1002/jcb.22581

PubMed ID: 20044576

Title: O-mannosyl phosphorylation of alpha-dystroglycan is required for laminin binding.

PubMed ID: 20044576

DOI: 10.1126/science.1180512

PubMed ID: 21269460

Title: Initial characterization of the human central proteome.

PubMed ID: 21269460

DOI: 10.1186/1752-0509-5-17

PubMed ID: 21987822

Title: Like-acetylglucosaminyltransferase (LARGE)-dependent modification of dystroglycan at Thr-317/319 is required for laminin binding and arenavirus infection.

PubMed ID: 21987822

DOI: 10.1073/pnas.1114836108

PubMed ID: 23723439

Title: HNK-1 sulfotransferase-dependent sulfation regulating laminin-binding glycans occurs in the post-phosphoryl moiety on alpha-dystroglycan.

PubMed ID: 23723439

DOI: 10.1093/glycob/cwt043

PubMed ID: 23186163

Title: Toward a comprehensive characterization of a human cancer cell phosphoproteome.

PubMed ID: 23186163

DOI: 10.1021/pr300630k

PubMed ID: 23234360

Title: LC-MS/MS characterization of O-glycosylation sites and glycan structures of human cerebrospinal fluid glycoproteins.

PubMed ID: 23234360

DOI: 10.1021/pr300963h

PubMed ID: 24256719

Title: AGO61-dependent GlcNAc modification primes the formation of functional glycans on alpha-dystroglycan.

PubMed ID: 24256719

DOI: 10.1038/srep03288

PubMed ID: 24275569

Title: An enzyme assisted RP-RPLC approach for in-depth analysis of human liver phosphoproteome.

PubMed ID: 24275569

DOI: 10.1016/j.jprot.2013.11.014

PubMed ID: 21388311

Title: A dystroglycan mutation associated with limb-girdle muscular dystrophy.

PubMed ID: 21388311

DOI: 10.1056/nejmoa1006939

PubMed ID: 24052401

Title: Homozygous dystroglycan mutation associated with a novel muscle-eye-brain disease-like phenotype with multicystic leucodystrophy.

PubMed ID: 24052401

DOI: 10.1007/s10048-013-0374-9

PubMed ID: 25503980

Title: DAG1 mutations associated with asymptomatic hyperCKemia and hypoglycosylation of alpha-dystroglycan.

PubMed ID: 25503980

DOI: 10.1212/wnl.0000000000001162

PubMed ID: 25934851

Title: Absence of alpha- and beta-dystroglycan is associated with Walker-Warburg syndrome.

PubMed ID: 25934851

DOI: 10.1212/wnl.0000000000001615

PubMed ID: 26848865

Title: CD93 and dystroglycan cooperation in human endothelial cell adhesion and migration adhesion and migration.

PubMed ID: 26848865

DOI: 10.18632/oncotarget.7136

PubMed ID: 10932245

Title: Structure of a WW domain containing fragment of dystrophin in complex with beta-dystroglycan.

PubMed ID: 10932245

DOI: 10.1038/77923

PubMed ID: 27493216

Title: Carbohydrate-binding domain of the POMGnT1 stem region modulates O-mannosylation sites of alpha-dystroglycan.

PubMed ID: 27493216

DOI: 10.1073/pnas.1525545113

PubMed ID: 28781947

Title: Structural flexibility of human alpha-dystroglycan.

PubMed ID: 28781947

DOI: 10.1002/2211-5463.12259

Sequence Information:

Length: 895
Mass: 97441
Checksum: 3AF6CBB0DCF91962
Sequence:

MRMSVGLSLL LPLSGRTFLL LLSVVMAQSH WPSEPSEAVR DWENQLEASM HSVLSDLHEA 
VPTVVGIPDG TAVVGRSFRV TIPTDLIASS GDIIKVSAAG KEALPSWLHW DSQSHTLEGL 
PLDTDKGVHY ISVSATRLGA NGSHIPQTSS VFSIEVYPED HSELQSVRTA SPDPGEVVSS 
ACAADEPVTV LTVILDADLT KMTPKQRIDL LHRMRSFSEV ELHNMKLVPV VNNRLFDMSA 
FMAGPGNAKK VVENGALLSW KLGCSLNQNS VPDIHGVEAP AREGAMSAQL GYPVVGWHIA 
NKKPPLPKRV RRQIHATPTP VTAIGPPTTA IQEPPSRIVP TPTSPAIAPP TETMAPPVRD 
PVPGKPTVTI RTRGAIIQTP TLGPIQPTRV SEAGTTVPGQ IRPTMTIPGY VEPTAVATPP 
TTTTKKPRVS TPKPATPSTD STTTTTRRPT KKPRTPRPVP RVTTKVSITR LETASPPTRI 
RTTTSGVPRG GEPNQRPELK NHIDRVDAWV GTYFEVKIPS DTFYDHEDTT TDKLKLTLKL 
REQQLVGEKS WVQFNSNSQL MYGLPDSSHV GKHEYFMHAT DKGGLSAVDA FEIHVHRRPQ 
GDRAPARFKA KFVGDPALVL NDIHKKIALV KKLAFAFGDR NCSTITLQNI TRGSIVVEWT 
NNTLPLEPCP KEQIAGLSRR IAEDDGKPRP AFSNALEPDF KATSITVTGS GSCRHLQFIP 
VVPPRRVPSE APPTEVPDRD PEKSSEDDVY LHTVIPAVVV AAILLIAGII AMICYRKKRK 
GKLTLEDQAT FIKKGVPIIF ADELDDSKPP PSSSMPLILQ EEKAPLPPPE YPNQSVPETT 
PLNQDTMGEY TPLRDEDPNA PPYQPPPPFT APMEGKGSRP KNMTPYRSPP PYVPP

Database document:

This is a preview of the gene's schema. Only a few entries are kept for 'singleCellExpressions,' 'mRNAExpressions,' and other large data arrays for visualization purposes. You can zoom in with the mouse wheel for a closer view, and the text will adjust automatically if necessary. For the full schema, download it here.

