P31016 (DLG4_RAT) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Disks large homolog 4

Alternative name(s):
Postsynaptic density protein 95
Short name=PSD-95
Synapse-associated protein 90
Short name=SAP-90
Short name=SAP90

Gene names

Name:	Dlg4
Synonyms:	Dlgh4, Psd95

Organism

Rattus norvegicus (Rat) [Reference proteome]

Taxonomic identifier

10116 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Opisthokonta › Metazoa › Eumetazoa › Bilateria › Deuterostomia › Chordata › Craniata › Vertebrata › Gnathostomata › Teleostomi › Euteleostomi › Sarcopterygii › Tetrapoda › Amniota › Mammalia › Theria › Eutheria › Euarchontoglires › Glires › Rodentia › Sciurognathi › Muroidea › Muridae › Murinae › Rattus

Protein attributes

Sequence length	724 AA.
Sequence status	Complete.
Protein existence	Evidence at protein level

General annotation (Comments)

Function	Interacts with the cytoplasmic tail of NMDA receptor subunits and shaker-type potassium channels. Required for synaptic plasticity associated with NMDA receptor signaling. Overexpression or depletion of DLG4 changes the ratio of excitatory to inhibitory synapses in hippocampal neurons. May reduce the amplitude of ASIC3 acid-evoked currents by retaining the channel intracellularly. May regulate the intracellular trafficking of ADR1B. Ref.17 Ref.19
Subunit structure	Interacts through its PDZ domains with NETO1. Interacts through its first two PDZ domains with KCNA1, KCNA2, KCNA3, KCNA4 and ERBB4. Interacts through its first PDZ domain with GRIK2, KCNA4 and CRIPT. Interacts through its third PDZ domain with NLGN1, and probably with NLGN2 and NLGN3. May interact with HTR2A. Interacts through its guanylate kinase-like domain with KIF13B. Isoform 2 interacts through an L27 domain with HGS/HRS and the first L27 domain of CASK By similarity. Interacts through its first two PDZ domains with GRIN2A, GRIN2B, GRIN2C, GRIN2D, ASIC3, certain splice forms of GRIN1, KCND2, CXADR and SYNGAP1. Interacts through its second PDZ domain with the PDZ domain of NOS1 or the C-terminus of CAPON. Interacts through its guanylate kinase-like domain with DLGAP1/GKAP, DLGAP2, DLGAP3, DLGAP4, MAP1A and BEGAIN. Interacts through its third PDZ domain with CRIPT. Interacts with ANKS1B, and PRR7. Interacts with ADAM22 and LGI1. Interacts with ANO2 through its PDZ domains By similarity. Interacts with FRMPD4 (via C-terminus). Interacts (via PDZ 1 and PDZ 2 domains) with LRRC4B and with LRRC4 By similarity. Interacts (via PDZ 1 and PDZ 2 domains) with SEMA4C. Interacts (via guanylate kinase-like domain) with SIPA1L1. Interacts with LRFN1 and LRFN2. Interacts also with LRFN4, but not with LRFN3 nor LRFN5 By similarity. Interacts with KLHL17. Ref.5 Ref.7 Ref.8 Ref.9 Ref.10 Ref.11 Ref.13 Ref.14 Ref.15 Ref.17 Ref.18 Ref.20 Ref.21 Ref.22 Ref.23 Ref.24 Ref.25 Ref.26 Ref.28
Subcellular location	Cell membrane; Peripheral membrane protein. Cell junction › synapse › postsynaptic cell membrane › postsynaptic density. Cell junction › synapse. Cell junction › synapse › synaptosome. Note: High levels in postsynaptic density of neurons in the forebrain. Also in presynaptic region of inhibitory synapses formed by cerebellar basket cells on axon hillocks of Purkinje cells. Ref.6 Ref.7 Ref.14
Tissue specificity	Detected in brain (at protein level). Brain. Highest levels of isoform 2 in cerebellum, cortex, hippocampus, and corpus striatum. Ref.14 Ref.16
Domain	The PDZ domain 3 mediates interaction with ADR1B By similarity. The L27 domain near the N-terminus of isoform 2 is required for HGS/HRS-dependent targeting to postsynaptic density By similarity.
Post-translational modification	Palmitoylation of isoform 1 is required for targeting to postsynaptic density. Ref.12
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 component	Cell junction Cell membrane Membrane Postsynaptic cell membrane Synapse Synaptosome
