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Protein

Dystroglycan

Gene

DAG1

Organism
Homo sapiens (Human)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

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

GO - Molecular functioni

  • actin binding Source: UniProtKB
  • alpha-actinin binding Source: UniProtKB
  • calcium ion binding Source: InterPro
  • laminin-1 binding Source: UniProtKB
  • SH2 domain binding Source: UniProtKB
  • structural constituent of muscle Source: UniProtKB
  • tubulin binding Source: UniProtKB
  • vinculin binding Source: UniProtKB
  • virus receptor activity Source: UniProtKB-KW

GO - Biological processi

  • basement membrane organization Source: Ensembl
  • branching involved in salivary gland morphogenesis Source: Ensembl
  • calcium-dependent cell-matrix adhesion Source: Ensembl
  • commissural neuron axon guidance Source: Ensembl
  • cytoskeletal anchoring at plasma membrane Source: UniProtKB
  • epithelial tube branching involved in lung morphogenesis Source: Ensembl
  • extracellular matrix organization Source: Reactome
  • membrane protein ectodomain proteolysis Source: UniProtKB
  • microtubule anchoring Source: UniProtKB
  • modulation by virus of host morphology or physiology Source: UniProtKB
  • morphogenesis of an epithelial sheet Source: Ensembl
  • myelination in peripheral nervous system Source: Ensembl
  • negative regulation of cell migration Source: UniProtKB
  • negative regulation of MAPK cascade Source: UniProtKB
  • negative regulation of protein kinase B signaling Source: UniProtKB
  • nerve maturation Source: Ensembl
  • NLS-bearing protein import into nucleus Source: UniProtKB
  • positive regulation of basement membrane assembly involved in embryonic body morphogenesis Source: UniProtKB
  • protein O-linked glycosylation Source: Reactome
  • regulation of embryonic cell shape Source: UniProtKB
  • regulation of epithelial to mesenchymal transition Source: UniProtKB
  • regulation of gastrulation Source: UniProtKB
  • response to peptide hormone Source: Ensembl
Complete GO annotation...

Keywords - Molecular functioni

Host cell receptor for virus entry, Receptor

Keywords - Biological processi

Host-virus interaction

Enzyme and pathway databases

BioCyciZFISH:ENSG00000173402-MONOMER.
ReactomeiR-HSA-216083. Integrin cell surface interactions.
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.
SIGNORiQ14118.

Protein family/group databases

MEROPSiS72.001.

Names & Taxonomyi

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
Gene namesi
Name:DAG1
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
Proteomesi
  • UP000005640 Componenti: Chromosome 3

Organism-specific databases

HGNCiHGNC:2666. DAG1.

Subcellular locationi

Beta-dystroglycan :
  • Cell membrane; Single-pass type I membrane protein
  • Cytoplasmcytoskeleton
  • Nucleusnucleoplasm
  • Cell membranesarcolemma By similarity
  • Cell junctionsynapsepostsynaptic cell membrane By similarity

  • Note: The monomeric form translocates to the nucleus via the action of importins and depends on RAN. Nuclear transport is inhibited by Tyr-892 phosphorylation. In skeletal muscle, this phosphorylated form locates to a vesicular internal membrane compartment. In muscle cells, sarcolemma localization requires the presence of ANK2, while localization to costameres requires the presence of ANK3. Localizes to neuromuscular junctions (NMJs) in the presence of ANK2 (By similarity). In peripheral nerves, localizes to the Schwann cell membrane. Colocalizes with ERM proteins in Schwann-cell microvilli.By similarity

Topology

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Topological domaini654 – 749ExtracellularSequence analysisAdd BLAST96
Transmembranei750 – 775HelicalSequence analysisAdd BLAST26
Topological domaini776 – 895CytoplasmicSequence analysisAdd BLAST120

