CPLM 1.0 - Compendium of Protein Lysine Modification
TagContent
CPLM ID CPLM-012244
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
  
Created Date
 July 27, 2013 
Organism
 Homo sapiens (Human) 
NCBI Taxa ID
 9606 
Lysine Modification
Position
Peptide
Type
References
226EVELHNMKLVPVVNNubiquitination[1]
533HEDTTTDKLKLTLKLubiquitination[1]
671LPLEPCPKEQIAGLSubiquitination[2]
782YRKKRKGKLTLEDQAubiquitination[1, 2, 3, 4, 5]
793EDQATFIKKGVPIIFubiquitination[1, 2, 3, 4, 5, 6, 7]
794DQATFIKKGVPIIFAubiquitination[1, 2, 7]
808ADELDDSKPPPSSSMubiquitination[1, 2, 7, 8]
Reference
 [1] Systematic and quantitative assessment of the ubiquitin-modified proteome.
 Kim W, Bennett EJ, Huttlin EL, Guo A, Li J, Possemato A, Sowa ME, Rad R, Rush J, Comb MJ, Harper JW, Gygi SP.
 Mol Cell. 2011 Oct 21;44(2):325-40. [PMID: 21906983]
 [2] Global identification of modular cullin-RING ligase substrates.
 Emanuele MJ, Elia AE, Xu Q, Thoma CR, Izhar L, Leng Y, Guo A, Chen YN, Rush J, Hsu PW, Yen HC, Elledge SJ.
 Cell. 2011 Oct 14;147(2):459-74. [PMID: 21963094]
 [3] A proteome-wide, quantitative survey of in vivo ubiquitylation sites reveals widespread regulatory roles.
 Wagner SA, Beli P, Weinert BT, Nielsen ML, Cox J, Mann M, Choudhary C.
 Mol Cell Proteomics. 2011 Oct;10(10):M111.013284. [PMID: 21890473]
 [4] Systems-wide analysis of ubiquitylation dynamics reveals a key role for PAF15 ubiquitylation in DNA-damage bypass.
 Povlsen LK, Beli P, Wagner SA, Poulsen SL, Sylvestersen KB, Poulsen JW, Nielsen ML, Bekker-Jensen S, Mailand N, Choudhary C.
 Nat Cell Biol. 2012 Oct;14(10):1089-98. [PMID: 23000965]
 [5] hCKSAAP_UbSite: improved prediction of human ubiquitination sites by exploiting amino acid pattern and properties.
 Chen Z, Zhou Y, Song J, Zhang Z.
 Biochim Biophys Acta. 2013 Aug;1834(8):1461-7. [PMID: 23603789]
 [6] Mass spectrometric analysis of lysine ubiquitylation reveals promiscuity at site level.
 Danielsen JM, Sylvestersen KB, Bekker-Jensen S, Szklarczyk D, Poulsen JW, Horn H, Jensen LJ, Mailand N, Nielsen ML.
 Mol Cell Proteomics. 2011 Mar;10(3):M110.003590. [PMID: 21139048]
 [7] Landscape of the PARKIN-dependent ubiquitylome in response to mitochondrial depolarization.
 Sarraf SA, Raman M, Guarani-Pereira V, Sowa ME, Huttlin EL, Gygi SP, Harper JW.
 Nature. 2013 Apr 18;496(7445):372-6. [PMID: 23503661]
 [8] Ubiquitin ligase substrate identification through quantitative proteomics at both the protein and peptide levels.
 Lee KA, Hammerle LP, Andrews PS, Stokes MP, Mustelin T, Silva JC, Black RA, Doedens JR.
 J Biol Chem. 2011 Dec 2;286(48):41530-8. [PMID: 21987572] 
Functional Description
 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. 
Sequence Annotation
 DOMAIN 500 733 Peptidase S72.
 REGION 30 408 Required for laminin recognition.
 REGION 169 200 O-glycosylated at one site.
 REGION 316 485 Mucin-like domain.
 REGION 463 485 O-glycosylated at seven sites with
 REGION 819 895 Required for interaction with CAV3.
 REGION 880 895 Required for binding DMD and UTRN.
 MOTIF 776 782 Nuclear localization signal.
 MOTIF 889 892 PPXY motif.
 MOD_RES 892 892 Phosphotyrosine; by SRC.
 CARBOHYD 63 63 O-linked (GalNAc...).
 CARBOHYD 141 141 N-linked (GlcNAc...) (Potential).
 CARBOHYD 367 367 O-linked (Hex...).
 CARBOHYD 369 369 O-linked (Hex...).
 CARBOHYD 372 372 O-linked (Hex...).
 CARBOHYD 379 379 O-linked (Man6P...).
 CARBOHYD 381 381 O-linked (Hex...).
 CARBOHYD 388 388 O-linked (Hex...).
 CARBOHYD 455 455 O-linked (GalNAc...).
 CARBOHYD 641 641 N-linked (GlcNAc...) (Potential).
 CARBOHYD 649 649 N-linked (GlcNAc...) (Potential).
 CARBOHYD 661 661 N-linked (GlcNAc...) (Potential).
 DISULFID 182 264 Potential.
 DISULFID 669 713 Potential.  
Keyword
 3D-structure; Cell junction; Cell membrane; Complete proteome; Cytoplasm; Cytoskeleton; Disease mutation; Disulfide bond; Glycoprotein; Host cell receptor for virus entry; Host-virus interaction; Limb-girdle muscular dystrophy; Membrane; Nucleus; Phosphoprotein; Polymorphism; Postsynaptic cell membrane; Receptor; Reference proteome; Secreted; Signal; Synapse; Transmembrane; Transmembrane helix. 