Coding sequence diversity	Alternative splicing
Domain	Repeat SH3 domain
PTM	Lipoprotein Palmitate Phosphoprotein
Technical term	3D-structure Complete proteome Direct protein sequencing Reference proteome
Gene Ontology (GO)
Biological_process	alpha-amino-3-hydroxy-5-methyl-4-isoxazole propionate receptor clustering Inferred from mutant phenotype PubMed 21525273. Source: BHF-UCL dendritic spine morphogenesis Inferred from mutant phenotype PubMed 21525273. Source: BHF-UCL establishment of protein localization Inferred from sequence or structural similarity. Source: BHF-UCL locomotory exploration behavior Inferred from sequence or structural similarity. Source: BHF-UCL negative regulation of receptor internalization Inferred from direct assay PubMed 11526121. Source: UniProtKB neuromuscular process controlling balance Inferred from sequence or structural similarity. Source: BHF-UCL neuronal ion channel clustering Traceable author statement PubMed 11152698. Source: UniProtKB positive regulation of excitatory postsynaptic membrane potential Inferred from direct assay PubMed 12930820. Source: BHF-UCL positive regulation of synaptic transmission Inferred from direct assay PubMed 12930820. Source: BHF-UCL protein complex assembly Inferred from sequence or structural similarity. Source: BHF-UCL receptor localization to synapse Inferred from mutant phenotype PubMed 21525273. Source: BHF-UCL regulation of N-methyl-D-aspartate selective glutamate receptor activity Inferred from direct assay PubMed 12930820. Source: BHF-UCL regulation of grooming behavior Inferred from sequence or structural similarity. Source: BHF-UCL regulation of long-term neuronal synaptic plasticity Inferred from electronic annotation. Source: Compara response to stress Non-traceable author statement PubMed 14741046. Source: RGD social behavior Inferred from sequence or structural similarity. Source: BHF-UCL synaptic vesicle maturation Inferred from electronic annotation. Source: Compara vocalization behavior Inferred from sequence or structural similarity. Source: BHF-UCL
Cellular_component	alpha-amino-3-hydroxy-5-methyl-4-isoxazolepropionic acid selective glutamate receptor complex Inferred from electronic annotation. Source: Compara cell junction Inferred from electronic annotation. Source: UniProtKB-KW cortical cytoskeleton Inferred from electronic annotation. Source: Compara dendrite cytoplasm Inferred from direct assay Ref.1. Source: BHF-UCL excitatory synapse Inferred from direct assay PubMed 19730411. Source: BHF-UCL extrinsic to internal side of plasma membrane Inferred from electronic annotation. Source: Compara juxtaparanode region of axon Inferred from direct assay PubMed 19109503. Source: MGI neuron projection terminus Inferred from electronic annotation. Source: Compara postsynaptic density Inferred from direct assay Ref.14. Source: UniProtKB postsynaptic membrane Inferred from direct assay PubMed 11483650. Source: MGI synaptic vesicle Inferred from electronic annotation. Source: Compara
Molecular_function	acetylcholine receptor binding Inferred from direct assay PubMed 22593058. Source: RGD scaffold protein binding Inferred from sequence or structural similarity. Source: BHF-UCL
Complete GO annotation...

Binary interactions

With	Entry	#Exp.	IntAct	Notes
Apc	P70478	2	EBI-375655,EBI-631663
Dlgap1	P97836	7	EBI-375655,EBI-80901
Dlgap2	P97837	2	EBI-375655,EBI-81025
Grin2b	Q00960	5	EBI-375655,EBI-396905
Lrfn2	Q460M5	3	EBI-375655,EBI-877185
Map1a	P34926	12	EBI-375655,EBI-631571
Shank1	Q9WV48	3	EBI-375655,EBI-80909
Slc6a9	P28572	2	EBI-375655,EBI-848783
Slc6a9	P28572-2	4	EBI-375655,EBI-848796

Alternative products

This entry describes 2 isoforms produced by alternative splicing. [Select]

Isoform 1 (identifier: P31016-1)

Also known as: PSD95-alpha;

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: P31016-2)

Also known as: PSD95-beta;

The sequence of this isoform is not available.

