E9Q9R9 · DLG5_MOUSE
- ProteinDisks large homolog 5
- GeneDlg5
- StatusUniProtKB reviewed (Swiss-Prot)
- Organism
- Amino acids1921 (go to sequence)
- Protein existenceEvidence at protein level
- Annotation score5/5
Function
function
Acts as a regulator of the Hippo signaling pathway. Negatively regulates the Hippo signaling pathway by mediating the interaction of MARK3 with STK3/4, bringing them together to promote MARK3-dependent hyperphosphorylation and inactivation of STK3 kinase activity toward LATS1 (PubMed:28087714).
Positively regulates the Hippo signaling by mediating the interaction of SCRIB with STK4/MST1 and LATS1 which is important for the activation of the Hippo signaling pathway. Involved in regulating cell proliferation, maintenance of epithelial polarity, epithelial-mesenchymal transition (EMT), cell migration and invasion (By similarity).
Plays an important role in dendritic spine formation and synaptogenesis in cortical neurons; regulates synaptogenesis by enhancing the cell surface localization of N-cadherin (PubMed:25232112).
Acts as a positive regulator of hedgehog (Hh) signaling pathway. Plays a critical role in the early point of the SMO activity cycle by interacting with SMO at the ciliary base to induce the accumulation of KIF7 and GLI2 at the ciliary tip for GLI2 activation (PubMed:25644602).
Positively regulates the Hippo signaling by mediating the interaction of SCRIB with STK4/MST1 and LATS1 which is important for the activation of the Hippo signaling pathway. Involved in regulating cell proliferation, maintenance of epithelial polarity, epithelial-mesenchymal transition (EMT), cell migration and invasion (By similarity).
Plays an important role in dendritic spine formation and synaptogenesis in cortical neurons; regulates synaptogenesis by enhancing the cell surface localization of N-cadherin (PubMed:25232112).
Acts as a positive regulator of hedgehog (Hh) signaling pathway. Plays a critical role in the early point of the SMO activity cycle by interacting with SMO at the ciliary base to induce the accumulation of KIF7 and GLI2 at the ciliary tip for GLI2 activation (PubMed:25644602).
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 5
Gene names
Organism names
- Organism
- Strain
- Taxonomic lineageEukaryota > Metazoa > Chordata > Craniata > Vertebrata > Euteleostomi > Mammalia > Eutheria > Euarchontoglires > Glires > Rodentia > Myomorpha > Muroidea > Muridae > Murinae > Mus > Mus
Accessions
- Primary accessionE9Q9R9
- Secondary accessions
Proteomes
Organism-specific databases
Subcellular Location
UniProt Annotation
GO Annotation
Cell membrane ; Peripheral membrane protein
Note: Localized at sites of cell-cell contact.
Keywords
- Cellular component
Phenotypes & Variants
Features
Showing features for natural variant.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Natural variant | 1642 | in allele LP; loss of neuronal function and disruption of interactions between the SH3 and guanylate kinase-like domains | ||||
Sequence: L → P |
Variants
We now provide the "Disease & Variants" viewer in its own tab.
