Protein:DLG1 |
Protein Summary |
Gene summary |
| Gene name: DLG1 | ASpdb.0 ID: 1739 | Gene | Gene symbol | DLG1 | Gene ID | 1739 |
| Gene name | discs large MAGUK scaffold protein 1 |
| Synonyms | DLGH1|SAP-97|SAP97|hdlg |
| Cytomap | 3q29 |
| Type of gene | protein-coding |
| Description | disks large homolog 1dJ1061C18.1.1discs large homolog 1, scribble cell polarity complex componentpresynaptic protein SAP97synapse-associated protein 97 |
| Modification date | 20240411 |
| UniProtAcc | Q12959 |
Gene ontology of this gene with evidence of Inferred from Direct Assay (IDA) from Entrez |
| Partner | Gene | GO ID | GO term | PubMed ID |
| Gene | DLG1 | GO:0001772 | immunological synapse | 20551903 |
| Gene | DLG1 | GO:0001935 | endothelial cell proliferation | 14699157 |
| Gene | DLG1 | GO:0005634 | nucleus | 17237226 |
| Gene | DLG1 | GO:0005737 | cytoplasm | 17237226|21615688 |
| Gene | DLG1 | GO:0005783 | endoplasmic reticulum | 21615688 |
| Gene | DLG1 | GO:0005794 | Golgi apparatus | 21615688 |
| Gene | DLG1 | GO:0005874 | microtubule | 21615688 |
| Gene | DLG1 | GO:0005911 | cell-cell junction | 21615688 |
| Gene | DLG1 | GO:0005923 | bicellular tight junction | 17332497 |
| Gene | DLG1 | GO:0007015 | actin filament organization | 14699157 |
| Gene | DLG1 | GO:0009898 | cytoplasmic side of plasma membrane | 21615688 |
| Gene | DLG1 | GO:0015459 | potassium channel regulator activity | 12970345 |
| Gene | DLG1 | GO:0016323 | basolateral plasma membrane | 8922391 |
| Gene | DLG1 | GO:0030054 | cell junction | 12857860|17237226 |
| Gene | DLG1 | GO:0030866 | cortical actin cytoskeleton organization | 14699157 |
| Gene | DLG1 | GO:0042391 | regulation of membrane potential | 12970345 |
| Gene | DLG1 | GO:0043268 | positive regulation of potassium ion transport | 12970345 |
| Gene | DLG1 | GO:0048471 | perinuclear region of cytoplasm | 21615688 |
| Gene | DLG1 | GO:0070830 | bicellular tight junction assembly | 17332497 |
| Gene | DLG1 | GO:0097025 | MPP7-DLG1-LIN7 complex | 17237226 |
| Gene | DLG1 | GO:0097060 | synaptic membrane | 23676497 |
| Gene | DLG1 | GO:0098609 | cell-cell adhesion | 14699157 |
| Gene | DLG1 | GO:1902473 | regulation of protein localization to synapse | 23676497 |
| Gene | DLG1 | GO:1903078 | positive regulation of protein localization to plasma membrane | 12970345 |
AS Summary |
Information of the canonical protein with experimentally identified structure from PDB (2023). |
| UniProt Acc | File name | PDB ID | Method | Resolution | Chain | Start | End |
| Q12959-1 | Q12959-1_3w9y_A.pdb | 3W9Y | X-ray | 2.2 | A | 712 | 904 |
ASpdb's canonical and alternatively spliced isoform information. |
| accession_id | gene_name | canonical_id | alternative_id | canonical_length | alternative_length | canonical_start | canonical_end | type | originalSEQ | variationSEQ | alternative_start | alternative_end |
| Q12959 | DLG1 | Q12959-1 | Q12959-2 | 904 | 926 | 669 | 680 | Substitution | EIPDDMGSKGLK | QSFNDKRKKNLFSRKFPFYKNKDQSEQETSDADQ | 669 | 702 |
| Q12959 | DLG1 | Q12959-1 | Q12959-3 | 904 | 871 | 162 | 194 | Deletion | none | none | 161 | 161 |
| Q12959 | DLG1 | Q12959-1 | Q12959-4 | 904 | 893 | 162 | 194 | Deletion | none | none | 161 | 161 |
| Q12959 | DLG1 | Q12959-1 | Q12959-4 | 904 | 893 | 669 | 680 | Substitution | EIPDDMGSKGLK | QSFNDKRKKNLFSRKFPFYKNKDQSEQETSDADQ | 636 | 669 |
| Q12959 | DLG1 | Q12959-1 | Q12959-5 | 904 | 853 | 162 | 194 | Deletion | none | none | 161 | 161 |
| Q12959 | DLG1 | Q12959-1 | Q12959-5 | 904 | 853 | 195 | 212 | Deletion | none | none | 161 | 161 |
| Q12959 | DLG1 | Q12959-1 | Q12959-6 | 904 | 891 | 681 | 693 | Deletion | none | none | 680 | 680 |
| Q12959 | DLG1 | Q12959-1 | Q12959-7 | 904 | 917 | 693 | 693 | Substitution | Y | YLILITDEYGCSKG | 693 | 706 |
