Q9WVQ1 · MAGI2_MOUSE
- ProteinMembrane-associated guanylate kinase, WW and PDZ domain-containing protein 2
- GeneMagi2
- StatusUniProtKB reviewed (Swiss-Prot)
- Organism
- Amino acids1275 (go to sequence)
- Protein existenceEvidence at protein level
- Annotation score5/5
Function
function
Seems to act as a scaffold molecule at synaptic junctions by assembling neurotransmitter receptors and cell adhesion proteins (By similarity).
Plays a role in nerve growth factor (NGF)-induced recruitment of RAPGEF2 to late endosomes and neurite outgrowth (By similarity).
May play a role in regulating activin-mediated signaling in neuronal cells (PubMed:10681527).
Enhances the ability of PTEN to suppress AKT1 activation (By similarity).
Plays a role in receptor-mediated clathrin-dependent endocytosis which is required for ciliogenesis (PubMed:24608321).
Plays a role in nerve growth factor (NGF)-induced recruitment of RAPGEF2 to late endosomes and neurite outgrowth (By similarity).
May play a role in regulating activin-mediated signaling in neuronal cells (PubMed:10681527).
Enhances the ability of PTEN to suppress AKT1 activation (By similarity).
Plays a role in receptor-mediated clathrin-dependent endocytosis which is required for ciliogenesis (PubMed:24608321).
GO annotations
all annotations | all molecular function | virus receptor activity | dna binding | rna binding | cytoskeletal motor activity | catalytic activity | gtpase activity | structural molecule activity | transporter activity | cytoskeletal protein binding | lipid binding | cyclase activity | antioxidant activity | oxidoreductase activity | transferase activity | hydrolase activity | lyase activity | isomerase activity | ligase activity | protein tag activity | cargo receptor activity | histone binding | protein folding chaperone | translation regulator activity | nutrient reservoir activity | receptor ligand activity | molecular transducer activity | molecular adaptor activity | toxin activity | cell adhesion mediator activity | molecular function regulator activity | virus coreceptor activity | catalytic activity, acting on a protein | catalytic activity, acting on dna | catalytic activity, acting on rna | molecular carrier activity | transcription regulator activity | general transcription initiation factor activity | molecular sensor activity | molecular sequestering activity | atp-dependent activity | other molecular function | all biological process | mitotic cell cycle | cytokinesis | cytoplasmic translation | immune system process | muscle system process | circulatory system process | renal system process | respiratory system process | carbohydrate metabolic process | generation of precursor metabolites and energy | dna replication | dna repair | dna recombination | chromatin organization | dna-templated transcription | regulation of dna-templated transcription | trna metabolic process | protein folding | protein glycosylation | amino acid metabolic process | modified amino acid metabolic process | lipid metabolic process | vitamin metabolic process | sulfur compound metabolic process | intracellular protein transport | nucleocytoplasmic transport | autophagy | inflammatory response | mitochondrion organization | cytoskeleton organization | microtubule-based movement | peroxisome organization | lysosome organization | chromosome segregation | cell adhesion | establishment or maintenance of cell polarity | programmed cell death | photosynthesis | mrna metabolic process | snrna metabolic process | vesicle-mediated transport | reproductive process | digestive system process | signaling | cell differentiation | protein catabolic process | extracellular matrix organization | regulatory ncrna-mediated gene silencing | telomere organization | cell junction organization | wound healing | ribosome biogenesis | cilium organization | anatomical structure development | cell motility | nervous system process | endocrine process | protein maturation | transmembrane transport | nucleobase-containing small molecule metabolic process | hepaticobiliary system process | membrane organization | protein-containing complex assembly | cell wall organization or biogenesis | nitrogen cycle metabolic process | protein localization to plasma membrane | defense response to other organism | detoxification | meiotic nuclear division | mitotic nuclear division | mitochondrial gene expression | carbohydrate derivative metabolic process | other biological process | all cellular component | nuclear chromosome | extracellular region | extracellular space | cell wall | nucleus | nuclear envelope | nucleoplasm | chromosome | nucleolus | mitochondrion | lysosome | endosome | vacuole | peroxisome | endoplasmic reticulum | golgi apparatus | lipid droplet | microtubule organizing center | cytosol | ribosome | cytoskeleton | plasma membrane | cilium | plastid | thylakoid | external encapsulating structure | extracellular matrix | cytoplasmic vesicle | organelle | other cellular component | |||
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Keywords
- Biological process
Names & Taxonomy
Protein names
- Recommended nameMembrane-associated guanylate kinase, WW and PDZ domain-containing protein 2
- Alternative names
Gene names
Organism names
- Organism
- Strains
- Taxonomic lineageEukaryota > Metazoa > Chordata > Craniata > Vertebrata > Euteleostomi > Mammalia > Eutheria > Euarchontoglires > Glires > Rodentia > Myomorpha > Muroidea > Muridae > Murinae > Mus > Mus
Accessions
- Primary accessionQ9WVQ1
- Secondary accessions
Proteomes
Organism-specific databases
Subcellular Location
UniProt Annotation
GO Annotation
Cell membrane ; Peripheral membrane protein
Note: Localized diffusely in the cytoplasm before nerve growth factor (NGF) stimulation. Recruited to late endosomes after NGF stimulation. Membrane-associated in synaptosomes (By similarity).
