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Q14118

- DAG1_HUMAN

UniProt

Q14118 - DAG1_HUMAN

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Protein

Dystroglycan

Gene
DAG1
Organism
Homo sapiens (Human)
Status
Reviewed - 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.4 Publications
Alpha-dystroglycan is an extracellular peripheral glycoprotein that acts as a receptor for both extracellular matrix proteins containing laminin-G domains, and for certain adenoviruses. Receptor for laminin-2 (LAMA2) and agrin in peripheral nerve Schwann cells. Also acts as a receptor for M.leprae in peripheral nerve Schwann cells but only in the presence of the G-domain of LAMA2, and for lymphocytic choriomeningitis virus, Old World Lassa fever virus, and clade C New World arenaviruses.4 Publications
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.4 Publications

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sitei653 – 6542Cleavage; by autolysis
Sitei715 – 7162Cleavage; by MMP9

GO - Molecular functioni

  1. actin binding Source: UniProtKB
  2. alpha-actinin binding Source: UniProtKB
  3. calcium ion binding Source: InterPro
  4. laminin-1 binding Source: UniProtKB
  5. protein binding Source: UniProtKB
  6. SH2 domain binding Source: UniProtKB
  7. structural constituent of muscle Source: UniProtKB
  8. tubulin binding Source: UniProtKB
  9. vinculin binding Source: UniProtKB
  10. virus receptor activity Source: UniProtKB-KW

GO - Biological processi

  1. basement membrane organization Source: Ensembl
  2. branching involved in salivary gland morphogenesis Source: Ensembl
  3. calcium-dependent cell-matrix adhesion Source: Ensembl
  4. commissural neuron axon guidance Source: Ensembl
  5. cytoskeletal anchoring at plasma membrane Source: UniProtKB
  6. epithelial tube branching involved in lung morphogenesis Source: Ensembl
  7. extracellular matrix organization Source: Reactome
  8. membrane protein ectodomain proteolysis Source: UniProtKB
  9. microtubule anchoring Source: UniProtKB
  10. modulation by virus of host morphology or physiology Source: UniProtKB
  11. morphogenesis of an epithelial sheet Source: Ensembl
  12. myelination in peripheral nervous system Source: Ensembl
  13. negative regulation of cell migration Source: UniProtKB
  14. negative regulation of MAPK cascade Source: UniProtKB
  15. negative regulation of protein kinase B signaling Source: UniProtKB
  16. nerve maturation Source: Ensembl
  17. NLS-bearing protein import into nucleus Source: UniProtKB
  18. 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

ReactomeiREACT_13552. Integrin cell surface interactions.
REACT_163874. Non-integrin membrane-ECM interactions.
REACT_163906. ECM proteoglycans.

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
ProteomesiUP000005640: Chromosome 3

Organism-specific databases

HGNCiHGNC:2666. DAG1.

Subcellular locationi

Chain Alpha-dystroglycan : Secretedextracellular space 4 Publications
Chain 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.4 Publications

Topology

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Topological domaini654 – 74996Extracellular Reviewed predictionAdd
BLAST
Transmembranei750 – 77526Helical; Reviewed predictionAdd
BLAST
Topological domaini776 – 895120Cytoplasmic Reviewed predictionAdd
BLAST

GO - Cellular componenti

  1. basement membrane Source: UniProtKB
  2. basolateral plasma membrane Source: Ensembl
  3. cell-cell adherens junction Source: Ensembl
  4. cell outer membrane Source: Ensembl
  5. contractile ring Source: UniProtKB
  6. costamere Source: Ensembl
  7. cytoplasm Source: UniProtKB
  8. cytoskeleton Source: UniProtKB-SubCell
  9. dystroglycan complex Source: Ensembl
  10. dystrophin-associated glycoprotein complex Source: UniProtKB
  11. extracellular region Source: Reactome
  12. extracellular space Source: UniProtKB
  13. extracellular vesicular exosome Source: UniProt
  14. filopodium Source: UniProtKB
  15. focal adhesion Source: Ensembl
  16. integral component of membrane Source: UniProtKB
  17. lamellipodium Source: UniProtKB
  18. membrane raft Source: Ensembl
  19. node of Ranvier Source: Ensembl
  20. nucleoplasm Source: UniProtKB
  21. plasma membrane Source: UniProtKB
  22. postsynaptic membrane Source: UniProtKB-SubCell
  23. 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) [MIM:613818]: An autosomal recessive muscular dystrophy showing onset in early childhood, and associated with mental retardation without structural brain anomalies.
Note: 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.1 Publication
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti192 – 1921T → M in MDDGC9; results in impaired interaction with LARGE and incomplete DAG1 glycosylation. 1 Publication
VAR_065266

