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Protein

Disks large homolog 1

Gene

Dlg1

Organism
Rattus norvegicus (Rat)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Essential multidomain scaffolding protein required for normal development (By similarity). Recruits channels, receptors and signaling molecules to discrete plasma membrane domains in polarized cells. Regulates the excitability of cardiac myocytes by modulating the functional expression of Kv4 channels. Functional regulator of Kv1.5 channel (By similarity). May play a role in adherens junction assembly, signal transduction, cell proliferation, synaptogenesis and lymphocyte activation.By similarity4 Publications

GO - Molecular functioni

  • ionotropic glutamate receptor binding Source: RGD
  • PDZ domain binding Source: RGD
  • phosphatase binding Source: UniProtKB
  • protein C-terminus binding Source: UniProtKB
  • protein kinase binding Source: UniProtKB

GO - Biological processi

  • actin filament organization Source: UniProtKB
  • cell adhesion Source: RGD
  • cortical actin cytoskeleton organization Source: UniProtKB
  • endothelial cell proliferation Source: UniProtKB
  • negative regulation of mitotic cell cycle Source: UniProtKB
  • positive regulation of potassium ion transport Source: RGD
  • regulation of protein localization Source: RGD
  • single organismal cell-cell adhesion Source: UniProtKB
Complete GO annotation...

Enzyme and pathway databases

BRENDAi2.7.4.8. 5301.

Names & Taxonomyi

Protein namesi
Recommended name:
Disks large homolog 1
Alternative name(s):
Synapse-associated protein 97
Short name:
SAP-97
Short name:
SAP97
Gene namesi
Name:Dlg1
Synonyms:Dlgh1
OrganismiRattus norvegicus (Rat)
Taxonomic identifieri10116 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeRattus
Proteomesi
  • UP000002494 Componenti: Unplaced

Organism-specific databases

RGDi2505. Dlg1.

Subcellular locationi

GO - Cellular componenti

  • basal plasma membrane Source: RGD
  • basolateral plasma membrane Source: UniProtKB
  • cell junction Source: UniProtKB-KW
  • cytosol Source: MGI
  • endoplasmic reticulum membrane Source: UniProtKB-SubCell
  • microvillus Source: MGI
  • neuron projection Source: RGD
  • paranode region of axon Source: MGI
  • plasma membrane Source: RGD
  • postsynaptic density Source: UniProtKB
  • postsynaptic membrane Source: RGD
  • presynaptic membrane Source: RGD
  • T-tubule Source: RGD
Complete GO annotation...

Keywords - Cellular componenti

Cell junction, Cell membrane, Endoplasmic reticulum, Membrane, Postsynaptic cell membrane, Synapse

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi39 – 391S → A: No enrichment in postsynaptic density upon CaMK2 activation. 1 Publication
Mutagenesisi39 – 391S → D: Localizes at the postsynaptic density. 1 Publication
Mutagenesisi232 – 2321S → A: No effect on association with GRIN2B. 1 Publication
Mutagenesisi232 – 2321S → D: Partial loss of association with GRIN2B. 1 Publication

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 911911Disks large homolog 1PRO_0000094550Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei39 – 391Phosphoserine; by CaMK21 Publication
Modified residuei122 – 1221PhosphoserineCombined sources
Modified residuei138 – 1381PhosphoserineCombined sources
Modified residuei158 – 1581PhosphoserineBy similarity
Modified residuei232 – 2321Phosphoserine; by CaMK21 Publication
Modified residuei398 – 3981PhosphotyrosineBy similarity
Modified residuei567 – 5671PhosphoserineBy similarity
Modified residuei572 – 5721PhosphoserineBy similarity
Modified residuei574 – 5741PhosphoserineBy similarity
Modified residuei597 – 5971PhosphoserineBy similarity
Modified residuei618 – 6181PhosphoserineCombined sources
Modified residuei684 – 6841PhosphoserineBy similarity
Modified residuei687 – 6871PhosphoserineBy similarity
Modified residuei841 – 8411PhosphoserineCombined sources

Post-translational modificationi

Phosphorylated by MAPK12 (By similarity). Phosphorylation of Ser-39 modulates transport to the plasma membrane and phosphorylation of Ser-232 regulates association with GRIN2A.By similarity2 Publications

Keywords - PTMi

Phosphoprotein

Proteomic databases

PaxDbiQ62696.
PRIDEiQ62696.

