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Q63622 (DLG2_RAT) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 128. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Interactions·Alt products·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Disks large homolog 2
Alternative name(s):
Channel-associated protein of synapse-110
Short name=Chapsyn-110
Postsynaptic density protein PSD-93
Gene names
Name:Dlg2
Synonyms:Dlgh2
OrganismRattus norvegicus (Rat) [Reference proteome]
Taxonomic identifier10116 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeRattus

Protein attributes

Sequence length852 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

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.

Subunit structure

Interacts through its PDZ domains with NETO1. Interacts with NOS1/nNOS through second PDZ domain. Interacts with KCNJ2/Kir2.1 (via C-terminus) through one of its PDZ domains By similarity. Interacts with FRMPD4 (via C-terminus). Interacts with LRFN1. Interacts with LRFN2 and LRFN4. Interacts with FASLG By similarity. Ref.5 Ref.8 Ref.9

Subcellular location

Membrane; Lipid-anchor. Cell junctionsynapsepostsynaptic cell membranepostsynaptic density. Cell junctionsynapse. Note: Concentrated in soma and postsynaptic density of a subset of neurons. Ref.5 Ref.7

Tissue specificity

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. Ref.4 Ref.5

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 E15 embryos. Ref.5

Post-translational modification

Palmitoylation of isoform 1 and isoform 2 is not required for targeting to postsynaptic density. Ref.6

Sequence similarities

Belongs to the MAGUK family.

Contains 1 guanylate kinase-like domain.

Contains 3 PDZ (DHR) domains.

Contains 1 SH3 domain.

Ontologies

Keywords
   Cellular componentCell junction
Cell membrane
Membrane
Postsynaptic cell membrane
Synapse
   Coding sequence diversityAlternative splicing
   DomainRepeat
SH3 domain
   PTMLipoprotein
Palmitate
Phosphoprotein
   Technical term3D-structure
Complete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processnegative regulation of phosphatase activity

Inferred from sequence or structural similarity. Source: UniProtKB

neuronal ion channel clustering

Inferred from mutant phenotype Ref.1. Source: RGD

receptor clustering

Inferred from mutant phenotype Ref.1. Source: RGD

   Cellular_componentcell junction

Inferred from electronic annotation. Source: UniProtKB-KW

cytoplasm

Inferred from direct assay Ref.1. Source: RGD

dendrite

Inferred from direct assay Ref.1. Source: RGD

juxtaparanode region of axon

Inferred from direct assay PubMed 19109503. Source: MGI

membrane

Inferred from direct assay Ref.1. Source: RGD

neuronal cell body

Inferred from direct assay Ref.1. Source: RGD

postsynaptic density

Traceable author statement PubMed 1127911. Source: UniProtKB

postsynaptic membrane

Inferred from electronic annotation. Source: UniProtKB-KW

   Molecular_functionPDZ domain binding

Inferred from physical interaction PubMed 15024025. Source: RGD

protein C-terminus binding

Inferred from physical interaction PubMed 11274188. Source: UniProtKB

protein heterodimerization activity

Inferred from physical interaction Ref.1. Source: RGD

protein phosphatase binding

Inferred from physical interaction PubMed 20410104. Source: BHF-UCL

Complete GO annotation...

Binary interactions

With

Entry

#Exp.

IntAct

Notes

ATP2B2Q01814-12EBI-396947,EBI-1174262From a different organism.
ATP2B4P23634-62EBI-396947,EBI-1174437From a different organism.
DgkiQ810C53EBI-396947,EBI-8523614
DgkzO085604EBI-396947,EBI-8570505
KIF1BO60333-33EBI-396947,EBI-465669From a different organism.
Map1aP349264EBI-396947,EBI-631571

Alternative products

This entry describes 7 isoforms produced by alternative splicing. [Align] [Select]
Isoform 1 (identifier: Q63622-1)

Also known as: PSD-93b;

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.
Isoform 2 (identifier: Q63622-2)

Also known as: PSD-93a;

The sequence of this isoform differs from the canonical sequence as follows:
     1-13: MFFACYCALRTNV → MICHCKVACTNNTLSLMFGC
Isoform 3 (identifier: Q63622-3)

Also known as: PSD-93c;

The sequence of this isoform differs from the canonical sequence as follows:
     1-61: Missing.
     62-68: SHISPLK → MQHAFIP
     341-392: Missing.
Isoform 4 (identifier: Q63622-4)

