DAG1_HUMAN - dbPTM
DAG1_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID DAG1_HUMAN
UniProt AC Q14118
Protein Name Dystroglycan
Gene Name DAG1
Organism Homo sapiens (Human).
Sequence Length 895
Subcellular Localization Alpha-dystroglycan: Secreted, extracellular space.
Beta-dystroglycan: Cell membrane
Single-pass type I membrane protein. Cytoplasm, cytoskeleton. Nucleus, nucleoplasm. Cell membrane, sarcolemma. Cell junction, synapse, postsynaptic cell membrane. T
Protein 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.; 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]
Protein Sequence MRMSVGLSLLLPLSGRTFLLLLSVVMAQSHWPSEPSEAVRDWENQLEASMHSVLSDLHEAVPTVVGIPDGTAVVGRSFRVTIPTDLIASSGDIIKVSAAGKEALPSWLHWDSQSHTLEGLPLDTDKGVHYISVSATRLGANGSHIPQTSSVFSIEVYPEDHSELQSVRTASPDPGEVVSSACAADEPVTVLTVILDADLTKMTPKQRIDLLHRMRSFSEVELHNMKLVPVVNNRLFDMSAFMAGPGNAKKVVENGALLSWKLGCSLNQNSVPDIHGVEAPAREGAMSAQLGYPVVGWHIANKKPPLPKRVRRQIHATPTPVTAIGPPTTAIQEPPSRIVPTPTSPAIAPPTETMAPPVRDPVPGKPTVTIRTRGAIIQTPTLGPIQPTRVSEAGTTVPGQIRPTMTIPGYVEPTAVATPPTTTTKKPRVSTPKPATPSTDSTTTTTRRPTKKPRTPRPVPRVTTKVSITRLETASPPTRIRTTTSGVPRGGEPNQRPELKNHIDRVDAWVGTYFEVKIPSDTFYDHEDTTTDKLKLTLKLREQQLVGEKSWVQFNSNSQLMYGLPDSSHVGKHEYFMHATDKGGLSAVDAFEIHVHRRPQGDRAPARFKAKFVGDPALVLNDIHKKIALVKKLAFAFGDRNCSTITLQNITRGSIVVEWTNNTLPLEPCPKEQIAGLSRRIAEDDGKPRPAFSNALEPDFKATSITVTGSGSCRHLQFIPVVPPRRVPSEAPPTEVPDRDPEKSSEDDVYLHTVIPAVVVAAILLIAGIIAMICYRKKRKGKLTLEDQATFIKKGVPIIFADELDDSKPPPSSSMPLILQEEKAPLPPPEYPNQSVPETTPLNQDTMGEYTPLRDEDPNAPPYQPPPPFTAPMEGKGSRPKNMTPYRSPPPYVPP
Overview of Protein Modification Sites with Functional and Structural Information
Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations Modification Substrate Peptides
&
Secondary Structure		 ASA (%) Reference Orthologous
Protein Cluster
14PhosphorylationLSLLLPLSGRTFLLL
HHHHEECCHHHHHHH		25.0430257219
63O-linked_GlycosylationDLHEAVPTVVGIPDG
HHHHHCCEEEECCCC		22.6423234360
130PhosphorylationDTDKGVHYISVSATR
CCCCCCEEEEEEEEE		7.77-
141N-linked_GlycosylationSATRLGANGSHIPQT
EEEECCCCCCCCCCC		51.18UniProtKB CARBOHYD
216PhosphorylationDLLHRMRSFSEVELH
HHHHHCCCCCCEEEC		24.6323312004
218PhosphorylationLHRMRSFSEVELHNM
HHHCCCCCCEEECCC		41.8123312004
226UbiquitinationEVELHNMKLVPVVNN
CEEECCCEEEEEECC		52.2121906983
317O-linked_GlycosylationVRRQIHATPTPVTAI
HHHHHCCCCCCCEEE		17.3421987822
319O-linked_GlycosylationRQIHATPTPVTAIGP
HHHCCCCCCCEEECC		26.4921987822
343O-linked_GlycosylationSRIVPTPTSPAIAPP
CCCCCCCCCCCCCCC		50.23OGP
353O-linked_GlycosylationAIAPPTETMAPPVRD
CCCCCCCCCCCCCCC		22.55OGP
367O-linked_GlycosylationDPVPGKPTVTIRTRG
CCCCCCCEEEEEECC		33.4955829823
369PhosphorylationVPGKPTVTIRTRGAI
CCCCCEEEEEECCEE		13.7624719451
369O-linked_GlycosylationVPGKPTVTIRTRGAI
CCCCCEEEEEECCEE		13.7655829829
372O-linked_GlycosylationKPTVTIRTRGAIIQT
CCEEEEEECCEEEEC		29.6020507882
379O-linked_GlycosylationTRGAIIQTPTLGPIQ
ECCEEEECCCCCCCC		14.0820044576
381O-linked_GlycosylationGAIIQTPTLGPIQPT
CEEEECCCCCCCCCE		47.9720044576