PTM databases

iPTMnetiQ62696.
PhosphoSiteiQ62696.
SwissPalmiQ62696.

Expressioni

Tissue specificityi

Widely expressed. Strongly expressed in epithelial cells, in the small intestine it is only detected in the vili. Expressed in brain, heart (at protein level), muscle, lung and liver. In the brain it was detected in olfactory bulbs, cerebral cortex, hippocampus, and spinal cord (at protein level).2 Publications

Inductioni

By BDNF.1 Publication

Interactioni

Subunit structurei

Homotetramer (Probable). Interacts (via guanylate kinase-like domain) with DLGAP1, DLGAP2, DLGAP3, DLGAP4 and MAP1A (PubMed:9115257, PubMed:9786987). Interacts (via guanylate kinase-like domain) with KIF13B (By similarity). May interact with HTR2A (By similarity). Interacts (via PDZ domains) with GRIA1 (PubMed:9677374). Interacts (via PDZ domains) with GRIN2A (PubMed:12933808). Interacts (via PDZ domains) with KCND2 and KCND3 (PubMed:19213956). Interacts (via PDZ domains) with KCNA1, KCNA2, KCNA3 and KCNA4 (By similarity). Interacts (via PDZ domains) with ADGRA3 (By similarity). Interacts with KCNF1 (By similarity). Interacts with CAMK2 (PubMed:19213956). Interacts with cytoskeleton-associated protein EPB41 (By similarity). Interacts with cytoskeleton-associated protein EZR (By similarity). Found in a complex with KCNA5 and CAV3 (By similarity). Found in a complex with APC and CTNNB1 (By similarity). Interacts with CDH1 through binding to PIK3R1 (By similarity). Forms multiprotein complexes with CASK, LIN7A, LIN7B, LIN7C, APBA1, and KCNJ12 (PubMed:11865057, PubMed:14960569). Interacts with TOPK (By similarity). Forms a tripartite complex composed of DLG1, MPP7 and LIN7 (LIN7A or LIN7C) (By similarity). May interact with TJAP1 (By similarity). Interacts with PTEN (PubMed:15951562). Interacts with FRMPD4 (via C-terminus) (PubMed:19118189). Interacts with LRFN1 and LRFN2 (PubMed:16495444, PubMed:16630835). Interacts with LRFN4 and SFPQ (By similarity). Interacts (via PDZ domains) with ADGRA2 (via PDZ-binding motif) (By similarity).By similarityCurated11 Publications

Binary interactionsi

WithEntry#Exp.IntActNotes
BTRCQ9Y2973EBI-389325,EBI-307461From a different organism.
DgkiQ810C53EBI-389325,EBI-8523614
DgkzO085604EBI-389325,EBI-8570505
Dlg4P310162EBI-389325,EBI-375655
DLGAP1O144902EBI-389325,EBI-1753207From a different organism.
E4P890794EBI-389325,EBI-7401124From a different organism.
Gpsm2Q8VDU07EBI-389325,EBI-7575403From a different organism.
Lrfn2Q460M52EBI-389325,EBI-877185
Map1aP349262EBI-389325,EBI-631571
PTENP604842EBI-389325,EBI-696162From a different organism.
Scn7aB1AYL13EBI-389325,EBI-8068354From a different organism.