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi654 – 6541S → A: Abolishes autoproteolysis and enhances laminin-binding. 2 Publications
Mutagenesisi663 – 6631T → A: Reduced N-linked glycosylation. No change in nuclear trnslocation. 1 Publication
Mutagenesisi776 – 7827RKKRKGK → AKKRKGA: Moderate reduction in nuclear accumulation.
Mutagenesisi777 – 7826KKRKGK → AARKGA: About 50% reduction in nuclear accumulation. 1 Publication
Mutagenesisi777 – 7826KKRKGK → RKKAAGA: Drastic reduction in nuclear accumulation. 1 Publication
Mutagenesisi777 – 7804KKRK → NPGE: Abolishes nuclear translocation. 1 Publication
Mutagenesisi779 – 7791R → A: Significant reduction in nuclear accumulation.
Mutagenesisi780 – 7801K → A: Significant reduction in nuclear accumulation.
Mutagenesisi793 – 7942KK → TA: Abolishes nuclear translocation.
Mutagenesisi823 – 8231K → A: No change in nuclear location. 1 Publication
Mutagenesisi828 – 8292PP → AA: No change in nuclear location.
Mutagenesisi831 – 8311Y → A: No change in nuclear location. 1 Publication
Mutagenesisi892 – 8921Y → A: Abolishes phosphorylation. No change in plasma membrane location. 2 Publications
Mutagenesisi892 – 8921Y → E: Redistributes to a vesicular internal membrane compartment. 2 Publications
Mutagenesisi892 – 8921Y → F: Abolishes phosphorylation. Increase in nuclear location. 2 Publications

Keywords - Diseasei

Disease mutation, Dystroglycanopathy, Limb-girdle muscular dystrophy

Organism-specific databases

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

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Signal peptidei1 – 2929 Reviewed predictionAdd
BLAST
Chaini30 – 653624Alpha-dystroglycanPRO_0000021065Add
BLAST
Chaini654 – 895242Beta-dystroglycanPRO_0000021066Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Glycosylationi63 – 631O-linked (GalNAc...)1 Publication
Glycosylationi141 – 1411N-linked (GlcNAc...) Reviewed prediction
Disulfide bondi182 ↔ 264 By similarity
Glycosylationi367 – 3671O-linked (Hex...)1 Publication
Glycosylationi369 – 3691O-linked (Hex...)1 Publication
Glycosylationi372 – 3721O-linked (Hex...)1 Publication
Glycosylationi379 – 3791O-linked (Man6P...)1 Publication
Glycosylationi381 – 3811O-linked (Hex...)1 Publication
Glycosylationi388 – 3881O-linked (Hex...)1 Publication
Glycosylationi455 – 4551O-linked (GalNAc...)1 Publication
Glycosylationi641 – 6411N-linked (GlcNAc...) Reviewed prediction
Glycosylationi649 – 6491N-linked (GlcNAc...) Reviewed prediction
Glycosylationi661 – 6611N-linked (GlcNAc...) Reviewed prediction
Disulfide bondi669 ↔ 7131 Publication
Modified residuei892 – 8921Phosphotyrosine; by SRC3 Publications

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-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 (LARGE) protein and is required for laminin binding. 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.5 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.
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.

Keywords - PTMi

Disulfide bond, Glycoprotein, Phosphoprotein

Proteomic databases

MaxQBiQ14118.
PaxDbiQ14118.
PRIDEiQ14118.

PTM databases

PhosphoSiteiQ14118.

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

ArrayExpressiQ14118.
BgeeiQ14118.
CleanExiHS_DAG1.
GenevestigatoriQ14118.