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 724

724

Disks large homolog 4

PRO_0000094562

Regions

Domain

65 – 151

87

PDZ 1

Domain

160 – 246

87

PDZ 2

Domain

313 – 393

81

PDZ 3

Domain

428 – 498

71

SH3

Domain

534 – 709

176

Guanylate kinase-like

Amino acid modifications

Modified residue

142

1

Phosphoserine By similarity

Modified residue

240

1

Phosphotyrosine By similarity

Modified residue

295

1

Phosphoserine By similarity

Modified residue

397

1

Phosphotyrosine By similarity

Modified residue

415

1

Phosphoserine By similarity

Modified residue

418

1

Phosphoserine By similarity

Modified residue

432

1

Phosphotyrosine By similarity

Modified residue

580

1

Phosphotyrosine By similarity

Modified residue

604

1

Phosphotyrosine By similarity

Modified residue

715

1

Phosphotyrosine By similarity

Lipidation

3

1

S-palmitoyl cysteine Ref.12

Lipidation

5

1

S-palmitoyl cysteine Ref.12

Experimental info

Mutagenesis

3

1

C → S: Loss of palmitoylation and targeting to postsynaptic density. Ref.12

Mutagenesis

5

1

C → S: Loss of palmitoylation and targeting to postsynaptic density. Ref.12

Sequence conflict

61

1

M → L in CAA47103. Ref.2

Sequence conflict

78

1

S → T in CAA47103. Ref.2

Sequence conflict

177 – 182

6

GVGNQH → ALGTSI in CAA47103. Ref.2

Sequence conflict

200

1

A → G in CAA47103. Ref.2

Sequence conflict

254

1

S → T in CAA47103. Ref.2

Sequence conflict

540 – 555

16

LGPTK…LLSEF → SLDPPKTVPTMIFSPSS in CAA47103. Ref.2

Sequence conflict

623 – 625

3

GKH → RDQ Ref.4

Secondary structure

1

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724

Helix Strand Turn

Details...

