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Q92796 (DLG3_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 149. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (6) | 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 3
Alternative name(s):
Neuroendocrine-DLG
Synapse-associated protein 102
Short name=SAP-102
Short name=SAP102
XLMR
Gene names
Name:DLG3
Synonyms:KIAA1232
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length817 AA.
Sequence statusComplete.
Protein existenceEvidence 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.7 Ref.8 Ref.10 Ref.11

Involvement in disease

Mental retardation, X-linked 90 (MRX90) [MIM:300850]: A disorder characterized by significantly below average general intellectual functioning associated with impairments in adaptive behavior and manifested during the developmental period. Intellectual deficiency is the only primary symptom of non-syndromic X-linked mental retardation, while syndromic mental retardation presents with associated physical, neurological and/or psychiatric manifestations.
Note: The disease is caused by mutations affecting the gene represented in this entry. Ref.9

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 diversityAlternative splicing
Polymorphism
   DiseaseMental retardation
   DomainRepeat
SH3 domain
   PTMPhosphoprotein
   Technical term3D-structure
Complete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processaxon guidance

Traceable author statement. Source: Reactome

establishment of planar polarity

Inferred from electronic annotation. Source: Ensembl

establishment or maintenance of epithelial cell apical/basal polarity

Inferred from electronic annotation. Source: Ensembl

negative regulation of cell proliferation

Non-traceable author statement Ref.1. Source: UniProtKB

negative regulation of phosphatase activity

Inferred from direct assay PubMed 19389623. Source: UniProtKB

synaptic transmission

Traceable author statement. Source: Reactome

   Cellular_componentalpha-amino-3-hydroxy-5-methyl-4-isoxazolepropionic acid selective glutamate receptor complex

Inferred from electronic annotation. Source: Ensembl

cytoplasm

Inferred from electronic annotation. Source: Ensembl

dendritic shaft

Inferred from electronic annotation. Source: Ensembl

extracellular space

Inferred from direct assay PubMed 22664934. Source: UniProt

growth cone

Inferred from electronic annotation. Source: Ensembl

neuronal cell body

Inferred from electronic annotation. Source: Ensembl

plasma membrane

Traceable author statement. Source: Reactome

synapse

Inferred from electronic annotation. Source: Ensembl

tight junction

Inferred from electronic annotation. Source: Ensembl

   Molecular_functionphosphatase binding

Inferred from direct assay PubMed 19389623. Source: UniProtKB

protein binding

Inferred from physical interaction Ref.11. Source: UniProtKB

Complete GO annotation...

Binary interactions

With

Entry

#Exp.

IntAct

Notes

PPP1CAP621362EBI-80440,EBI-357253

Alternative products

This entry describes 3 isoforms produced by alternative splicing. [Align] [Select]
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.
Isoform 3 (identifier: Q92796-3)

The sequence of this isoform differs from the canonical sequence as follows:
     1-483: Missing.
     592-606: DFPGLSDDYYGAKNL → SIKTKRKKSFRLSRKFPFYKSKENMAQESSIQEQGVTSNTSDSESSS
Note: No experimental confirmation available.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 817817Disks large homolog 3
PRO_0000094557

Regions

Domain130 – 21788PDZ 1
Domain226 – 31186PDZ 2
Domain379 – 46587PDZ 3
Domain503 – 56866SH3
Domain627 – 802176Guanylate kinase-like

Amino acid modifications

Modified residue6731Phosphotyrosine By similarity

Natural variations

Alternative sequence1 – 483483Missing in isoform 3.
VSP_043717
Alternative sequence1 – 336336Missing in isoform 2.
VSP_035940
Alternative sequence337 – 38145HISHN…EEDFT → MERARKFSGSGLAMGLGSAS ASAWRRASQRWAWPLRSLRP GGDA in isoform 2.
VSP_035941
Alternative sequence592 – 60615DFPGL…GAKNL → SIKTKRKKSFRLSRKFPFYK SKENMAQESSIQEQGVTSNT SDSESSS in isoform 2 and isoform 3.
VSP_035942
Natural variant401G → R in a colorectal cancer sample; somatic mutation. Ref.16
VAR_036591

Experimental info

Sequence conflict871P → L in AAB61453. Ref.1
Sequence conflict1901D → E in AAB61453. Ref.1

Secondary structure

............................................ 817
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
Isoform 1 [UniParc].

Last modified December 16, 2008. Version 2.
Checksum: CE125E9BEE3EEC66

FASTA81790,314
        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 

« Hide

Isoform 2 [UniParc].

Checksum: 9330A330FF9F8FE5
Show »

FASTA51257,937
Isoform 3 [UniParc].