Sequence Source
 UniProt (SWISSPROT/TrEMBL); GenBank; EMBL 
Protein Length
 895 AA 
Protein Sequence
MRMSVGLSLL LPLSGRTFLL LLSVVMAQSH WPSEPSEAVR DWENQLEASM HSVLSDLHEA 60
VPTVVGIPDG TAVVGRSFRV TIPTDLIASS GDIIKVSAAG KEALPSWLHW DSQSHTLEGL 120
PLDTDKGVHY ISVSATRLGA NGSHIPQTSS VFSIEVYPED HSELQSVRTA SPDPGEVVSS 180
ACAADEPVTV LTVILDADLT KMTPKQRIDL LHRMRSFSEV ELHNMKLVPV VNNRLFDMSA 240
FMAGPGNAKK VVENGALLSW KLGCSLNQNS VPDIHGVEAP AREGAMSAQL GYPVVGWHIA 300
NKKPPLPKRV RRQIHATPTP VTAIGPPTTA IQEPPSRIVP TPTSPAIAPP TETMAPPVRD 360
PVPGKPTVTI RTRGAIIQTP TLGPIQPTRV SEAGTTVPGQ IRPTMTIPGY VEPTAVATPP 420
TTTTKKPRVS TPKPATPSTD STTTTTRRPT KKPRTPRPVP RVTTKVSITR LETASPPTRI 480
RTTTSGVPRG GEPNQRPELK NHIDRVDAWV GTYFEVKIPS DTFYDHEDTT TDKLKLTLKL 540
REQQLVGEKS WVQFNSNSQL MYGLPDSSHV GKHEYFMHAT DKGGLSAVDA FEIHVHRRPQ 600
GDRAPARFKA KFVGDPALVL NDIHKKIALV KKLAFAFGDR NCSTITLQNI TRGSIVVEWT 660
NNTLPLEPCP KEQIAGLSRR IAEDDGKPRP AFSNALEPDF KATSITVTGS GSCRHLQFIP 720
VVPPRRVPSE APPTEVPDRD PEKSSEDDVY LHTVIPAVVV AAILLIAGII AMICYRKKRK 780
GKLTLEDQAT FIKKGVPIIF ADELDDSKPP PSSSMPLILQ EEKAPLPPPE YPNQSVPETT 840
PLNQDTMGEY TPLRDEDPNA PPYQPPPPFT APMEGKGSRP KNMTPYRSPP PYVPP 895 
Gene Ontology
 GO:0005604; C:basement membrane; IDA:UniProtKB.
 GO:0030054; C:cell junction; IEA:UniProtKB-KW.
 GO:0009279; C:cell outer membrane; IEA:Compara.
 GO:0070938; C:contractile ring; IDA:UniProtKB.
 GO:0005737; C:cytoplasm; IDA:UniProtKB.
 GO:0005856; C:cytoskeleton; IEA:UniProtKB-SubCell.
 GO:0016011; C:dystroglycan complex; IEA:Compara.
 GO:0016010; C:dystrophin-associated glycoprotein complex; IDA:UniProtKB.
 GO:0005615; C:extracellular space; IDA:UniProtKB.
 GO:0030175; C:filopodium; IDA:UniProtKB.
 GO:0016021; C:integral to membrane; IDA:UniProtKB.
 GO:0030027; C:lamellipodium; IDA:UniProtKB.
 GO:0045121; C:membrane raft; IEA:Compara.
 GO:0033268; C:node of Ranvier; IEA:Compara.
 GO:0005654; C:nucleoplasm; IDA:UniProtKB.
 GO:0045211; C:postsynaptic membrane; IEA:UniProtKB-SubCell.
 GO:0042383; C:sarcolemma; IEA:UniProtKB-SubCell.
 GO:0003779; F:actin binding; IDA:UniProtKB.
 GO:0051393; F:alpha-actinin binding; IDA:UniProtKB.
 GO:0005509; F:calcium ion binding; IEA:InterPro.
 GO:0043237; F:laminin-1 binding; ISS:UniProtKB.
 GO:0042169; F:SH2 domain binding; IDA:UniProtKB.
 GO:0008307; F:structural constituent of muscle; IMP:UniProtKB.
 GO:0015631; F:tubulin binding; IDA:UniProtKB.
 GO:0060445; P:branching involved in salivary gland morphogenesis; IEA:Compara.
 GO:0007016; P:cytoskeletal anchoring at plasma membrane; IMP:UniProtKB.
 GO:0060441; P:epithelial tube branching involved in lung morphogenesis; IEA:Compara.
 GO:0006509; P:membrane protein ectodomain proteolysis; IDA:UniProtKB.
 GO:0034453; P:microtubule anchoring; IMP:UniProtKB.
 GO:0002011; P:morphogenesis of an epithelial sheet; IEA:Compara.
 GO:0022011; P:myelination in peripheral nervous system; IEA:Compara.
 GO:0030336; P:negative regulation of cell migration; IMP:UniProtKB.
 GO:0043409; P:negative regulation of MAPK cascade; IMP:UniProtKB.
 GO:0051898; P:negative regulation of protein kinase B signaling cascade; IMP:UniProtKB.
 GO:0021682; P:nerve maturation; IEA:Compara.
 GO:0006607; P:NLS-bearing substrate import into nucleus; IDA:UniProtKB.
 GO:0019048; P:virus-host interaction; IDA:UniProtKB. 
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