Q92796 (DLG3_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Disks large homolog 3

Alternative name(s):
Neuroendocrine-DLG
Synapse-associated protein 102
Short name=SAP-102
Short name=SAP102
XLMR

Gene names

Name:	DLG3
Synonyms:	KIAA1232

Organism

Homo sapiens (Human)

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Primates › Haplorrhini › Catarrhini › Hominidae › Homo

Protein attributes

Sequence length	817 AA.
Sequence status	Complete.
Protein existence	Evidence at protein level

General annotation (Comments)

Function	Required for learning most likely through its role in synaptic plasticity following NMDA receptor signaling.
Subunit structure	Interacts through its PDZ domains with NETO1, GRIN2B and SYNGAP1. Interacts through its guanylate kinase-like domain with DLGAP1, DLGAP2, DLGAP3 and DLGAP4 By similarity. Interacts through its PDZ domains with APC. Interacts through its first two PDZ domains with ERBB4. Interacts through its third PDZ domain with NLGN1, and probably with NLGN2 and NLGN3. Interacts with FRMPD4 (via C-terminus). Interacts with LRFN1, LRFN2 and LRFN4. Ref.1 Ref.6 Ref.7 Ref.9 Ref.12
Involvement in disease	Defects in DLG3 are the cause of mental retardation X-linked type 90 (MRX90) [MIM:300850]. Mental retardation is characterized by significantly sub-average general intellectual functioning associated with impairments in adaptative behavior and manifested during the developmental period. Non-syndromic mental retardation patients do not manifest other clinical signs. Ref.8
Sequence similarities	Belongs to the MAGUK family. Contains 1 guanylate kinase-like domain. Contains 3 PDZ (DHR) domains. Contains 1 SH3 domain.
Sequence caution	The sequence BAA86546.1 differs from that shown. Reason: Erroneous initiation.

Ontologies

Keywords
Coding sequence diversity	Alternative splicing Polymorphism
Disease	Mental retardation
Domain	Repeat SH3 domain
PTM	Acetylation Phosphoprotein
Technical term	3D-structure Complete proteome Reference proteome
Gene Ontology (GO)
Biological process	axon guidance Traceable author statement. Source: Reactome negative regulation of cell proliferation Non-traceable author statement Ref.1. Source: UniProtKB negative regulation of phosphatase activity Inferred from direct assay. Source: UniProtKB synaptic transmission Traceable author statement. Source: Reactome
Cellular component	plasma membrane Traceable author statement. Source: Reactome
Molecular function	guanylate kinase activity Non-traceable author statement. Source: UniProtKB
Complete GO annotation...

Alternative products

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

Note: Named isoforms=2.

Isoform 1 (identifier: Q92796-1)

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: Q92796-2)

The sequence of this isoform differs from the canonical sequence as follows:
     1-336: Missing.
     337-381: HISHNSSLGY...RHMLAEEDFT → MERARKFSGS...LRSLRPGGDA
     592-606: DFPGLSDDYYGAKNL → SIKTKRKKSFRLSRKFPFYKSKENMAQESSIQEQGVTSNTSDSESSS

Note: No experimental confirmation available.

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 817

817

Disks large homolog 3

PRO_0000094557

Regions

Domain

130 – 217

88

PDZ 1

Domain

226 – 311

86

PDZ 2

Domain

379 – 465

87

PDZ 3

Domain

503 – 568

66

SH3

Domain

627 – 802

176

Guanylate kinase-like

Amino acid modifications

Modified residue

673

1

Phosphotyrosine Ref.10 Ref.11 Ref.13 Ref.14

Modified residue

765

1

N6-acetyllysine Ref.15

Modified residue

808

1

Phosphotyrosine Ref.10

Natural variations

Alternative sequence

1 – 336

336

Missing in isoform 2.

VSP_035940

Alternative sequence

337 – 381

45

HISHN…EEDFT → MERARKFSGSGLAMGLGSAS ASAWRRASQRWAWPLRSLRP GGDA in isoform 2.