Beta strand

61 – 69

9

Beta strand

71 – 73

3

Beta strand

74 – 80

7

Beta strand

82 – 85

4

Beta strand

88 – 91

4

Beta strand

94 – 99

6

Beta strand

101 – 103

3

Helix

104 – 108

5

Beta strand

116 – 120

5

Helix

125 – 127

3

Helix

130 – 138

9

Beta strand

142 – 151

10

Beta strand

156 – 166

11

Beta strand

172 – 178

7

Beta strand

189 – 194

6

Helix

199 – 203

5

Beta strand

211 – 215

5

Beta strand

221 – 224

4

Helix

225 – 233

9

Beta strand

237 – 247

11

Helix

302 – 304

3

Beta strand

312 – 317

6

Beta strand

325 – 329

5

Helix

331 – 333

3

Beta strand

336 – 341

6

Helix

346 – 350

5

Beta strand

357 – 362

6

Helix

372 – 380

9

Beta strand

384 – 392

9

Helix

394 – 398

5

Beta strand

431 – 437

7

Helix

441 – 445

5

Beta strand

449 – 451

3

Beta strand

459 – 464

6

Beta strand

467 – 475

9

Beta strand

486 – 489

4

Helix

491 – 499

9

Turn

504 – 507

4

Beta strand

523 – 530

8

Beta strand

537 – 541

5

Helix

544 – 554

11

Turn

556 – 558

3

Turn

576 – 578

3

Helix

586 – 594

9

Beta strand

598 – 604

7

Beta strand

607 – 612

6

Helix

613 – 621

9

Beta strand

625 – 628

4

Helix

634 – 640

7

Beta strand

646 – 650

5

Helix

655 – 661

7

Beta strand

663 – 665

3

Helix

667 – 684

18

Helix

685 – 687

3

Beta strand

689 – 692

4

Helix

697 – 711

15

Beta strand

714 – 719

6

Sequences

	Sequence		Length	Mass (Da)
	Isoform 1 (PSD95-alpha) [UniParc]. Last modified July 1, 1993. Version 1. Checksum: 7922D4E8E0F9AD85	FASTA	724	80,465
	10 20 30 40 50 60 MDCLCIVTTK KYRYQDEDTP PLEHSPAHLP NQANSPPVIV NTDTLEAPGY ELQVNGTEGE 70 80 90 100 110 120 MEYEEITLER GNSGLGFSIA GGTDNPHIGD DPSIFITKII PGGAAAQDGR LRVNDSILFV 130 140 150 160 170 180 NEVDVREVTH SAAVEALKEA GSIVRLYVMR RKPPAEKVME IKLIKGPKGL GFSIAGGVGN 190 200 210 220 230 240 QHIPGDNSIY VTKIIEGGAA HKDGRLQIGD KILAVNSVGL EDVMHEDAVA ALKNTYDVVY 250 260 270 280 290 300 LKVAKPSNAY LSDSYAPPDI TTSYSQHLDN EISHSSYLGT DYPTAMTPTS PRRYSPVAKD 310 320 330 340 350 360 LLGEEDIPRE PRRIVIHRGS TGLGFNIVGG EDGEGIFISF ILAGGPADLS GELRKGDQIL 370 380 390 400 410 420 SVNGVDLRNA SHEQAAIALK NAGQTVTIIA QYKPEEYSRF EAKIHDLREQ LMNSSLGSGT 430 440 450 460 470 480 ASLRSNPKRG FYIRALFDYD KTKDCGFLSQ ALSFRFGDVL HVIDAGDEEW WQARRVHSDS 490 500 510 520 530 540 ETDDIGFIPS KRRVERREWS RLKAKDWGSS SGSQGREDSV LSYETVTQME VHYARPIIIL 550 560 570 580 590 600 GPTKDRANDD LLSEFPDKFG SCVPHTTRPK REYEIDGRDY HFVSSREKME KDIQAHKFIE 610 620 630 640 650 660 AGQYNSHLYG TSVQSVREVA EQGKHCILDV SANAVRRLQA AHLHPIAIFI RPRSLENVLE 670 680 690 700 710 720 INKRITEEQA RKAFDRATKL EQEFTECFSA IVEGDSFEEI YHKVKRVIED LSGPYIWVPA RERL
	Isoform 2 (PSD95-beta) (Sequence not available).		–	–