| Q12959 | DLG1 | Q12959-1 | Q12959-8 | 904 | 788 | 1 | 77 | Substitution | MPVRKQDTQRALHLLEEYRSKLSQTEDRQLRSSIERVINIFQSNLFQALIDIQEFYEVTLLDNPKCIDRSKPSEPIQ | MNYIFGNNTLLYSRGSRGGNTSSSHGSAGPKQKHWAKKGSSDELQAEPEPSRWQQIVAFFTRRHSFIDCISVATSST | 1 | 77 |
| Q12959 | DLG1 | Q12959-1 | Q12959-8 | 904 | 788 | 78 | 193 | Deletion | none | none | 77 | 77 |
| Q12959 | DLG1 | Q12959-1 | Q12959-9 | 904 | 800 | 1 | 77 | Substitution | MPVRKQDTQRALHLLEEYRSKLSQTEDRQLRSSIERVINIFQSNLFQALIDIQEFYEVTLLDNPKCIDRSKPSEPIQ | MNYIFGNNTLLYSRGSRGGNTSSSHGSAGPKQKHWAKKGSSDELQAEPEPSRWQQIVAFFTRRHSFIDCISVATSST | 1 | 77 |
| Q12959 | DLG1 | Q12959-1 | Q12959-9 | 904 | 800 | 78 | 193 | Deletion | none | none | 77 | 77 |
| Q12959 | DLG1 | Q12959-1 | Q12959-9 | 904 | 800 | 693 | 693 | Substitution | Y | YLILITDEYGCSKG | 577 | 590 |
| Q12959 | DLG1 | Q12959-1 | Q12959-9 | 904 | 800 | 694 | 694 | Deletion | none | none | 590 | 590 |
Multiple sequence alignment of our canonical and alternatively spliced DLG1 |
Matched gene isoform IDs with Ensembl and RefSeq of our canonical and alternative spliced genes of DLG1 |
| UniProt-id | ENSG | ENST | ENSP |
| Q12959-1 | ENSG00000075711.21 | ENST00000419354.5 | ENSP00000407531.1 |
| Q12959-1 | ENSG00000075711.21 | ENST00000448528.6 | ENSP00000391732.2 |
| Q12959-1 | ENSG00000075711.21 | ENST00000670935.1 | ENSP00000499437.1 |
| Q12959-2 | ENSG00000075711.21 | ENST00000346964.6 | ENSP00000345731.2 |
| Q12959-3 | ENSG00000075711.21 | ENST00000392382.6 | ENSP00000376187.2 |
| Q12959-3 | ENSG00000075711.21 | ENST00000655488.1 | ENSP00000499657.1 |
| Q12959-3 | ENSG00000075711.21 | ENST00000659716.1 | ENSP00000499602.1 |
| Q12959-3 | ENSG00000075711.21 | ENST00000661453.1 | ENSP00000499514.1 |
| Q12959-3 | ENSG00000075711.21 | ENST00000663148.1 | ENSP00000499384.1 |
| Q12959-3 | ENSG00000075711.21 | ENST00000671185.1 | ENSP00000499580.1 |
| Q12959-4 | ENSG00000075711.21 | ENST00000357674.9 | ENSP00000350303.6 |
| Q12959-4 | ENSG00000075711.21 | ENST00000450955.5 | ENSP00000411278.1 |
| Q12959-4 | ENSG00000075711.21 | ENST00000667157.1 | ENSP00000499414.1 |
| Q12959-4 | ENSG00000075711.21 | ENST00000669565.1 | ENSP00000499413.1 |
| Q12959-4 | ENSG00000075711.21 | ENST00000670455.1 | ENSP00000499542.1 |
| Q12959-5 | ENSG00000075711.21 | ENST00000422288.6 | ENSP00000413238.1 |
| Q12959-5 | ENSG00000075711.21 | ENST00000666007.1 | ENSP00000499793.1 |
| Q12959-8 | ENSG00000075711.21 | ENST00000452595.5 | ENSP00000398939.1 |
| Q12959-9 | ENSG00000075711.21 | ENST00000443183.5 | ENSP00000396658.1 |
| UniProt-id | NM ID | NP ID |
| Q12959-1 | NM_001098424.1 | NP_001091894.1 |
| Q12959-1 | NM_001290983.1 | NP_001277912.1 |
| Q12959-1 | XM_011512502.2 | XP_011510804.1 |
| Q12959-2 | NM_004087.2 | NP_004078.2 |
| Q12959-2 | XM_005269289.3 | XP_005269346.1 |
| Q12959-2 | XM_017005800.1 | XP_016861289.1 |
| Q12959-2 | XM_017005801.1 | XP_016861290.1 |
| Q12959-2 | XM_017005802.1 | XP_016861291.1 |
| Q12959-2 | XM_017005803.1 | XP_016861292.1 |
| Q12959-8 | NM_001204388.1 | NP_001191317.1 |
| Q12959-9 | NM_001204387.1 | NP_001191316.1 |
Amino acid sequences of our canonical and alternatively spliced DLG1 |
| accession_id | Protein sequence |
| Q12959-1 | MPVRKQDTQRALHLLEEYRSKLSQTEDRQLRSSIERVINIFQSNLFQALIDIQEFYEVTLLDNPKCIDRSKPSEPIQPVNTWEISSLPSS TVTSETLPSSLSPSVEKYRYQDEDTPPQEHISPQITNEVIGPELVHVSEKNLSEIENVHGFVSHSHISPIKPTEAVLPSPPTVPVIPVLP VPAENTVILPTIPQANPPPVLVNTDSLETPTYVNGTDADYEYEEITLERGNSGLGFSIAGGTDNPHIGDDSSIFITKIITGGAAAQDGRL RVNDCILRVNEVDVRDVTHSKAVEALKEAGSIVRLYVKRRKPVSEKIMEIKLIKGPKGLGFSIAGGVGNQHIPGDNSIYVTKIIEGGAAH KDGKLQIGDKLLAVNNVCLEEVTHEEAVTALKNTSDFVYLKVAKPTSMYMNDGYAPPDITNSSSQPVDNHVSPSSFLGQTPASPARYSPV SKAVLGDDEITREPRKVVLHRGSTGLGFNIVGGEDGEGIFISFILAGGPADLSGELRKGDRIISVNSVDLRAASHEQAAAALKNAGQAVT IVAQYRPEEYSRFEAKIHDLREQMMNSSISSGSGSLRTSQKRSLYVRALFDYDKTKDSGLPSQGLNFKFGDILHVINASDDEWWQARQVT PDGESDEVGVIPSKRRVEKKERARLKTVKFNSKTRDKGEIPDDMGSKGLKHVTSNASDSESSYRGQEEYVLSYEPVNQQEVNYTRPVIIL GPMKDRINDDLISEFPDKFGSCVPHTTRPKRDYEVDGRDYHFVTSREQMEKDIQEHKFIEAGQYNNHLYGTSVQSVREVAEKGKHCILDV SGNAIKRLQIAQLYPISIFIKPKSMENIMEMNKRLTEEQARKTFERAMKLEQEFTEHFTAIVQGDTLEDIYNQVKQIIEEQSGSYIWVPA |