Also known as: PSD-93-delta;

The sequence of this isoform differs from the canonical sequence as follows:
     1-68: MFFACYCALR...VLQSHISPLK → MNAYLTKQHS...CPHGWFSPAQ
Isoform 5 (identifier: Q63622-5)

Also known as: PSD-93d;

The sequence of this isoform differs from the canonical sequence as follows:
     1-246: Missing.
Note: No experimental confirmation available.
Isoform 6 (identifier: Q63622-6)

The sequence of this isoform differs from the canonical sequence as follows:
     450-454: Missing.
     626-641: Missing.
Isoform 7 (identifier: Q63622-7)

The sequence of this isoform differs from the canonical sequence as follows:
     626-641: GDIPGLGDDGYGTKTL → GSFNDKRKKSFIFSRKFPFYKNKEQSEQETSDPE

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 852852Disks large homolog 2
PRO_0000094555

Regions

Domain98 – 18487PDZ 1
Domain193 – 27987PDZ 2
Domain421 – 50181PDZ 3
Domain536 – 60671SH3
Domain662 – 837176Guanylate kinase-like

Amino acid modifications

Modified residue281Phosphoserine By similarity
Modified residue581Phosphotyrosine By similarity
Modified residue651Phosphoserine By similarity
Modified residue4141Phosphoserine By similarity
Modified residue5051Phosphotyrosine By similarity
Modified residue7321Phosphotyrosine By similarity
Modified residue7371Phosphotyrosine By similarity
Lipidation51S-palmitoyl cysteine Ref.6
Lipidation71S-palmitoyl cysteine Ref.6

Natural variations

Alternative sequence1 – 246246Missing in isoform 5.
VSP_015525
Alternative sequence1 – 6868MFFAC…ISPLK → MNAYLTKQHSCSRGSDGMDA GRGVPTLIRDAHCACGWQRN AQGLGYSSQTMPSSGPGGPA SNRTKLVTLWDSVRKSPHKT STKGKGNCGERCACPHGWFS PAQ in isoform 4.
VSP_015526
Alternative sequence1 – 6161Missing in isoform 3.
VSP_015527
Alternative sequence1 – 1313MFFAC…LRTNV → MICHCKVACTNNTLSLMFGC in isoform 2.
VSP_015528
Alternative sequence62 – 687SHISPLK → MQHAFIP in isoform 3.
VSP_015529
Alternative sequence341 – 39252Missing in isoform 3.
VSP_015530
Alternative sequence450 – 4545Missing in isoform 6.
VSP_015531
Alternative sequence626 – 64116Missing in isoform 6.
VSP_015533
Alternative sequence626 – 64116GDIPG…GTKTL → GSFNDKRKKSFIFSRKFPFY KNKEQSEQETSDPE in isoform 7.
VSP_015532

Experimental info

Mutagenesis51C → S: Loss of palmitoylation and targeting to postsynaptic density. Ref.6
Mutagenesis71C → S: Loss of palmitoylation and targeting to postsynaptic density. Ref.6
Sequence conflict181 – 1822VR → IL in AAC52643. Ref.2
Sequence conflict2281I → M in AAC52643. Ref.2
Sequence conflict3261R → K in AAC52643. Ref.2
Sequence conflict3391D → E in AAB48562. Ref.3
Sequence conflict464 – 4652GD → RK in AAC52643. Ref.2
Sequence conflict4741D → H Ref.2
Sequence conflict4761R → P Ref.2
Sequence conflict4781A → D Ref.2
Sequence conflict484 – 4863AAA → LP in AAC52643. Ref.2
Sequence conflict5061A → S in AAC52643. Ref.2
Sequence conflict5691H → N in AAC52643. Ref.2
Sequence conflict5861L → Q in AAC52643. Ref.2
Sequence conflict627 – 6304DIPG → TSR Ref.5
Sequence conflict6391K → A in AAB48562. Ref.3
Sequence conflict7261F → L in AAB53243. Ref.1
Sequence conflict7331N → Y in AAC52643. Ref.2
Sequence conflict7491E → V in AAB53243. Ref.1
Sequence conflict7561L → H in AAC52643. Ref.2
Sequence conflict791 – 7922KR → NG Ref.2
Sequence conflict7941T → M Ref.2

Secondary structure

................. 852
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
Isoform 1 (PSD-93b) [UniParc].