VSP_035941

Alternative sequence

592 – 606

15

DFPGL…GAKNL → SIKTKRKKSFRLSRKFPFYK SKENMAQESSIQEQGVTSNT SDSESSS in isoform 2.

VSP_035942

Natural variant

40

1

G → R in a colorectal cancer sample; somatic mutation. Ref.18

VAR_036591

Experimental info

Sequence conflict

87

1

P → L in AAB61453. Ref.1

Sequence conflict

190

1

D → E in AAB61453. Ref.1

Secondary structure

1

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

817

Helix Strand Turn

Details...

Beta strand

127 – 135

9

Beta strand

142 – 147

6

Beta strand

160 – 165

6

Helix

170 – 174

5

Beta strand

182 – 186

5

Helix

196 – 205

10

Beta strand

208 – 217

10

Beta strand

224 – 230

7

Beta strand

238 – 242

5

Beta strand

255 – 260

6

Helix

265 – 269

5

Beta strand

277 – 281

5

Helix

291 – 299

9

Beta strand

303 – 310

8

Beta strand

383 – 390

8

Beta strand

396 – 398

3

Beta strand

416 – 418

3

Helix

419 – 422

4

Beta strand

431 – 437

7

Helix

445 – 453

9

Beta strand

457 – 464

8

Sequences

	Sequence		Length	Mass (Da)
	Isoform 1 [UniParc]. Last modified December 16, 2008. Version 2. Checksum: CE125E9BEE3EEC66	FASTA	817	90,314
	10 20 30 40 50 60 MHKHQHCCKC PECYEVTRLA ALRRLEPPGY GDWQVPDPYG PGGGNGASAG YGGYSSQTLP 70 80 90 100 110 120 SQAGATPTPR TKAKLIPTGR DVGPVPPKPV PGKSTPKLNG SGPSWWPECT CTNRDWYEQV 130 140 150 160 170 180 NGSDGMFKYE EIVLERGNSG LGFSIAGGID NPHVPDDPGI FITKIIPGGA AAMDGRLGVN 190 200 210 220 230 240 DCVLRVNEVD VSEVVHSRAV EALKEAGPVV RLVVRRRQPP PETIMEVNLL KGPKGLGFSI 250 260 270 280 290 300 AGGIGNQHIP GDNSIYITKI IEGGAAQKDG RLQIGDRLLA VNNTNLQDVR HEEAVASLKN 310 320 330 340 350 360 TSDMVYLKVA KPGSLHLNDM YAPPDYASTF TALADNHISH NSSLGYLGAV ESKVSYPAPP 370 380 390 400 410 420 QVPPTRYSPI PRHMLAEEDF TREPRKIILH KGSTGLGFNI VGGEDGEGIF VSFILAGGPA 430 440 450 460 470 480 DLSGELRRGD RILSVNGVNL RNATHEQAAA ALKRAGQSVT IVAQYRPEEY SRFESKIHDL 490 500 510 520 530 540 REQMMNSSMS SGSGSLRTSE KRSLYVRALF DYDRTRDSCL PSQGLSFSYG DILHVINASD 550 560 570 580 590 600 DEWWQARLVT PHGESEQIGV IPSKKRVEKK ERARLKTVKF HARTGMIESN RDFPGLSDDY 610 620 630 640 650 660 YGAKNLKGQE DAILSYEPVT RQEIHYARPV IILGPMKDRV NDDLISEFPH KFGSCVPHTT 670 680 690 700 710 720 RPRRDNEVDG QDYHFVVSRE QMEKDIQDNK FIEAGQFNDN LYGTSIQSVR AVAERGKHCI 730 740 750 760 770 780 LDVSGNAIKR LQQAQLYPIA IFIKPKSIEA LMEMNRRQTY EQANKIYDKA MKLEQEFGEY 790 800 810 FTAIVQGDSL EEIYNKIKQI IEDQSGHYIW VPSPEKL
	Isoform 2 [UniParc]. Checksum: 9330A330FF9F8FE5	FASTA	512	57,937
	10 20 30 40 50 60 MERARKFSGS GLAMGLGSAS ASAWRRASQR WAWPLRSLRP GGDAREPRKI ILHKGSTGLG 70 80 90 100 110 120 FNIVGGEDGE GIFVSFILAG GPADLSGELR RGDRILSVNG VNLRNATHEQ AAAALKRAGQ 130 140 150 160 170 180 SVTIVAQYRP EEYSRFESKI HDLREQMMNS SMSSGSGSLR TSEKRSLYVR ALFDYDRTRD 190 200 210 220 230 240 SCLPSQGLSF SYGDILHVIN ASDDEWWQAR LVTPHGESEQ IGVIPSKKRV EKKERARLKT 250 260 270 280 290 300 VKFHARTGMI ESNRSIKTKR KKSFRLSRKF PFYKSKENMA QESSIQEQGV TSNTSDSESS 310 320 330 340 350 360 SKGQEDAILS YEPVTRQEIH YARPVIILGP MKDRVNDDLI SEFPHKFGSC VPHTTRPRRD 370 380 390 400 410 420 NEVDGQDYHF VVSREQMEKD IQDNKFIEAG QFNDNLYGTS IQSVRAVAER GKHCILDVSG 430 440 450 460 470 480 NAIKRLQQAQ LYPIAIFIKP KSIEALMEMN RRQTYEQANK IYDKAMKLEQ EFGEYFTAIV 490 500 510 QGDSLEEIYN KIKQIIEDQS GHYIWVPSPE KL