Checksum: 91BEFB73D3CA7C8D
Show »

FASTA36642,112

References

« Hide '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] [Europe PMC] [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] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
Tissue: Brain.
[3]"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. expand/collapse author list , 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] (ISOFORMS 2 AND 3).
Tissue: Thymus and Trachea.
[4]"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. expand/collapse author list , 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] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[5]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. expand/collapse author list , 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].
[6]"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] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
Tissue: Brain.
[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]"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.
[9]"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. expand/collapse author list , 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] [Europe PMC] [Abstract]
Cited for: INVOLVEMENT IN MRX90.
[10]"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.
[11]"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.
[12]"System-wide temporal characterization of the proteome and phosphoproteome of human embryonic stem cell differentiation."
Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J., Johansen P.T., Kratchmarova I., Kassem M., Mann M., Olsen J.V., Blagoev B.
Sci. Signal. 4:RS3-RS3(2011) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[13]"N-terminal acetylome analyses and functional insights of the N-terminal acetyltransferase NatB."
Van Damme P., Lasa M., Polevoda B., Gazquez C., Elosegui-Artola A., Kim D.S., De Juan-Pardo E., Demeyer K., Hole K., Larrea E., Timmerman E., Prieto J., Arnesen T., Sherman F., Gevaert K., Aldabe R.
Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[14]"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.
[15]"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.
[16]"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. expand/collapse author list , 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] [Europe PMC] [Abstract]
Cited for: VARIANT [LARGE SCALE ANALYSIS] ARG-40.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
U49089 mRNA. Translation: AAB61453.1.
AB033058 mRNA. Translation: BAA86546.1. Different initiation.
AK303377 mRNA. Translation: BAG64433.1.
AK304020 mRNA. Translation: BAG64935.1.
AK316518 mRNA. Translation: BAH14889.1.
AL139109 Genomic DNA. No translation available.
AL139398 Genomic DNA. Translation: CAI41022.1.
AL139398 Genomic DNA. Translation: CAI41023.1.
CH471132 Genomic DNA. Translation: EAX05333.1.
CH471132 Genomic DNA. Translation: EAX05335.1.
CH471132 Genomic DNA. Translation: EAX05337.1.
CH471132 Genomic DNA. Translation: EAX05338.1.
BC093864 mRNA. Translation: AAH93864.1.
BC093866 mRNA. Translation: AAH93866.1.
CCDSCCDS14403.1. [Q92796-1]
CCDS43967.1. [Q92796-2]
CCDS55439.1. [Q92796-3]
RefSeqNP_001159750.1. NM_001166278.1. [Q92796-3]
NP_065781.1. NM_020730.2. [Q92796-2]
NP_066943.2. NM_021120.3. [Q92796-1]
XP_005262305.1. XM_005262248.1. [Q92796-3]
UniGeneHs.721586.

3D structure databases

PDBe
RCSB-PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
1UM7NMR-A382-475[»]
2FE5X-ray1.10A223-314[»]
2I1NX-ray1.85A/B126-222[»]
ProteinModelPortalQ92796.
SMRQ92796. Positions 61-314, 332-817.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid108085. 42 interactions.
IntActQ92796. 3 interactions.
MINTMINT-109320.
STRING9606.ENSP00000363480.

PTM databases

PhosphoSiteQ92796.

Polymorphism databases

DMDM218512007.

Proteomic databases

MaxQBQ92796.
PaxDbQ92796.
PRIDEQ92796.

Protocols and materials databases

DNASU1741.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000374355; ENSP00000363475; ENSG00000082458. [Q92796-2]
ENST00000374360; ENSP00000363480; ENSG00000082458. [Q92796-1]
ENST00000542398; ENSP00000441393; ENSG00000082458. [Q92796-3]
GeneID1741.
KEGGhsa:1741.
UCSCuc004dyi.2. human. [Q92796-1]
uc004dyj.2. human. [Q92796-2]
uc011mpn.2. human. [Q92796-3]

Organism-specific databases

CTD1741.
GeneCardsGC0XP069664.
H-InvDBHIX0016853.
HGNCHGNC:2902. DLG3.
HPAHPA001733.
MIM300189. gene.
300850. phenotype.
neXtProtNX_Q92796.
Orphanet777. X-linked non-syndromic intellectual disability.
PharmGKBPA164741439.
HUGESearch...
GenAtlasSearch...

Phylogenomic databases

eggNOGCOG0194.
HOGENOMHOG000232102.
HOVERGENHBG107814.
KOK12075.
OMARASQRWA.
PhylomeDBQ92796.
TreeFamTF323171.

Enzyme and pathway databases

ReactomeREACT_111045. Developmental Biology.
REACT_13685. Neuronal System.

Gene expression databases

ArrayExpressQ92796.
BgeeQ92796.
CleanExHS_DLG3.
GenevestigatorQ92796.

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.
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.
PF00018. SH3_1. 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

ChiTaRSDLG3. human.
EvolutionaryTraceQ92796.
GenomeRNAi1741.
NextBio7061.
PROQ92796.
SOURCESearch...

Entry information

Entry nameDLG3_HUMAN
AccessionPrimary (citable) accession number: Q92796
Secondary accession number(s): B4E0H1 expand/collapse secondary AC list , D3DVU5, Q5JUW6, Q5JUW7, Q9ULI8
Entry history
Integrated into UniProtKB/Swiss-Prot: November 1, 1997
Last sequence update: December 16, 2008
Last modified: July 9, 2014
This is version 149 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
DisclaimerAny 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.

Relevant documents

SIMILARITY comments

Index of protein domains and families

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

MIM cross-references

Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot

Human polymorphisms and disease mutations

Index of human polymorphisms and disease mutations

Human entries with polymorphisms or disease mutations

List of human entries with polymorphisms or disease mutations

Human chromosome X

Human chromosome X: entries, gene names and cross-references to MIM