Tag | Content |
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UniProt Accession | DAG1_MOUSE; Q62165; |
Entrez ID | 13138 |
GenBank Protein ID | NM_001276481.1; NM_001276482.1; NM_001276485.1; NM_001276486.1; NM_001276492.1; NM_001276493.1; NM_010017.4; XM_006511636.2; |
GenBank Nucleotide ID | NP_001263410.1; NP_001263411.1; NP_001263414.1; NP_001263415.1; NP_001263421.1; NP_001263422.1; NP_034147.1; XP_006511699.1; |
Protein Name | Dystroglycan (Dystrophin-associated glycoprotein 1) [Cleaved into: Alpha-dystroglycan (Alpha-DG); Beta-dystroglycan (Beta-DG)] |
Gene Name | Dag1; Dag-1 |
Organism | Mus musculus |
NCBI Taxa ID | 10090 |
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.;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). |
Sequence (Fasta) | 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 894 |
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Database | Annotation |
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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 |
PTM | Modification Sites |
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Phosphorylation (count: 10) (view all) | 315 LRRQIHATPTPVTAI dbPAF
317 RQIHATPTPVTAIGP dbPAF 334 TAIQEPPSRIVPTPT dbPAF 788 LTLEDQATFIKKGVP dbPAF 810 DDSKPPPSSSMPLIL dbPAF 811 DSKPPPSSSMPLILQ dbPAF |
Acetylation (count: 1) | 630 KKIALVKKLAFAFGD PLMD |
Ubiquitination (count: 5) | 778 ICYRKKRKGKLTLED PLMD
780 YRKKRKGKLTLEDQA PLMD 791 EDQATFIKKGVPIIF PLMD 792 DQATFIKKGVPIIFA PLMD 806 ADELDDSKPPPSSSM PLMD |
Network | Interaction | |||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
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A | B | Source | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
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