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Q14118 (DAG1_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 141. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (7) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Interactions·Sequence annotation·Sequences·References·Web links·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Dystroglycan
Alternative name(s):
Dystrophin-associated glycoprotein 1

Cleaved into the following 2 chains:

  1. Alpha-dystroglycan
    Short name=Alpha-DG
  2. Beta-dystroglycan
    Short name=Beta-DG
Gene names
Name:DAG1
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length895 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

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. Ref.7 Ref.11 Ref.17 Ref.19

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. Ref.7 Ref.11 Ref.17 Ref.19

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. Ref.7 Ref.11 Ref.17 Ref.19

Subunit structure

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. Ref.6 Ref.7 Ref.8 Ref.9 Ref.10 Ref.11 Ref.12 Ref.15 Ref.16 Ref.22

Subcellular location

Alpha-dystroglycan: Secretedextracellular space Ref.7 Ref.14 Ref.21 Ref.25.

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. Ref.7 Ref.14 Ref.21 Ref.25

Tissue specificity

Expressed in a variety of fetal and adult tissues. In epidermal tissue, located to the basement membrane. Also expressed in keratinocytes and fibroblasts. Ref.1 Ref.16

Post-translational modification

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. Ref.10 Ref.11 Ref.12 Ref.14 Ref.25

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.

Involvement in disease

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. Ref.30

Sequence similarities

Contains 1 peptidase S72 domain.

Ontologies

Keywords
   Biological processHost-virus interaction
   Cellular componentCell junction
Cell membrane
Cytoplasm
Cytoskeleton
Membrane
Nucleus
Postsynaptic cell membrane
Secreted
Synapse
   Coding sequence diversityPolymorphism
   DiseaseDisease mutation
Dystroglycanopathy
Limb-girdle muscular dystrophy
   DomainSignal
Transmembrane
Transmembrane helix
   Molecular functionHost cell receptor for virus entry
Receptor
   PTMDisulfide bond
Glycoprotein
Phosphoprotein
   Technical term3D-structure
Complete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processNLS-bearing protein import into nucleus

Inferred from direct assay Ref.25. Source: UniProtKB

basement membrane organization

Inferred from electronic annotation. Source: Ensembl

branching involved in salivary gland morphogenesis

Inferred from electronic annotation. Source: Ensembl

calcium-dependent cell-matrix adhesion

Inferred from electronic annotation. Source: Ensembl

commissural neuron axon guidance

Inferred from electronic annotation. Source: Ensembl

cytoskeletal anchoring at plasma membrane

Inferred from mutant phenotype PubMed 18341635. Source: UniProtKB

epithelial tube branching involved in lung morphogenesis

Inferred from electronic annotation. Source: Ensembl

extracellular matrix organization

Traceable author statement. Source: Reactome

membrane protein ectodomain proteolysis

Inferred from direct assay Ref.22. Source: UniProtKB

microtubule anchoring

Inferred from mutant phenotype PubMed 18341635. Source: UniProtKB

modulation by virus of host morphology or physiology

Inferred from direct assay Ref.17. Source: UniProtKB

morphogenesis of an epithelial sheet

Inferred from electronic annotation. Source: Ensembl

myelination in peripheral nervous system

Inferred from electronic annotation. Source: Ensembl

negative regulation of MAPK cascade

Inferred from mutant phenotype PubMed 19587235. Source: UniProtKB

negative regulation of cell migration

Inferred from mutant phenotype PubMed 19587235. Source: UniProtKB

negative regulation of protein kinase B signaling

Inferred from mutant phenotype PubMed 19587235. Source: UniProtKB

nerve maturation

Inferred from electronic annotation. Source: Ensembl

response to peptide hormone

Inferred from electronic annotation. Source: Ensembl

   Cellular_componentbasement membrane

Inferred from direct assay PubMed 19348877. Source: UniProtKB

basolateral plasma membrane

Inferred from electronic annotation. Source: Ensembl

cell outer membrane

Inferred from electronic annotation. Source: Ensembl

cell-cell adherens junction

Inferred from electronic annotation. Source: Ensembl

contractile ring

Inferred from direct assay PubMed 18341635. Source: UniProtKB

costamere

Inferred from electronic annotation. Source: Ensembl

cytoplasm

Inferred from direct assay Ref.21. Source: UniProtKB

cytoskeleton

Inferred from electronic annotation. Source: UniProtKB-SubCell

dystroglycan complex

Inferred from electronic annotation. Source: Ensembl

dystrophin-associated glycoprotein complex

Inferred from direct assay PubMed 17993586. Source: UniProtKB

extracellular region

Traceable author statement. Source: Reactome

extracellular space

Inferred from direct assay PubMed 18201566. Source: UniProtKB

extracellular vesicular exosome

Inferred from direct assay PubMed 19199708PubMed 23376485. Source: UniProt

filopodium

Inferred from direct assay PubMed 18341635. Source: UniProtKB

focal adhesion

Inferred from electronic annotation. Source: Ensembl

integral component of membrane

Inferred from direct assay PubMed 17628813. Source: UniProtKB

lamellipodium

Inferred from direct assay PubMed 18341635. Source: UniProtKB

membrane raft

Inferred from electronic annotation. Source: Ensembl

node of Ranvier

Inferred from electronic annotation. Source: Ensembl

nucleoplasm

Inferred from direct assay Ref.21. Source: UniProtKB

plasma membrane

Inferred from direct assay PubMed 18341635Ref.21PubMed 8017170. Source: UniProtKB