| Q12959-2 | MPVRKQDTQRALHLLEEYRSKLSQTEDRQLRSSIERVINIFQSNLFQALIDIQEFYEVTLLDNPKCIDRSKPSEPIQPVNTWEISSLPSS TVTSETLPSSLSPSVEKYRYQDEDTPPQEHISPQITNEVIGPELVHVSEKNLSEIENVHGFVSHSHISPIKPTEAVLPSPPTVPVIPVLP VPAENTVILPTIPQANPPPVLVNTDSLETPTYVNGTDADYEYEEITLERGNSGLGFSIAGGTDNPHIGDDSSIFITKIITGGAAAQDGRL RVNDCILRVNEVDVRDVTHSKAVEALKEAGSIVRLYVKRRKPVSEKIMEIKLIKGPKGLGFSIAGGVGNQHIPGDNSIYVTKIIEGGAAH KDGKLQIGDKLLAVNNVCLEEVTHEEAVTALKNTSDFVYLKVAKPTSMYMNDGYAPPDITNSSSQPVDNHVSPSSFLGQTPASPARYSPV SKAVLGDDEITREPRKVVLHRGSTGLGFNIVGGEDGEGIFISFILAGGPADLSGELRKGDRIISVNSVDLRAASHEQAAAALKNAGQAVT IVAQYRPEEYSRFEAKIHDLREQMMNSSISSGSGSLRTSQKRSLYVRALFDYDKTKDSGLPSQGLNFKFGDILHVINASDDEWWQARQVT PDGESDEVGVIPSKRRVEKKERARLKTVKFNSKTRDKGQSFNDKRKKNLFSRKFPFYKNKDQSEQETSDADQHVTSNASDSESSYRGQEE YVLSYEPVNQQEVNYTRPVIILGPMKDRINDDLISEFPDKFGSCVPHTTRPKRDYEVDGRDYHFVTSREQMEKDIQEHKFIEAGQYNNHL YGTSVQSVREVAEKGKHCILDVSGNAIKRLQIAQLYPISIFIKPKSMENIMEMNKRLTEEQARKTFERAMKLEQEFTEHFTAIVQGDTLE |
| Q12959-3 | MPVRKQDTQRALHLLEEYRSKLSQTEDRQLRSSIERVINIFQSNLFQALIDIQEFYEVTLLDNPKCIDRSKPSEPIQPVNTWEISSLPSS TVTSETLPSSLSPSVEKYRYQDEDTPPQEHISPQITNEVIGPELVHVSEKNLSEIENVHGFVSHSHISPIKANPPPVLVNTDSLETPTYV NGTDADYEYEEITLERGNSGLGFSIAGGTDNPHIGDDSSIFITKIITGGAAAQDGRLRVNDCILRVNEVDVRDVTHSKAVEALKEAGSIV RLYVKRRKPVSEKIMEIKLIKGPKGLGFSIAGGVGNQHIPGDNSIYVTKIIEGGAAHKDGKLQIGDKLLAVNNVCLEEVTHEEAVTALKN TSDFVYLKVAKPTSMYMNDGYAPPDITNSSSQPVDNHVSPSSFLGQTPASPARYSPVSKAVLGDDEITREPRKVVLHRGSTGLGFNIVGG EDGEGIFISFILAGGPADLSGELRKGDRIISVNSVDLRAASHEQAAAALKNAGQAVTIVAQYRPEEYSRFEAKIHDLREQMMNSSISSGS GSLRTSQKRSLYVRALFDYDKTKDSGLPSQGLNFKFGDILHVINASDDEWWQARQVTPDGESDEVGVIPSKRRVEKKERARLKTVKFNSK TRDKGEIPDDMGSKGLKHVTSNASDSESSYRGQEEYVLSYEPVNQQEVNYTRPVIILGPMKDRINDDLISEFPDKFGSCVPHTTRPKRDY EVDGRDYHFVTSREQMEKDIQEHKFIEAGQYNNHLYGTSVQSVREVAEKGKHCILDVSGNAIKRLQIAQLYPISIFIKPKSMENIMEMNK |
| Q12959-4 | MPVRKQDTQRALHLLEEYRSKLSQTEDRQLRSSIERVINIFQSNLFQALIDIQEFYEVTLLDNPKCIDRSKPSEPIQPVNTWEISSLPSS TVTSETLPSSLSPSVEKYRYQDEDTPPQEHISPQITNEVIGPELVHVSEKNLSEIENVHGFVSHSHISPIKANPPPVLVNTDSLETPTYV NGTDADYEYEEITLERGNSGLGFSIAGGTDNPHIGDDSSIFITKIITGGAAAQDGRLRVNDCILRVNEVDVRDVTHSKAVEALKEAGSIV RLYVKRRKPVSEKIMEIKLIKGPKGLGFSIAGGVGNQHIPGDNSIYVTKIIEGGAAHKDGKLQIGDKLLAVNNVCLEEVTHEEAVTALKN TSDFVYLKVAKPTSMYMNDGYAPPDITNSSSQPVDNHVSPSSFLGQTPASPARYSPVSKAVLGDDEITREPRKVVLHRGSTGLGFNIVGG EDGEGIFISFILAGGPADLSGELRKGDRIISVNSVDLRAASHEQAAAALKNAGQAVTIVAQYRPEEYSRFEAKIHDLREQMMNSSISSGS GSLRTSQKRSLYVRALFDYDKTKDSGLPSQGLNFKFGDILHVINASDDEWWQARQVTPDGESDEVGVIPSKRRVEKKERARLKTVKFNSK TRDKGQSFNDKRKKNLFSRKFPFYKNKDQSEQETSDADQHVTSNASDSESSYRGQEEYVLSYEPVNQQEVNYTRPVIILGPMKDRINDDL ISEFPDKFGSCVPHTTRPKRDYEVDGRDYHFVTSREQMEKDIQEHKFIEAGQYNNHLYGTSVQSVREVAEKGKHCILDVSGNAIKRLQIA |
| Q12959-5 | MPVRKQDTQRALHLLEEYRSKLSQTEDRQLRSSIERVINIFQSNLFQALIDIQEFYEVTLLDNPKCIDRSKPSEPIQPVNTWEISSLPSS TVTSETLPSSLSPSVEKYRYQDEDTPPQEHISPQITNEVIGPELVHVSEKNLSEIENVHGFVSHSHISPIKVNGTDADYEYEEITLERGN SGLGFSIAGGTDNPHIGDDSSIFITKIITGGAAAQDGRLRVNDCILRVNEVDVRDVTHSKAVEALKEAGSIVRLYVKRRKPVSEKIMEIK LIKGPKGLGFSIAGGVGNQHIPGDNSIYVTKIIEGGAAHKDGKLQIGDKLLAVNNVCLEEVTHEEAVTALKNTSDFVYLKVAKPTSMYMN DGYAPPDITNSSSQPVDNHVSPSSFLGQTPASPARYSPVSKAVLGDDEITREPRKVVLHRGSTGLGFNIVGGEDGEGIFISFILAGGPAD LSGELRKGDRIISVNSVDLRAASHEQAAAALKNAGQAVTIVAQYRPEEYSRFEAKIHDLREQMMNSSISSGSGSLRTSQKRSLYVRALFD YDKTKDSGLPSQGLNFKFGDILHVINASDDEWWQARQVTPDGESDEVGVIPSKRRVEKKERARLKTVKFNSKTRDKGEIPDDMGSKGLKH VTSNASDSESSYRGQEEYVLSYEPVNQQEVNYTRPVIILGPMKDRINDDLISEFPDKFGSCVPHTTRPKRDYEVDGRDYHFVTSREQMEK DIQEHKFIEAGQYNNHLYGTSVQSVREVAEKGKHCILDVSGNAIKRLQIAQLYPISIFIKPKSMENIMEMNKRLTEEQARKTFERAMKLE |