The viewer provides 108 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_0000440556 | 1-1921 | Disks large homolog 5 | |||
Sequence: MEPQRRELLAQCQQSLAQAMTEVEAVLGLLEAAGALSPGERRQLDEEAGGAKAELLLQLLLAKEQDHFQDLRAALEKTQPHLLPILYLNGVVGPPQSTEGAGSTYSVLSIMPSDSESSSSLSSVGTTGKAPSPPPLLTEQQANDTVENLSIQLRLMTRERNELRKRLAFATHGATFDKRPYHRLNPDYERLKIQCVRAMSDLQSLQNQHTNALKRCEEVAKETDFYHTLHSRLLSDQTQLKDDVDMLRRENGKLRRERNLLQQSWEDMKRLREEDQKEIGDLRAQQQQVLKHNGSSEILNKLYDTAMDKLEVVKKDYDALRKRYSEKVAMHNSDLSRLEQLGEENQRLQKQTEMLTQQRDTAIQLQHQCALSLRRFETIHHELSKATAQNKDLQWEMELLQSELTELRSKQVKTAKESEKYKEERDAVYSEYKLIMSERDQVISELDKLQTEVELAESKLKSSTSEKKAASEEMEALRQIKDTVTMDAGRANKEVEILRKQCKALCQELKEALQEADVAKCRRDWAFQERDKIVAERDSIRTLCDNLRRERDRAVSELAEALRSLDDTRKQKNDVSRELKELKEQMECQLEKEARFRQLMAHSSHDSAIDTDSMEWETEVVEFERETEDIDLKALGFDMAEGVNEPCFPGDCGIFVTKVDKGSIADGRLRVNDWLLRINDVDLINKDKKQAIKALLNGEGAINMVVRRRKSLGGKVVTPLHINLSGQKDSGISLENGVYAAAVVPGSPAAKEGSLAVGDRIVAINGIALDNKSLNECESLLRSCQDSLTLSLLKVFPQSSSWSGQNIFENIKDSDRMLSCRAHGPEVQAHNKRNLLQHNNSTQTDIFYTDRLEDRKELGHSGGSSSFLHKPFSGSSSPVSPQACPSTSERSLNSFRSDTSAERGYGLVDMRSQRPLLSFETEVGPCGAVEVPLDKIDPEGSNSGGTWPKAVLGSTSGPEKLSVYKKPKQRKSIFDPNTFKRPQTPPKIDYLLPGPGLTHSPQPSKRVGSLTPPKPPRRSDSIKFQHRLETSSESEATLVGSSPSTSPPSAPPPSMDPSEPTHASPPRKARVRIASSYHSEGDGDTSYLPAKKPCDEDLTSQKVDELGQKRRRPKSAPSFRPKISPVVIPAQCLEEQECVPAIGELSPEGQEWSPYSPGHASRHGNPLLYPNRPSVGTVPRSMTPGTTVGSILRNPIYTVRSHRVLPCGSPPVPRDAGSQSLSPSVQHQGRLSLDLSHRACSDYSEMRASQGSNSLPSSARLGSSSNLQFKAERIKIPLTPRYPRSVMGSDRGSLSHSECSTPPRSPLNIDTLSSCSQPQTTASTLPRIAVNPSSHGERRKDRPFVEEPRHVKVQKGSEPLGISIVSGEKGGVYVSKVTLGSIAHQAGLEYGDQLLEFNGINLRSATEQQARLIIGQQCDTITILAQYNPHIHQLNSHSRSSSHLDPAATPHSTLQGSSAGTPEHPSVIDPLMEQDEGPGTPPAKQSASSTRSVGDTTKKTPDPRIVFIKKSQLDLGVHLCGGNLHGVFVAEVEDDSPAKGPDGLVPGDLILEYGSLDMRSRTVEDVYVEMLKPKDSLRLKVQYRHEEFTRVKGLPGDSFYIRALYDRLAEVEPELSFKKDDILYVDDTLPQGVFGSWMAWQLDENAQKIQRGQIPSKYVMDQEFSRRLSMSEVKDDNTAKTLSAAARRSFFRRKHKHKRSGSKDGKDLLALDTFSNDSIPLFEDSVSLAYQRVQKVDCTSLRPVLLLGPLLDVVKEMLVNEAPGKFCRCPLEVMKASQQAIERGVKDCLFVDYKRRSGHFDVTTVASIKEITEKNRHCLLDIAPHAIERLHHMHIYPIVIFIRYKSAKHIKEQRDPVYLRDKVTQRHSKEQFETAQKIDQEYSRYFTGVVQGGALSSICTQILAMVSQEQSKVLWIPACPP | ||||||
Modified residue | 264 | Phosphoserine | ||||
Sequence: S | ||||||
Modified residue | 295 | Phosphoserine | ||||
Sequence: S | ||||||
Modified residue | 900 | Phosphoserine | ||||
Sequence: S | ||||||
Modified residue | 984 | Phosphothreonine | ||||
Sequence: T | ||||||
Modified residue | 1000 | Phosphoserine | ||||
Sequence: S | ||||||
Modified residue | 1011 | Phosphothreonine | ||||
Sequence: T | ||||||
Modified residue | 1021 | Phosphoserine | ||||
Sequence: S | ||||||
Modified residue | 1183 | Phosphothreonine | ||||
Sequence: T | ||||||
Modified residue | 1209 | Phosphoserine | ||||
Sequence: S | ||||||
Modified residue | 1263 | Phosphoserine | ||||
Sequence: S | ||||||
Modified residue | 1334 | Phosphoserine | ||||
Sequence: S | ||||||
Modified residue | 1669 | Phosphoserine | ||||
Sequence: S |
Keywords
- PTM
Proteomic databases
PTM databases
Expression
Interaction
Subunit
Interacts with MPP1. Interacts with CTNNB1 and with the third SH3 domain of SORBS3 to form a ternary complex (By similarity).
