Q63622 · DLG2_RAT
- ProteinDisks large homolog 2
- GeneDlg2
- StatusUniProtKB reviewed (Swiss-Prot)
- Organism
- Amino acids852 (go to sequence)
- Protein existenceEvidence at protein level
- Annotation score5/5
Function
function
Required for perception of chronic pain through NMDA receptor signaling. Regulates surface expression of NMDA receptors in dorsal horn neurons of the spinal cord. Interacts with the cytoplasmic tail of NMDA receptor subunits as well as inward rectifying potassium channels. Involved in regulation of synaptic stability at cholinergic synapses. Part of the postsynaptic protein scaffold of excitatory synapses (By similarity).
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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Enzyme and pathway databases
Names & Taxonomy
Protein names
- Recommended nameDisks large homolog 2
- Alternative names
Gene names
Organism names
- Organism
- Taxonomic lineageEukaryota > Metazoa > Chordata > Craniata > Vertebrata > Euteleostomi > Mammalia > Eutheria > Euarchontoglires > Glires > Rodentia > Myomorpha > Muroidea > Muridae > Murinae > Rattus
Accessions
- Primary accessionQ63622
- Secondary accessions
Proteomes
Organism-specific databases
Subcellular Location
UniProt Annotation
GO Annotation
Cell membrane ; Lipid-anchor
Note: Concentrated in soma and postsynaptic density of a subset of neurons (PubMed:11095503).
Keywords
- Cellular component
Phenotypes & Variants
Features
Showing features for mutagenesis.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Mutagenesis | 5 | Loss of palmitoylation and targeting to postsynaptic density. | ||||
Sequence: C → S | ||||||
Mutagenesis | 7 | Loss of palmitoylation and targeting to postsynaptic density. | ||||
Sequence: C → S |
PTM/Processing
Features
Showing features for chain, lipidation, modified residue.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Chain | PRO_0000094555 | 1-852 | Disks large homolog 2 | |||
Sequence: MFFACYCALRTNVKKYRYQDEDGPHDHSLPRLTHEVRGPELVHVSEKNLSQIENVHGYVLQSHISPLKASPAPIIVNTDTLDTIPYVNGTEIEYEFEEITLERGNSGLGFSIAGGTDNPHIGDDPGIFITKIIPGGAAAEDGRLRVNDCILRVNEVDVSEVSHSKAVEALKEAGSIVRLYVRRRRPILETVVEIKLFKGPKGLGFSIAGGVGNQHIPGDNSIYVTKIIDGGAAQKDGRLQVGDRLLMVNNYSLEEVTHEEAVAILKNTSDVVYLKVGKPTTIYMTDPYGPPDITHSYSPPMENHLLSGNNGTLEYKTSLPPISPGRYSPIPKHMLVEDDYTRPPEPVYSTVNKLCDKPASPRHYSPVECDKSFLLSTPYPHYHLGLLPDSDMTSHSQHSTATRQPSVTLQRAISLEGEPRKVVLHKGSTGLGFNIVGGEDGEGIFVSFILAGGPADLSGELQRGDQILSVNGIDLRGASHEQAAAALKGAGQTVTIIAQYQPEDYARFEAKIHDLREQMMNHSMSSGSGSLRTNQKRSLYVRAMFDYDKSKDSGLPSQGLSFKYGDILHVINASDDEWWQARRVILDGDSEEMGVIPSKRRVERKERARLKTVKFNAKPGVIDSKGDIPGLGDDGYGTKTLRGQEDLILSYEPVTRQEINYTRPVIILGPMKDRINDDLISEFPDKFGSCVPHTTRPKRDYEVDGRDYHFVISREQMEKDIQEHKFIEAGQYNDNLYGTSVQSVRFVAERGKHCILDVSGNAIKRLQVAQLYPIAIFIKPKSLEPLMEMNKRLTEEQAKKTYDRAIKLEQEFGEYFTAIVQGDTLEDIYNQCKLVIEEQSGPFIWIPSKEKL | ||||||
Lipidation | 5 | S-palmitoyl cysteine | ||||
Sequence: C | ||||||
Lipidation | 7 | S-palmitoyl cysteine | ||||
Sequence: C | ||||||