GO - Cellular componenti

  • basement membrane Source: UniProtKB
  • basolateral plasma membrane Source: Ensembl
  • cell-cell adherens junction Source: Ensembl
  • cell outer membrane Source: Ensembl
  • contractile ring Source: UniProtKB
  • costamere Source: Ensembl
  • cytoplasm Source: UniProtKB
  • cytoskeleton Source: UniProtKB-SubCell
  • cytosol Source: Reactome
  • dystroglycan complex Source: Ensembl
  • dystrophin-associated glycoprotein complex Source: UniProtKB
  • extracellular exosome Source: UniProtKB
  • extracellular region Source: Reactome
  • extracellular space Source: UniProtKB
  • filopodium Source: UniProtKB
  • focal adhesion Source: UniProtKB
  • integral component of membrane Source: UniProtKB
  • lamellipodium Source: UniProtKB
  • membrane raft Source: Ensembl
  • node of Ranvier Source: Ensembl
  • nucleoplasm Source: UniProtKB
  • plasma membrane Source: UniProtKB
  • postsynaptic membrane Source: UniProtKB-SubCell
  • sarcolemma Source: UniProtKB-SubCell
Complete GO annotation...

Keywords - Cellular componenti

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

Pathology & Biotechi

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.
See also OMIM:613818
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Natural variantiVAR_07580974V → I in MDDGC9; no effect on dystroglycan expression; impairs alpha-dystroglycan glycosylation. 1 PublicationCorresponds to variant rs189360006dbSNPEnsembl.1
Natural variantiVAR_075810111D → N in MDDGC9; does not affect dystroglycan expression; impairs alpha-dystroglycan glycosylation. 1 PublicationCorresponds to variant rs117209107dbSNPEnsembl.1
Natural variantiVAR_065266192T → M in MDDGC9; results in impaired interaction with LARGE1 and incomplete DAG1 glycosylation. 1 PublicationCorresponds to variant rs193922955dbSNPEnsembl.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.
See also OMIM:616538
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Natural variantiVAR_075811669C → F in MDDGA9. 1 Publication1

Mutagenesis

Feature keyPosition(s)DescriptionActionsGraphical viewLength
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 trnslocation. 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

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

Organism-specific databases

DisGeNETi1605.
MalaCardsiDAG1.
MIMi613818. phenotype.
616538. phenotype.
OpenTargetsiENSG00000173402.
Orphaneti280333. Autosomal recessive limb-girdle muscular dystrophy type 2P.
370997. Muscle-eye-brain disease with bilateral multicystic leucodystrophy.
PharmGKBiPA27138.

Polymorphism and mutation databases

BioMutaiDAG1.
DMDMi229462879.

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Signal peptidei1 – 29Sequence analysisAdd BLAST29
ChainiPRO_000002106530 – 653Alpha-dystroglycanAdd BLAST624
ChainiPRO_0000021066654 – 895Beta-dystroglycanAdd BLAST242

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Glycosylationi63O-linked (GalNAc...)1 Publication1
Glycosylationi141N-linked (GlcNAc...)Sequence analysis1
Disulfide bondi182 ↔ 264By similarity
Glycosylationi317O-linked (Man6P...)2 Publications1
Glycosylationi319O-linked (Man6P...)2 Publications1
Glycosylationi367O-linked (Hex...)1 Publication1
Glycosylationi369O-linked (Hex...)1 Publication1
Glycosylationi372O-linked (Hex...)1 Publication1
Glycosylationi379O-linked (Man6P...)1 Publication1
Glycosylationi381O-linked (Hex...)1 Publication1
Glycosylationi388O-linked (Hex...)1 Publication1
Glycosylationi455O-linked (GalNAc...)1 Publication1
Glycosylationi641N-linked (GlcNAc...)Sequence analysis1
Glycosylationi649N-linked (GlcNAc...)Sequence analysis1
Glycosylationi661N-linked (GlcNAc...)Sequence analysis1
Disulfide bondi669 ↔ 7131 Publication
Modified residuei790PhosphothreonineCombined sources1
Modified residuei892Phosphotyrosine; by SRC3 Publications1

Post-translational modificationi

O- and N-glycosylated. 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. The beta subunit is N-glycosylated.10 Publications
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
Sitei653 – 654Cleavage; by autolysis2
Sitei715 – 716Cleavage; by MMP92

Keywords - PTMi

Autocatalytic cleavage, Disulfide bond, Glycoprotein, Phosphoprotein

Proteomic databases

EPDiQ14118.
MaxQBiQ14118.
PaxDbiQ14118.
PeptideAtlasiQ14118.
PRIDEiQ14118.
TopDownProteomicsiQ14118.