GO - Molecular functioni

  • ionotropic glutamate receptor binding Source: RGD
  • PDZ domain binding Source: RGD
  • phosphatase binding Source: UniProtKB
  • protein C-terminus binding Source: UniProtKB
  • protein kinase binding Source: UniProtKB

Protein-protein interaction databases

BioGridi247292. 16 interactions.
DIPiDIP-31527N.
IntActiQ62696. 27 interactions.
MINTiMINT-93379.
STRINGi10116.ENSRNOP00000055672.

Structurei

Secondary structure

1
911
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi5 – 2016Combined sources
Beta strandi23 – 264Combined sources
Helixi28 – 4215Combined sources
Helixi44 – 529Combined sources
Beta strandi55 – 617Combined sources
Beta strandi225 – 2273Combined sources
Beta strandi235 – 2395Combined sources
Beta strandi242 – 2465Combined sources
Beta strandi254 – 2585Combined sources
Beta strandi260 – 2623Combined sources
Helixi263 – 2675Combined sources
Beta strandi277 – 2793Combined sources
Helixi289 – 2979Combined sources
Beta strandi301 – 3066Combined sources
Beta strandi316 – 3227Combined sources
Beta strandi327 – 3348Combined sources
Beta strandi347 – 3526Combined sources
Helixi357 – 3615Combined sources
Beta strandi369 – 3735Combined sources
Helixi383 – 3919Combined sources
Beta strandi395 – 4028Combined sources
Beta strandi405 – 4073Combined sources
Beta strandi464 – 4696Combined sources
Beta strandi476 – 4816Combined sources
Beta strandi483 – 4864Combined sources
Beta strandi488 – 4936Combined sources
Helixi498 – 5025Combined sources
Helixi524 – 5329Combined sources
Beta strandi536 – 5427Combined sources
Beta strandi583 – 5875Combined sources
Turni593 – 5953Combined sources
Beta strandi611 – 6166Combined sources
Beta strandi619 – 62810Combined sources
Beta strandi638 – 6414Combined sources
Helixi643 – 6519Combined sources
Beta strandi709 – 7179Combined sources
Beta strandi724 – 7285Combined sources
Helixi731 – 74111Combined sources
Turni743 – 7453Combined sources
Turni763 – 7653Combined sources
Helixi773 – 7819Combined sources
Beta strandi785 – 7917Combined sources
Beta strandi794 – 7996Combined sources
Helixi800 – 8078Combined sources
Turni808 – 8103Combined sources
Beta strandi812 – 8154Combined sources
Helixi820 – 8278Combined sources
Beta strandi833 – 8375Combined sources
Helixi842 – 8487Combined sources
Helixi854 – 87118Combined sources
Helixi872 – 8743Combined sources
Beta strandi876 – 8794Combined sources
Helixi884 – 89815Combined sources
Beta strandi900 – 9067Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1RSONMR-A/C4-63[»]
1ZOKNMR-A221-313[»]
2AWUX-ray2.44A/B314-409[»]
2AWWX-ray2.21A/B314-409[»]
2AWXX-ray1.80A/B314-409[»]
2G2LX-ray2.35A/B314-409[»]
2I0IX-ray2.80A/B/C459-543[»]
2I0LX-ray2.31A/B318-401[»]
3UATX-ray2.70A578-911[»]
ProteinModelPortaliQ62696.
SMRiQ62696. Positions 4-63, 221-313, 318-400, 462-542, 583-911.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiQ62696.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini4 – 6461L27PROSITE-ProRule annotationAdd
BLAST
Domaini224 – 31087PDZ 1PROSITE-ProRule annotationAdd
BLAST
Domaini318 – 40487PDZ 2PROSITE-ProRule annotationAdd
BLAST
Domaini465 – 54581PDZ 3PROSITE-ProRule annotationAdd
BLAST
Domaini580 – 65071SH3PROSITE-ProRule annotationAdd
BLAST
Domaini721 – 896176Guanylate kinase-likePROSITE-ProRule annotationAdd
BLAST