Last modified November 1, 1997. Version 1.
Checksum: F8D414A8B9CF5B09

FASTA85294,934
        10         20         30         40         50         60 
MFFACYCALR TNVKKYRYQD EDGPHDHSLP RLTHEVRGPE LVHVSEKNLS QIENVHGYVL 

        70         80         90        100        110        120 
QSHISPLKAS PAPIIVNTDT LDTIPYVNGT EIEYEFEEIT LERGNSGLGF SIAGGTDNPH 

       130        140        150        160        170        180 
IGDDPGIFIT KIIPGGAAAE DGRLRVNDCI LRVNEVDVSE VSHSKAVEAL KEAGSIVRLY 

       190        200        210        220        230        240 
VRRRRPILET VVEIKLFKGP KGLGFSIAGG VGNQHIPGDN SIYVTKIIDG GAAQKDGRLQ 

       250        260        270        280        290        300 
VGDRLLMVNN YSLEEVTHEE AVAILKNTSD VVYLKVGKPT TIYMTDPYGP PDITHSYSPP 

       310        320        330        340        350        360 
MENHLLSGNN GTLEYKTSLP PISPGRYSPI PKHMLVEDDY TRPPEPVYST VNKLCDKPAS 

       370        380        390        400        410        420 
PRHYSPVECD KSFLLSTPYP HYHLGLLPDS DMTSHSQHST ATRQPSVTLQ RAISLEGEPR 

       430        440        450        460        470        480 
KVVLHKGSTG LGFNIVGGED GEGIFVSFIL AGGPADLSGE LQRGDQILSV NGIDLRGASH 

       490        500        510        520        530        540 
EQAAAALKGA GQTVTIIAQY QPEDYARFEA KIHDLREQMM NHSMSSGSGS LRTNQKRSLY 

       550        560        570        580        590        600 
VRAMFDYDKS KDSGLPSQGL SFKYGDILHV INASDDEWWQ ARRVILDGDS EEMGVIPSKR 

       610        620        630        640        650        660 
RVERKERARL KTVKFNAKPG VIDSKGDIPG LGDDGYGTKT LRGQEDLILS YEPVTRQEIN 

       670        680        690        700        710        720 
YTRPVIILGP MKDRINDDLI SEFPDKFGSC VPHTTRPKRD YEVDGRDYHF VISREQMEKD 

       730        740        750        760        770        780 
IQEHKFIEAG QYNDNLYGTS VQSVRFVAER GKHCILDVSG NAIKRLQVAQ LYPIAIFIKP 

       790        800        810        820        830        840 
KSLEPLMEMN KRLTEEQAKK TYDRAIKLEQ EFGEYFTAIV QGDTLEDIYN QCKLVIEEQS 

       850 
GPFIWIPSKE KL 

« Hide

Isoform 2 (PSD-93a) [UniParc].

Checksum: 4843703C194A1CE8
Show »

FASTA85995,585
Isoform 3 (PSD-93c) [UniParc].

Checksum: 6C33B93499B8E70A
Show »

FASTA73981,962
Isoform 4 (PSD-93-delta) [UniParc].

Checksum: FBB0E9EF8F855A59
Show »

FASTA88797,938
Isoform 5 (PSD-93d) [UniParc].

Checksum: F87FF88D002EA965
Show »

FASTA60668,062
Isoform 6 [UniParc].

Checksum: 0B9B45B7A317B263
Show »

FASTA83192,978
Isoform 7 [UniParc].

Checksum: A6890D04BE125927
Show »