postsynaptic membrane

Inferred from electronic annotation. Source: UniProtKB-SubCell

sarcolemma

Inferred from electronic annotation. Source: UniProtKB-SubCell

   Molecular_functionSH2 domain binding

Inferred from direct assay Ref.11. Source: UniProtKB

actin binding

Inferred from direct assay PubMed 18341635. Source: UniProtKB

alpha-actinin binding

Inferred from direct assay PubMed 18341635. Source: UniProtKB

calcium ion binding

Inferred from electronic annotation. Source: InterPro

laminin-1 binding

Inferred from sequence or structural similarity. Source: UniProtKB

protein binding

Inferred from physical interaction Ref.8Ref.9Ref.12Ref.15PubMed 18341635PubMed 9417121. Source: UniProtKB

structural constituent of muscle

Inferred from mutant phenotype PubMed 18691338. Source: UniProtKB

tubulin binding

Inferred from direct assay PubMed 18341635. Source: UniProtKB

vinculin binding

Inferred from physical interaction PubMed 18341635. Source: UniProtKB

virus receptor activity

Inferred from electronic annotation. Source: UniProtKB-KW

Complete GO annotation...

Binary interactions

With

Entry

#Exp.

IntAct

Notes

Ank3Q3T1J52EBI-1755945,EBI-2133962From a different organism.
NCK1P163332EBI-1755945,EBI-389883

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Signal peptide1 – 2929 Potential
Chain30 – 653624Alpha-dystroglycan
PRO_0000021065
Chain654 – 895242Beta-dystroglycan
PRO_0000021066

Regions

Topological domain654 – 74996Extracellular Potential
Transmembrane750 – 77526Helical; Potential
Topological domain776 – 895120Cytoplasmic Potential
Domain603 – 712110Peptidase S72
Region30 – 408379Required for laminin recognition
Region169 – 20032O-glycosylated at one site
Region316 – 485170Mucin-like domain
Region463 – 48523O-glycosylated at seven sites with GalNAc
Region819 – 89577Required for interaction with CAV3
Region880 – 89516Required for binding DMD and UTRN
Motif776 – 7827Nuclear localization signal Ref.25
Motif889 – 8924PPXY motif
Compositional bias317 – 484168Thr-rich
Compositional bias809 – 89587Pro-rich

Sites

Site653 – 6542Cleavage; by autolysis
Site715 – 7162Cleavage; by MMP9

Amino acid modifications

Modified residue8921Phosphotyrosine; by SRC Ref.12 Ref.14 Ref.25
Glycosylation631O-linked (GalNAc...) Ref.28
Glycosylation1411N-linked (GlcNAc...) Potential
Glycosylation3671O-linked (Hex...) Ref.24
Glycosylation3691O-linked (Hex...) Ref.24
Glycosylation3721O-linked (Hex...) Ref.24
Glycosylation3791O-linked (Man6P...) Ref.26
Glycosylation3811O-linked (Hex...) Ref.26
Glycosylation3881O-linked (Hex...) Ref.26
Glycosylation4551O-linked (GalNAc...) Ref.24
Glycosylation6411N-linked (GlcNAc...) Potential
Glycosylation6491N-linked (GlcNAc...) Potential
Glycosylation6611N-linked (GlcNAc...) Potential
Disulfide bond182 ↔ 264 By similarity
Disulfide bond669 ↔ 713 Ref.18

Natural variations

Natural variant141S → W. Ref.1 Ref.2 Ref.4 Ref.5
Corresponds to variant rs2131107 [ dbSNP | Ensembl ].
VAR_024335
Natural variant1921T → M in MDDGC9; results in impaired interaction with LARGE and incomplete DAG1 glycosylation. Ref.30
VAR_065266