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Cloning and characterization of NE-dlg: a novel human homolog of the Drosophila discs large (dlg) tumor suppressor protein interacts with the APC protein." Makino K., Kuwahara H., Masuko N., Nishiyama Y., Morisaki T., Sasaki J., Nakao M., Kuwano A., Nakata M., Ushio Y., Saya H. Oncogene 14:2425-2433(1997) [PubMed: 9188857] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), INTERACTION WITH APC. Tissue: Fetal brain.
[2]	"Prediction of the coding sequences of unidentified human genes. XV. The complete sequences of 100 new cDNA clones from brain which code for large proteins in vitro." Nagase T., Ishikawa K., Kikuno R., Hirosawa M., Nomura N., Ohara O. DNA Res. 6:337-345(1999) [PubMed: 10574462] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2). Tissue: Brain.
[3]	"The DNA sequence of the human X chromosome." Ross M.T., Grafham D.V., Coffey A.J., Scherer S., McLay K., Muzny D., Platzer M., Howell G.R., Burrows C., Bird C.P., Frankish A., Lovell F.L., Howe K.L., Ashurst J.L., Fulton R.S., Sudbrak R., Wen G., Jones M.C. , Hurles M.E., Andrews T.D., Scott C.E., Searle S., Ramser J., Whittaker A., Deadman R., Carter N.P., Hunt S.E., Chen R., Cree A., Gunaratne P., Havlak P., Hodgson A., Metzker M.L., Richards S., Scott G., Steffen D., Sodergren E., Wheeler D.A., Worley K.C., Ainscough R., Ambrose K.D., Ansari-Lari M.A., Aradhya S., Ashwell R.I., Babbage A.K., Bagguley C.L., Ballabio A., Banerjee R., Barker G.E., Barlow K.F., Barrett I.P., Bates K.N., Beare D.M., Beasley H., Beasley O., Beck A., Bethel G., Blechschmidt K., Brady N., Bray-Allen S., Bridgeman A.M., Brown A.J., Brown M.J., Bonnin D., Bruford E.A., Buhay C., Burch P., Burford D., Burgess J., Burrill W., Burton J., Bye J.M., Carder C., Carrel L., Chako J., Chapman J.C., Chavez D., Chen E., Chen G., Chen Y., Chen Z., Chinault C., Ciccodicola A., Clark S.Y., Clarke G., Clee C.M., Clegg S., Clerc-Blankenburg K., Clifford K., Cobley V., Cole C.G., Conquer J.S., Corby N., Connor R.E., David R., Davies J., Davis C., Davis J., Delgado O., Deshazo D., Dhami P., Ding Y., Dinh H., Dodsworth S., Draper H., Dugan-Rocha S., Dunham A., Dunn M., Durbin K.J., Dutta I., Eades T., Ellwood M., Emery-Cohen A., Errington H., Evans K.L., Faulkner L., Francis F., Frankland J., Fraser A.E., Galgoczy P., Gilbert J., Gill R., Gloeckner G., Gregory S.G., Gribble S., Griffiths C., Grocock R., Gu Y., Gwilliam R., Hamilton C., Hart E.A., Hawes A., Heath P.D., Heitmann K., Hennig S., Hernandez J., Hinzmann B., Ho S., Hoffs M., Howden P.J., Huckle E.J., Hume J., Hunt P.J., Hunt A.R., Isherwood J., Jacob L., Johnson D., Jones S., de Jong P.J., Joseph S.S., Keenan S., Kelly S., Kershaw J.K., Khan Z., Kioschis P., Klages S., Knights A.J., Kosiura A., Kovar-Smith C., Laird G.K., Langford C., Lawlor S., Leversha M., Lewis L., Liu W., Lloyd C., Lloyd D.M., Loulseged H., Loveland J.E., Lovell J.D., Lozado R., Lu J., Lyne R., Ma