FASTA87097,486

References

[1]"Heteromultimerization and NMDA receptor-clustering activity of Chapsyn-110, a member of the PSD-95 family of proteins."
Kim E., Cho K.-O., Rothschild A., Sheng M.
Neuron 17:103-113(1996) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
[2]"Interaction of nitric oxide synthase with the postsynaptic density protein PSD-95 and alpha1-syntrophin mediated by PDZ domains."
Brenman J.E., Chao D.S., Gee S.H., McGee A.W., Craven S.E., Santillano D.R., Wu Z., Huang F., Xia H., Peters M.F., Froehner S.C., Bredt D.S.
Cell 84:757-767(1996) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 6).
[3]Irie M., Hata Y., Takai Y.
Submitted (SEP-1996) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
[4]"An alternatively spliced isoform of PSD-93/chapsyn 110 binds to the inwardly rectifying potassium channel, Kir2.1."
Leyland M.L., Dart C.
J. Biol. Chem. 279:43427-43436(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: PARTIAL NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 4), TISSUE SPECIFICITY.
[5]"Cloning and characterization of postsynaptic density 93, a nitric oxide synthase interacting protein."
Brenman J.E., Christopherson K.S., Craven S.E., McGee A.W., Bredt D.S.
J. Neurosci. 16:7407-7415(1996) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1; 2; 3 AND 5), SUBCELLULAR LOCATION, TISSUE SPECIFICITY, DEVELOPMENTAL STAGE, INTERACTION WITH NOS1.
[6]"Ion channel clustering by membrane-associated guanylate kinases. Differential regulation by N-terminal lipid and metal binding motifs."
El-Husseini A.E., Topinka J.R., Lehrer-Graiwer J.E., Firestein B.L., Craven S.E., Aoki C., Bredt D.S.
J. Biol. Chem. 275:23904-23910(2000) [PubMed] [Europe PMC] [Abstract]
Cited for: MUTAGENESIS OF CYS-5 AND CYS-7, PALMITOYLATION AT CYS-5 AND CYS-7.
[7]"Postsynaptic targeting of MAGUKs mediated by distinct N-terminal domains."
Firestein B.L., Craven S.E., Bredt D.S.
NeuroReport 11:3479-3484(2000) [PubMed] [Europe PMC] [Abstract]
Cited for: SUBCELLULAR LOCATION.
[8]"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.
[9]"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.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
U49049 mRNA. Translation: AAB53243.1.
U50717 mRNA. Translation: AAC52643.1.
U53368 mRNA. Translation: AAB48562.1.
PIRT10811.
RefSeqNP_071618.1. NM_022282.1.
UniGeneRn.202966.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
4H11X-ray1.67A/B95-188[»]
ProteinModelPortalQ63622.
SMRQ63622. Positions 95-185, 190-283, 418-514, 539-852.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid248965. 7 interactions.
IntActQ63622. 15 interactions.
MINTMINT-155119.

PTM databases

PhosphoSiteQ63622.

Proteomic databases

PaxDbQ63622.
PRIDEQ63622.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

GeneID64053.
KEGGrno:64053.
UCSCRGD:619895. rat. [Q63622-1]

Organism-specific databases

CTD1740.
RGD619895. Dlg2.

Phylogenomic databases

eggNOGCOG0194.
HOGENOMHOG000232102.
HOVERGENHBG107814.
KOK12075.

Gene expression databases

GenevestigatorQ63622.

Family and domain databases

Gene3D2.30.42.10. 3 hits.
3.40.50.300. 2 hits.
InterProIPR016313. DLG1.
IPR008145. GK/Ca_channel_bsu.
IPR008144. Guanylate_kin-like.
IPR020590. Guanylate_kinase_CS.
IPR019590. MAGUK_PEST_N.
IPR027417. P-loop_NTPase.
IPR001478. PDZ.
IPR019583. PDZ_assoc.
IPR011511. SH3_2.
IPR001452. SH3_domain.
[Graphical view]
PANTHERPTHR23119. PTHR23119. 1 hit.
PfamPF00625. Guanylate_kin. 1 hit.
PF10608. MAGUK_N_PEST. 1 hit.
PF00595. PDZ. 3 hits.
PF10600. PDZ_assoc. 1 hit.
PF07653. SH3_2. 1 hit.
[Graphical view]
PIRSFPIRSF001741. MAGUK_DLGH. 1 hit.
SMARTSM00072. GuKc. 1 hit.
SM00228. PDZ. 3 hits.
SM00326. SH3. 1 hit.
[Graphical view]
SUPFAMSSF50044. SSF50044. 2 hits.
SSF50156. SSF50156. 3 hits.
SSF52540. SSF52540. 1 hit.
PROSITEPS00856. GUANYLATE_KINASE_1. 1 hit.
PS50052. GUANYLATE_KINASE_2. 1 hit.
PS50106. PDZ. 3 hits.
PS50002. SH3. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

NextBio612717.
PROQ63622.

Entry information

Entry nameDLG2_RAT
AccessionPrimary (citable) accession number: Q63622
Secondary accession number(s): P70548, Q62939
Entry history
Integrated into UniProtKB/Swiss-Prot: November 1, 1997
Last sequence update: November 1, 1997
Last modified: April 16, 2014
This is version 128 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

PDB cross-references

Index of Protein Data Bank (PDB) cross-references