Q14118

※ Protein Information

Tag	Content
UniProt Accession	DAG1_HUMAN; Q14118;
Entrez ID	1605
GenBank Protein ID	NM_001165928.3; NM_001177634.2; NM_001177635.2; NM_001177636.2; NM_001177637.2; NM_001177638.2; NM_001177639.2; NM_001177640.2; NM_001177641.2; NM_001177642.2; NM_001177643.2; NM_001177644.2; NM_004393.5;
GenBank Nucleotide ID	NP_001159400.2; NP_001171105.1; NP_001171106.1; NP_001171107.1; NP_001171108.1; NP_001171109.1; NP_001171110.1; NP_001171111.1; NP_001171112.1; NP_001171113.1; NP_001171114.1; NP_001171115.1; NP_004384.4;
Protein Name	Dystroglycan (Dystrophin-associated glycoprotein 1) [Cleaved into: Alpha-dystroglycan (Alpha-DG); Beta-dystroglycan (Beta-DG)]
Gene Name	DAG1
Organism	Homo sapiens
NCBI Taxa ID	9606
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.;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 c(view all) 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.;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, PubMed:19324387, PubMed:17360738). Alpha-dystroglycan acts as a Schwann cell receptor for Mycobacterium leprae, the causative organism of leprosy, but only in the presence of the G-domain of LAMA2 (PubMed:9851927).
Sequence (Fasta)	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 896 Fasta Sequence >Q14118\|DAG1\|Homo sapiens (Human) MRMSVGLSLLLPLSGRTFLLLLSVVMAQSHWPSEPSEAVRDWENQLEASMHSVLSDLHEAVPTVVGIPDGTAVVGRSFRVTIPTDLIASSGDIIKVSAAGKEALPSWLHWDSQSHTLEGLPLDTDKGVHYISVSATRLGANGSHIPQTSSVFSIEVYPEDHSELQSVRTASPDPGEVVSSACAADEPVTVLTVILDADLTKMTPKQRIDLLHRMRSFSEVELHNMKLVPVVNNRLFDMSAFMAGPGNAKKVVENGALLSWKLGCSLNQNSVPDIHGVEAPAREGAMSAQLGYPVVGWHIANKKPPLPKRVRRQIHATPTPVTAIGPPTTAIQEPPSRIVPTPTSPAIAPPTETMAPPVRDPVPGKPTVTIRTRGAIIQTPTLGPIQPTRVSEAGTTVPGQIRPTMTIPGYVEPTAVATPPTTTTKKPRVSTPKPATPSTDSTTTTTRRPTKKPRTPRPVPRVTTKVSITRLETASPPTRIRTTTSGVPRGGEPNQRPELKNHIDRVDAWVGTYFEVKIPSDTFYDHEDTTTDKLKLTLKLREQQLVGEKSWVQFNSNSQLMYGLPDSSHVGKHEYFMHATDKGGLSAVDAFEIHVHRRPQGDRAPARFKAKFVGDPALVLNDIHKKIALVKKLAFAFGDRNCSTITLQNITRGSIVVEWTNNTLPLEPCPKEQIAGLSRRIAEDDGKPRPAFSNALEPDFKATSITVTGSGSCRHLQFIPVVPPRRVPSEAPPTEVPDRDPEKSSEDDVYLHTVIPAVVVAAILLIAGIIAMICYRKKRKGKLTLEDQATFIKKGVPIIFADELDDSKPPPSSSMPLILQEEKAPLPPPEYPNQSVPETTPLNQDTMGEYTPLRDEDPNAPPYQPPPPFTAPMEGKGSRPKNMTPYRSPPPYVPP

※ PTM-Disease Association

Num	PTM	Disease	Cell Type	Type	PTM Site	PMID
1	Glycosylation	Renal cancer/carcinoma		P		3823392; 23970118
1	[Reference]: These results implicate VHL in the regulation of glycosylation and raise interesting questions regarding the extent and importance of such changes in RCC.