References

[1]	"The rat brain postsynaptic density fraction contains a homolog of the Drosophila discs-large tumor suppressor protein." Cho K.-O., Hunt C.A., Kennedy M.B. Neuron 9:929-942(1992) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA]. Strain: Sprague-Dawley. Tissue: Brain.
[2]	"SAP90, a rat presynaptic protein related to the product of the Drosophila tumor suppressor gene dlg-A." Kistner U., Wenzel B.M., Veh R.W., Cases-Langhoff C., Garner A.M., Appeltauer U., Voss B., Gundelfinger E.D., Garner C.C. J. Biol. Chem. 268:4580-4583(1993) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA]. Strain: Sprague-Dawley. Tissue: Brain.
[3]	Lubec G., Diao W. Submitted (APR-2007) to UniProtKB Cited for: PROTEIN SEQUENCE OF 113-126; 212-233; 300-312; 381-399 AND 598-617, MASS SPECTROMETRY. Strain: Sprague-Dawley. Tissue: Hippocampus.
[4]	Adams L.D., Werny I., Schwartz S.M. Submitted (NOV-1996) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 566-625. Strain: Wistar Kyoto. Tissue: Vascular smooth muscle.
[5]	"Domain interaction between NMDA receptor subunits and the postsynaptic density protein PSD-95." Kornau H.C., Schenker L.T., Kennedy M.B., Seeburg P.H. Science 269:1737-1740(1995) [PubMed] [Europe PMC] [Abstract] Cited for: INTERACTION WITH GRIN2A; GRIN2B; GRIN2C AND GRIN2D.
[6]	"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: SUBCELLULAR LOCATION.
[7]	"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, SUBCELLULAR LOCATION. Tissue: Brain.
[8]	"BEGAIN (brain-enriched guanylate kinase-associated protein), a novel neuronal PSD-95/SAP90-binding protein." Deguchi M., Hata Y., Takeuchi M., Ide N., Hirao K., Yao I., Irie M., Toyoda A., Takai Y. J. Biol. Chem. 273:26269-26272(1998) [PubMed] [Europe PMC] [Abstract] Cited for: INTERACTION WITH BEGAIN AND DLGAP1.
[9]	"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.
[10]	"SynGAP: a synaptic RasGAP that associates with the PSD-95/SAP90 protein family." Kim J.H., Liao D., Lau L.-F., Huganir R.L. Neuron 20:683-691(1998) [PubMed] [Europe PMC] [Abstract] Cited for: INTERACTION WITH SYNGAP1.
[11]	"CRIPT, a novel postsynaptic protein that binds to the third PDZ domain of PSD-95/SAP90." Niethammer M., Valtschanoff J.G., Kapoor T.M., Allison D.W., Weinberg R.J., Craig A.M., Sheng M. Neuron 20:693-707(1998) [PubMed] [Europe PMC] [Abstract] Cited for: INTERACTION WITH CRIPT.
[12]	"Dual palmitoylation of PSD-95 mediates its vesiculotubular sorting, postsynaptic targeting, and ion channel clustering." El-Husseini A.E., Craven S.E., Chetkovich D.M., Firestein B.L., Schnell E., Aoki C., Bredt D.S. J. Cell Biol. 148:159-172(2000) [PubMed] [Europe PMC] [Abstract] Cited for: MUTAGENESIS OF CYS-3 AND CYS-5, PALMITOYLATION AT CYS-3 AND CYS-5.
[13]	"Sema4c, a transmembrane semaphorin, interacts with a post-synaptic density protein, PSD-95." Inagaki S., Ohoka Y., Sugimoto H., Fujioka S., Amazaki M., Kurinami H., Miyazaki N., Tohyama M., Furuyama T. J. Biol. Chem. 276:9174-9181(2001) [PubMed] [Europe PMC] [Abstract] Cited for: INTERACTION WITH SEMA4C.
[14]	"Regulation of dendritic spine morphology by SPAR, a PSD-95-associated RapGAP." Pak D.T., Yang S., Rudolph-Correia S., Kim E., Sheng M. Neuron 31:289-303(2001) [PubMed] [Europe PMC] [Abstract] Cited for: INTERACTION WITH SIPA1L1, SUBCELLULAR LOCATION, TISSUE SPECIFICITY.
[15]	"Cell surface targeting and clustering interactions between heterologously expressed PSD-95 and the Shal voltage-gated potassium channel, Kv4.2." Wong W., Newell E.W., Jugloff D.G.M., Jones O.T., Schlichter L.C. J. Biol. Chem. 277:20423-20430(2002) [PubMed] [Europe PMC] [Abstract] Cited for: INTERACTION WITH KCND2.
[16]	"Postsynaptic targeting of alternative postsynaptic density-95 isoforms by distinct mechanisms." Chetkovich D.M., Bunn R.C., Kuo S.-H., Kawasaki Y., Kohwi M., Bredt D.S. J. Neurosci. 22:6415-6425(2002) [PubMed] [Europe PMC] [Abstract] Cited for: ALTERNATIVE SPLICING, TISSUE SPECIFICITY.