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 LARGE; the interaction enhances laminin binding By similarity. Interacts with SGCD. Interacts with AGR2 and AGR3. Interacts (betaDAG1) with DMD; the interaction is inhibited by phosphorylaion 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.10 Publications

Binary interactionsi

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

Protein-protein interaction databases

BioGridi107975. 30 interactions.
DIPiDIP-40928N.
IntActiQ14118. 8 interactions.
MINTiMINT-5004541.
STRINGi9606.ENSP00000312435.

Structurei

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1EG4X-ray2.00P881-895[»]
ProteinModelPortaliQ14118.
SMRiQ14118. Positions 60-304.

Miscellaneous databases

EvolutionaryTraceiQ14118.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini603 – 712110Peptidase S72Add
BLAST

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni30 – 408379Required for laminin recognitionAdd
BLAST
Regioni169 – 20032O-glycosylated at one siteAdd
BLAST
Regioni316 – 485170Mucin-like domainAdd
BLAST
Regioni463 – 48523O-glycosylated at seven sites with GalNAcAdd
BLAST
Regioni819 – 89577Required for interaction with CAV3Add
BLAST
Regioni880 – 89516Required for binding DMD and UTRNAdd
BLAST

Motif

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Motifi776 – 7827Nuclear localization signal1 Publication
Motifi889 – 8924PPXY motif

Compositional bias

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Compositional biasi317 – 484168Thr-richAdd
BLAST
Compositional biasi809 – 89587Pro-richAdd
BLAST

Sequence similaritiesi

Keywords - Domaini

Signal, Transmembrane, Transmembrane helix

Phylogenomic databases

eggNOGiNOG266557.
HOGENOMiHOG000072580.
HOVERGENiHBG000078.
InParanoidiQ14118.
KOiK06265.
OMAiAMICYRK.
OrthoDBiEOG7KSX82.
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.
[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

MRMSVGLSLL LPLSGRTFLL LLSVVMAQSH WPSEPSEAVR DWENQLEASM    50
HSVLSDLHEA VPTVVGIPDG TAVVGRSFRV TIPTDLIASS GDIIKVSAAG 100
KEALPSWLHW DSQSHTLEGL PLDTDKGVHY ISVSATRLGA NGSHIPQTSS 150
VFSIEVYPED HSELQSVRTA SPDPGEVVSS ACAADEPVTV LTVILDADLT 200
KMTPKQRIDL LHRMRSFSEV ELHNMKLVPV VNNRLFDMSA FMAGPGNAKK 250
VVENGALLSW KLGCSLNQNS VPDIHGVEAP AREGAMSAQL GYPVVGWHIA 300
NKKPPLPKRV RRQIHATPTP VTAIGPPTTA IQEPPSRIVP TPTSPAIAPP 350
TETMAPPVRD PVPGKPTVTI RTRGAIIQTP TLGPIQPTRV SEAGTTVPGQ 400
IRPTMTIPGY VEPTAVATPP TTTTKKPRVS TPKPATPSTD STTTTTRRPT 450
KKPRTPRPVP RVTTKVSITR LETASPPTRI RTTTSGVPRG GEPNQRPELK 500
NHIDRVDAWV GTYFEVKIPS DTFYDHEDTT TDKLKLTLKL REQQLVGEKS 550
WVQFNSNSQL MYGLPDSSHV GKHEYFMHAT DKGGLSAVDA FEIHVHRRPQ 600
GDRAPARFKA KFVGDPALVL NDIHKKIALV KKLAFAFGDR NCSTITLQNI 650
TRGSIVVEWT NNTLPLEPCP KEQIAGLSRR IAEDDGKPRP AFSNALEPDF 700
KATSITVTGS GSCRHLQFIP VVPPRRVPSE APPTEVPDRD PEKSSEDDVY 750
LHTVIPAVVV AAILLIAGII AMICYRKKRK GKLTLEDQAT FIKKGVPIIF 800
ADELDDSKPP PSSSMPLILQ EEKAPLPPPE YPNQSVPETT PLNQDTMGEY 850
TPLRDEDPNA PPYQPPPPFT APMEGKGSRP KNMTPYRSPP PYVPP 895
Length:895
Mass (Da):97,441
Last modified:May 5, 2009 - v2
Checksum:i3AF6CBB0DCF91962
GO