※ Disease Cross-ref Annotation

Database	Annotation
CTD (Curated) (count: 4)	MESH:D007835 ; Lassa Fever OMIM:613818 ; MUSCULAR DYSTROPHY-DYSTROGLYCANOPATHY (LIMB-GIRDLE), TYPE C, 9 MESH:D011471 ; Prostatic Neoplasms MESH:D058494 ; Walker-Warburg Syndrome
DisGeNet (Curated) (count: 57) (view all)	C0020255; Hydrocephalus C0020302; Hydrophthalmos C0023012; Language Delay C0023092; Lassa Fever C0023520; Leukodystrophy C0025362; Mental Retardation C0026010; Microphthalmos C0026827; Muscle hypotonia C0026850; Muscular Dystrophy C0027092; Myopia C0033578; Prostatic Neoplasms C0086543; Cataract C0151576; Elevated creatine kinase C0233715; Speech impairment C0234182; Gowers sign C0241005; Creatine phosphokinase serum increased C0241210; Speech Delay C0265221; Walker-Warburg congenital muscular dystrophy C0266464; Polymicrogyria C0270685; Cerebral calcification C0344482; Hypoplasia of corpus callosum C0423221; Globe of eye large C0423903; Low intelligence C0454644; Delayed speech and language development C0557874; Global developmental delay C0575071; Gowers sign present C0746940; nonverbal C0854723; Retinal Dystrophies C0917816; Mental deficiency C1145670; Respiratory Failure C1184923; Lumbar lordosis C1510497; Lens Opacities C1836038; Poor head control C1837407; Ankle contracture C1840379; Cerebellar vermis hypoplasia C1843367; Poor school performance C1847762; Cerebellar cyst C1848924; Infantile onset C1854882; Absent speech C1858127; Limb-girdle muscle weakness C1861403; Variable expressivity C1864711; Muscle biopsy shows dystrophic changes C1864897; Cognitive delay C1866862; Highly variable severity C3151184; MUSCULAR DYSTROPHY-DYSTROGLYCANOPATHY (LIMB-GIRDLE), TYPE C, 9 C3278923; Dilated ventricles (finding) C3714756; Intellectual Disability C4020875; Mental and motor retardation C4020876; Dull intelligence C4020899; Autosomal recessive predisposition C4083076; Increased head circumference C4225291; MUSCULAR DYSTROPHY-DYSTROGLYCANOPATHY (CONGENITAL WITH BRAIN AND EYE ANOMALIES), TYPE A, 9 C4255213; Increased size of skull C4280625; Decreased size of eyeball C4280663; Increased size of cranium C4280664; Big calvaria C4280808; Abnormally small eyeball
HGMD (count: 1)	CM076143; Bronchopulmonary dysplasia in premature newborns, association; Missense/nonsense
GWASdb (count: 15) (view all)	rs1568661; Crohn's disease; Crohn's disease rs4855864; Crohn's disease; Crohn's disease rs3924462; Crohn's disease; Crohn's disease rs3924462; Premature ovarian failure; premature ovarian failure rs4855861; Crohn's disease; Crohn's disease rs7637999; Crohn's disease; Crohn's disease rs11130199; Crohn's disease; Crohn's disease rs11130199; Premature ovarian failure; premature ovarian failure rs3870338; Multiple complex diseases; Null rs3870338; Crohn's disease; Crohn's disease rs1801143; Multiple complex diseases; Null rs1801143; Bipolar disorder, schizoaffective; bipolar disorder\|schizoaffective disorder rs1050088; Multiple complex diseases; Null rs1050088; Crohn's disease; Crohn's disease rs1050088; Lymphocyte counts; asthma\|leukemia\|lymphoma\|lymphopenia\|cardiovascular system disease

※ PTM Sites

PTM	Modification Sites
Phosphorylation (count: 25) (view all)	216 DLLHRMRSFSEVELH dbPAF 218 LHRMRSFSEVELHNM dbPAF 414 IPGYVEPTAVATPPT dbPAF 463 PRPVPRVTTKVSITR dbPAF 464 RPVPRVTTKVSITRL dbPAF 467 PRVTTKVSITRLETA dbPAF 469 VTTKVSITRLETASP dbPAF 473 VSITRLETASPPTRI dbPAF 475 ITRLETASPPTRIRT dbPAF 478 LETASPPTRIRTTTS dbPAF 482 SPPTRIRTTTSGVPR dbPAF 483 PPTRIRTTTSGVPRG dbPAF 484 PTRIRTTTSGVPRGG dbPAF 485 TRIRTTTSGVPRGGE dbPAF 512 RVDAWVGTYFEVKIP dbPAF 784 KKRKGKLTLEDQATF dbPAF 790 LTLEDQATFIKKGVP dbPAF 807 FADELDDSKPPPSSS dbPAF 812 DDSKPPPSSSMPLIL dbPAF 814 SKPPPSSSMPLILQE dbPAF 863 EDPNAPPYQPPPPFT dbPAF 884 GSRPKNMTPYRSPPP dbPAF 886 RPKNMTPYRSPPPYV dbPAF 888 KNMTPYRSPPPYVPP dbPAF 892 PYRSPPPYVPP**** dbPAF
Ubiquitination (count: 12) (view all)	226 EVELHNMKLVPVVNN PLMD 249 MAGPGNAKKVVENGA PLMD 261 NGALLSWKLGCSLNQ PLMD 433 KPRVSTPKPATPSTD PLMD 533 HEDTTTDKLKLTLKL PLMD 611 APARFKAKFVGDPAL PLMD 671 LPLEPCPKEQIAGLS PLMD 782 YRKKRKGKLTLEDQA PLMD 793 EDQATFIKKGVPIIF PLMD 794 DQATFIKKGVPIIFA PLMD 808 ADELDDSKPPPSSSM PLMD 95 ASSGDIIKVSAAGKE PLMD
Glycation (count: 1)	95 ASSGDIIKVSAAGKE PLMD
Methylation (count: 1)	626 VLNDIHKKIALVKKL PLMD

※ Protein-Protein Interaction

Network

Interaction

Source

O00308	Q14118	HPRD
O15230	Q14118	HPRD
P06241	Q14118	IntAct; MINT
P11532	Q14118	HPRD;IntAct
P12931	Q14118	HPRD; IntAct; MINT
P16333	Q14118	IntAct
P21810	Q14118	HPRD
P24043	Q14118	HPRD; MINT
P25391	Q14118	HPRD
P27986	Q14118	IntAct; MINT
P29353	Q14118	HPRD
P46939	Q14118	HPRD; MINT
P49768	Q14118	DIP
P50748	Q14118	BioGRID
P56539	Q14118	HPRD
P62993	Q14118	HPRD; IntAct; MINT
Q13474	Q14118	HPRD
Q13702	Q14118	HPRD
Q14118	Q14118	HPRD; MINT
Q14118	Q8TD06	HPRD
Q14118	Q8WV24	BioGRID
Q14118	Q92542	DIP
Q14118	Q96QZ7	HPRD
Q14118	Q9H0M0	HPRD

PTMD Annotation Information

※ Protein Information

Functional Description

Fasta Sequence

※ PTM-Disease Association

※ Disease Cross-ref Annotation

※ PTM Sites

※ Protein-Protein Interaction