388O-linked_GlycosylationTLGPIQPTRVSEAGT
CCCCCCCEEEECCCC		27.5920044576
404PhosphorylationVPGQIRPTMTIPGYV
CCCEECCCEEECCCC		19.6624719451
406PhosphorylationGQIRPTMTIPGYVEP
CEECCCEEECCCCCC		26.8824719451
410PhosphorylationPTMTIPGYVEPTAVA
CCEEECCCCCCCEEE		9.0424719451
414PhosphorylationIPGYVEPTAVATPPT
ECCCCCCCEEECCCC		21.9128634298
430O-linked_GlycosylationTTKKPRVSTPKPATP
CCCCCCCCCCCCCCC		40.0355829143
431O-linked_GlycosylationTKKPRVSTPKPATPS
CCCCCCCCCCCCCCC		32.2655829149
433UbiquitinationKPRVSTPKPATPSTD
CCCCCCCCCCCCCCC		47.58-
436O-linked_GlycosylationVSTPKPATPSTDSTT
CCCCCCCCCCCCCCC		26.7155829155
436PhosphorylationVSTPKPATPSTDSTT
CCCCCCCCCCCCCCC		26.7122210691
438O-linked_GlycosylationTPKPATPSTDSTTTT
CCCCCCCCCCCCCCC		40.2655829161
439O-linked_GlycosylationPKPATPSTDSTTTTT
CCCCCCCCCCCCCCC		34.8655829167
441O-linked_GlycosylationPATPSTDSTTTTTRR
CCCCCCCCCCCCCCC		27.9555829173
442O-linked_GlycosylationATPSTDSTTTTTRRP
CCCCCCCCCCCCCCC		30.8555829179
443O-linked_GlycosylationTPSTDSTTTTTRRPT
CCCCCCCCCCCCCCC		26.5455829183
444PhosphorylationPSTDSTTTTTRRPTK
CCCCCCCCCCCCCCC		26.6822210691
444O-linked_GlycosylationPSTDSTTTTTRRPTK
CCCCCCCCCCCCCCC		26.6855829189
445PhosphorylationSTDSTTTTTRRPTKK
CCCCCCCCCCCCCCC		19.0622210691
445O-linked_GlycosylationSTDSTTTTTRRPTKK
CCCCCCCCCCCCCCC		19.0655829195
446O-linked_GlycosylationTDSTTTTTRRPTKKP
CCCCCCCCCCCCCCC		23.6955829201
450O-linked_GlycosylationTTTTRRPTKKPRTPR
CCCCCCCCCCCCCCC		50.3055829207
455O-linked_GlycosylationRPTKKPRTPRPVPRV
CCCCCCCCCCCCCCE		31.9820507882
463O-linked_GlycosylationPRPVPRVTTKVSITR
CCCCCCEEEEEEEEE		23.3723301498
463PhosphorylationPRPVPRVTTKVSITR
CCCCCCEEEEEEEEE		23.37-
464O-linked_GlycosylationRPVPRVTTKVSITRL
CCCCCEEEEEEEEEE		26.9623301498
464PhosphorylationRPVPRVTTKVSITRL
CCCCCEEEEEEEEEE		26.96-
467PhosphorylationPRVTTKVSITRLETA
CCEEEEEEEEEEEEC		21.5724719451
469PhosphorylationVTTKVSITRLETASP
EEEEEEEEEEEECCC		22.99-
469O-linked_GlycosylationVTTKVSITRLETASP
EEEEEEEEEEEECCC		22.9946195193
473PhosphorylationVSITRLETASPPTRI
EEEEEEEECCCCCEE		36.7124719451
473O-linked_GlycosylationVSITRLETASPPTRI
EEEEEEEECCCCCEE		36.7155824173
475PhosphorylationITRLETASPPTRIRT
EEEEEECCCCCEEEE		38.5420068231
475O-linked_GlycosylationITRLETASPPTRIRT
EEEEEECCCCCEEEE		38.5455824179
478PhosphorylationLETASPPTRIRTTTS
EEECCCCCEEEECCC		41.9520068231
478O-linked_GlycosylationLETASPPTRIRTTTS
EEECCCCCEEEECCC		41.9546195199
482PhosphorylationSPPTRIRTTTSGVPR
CCCCEEEECCCCCCC		31.8620068231
482O-linked_GlycosylationSPPTRIRTTTSGVPR
CCCCEEEECCCCCCC		31.8655835679
483O-linked_GlycosylationPPTRIRTTTSGVPRG
CCCEEEECCCCCCCC		14.7655835685
483PhosphorylationPPTRIRTTTSGVPRG
CCCEEEECCCCCCCC		14.7620068231
484O-linked_GlycosylationPTRIRTTTSGVPRGG
CCEEEECCCCCCCCC		23.9155835691
484PhosphorylationPTRIRTTTSGVPRGG
CCEEEECCCCCCCCC		23.9120068231
485PhosphorylationTRIRTTTSGVPRGGE
CEEEECCCCCCCCCC		35.3820068231
485O-linked_GlycosylationTRIRTTTSGVPRGGE