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti14 – 141S → W.4 Publications
Corresponds to variant rs2131107 [ dbSNP | Ensembl ].
VAR_024335
Natural varianti192 – 1921T → M in MDDGC9; results in impaired interaction with LARGE and incomplete DAG1 glycosylation. 1 Publication
VAR_065266

Sequence conflict

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti163 – 1631E → D in AAA81779. 1 Publication
Sequence conflicti248 – 2481A → P in AAA81779. 1 Publication
Sequence conflicti319 – 3191T → A in BAF84381. 1 Publication
Sequence conflicti871 – 8711A → V in AAA81779. 1 Publication

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
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.4. human.

Polymorphism databases

DMDMi229462879.

Keywords - Coding sequence diversityi

Polymorphism

Cross-referencesi

Web resourcesi

Wikipedia

Dystroglycan entry

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
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 .
CCDSi CCDS2799.1.
PIRi I54343.
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.
UniGenei Hs.76111.

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
1EG4 X-ray 2.00 P 881-895 [» ]
ProteinModelPortali Q14118.
SMRi Q14118. Positions 60-304.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 107975. 30 interactions.
DIPi DIP-40928N.
IntActi Q14118. 8 interactions.
MINTi MINT-5004541.
STRINGi 9606.ENSP00000312435.

Protein family/group databases

MEROPSi S72.001.

PTM databases

PhosphoSitei Q14118.

Polymorphism databases

DMDMi 229462879.

Proteomic databases

MaxQBi Q14118.
PaxDbi Q14118.
PRIDEi Q14118.

Protocols and materials databases

DNASUi 1605.
Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENST00000308775 ; ENSP00000312435 ; ENSG00000173402 .
ENST00000515359 ; ENSP00000440705 ; ENSG00000173402 .
ENST00000538711 ; ENSP00000438421 ; ENSG00000173402 .
ENST00000539901 ; ENSP00000439334 ; ENSG00000173402 .
ENST00000541308 ; ENSP00000440590 ; ENSG00000173402 .
ENST00000545947 ; ENSP00000442600 ; ENSG00000173402 .
GeneIDi 1605.
KEGGi hsa:1605.
UCSCi uc003cxc.4. human.

Organism-specific databases

CTDi 1605.
GeneCardsi GC03P049482.
HGNCi HGNC:2666. DAG1.
HPAi CAB001960.
CAB016353.
MIMi 128239. gene.
613818. phenotype.
neXtProti NX_Q14118.
Orphaneti 280333. Autosomal recessive limb-girdle muscular dystrophy type 2P.
370997. Muscle-eye-brain disease with bilateral multicystic leucodystrophy.
PharmGKBi PA27138.
GenAtlasi Search...

Phylogenomic databases

eggNOGi NOG266557.
HOGENOMi HOG000072580.
HOVERGENi HBG000078.
InParanoidi Q14118.
KOi K06265.
OMAi AMICYRK.
OrthoDBi EOG7KSX82.
PhylomeDBi Q14118.
TreeFami TF328370.

Enzyme and pathway databases

Reactomei REACT_13552. Integrin cell surface interactions.
REACT_163874. Non-integrin membrane-ECM interactions.
REACT_163906. ECM proteoglycans.

Miscellaneous databases

ChiTaRSi DAG1. human.
EvolutionaryTracei Q14118.
GeneWikii Dystroglycan.
GenomeRNAii 1605.
NextBioi 6586.
PROi Q14118.
SOURCEi Search...

Gene expression databases

ArrayExpressi Q14118.
Bgeei Q14118.
CleanExi HS_DAG1.
Genevestigatori Q14118.