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni162 – 21251Interaction with SH3 domainsBy similarityAdd
BLAST

Domaini

The PDZ domains may also mediate association to membranes by binding to EPB41 and ADGRA2 together with the L27 domain that binds CASK and DLG2.By similarity
The L27 domain may regulate DLG1 self-association. The N-terminal alternatively spliced region is capable of binding several SH3 domains and also moderates the level of protein oligomerization (By similarity).By similarity

Sequence similaritiesi

Belongs to the MAGUK family.Curated
Contains 1 guanylate kinase-like domain.PROSITE-ProRule annotation
Contains 1 L27 domain.PROSITE-ProRule annotation
Contains 3 PDZ (DHR) domains.PROSITE-ProRule annotation
Contains 1 SH3 domain.PROSITE-ProRule annotation

Keywords - Domaini

Repeat, SH3 domain

Phylogenomic databases

eggNOGiKOG0708. Eukaryota.
COG0194. LUCA.
HOGENOMiHOG000232102.
HOVERGENiHBG107814.
InParanoidiQ62696.
KOiK12076.
PhylomeDBiQ62696.

Family and domain databases

Gene3Di2.30.42.10. 3 hits.
3.40.50.300. 2 hits.
InterProiIPR016313. DLG1.
IPR019590. DLG1_PEST_dom.
IPR008145. GK/Ca_channel_bsu.
IPR008144. Guanylate_kin-like_dom.
IPR020590. Guanylate_kinase_CS.
IPR015143. L27_1.
IPR004172. L27_dom.
IPR027417. P-loop_NTPase.
IPR001478. PDZ.
IPR019583. PDZ_assoc.
IPR001452. SH3_domain.
[Graphical view]
PfamiPF00625. Guanylate_kin. 1 hit.
PF09058. L27_1. 1 hit.
PF10608. MAGUK_N_PEST. 1 hit.
PF00595. PDZ. 3 hits.
PF10600. PDZ_assoc. 1 hit.
PF00018. SH3_1. 1 hit.
[Graphical view]
PIRSFiPIRSF001741. MAGUK_DLGH. 1 hit.
SMARTiSM00072. GuKc. 1 hit.
SM00569. L27. 1 hit.
SM01277. MAGUK_N_PEST. 1 hit.
SM00228. PDZ. 3 hits.
SM00326. SH3. 1 hit.
[Graphical view]
SUPFAMiSSF101288. SSF101288. 1 hit.
SSF50044. SSF50044. 2 hits.
SSF50156. SSF50156. 3 hits.
SSF52540. SSF52540. 1 hit.
PROSITEiPS00856. GUANYLATE_KINASE_1. 1 hit.
PS50052. GUANYLATE_KINASE_2. 1 hit.
PS51022. L27. 1 hit.
PS50106. PDZ. 3 hits.
PS50002. SH3. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Q62696-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MPVRKQDTQR ALHLLEEYRS KLSQTEDRQL RSSIERVISI FQSNLFQALI
60 70 80 90 100
DIQEFYEVTL LDNPKCVDHS KQCEPVQPGN PWESGSLSSA AVTSESLPGG
110 120 130 140 150
LSPPVEKYRY QDEEVLPSER ISPQVPNEVL GPELVHVSEK SLSEIENVHG
160 170 180 190 200
FVSHSHISPI KPTEAVPPSS PIVPVTPALP VPAESPVVLP STPQANPPPV
210 220 230 240 250
LVNTDSLETP TYVNGTDADY EYEEITLERG NSGLGFSIAG GTDNPHIGDD
260 270 280 290 300
SSIFITKIIT GGAAAQDGRL RVNDCILRVN EADVRDVTHS KAVEALKEAG
310 320 330 340 350
SIVRLYVKRR KAFRKNHEIK LIKGPKGLGF SIAGGVGNQH IPGDNSIYVT
360 370 380 390 400
KIIEGGAAHK DGKLQIGDKL LAVNSVCLEE VTHEEAVTAL KNTSDFVYLK
410 420 430 440 450
AAKPTSMYIN DGYAPPDITN SSSQSVDNHV SPSSYLGQTP ASPARYSPIS
460 470 480 490 500
KAVLGDDEIT REPRKVVLHR GSTGLGFNIV GGEDGEGIFI SFILAGGPAD
510 520 530 540 550
LSGELRKGDR IISVNSVDLR AASHEQAAAA LKNAGQAVTI VAQYRPEEYS
560 570 580 590 600
RFEAKIHDLR ETMMNSSVSS GSGSLRTSQK RSLYVRALFD YDKTKDSGLP
610 620 630 640 650
SQGLNFKFGD ILHVINASDD EWWQARQVTP DGESDEVGVI PSKRRVEKKE
660 670 680 690 700
RARLKTVKFN SKTRGDKGEI PDDMGSKGLK HVTSNASDSE SSYHEYGCSK
710 720 730 740 750
GGQEEYVLSY EPVNQQEVNY TRPVIILGPM KDRVNDDLIS EFPDKFGSCV
760 770 780 790 800
PHTTRPKRDY EVDGRDYHFV TSREQMEKDI QEHKFIEAGQ YNNHLYGTSV
810 820 830 840 850
QSVRAVAEKG KHCILDVSGN AIKRLQIAQL YPISIFIKPK SMENIMEMNK
860 870 880 890 900
RLTDEQARKT FERAVRLEQE FTEHFTAIVQ GDTLEDIYNQ VKQIIEEQSG
910
PYIWVPAKEK L
Length:911
Mass (Da):100,571
Last modified:November 1, 1997 - v1
Checksum:i18CEBD31DD0CAF8B
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U14950 mRNA. Translation: AAA79976.1.
PIRiI56552.
RefSeqiNP_036920.1. NM_012788.1.
UniGeneiRn.89331.