Keywords
- Cellular component
Phenotypes & Variants
Features
Showing features for mutagenesis.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Mutagenesis | 1152 | Does not affect interaction with USH1G. | ||||
Sequence: S → A |
Variants
We now provide the "Disease & Variants" viewer in its own tab.
The viewer provides 56 variants from UniProt as well as other sources including ClinVar and dbSNP.
PTM/Processing
Features
Showing features for chain, modified residue.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Chain | PRO_0000094587 | 1-1275 | Membrane-associated guanylate kinase, WW and PDZ domain-containing protein 2 | |||
Sequence: MSKSLKKKSHWTSKVHESVIGRNPEGQLGFELKGGAENGQFPYLGEVKPGKVAYESGSKLVSEELLLEVNETPVAGLTIRDVLAVIKHCKDPLRLKCVKQGGIVDKDLRHYLNLRFQKGSVDHELQQIIRDNLYLRTVPCTTRPHKEGEVPGVDYIFITVEEFMELEKSGALLESGTYEDNYYGTPKPPAEPAPLLNVTDQILPGATPSAEGKRKRNKSVTNMEKASIEPPEEEEEERPVVNGNGVVITPESSEHEDKSAGASGETPSQPYPAPVYSQPEELKDQMDDTKPTKPEENEDSDPLPDNWEMAYTEKGEVYFIDHNTKTTSWLDPRLAKKAKPPEECKENELPYGWEKIDDPIYGTYYVDHINRRTQFENPVLEAKRKLQQHNMPHTELGAKPLQAPGFREKPLFTRDASQLKGTFLSTTLKKSNMGFGFTIIGGDEPDEFLQVKSVIPDGPAAQDGKMETGDVIVYINEVCVLGHTHADVVKLFQSVPIGQSVNLVLCRGYPLPFDPEDPANSMVPPLAIMERPPPVMVNGRHNYETYLEYISRTSQSVPDITDRPPHSLHSMPADGQLDGTYPPPVHDDNVSMASSGATQAELMTLTIVKGAQGFGFTIADSPTGQRVKQILDIQGCPGLCEGDLIVEINQQNVQNLSHTEVVDILKDCPVGSETSLIIHRGGFFSPWKTPKPMMDRWENQGSPQTSLSAPAVPQNLPFPPALHRSSFPDSTEAFDPRKPDPYELYEKSRAIYESRQQVPPRTSFRMDSSGPDYKELDVHLRRMESGFGFRILGGDEPGQPILIGAVIAMGSADRDGRLHPGDELVYVDGIPVAGKTHRYVIDLMHHAARNGQVNLTVRRKVLCGGEPCPENGRSPGSVSTHHSSPRSDYATYSNSNHAAPSSNASPPEGFASHSLQTSDVVIHRKENEGFGFVIISSLNRPESGATITVPHKIGRIIDGSPADRCAKLKVGDRILAVNGQSIINMPHADIVKLIKDAGLSVTLRIIPQEELNSPTSAPSSEKQSPMAQQHSPLAQQSPLAQPSPATPNSPVAQPAPPQPLQLQGHENSYRSEVKARQDVKPDIRQPPFTDYRQPPLDYRQPPGGDYSQPPPLDYRQHSPDTRQYPLSDYRQPQDFDYFTVDMEKGAKGFGFSIRGGREYKMDLYVLRLAEDGPAIRNGRMRVGDQIIEINGESTRDMTHARAIELIKSGGRRVRLLLKRGTGQVPEYGMVPSSLSMCMKSDKHGSPYFYLLGHPKDTTNPTPGVLPLPPPQACRK | ||||||
Modified residue | 361 | Phosphotyrosine | ||||
Sequence: Y | ||||||
Modified residue | 685 | Phosphoserine | ||||
Sequence: S | ||||||
Modified residue | 826 | Phosphotyrosine | ||||
Sequence: Y | ||||||
Modified residue | 883 | Phosphoserine | ||||
Sequence: S | ||||||
Modified residue | 884 | Phosphoserine | ||||
Sequence: S | ||||||
Modified residue | 1013 | Phosphoserine | ||||
Sequence: S |
Keywords
- PTM
Proteomic databases
PTM databases
Expression
Tissue specificity
Expressed throughout the retina except in the nuclear layers and the photoreceptor outer segments (at protein level) (PubMed:24608321).