Family and domain databases

Gene3Di 2.60.40.10. 2 hits.
3.30.70.1040. 1 hit.
InterProi IPR027468. Alpha-dystroglycan_domain_2.
IPR006644. Cadg.
IPR015919. Cadherin-like.
IPR008465. DAG1.
IPR013783. Ig-like_fold.
[Graphical view ]
Pfami PF05454. DAG1. 1 hit.
[Graphical view ]
SMARTi SM00736. CADG. 2 hits.
[Graphical view ]
SUPFAMi SSF111006. SSF111006. 1 hit.
SSF49313. SSF49313. 2 hits.
PROSITEi PS51699. SEA_DG. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  1. "Human dystroglycan: skeletal muscle cDNA, genomic structure, origin of tissue specific isoforms and chromosomal localization."
    Ibraghimov-Beskrovnaya O., Milatovich A., Ozcelik T., Yang B., Koepnick K., Francke U., Campbell K.P.
    Hum. Mol. Genet. 2:1651-1657(1993) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA], TISSUE SPECIFICITY, VARIANT TRP-14.
    Tissue: Skeletal muscle.
  2. "Complete sequencing and characterization of 21,243 full-length human cDNAs."
    Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.
    , Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.
    Nat. Genet. 36:40-45(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA], VARIANT TRP-14.
    Tissue: Placenta.
  3. "The DNA sequence, annotation and analysis of human chromosome 3."
    Muzny D.M., Scherer S.E., Kaul R., Wang J., Yu J., Sudbrak R., Buhay C.J., Chen R., Cree A., Ding Y., Dugan-Rocha S., Gill R., Gunaratne P., Harris R.A., Hawes A.C., Hernandez J., Hodgson A.V., Hume J.
    , Jackson A., Khan Z.M., Kovar-Smith C., Lewis L.R., Lozado R.J., Metzker M.L., Milosavljevic A., Miner G.R., Morgan M.B., Nazareth L.V., Scott G., Sodergren E., Song X.-Z., Steffen D., Wei S., Wheeler D.A., Wright M.W., Worley K.C., Yuan Y., Zhang Z., Adams C.Q., Ansari-Lari M.A., Ayele M., Brown M.J., Chen G., Chen Z., Clendenning J., Clerc-Blankenburg K.P., Chen R., Chen Z., Davis C., Delgado O., Dinh H.H., Dong W., Draper H., Ernst S., Fu G., Gonzalez-Garay M.L., Garcia D.K., Gillett W., Gu J., Hao B., Haugen E., Havlak P., He X., Hennig S., Hu S., Huang W., Jackson L.R., Jacob L.S., Kelly S.H., Kube M., Levy R., Li Z., Liu B., Liu J., Liu W., Lu J., Maheshwari M., Nguyen B.-V., Okwuonu G.O., Palmeiri A., Pasternak S., Perez L.M., Phelps K.A., Plopper F.J., Qiang B., Raymond C., Rodriguez R., Saenphimmachak C., Santibanez J., Shen H., Shen Y., Subramanian S., Tabor P.E., Verduzco D., Waldron L., Wang J., Wang J., Wang Q., Williams G.A., Wong G.K.-S., Yao Z., Zhang J., Zhang X., Zhao G., Zhou J., Zhou Y., Nelson D., Lehrach H., Reinhardt R., Naylor S.L., Yang H., Olson M., Weinstock G., Gibbs R.A.
    Nature 440:1194-1198(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  4. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA], VARIANT TRP-14.
  5. "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
    The MGC Project Team
    Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA], VARIANT TRP-14.
    Tissue: Muscle.
  6. "Identification and characterization of the dystrophin anchoring site on beta-dystroglycan."
    Jung D., Yang B., Meyer J., Chamberlain J.S., Campbell K.P.
    J. Biol. Chem. 270:27305-27310(1995) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH DMD.
  7. "Role of alpha-dystroglycan as a Schwann cell receptor for Mycobacterium leprae."
    Rambukkana A., Yamada H., Zanazzi G., Mathus T., Salzer J.L., Yurchenco P.D., Campbell K.P., Fischetti V.A.
    Science 282:2076-2079(1998) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION AS RECEPTOR FOR MYCOBACTERIUM LEPRAE, SUBCELLULAR LOCATION, INTERACTION WITH LAMA2.
  8. "Contribution of the different modules in the utrophin carboxy-terminal region to the formation and regulation of the DAP complex."
    Tommasi di Vignano A., Di Zenzo G., Sudol M., Cesareni G., Dente L.