| Q12959-6 | MPVRKQDTQRALHLLEEYRSKLSQTEDRQLRSSIERVINIFQSNLFQALIDIQEFYEVTLLDNPKCIDRSKPSEPIQPVNTWEISSLPSS TVTSETLPSSLSPSVEKYRYQDEDTPPQEHISPQITNEVIGPELVHVSEKNLSEIENVHGFVSHSHISPIKPTEAVLPSPPTVPVIPVLP VPAENTVILPTIPQANPPPVLVNTDSLETPTYVNGTDADYEYEEITLERGNSGLGFSIAGGTDNPHIGDDSSIFITKIITGGAAAQDGRL RVNDCILRVNEVDVRDVTHSKAVEALKEAGSIVRLYVKRRKPVSEKIMEIKLIKGPKGLGFSIAGGVGNQHIPGDNSIYVTKIIEGGAAH KDGKLQIGDKLLAVNNVCLEEVTHEEAVTALKNTSDFVYLKVAKPTSMYMNDGYAPPDITNSSSQPVDNHVSPSSFLGQTPASPARYSPV SKAVLGDDEITREPRKVVLHRGSTGLGFNIVGGEDGEGIFISFILAGGPADLSGELRKGDRIISVNSVDLRAASHEQAAAALKNAGQAVT IVAQYRPEEYSRFEAKIHDLREQMMNSSISSGSGSLRTSQKRSLYVRALFDYDKTKDSGLPSQGLNFKFGDILHVINASDDEWWQARQVT PDGESDEVGVIPSKRRVEKKERARLKTVKFNSKTRDKGEIPDDMGSKGLKRGQEEYVLSYEPVNQQEVNYTRPVIILGPMKDRINDDLIS EFPDKFGSCVPHTTRPKRDYEVDGRDYHFVTSREQMEKDIQEHKFIEAGQYNNHLYGTSVQSVREVAEKGKHCILDVSGNAIKRLQIAQL |
| Q12959-7 | MPVRKQDTQRALHLLEEYRSKLSQTEDRQLRSSIERVINIFQSNLFQALIDIQEFYEVTLLDNPKCIDRSKPSEPIQPVNTWEISSLPSS TVTSETLPSSLSPSVEKYRYQDEDTPPQEHISPQITNEVIGPELVHVSEKNLSEIENVHGFVSHSHISPIKPTEAVLPSPPTVPVIPVLP VPAENTVILPTIPQANPPPVLVNTDSLETPTYVNGTDADYEYEEITLERGNSGLGFSIAGGTDNPHIGDDSSIFITKIITGGAAAQDGRL RVNDCILRVNEVDVRDVTHSKAVEALKEAGSIVRLYVKRRKPVSEKIMEIKLIKGPKGLGFSIAGGVGNQHIPGDNSIYVTKIIEGGAAH KDGKLQIGDKLLAVNNVCLEEVTHEEAVTALKNTSDFVYLKVAKPTSMYMNDGYAPPDITNSSSQPVDNHVSPSSFLGQTPASPARYSPV SKAVLGDDEITREPRKVVLHRGSTGLGFNIVGGEDGEGIFISFILAGGPADLSGELRKGDRIISVNSVDLRAASHEQAAAALKNAGQAVT IVAQYRPEEYSRFEAKIHDLREQMMNSSISSGSGSLRTSQKRSLYVRALFDYDKTKDSGLPSQGLNFKFGDILHVINASDDEWWQARQVT PDGESDEVGVIPSKRRVEKKERARLKTVKFNSKTRDKGEIPDDMGSKGLKHVTSNASDSESSYLILITDEYGCSKGRGQEEYVLSYEPVN QQEVNYTRPVIILGPMKDRINDDLISEFPDKFGSCVPHTTRPKRDYEVDGRDYHFVTSREQMEKDIQEHKFIEAGQYNNHLYGTSVQSVR EVAEKGKHCILDVSGNAIKRLQIAQLYPISIFIKPKSMENIMEMNKRLTEEQARKTFERAMKLEQEFTEHFTAIVQGDTLEDIYNQVKQI |
| Q12959-8 | MNYIFGNNTLLYSRGSRGGNTSSSHGSAGPKQKHWAKKGSSDELQAEPEPSRWQQIVAFFTRRHSFIDCISVATSSTQANPPPVLVNTDS LETPTYVNGTDADYEYEEITLERGNSGLGFSIAGGTDNPHIGDDSSIFITKIITGGAAAQDGRLRVNDCILRVNEVDVRDVTHSKAVEAL KEAGSIVRLYVKRRKPVSEKIMEIKLIKGPKGLGFSIAGGVGNQHIPGDNSIYVTKIIEGGAAHKDGKLQIGDKLLAVNNVCLEEVTHEE AVTALKNTSDFVYLKVAKPTSMYMNDGYAPPDITNSSSQPVDNHVSPSSFLGQTPASPARYSPVSKAVLGDDEITREPRKVVLHRGSTGL GFNIVGGEDGEGIFISFILAGGPADLSGELRKGDRIISVNSVDLRAASHEQAAAALKNAGQAVTIVAQYRPEEYSRFEAKIHDLREQMMN SSISSGSGSLRTSQKRSLYVRALFDYDKTKDSGLPSQGLNFKFGDILHVINASDDEWWQARQVTPDGESDEVGVIPSKRRVEKKERARLK TVKFNSKTRDKGEIPDDMGSKGLKHVTSNASDSESSYRGQEEYVLSYEPVNQQEVNYTRPVIILGPMKDRINDDLISEFPDKFGSCVPHT TRPKRDYEVDGRDYHFVTSREQMEKDIQEHKFIEAGQYNNHLYGTSVQSVREVAEKGKHCILDVSGNAIKRLQIAQLYPISIFIKPKSME |
| Q12959-9 | MNYIFGNNTLLYSRGSRGGNTSSSHGSAGPKQKHWAKKGSSDELQAEPEPSRWQQIVAFFTRRHSFIDCISVATSSTQANPPPVLVNTDS LETPTYVNGTDADYEYEEITLERGNSGLGFSIAGGTDNPHIGDDSSIFITKIITGGAAAQDGRLRVNDCILRVNEVDVRDVTHSKAVEAL KEAGSIVRLYVKRRKPVSEKIMEIKLIKGPKGLGFSIAGGVGNQHIPGDNSIYVTKIIEGGAAHKDGKLQIGDKLLAVNNVCLEEVTHEE AVTALKNTSDFVYLKVAKPTSMYMNDGYAPPDITNSSSQPVDNHVSPSSFLGQTPASPARYSPVSKAVLGDDEITREPRKVVLHRGSTGL GFNIVGGEDGEGIFISFILAGGPADLSGELRKGDRIISVNSVDLRAASHEQAAAALKNAGQAVTIVAQYRPEEYSRFEAKIHDLREQMMN SSISSGSGSLRTSQKRSLYVRALFDYDKTKDSGLPSQGLNFKFGDILHVINASDDEWWQARQVTPDGESDEVGVIPSKRRVEKKERARLK TVKFNSKTRDKGEIPDDMGSKGLKHVTSNASDSESSYLILITDEYGCSKGGQEEYVLSYEPVNQQEVNYTRPVIILGPMKDRINDDLISE FPDKFGSCVPHTTRPKRDYEVDGRDYHFVTSREQMEKDIQEHKFIEAGQYNNHLYGTSVQSVREVAEKGKHCILDVSGNAIKRLQIAQLY |
Protein Functional Features |
Main function of this protein. (from UniProt) |
| DLG1 (go to UniProt):Q12959 |
Retention analysis result of protein across 39 protein features of UniProt such as six molecule processing features, 13 region features, four site features, six amino acid modification features, two natural variation features, five experimental info features, and 3 secondary structure features. Here, because of limited space for viewing, we only show the protein feature retention information belong to the 13 regional features. All retention annotation result can be downloaded at * Minus value of BPloci means that the break pointn is located before the CDS. |