Details for: DAG1

Associated with

Cells (max top 100)

Other Information

Human dystroglycan: skeletal muscle cDNA, genomic structure, origin of tissue specific isoforms and chromosomal localization. PubMed ID: 8268918

Complete sequencing and characterization of 21,243 full-length human cDNAs. PubMed ID: 14702039

The DNA sequence, annotation and analysis of human chromosome 3. PubMed ID: 16641997

The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC). PubMed ID: 15489334

Identification and characterization of the dystrophin anchoring site on beta-dystroglycan. PubMed ID: 7592992

Role of alpha-dystroglycan as a Schwann cell receptor for Mycobacterium leprae. PubMed ID: 9851927

Contribution of the different modules in the utrophin carboxy-terminal region to the formation and regulation of the DAP complex. PubMed ID: 10767429

Caveolin-3 directly interacts with the C-terminal tail of beta -dystroglycan. Identification of a central WW-like domain within caveolin family members. PubMed ID: 10988290

Adhesion-dependent tyrosine phosphorylation of (beta)-dystroglycan regulates its interaction with utrophin. PubMed ID: 10769203

Tyrosine phosphorylation of beta-dystroglycan at its WW domain binding motif, PPxY, recruits SH2 domain containing proteins. PubMed ID: 11724572

The interaction of dystrophin with beta-dystroglycan is regulated by tyrosine phosphorylation. PubMed ID: 11495720

Post-translational disruption of dystroglycan-ligand interactions in congenital muscular dystrophies. PubMed ID: 12140558

Localization of phospho-beta-dystroglycan (pY892) to an intracellular vesicular compartment in cultured cells and skeletal muscle fibers in vivo. PubMed ID: 12795607

hAG-2 and hAG-3, human homologues of genes involved in differentiation, are associated with oestrogen receptor-positive breast tumours and interact with metastasis gene C4.4a and dystroglycan. PubMed ID: 12592373

Dystroglycan in skin and cutaneous cells: beta-subunit is shed from the cell surface. PubMed ID: 15175026

O Mannosylation of alpha-dystroglycan is essential for lymphocytic choriomeningitis virus receptor function. PubMed ID: 16254364

Cys669-Cys713 disulfide bridge formation is a key to dystroglycan cleavage and subunit association. PubMed ID: 17212656

Old World and clade C New World arenaviruses mimic the molecular mechanism of receptor recognition used by alpha-dystroglycan's host-derived ligands. PubMed ID: 17360738

SEA domain proteolysis determines the functional composition of dystroglycan. PubMed ID: 17905726

Nuclear translocation of beta-dystroglycan reveals a distinctive trafficking pattern of autoproteolyzed mucins. PubMed ID: 18764929

Enzymatic processing of beta-dystroglycan recombinant ectodomain by MMP-9: identification of the main cleavage site. PubMed ID: 19946898

Enrichment of glycopeptides for glycan structure and attachment site identification. PubMed ID: 19838169

Receptor binding and cell entry of Old World arenaviruses reveal novel aspects of virus-host interaction. PubMed ID: 19324387

Characterization of site-specific O-glycan structures within the mucin-like domain of {alpha}-dystroglycan from human skeletal muscle. PubMed ID: 20507882

Characterization of an Importin alpha/beta-recognized nuclear localization signal in beta-dystroglycan. PubMed ID: 20512930

O-mannosyl phosphorylation of alpha-dystroglycan is required for laminin binding. PubMed ID: 20044576

Initial characterization of the human central proteome. PubMed ID: 21269460

Like-acetylglucosaminyltransferase (LARGE)-dependent modification of dystroglycan at Thr-317/319 is required for laminin binding and arenavirus infection. PubMed ID: 21987822

HNK-1 sulfotransferase-dependent sulfation regulating laminin-binding glycans occurs in the post-phosphoryl moiety on alpha-dystroglycan. PubMed ID: 23723439

Toward a comprehensive characterization of a human cancer cell phosphoproteome. PubMed ID: 23186163

LC-MS/MS characterization of O-glycosylation sites and glycan structures of human cerebrospinal fluid glycoproteins. PubMed ID: 23234360

AGO61-dependent GlcNAc modification primes the formation of functional glycans on alpha-dystroglycan. PubMed ID: 24256719

An enzyme assisted RP-RPLC approach for in-depth analysis of human liver phosphoproteome. PubMed ID: 24275569

A dystroglycan mutation associated with limb-girdle muscular dystrophy. PubMed ID: 21388311

Homozygous dystroglycan mutation associated with a novel muscle-eye-brain disease-like phenotype with multicystic leucodystrophy. PubMed ID: 24052401

DAG1 mutations associated with asymptomatic hyperCKemia and hypoglycosylation of alpha-dystroglycan. PubMed ID: 25503980

Absence of alpha- and beta-dystroglycan is associated with Walker-Warburg syndrome. PubMed ID: 25934851

CD93 and dystroglycan cooperation in human endothelial cell adhesion and migration adhesion and migration. PubMed ID: 26848865

Structure of a WW domain containing fragment of dystrophin in complex with beta-dystroglycan. PubMed ID: 10932245

Carbohydrate-binding domain of the POMGnT1 stem region modulates O-mannosylation sites of alpha-dystroglycan. PubMed ID: 27493216

Structural flexibility of human alpha-dystroglycan. PubMed ID: 28781947