Modified residue | 28 | Phosphoserine | ||||
Sequence: S | ||||||
Modified residue | 58 | Phosphotyrosine | ||||
Sequence: Y | ||||||
Modified residue | 65 | Phosphoserine | ||||
Sequence: S | ||||||
Modified residue | 307 | Phosphoserine | ||||
Sequence: S | ||||||
Modified residue | 328 | Phosphoserine | ||||
Sequence: S | ||||||
Modified residue | 360 | Phosphoserine | ||||
Sequence: S | ||||||
Modified residue | 365 | Phosphoserine | ||||
Sequence: S | ||||||
Modified residue | 406 | Phosphoserine | ||||
Sequence: S | ||||||
Modified residue | 414 | Phosphoserine | ||||
Sequence: S | ||||||
Modified residue | 505 | Phosphotyrosine | ||||
Sequence: Y | ||||||
Modified residue | 528 | Phosphoserine | ||||
Sequence: S | ||||||
Modified residue | 530 | Phosphoserine | ||||
Sequence: S | ||||||
Modified residue | 553 | Phosphoserine | ||||
Sequence: S | ||||||
Modified residue | 732 | Phosphotyrosine | ||||
Sequence: Y | ||||||
Modified residue | 737 | Phosphotyrosine | ||||
Sequence: Y |
Post-translational modification
Keywords
- PTM
Proteomic databases
PTM databases
Expression
Tissue specificity
Detected in juxtaparanodal zones in the central nervous system and at nerve terminal plexuses of basket cells in the cerebellum (at protein level) (PubMed:20089912).
Brain. High levels in cerebellar Purkinje cells. Expressed in pyramidal cells of the Ammons's horn and granular cells of the dentate gyrus in the hippocampus as well as cerebral cortex and striatum. High levels in dorsal horn of spinal cord
Brain. High levels in cerebellar Purkinje cells. Expressed in pyramidal cells of the Ammons's horn and granular cells of the dentate gyrus in the hippocampus as well as cerebral cortex and striatum. High levels in dorsal horn of spinal cord
Developmental stage
High levels in developing brain and spinal chord, sensory neurons of dorsal root and trigeminal ganglia, myenteric neurons of the intestine as well as in non-neuronal cells of adrenal, thymus and submandibular glands of 15 dpc embryos.
Interaction
Subunit
Interacts through its PDZ domains with NETO1. Interacts with NOS1/nNOS through second PDZ domain (PubMed:8922396).
Interacts with KCNJ2/Kir2.1 (via C-terminus) through one of its PDZ domains (By similarity).
Interacts with KCNJ4 (By similarity).
Interacts with FRMPD4 (via C-terminus) (PubMed:19118189).
Interacts with LRFN1 (PubMed:16630835).
Interacts with LRFN2 and LRFN4. Interacts with FASLG (By similarity).
Interacts with ADAM22 (PubMed:20089912).
Interacts with DGKI (via PDZ-binding motif) (PubMed:21119615).
Interacts with KCNJ2/Kir2.1 (via C-terminus) through one of its PDZ domains (By similarity).
Interacts with KCNJ4 (By similarity).
Interacts with FRMPD4 (via C-terminus) (PubMed:19118189).
Interacts with LRFN1 (PubMed:16630835).
Interacts with LRFN2 and LRFN4. Interacts with FASLG (By similarity).
Interacts with ADAM22 (PubMed:20089912).
Interacts with DGKI (via PDZ-binding motif) (PubMed:21119615).
