Reviewed,
UniProtKB/Swiss-Prot Q92796 (DLG3_HUMAN)
Last modified
February 9, 2010.
Version 102.
History...
Clusters with 100%,
90%,
50% identity |
Documents (6) |
Third-party data |
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Names and origin
| Protein names | Recommended name: Disks large homolog 3 Alternative name(s): Synapse-associated protein 102 Short name=SAP-102 Short name=SAP102 Neuroendocrine-DLG XLMR | ||||
| Gene names |
| ||||
| Organism | Homo sapiens (Human) [Complete proteome] | ||||
| 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 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). Ref.1 Ref.6 Ref.7 Ref.10 |
| Involvement in disease | Defects in DLG3 are the cause of mental retardation X-linked type 90 (MRX90) [MIM:300189]. 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. |
Ontologies
| Keywords | |
|---|---|
| Coding sequence diversity | Alternative splicing Polymorphism |
| Disease | Mental retardation |
| Domain | Repeat SH3 domain |
| PTM | Acetylation Phosphoprotein |
| Technical term | 3D-structure Complete proteome |
| Gene Ontology (GO) | |
| Biological process | negative regulation of cell proliferation Ref.1 Non-traceable author statement. Source: UniProtKB |
| Molecular function | guanylate kinase activity Non-traceable author statement. Source: UniProtKB protein binding Ref.10Inferred from physical interaction. Source: UniProtKB |
| Complete GO annotation... | |
Binary interactions
With | Entry | #Exp. | IntAct | Notes |
|---|---|---|---|---|
| ABCA1 | O95477 | 1 | EBI-80440,EBI-784112 | |
| ANXA1 | P04083 | 1 | EBI-80440,EBI-354007 | |
| CAMK2A | Q9UQM7 | 1 | EBI-80440,EBI-1383687 | |
| CUL2 | Q13617 | 1 | EBI-80440,EBI-456179 | |
| HIST1H2BC | P62807 | 1 | EBI-80440,EBI-354552 | |
| KLHDC3 | Q9BQ90 | 1 | EBI-80440,EBI-1055396 | |
| KRT31 | Q15323 | 1 | EBI-80440,EBI-948001 | |
| KRT34 | O76011 | 1 | EBI-80440,EBI-1047093 | |
| KRT82 | Q9NSB4 | 1 | EBI-80440,EBI-1045341 | |
| KRT85 | P78386 | 1 | EBI-80440,EBI-1049371 | |
| S100A3 | P33764 | 1 | EBI-80440,EBI-1044747 |
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.9 Ref.11 Ref.12 | |||||||||||||||||||||||||||||||||||||||||||||||
| Modified residue | 765 | 1 | N6-acetyllysine Ref.13 | |||||||||||||||||||||||||||||||||||||||||||||||
| Modified residue | 808 | 1 | Phosphotyrosine Ref.9 | |||||||||||||||||||||||||||||||||||||||||||||||
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.16 | 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 | ||||||||||||||||||||||||||||||||||||||||||||||||||
Helix Strand Turn | ||||||||||||||||||||||||||||||||||||||||||||||||||
| 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
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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: 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. 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. 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. Raymond F.L.Am. J. Hum. Genet. 75:318-324(2004) [PubMed: 15185169] [Abstract] Cited for: DISEASE. |
| [9] | "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. 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. |
| [10] | "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. |
| [11] | "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. |
| [12] | "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: T-cell. |
| [13] | "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. |
| [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. Velculescu V.E.Science 314:268-274(2006) [PubMed: 16959974] [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. AL139398 Genomic DNA. Translation: CAI41022.1. CH471132 Genomic DNA. Translation: EAX05337.1. BC093864 mRNA. Translation: AAH93864.1. BC093866 mRNA. Translation: AAH93866.1. | ||||||||||||||||||||||||
| IPI | IPI00023343. IPI00647338. | ||||||||||||||||||||||||
| RefSeq | NP_001159750.1. NP_065781.1. NP_066943.2. | ||||||||||||||||||||||||
3D structure databases | |||||||||||||||||||||||||
| PDBe RCSB PDB PDBj |
| ||||||||||||||||||||||||
| SMR | Q92796. Positions 129-312, 225-468, 504-817. | ||||||||||||||||||||||||
| ModBase | Search... | ||||||||||||||||||||||||
Protein-protein interaction databases | |||||||||||||||||||||||||
| IntAct | Q92796. 13 interactions. | ||||||||||||||||||||||||
| STRING | Q92796. | ||||||||||||||||||||||||
PTM databases | |||||||||||||||||||||||||
| PhosphoSite | Q92796. | ||||||||||||||||||||||||
Proteomic databases | |||||||||||||||||||||||||
| PRIDE | Q92796. | ||||||||||||||||||||||||
Genome annotation databases | |||||||||||||||||||||||||
| Ensembl | ENST00000374360; ENSP00000363480; ENSG00000082458; Homo sapiens. [Genome view] | ||||||||||||||||||||||||
| GeneID | 1741. | ||||||||||||||||||||||||
Organism-specific databases | |||||||||||||||||||||||||
| CTD | 1741. | ||||||||||||||||||||||||
| GeneCards | GC0XP069581. | ||||||||||||||||||||||||
| H-InvDB | HIX0016853. | ||||||||||||||||||||||||
| HGNC | HGNC:2902. DLG3. | ||||||||||||||||||||||||
| HPA | HPA001733. | ||||||||||||||||||||||||
| MIM | 300189. gene+phenotype. | ||||||||||||||||||||||||
| Orphanet | 101685. Rare intellectual deficit without developmental anomaly. | ||||||||||||||||||||||||
| PharmGKB | PA27358. | ||||||||||||||||||||||||
| HUGE | Search... | ||||||||||||||||||||||||
| GenAtlas | Search... | ||||||||||||||||||||||||
Phylogenomic databases | |||||||||||||||||||||||||
| HOVERGEN | Q92796. | ||||||||||||||||||||||||
| OMA | AWRRASQ. | ||||||||||||||||||||||||
| PhylomeDB | Q92796. | ||||||||||||||||||||||||
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] | ||||||||||||||||||||||||
| 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] | ||||||||||||||||||||||||
| 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 Resources | |||||||||||||||||||||||||
| NextBio | 7061. | ||||||||||||||||||||||||
| SOURCE | Search... | ||||||||||||||||||||||||
Entry information
| Entry name | DLG3_HUMAN | ||||||||
| Accession | Primary (citable) accession number: Q92796 Secondary accession number(s): Q5JUW7, Q9ULI8 | ||||||||
| Entry history |
| ||||||||
| Entry status | Reviewed (UniProtKB/Swiss-Prot) | ||||||||
| Annotation project | HPI (Human Proteome Initiative) | ||||||||
| 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. | ||||||||
Relevant documents
| Human chromosome X Human chromosome X: entries, gene names and cross-references to MIM |
| Human entries with polymorphisms or disease mutations List of human entries with polymorphisms or disease mutations |
| Human polymorphisms and disease mutations Index of human polymorphisms and disease mutations |
| MIM cross-references Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot |
| PDB cross-references Index of Protein Data Bank (PDB) cross-references |
| SIMILARITY comments Index of protein domains and families |

Clusters with