J., Maheshwari M., Matthews L.H., McDowall J., McLaren S., McMurray A., Meidl P., Meitinger T., Milne S., Miner G., Mistry S.L., Morgan M., Morris S., Mueller I., Mullikin J.C., Nguyen N., Nordsiek G., Nyakatura G., O'dell C.N., Okwuonu G., Palmer S., Pandian R., Parker D., Parrish J., Pasternak S., Patel D., Pearce A.V., Pearson D.M., Pelan S.E., Perez L., Porter K.M., Ramsey Y., Reichwald K., Rhodes S., Ridler K.A., Schlessinger D., Schueler M.G., Sehra H.K., Shaw-Smith C., Shen H., Sheridan E.M., Shownkeen R., Skuce C.D., Smith M.L., Sotheran E.C., Steingruber H.E., Steward C.A., Storey R., Swann R.M., Swarbreck D., Tabor P.E., Taudien S., Taylor T., Teague B., Thomas K., Thorpe A., Timms K., Tracey A., Trevanion S., Tromans A.C., d'Urso M., Verduzco D., Villasana D., Waldron L., Wall M., Wang Q., Warren J., Warry G.L., Wei X., West A., Whitehead S.L., Whiteley M.N., Wilkinson J.E., Willey D.L., Williams G., Williams L., Williamson A., Williamson H., Wilming L., Woodmansey R.L., Wray P.W., Yen J., Zhang J., Zhou J., Zoghbi H., Zorilla S., Buck D., Reinhardt R., Poustka A., Rosenthal A., Lehrach H., Meindl A., Minx P.J., Hillier L.W., Willard H.F., Wilson R.K., Waterston R.H., Rice C.M., Vaudin M., Coulson A., Nelson D.L., Weinstock G., Sulston J.E., Durbin R.M., Hubbard T., Gibbs R.A., Beck S., Rogers J., Bentley D.R. Nature 434:325-337(2005) [PubMed: 15772651] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[4]	Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S., Turner R. , Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W., Venter J.C. Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[5]	"The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)." The MGC Project Team Genome Res. 14:2121-2127(2004) [PubMed: 15489334] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1). Tissue: Brain.
[6]	"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: 9278515] [Abstract] Cited for: INTERACTION WITH NLGN1; NLGN2 AND NLGN3.
[7]	"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: 10725395] [Abstract] Cited for: INTERACTION WITH ERBB4.
[8]	"Mutations in the DLG3 gene cause nonsyndromic X-linked mental retardation." Tarpey P., Parnau J., Blow M., Woffendin H., Bignell G., Cox C., Cox J., Davies H., Edkins S., Holden S., Korny A., Mallya U., Moon J., O'Meara S., Parker A., Stephens P., Stevens C., Teague J. , Donnelly A., Mangelsdorf M., Mulley J., Partington M., Turner G., Stevenson R., Schwartz C., Young I., Easton D., Bobrow M., Futreal P.A., Stratton M.R., Gecz J., Wooster R., Raymond F.L. Am. J. Hum. Genet. 75:318-324(2004) [PubMed: 15185169] [Abstract] Cited for: INVOLVEMENT IN MRX90.
[9]	"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: 16630835] [Abstract] Cited for: INTERACTION WITH LRFN1; LRFN2 AND LRFN4.