| - Retained protein feature among the 13 regional features. |
| Accession_id | Subsection | Start | End | Funcitonal feature | Splicing information |
| Q12959 | Domain | 4 | 64 | Note=L27;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00365 | Type=Substitution;Start=1;End=77 |
| Q12959 | Domain | 4 | 64 | Note=L27;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00365 | Type=Substitution;Start=1;End=77 |
| Q12959 | Region | 162 | 212 | Note=Interaction with SH3 domains | Type=Deletion;Start=162;End=194 |
| Q12959 | Region | 162 | 212 | Note=Interaction with SH3 domains | Type=Deletion;Start=162;End=194 |
| Q12959 | Region | 162 | 212 | Note=Interaction with SH3 domains | Type=Deletion;Start=162;End=194 |
| Q12959 | Region | 162 | 212 | Note=Interaction with SH3 domains | Type=Deletion;Start=195;End=212 |
| Q12959 | Region | 162 | 212 | Note=Interaction with SH3 domains | Type=Deletion;Start=78;End=193 |
| Q12959 | Region | 162 | 212 | Note=Interaction with SH3 domains | Type=Deletion;Start=78;End=193 |
| Q12959 | Region | 662 | 693 | Note=Disordered;Ontology_term=ECO:0000256;evidence=ECO:0000256|SAM:MobiDB-lite | Type=Substitution;Start=669;End=680 |
| Q12959 | Region | 662 | 693 | Note=Disordered;Ontology_term=ECO:0000256;evidence=ECO:0000256|SAM:MobiDB-lite | Type=Substitution;Start=669;End=680 |
| Q12959 | Region | 662 | 693 | Note=Disordered;Ontology_term=ECO:0000256;evidence=ECO:0000256|SAM:MobiDB-lite | Type=Deletion;Start=681;End=693 |
| Q12959 | Region | 662 | 693 | Note=Disordered;Ontology_term=ECO:0000256;evidence=ECO:0000256|SAM:MobiDB-lite | Type=Substitution;Start=693;End=693 |
| Q12959 | Region | 662 | 693 | Note=Disordered;Ontology_term=ECO:0000256;evidence=ECO:0000256|SAM:MobiDB-lite | Type=Substitution;Start=693;End=693 |
| Q12959 | Compositional bias | 662 | 676 | Note=Basic and acidic residues;Ontology_term=ECO:0000256;evidence=ECO:0000256|SAM:MobiDB-lite | Type=Substitution;Start=669;End=680 |
| Q12959 | Compositional bias | 662 | 676 | Note=Basic and acidic residues;Ontology_term=ECO:0000256;evidence=ECO:0000256|SAM:MobiDB-lite | Type=Substitution;Start=669;End=680 |
Gene Isoform Structures and Expression Levels for DLG1 |
Gene structures of our canonical and alternative spliced genes of DLG1* Click on the image to open the UCSC genome browser with custom track showing this image in a new window. |
Expression levels of gene isoforms across GTEx. |
Expression levels of gene isoforms across TCGA. |
Protein Structures |
PDB and CIF files of the predicted protein structures * Here we show the 3D structure of the proteins using Mol*. AlphaFold produces a per-residue confidence score (pLDDT) between 0 and 100. Model confidence is shown from the pLDDT values per residue. pLDDT corresponds to the model’s prediction of its score on the local Distance Difference Test. It is a measure of local accuracy (from AlphfaFold website). To color code individual residues, we transformed individual PDB files into CIF format. |
| 3D view using mol* of Q12959-1 |
| 3D view using mol* of Q12959-2 |
| 3D view using mol* of Q12959-3 |
| 3D view using mol* of Q12959-4 |
| 3D view using mol* of Q12959-5 |
| 3D view using mol* of Q12959-6 |
| 3D view using mol* of Q12959-7 |
| 3D view using mol* of Q12959-8 |
| 3D view using mol* of Q12959-9 |
pLDDT Score Distribution |
pLDDT score distribution of the predicted protein structures from AlphaFold2* AlphaFold produces a per-residue confidence score (pLDDT) between 0 and 100. |
Ramachandran Plot of Protein Structures |
Ramachandran plot of the torsional angles - phi (φ)and psi (ψ) - of the residues (amino acids) contained in this protein peptide. |
