DAG1_MOUSE - PTM Information in dbPTM

Basic Information of Protein

• UniProt ID: DAG1_MOUSE
• UniProt AC: Q62165
• Protein Name: Dystroglycan
• Gene Name: Dag1
• Organism: Mus musculus (Mouse).
• Sequence Length: 893
• 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, sacrolemmal 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, and for certain adenoviruses. Receptor for laminin-2 (LAMA2) and agrin in peripheral nerve Schwann cells. Also receptor for lymphocytic choriomeningitis virus, Old World Lassa fever virus, and clade C New World arenaviruses.; 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 (By similarity)..
• Protein Sequence: MSVDNWLLHPLWGQTFLLLLSVAVAQAHWPSEPSEAVRDWKNQLEASMHSVLSDFQEAVPTVVGIPDGTAVVGRSFRVSIPTDLIASSGEIIKVSAAGKEALPSWLHWDPHSHILEGLPLDTDKGVHYISVSAARLGANGSHVPQTSSVFSIEVYPEDHNEPQSVRAASSDPGEVVPSACAADEPVTVLTVILDADLTKMTPKQRIDLLNRMQSFSEVELHNMKLVPVVNNRLFDMSAFMAGPGNAKKVVENGALLSWKLGCSLNQNSVPDIRGVETPAREGAMSAQLGYPVVGWHIANKKPTLPKRLRRQIHATPTPVTAIGPPTTAIQEPPSRIVPTPTSPAIAPPTETMAPPVRDPVPGKPTVTIRTRGAIIQTPTLGPIQPTRVSEAGTTVPGQIRPTLTIPGYVEPTAVITPPTTTTKKPRVSTPKPATPSTDSSTTTTRRPTKKPRTPRPVPRVTTKAPITRLETASPPTRIRTTTSGVPRGGEPNQRPELKNHIDRVDAWVGTYFEVKIPSDTFYDNEDTTTDKLKLTLKLREQQLVGEKSWVQFNSNSQLMYGLPDSSHVGKHEYFMHATDKGGLSAVDAFEIHVHKRPQGDKAPARFKARLAGDPAPVVNDIHKKIALVKKLAFAFGDRNCSSITLQNITRGSIVVEWTNNTLPLEPCPKEQIIGLSRRIADENGKPRPAFSNALEPDFKALSIAVTGSGSCRHLQFIPVAPPSPGSSAAPATEVPDRDPEKSSEDDVYLHTVIPAVVVAAILLIAGIIAMICYRKKRKGKLTLEDQATFIKKGVPIIFADELDDSKPPPSSSMPLILQEEKAPLPPPEYPNQSMPETTPLNQDTVGEYTPLRDEDPNAPPYQPPPPFTAPMEGKGSRPKNMTPYRSPPPYVPP