Experimental info

Mutagenesis6541S → A: Abolishes autoproteolysis and enhances laminin-binding. Ref.20 Ref.21
Mutagenesis6631T → A: Reduced N-linked glycosylation. No change in nuclear trnslocation. Ref.21
Mutagenesis776 – 7827RKKRKGK → AKKRKGA: Moderate reduction in nuclear accumulation.
Mutagenesis777 – 7826KKRKGK → AARKGA: About 50% reduction in nuclear accumulation. Ref.25
Mutagenesis777 – 7826KKRKGK → RKKAAGA: Drastic reduction in nuclear accumulation. Ref.25
Mutagenesis777 – 7804KKRK → NPGE: Abolishes nuclear translocation. Ref.21
Mutagenesis7791R → A: Significant reduction in nuclear accumulation.
Mutagenesis7801K → A: Significant reduction in nuclear accumulation.
Mutagenesis793 – 7942KK → TA: Abolishes nuclear translocation.
Mutagenesis8231K → A: No change in nuclear location. Ref.21
Mutagenesis828 – 8292PP → AA: No change in nuclear location.
Mutagenesis8311Y → A: No change in nuclear location. Ref.21
Mutagenesis8921Y → A: Abolishes phosphorylation. No change in plasma membrane location. Ref.14 Ref.25
Mutagenesis8921Y → E: Redistributes to a vesicular internal membrane compartment. Ref.14 Ref.25
Mutagenesis8921Y → F: Abolishes phosphorylation. Increase in nuclear location. Ref.14 Ref.25
Sequence conflict1631E → D in AAA81779. Ref.1
Sequence conflict2481A → P in AAA81779. Ref.1
Sequence conflict3191T → A in BAF84381. Ref.2
Sequence conflict8711A → V in AAA81779. Ref.1

Sequences

Sequence LengthMass (Da)Tools
Q14118 [UniParc].

Last modified May 5, 2009. Version 2.
Checksum: 3AF6CBB0DCF91962

FASTA89597,441
        10         20         30         40         50         60 
MRMSVGLSLL LPLSGRTFLL LLSVVMAQSH WPSEPSEAVR DWENQLEASM HSVLSDLHEA 

        70         80         90        100        110        120 
VPTVVGIPDG TAVVGRSFRV TIPTDLIASS GDIIKVSAAG KEALPSWLHW DSQSHTLEGL 

       130        140        150        160        170        180 
PLDTDKGVHY ISVSATRLGA NGSHIPQTSS VFSIEVYPED HSELQSVRTA SPDPGEVVSS 

       190        200        210        220        230        240 
ACAADEPVTV LTVILDADLT KMTPKQRIDL LHRMRSFSEV ELHNMKLVPV VNNRLFDMSA 

       250        260        270        280        290        300 
FMAGPGNAKK VVENGALLSW KLGCSLNQNS VPDIHGVEAP AREGAMSAQL GYPVVGWHIA 

       310        320        330        340        350        360 
NKKPPLPKRV RRQIHATPTP VTAIGPPTTA IQEPPSRIVP TPTSPAIAPP TETMAPPVRD 

       370        380        390        400        410        420 
PVPGKPTVTI RTRGAIIQTP TLGPIQPTRV SEAGTTVPGQ IRPTMTIPGY VEPTAVATPP 

       430        440        450        460        470        480 
TTTTKKPRVS TPKPATPSTD STTTTTRRPT KKPRTPRPVP RVTTKVSITR LETASPPTRI 

       490        500        510        520        530        540 
RTTTSGVPRG GEPNQRPELK NHIDRVDAWV GTYFEVKIPS DTFYDHEDTT TDKLKLTLKL 

       550        560        570        580        590        600 
REQQLVGEKS WVQFNSNSQL MYGLPDSSHV GKHEYFMHAT DKGGLSAVDA FEIHVHRRPQ 

       610        620        630        640        650        660 
GDRAPARFKA KFVGDPALVL NDIHKKIALV KKLAFAFGDR NCSTITLQNI TRGSIVVEWT 

       670        680        690        700        710        720 
NNTLPLEPCP KEQIAGLSRR IAEDDGKPRP AFSNALEPDF KATSITVTGS GSCRHLQFIP 

       730        740        750        760        770        780 
VVPPRRVPSE APPTEVPDRD PEKSSEDDVY LHTVIPAVVV AAILLIAGII AMICYRKKRK 

       790        800        810        820        830        840 
GKLTLEDQAT FIKKGVPIIF ADELDDSKPP PSSSMPLILQ EEKAPLPPPE YPNQSVPETT 