Potential Active Site Information |
The potential binding sites of these proteins were identified using SiteMap, a module of the Schrodinger suite. |
| UniProt-id | Site score | Size | D score | Volume | Exposure | Enclosure | Contact | Phobic | Philic | Balance | Don/Acc | Residues |
| Q12959-1 | 1.051 | 614 | 1.075 | 1812.069 | 0.497 | 0.754 | 0.963 | 0.732 | 0.972 | 0.753 | 0.857 | 129,130,131,132,133,134,135,136,137,141,142,144,14 5,146,147,148,149,150,151,152,153,154,324,327,328, 329,330,331,332,333,339,352,354,384,388,391,392,71 8,719,720,721,722,723,724,725,728,729,732,741,742, 743,744,745,748,751,753,754,758,759,760,761,770,77 3,774,776,778,779,780,781,782,783,784,788,789,790, 791,792,795,798,799,802,807,808,809,810,811,813,81 4,816,817,820,838,842,845,849,853,856,857,860 |
| Q12959-2 | 1.083 | 285 | 1.118 | 1050.952 | 0.487 | 0.775 | 0.984 | 0.979 | 0.879 | 1.115 | 1.203 | 135,136,137,141,142,144,145,146,148,149,151,152,74 2,743,744,745,746,747,748,750,751,754,763,764,765, 766,770,773,782,802,803,804,805,806,811,812,813,82 9,830,831,832,833,860,864,867,875,878,879,881,882 |
| Q12959-3 | 1.046 | 262 | 1.091 | 971.376 | 0.581 | 0.709 | 0.918 | 0.793 | 0.842 | 0.942 | 1.049 | 132,133,134,135,136,137,139,153,154,155,156,157,15 8,159,160,686,687,688,689,690,691,692,693,711,727, 746,747,748,749,750,751,756,757,758,775,776,777,77 8,780,781,784,808,809,820,823,824,826,827,843,844, 845,848 |
| Q12959-4 | 1.05 | 271 | 1.101 | 1170.316 | 0.622 | 0.704 | 0.863 | 0.692 | 0.801 | 0.863 | 1.193 | 135,136,137,141,142,144,145,146,148,149,709,710,71 1,712,713,714,717,718,729,730,731,732,733,734,747, 748,749,750,761,766,767,769,770,771,772,773,778,77 9,780,781,783,784,787,788,791,796,797,798,799,800, 802,834,841,842,845,846,848,849,852,853 |
| Q12959-5 | 1.132 | 118 | 1.161 | 177.674 | 0.263 | 0.852 | 1.137 | 1.781 | 0.889 | 2.003 | 1.27 | 134,135,136,137,139,722,723,725,727,728,729,730,73 1,737,760,762,763,765,766 |
| Q12959-6 | 1.005 | 299 | 1.047 | 1090.74 | 0.629 | 0.661 | 0.824 | 0.593 | 0.887 | 0.669 | 0.675 | 134,135,136,137,138,139,140,141,142,143,144,146,14 7,148,149,707,708,709,710,711,712,713,715,728,729, 731,767,768,769,770,771,772,773,776,777,778,794,79 5,796,797,798,825,829,832,836,839,840,843,844,846, 847 |
| Q12959-7 | 1.015 | 220 | 1.046 | 985.782 | 0.625 | 0.695 | 0.89 | 0.553 | 0.954 | 0.58 | 0.936 | 151,152,153,154,155,156,157,321,322,323,324,325,32 6,327,328,332,352,354,355,356,357,358,361,362,693, 694,737,738,741,742,745,754,755,757,764,766,767,77 2,773,793,794,795,797,802,803,804,820,821,822,823 |
| Q12959-8 | 1.044 | 143 | 1.062 | 260.68 | 0.507 | 0.758 | 0.955 | 0.765 | 1.021 | 0.749 | 0.784 | 1,2,3,4,6,609,612,616,625,626,627,628,642,643,645, 664,665,666,674,675,679,682,683,686,691,692,693,69 4 |
| Q12959-9 | 1.025 | 654 | 1.045 | 2076.865 | 0.539 | 0.731 | 0.909 | 0.51 | 1.024 | 0.498 | 0.684 | 1,2,3,4,5,6,7,8,9,10,11,12,78,79,80,81,82,83,84,85 ,86,208,211,212,213,214,215,216,217,236,237,238,23 9,272,275,276,574,577,578,614,615,616,617,618,619, 620,621,622,624,625,628,636,637,638,639,640,644,64 7,649,650,651,653,654,655,656,657,676,678,680,681, 683,685,686,687,691,694,695,698,700,703,704,705,70 6,707,737,738,741,742,743,744,745,748,749,752,753, 755,756,773 |
Protein Structure and Feature Comparision |
Protein Structure Comparision Using Template Modeling Scores (TM-score). |
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Protein Structure Comparision Visualization with mol*. between Canonical predicted structure (AF2)(orange) vs Canonical validated structure (PDB)(green) |
| 3D view using mol* of Q12959-1_Q12959-1_3w9y_A.pdb |
Protein Structure Comparision Visualization with mol*. between Canonical validated structure (PDB)(orange) vs Alternative predicted structure (AF2)(green) |