PTM databases

iPTMnetiQ14118.
PhosphoSitePlusiQ14118.
SwissPalmiQ14118.
UniCarbKBiQ14118.

Expressioni

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

BgeeiENSG00000173402.
CleanExiHS_DAG1.
ExpressionAtlasiQ14118. baseline and differential.
GenevisibleiQ14118. HS.

Organism-specific databases

HPAiCAB001960.
CAB016353.

Interactioni

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).By similarity
(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

Binary interactionsi

WithEntry#Exp.IntActNotes
Ank3Q3T1J52EBI-1755945,EBI-2133962From a different organism.
NCK1P163332EBI-1755945,EBI-389883

GO - Molecular functioni

  • actin binding Source: UniProtKB
  • alpha-actinin binding Source: UniProtKB
  • laminin-1 binding Source: UniProtKB
  • SH2 domain binding Source: UniProtKB
  • tubulin binding Source: UniProtKB
  • vinculin binding Source: UniProtKB

Protein-protein interaction databases

BioGridi107975. 50 interactors.
DIPiDIP-40928N.
IntActiQ14118. 9 interactors.
MINTiMINT-5004541.
STRINGi9606.ENSP00000312435.

Structurei

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1EG4X-ray2.00P881-895[»]
2MK7NMR-A419-427[»]
5GGPX-ray1.60C/D316-325[»]
ProteinModelPortaliQ14118.
SMRiQ14118.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiQ14118.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Domaini603 – 712Peptidase S72Add BLAST110

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
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
Motifi776 – 782Nuclear localization signal1 Publication7
Motifi889 – 892PPXY motif4

Compositional bias

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Compositional biasi317 – 484Thr-richAdd BLAST168
Compositional biasi809 – 895Pro-richAdd BLAST87

Sequence similaritiesi

Contains 1 peptidase S72 domain.Curated

Keywords - Domaini

Signal, Transmembrane, Transmembrane helix

Phylogenomic databases

eggNOGiKOG3781. Eukaryota.
ENOG410XQTU. LUCA.
GeneTreeiENSGT00390000008429.
HOGENOMiHOG000072580.
HOVERGENiHBG000078.
InParanoidiQ14118.
KOiK06265.
OMAiAMICYRK.
OrthoDBiEOG091G05R9.
PhylomeDBiQ14118.
TreeFamiTF328370.

Family and domain databases

Gene3Di2.60.40.10. 2 hits.
3.30.70.1040. 1 hit.
InterProiIPR027468. Alpha-dystroglycan_domain_2.
IPR006644. Cadg.
IPR015919. Cadherin-like.
IPR008465. DAG1.
IPR013783. Ig-like_fold.
IPR030398. SEA_DG_dom.
[Graphical view]
PfamiPF05454. DAG1. 1 hit.
[Graphical view]
SMARTiSM00736. CADG. 2 hits.
[Graphical view]
SUPFAMiSSF111006. SSF111006. 1 hit.
SSF49313. SSF49313. 2 hits.
PROSITEiPS51699. SEA_DG. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

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
Checksum:i3AF6CBB0DCF91962
GO

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
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 → W.4 PublicationsCorresponds to variant rs2131107dbSNPEnsembl.1
Natural variantiVAR_07580974V → I in MDDGC9; no effect on dystroglycan expression; impairs alpha-dystroglycan glycosylation. 1 PublicationCorresponds to variant rs189360006dbSNPEnsembl.1
Natural variantiVAR_075810111D → N in MDDGC9; does not affect dystroglycan expression; impairs alpha-dystroglycan glycosylation. 1 PublicationCorresponds to variant rs117209107dbSNPEnsembl.1
Natural variantiVAR_065266192T → M in MDDGC9; results in impaired interaction with LARGE1 and incomplete DAG1 glycosylation. 1 PublicationCorresponds to variant rs193922955dbSNPEnsembl.1
Natural variantiVAR_075811669C → F in MDDGA9. 1 Publication1

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.
UniGeneiHs.76111.