Highest retinal expression is observed in the outer plexiform layer, the outer limiting membrane and the inner segment of photoreceptor cells (at protein level) (PubMed:24608321).
Expressed in brain
Highest retinal expression is observed in the outer plexiform layer, the outer limiting membrane and the inner segment of photoreceptor cells (at protein level) (PubMed:24608321).
Expressed in brain
Gene expression databases
Interaction
Subunit
Interacts (via its WW domains) with DRPLA (By similarity).
Interacts (via its second PDZ domain) with PTEN (via unphosphorylated C-terminus); this interaction diminishes the degradation rate of PTEN (By similarity).
Interacts (via guanylate kinase domain) with DLGAP1 (By similarity).
Interacts (via the PDZ domains) with GRIN2A, GRID2 and NLGN1 (By similarity).
Interacts with CTNND2, CTNNB1 and MAGUIN-1 (By similarity).
Interacts with ACVR2A, SMAD2 and SMAD3 (PubMed:10681527).
Part of a complex consisting of MAGI2/ARIP1, ACVR2A, ACVR1B and SMAD3 (PubMed:10681527).
May interact with HTR2A (PubMed:14988405).
Interacts with RAPGEF2 (By similarity).
Identified in a complex with ACTN4, CASK, IQGAP1, NPHS1, SPTAN1 and SPTBN1 (By similarity).
Interacts with DDN (By similarity).
Found in a complex, at least composed of KIDINS220, MAGI2, NTRK1 and RAPGEF2; the complex is mainly formed at late endosomes in a NGF-dependent manner (By similarity).
Interacts with RAPGEF2; the interaction occurs before or after nerve growth factor (NGF) stimulation (By similarity).
Interacts (via PDZ domain) with KIDINS220 (via C-terminal domain) (By similarity).
Interacts with IGSF9 and HTR4 (PubMed:15340156, PubMed:15466885).
Interacts with DLL1 (PubMed:15509766).
Found in a complex with IGSF9B and NLGN2; the interaction with IGSF9B is mediated via the PDZ 5 and PDZ 6 domains, while the interaction with NLGN2 is mediated via the WW1, WW2 and PDZ2 domains (PubMed:23751499).
Interacts (via PDZ 6 domain) with USH1G (via SAM domain); the interaction is triggered by phosphorylation of USH1G by CK2 and negatively regulates MAGI2-mediated endocytosis (PubMed:24608321).
Interacts (via its second PDZ domain) with PTEN (via unphosphorylated C-terminus); this interaction diminishes the degradation rate of PTEN (By similarity).
Interacts (via guanylate kinase domain) with DLGAP1 (By similarity).
Interacts (via the PDZ domains) with GRIN2A, GRID2 and NLGN1 (By similarity).
Interacts with CTNND2, CTNNB1 and MAGUIN-1 (By similarity).
Interacts with ACVR2A, SMAD2 and SMAD3 (PubMed:10681527).
Part of a complex consisting of MAGI2/ARIP1, ACVR2A, ACVR1B and SMAD3 (PubMed:10681527).
May interact with HTR2A (PubMed:14988405).
Interacts with RAPGEF2 (By similarity).
Identified in a complex with ACTN4, CASK, IQGAP1, NPHS1, SPTAN1 and SPTBN1 (By similarity).
Interacts with DDN (By similarity).
Found in a complex, at least composed of KIDINS220, MAGI2, NTRK1 and RAPGEF2; the complex is mainly formed at late endosomes in a NGF-dependent manner (By similarity).
Interacts with RAPGEF2; the interaction occurs before or after nerve growth factor (NGF) stimulation (By similarity).
Interacts (via PDZ domain) with KIDINS220 (via C-terminal domain) (By similarity).
Interacts with IGSF9 and HTR4 (PubMed:15340156, PubMed:15466885).
Interacts with DLL1 (PubMed:15509766).
Found in a complex with IGSF9B and NLGN2; the interaction with IGSF9B is mediated via the PDZ 5 and PDZ 6 domains, while the interaction with NLGN2 is mediated via the WW1, WW2 and PDZ2 domains (PubMed:23751499).
