CPLM 1.0 - Compendium of Protein Lysine Modification
TagContent
CPLM ID CPLM-014403
UniProt Accession
Genbank Protein ID
Genbank Nucleotide ID
Protein Name
 Dystroglycan 
Protein Synonyms/Alias
 Dystrophin-associated glycoprotein 1; Alpha-dystroglycan; Alpha-DG; Beta-dystroglycan; Beta-DG 
Gene Name
 Dag1 
Gene Synonyms/Alias
 Dag-1 
Created Date
 July 27, 2013 
Organism
 Mus musculus (Mouse) 
NCBI Taxa ID
 10090 
Lysine Modification
Position
Peptide
Type
References
630KKIALVKKLAFAFGDacetylation[1]
778ICYRKKRKGKLTLEDubiquitination[2]
780YRKKRKGKLTLEDQAubiquitination[2]
791EDQATFIKKGVPIIFubiquitination[2]
792DQATFIKKGVPIIFAubiquitination[2]
806ADELDDSKPPPSSSMubiquitination[2]
Reference
 [1] Quantitative acetylome analysis reveals the roles of SIRT1 in regulating diverse substrates and cellular pathways.
 Chen Y, Zhao W, Yang JS, Cheng Z, Luo H, Lu Z, Tan M, Gu W, Zhao Y.
 Mol Cell Proteomics. 2012 Oct;11(10):1048-62. [PMID: 22826441]
 [2] Proteomic analyses reveal divergent ubiquitylation site patterns in murine tissues.
 Wagner SA, Beli P, Weinert BT, Schölz C, Kelstrup CD, Young C, Nielsen ML, Olsen JV, Brakebusch C, Choudhary C.
 Mol Cell Proteomics. 2012 Dec;11(12):1578-85. [PMID: 22790023] 
Functional Description
 The dystroglycan complex is involved in a number of processes including laminin and basement membrane assembly, sacrolemmal stability, cell survival, peripheral nerve myelination, nodal structure, cell migration, and epithelial polarization. 
Sequence Annotation
 DOMAIN 498 731 Peptidase S72.
 REGION 28 406 Required for laminin recognition (By
 REGION 47 69 O-glycosylated at one site (By
 REGION 314 483 Mucin-like domain (By similarity).
 REGION 461 483 O-glycosylated at seven sites with GalNAc
 REGION 817 893 Required for interaction with CAV3 (By
 REGION 878 893 Required for binding DMD and UTRN (By
 MOTIF 774 780 Nuclear localization signal (By
 MOTIF 887 890 PPXY motif (By similarity).
 MOD_RES 890 890 Phosphotyrosine; by SRC (By similarity).
 CARBOHYD 139 139 N-linked (GlcNAc...) (Potential).
 CARBOHYD 377 377 O-linked (Man6P...) (By similarity).
 CARBOHYD 639 639 N-linked (GlcNAc...) (Potential).
 CARBOHYD 647 647 N-linked (GlcNAc...) (Potential).
 CARBOHYD 659 659 N-linked (GlcNAc...) (Potential).
 DISULFID 180 262
 DISULFID 667 711 Potential.  
Keyword
 3D-structure; Cell junction; Cell membrane; Complete proteome; Cytoplasm; Cytoskeleton; Disulfide bond; Glycoprotein; Host-virus interaction; Membrane; Nucleus; Phosphoprotein; Postsynaptic cell membrane; Reference proteome; Secreted; Signal; Synapse; Transmembrane; Transmembrane helix. 
