P78352 (DLG4_HUMAN) 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:	PSD95

Organism

Homo sapiens (Human) [Reference proteome]

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Opisthokonta › Metazoa › Eumetazoa › Bilateria › Deuterostomia › Chordata › Craniata › Vertebrata › Gnathostomata › Teleostomi › Euteleostomi › Sarcopterygii › Tetrapoda › Amniota › Mammalia › Theria › Eutheria › Euarchontoglires › Primates › Haplorrhini › Simiiformes › Catarrhini › Hominoidea › Hominidae › Homininae › Homo

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 By similarity.
Subunit structure	Interacts with ANKS1B, KLHL17 and PRR7 By similarity. Interacts through its PDZ domains with NETO1. 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. May interact with HTR2A. Interacts through its guanylate kinase-like domain with DLGAP1/GKAP, DLGAP2, DLGAP3, DLGAP4, MAP1A and BEGAIN. Interacts through its third PDZ domain with CRIPT By similarity. 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. 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. Interacts with LRFN1, LRFN2 and LRFN4. Interacts with ANO2, ADAM22 and LGI1 By similarity. Interacts with FRMPD4 (via C-terminus). Interacts (via PDZ1 and PDZ2 domains) with LRRC4; LRRC4B and SEMA4C. Interacts (via guanylate kinase-like domain) with SIPA1L1 By similarity. Ref.6 Ref.7 Ref.8 Ref.9 Ref.10 Ref.11 Ref.12 Ref.14
Subcellular location	Cell membrane; Peripheral membrane protein. Cell junction › synapse › postsynaptic cell membrane › postsynaptic density. Cell junction › synapse. Cell junction › synapse › synaptosome By similarity. 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.10
Tissue specificity	Brain.
Domain	The PDZ domain 3 mediates interaction with ADR1B. The L27 domain near the N-terminus of isoform 2 is required for HGS/HRS-dependent targeting to postsynaptic density.
Post-translational modification	Palmitoylation of isoform 1 is required for targeting to postsynaptic density By similarity.
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 Reference proteome
Gene Ontology (GO)
Biological_process	alpha-amino-3-hydroxy-5-methyl-4-isoxazole propionate receptor clustering Inferred from sequence or structural similarity. Source: BHF-UCL axon guidance Traceable author statement. Source: Reactome dendritic spine morphogenesis Inferred from sequence or structural similarity. Source: BHF-UCL establishment of protein localization Inferred from direct assay PubMed 15496675. Source: BHF-UCL learning Traceable author statement PubMed 9853749. Source: ProtInc locomotory exploration behavior Inferred from electronic annotation. Source: Compara negative regulation of receptor internalization Inferred from electronic annotation. Source: Compara neuromuscular process controlling balance Inferred from electronic annotation. Source: Compara positive regulation of excitatory postsynaptic membrane potential Inferred from sequence or structural similarity. Source: BHF-UCL positive regulation of synaptic transmission Inferred from sequence or structural similarity. Source: BHF-UCL positive regulation of transcription from RNA polymerase II promoter Inferred from sequence or structural similarity. Source: BHF-UCL protein complex assembly Inferred from direct assay PubMed 15496675. Source: BHF-UCL receptor localization to synapse Inferred from sequence or structural similarity. Source: BHF-UCL regulation of N-methyl-D-aspartate selective glutamate receptor activity Inferred from sequence or structural similarity. Source: BHF-UCL regulation of grooming behavior Inferred from electronic annotation. Source: Compara regulation of long-term neuronal synaptic plasticity Inferred from electronic annotation. Source: Compara social behavior Inferred from electronic annotation. Source: Compara synaptic vesicle maturation Inferred from electronic annotation. Source: Compara vocalization behavior Inferred from electronic annotation. Source: Compara
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 direct assay Ref.10. Source: UniProtKB dendrite cytoplasm Inferred from sequence or structural similarity. Source: BHF-UCL endocytic vesicle membrane Traceable author statement. Source: Reactome excitatory synapse Inferred from sequence or structural similarity. Source: BHF-UCL extrinsic to internal side of plasma membrane Inferred from electronic annotation. Source: Compara juxtaparanode region of axon Inferred from electronic annotation. Source: Compara neuron projection terminus Inferred from electronic annotation. Source: Compara plasma membrane Traceable author statement. Source: Reactome postsynaptic density Inferred from sequence or structural similarity. Source: UniProtKB postsynaptic membrane Inferred from direct assay Ref.10. Source: UniProtKB synaptic vesicle Inferred from electronic annotation. Source: Compara
Molecular_function	ADP-activated nucleotide receptor activity Inferred from sequence or structural similarity. Source: BHF-UCL ATP-activated nucleotide receptor activity Inferred from sequence or structural similarity. Source: BHF-UCL P2Y1 nucleotide receptor binding Inferred from sequence or structural similarity. Source: BHF-UCL ionotropic glutamate receptor binding Inferred from sequence or structural similarity. Source: BHF-UCL scaffold protein binding Inferred from sequence or structural similarity. Source: BHF-UCL
Complete GO annotation...