    FEBS Lett. 471:229-234(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH UTRN.
  9. "Caveolin-3 directly interacts with the C-terminal tail of beta -dystroglycan. Identification of a central WW-like domain within caveolin family members."
    Sotgia F., Lee J.K., Das K., Bedford M., Petrucci T.C., Macioce P., Sargiacomo M., Bricarelli F.D., Minetti C., Sudol M., Lisanti M.P.
    J. Biol. Chem. 275:38048-38058(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH CAV3.
  10. "Adhesion-dependent tyrosine phosphorylation of (beta)-dystroglycan regulates its interaction with utrophin."
    James M., Nuttall A., Ilsley J.L., Ottersbach K., Tinsley J.M., Sudol M., Winder S.J.
    J. Cell Sci. 113:1717-1726(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION, INTERACTION WITH UTRN.
  11. "Tyrosine phosphorylation of beta-dystroglycan at its WW domain binding motif, PPxY, recruits SH2 domain containing proteins."
    Sotgia F., Lee H., Bedford M.T., Petrucci T., Sudol M., Lisanti M.P.
    Biochemistry 40:14585-14592(2001) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION, INTERACTION WITH FYN; CSK; NCK AND SHC, POSSIBLE FUNCTION.
  12. "The interaction of dystrophin with beta-dystroglycan is regulated by tyrosine phosphorylation."
    Ilsley J.L., Sudol M., Winder S.J.
    Cell. Signal. 13:625-632(2001) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION AT TYR-892, INTERACTION WITH DMD.
  13. "Post-translational disruption of dystroglycan-ligand interactions in congenital muscular dystrophies."
    Michele D.E., Barresi R., Kanagawa M., Saito F., Cohn R.D., Satz J.S., Dollar J., Nishino I., Kelley R.I., Somer H., Straub V., Mathews K.D., Moore S.A., Campbell K.P.
    Nature 418:417-422(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: GLYCOSYLATION, LIGAND-BINDING, ASSOCIATION WITH CONGENITAL MUSCULAR DYSTROPHIES.
  14. "Localization of phospho-beta-dystroglycan (pY892) to an intracellular vesicular compartment in cultured cells and skeletal muscle fibers in vivo."
    Sotgia F., Bonuccelli G., Bedford M., Brancaccio A., Mayer U., Wilson M.T., Campos-Gonzalez R., Brooks J.W., Sudol M., Lisanti M.P.
    Biochemistry 42:7110-7123(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION AT TYR-892, SUBCELLULAR LOCATION, MUTAGENESIS OF TYR-892.
  15. "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."
    Fletcher G.C., Patel S., Tyson K., Adam P.J., Schenker M., Loader J.A., Daviet L., Legrain P., Parekh R., Harris A.L., Terrett J.A.
    Br. J. Cancer 88:579-585(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH AGR2 AND AGR3.
  16. Cited for: PROTEOLYTIC PROCESSING OF THE BETA SUBUNIT, TISSUE SPECIFICITY.
  17. "O Mannosylation of alpha-dystroglycan is essential for lymphocytic choriomeningitis virus receptor function."
    Imperiali M., Thoma C., Pavoni E., Brancaccio A., Callewaert N., Oxenius A.
    J. Virol. 79:14297-14308(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: GLYCOSYLATION, FUNCTION AS RECEPTOR FOR LYMPHOCYCTIC CHORIOMENINGITIS VIRUS.
  18. "Cys669-Cys713 disulfide bridge formation is a key to dystroglycan cleavage and subunit association."
    Watanabe N., Sasaoka T., Noguchi S., Nishino I., Tanaka T.
    Genes Cells 12:75-88(2007) [PubMed] [Europe PMC] [Abstract]
    Cited for: DISULFIDE BOND.
  19. "Old World and clade C New World arenaviruses mimic the molecular mechanism of receptor recognition used by alpha-dystroglycan's host-derived ligands."
    Rojek J.M., Spiropoulou C.F., Campbell K.P., Kunz S.
    J. Virol. 81:5685-5695(2007) [PubMed] [Europe PMC] [Abstract]
    Cited for: GLYCOSYLATION, FUNCTION AS RECEPTOR FOR OLD WORLD AND CLADE C NEW WORLD ARENAVIRUSES.