Interacts (via coiled-coil domain) with MARK3. Interacts (via PDZ domain 3) with STK3/MST2 and STK4/MST1 (PubMed:28087714).
Interacts with SCRIB (By similarity).
Interacts with CTNB1 (PubMed:25232112).
Interacts with SMO and (via PDZ4 or guanylate kinase-like domain) with KIF7 (PubMed:25644602).
Interacts (via coiled-coil domain) with MARK3. Interacts (via PDZ domain 3) with STK3/MST2 and STK4/MST1 (PubMed:28087714).
Interacts with SCRIB (By similarity).
Interacts with CTNB1 (PubMed:25232112).
Interacts with SMO and (via PDZ4 or guanylate kinase-like domain) with KIF7 (PubMed:25644602).
Protein-protein interaction databases
Miscellaneous
Structure
Family & Domains
Features
Showing features for domain, region, coiled coil, compositional bias.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Domain | 1-90 | CARD | ||||
Sequence: MEPQRRELLAQCQQSLAQAMTEVEAVLGLLEAAGALSPGERRQLDEEAGGAKAELLLQLLLAKEQDHFQDLRAALEKTQPHLLPILYLNG | ||||||
Region | 116-143 | Disordered | ||||
Sequence: ESSSSLSSVGTTGKAPSPPPLLTEQQAN | ||||||
Coiled coil | 139-601 | |||||
Sequence: EQQANDTVENLSIQLRLMTRERNELRKRLAFATHGATFDKRPYHRLNPDYERLKIQCVRAMSDLQSLQNQHTNALKRCEEVAKETDFYHTLHSRLLSDQTQLKDDVDMLRRENGKLRRERNLLQQSWEDMKRLREEDQKEIGDLRAQQQQVLKHNGSSEILNKLYDTAMDKLEVVKKDYDALRKRYSEKVAMHNSDLSRLEQLGEENQRLQKQTEMLTQQRDTAIQLQHQCALSLRRFETIHHELSKATAQNKDLQWEMELLQSELTELRSKQVKTAKESEKYKEERDAVYSEYKLIMSERDQVISELDKLQTEVELAESKLKSSTSEKKAASEEMEALRQIKDTVTMDAGRANKEVEILRKQCKALCQELKEALQEADVAKCRRDWAFQERDKIVAERDSIRTLCDNLRRERDRAVSELAEALRSLDDTRKQKNDVSRELKELKEQMECQLEKEARFRQLMA | ||||||
Domain | 620-710 | PDZ 1 | ||||
Sequence: VVEFERETEDIDLKALGFDMAEGVNEPCFPGDCGIFVTKVDKGSIADGRLRVNDWLLRINDVDLINKDKKQAIKALLNGEGAINMVVRRRK | ||||||
Domain | 705-796 | PDZ 2 | ||||
Sequence: VVRRRKSLGGKVVTPLHINLSGQKDSGISLENGVYAAAVVPGSPAAKEGSLAVGDRIVAINGIALDNKSLNECESLLRSCQDSLTLSLLKVF | ||||||
Region | 857-898 | Disordered | ||||
Sequence: ELGHSGGSSSFLHKPFSGSSSPVSPQACPSTSERSLNSFRSD | ||||||
Compositional bias | 866-898 | Polar residues | ||||
Sequence: SFLHKPFSGSSSPVSPQACPSTSERSLNSFRSD | ||||||
Region | 930-1121 | Disordered | ||||
Sequence: EVPLDKIDPEGSNSGGTWPKAVLGSTSGPEKLSVYKKPKQRKSIFDPNTFKRPQTPPKIDYLLPGPGLTHSPQPSKRVGSLTPPKPPRRSDSIKFQHRLETSSESEATLVGSSPSTSPPSAPPPSMDPSEPTHASPPRKARVRIASSYHSEGDGDTSYLPAKKPCDEDLTSQKVDELGQKRRRPKSAPSFRP | ||||||
Compositional bias | 1045-1060 | Pro residues | ||||
Sequence: TSPPSAPPPSMDPSEP | ||||||
Compositional bias | 1089-1112 | Basic and acidic residues | ||||
Sequence: PAKKPCDEDLTSQKVDELGQKRRR | ||||||
Region | 1204-1227 | Disordered | ||||
Sequence: VLPCGSPPVPRDAGSQSLSPSVQH | ||||||
Region | 1243-1266 | Disordered | ||||
Sequence: YSEMRASQGSNSLPSSARLGSSSN | ||||||