Genome annotation databases

GeneIDi25252.
KEGGirno:25252.
UCSCiRGD:2505. rat.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U14950 mRNA. Translation: AAA79976.1.
PIRiI56552.
RefSeqiNP_036920.1. NM_012788.1.
UniGeneiRn.89331.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1RSONMR-A/C4-63[»]
1ZOKNMR-A221-313[»]
2AWUX-ray2.44A/B314-409[»]
2AWWX-ray2.21A/B314-409[»]
2AWXX-ray1.80A/B314-409[»]
2G2LX-ray2.35A/B314-409[»]
2I0IX-ray2.80A/B/C459-543[»]
2I0LX-ray2.31A/B318-401[»]
3UATX-ray2.70A578-911[»]
ProteinModelPortaliQ62696.
SMRiQ62696. Positions 4-63, 221-313, 318-400, 462-542, 583-911.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi247292. 16 interactions.
DIPiDIP-31527N.
IntActiQ62696. 27 interactions.
MINTiMINT-93379.
STRINGi10116.ENSRNOP00000055672.

PTM databases

iPTMnetiQ62696.
PhosphoSiteiQ62696.
SwissPalmiQ62696.

Proteomic databases

PaxDbiQ62696.
PRIDEiQ62696.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

GeneIDi25252.
KEGGirno:25252.
UCSCiRGD:2505. rat.

Organism-specific databases

CTDi1739.
RGDi2505. Dlg1.

Phylogenomic databases

eggNOGiKOG0708. Eukaryota.
COG0194. LUCA.
HOGENOMiHOG000232102.
HOVERGENiHBG107814.
InParanoidiQ62696.
KOiK12076.
PhylomeDBiQ62696.

Enzyme and pathway databases

BRENDAi2.7.4.8. 5301.

Miscellaneous databases

EvolutionaryTraceiQ62696.
PROiQ62696.