Interacts (via PDZ 6 domain) with USH1G (via SAM domain); the interaction is triggered by phosphorylation of USH1G by CK2 and negatively regulates MAGI2-mediated endocytosis (PubMed:24608321).
Binary interactions
Type | Entry 1 | Entry 2 | Number of experiments | Intact | |
---|---|---|---|---|---|
BINARY | Q9WVQ1 | Dll1 Q61483 | 3 | EBI-297151, EBI-297125 |
Protein-protein interaction databases
Miscellaneous
Structure
Family & Domains
Features
Showing features for domain, region, compositional bias.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Domain | 17-101 | PDZ 1 | ||||
Sequence: ESVIGRNPEGQLGFELKGGAENGQFPYLGEVKPGKVAYESGSKLVSEELLLEVNETPVAGLTIRDVLAVIKHCKDPLRLKCVKQG | ||||||
Domain | 109-283 | Guanylate kinase-like | ||||
Sequence: RHYLNLRFQKGSVDHELQQIIRDNLYLRTVPCTTRPHKEGEVPGVDYIFITVEEFMELEKSGALLESGTYEDNYYGTPKPPAEPAPLLNVTDQILPGATPSAEGKRKRNKSVTNMEKASIEPPEEEEEERPVVNGNGVVITPESSEHEDKSAGASGETPSQPYPAPVYSQPEELK | ||||||
Region | 203-305 | Disordered | ||||
Sequence: LPGATPSAEGKRKRNKSVTNMEKASIEPPEEEEEERPVVNGNGVVITPESSEHEDKSAGASGETPSQPYPAPVYSQPEELKDQMDDTKPTKPEENEDSDPLPD | ||||||
Compositional bias | 281-300 | Basic and acidic residues | ||||
Sequence: ELKDQMDDTKPTKPEENEDS | ||||||
Domain | 301-334 | WW 1 | ||||
Sequence: DPLPDNWEMAYTEKGEVYFIDHNTKTTSWLDPRL | ||||||
Region | 301-380 | Interaction with DDN | ||||
Sequence: DPLPDNWEMAYTEKGEVYFIDHNTKTTSWLDPRLAKKAKPPEECKENELPYGWEKIDDPIYGTYYVDHINRRTQFENPVL | ||||||
Domain | 347-380 | WW 2 | ||||
Sequence: NELPYGWEKIDDPIYGTYYVDHINRRTQFENPVL | ||||||
Domain | 425-509 | PDZ 2 | ||||
Sequence: STTLKKSNMGFGFTIIGGDEPDEFLQVKSVIPDGPAAQDGKMETGDVIVYINEVCVLGHTHADVVKLFQSVPIGQSVNLVLCRGY | ||||||
Domain | 604-682 | PDZ 3 | ||||
Sequence: TLTIVKGAQGFGFTIADSPTGQRVKQILDIQGCPGLCEGDLIVEINQQNVQNLSHTEVVDILKDCPVGSETSLIIHRGG | ||||||
Compositional bias | 698-712 | Polar residues | ||||
Sequence: ENQGSPQTSLSAPAV | ||||||
Region | 698-740 | Disordered | ||||
Sequence: ENQGSPQTSLSAPAVPQNLPFPPALHRSSFPDSTEAFDPRKPD | ||||||
Domain | 777-859 | PDZ 4 | ||||
Sequence: DVHLRRMESGFGFRILGGDEPGQPILIGAVIAMGSADRDGRLHPGDELVYVDGIPVAGKTHRYVIDLMHHAARNGQVNLTVRR | ||||||
Region | 868-912 | Disordered | ||||
Sequence: CPENGRSPGSVSTHHSSPRSDYATYSNSNHAAPSSNASPPEGFAS | ||||||
Compositional bias | 873-912 | Polar residues | ||||
Sequence: RSPGSVSTHHSSPRSDYATYSNSNHAAPSSNASPPEGFAS | ||||||
Domain | 919-1009 | PDZ 5 | ||||
Sequence: DVVIHRKENEGFGFVIISSLNRPESGATITVPHKIGRIIDGSPADRCAKLKVGDRILAVNGQSIINMPHADIVKLIKDAGLSVTLRIIPQE | ||||||
Compositional bias | 1010-1042 | Polar residues | ||||
Sequence: ELNSPTSAPSSEKQSPMAQQHSPLAQQSPLAQP | ||||||
Region | 1010-1128 | Disordered | ||||
Sequence: ELNSPTSAPSSEKQSPMAQQHSPLAQQSPLAQPSPATPNSPVAQPAPPQPLQLQGHENSYRSEVKARQDVKPDIRQPPFTDYRQPPLDYRQPPGGDYSQPPPLDYRQHSPDTRQYPLSD | ||||||
Compositional bias | 1043-1057 | Pro residues | ||||
Sequence: SPATPNSPVAQPAPP | ||||||
Compositional bias | 1069-1085 | Basic and acidic residues | ||||
Sequence: YRSEVKARQDVKPDIRQ | ||||||
Domain | 1139-1221 | PDZ 6 | ||||
Sequence: TVDMEKGAKGFGFSIRGGREYKMDLYVLRLAEDGPAIRNGRMRVGDQIIEINGESTRDMTHARAIELIKSGGRRVRLLLKRGT |
Sequence similarities
Belongs to the MAGUK family.