[10]	"Global survey of phosphotyrosine signaling identifies oncogenic kinases in lung cancer." Rikova K., Guo A., Zeng Q., Possemato A., Yu J., Haack H., Nardone J., Lee K., Reeves C., Li Y., Hu Y., Tan Z., Stokes M., Sullivan L., Mitchell J., Wetzel R., Macneill J., Ren J.M. , Yuan J., Bakalarski C.E., Villen J., Kornhauser J.M., Smith B., Li D., Zhou X., Gygi S.P., Gu T.-L., Polakiewicz R.D., Rush J., Comb M.J. Cell 131:1190-1203(2007) [PubMed: 18083107] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-673 AND TYR-808, MASS SPECTROMETRY. Tissue: Lung carcinoma.
[11]	"Multiple reaction monitoring for robust quantitative proteomic analysis of cellular signaling networks." Wolf-Yadlin A., Hautaniemi S., Lauffenburger D.A., White F.M. Proc. Natl. Acad. Sci. U.S.A. 104:5860-5865(2007) [PubMed: 17389395] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-673, MASS SPECTROMETRY. Tissue: Mammary epithelium.
[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: 19118189] [Abstract] Cited for: INTERACTION WITH FRMPD4.
[13]	"An extensive survey of tyrosine phosphorylation revealing new sites in human mammary epithelial cells." Heibeck T.H., Ding S.-J., Opresko L.K., Zhao R., Schepmoes A.A., Yang F., Tolmachev A.V., Monroe M.E., Camp D.G. II, Smith R.D., Wiley H.S., Qian W.-J. J. Proteome Res. 8:3852-3861(2009) [PubMed: 19534553] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-673, MASS SPECTROMETRY. Tissue: Mammary epithelium.
[14]	"Quantitative phosphoproteomic analysis of T cell receptor signaling reveals system-wide modulation of protein-protein interactions." Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K., Rodionov V., Han D.K. Sci. Signal. 2:RA46-RA46(2009) [PubMed: 19690332] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-673, MASS SPECTROMETRY. Tissue: Leukemic T-cell.
[15]	"Lysine acetylation targets protein complexes and co-regulates major cellular functions." Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T., Olsen J.V., Mann M. Science 325:834-840(2009) [PubMed: 19608861] [Abstract] Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-765, MASS SPECTROMETRY.
[16]	"Solution structure of the third PDZ domain of synapse-associated protein 102." RIKEN structural genomics initiative (RSGI) Submitted (MAR-2004) to the PDB data bank Cited for: STRUCTURE BY NMR OF 382-475.
[17]	"The crystal structure of the second PDZ domain of human DLG3." Structural genomics consortium (SGC) Submitted (DEC-2005) to the PDB data bank Cited for: X-RAY CRYSTALLOGRAPHY (1.1 ANGSTROMS) OF 223-314.
[18]	"The consensus coding sequences of human breast and colorectal cancers." Sjoeblom T., Jones S., Wood L.D., Parsons D.W., Lin J., Barber T.D., Mandelker D., Leary R.J., Ptak J., Silliman N., Szabo S., Buckhaults P., Farrell C., Meeh P., Markowitz S.D., Willis J., Dawson D., Willson J.K.V. , Gazdar A.F., Hartigan J., Wu L., Liu C., Parmigiani G., Park B.H., Bachman K.E., Papadopoulos N., Vogelstein B., Kinzler K.W., Velculescu V.E. Science 314:268-274(2006) [PubMed: 16959974] [Abstract] Cited for: VARIANT [LARGE SCALE ANALYSIS] ARG-40.
+	Additional computationally mapped references.