       850        860        870        880        890 
PLNQDTMGEY TPLRDEDPNA PPYQPPPPFT APMEGKGSRP KNMTPYRSPP PYVPP 

« Hide

References

« Hide 'large scale' references
[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. expand/collapse author list , 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. expand/collapse author list , 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]Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S., Turner R. expand/collapse author list , Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W., Venter J.C.
Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases
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]"Dystroglycan in skin and cutaneous cells: beta-subunit is shed from the cell surface."
Herzog C., Has C., Franzke C.W., Echtermeyer F.G., Schlotzer-Schrehardt U., Kroger S., Gustafsson E., Fassler R., Bruckner-Tuderman L.
J. Invest. Dermatol. 122:1372-1380(2004) [PubMed] [Europe PMC] [Abstract]
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]"Initial characterization of the human central proteome."
Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.
BMC Syst. Biol. 5:17-17(2011) [PubMed] [Europe PMC] [Abstract]
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]"A dystroglycan mutation associated with limb-girdle muscular dystrophy."
Hara Y., Balci-Hayta B., Yoshida-Moriguchi T., Kanagawa M., Beltran-Valero de Bernabe D., Gundesli H., Willer T., Satz J.S., Crawford R.W., Burden S.J., Kunz S., Oldstone M.B., Accardi A., Talim B., Muntoni F., Topaloglu H., Dincer P., Campbell K.P.
N. Engl. J. Med. 364:939-946(2011) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANT MDDGC9 MET-192, CHARACTERIZATION OF VARIANT MDDGC9 MET-192.
+Additional computationally mapped references.

Web resources

Wikipedia

Dystroglycan entry

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
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.
CCDSCCDS2799.1.
PIRI54343.
RefSeqNP_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.
UniGeneHs.76111.

3D structure databases

PDBe
RCSB-PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
1EG4X-ray2.00P881-895[»]
ProteinModelPortalQ14118.
SMRQ14118. Positions 60-304.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid107975. 30 interactions.
DIPDIP-40928N.
IntActQ14118. 8 interactions.
MINTMINT-5004541.
STRING9606.ENSP00000312435.

Protein family/group databases

MEROPSS72.001.

PTM databases

PhosphoSiteQ14118.

Polymorphism databases

DMDM229462879.

Proteomic databases

MaxQBQ14118.
PaxDbQ14118.
PRIDEQ14118.

Protocols and materials databases

DNASU1605.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000308775; ENSP00000312435; ENSG00000173402.
ENST00000515359; ENSP00000440705; ENSG00000173402.
ENST00000538711; ENSP00000438421; ENSG00000173402.
ENST00000539901; ENSP00000439334; ENSG00000173402.
ENST00000541308; ENSP00000440590; ENSG00000173402.
ENST00000545947; ENSP00000442600; ENSG00000173402.
GeneID1605.
KEGGhsa:1605.
UCSCuc003cxc.4. human.

Organism-specific databases

CTD1605.
GeneCardsGC03P049482.
HGNCHGNC:2666. DAG1.
HPACAB001960.
CAB016353.
MIM128239. gene.
613818. phenotype.
neXtProtNX_Q14118.
Orphanet280333. Autosomal recessive limb-girdle muscular dystrophy type 2P.
370997. Muscle-eye-brain disease with bilateral multicystic leucodystrophy.
PharmGKBPA27138.
GenAtlasSearch...

Phylogenomic databases

eggNOGNOG266557.
HOGENOMHOG000072580.
HOVERGENHBG000078.
InParanoidQ14118.
KOK06265.
OMAAMICYRK.
OrthoDBEOG7KSX82.
PhylomeDBQ14118.
TreeFamTF328370.

Enzyme and pathway databases

ReactomeREACT_118779. Extracellular matrix organization.

Gene expression databases

ArrayExpressQ14118.
BgeeQ14118.
CleanExHS_DAG1.
GenevestigatorQ14118.

Family and domain databases

Gene3D2.60.40.10. 2 hits.
3.30.70.1040. 1 hit.
InterProIPR027468. Alpha-dystroglycan_domain_2.
IPR006644. Cadg.
IPR015919. Cadherin-like.
IPR008465. DAG1.
IPR013783. Ig-like_fold.
[Graphical view]
PfamPF05454. DAG1. 1 hit.
[Graphical view]
SMARTSM00736. CADG. 2 hits.
[Graphical view]
SUPFAMSSF111006. SSF111006. 1 hit.
SSF49313. SSF49313. 2 hits.
PROSITEPS51699. SEA_DG. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

ChiTaRSDAG1. human.
EvolutionaryTraceQ14118.
GeneWikiDystroglycan.
GenomeRNAi1605.
NextBio6586.
PROQ14118.
SOURCESearch...

Entry information

Entry nameDAG1_HUMAN
AccessionPrimary (citable) accession number: Q14118
Secondary accession number(s): A8K6M7, Q969J9
Entry history
Integrated into UniProtKB/Swiss-Prot: November 1, 1997
Last sequence update: May 5, 2009
Last modified: July 9, 2014
This is version 141 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (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.

Relevant documents

SIMILARITY comments

Index of protein domains and families

Peptidase families

Classification of peptidase families and list of entries

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

MIM cross-references

Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot

Human polymorphisms and disease mutations

Index of human polymorphisms and disease mutations

Human entries with polymorphisms or disease mutations

List of human entries with polymorphisms or disease mutations

Human chromosome 3

Human chromosome 3: entries, gene names and cross-references to MIM