Family and domain databases

Gene3Di2.30.42.10. 3 hits.
3.40.50.300. 2 hits.
InterProiIPR016313. DLG1.
IPR019590. DLG1_PEST_dom.
IPR008145. GK/Ca_channel_bsu.
IPR008144. Guanylate_kin-like_dom.
IPR020590. Guanylate_kinase_CS.
IPR015143. L27_1.
IPR004172. L27_dom.
IPR027417. P-loop_NTPase.
IPR001478. PDZ.
IPR019583. PDZ_assoc.
IPR001452. SH3_domain.
[Graphical view]
PfamiPF00625. Guanylate_kin. 1 hit.
PF09058. L27_1. 1 hit.
PF10608. MAGUK_N_PEST. 1 hit.
PF00595. PDZ. 3 hits.
PF10600. PDZ_assoc. 1 hit.
PF00018. SH3_1. 1 hit.
[Graphical view]
PIRSFiPIRSF001741. MAGUK_DLGH. 1 hit.
SMARTiSM00072. GuKc. 1 hit.
SM00569. L27. 1 hit.
SM01277. MAGUK_N_PEST. 1 hit.
SM00228. PDZ. 3 hits.
SM00326. SH3. 1 hit.
[Graphical view]
SUPFAMiSSF101288. SSF101288. 1 hit.
SSF50044. SSF50044. 2 hits.
SSF50156. SSF50156. 3 hits.
SSF52540. SSF52540. 1 hit.
PROSITEiPS00856. GUANYLATE_KINASE_1. 1 hit.
PS50052. GUANYLATE_KINASE_2. 1 hit.
PS51022. L27. 1 hit.
PS50106. PDZ. 3 hits.
PS50002. SH3. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "Molecular characterization and spatial distribution of SAP97, a novel presynaptic protein homologous to SAP90 and the Drosophila discs-large tumor suppressor protein."
    Mueller B.M., Kistner U., Veh R.W., Cases-Langhoff C., Becker B., Gundelfinger E.D., Garner C.C.
    J. Neurosci. 15:2354-2366(1995) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA], TISSUE SPECIFICITY, SUBCELLULAR LOCATION.
    Tissue: Brain.
  2. "SAPAPs. A family of PSD-95/SAP90-associated proteins localized at postsynaptic density."
    Takeuchi M., Hata Y., Hirao K., Toyoda A., Irie M., Takai Y.
    J. Biol. Chem. 272:11943-11951(1997) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH DLGAP1; DLGAP2; DLGAP3 AND DLGAP4.
  3. "SAP97 is associated with the alpha-amino-3-hydroxy-5-methylisoxazole-4-propionic acid receptor GluR1 subunit."
    Leonard A.S., Davare M.A., Horne M.C., Garner C.C., Hell J.W.
    J. Biol. Chem. 273:19518-19524(1998) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH GRIA1.
  4. "Localization of postsynaptic density-93 to dendritic microtubules and interaction with microtubule-associated protein 1A."
    Brenman J.E., Topinka J.R., Cooper E.C., McGee A.W., Rosen J., Milroy T., Ralston H.J., Bredt D.S.
    J. Neurosci. 18:8805-8813(1998) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH MAP1A.
  5. "PSD-95 and SAP97 exhibit distinct mechanisms for regulating K(+) channel surface expression and clustering."
    Tiffany A.M., Manganas L.N., Kim E., Hsueh Y.P., Sheng M., Trimmer J.S.
    J. Cell Biol. 148:147-158(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: SUBCELLULAR LOCATION.
  6. "A novel and conserved protein-protein interaction domain of mammalian Lin-2/CASK binds and recruits SAP97 to the lateral surface of epithelia."
    Lee S., Fan S., Makarova O., Straight S., Margolis B.
    Mol. Cell. Biol. 22:1778-1791(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH CASK, SUBCELLULAR LOCATION.
  7. "Brain-derived neurotrophic factor signal enhances and maintains the expression of AMPA receptor-associated PDZ proteins in developing cortical neurons."
    Jourdi H., Iwakura Y., Narisawa-Saito M., Ibaraki K., Xiong H., Watanabe M., Hayashi Y., Takei N., Nawa H.
    Dev. Biol. 263:216-230(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: INDUCTION BY BDNF.
  8. Cited for: MUTAGENESIS OF SER-232, PHOSPHORYLATION AT SER-232, INTERACTION WITH GRIN2A.
