Details for: Dlg1
Associated with
Other Information
Genular Protein ID: 3999891715
Symbol: DLG1_RAT
Name: Synapse-associated protein 97
UniProtKB Accession Codes:
Database IDs:
Citations:
PubMed ID: 7891172
Title: Molecular characterization and spatial distribution of SAP97, a novel presynaptic protein homologous to SAP90 and the Drosophila discs-large tumor suppressor protein.
PubMed ID: 7891172
PubMed ID: 9115257
Title: SAPAPs. A family of PSD-95/SAP90-associated proteins localized at postsynaptic density.
PubMed ID: 9115257
PubMed ID: 9677374
Title: SAP97 is associated with the alpha-amino-3-hydroxy-5-methylisoxazole-4-propionic acid receptor GluR1 subunit.
PubMed ID: 9677374
PubMed ID: 9786987
Title: Localization of postsynaptic density-93 to dendritic microtubules and interaction with microtubule-associated protein 1A.
PubMed ID: 9786987
PubMed ID: 10629225
Title: PSD-95 and SAP97 exhibit distinct mechanisms for regulating K(+) channel surface expression and clustering.
PubMed ID: 10629225
PubMed ID: 11865057
Title: A novel and conserved protein-protein interaction domain of mammalian Lin-2/CASK binds and recruits SAP97 to the lateral surface of epithelia.
PubMed ID: 11865057
PubMed ID: 14597197
Title: Brain-derived neurotrophic factor signal enhances and maintains the expression of AMPA receptor-associated PDZ proteins in developing cortical neurons.
PubMed ID: 14597197
PubMed ID: 12933808
Title: CaMKII-dependent phosphorylation regulates SAP97/NR2A interaction.
PubMed ID: 12933808
PubMed ID: 14960569
Title: A multiprotein trafficking complex composed of SAP97, CASK, Veli, and Mint1 is associated with inward rectifier Kir2 potassium channels.
PubMed ID: 14960569
PubMed ID: 15044483
Title: Calcium/calmodulin-dependent protein kinase II phosphorylation drives synapse-associated protein 97 into spines.
PubMed ID: 15044483
PubMed ID: 15504326
Title: Quaternary structure, protein dynamics, and synaptic function of SAP97 controlled by L27 domain interactions.
PubMed ID: 15504326
PubMed ID: 15951562
Title: Binding of PTEN to specific PDZ domains contributes to PTEN protein stability and phosphorylation by microtubule-associated serine/threonine kinases.
PubMed ID: 15951562
PubMed ID: 16495444
Title: A novel family of adhesion-like molecules that interacts with the NMDA receptor.
PubMed ID: 16495444
PubMed ID: 16630835
Title: SALM synaptic cell adhesion-like molecules regulate the differentiation of excitatory synapses.
PubMed ID: 16630835
PubMed ID: 17980554
Title: DLG1 is an anchor for the E3 ligase MARCH2 at sites of cell-cell contact.
PubMed ID: 17980554
PubMed ID: 19118189
Title: Preso, a novel PSD-95-interacting FERM and PDZ domain protein that regulates dendritic spine morphogenesis.
PubMed ID: 19118189
PubMed ID: 19213956
Title: Kv4 potassium channels form a tripartite complex with the anchoring protein SAP97 and CaMKII in cardiac myocytes.
PubMed ID: 19213956
PubMed ID: 21119615
Title: DGKiota regulates presynaptic release during mGluR-dependent LTD.
PubMed ID: 21119615
PubMed ID: 22673903
Title: Quantitative maps of protein phosphorylation sites across 14 different rat organs and tissues.
PubMed ID: 22673903
DOI: 10.1038/ncomms1871
Sequence Information:
- Length: 911
- Mass: 100571
- Checksum: 18CEBD31DD0CAF8B
- Sequence:
MPVRKQDTQR ALHLLEEYRS KLSQTEDRQL RSSIERVISI FQSNLFQALI DIQEFYEVTL LDNPKCVDHS KQCEPVQPGN PWESGSLSSA AVTSESLPGG LSPPVEKYRY QDEEVLPSER ISPQVPNEVL GPELVHVSEK SLSEIENVHG FVSHSHISPI KPTEAVPPSS PIVPVTPALP VPAESPVVLP STPQANPPPV LVNTDSLETP TYVNGTDADY EYEEITLERG NSGLGFSIAG GTDNPHIGDD SSIFITKIIT GGAAAQDGRL RVNDCILRVN EADVRDVTHS KAVEALKEAG SIVRLYVKRR KAFRKNHEIK LIKGPKGLGF SIAGGVGNQH IPGDNSIYVT KIIEGGAAHK DGKLQIGDKL LAVNSVCLEE VTHEEAVTAL KNTSDFVYLK AAKPTSMYIN DGYAPPDITN SSSQSVDNHV SPSSYLGQTP ASPARYSPIS KAVLGDDEIT REPRKVVLHR GSTGLGFNIV GGEDGEGIFI SFILAGGPAD LSGELRKGDR IISVNSVDLR AASHEQAAAA LKNAGQAVTI VAQYRPEEYS RFEAKIHDLR ETMMNSSVSS GSGSLRTSQK RSLYVRALFD YDKTKDSGLP SQGLNFKFGD ILHVINASDD EWWQARQVTP DGESDEVGVI PSKRRVEKKE RARLKTVKFN SKTRGDKGEI PDDMGSKGLK HVTSNASDSE SSYHEYGCSK GGQEEYVLSY EPVNQQEVNY TRPVIILGPM KDRVNDDLIS EFPDKFGSCV PHTTRPKRDY EVDGRDYHFV TSREQMEKDI QEHKFIEAGQ YNNHLYGTSV QSVRAVAEKG KHCILDVSGN AIKRLQIAQL YPISIFIKPK SMENIMEMNK RLTDEQARKT FERAVRLEQE FTEHFTAIVQ GDTLEDIYNQ VKQIIEEQSG PYIWVPAKEK L
Database document:
This is a preview of the gene's schema. Only a few entries are kept for 'singleCellExpressions,' 'mRNAExpressions,' and other large data arrays for visualization purposes. You can zoom in with the mouse wheel for a closer view, and the text will adjust automatically if necessary. For the full schema, download it here.