CEEEECCCCCCCCCC		35.3836016953
512PhosphorylationRVDAWVGTYFEVKIP
HHHHEEECEEEEECC		18.5421406692
513PhosphorylationVDAWVGTYFEVKIPS
HHHEEECEEEEECCC		7.5721406692
520PhosphorylationYFEVKIPSDTFYDHE
EEEEECCCCCCCCCC		53.40-
531O-linked_GlycosylationYDHEDTTTDKLKLTL
CCCCCCCCCHHHEEE		32.98OGP
533UbiquitinationHEDTTTDKLKLTLKL
CCCCCCCHHHEEEEH		45.4921906983
5332-HydroxyisobutyrylationHEDTTTDKLKLTLKL
CCCCCCCHHHEEEEH		45.49-
537PhosphorylationTTDKLKLTLKLREQQ
CCCHHHEEEEHHHHH		21.9124719451
575PhosphorylationSHVGKHEYFMHATDK
CCCCCCEEEEEEECC		13.11-
580O-linked_GlycosylationHEYFMHATDKGGLSA
CEEEEEEECCCCCCE		24.46OGP
611UbiquitinationAPARFKAKFVGDPAL
CCHHHEEEECCCHHH		40.97-
625UbiquitinationLVLNDIHKKIALVKK
HHHHHHHHHHHHHHH		46.32-
626MethylationVLNDIHKKIALVKKL
HHHHHHHHHHHHHHH		21.03-
641N-linked_GlycosylationAFAFGDRNCSTITLQ
HHHHCCCCCEEEEEE		28.9117660510
649N-linked_GlycosylationCSTITLQNITRGSIV
CEEEEEEECCCCCEE		40.4917660510
661N-linked_GlycosylationSIVVEWTNNTLPLEP
CEEEEECCCCCCCCC		40.3318764929
671UbiquitinationLPLEPCPKEQIAGLS
CCCCCCCHHHHHCHH		69.81-
687UbiquitinationRIAEDDGKPRPAFSN
HHHCCCCCCCCCCCC		44.86-
729O-linked_GlycosylationVPPRRVPSEAPPTEV
CCCCCCCCCCCCCCC		43.4655829713
734O-linked_GlycosylationVPSEAPPTEVPDRDP
CCCCCCCCCCCCCCC		48.8655829719
780UbiquitinationICYRKKRKGKLTLED
HHHHHCCCCCCCHHH		70.09-
782UbiquitinationYRKKRKGKLTLEDQA
HHHCCCCCCCHHHHH		41.1421906983
784PhosphorylationKKRKGKLTLEDQATF
HCCCCCCCHHHHHHH		31.4225159151
790PhosphorylationLTLEDQATFIKKGVP
CCHHHHHHHHHCCCC		21.9119664994
793UbiquitinationEDQATFIKKGVPIIF
HHHHHHHHCCCCEEE		39.0021906983
7932-HydroxyisobutyrylationEDQATFIKKGVPIIF
HHHHHHHHCCCCEEE		39.00-
794UbiquitinationDQATFIKKGVPIIFA
HHHHHHHCCCCEEEC		61.3921906983
807PhosphorylationFADELDDSKPPPSSS
ECCCCCCCCCCCCCC		46.8826657352
808UbiquitinationADELDDSKPPPSSSM
CCCCCCCCCCCCCCC		69.4121906983
812PhosphorylationDDSKPPPSSSMPLIL
CCCCCCCCCCCCEEE		40.6025849741
813PhosphorylationDSKPPPSSSMPLILQ
CCCCCCCCCCCEEEE		36.1126657352
814PhosphorylationSKPPPSSSMPLILQE
CCCCCCCCCCEEEEE		28.8525849741
863PhosphorylationEDPNAPPYQPPPPFT
CCCCCCCCCCCCCCC		32.3722817900
881UbiquitinationEGKGSRPKNMTPYRS
CCCCCCCCCCCCCCC		59.23-
884PhosphorylationGSRPKNMTPYRSPPP
CCCCCCCCCCCCCCC		26.9321945579
884O-linked_GlycosylationGSRPKNMTPYRSPPP
CCCCCCCCCCCCCCC		26.9330379171
886PhosphorylationRPKNMTPYRSPPPYV
CCCCCCCCCCCCCCC		17.9821945579
888PhosphorylationKNMTPYRSPPPYVPP
CCCCCCCCCCCCCCC		35.6021945579
892PhosphorylationPYRSPPPYVPP----
CCCCCCCCCCC----		31.2221945579
Upstream regulatory proteins (kinases for phosphorylation sites, E3 ubiquitin ligases of ubiquitination sites, ...)
Modified Location Modified Residue Modification Type of Upstream Proteins Gene Name of Upstream Proteins UniProt AC of Upstream Proteins Sources
892YPhosphorylationKinaseSRCP12931
Uniprot
892YPhosphorylationKinaseSRC64-PhosphoELM
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference
317TAcetylation