Binary interactions

With	Entry	#Exp.	IntAct	Notes
Dlgap1	P97836-5	3	EBI-80389,EBI-6269434	From a different organism.
ERBB4	Q15303	6	EBI-80389,EBI-80371
Kcna1	P10499	2	EBI-80389,EBI-631463	From a different organism.
Kcna2	P63142	2	EBI-80389,EBI-631446	From a different organism.
Kcna3	P15384	2	EBI-80389,EBI-631478	From a different organism.
Kcna4	P15385	9	EBI-80389,EBI-631417	From a different organism.
KIF1B	O60333-3	4	EBI-80389,EBI-465669

Alternative products

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

Isoform 1 (identifier: P78352-1)

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: P78352-2)

Also known as: PSD95-beta;

The sequence of this isoform differs from the canonical sequence as follows:
     1-10: MDCLCIVTTK → MSQRPRAPRSALWLLAPPLLRWAPPLLTVLHSDLFQALLDILDYYEASLSESQ

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 724

724

Disks large homolog 4

PRO_0000094560

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 By similarity

Lipidation

5

1

S-palmitoyl cysteine By similarity

Natural variations

Alternative sequence

1 – 10

10

MDCLCIVTTK → MSQRPRAPRSALWLLAPPLL RWAPPLLTVLHSDLFQALLD ILDYYEASLSESQ in isoform 2.

VSP_014929

Experimental info

Isoform 2:

Sequence conflict

46

1

E → V in AAD56173. Ref.3

Secondary structure

1

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724

Helix Strand Turn

Details...