| 3D view using mol* of Q12959-1_3w9y_A_Q12959-2.pdb |
| 3D view using mol* of Q12959-1_3w9y_A_Q12959-3.pdb |
| 3D view using mol* of Q12959-1_3w9y_A_Q12959-4.pdb |
| 3D view using mol* of Q12959-1_3w9y_A_Q12959-5.pdb |
| 3D view using mol* of Q12959-1_3w9y_A_Q12959-6.pdb |
| 3D view using mol* of Q12959-1_3w9y_A_Q12959-7.pdb |
| 3D view using mol* of Q12959-1_3w9y_A_Q12959-8.pdb |
| 3D view using mol* of Q12959-1_3w9y_A_Q12959-9.pdb |
Protein Structure Comparision Visualization with mol*. between Canonical predicted structure (AF2)(orange) vs Alternative predicted structure (AF2)(green) |
| 3D view using mol* of Q12959-1_Q12959-2.pdb |
| 3D view using mol* of Q12959-1_Q12959-3.pdb |
| 3D view using mol* of Q12959-1_Q12959-4.pdb |
| 3D view using mol* of Q12959-1_Q12959-5.pdb |
| 3D view using mol* of Q12959-1_Q12959-6.pdb |
| 3D view using mol* of Q12959-1_Q12959-7.pdb |
| 3D view using mol* of Q12959-1_Q12959-8.pdb |
| 3D view using mol* of Q12959-1_Q12959-9.pdb |
Protein Feature Comparison of the protein sequendary structures among the protiens. |
Protein Feature Comparison of the relative accessible surface area (ASA) among the protiens. |
Protein-Protein Interaction |
Interactors from UniProt. |
| Accession_id | Subsection | Start | End | Funcitonal feature | Splicing information |
| Q12959 | Region | 162 | 212 | Note=Interaction with SH3 domains | Type=Deletion;Start=162;End=194 |
| Q12959 | Region | 162 | 212 | Note=Interaction with SH3 domains | Type=Deletion;Start=162;End=194 |
| Q12959 | Region | 162 | 212 | Note=Interaction with SH3 domains | Type=Deletion;Start=162;End=194 |
| Q12959 | Region | 162 | 212 | Note=Interaction with SH3 domains | Type=Deletion;Start=195;End=212 |
| Q12959 | Region | 162 | 212 | Note=Interaction with SH3 domains | Type=Deletion;Start=78;End=193 |
| Q12959 | Region | 162 | 212 | Note=Interaction with SH3 domains | Type=Deletion;Start=78;End=193 |
Interactors from STRING. |
| Gene name | Interactors |
Related Drugs to DLG1 |
Drugs targeting this gene/protein. (DrugBank) |
| UniProt accession | Gene name | DrugBank ID | Drug name | Drug group | Actions |
Related Diseases to DLG1 |
Previous studies relating to the alternative splicing of DLG1 and disease information from the MeSH term (PubMed) |
| Gene | PMID | Title | Abstract | MeSH ID | MeSH term |
| DLG1 | 9621517 | Identification of brain-specific splicing variants of the hDLG1 gene and altered splicing in neuroblastoma cell lines. | The human homologue of Drosophila tumor suppressor dlg, hDLG1, is one of the proteins known to interact with APC, a tumor suppressor for colorectal cancer. Alternative splicing of this gene generates transcripts either with [insertion 1 (I1)] or without 99 nucleotides in the 5' part of the dlg homology repeats (DHR) domain. We found almost equivalent expression of these two splicing variants in most human tissues; however, in skeletal muscle the transcript with the 99-bp insertion was predominant, and in the brain, that without the 99-bp insertion was expressed predominantly. We also examined alternative splicing in the region between the SH3 and GUK domains where two different sizes of insertions, 34 nucleotides (I2) or 100 nucleotides (I3), had been reported, and found various splicing patterns among the tissues examined. In brain we detected six different, alternatively spliced transcripts, two of which included a novel, 36-bp, brain-specific exon encoding a peptide bearing significant homology to a portion of rat synapse-associated protein, SAP97/PSD95. Subsequently, we investigated the splicing patterns of the hDLG1 gene in 24 neuroblastoma cell lines. In two-thirds of these lines, the splicing patterns were altered from those observed in normal brain tissue. As one-third retained the normal brain-splicing pattern, the loss of normal splicing of hDLG1 may not in itself cause formation of tumors, but it might reflect the biological character of individual neuroblastomas. | D001932 | Brain Neoplasms |