  20. "SEA domain proteolysis determines the functional composition of dystroglycan."
    Akhavan A., Crivelli S.N., Singh M., Lingappa V.R., Muschler J.L.
    FASEB J. 22:612-621(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: PROTEOLYTIC PROCESSING, CLEAVAGE AT GLY-653, GLYCOSYLATION, LIGAND-BINDING, MUTAGENESIS OF SER-654.
  21. "Nuclear translocation of beta-dystroglycan reveals a distinctive trafficking pattern of autoproteolyzed mucins."
    Oppizzi M.L., Akhavan A., Singh M., Fata J.E., Muschler J.L.
    Traffic 9:2063-2072(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: SUBCELLULAR LOCATION, PROTEOLYTIC PROCESSING, MUTAGENESIS OF SER-654; THR-663; 777-LYS--LYS-780; 793-LYS-LYS-794; LYS-823; 828-PRO-PRO-829 AND TYR-831.
  22. "Enzymatic processing of beta-dystroglycan recombinant ectodomain by MMP-9: identification of the main cleavage site."
    Bozzi M., Inzitari R., Sbardell D., Monaco S., Pavoni E., Gioia M., Marini S., Morlacchi S., Sciandra F., Castagnola M., Giardina B., Brancaccio A., Coletta M.
    IUBMB Life 61:1143-1152(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: PROTEOLYTIC PROCESSING OF BETA SUBUNIT, CLEAVAGE AT HIS-715, IDENTIFICATION BY MASS SPECTROMETRY.
  23. "Enrichment of glycopeptides for glycan structure and attachment site identification."
    Nilsson J., Rueetschi U., Halim A., Hesse C., Carlsohn E., Brinkmalm G., Larson G.
    Nat. Methods 6:809-811(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: GLYCOSYLATION [LARGE SCALE ANALYSIS], STRUCTURE OF CARBOHYDRATES.
    Tissue: Cerebrospinal fluid.
  24. "Characterization of site-specific O-glycan structures within the mucin-like domain of {alpha}-dystroglycan from human skeletal muscle."
    Nilsson J., Nilsson J., Larson G., Grahn A.
    Glycobiology 20:1160-1169(2010) [PubMed] [Europe PMC] [Abstract]
    Cited for: STRUCTURE OF CARBOHYDRATES, IDENTIFICATION BY MASS SPECTROMETRY, GLYCOSYLATION AT THR-367; THR-369; THR-372 AND THR-455.
  25. "Characterization of an Importin alpha/beta-recognized nuclear localization signal in beta-dystroglycan."
    Lara-Chacon B., de Leon M.B., Leocadio D., Gomez P., Fuentes-Mera L., Martinez-Vieyra I., Ortega A., Jans D.A., Cisneros B.
    J. Cell. Biochem. 110:706-717(2010) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION AT TYR-892, NUCLEAR LOCALIZATION SIGNAL, SUBCELLULAR LOCATION, MUTAGENESIS OF 777-LYS--LYS-782 AND TYR-892.
  26. "O-mannosyl phosphorylation of alpha-dystroglycan is required for laminin binding."
    Yoshida-Moriguchi T., Yu L., Stalnaker S.H., Davis S., Kunz S., Madson M., Oldstone M.B., Schachter H., Wells L., Campbell K.P.
    Science 327:88-92(2010) [PubMed] [Europe PMC] [Abstract]
    Cited for: GLYCOSYLATION AT THR-379; THR-381 AND THR-388, IDENTIFICATION BY MASS SPECTROMETRY.
  27. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  28. "LC-MS/MS characterization of O-glycosylation sites and glycan structures of human cerebrospinal fluid glycoproteins."
    Halim A., Ruetschi U., Larson G., Nilsson J.
    J. Proteome Res. 12:573-584(2013) [PubMed] [Europe PMC] [Abstract]
    Cited for: GLYCOSYLATION AT THR-63, IDENTIFICATION BY MASS SPECTROMETRY.
  29. "Structure of a WW domain containing fragment of dystrophin in complex with beta-dystroglycan."
    Huang X., Poy F., Zhang R., Joachimiak A., Sudol M., Eck M.J.
    Nat. Struct. Biol. 7:634-638(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS) OF 881-895.
  30. Cited for: VARIANT MDDGC9 MET-192, CHARACTERIZATION OF VARIANT MDDGC9 MET-192.

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: September 3, 2014
This is version 142 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

External Data

Dasty 3

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