[17]	"PSD-95 and Lin-7b interact with acid-sensing ion channel-3 and have opposite effects on H+- gated current." Hruska-Hageman A.M., Benson C.J., Leonard A.S., Price M.P., Welsh M.J. J. Biol. Chem. 279:46962-46968(2004) [PubMed] [Europe PMC] [Abstract] Cited for: INTERACTION WITH ASIC3, FUNCTION.
[18]	"A role for the PDZ-binding domain of the coxsackie B virus and adenovirus receptor (CAR) in cell adhesion and growth." Ashbourne-Excoffon K.J.D., Hruska-Hageman A.M., Klotz M., Traver G.L., Zabner J. J. Cell Sci. 117:4401-4409(2004) [PubMed] [Europe PMC] [Abstract] Cited for: INTERACTION WITH CXADR.
[19]	"A balance between excitatory and inhibitory synapses is controlled by PSD-95 and neuroligin." Prange O., Wong T.P., Gerrow K., Wang Y.T., El-Husseini A. Proc. Natl. Acad. Sci. U.S.A. 101:13915-13920(2004) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION.
[20]	"Proteomic analysis revealed a novel synaptic proline-rich membrane protein (PRR7) associated with PSD-95 and NMDA receptor." Murata Y., Doi T., Taniguchi H., Fujiyoshi Y. Biochem. Biophys. Res. Commun. 327:183-191(2005) [PubMed] [Europe PMC] [Abstract] Cited for: INTERACTION WITH PRR7.
[21]	"Interactions between CAP70 and actinfilin are important for integrity of actin cytoskeleton structures in neurons." Chen Y., Li M. Neuropharmacology 49:1026-1041(2005) [PubMed] [Europe PMC] [Abstract] Cited for: INTERACTION WITH KLHL17.
[22]	"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.
[23]	"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.
[24]	"Epilepsy-related ligand/receptor complex LGI1 and ADAM22 regulate synaptic transmission." Fukata Y., Adesnik H., Iwanaga T., Bredt D.S., Nicoll R.A., Fukata M. Science 313:1792-1795(2006) [PubMed] [Europe PMC] [Abstract] Cited for: INTERACTION WITH ADAM22 AND LGI1.
[25]	"Activity-dependent AIDA-1 nuclear signaling regulates nucleolar numbers and protein synthesis in neurons." Jordan B.A., Fernholz B.D., Khatri L., Ziff E.B. Nat. Neurosci. 10:427-435(2007) [PubMed] [Europe PMC] [Abstract] Cited for: INTERACTION WITH ANKS1B.
[26]	"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.
[27]	"Crystal structures of a complexed and peptide-free membrane protein-binding domain: molecular basis of peptide recognition by PDZ." Doyle D.A., Lee A., Lewis J., Kim E., Sheng M., Mackinnon R. Cell 85:1067-1076(1996) [PubMed] [Europe PMC] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (1.82 ANGSTROMS) OF 302-402.
[28]	"Solution structure and backbone dynamics of the second PDZ domain of postsynaptic density-95." Tochio H., Hung F., Li M., Bredt D.S., Zhang M. J. Mol. Biol. 295:225-237(2000) [PubMed] [Europe PMC] [Abstract] Cited for: STRUCTURE BY NMR OF 155-246, INTERACTION WITH NOS1 AND CAPON.
[29]	"Structure of the SH3-guanylate kinase module from PSD-95 suggests a mechanism for regulated assembly of MAGUK scaffolding proteins." McGee A.W., Dakoji S.R., Olsen O., Bredt D.S., Lim W.A., Prehoda K.E. Mol. Cell 8:1291-1301(2001) [PubMed] [Europe PMC] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (1.8 ANGSTROMS) OF 430-724.
[30]	"Structural characterization of the intramolecular interaction between the SH3 and guanylate kinase domains of PSD-95." Tavares G.A., Panepucci E.H., Brunger A.T. Mol. Cell 8:1313-1325(2001) [PubMed] [Europe PMC] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS) OF 430-724.
[31]	"Targeting specific PDZ domains of PSD-95; structural basis for enhanced affinity and enzymatic stability of a cyclic peptide." Piserchio A., Salinas G.D., Li T., Marshall J., Spaller M.R., Mierke D.F. Chem. Biol. 11:469-473(2004) [PubMed] [Europe PMC] [Abstract] Cited for: STRUCTURE BY NMR OF 62-154 IN COMPLEX WITH CYCLIC PEPTIDE.
[32]	"Creating conformational entropy by increasing interdomain mobility in ligand binding regulation: a revisit to N-terminal tandem PDZ domains of PSD-95." Wang W., Weng J., Zhang X., Liu M., Zhang M. J. Am. Chem. Soc. 131:787-796(2009) [PubMed] [Europe PMC] [Abstract] Cited for: STRUCTURE BY NMR OF 61-249 IN COMPLEX WITH PEPTIDE.
+	Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ

M96853 mRNA. Translation: AAA41971.1.
X66474 mRNA. Translation: CAA47103.1.
U77090 mRNA. Translation: AAB38270.1.

IPI

IPI00566635.

PIR

A45436.
JH0800.

RefSeq

NP_062567.1. NM_019621.1.

UniGene

Rn.9765.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
1BE9	X-ray	1.82	A	302-402	[»]
1BFE	X-ray	2.30	A	302-402	[»]
1IU0	NMR	-	A	61-151	[»]
1IU2	NMR	-	A	61-151	[»]
1JXM	X-ray	2.00	A	430-724	[»]
1JXO	X-ray	2.30	A/B	430-724	[»]
1KJW	X-ray	1.80	A	430-724	[»]
1QLC	NMR	-	A	155-249	[»]
1RGR	NMR	-	A	62-154	[»]
1TP3	X-ray	1.99	A	302-402	[»]
1TP5	X-ray	1.54	A	302-402	[»]
1TQ3	X-ray	1.89	A	302-402	[»]
2KA9	NMR	-	A	61-249	[»]
2XKX	Other	22.90	A/B	1-724	[»]
3GSL	X-ray	2.05	A/B	61-249	[»]

ProteinModelPortal

P31016.

SMR

P31016. Positions 62-249, 306-402, 430-724.

ModBase

Search...

Protein-protein interaction databases

DIP

DIP-29264N.

IntAct

P31016. 29 interactions.

MINT

MINT-93329.

PTM databases

PhosphoSite

P31016.

Proteomic databases

PaxDb

P31016.

PRIDE

P31016.

Protocols and materials databases

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

Ensembl

ENSRNOT00000068493; ENSRNOP00000059045; ENSRNOG00000018526.

GeneID

29495.

KEGG

rno:29495.

UCSC

RGD:68424. rat.

Organism-specific databases

CTD

1742.

RGD

68424. Dlg4.

Phylogenomic databases

eggNOG

COG0194.

GeneTree

ENSGT00660000095130.

HOGENOM

HOG000232102.

HOVERGEN

HBG107814.

InParanoid

P31016.

KO

K11828.

OrthoDB

EOG447FSN.

Gene expression databases

ArrayExpress

P31016.

Genevestigator

P31016.

GermOnline

ENSRNOG00000018526. Rattus norvegicus.

Family and domain databases

InterPro

IPR008144. Guanylate_kin.
IPR008145. Guanylate_kin/L-typ_Ca_channel.
IPR020590. Guanylate_kinase_CS.
IPR016313. M-assoc_guanylate_kinase.
IPR019590. MAGUK_PEST_N.
IPR001478. PDZ.
IPR019583. PDZ_assoc.
IPR011511. SH3_2.
IPR001452. SH3_domain.
[Graphical view]

Pfam

PF00625. Guanylate_kin. 1 hit.
PF10608. MAGUK_N_PEST. 2 hits.
PF00595. PDZ. 3 hits.
PF10600. PDZ_assoc. 1 hit.
PF07653. SH3_2. 1 hit.
[Graphical view]

PIRSF

PIRSF001741. MAGUK_DLGH. 1 hit.

SMART

SM00072. GuKc. 1 hit.
SM00228. PDZ. 3 hits.
SM00326. SH3. 1 hit.
[Graphical view]

SUPFAM

SSF50156. PDZ. 3 hits.
SSF50044. SH3. 1 hit.

PROSITE

PS00856. GUANYLATE_KINASE_1. 1 hit.
PS50052. GUANYLATE_KINASE_2. 1 hit.
PS50106. PDZ. 3 hits.
PS50002. SH3. 1 hit.
[Graphical view]

ProtoNet

Search...

Other

DrugBank

DB00536. Guanidine.

EvolutionaryTrace

P31016.

NextBio

609380.

Entry information

Entry name

DLG4_RAT

Accession

Primary (citable) accession number: P31016
Secondary accession number(s): P97631

Entry history

Integrated into UniProtKB/Swiss-Prot:	July 1, 1993
Last sequence update:	July 1, 1993
Last modified:	April 3, 2013
This is version 149 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program