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
75	Phosphorylation	GTAVVGRSFRVSIPT CCEEECCEEEEECCC	16.10	24719451
139	N-linked_Glycosylation	SAARLGANGSHVPQT EEEECCCCCCCCCCC	51.18	-
315	O-linked_Glycosylation	LRRQIHATPTPVTAI HHHHHHCCCCCCEEE	17.34	-
315	Phosphorylation	LRRQIHATPTPVTAI HHHHHHCCCCCCEEE	17.34	21987822
317	O-linked_Glycosylation	RQIHATPTPVTAIGP HHHHCCCCCCEEECC	26.49	-
317	Phosphorylation	RQIHATPTPVTAIGP HHHHCCCCCCEEECC	26.49	21987822
334	Phosphorylation	TAIQEPPSRIVPTPT CCCCCCCCCCCCCCC	45.41	-
377	O-linked_Glycosylation	TRGAIIQTPTLGPIQ ECCEEEECCCCCCCC	14.08	-
630	Acetylation	KKIALVKKLAFAFGD HHHHHHHHHHHHHCC	37.25	22826441
639	N-linked_Glycosylation	AFAFGDRNCSSITLQ HHHHCCCCCCEEEEE	34.46	-
647	N-linked_Glycosylation	CSSITLQNITRGSIV CCEEEEEECCCCCEE	40.49	-
659	N-linked_Glycosylation	SIVVEWTNNTLPLEP CEEEEECCCCCCCCC	40.33	-
778	Ubiquitination	ICYRKKRKGKLTLED HHHHHCCCCCCCHHH	70.09	-
780	Ubiquitination	YRKKRKGKLTLEDQA HHHCCCCCCCHHHHH	41.14	-
788	Phosphorylation	LTLEDQATFIKKGVP CCHHHHHHHHHCCCC	21.91	26824392
791	Ubiquitination	EDQATFIKKGVPIIF HHHHHHHHCCCCEEE	39.00	-
792	Ubiquitination	DQATFIKKGVPIIFA HHHHHHHCCCCEEEC	61.39	-
805	Phosphorylation	FADELDDSKPPPSSS ECCCCCCCCCCCCCC	46.88	23737553
806	Ubiquitination	ADELDDSKPPPSSSM CCCCCCCCCCCCCCC	69.41	-
810	Phosphorylation	DDSKPPPSSSMPLIL CCCCCCCCCCCCEEE	40.60	26239621
811	Phosphorylation	DSKPPPSSSMPLILQ CCCCCCCCCCCEEEE	36.11	26239621
812	Phosphorylation	SKPPPSSSMPLILQE CCCCCCCCCCEEEEE	28.85	26824392
882	Phosphorylation	GSRPKNMTPYRSPPP CCCCCCCCCCCCCCC	26.93	24759943
884	Phosphorylation	RPKNMTPYRSPPPYV CCCCCCCCCCCCCCC	17.98	24759943
886	Phosphorylation	KNMTPYRSPPPYVPP CCCCCCCCCCCCCCC	35.60	23608596
890	Phosphorylation	PYRSPPPYVPP---- CCCCCCCCCCC----	31.22	12795607

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
890	Y	Phosphorylation	Kinase	SRC	P12931	PSP
890	Y	Phosphorylation	Kinase	SRC	P05480	Uniprot

Functions of PTM Sites

Modified Location	Modified Residue	Modification	Function	Reference
315	T	Acetylation	In muscle, glycosylation on Thr-315, Thr-317, 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 (LARGE1) protein amd is required for laminin binding.	20044576
315	T	Glycosylation	In muscle, glycosylation on Thr-315, Thr-317, 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 (LARGE1) protein amd is required for laminin binding.	20044576
315	T	Phosphorylation	In muscle, glycosylation on Thr-315, Thr-317, 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 (LARGE1) protein amd is required for laminin binding.	20044576
317	T	Acetylation	In muscle, glycosylation on Thr-315, Thr-317, 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 (LARGE1) protein amd is required for laminin binding.	20044576
317	T	Glycosylation	In muscle, glycosylation on Thr-315, Thr-317, 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 (LARGE1) protein amd is required for laminin binding.	20044576
317	T	Phosphorylation	In muscle, glycosylation on Thr-315, Thr-317, 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 (LARGE1) protein amd is required for laminin binding.	20044576
379	T	Acetylation	In muscle, glycosylation on Thr-315, Thr-317, 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 (LARGE1) protein amd is required for laminin binding.	20044576
379	T	Glycosylation	In muscle, glycosylation on Thr-315, Thr-317, 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 (LARGE1) protein amd is required for laminin binding.	20044576
379	T	Phosphorylation	In muscle, glycosylation on Thr-315, Thr-317, 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 (LARGE1) protein amd is required for laminin binding.	20044576

Disease-associated PTM Sites based on SAP

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

Oops, there are no SNP-PTM records of DAG1_MOUSE !!

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference
SGCD_MOUSE	Sgcd	physical	9864373
SGCA_MOUSE	Sgca	physical	1461282
SGCB_MOUSE	Sgcb	physical	1461282
SGCD_MOUSE	Sgcd	physical	1461282

Drug and Disease Associations

• Kegg Drug
• DrugBank
• There are no disease associations of PTM sites.