Region | 1280-1343 | Disordered | ||||
Sequence: PRYPRSVMGSDRGSLSHSECSTPPRSPLNIDTLSSCSQPQTTASTLPRIAVNPSSHGERRKDRP | ||||||
Compositional bias | 1290-1330 | Polar residues | ||||
Sequence: DRGSLSHSECSTPPRSPLNIDTLSSCSQPQTTASTLPRIAV | ||||||
Domain | 1350-1429 | PDZ 3 | ||||
Sequence: HVKVQKGSEPLGISIVSGEKGGVYVSKVTLGSIAHQAGLEYGDQLLEFNGINLRSATEQQARLIIGQQCDTITILAQYNP | ||||||
Compositional bias | 1434-1462 | Polar residues | ||||
Sequence: LNSHSRSSSHLDPAATPHSTLQGSSAGTP | ||||||
Region | 1434-1501 | Disordered | ||||
Sequence: LNSHSRSSSHLDPAATPHSTLQGSSAGTPEHPSVIDPLMEQDEGPGTPPAKQSASSTRSVGDTTKKTP | ||||||
Compositional bias | 1481-1496 | Polar residues | ||||
Sequence: PPAKQSASSTRSVGDT | ||||||
Domain | 1504-1585 | PDZ 4 | ||||
Sequence: RIVFIKKSQLDLGVHLCGGNLHGVFVAEVEDDSPAKGPDGLVPGDLILEYGSLDMRSRTVEDVYVEMLKPKDSLRLKVQYRH | ||||||
Domain | 1596-1664 | SH3 | ||||
Sequence: GDSFYIRALYDRLAEVEPELSFKKDDILYVDDTLPQGVFGSWMAWQLDENAQKIQRGQIPSKYVMDQEF | ||||||
Domain | 1724-1907 | Guanylate kinase-like | ||||
Sequence: DSVSLAYQRVQKVDCTSLRPVLLLGPLLDVVKEMLVNEAPGKFCRCPLEVMKASQQAIERGVKDCLFVDYKRRSGHFDVTTVASIKEITEKNRHCLLDIAPHAIERLHHMHIYPIVIFIRYKSAKHIKEQRDPVYLRDKVTQRHSKEQFETAQKIDQEYSRYFTGVVQGGALSSICTQILAMVS |
Domain
The guanylate kinase-like domain interacts with the SH3 domain.
Sequence similarities
Belongs to the MAGUK family.
Keywords
- Domain
Phylogenomic databases
Family and domain databases
Sequence
- Sequence statusComplete
- Length1,921
- Mass (Da)214,386
- Last updated2011-04-05 v1
- Checksum0B2C62F913B3B26E
Computationally mapped potential isoform sequences
There are 5 potential isoforms mapped to this entry
Features
Showing features for compositional bias, sequence conflict.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Compositional bias | 866-898 | Polar residues | ||||
Sequence: SFLHKPFSGSSSPVSPQACPSTSERSLNSFRSD | ||||||
Sequence conflict | 946 | in Ref. 1; BAE28082 | ||||
Sequence: T → P | ||||||
Compositional bias | 1045-1060 | Pro residues | ||||
Sequence: TSPPSAPPPSMDPSEP | ||||||
Compositional bias | 1089-1112 | Basic and acidic residues | ||||
Sequence: PAKKPCDEDLTSQKVDELGQKRRR | ||||||
Compositional bias | 1290-1330 | Polar residues | ||||
Sequence: DRGSLSHSECSTPPRSPLNIDTLSSCSQPQTTASTLPRIAV | ||||||
Compositional bias | 1434-1462 | Polar residues | ||||
Sequence: LNSHSRSSSHLDPAATPHSTLQGSSAGTP | ||||||
Compositional bias | 1481-1496 | Polar residues | ||||
Sequence: PPAKQSASSTRSVGDT |
Keywords
- Technical term
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
AK147699 EMBL· GenBank· DDBJ | BAE28082.1 EMBL· GenBank· DDBJ | mRNA | ||
AC163638 EMBL· GenBank· DDBJ | - | Genomic DNA | No translation available. |