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.

Keywords - Coding sequence diversityi

Polymorphism

Cross-referencesi

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.
UniGeneiHs.76111.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1EG4X-ray2.00P881-895[»]
2MK7NMR-A419-427[»]
5GGPX-ray1.60C/D316-325[»]
ProteinModelPortaliQ14118.
SMRiQ14118.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi107975. 50 interactors.
DIPiDIP-40928N.
IntActiQ14118. 9 interactors.
MINTiMINT-5004541.
STRINGi9606.ENSP00000312435.

Protein family/group databases

MEROPSiS72.001.

PTM databases

iPTMnetiQ14118.
PhosphoSitePlusiQ14118.
SwissPalmiQ14118.
UniCarbKBiQ14118.

Polymorphism and mutation databases

BioMutaiDAG1.
DMDMi229462879.

Proteomic databases

EPDiQ14118.
MaxQBiQ14118.
PaxDbiQ14118.
PeptideAtlasiQ14118.
PRIDEiQ14118.
TopDownProteomicsiQ14118.

Protocols and materials databases

DNASUi1605.
Structural Biology KnowledgebaseSearch...

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

CTDi1605.
DisGeNETi1605.
GeneCardsiDAG1.
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.
PharmGKBiPA27138.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiKOG3781. Eukaryota.
ENOG410XQTU. LUCA.
GeneTreeiENSGT00390000008429.
HOGENOMiHOG000072580.
HOVERGENiHBG000078.
InParanoidiQ14118.
KOiK06265.
OMAiAMICYRK.
OrthoDBiEOG091G05R9.
PhylomeDBiQ14118.
TreeFamiTF328370.

Enzyme and pathway databases

BioCyciZFISH:ENSG00000173402-MONOMER.
ReactomeiR-HSA-216083. Integrin cell surface interactions.
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.
SIGNORiQ14118.

Miscellaneous databases

ChiTaRSiDAG1. human.
EvolutionaryTraceiQ14118.
GeneWikiiDystroglycan.
GenomeRNAii1605.
PROiQ14118.
SOURCEiSearch...

Gene expression databases

BgeeiENSG00000173402.
CleanExiHS_DAG1.
ExpressionAtlasiQ14118. baseline and differential.
GenevisibleiQ14118. HS.

Family and domain databases

Gene3Di2.60.40.10. 2 hits.
3.30.70.1040. 1 hit.
InterProiIPR027468. Alpha-dystroglycan_domain_2.
IPR006644. Cadg.
IPR015919. Cadherin-like.
IPR008465. DAG1.
IPR013783. Ig-like_fold.
IPR030398. SEA_DG_dom.
[Graphical view]
PfamiPF05454. DAG1. 1 hit.
[Graphical view]
SMARTiSM00736. CADG. 2 hits.
[Graphical view]
SUPFAMiSSF111006. SSF111006. 1 hit.
SSF49313. SSF49313. 2 hits.
PROSITEiPS51699. SEA_DG. 1 hit.
[Graphical view]
ProtoNetiSearch...

Entry informationi

Entry nameiDAG1_HUMAN
AccessioniPrimary (citable) accession number: Q14118
Secondary accession number(s): A8K6M7, Q969J9
Entry historyi
Integrated into UniProtKB/Swiss-Prot: November 1, 1997
Last sequence update: May 5, 2009
Last modified: November 2, 2016
This is version 164 of the entry and version 2 of the sequence. [Complete history]
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.

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. Human entries with polymorphisms or disease mutations
    List of human entries with polymorphisms or disease mutations
  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. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  6. Peptidase families
    Classification of peptidase families and list of entries
  7. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.