Sequence Source
 UniProt (SWISSPROT/TrEMBL); GenBank; EMBL 
Protein Length
 893 AA 
Protein Sequence
MSVDNWLLHP LWGQTFLLLL SVAVAQAHWP SEPSEAVRDW KNQLEASMHS VLSDFQEAVP 60
TVVGIPDGTA VVGRSFRVSI PTDLIASSGE IIKVSAAGKE ALPSWLHWDP HSHILEGLPL 120
DTDKGVHYIS VSAARLGANG SHVPQTSSVF SIEVYPEDHN EPQSVRAASS DPGEVVPSAC 180
AADEPVTVLT VILDADLTKM TPKQRIDLLN RMQSFSEVEL HNMKLVPVVN NRLFDMSAFM 240
AGPGNAKKVV ENGALLSWKL GCSLNQNSVP DIRGVETPAR EGAMSAQLGY PVVGWHIANK 300
KPTLPKRLRR QIHATPTPVT AIGPPTTAIQ EPPSRIVPTP TSPAIAPPTE TMAPPVRDPV 360
PGKPTVTIRT RGAIIQTPTL GPIQPTRVSE AGTTVPGQIR PTLTIPGYVE PTAVITPPTT 420
TTKKPRVSTP KPATPSTDSS TTTTRRPTKK PRTPRPVPRV TTKAPITRLE TASPPTRIRT 480
TTSGVPRGGE PNQRPELKNH IDRVDAWVGT YFEVKIPSDT FYDNEDTTTD KLKLTLKLRE 540
QQLVGEKSWV QFNSNSQLMY GLPDSSHVGK HEYFMHATDK GGLSAVDAFE IHVHKRPQGD 600
KAPARFKARL AGDPAPVVND IHKKIALVKK LAFAFGDRNC SSITLQNITR GSIVVEWTNN 660
TLPLEPCPKE QIIGLSRRIA DENGKPRPAF SNALEPDFKA LSIAVTGSGS CRHLQFIPVA 720
PPSPGSSAAP ATEVPDRDPE KSSEDDVYLH TVIPAVVVAA ILLIAGIIAM ICYRKKRKGK 780
LTLEDQATFI KKGVPIIFAD ELDDSKPPPS SSMPLILQEE KAPLPPPEYP NQSMPETTPL 840
NQDTVGEYTP LRDEDPNAPP YQPPPPFTAP MEGKGSRPKN MTPYRSPPPY VPP 893 
Gene Ontology
 GO:0005604; C:basement membrane; IDA:MGI.
 GO:0009279; C:cell outer membrane; IDA:UniProtKB.
 GO:0070938; C:contractile ring; IEA:Compara.
 GO:0005737; C:cytoplasm; IEA:UniProtKB-KW.
 GO:0005856; C:cytoskeleton; IEA:UniProtKB-SubCell.
 GO:0016011; C:dystroglycan complex; IDA:MGI.
 GO:0005615; C:extracellular space; IEA:UniProtKB-SubCell.
 GO:0030175; C:filopodium; IEA:Compara.
 GO:0005925; C:focal adhesion; IEA:Compara.
 GO:0016021; C:integral to membrane; IEA:UniProtKB-KW.
 GO:0030027; C:lamellipodium; IEA:Compara.
 GO:0045121; C:membrane raft; IDA:MGI.
 GO:0033268; C:node of Ranvier; IMP:UniProtKB.
 GO:0005654; C:nucleoplasm; IEA:UniProtKB-SubCell.
 GO:0045211; C:postsynaptic membrane; IEA:UniProtKB-SubCell.
 GO:0042383; C:sarcolemma; IDA:MGI.
 GO:0005509; F:calcium ion binding; IEA:InterPro.
 GO:0008307; F:structural constituent of muscle; IEA:Compara.
 GO:0071711; P:basement membrane organization; IMP:MGI.
 GO:0060445; P:branching involved in salivary gland morphogenesis; IMP:MGI.
 GO:0071679; P:commissural neuron axon guidance; IMP:MGI.
 GO:0007016; P:cytoskeletal anchoring at plasma membrane; IEA:InterPro.
 GO:0060441; P:epithelial tube branching involved in lung morphogenesis; IMP:MGI.
 GO:0006509; P:membrane protein ectodomain proteolysis; IEA:Compara.
 GO:0034453; P:microtubule anchoring; IEA:Compara.
 GO:0002011; P:morphogenesis of an epithelial sheet; IMP:MGI.
 GO:0022011; P:myelination in peripheral nervous system; IMP:UniProtKB.
 GO:0030336; P:negative regulation of cell migration; IEA:Compara.
 GO:0043409; P:negative regulation of MAPK cascade; IEA:Compara.
 GO:0051898; P:negative regulation of protein kinase B signaling cascade; IEA:Compara.
 GO:0021682; P:nerve maturation; IMP:UniProtKB.
 GO:0006607; P:NLS-bearing substrate import into nucleus; IEA:Compara.
 GO:0019048; P:virus-host interaction; IEA:UniProtKB-KW. 
Interpro
 IPR027468; Alpha-dystroglycan_domain_2.
 IPR006644; Cadg.
 IPR015919; Cadherin-like.
 IPR008465; DAG1.
 IPR013783; Ig-like_fold. 
Pfam
 PF05454; DAG1 
SMART
 SM00736; CADG 
PROSITE
  
PRINTS