Web resources

GeneReviews

Cross-references

Sequence databases

EMBL
GenBank
DDBJ

U49089 mRNA. Translation: AAB61453.1.
AB033058 mRNA. Translation: BAA86546.1. Different initiation.
AL139398 Genomic DNA. Translation: CAI41022.1.
CH471132 Genomic DNA. Translation: EAX05337.1.
CH471132 Genomic DNA. Translation: EAX05338.1.
BC093864 mRNA. Translation: AAH93864.1.
BC093866 mRNA. Translation: AAH93866.1.

IPI

IPI00023343.
IPI00647338.

RefSeq

NP_001159750.1. NM_001166278.1.
NP_065781.1. NM_020730.2.
NP_066943.2. NM_021120.3.

UniGene

Hs.726128.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
1UM7	NMR	-	A	382-475	[»]
2FE5	X-ray	1.10	A	223-314	[»]
2I1N	X-ray	1.85	A/B	126-222	[»]

ProteinModelPortal

Q92796.

SMR

Q92796. Positions 126-817.

ModBase

Search...

Protein-protein interaction databases

IntAct

Q92796. 2 interactions.

MINT

MINT-109320.

STRING

Q92796.

PTM databases

PhosphoSite

Q92796.

Polymorphism databases

DMDM

218512007.

Proteomic databases

PRIDE

Q92796.

Protocols and materials databases

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

Ensembl

ENST00000374360; ENSP00000363480; ENSG00000082458.

GeneID

1741.

KEGG

hsa:1741.

Organism-specific databases

CTD

1741.

GeneCards

GC0XP069664.

H-InvDB

HIX0016853.

HGNC

HGNC:2902. DLG3.

HPA

HPA001733.

MIM

300189. gene.
300850. phenotype.

neXtProt

NX_Q92796.

Orphanet

777. X-linked nonsyndromic intellectual deficit.

HUGE

Search...

GenAtlas

Search...

Phylogenomic databases

GeneTree

ENSGT00560000076879.

HOVERGEN

HBG107814.

OMA

RRASQRW.

PhylomeDB

Q92796.

Enzyme and pathway databases

Reactome

REACT_111045. Developmental Biology.
REACT_13685. Neuronal System.

Gene expression databases

ArrayExpress

Q92796.

Bgee

Q92796.

CleanEx

HS_DLG3.

Genevestigator

Q92796.

GermOnline

ENSG00000082458. 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.
IPR001478. PDZ/DHR/GLGF.
IPR019583. PDZ_assoc.
IPR001452. SH3_domain.
[Graphical view]

KO

K12075.

Pfam

PF00625. Guanylate_kin. 1 hit.
PF10608. MAGUK_N_PEST. 1 hit.
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.

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

NextBio

7061.

SOURCE

Search...

Entry information

Entry name

DLG3_HUMAN

Accession

Primary (citable) accession number: Q92796
Secondary accession number(s): D3DVU5, Q5JUW7, Q9ULI8

Entry history

Integrated into UniProtKB/Swiss-Prot:	November 1, 1997
Last sequence update:	December 16, 2008
Last modified:	January 25, 2012
This is version 122 of the entry and version 2 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.