| DLG1 | 9621517 | Identification of brain-specific splicing variants of the hDLG1 gene and altered splicing in neuroblastoma cell lines. | The human homologue of Drosophila tumor suppressor dlg, hDLG1, is one of the proteins known to interact with APC, a tumor suppressor for colorectal cancer. Alternative splicing of this gene generates transcripts either with [insertion 1 (I1)] or without 99 nucleotides in the 5' part of the dlg homology repeats (DHR) domain. We found almost equivalent expression of these two splicing variants in most human tissues; however, in skeletal muscle the transcript with the 99-bp insertion was predominant, and in the brain, that without the 99-bp insertion was expressed predominantly. We also examined alternative splicing in the region between the SH3 and GUK domains where two different sizes of insertions, 34 nucleotides (I2) or 100 nucleotides (I3), had been reported, and found various splicing patterns among the tissues examined. In brain we detected six different, alternatively spliced transcripts, two of which included a novel, 36-bp, brain-specific exon encoding a peptide bearing significant homology to a portion of rat synapse-associated protein, SAP97/PSD95. Subsequently, we investigated the splicing patterns of the hDLG1 gene in 24 neuroblastoma cell lines. In two-thirds of these lines, the splicing patterns were altered from those observed in normal brain tissue. As one-third retained the normal brain-splicing pattern, the loss of normal splicing of hDLG1 may not in itself cause formation of tumors, but it might reflect the biological character of individual neuroblastomas. | D005909 | Glioblastoma |
| DLG1 | 9621517 | Identification of brain-specific splicing variants of the hDLG1 gene and altered splicing in neuroblastoma cell lines. | The human homologue of Drosophila tumor suppressor dlg, hDLG1, is one of the proteins known to interact with APC, a tumor suppressor for colorectal cancer. Alternative splicing of this gene generates transcripts either with [insertion 1 (I1)] or without 99 nucleotides in the 5' part of the dlg homology repeats (DHR) domain. We found almost equivalent expression of these two splicing variants in most human tissues; however, in skeletal muscle the transcript with the 99-bp insertion was predominant, and in the brain, that without the 99-bp insertion was expressed predominantly. We also examined alternative splicing in the region between the SH3 and GUK domains where two different sizes of insertions, 34 nucleotides (I2) or 100 nucleotides (I3), had been reported, and found various splicing patterns among the tissues examined. In brain we detected six different, alternatively spliced transcripts, two of which included a novel, 36-bp, brain-specific exon encoding a peptide bearing significant homology to a portion of rat synapse-associated protein, SAP97/PSD95. Subsequently, we investigated the splicing patterns of the hDLG1 gene in 24 neuroblastoma cell lines. In two-thirds of these lines, the splicing patterns were altered from those observed in normal brain tissue. As one-third retained the normal brain-splicing pattern, the loss of normal splicing of hDLG1 may not in itself cause formation of tumors, but it might reflect the biological character of individual neuroblastomas. | D009447 | Neuroblastoma |
Clinically important variants in DLG1 |
(ClinVar, 04/20/2024) |
| accession_id | uniprot_id | gene_name | Type | Variant | Clinical_significance |
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