21987822
317TGlycosylation

21987822
317TPhosphorylation

21987822
319TAcetylation

21987822
319TGlycosylation

21987822
319TPhosphorylation

21987822
379TAcetylation

20044576
379TGlycosylation

20044576
379TPhosphorylation

20044576
Disease-associated PTM Sites based on SAP

* Distance = the distance between SAP position and PTM sites.

Modified Location Modification Variant Position
(Distance <= 10) 		Residue Change SAP Related Disease Reference

Oops, there are no SNP-PTM records of DAG1_HUMAN !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
GRB2_HUMANGRB2physical
7744812
CAV3_HUMANCAV3physical
10988290
SRC_HUMANSRCphysical
11724572
FYN_HUMANFYNphysical
11724572
CSK_HUMANCSKphysical
11724572
NCK1_HUMANNCK1physical
11724572
SHC1_HUMANSHC1physical
11724572
CAV1_HUMANCAV1physical
11724572
AGRIN_HUMANAGRNphysical
8205617
UTRO_HUMANUTRNphysical
10769203
LAMA2_HUMANLAMA2physical
7925941
LAMA5_HUMANLAMA5physical
10207021
TBA1A_HUMANTUBA1Aphysical
18341635
ACTN1_HUMANACTN1physical
18341635
MTAP2_HUMANMAP2physical
18341635
ITB1_HUMANITGB1physical
18341635
Drug and Disease Associations
Kegg Disease
H00593 Limb-girdle muscular dystrophy (LGMD)
OMIM Disease
613818Muscular dystrophy-dystroglycanopathy limb-girdle C9 (MDDGC9)
Kegg Drug
There are no disease associations of PTM sites.
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of DAG1_HUMAN

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Related Literatures of Post-Translational Modification
O-linked Glycosylation
ReferencePubMed
"Characterization of site-specific O-glycan structures within themucin-like domain of {alpha}-dystroglycan from human skeletalmuscle.";
Nilsson J., Nilsson J., Larson G., Grahn A.;
Glycobiology 20:1160-1169(2010).
Cited for: STRUCTURE OF CARBOHYDRATES, MASS SPECTROMETRY, AND GLYCOSYLATION ATTHR-367; THR-369; THR-372 AND THR-455.
"O-mannosyl phosphorylation of alpha-dystroglycan is required forlaminin 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).
Cited for: MASS SPECTROMETRY, AND GLYCOSYLATION AT THR-379; THR-381 AND THR-388.
Phosphorylation
ReferencePubMed
"Characterization of an Importin alpha/beta-recognized nuclearlocalization 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).
Cited for: PHOSPHORYLATION AT TYR-892, NUCLEAR LOCALIZATION SIGNAL, SUBCELLULARLOCATION, AND MUTAGENESIS OF 777-LYS--LYS-782 AND TYR-892.
"Localization of phospho-beta-dystroglycan (pY892) to an intracellularvesicular compartment in cultured cells and skeletal muscle fibers invivo.";
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).
Cited for: PHOSPHORYLATION AT TYR-892, SUBCELLULAR LOCATION, AND MUTAGENESIS OFTYR-892.
"The interaction of dystrophin with beta-dystroglycan is regulated bytyrosine phosphorylation.";
Ilsley J.L., Sudol M., Winder S.J.;
Cell. Signal. 13:625-632(2001).
Cited for: PHOSPHORYLATION AT TYR-892, AND INTERACTION WITH DMD.

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