Binary interactions
Type | Entry 1 | Entry 2 | Number of experiments | Intact | |
---|---|---|---|---|---|
XENO | Q63622 | ATP2B2 Q01814-1 | 2 | EBI-396947, EBI-1174262 | |
XENO | Q63622 | ATP2B4 P23634-6 | 2 | EBI-396947, EBI-1174437 | |
XENO | Q63622 | CRHR1 P34998 | 2 | EBI-396947, EBI-3870393 | |
BINARY | Q63622 | Dgki F1MAB7 | 2 | EBI-396947, EBI-8523614 | |
BINARY | Q63622 | Dgkz O08560 | 4 | EBI-396947, EBI-8570505 | |
XENO | Q63622 | KIF1B O60333-3 | 3 | EBI-396947, EBI-465669 | |
BINARY | Q63622 | Map1a P34926 | 4 | EBI-396947, EBI-631571 |
Protein-protein interaction databases
Structure
Family & Domains
Features
Showing features for domain.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Domain | 98-184 | PDZ 1 | ||||
Sequence: EITLERGNSGLGFSIAGGTDNPHIGDDPGIFITKIIPGGAAAEDGRLRVNDCILRVNEVDVSEVSHSKAVEALKEAGSIVRLYVRRR | ||||||
Domain | 193-279 | PDZ 2 | ||||
Sequence: EIKLFKGPKGLGFSIAGGVGNQHIPGDNSIYVTKIIDGGAAQKDGRLQVGDRLLMVNNYSLEEVTHEEAVAILKNTSDVVYLKVGKP | ||||||
Domain | 421-501 | PDZ 3 | ||||
Sequence: KVVLHKGSTGLGFNIVGGEDGEGIFVSFILAGGPADLSGELQRGDQILSVNGIDLRGASHEQAAAALKGAGQTVTIIAQYQ | ||||||
Domain | 536-606 | SH3 | ||||
Sequence: KRSLYVRAMFDYDKSKDSGLPSQGLSFKYGDILHVINASDDEWWQARRVILDGDSEEMGVIPSKRRVERKE | ||||||
Domain | 662-837 | Guanylate kinase-like | ||||
Sequence: TRPVIILGPMKDRINDDLISEFPDKFGSCVPHTTRPKRDYEVDGRDYHFVISREQMEKDIQEHKFIEAGQYNDNLYGTSVQSVRFVAERGKHCILDVSGNAIKRLQVAQLYPIAIFIKPKSLEPLMEMNKRLTEEQAKKTYDRAIKLEQEFGEYFTAIVQGDTLEDIYNQCKLVIE |
Sequence similarities
Belongs to the MAGUK family.
Keywords
- Domain
Phylogenomic databases
Family and domain databases
Sequence & Isoforms
- Sequence statusComplete
This entry describes 7 isoforms produced by Alternative splicing.
Q63622-1
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
- SynonymsPSD-93b
- Length852
- Mass (Da)94,934
- Last updated1997-11-01 v1
- ChecksumF8D414A8B9CF5B09
Q63622-2
- Name2
- SynonymsPSD-93a
- Differences from canonical
- 1-13: MFFACYCALRTNV → MICHCKVACTNNTLSLMFGC
Q63622-3
- Name3
- SynonymsPSD-93c
Q63622-4
- Name4
- SynonymsPSD-93-delta
- Differences from canonical
- 1-68: MFFACYCALRTNVKKYRYQDEDGPHDHSLPRLTHEVRGPELVHVSEKNLSQIENVHGYVLQSHISPLK → MNAYLTKQHSCSRGSDGMDAGRGVPTLIRDAHCACGWQRNAQGLGYSSQTMPSSGPGGPASNRTKLVTLWDSVRKSPHKTSTKGKGNCGERCACPHGWFSPAQ
Q63622-5
- Name5
- SynonymsPSD-93d
- Differences from canonical
- 1-246: Missing
Q63622-6
- Name6
Q63622-7
- Name7
- Differences from canonical
- 626-641: GDIPGLGDDGYGTKTL → GSFNDKRKKSFIFSRKFPFYKNKEQSEQETSDPE
Computationally mapped potential isoform sequences
There are 7 potential isoforms mapped to this entry
Entry | Entry name | Gene name | Length | ||
---|---|---|---|---|---|
A0A8I6APM7 | A0A8I6APM7_RAT | Dlg2 | 901 | ||
A0A8I6ABF7 | A0A8I6ABF7_RAT | Dlg2 | 755 | ||
A0A8I6GD69 | A0A8I6GD69_RAT | Dlg2 | 872 | ||
A0A8I5ZK38 | A0A8I5ZK38_RAT | Dlg2 | 994 | ||
A0A8I5ZMA3 | A0A8I5ZMA3_RAT | Dlg2 | 919 | ||
F1M907 | F1M907_RAT | Dlg2 | 740 | ||
A0A8I6G5H5 | A0A8I6G5H5_RAT | Dlg2 | 873 |
Features