  9. "A multiprotein trafficking complex composed of SAP97, CASK, Veli, and Mint1 is associated with inward rectifier Kir2 potassium channels."
    Leonoudakis D., Conti L.R., Radeke C.M., McGuire L.M., Vandenberg C.A.
    J. Biol. Chem. 279:19051-19063(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH CASK; LIN7A; LIN7B; LIN7C; APBA1 AND KCNJ12, FUNCTION.
  10. "Calcium/calmodulin-dependent protein kinase II phosphorylation drives synapse-associated protein 97 into spines."
    Mauceri D., Cattabeni F., Di Luca M., Gardoni F.
    J. Biol. Chem. 279:23813-23821(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: MUTAGENESIS OF SER-39, PHOSPHORYLATION AT SER-39, SUBCELLULAR LOCATION, FUNCTION.
  11. "Quaternary structure, protein dynamics, and synaptic function of SAP97 controlled by L27 domain interactions."
    Nakagawa T., Futai K., Lashuel H.A., Lo I., Okamoto K., Walz T., Hayashi Y., Sheng M.
    Neuron 44:453-467(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION.
  12. "Binding of PTEN to specific PDZ domains contributes to PTEN protein stability and phosphorylation by microtubule-associated serine/threonine kinases."
    Valiente M., Andres-Pons A., Gomar B., Torres J., Gil A., Tapparel C., Antonarakis S.E., Pulido R.
    J. Biol. Chem. 280:28936-28943(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH PTEN.
  13. "A novel family of adhesion-like molecules that interacts with the NMDA receptor."
    Wang C.Y., Chang K., Petralia R.S., Wang Y.X., Seabold G.K., Wenthold R.J.
    J. Neurosci. 26:2174-2183(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH LRFN2.
  14. "SALM synaptic cell adhesion-like molecules regulate the differentiation of excitatory synapses."
    Ko J., Kim S., Chung H.S., Kim K., Han K., Kim H., Jun H., Kaang B.-K., Kim E.
    Neuron 50:233-245(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH LRFN1.
  15. "Preso, a novel PSD-95-interacting FERM and PDZ domain protein that regulates dendritic spine morphogenesis."
    Lee H.W., Choi J., Shin H., Kim K., Yang J., Na M., Choi S.Y., Kang G.B., Eom S.H., Kim H., Kim E.
    J. Neurosci. 28:14546-14556(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH FRMPD4.
  16. "Kv4 potassium channels form a tripartite complex with the anchoring protein SAP97 and CaMKII in cardiac myocytes."
    El-Haou S., Balse E., Neyroud N., Dilanian G., Gavillet B., Abriel H., Coulombe A., Jeromin A., Hatem S.N.
    Circ. Res. 104:758-769(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, TISSUE SPECIFICITY, SUBCELLULAR LOCATION, INTERACTION WITH KCND2; KCND3 AND CAMK2.
  17. "Quantitative maps of protein phosphorylation sites across 14 different rat organs and tissues."
    Lundby A., Secher A., Lage K., Nordsborg N.B., Dmytriyev A., Lundby C., Olsen J.V.
    Nat. Commun. 3:876-876(2012) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-122; SER-138; SER-618 AND SER-841, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].

Entry informationi

Entry nameiDLG1_RAT
AccessioniPrimary (citable) accession number: Q62696
Entry historyi
Integrated into UniProtKB/Swiss-Prot: November 1, 1997
Last sequence update: November 1, 1997
Last modified: June 8, 2016
This is version 157 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

Documents

  1. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  2. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.