Beta strand

61 – 69

9

Beta strand

72 – 74

3

Beta strand

77 – 81

5

Beta strand

83 – 85

3

Beta strand

87 – 90

4

Beta strand

94 – 99

6

Helix

104 – 108

5

Beta strand

116 – 120

5

Beta strand

126 – 128

3

Helix

130 – 138

9

Beta strand

142 – 151

10

Beta strand

156 – 164

9

Beta strand

169 – 176

8

Beta strand

178 – 180

3

Beta strand

189 – 194

6

Helix

199 – 203

5

Beta strand

211 – 215

5

Helix

225 – 233

9

Beta strand

237 – 245

9

Beta strand

312 – 317

6

Beta strand

324 – 329

6

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 – 401

8

Sequences

	Sequence		Length	Mass (Da)
	Isoform 1 (PSD95-alpha) [UniParc]. Last modified August 2, 2005. Version 3. Checksum: 7922D3F220F9A101	FASTA	724	80,495
	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 HVIDASDEEW 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) [UniParc]. Checksum: BE1019159E65B2D8	FASTA	767	85,430
	10 20 30 40 50 60 MSQRPRAPRS ALWLLAPPLL RWAPPLLTVL HSDLFQALLD ILDYYEASLS ESQKYRYQDE 70 80 90 100 110 120 DTPPLEHSPA HLPNQANSPP VIVNTDTLEA PGYELQVNGT EGEMEYEEIT LERGNSGLGF 130 140 150 160 170 180 SIAGGTDNPH IGDDPSIFIT KIIPGGAAAQ DGRLRVNDSI LFVNEVDVRE VTHSAAVEAL 190 200 210 220 230 240 KEAGSIVRLY VMRRKPPAEK VMEIKLIKGP KGLGFSIAGG VGNQHIPGDN SIYVTKIIEG 250 260 270 280 290 300 GAAHKDGRLQ IGDKILAVNS VGLEDVMHED AVAALKNTYD VVYLKVAKPS NAYLSDSYAP 310 320 330 340 350 360 PDITTSYSQH LDNEISHSSY LGTDYPTAMT PTSPRRYSPV AKDLLGEEDI PREPRRIVIH 370 380 390 400 410 420 RGSTGLGFNI VGGEDGEGIF ISFILAGGPA DLSGELRKGD QILSVNGVDL RNASHEQAAI 430 440 450 460 470 480 ALKNAGQTVT IIAQYKPEEY SRFEAKIHDL REQLMNSSLG SGTASLRSNP KRGFYIRALF 490 500 510 520 530 540 DYDKTKDCGF LSQALSFRFG DVLHVIDASD EEWWQARRVH SDSETDDIGF IPSKRRVERR 550 560 570 580 590 600 EWSRLKAKDW GSSSGSQGRE DSVLSYETVT QMEVHYARPI IILGPTKDRA NDDLLSEFPD 610 620 630 640 650 660 KFGSCVPHTT RPKREYEIDG RDYHFVSSRE KMEKDIQAHK FIEAGQYNSH LYGTSVQSVR 670 680 690 700 710 720 EVAEQGKHCI LDVSANAVRR LQAAHLHPIA IFIRPRSLEN VLEINKRITE EQARKAFDRA 730 740 750 760 TKLEQEFTEC FSAIVEGDSF EEIYHKVKRV IEDLSGPYIW VPARERL

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Human postsynaptic density-95 (PSD95): location of the gene (DLG4) and possible function in nonneural as well as in neural tissues." Stathakis D.G., Hoover K.B., You Z., Bryant P.J. Genomics 44:71-82(1997) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2). Tissue: Mammary gland.
[2]	Stathakis D.G., Hoover K.H., You Z., Bryant P.J. Submitted (JUL-1998) to the EMBL/GenBank/DDBJ databases Cited for: SEQUENCE REVISION.
[3]	"Genomic organization of human DLG4, the gene encoding postsynaptic density 95." Stathakis D.G., Udar N., Sandgren O., Andreasson S., Bryant P.J., Small K., Forsman-Semb K. J. Neurochem. 73:2250-2265(1999) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[4]	"Complete sequencing and characterization of 21,243 full-length human cDNAs." Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S. , Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S. Nat. Genet. 36:40-45(2004) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1). Tissue: Cerebellum.
[5]	Brenman J.E., Bredt D.S., Parkinson J.F., Manzana W.P., McClary J.A. Submitted (AUG-1996) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 84-398. Tissue: Brain.
[6]	"Clustering of Shaker-type K+ channels by interaction with a family of membrane-associated guanylate kinases." Kim E., Niethammer M., Rothschild A., Jan Y.N., Sheng M. Nature 378:85-88(1995) [PubMed] [Europe PMC] [Abstract] Cited for: INTERACTION WITH KCNA1; KCNA2; KCNA3 AND KCNA4.
[7]	"Binding of neuroligins to PSD-95." Irie M., Hata Y., Takeuchi M., Ichtchenko K., Toyoda A., Hirao K., Takai Y., Rosahl T.W., Suedhof T.C. Science 277:1511-1515(1997) [PubMed] [Europe PMC] [Abstract] Cited for: INTERACTION WITH NLGN1; NLGN2 AND NLGN3.
[8]	"GAKIN, a novel kinesin-like protein associates with the human homologue of the Drosophila discs large tumor suppressor in T lymphocytes." Hanada T., Lin L., Tibaldi E.V., Reinherz E.L., Chishti A.H. J. Biol. Chem. 275:28774-28784(2000) [PubMed] [Europe PMC] [Abstract] Cited for: INTERACTION WITH KIF13B.
[9]	"The neuregulin receptor ErbB-4 interacts with PDZ-containing proteins at neuronal synapses." Garcia R.A., Vasudevan K., Buonanno A. Proc. Natl. Acad. Sci. U.S.A. 97:3596-3601(2000) [PubMed] [Europe PMC] [Abstract] Cited for: INTERACTION WITH ERBB4.
[10]	"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, SUBCELLULAR LOCATION, INTERACTION WITH CASK AND HGS.
[11]	"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; LRFN2 AND LRFN4.
[12]	"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.
[13]	"Initial characterization of the human central proteome." Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J. BMC Syst. Biol. 5:17-17(2011) [PubMed] [Europe PMC] [Abstract] Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[14]	"The PDZ1 domain of SAP90. Characterization of structure and binding." Piserchio A., Pellegrini M., Mehta S., Blackman S.M., Garcia E.P., Marshall J., Mierke D.F. J. Biol. Chem. 277:6967-6973(2002) [PubMed] [Europe PMC] [Abstract] Cited for: STRUCTURE BY NMR OF 105-197, INTERACTION WITH GRIK2; KCNA4 AND CRIPT.
+	Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ

U83192 mRNA. Translation: AAC52113.1.
AF156495 Genomic DNA. Translation: AAD56173.1.
AK293835 mRNA. Translation: BAH11607.1.
U68138 mRNA. Translation: AAB07736.1. Sequence problems.

IPI

IPI00019213.
IPI00619928.

PIR

T09599.

RefSeq

NP_001356.1. NM_001365.3.

UniGene

Hs.463928.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
1KEF	NMR	-	A	62-154	[»]
3I4W	X-ray	1.35	A/B/C/D	302-403	[»]
3K82	X-ray	1.40	A	305-402	[»]
3ZRT	X-ray	3.40	A/B/C/D	61-249	[»]

ProteinModelPortal

P78352.

ModBase

Search...

Protein-protein interaction databases

DIP

DIP-30919N.

IntAct

P78352. 10 interactions.

MINT

MINT-199061.

STRING

9606.ENSP00000293813.

PTM databases

PhosphoSite

P78352.

Polymorphism databases

DMDM

71658825.

Proteomic databases

PaxDb

P78352.

PRIDE

P78352.

Protocols and materials databases

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

Ensembl

ENST00000293813; ENSP00000293813; ENSG00000132535.

GeneID

1742.

KEGG

hsa:1742.

UCSC

uc002get.4. human.
uc010vtn.2. human.

Organism-specific databases

CTD

1742.

GeneCards

GC17M007033.

HGNC

HGNC:2903. DLG4.

HPA

CAB001999.
CAB002000.
HPA010122.

MIM

602887. gene.

neXtProt

NX_P78352.

PharmGKB

PA27359.

GenAtlas

Search...

Phylogenomic databases

eggNOG

COG0194.

HOGENOM

HOG000232102.

HOVERGEN

HBG107814.

KO

K11828.

Enzyme and pathway databases

Reactome

REACT_111045. Developmental Biology.
REACT_13685. Neuronal System.

SignaLink

P78352.

Gene expression databases

ArrayExpress

P78352.

Bgee

P78352.

CleanEx

HS_DLG4.

Genevestigator

P78352.

GermOnline

ENSG00000132535. Homo sapiens.

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.
IPR027417. P-loop_NTPase.
IPR001478. PDZ.
IPR019583. PDZ_assoc.
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.
PF00018. SH3_1. 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.
SSF52540. SSF52540. 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

BindingDB

P78352.

ChEMBL

CHEMBL5666.

ChiTaRS

DLG4. human.

EvolutionaryTrace

P78352.

GenomeRNAi

1742.

NextBio

7067.

SOURCE

Search...

Entry information

Entry name

DLG4_HUMAN

Accession

Primary (citable) accession number: P78352
Secondary accession number(s): B7Z1S1, Q92941, Q9UKK8

Entry history

Integrated into UniProtKB/Swiss-Prot:	November 1, 1997
Last sequence update:	August 2, 2005
Last modified:	May 29, 2013
This is version 152 of the entry and version 3 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program

Disclaimer

Any medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.