Showing features for alternative sequence, sequence conflict.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Alternative sequence | VSP_015528 | 1-13 | in isoform 2 | |||
Sequence: MFFACYCALRTNV → MICHCKVACTNNTLSLMFGC | ||||||
Alternative sequence | VSP_015527 | 1-61 | in isoform 3 | |||
Sequence: Missing | ||||||
Alternative sequence | VSP_015526 | 1-68 | in isoform 4 | |||
Sequence: MFFACYCALRTNVKKYRYQDEDGPHDHSLPRLTHEVRGPELVHVSEKNLSQIENVHGYVLQSHISPLK → MNAYLTKQHSCSRGSDGMDAGRGVPTLIRDAHCACGWQRNAQGLGYSSQTMPSSGPGGPASNRTKLVTLWDSVRKSPHKTSTKGKGNCGERCACPHGWFSPAQ | ||||||
Alternative sequence | VSP_015525 | 1-246 | in isoform 5 | |||
Sequence: Missing | ||||||
Alternative sequence | VSP_015529 | 62-68 | in isoform 3 | |||
Sequence: SHISPLK → MQHAFIP | ||||||
Sequence conflict | 181-182 | in Ref. 2; AAC52643 | ||||
Sequence: VR → IL | ||||||
Sequence conflict | 228 | in Ref. 2; AAC52643 | ||||
Sequence: I → M | ||||||
Sequence conflict | 326 | in Ref. 2; AAC52643 | ||||
Sequence: R → K | ||||||
Sequence conflict | 339 | in Ref. 3; AAB48562 | ||||
Sequence: D → E | ||||||
Alternative sequence | VSP_015530 | 341-392 | in isoform 3 | |||
Sequence: Missing | ||||||
Alternative sequence | VSP_015531 | 450-454 | in isoform 6 | |||
Sequence: Missing | ||||||
Sequence conflict | 464-465 | in Ref. 2; AAC52643 | ||||
Sequence: GD → RK | ||||||
Sequence conflict | 474 | in Ref. 2 | ||||
Sequence: D → H | ||||||
Sequence conflict | 476 | in Ref. 2 | ||||
Sequence: R → P | ||||||
Sequence conflict | 478 | in Ref. 2 | ||||
Sequence: A → D | ||||||
Sequence conflict | 484-486 | in Ref. 2; AAC52643 | ||||
Sequence: AAA → LP | ||||||
Sequence conflict | 506 | in Ref. 2; AAC52643 | ||||
Sequence: A → S | ||||||
Sequence conflict | 569 | in Ref. 2; AAC52643 | ||||
Sequence: H → N | ||||||
Sequence conflict | 586 | in Ref. 2; AAC52643 | ||||
Sequence: L → Q | ||||||
Alternative sequence | VSP_015533 | 626-641 | in isoform 6 | |||
Sequence: Missing | ||||||
Alternative sequence | VSP_015532 | 626-641 | in isoform 7 | |||
Sequence: GDIPGLGDDGYGTKTL → GSFNDKRKKSFIFSRKFPFYKNKEQSEQETSDPE | ||||||
Sequence conflict | 627-630 | in Ref. 5 | ||||
Sequence: DIPG → TSR | ||||||
Sequence conflict | 639 | in Ref. 3; AAB48562 | ||||
Sequence: K → A | ||||||
Sequence conflict | 726 | in Ref. 1; AAB53243 | ||||
Sequence: F → L | ||||||
Sequence conflict | 733 | in Ref. 2; AAC52643 | ||||
Sequence: N → Y | ||||||
Sequence conflict | 749 | in Ref. 1; AAB53243 | ||||
Sequence: E → V | ||||||
Sequence conflict | 756 | in Ref. 2; AAC52643 | ||||
Sequence: L → H | ||||||
Sequence conflict | 791-792 | in Ref. 2 | ||||
Sequence: KR → NG | ||||||
Sequence conflict | 794 | in Ref. 2 | ||||
Sequence: T → M |
Keywords
- Coding sequence diversity
- Technical term
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
U49049 EMBL· GenBank· DDBJ | AAB53243.1 EMBL· GenBank· DDBJ | mRNA | ||
U50717 EMBL· GenBank· DDBJ | AAC52643.1 EMBL· GenBank· DDBJ | mRNA | ||
U53368 EMBL· GenBank· DDBJ | AAB48562.1 EMBL· GenBank· DDBJ | mRNA |