Keywords
- Domain
Phylogenomic databases
Family and domain databases
Sequence & Isoforms
- Sequence statusComplete
This entry describes 4 isoforms produced by Alternative splicing.
Q9WVQ1-1
This isoform has been chosen as the canonical sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.
- Name1
- Synonymslong
- Length1,275
- Mass (Da)140,919
- Last updated2003-10-03 v2
- ChecksumF17DC52517806354
Q9WVQ1-2
- Name2
- Synonymsshort
- NoteMajor.
- Differences from canonical
- 1-163: Missing
Q9WVQ1-3
- Name3
- NoteMay be due to an intron retention.
- Differences from canonical
- 1-390: Missing
- 1229-1275: MVPSSLSMCMKSDKHGSPYFYLLGHPKDTTNPTPGVLPLPPPQACRK → AFHSFLHLCSAFSVF
Q9WVQ1-4
- Name4
Computationally mapped potential isoform sequences
There are 6 potential isoforms mapped to this entry
Entry | Entry name | Gene name | Length | ||
---|---|---|---|---|---|
A0A0G2JGI5 | A0A0G2JGI5_MOUSE | Magi2 | 188 | ||
A0A0G2JE00 | A0A0G2JE00_MOUSE | Magi2 | 1414 | ||
A0A0G2JE05 | A0A0G2JE05_MOUSE | Magi2 | 38 | ||
A0A140LHL1 | A0A140LHL1_MOUSE | Magi2 | 837 | ||
A0A0G2JEG6 | A0A0G2JEG6_MOUSE | Magi2 | 1400 | ||
A0A140LHB5 | A0A140LHB5_MOUSE | Magi2 | 238 |
Features
Showing features for alternative sequence, compositional bias.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Alternative sequence | VSP_008436 | 1-163 | in isoform 2 and isoform 4 | |||
Sequence: Missing | ||||||
Alternative sequence | VSP_018580 | 1-390 | in isoform 3 | |||
Sequence: Missing | ||||||
Compositional bias | 281-300 | Basic and acidic residues | ||||
Sequence: ELKDQMDDTKPTKPEENEDS | ||||||
Compositional bias | 698-712 | Polar residues | ||||
Sequence: ENQGSPQTSLSAPAV | ||||||
Alternative sequence | VSP_018581 | 756-770 | in isoform 4 | |||
Sequence: QQVPPRTSFRMDSSG → R | ||||||
Compositional bias | 873-912 | Polar residues | ||||
Sequence: RSPGSVSTHHSSPRSDYATYSNSNHAAPSSNASPPEGFAS | ||||||
Compositional bias | 1010-1042 | Polar residues | ||||
Sequence: ELNSPTSAPSSEKQSPMAQQHSPLAQQSPLAQP | ||||||
Compositional bias | 1043-1057 | Pro residues | ||||
Sequence: SPATPNSPVAQPAPP | ||||||
Compositional bias | 1069-1085 | Basic and acidic residues | ||||
Sequence: YRSEVKARQDVKPDIRQ | ||||||
Alternative sequence | VSP_008437 | 1229-1275 | in isoform 3 | |||
Sequence: MVPSSLSMCMKSDKHGSPYFYLLGHPKDTTNPTPGVLPLPPPQACRK → AFHSFLHLCSAFSVF |
Keywords
- Coding sequence diversity
- Technical term
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
AB029485 EMBL· GenBank· DDBJ | BAA82294.1 EMBL· GenBank· DDBJ | mRNA | ||
AK039336 EMBL· GenBank· DDBJ | BAC30321.1 EMBL· GenBank· DDBJ | mRNA | ||
AK147530 EMBL· GenBank· DDBJ | BAE27976.1 EMBL· GenBank· DDBJ | mRNA | ||
BC059005 EMBL· GenBank· DDBJ | AAH59005.1 EMBL· GenBank· DDBJ | mRNA |