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Protein

Disks large homolog 3

Gene

DLG3

Organism
Homo sapiens (Human)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Required for learning most likely through its role in synaptic plasticity following NMDA receptor signaling.

GO - Molecular functioni

  1. guanylate kinase activity Source: GO_Central
  2. ionotropic glutamate receptor binding Source: GO_Central
  3. phosphatase binding Source: UniProtKB

GO - Biological processi

  1. axon guidance Source: Reactome
  2. establishment of planar polarity Source: Ensembl
  3. establishment or maintenance of epithelial cell apical/basal polarity Source: GO_Central
  4. negative regulation of cell proliferation Source: UniProtKB
  5. negative regulation of phosphatase activity Source: UniProtKB
  6. nervous system development Source: GO_Central
  7. nucleotide phosphorylation Source: GOC
  8. receptor clustering Source: GO_Central
  9. receptor localization to synapse Source: GO_Central
  10. synaptic transmission Source: GO_Central
Complete GO annotation...

Enzyme and pathway databases

ReactomeiREACT_21346. Activation of Ca-permeable Kainate Receptor.
REACT_22329. NrCAM interactions.

Names & Taxonomyi

Protein namesi
Recommended name:
Disks large homolog 3
Alternative name(s):
Neuroendocrine-DLG
Synapse-associated protein 102
Short name:
SAP-102
Short name:
SAP102
XLMR
Gene namesi
Name:DLG3
Synonyms:KIAA1232
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640 Componenti: Chromosome X

Organism-specific databases

HGNCiHGNC:2902. DLG3.

Subcellular locationi

GO - Cellular componenti

  1. alpha-amino-3-hydroxy-5-methyl-4-isoxazolepropionic acid selective glutamate receptor complex Source: Ensembl
  2. basolateral plasma membrane Source: GO_Central
  3. cytoplasm Source: Ensembl
  4. dendritic shaft Source: Ensembl
  5. extracellular space Source: UniProtKB
  6. growth cone Source: Ensembl
  7. neuronal cell body Source: Ensembl
  8. plasma membrane Source: Reactome
  9. postsynaptic density Source: GO_Central
  10. postsynaptic membrane Source: GO_Central
  11. tight junction Source: Ensembl
Complete GO annotation...

Pathology & Biotechi

Involvement in diseasei

Mental retardation, X-linked 90 (MRX90)1 Publication

The disease is caused by mutations affecting the gene represented in this entry.

Disease descriptionA 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.

See also OMIM:300850

Keywords - Diseasei

Mental retardation

Organism-specific databases

MIMi300850. phenotype.
Orphaneti777. X-linked non-syndromic intellectual disability.
PharmGKBiPA164741439.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 817817Disks large homolog 3PRO_0000094557Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei673 – 6731PhosphotyrosineBy similarity

Keywords - PTMi

Acetylation, Phosphoprotein

Proteomic databases

MaxQBiQ92796.
PaxDbiQ92796.
PRIDEiQ92796.

PTM databases

PhosphoSiteiQ92796.

Expressioni

Gene expression databases

BgeeiQ92796.
CleanExiHS_DLG3.
ExpressionAtlasiQ92796. baseline and differential.
GenevestigatoriQ92796.

Organism-specific databases

HPAiHPA001733.

Interactioni

Subunit structurei

Interacts through its PDZ domains with NETO1, GRIN2B and SYNGAP1. Interacts through its guanylate kinase-like domain with DLGAP1, DLGAP2, DLGAP3 and DLGAP4. Interacts with FLTP/C1orf192 (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.By similarity5 Publications

Binary interactionsi

WithEntry#Exp.IntActNotes
PPP1CAP621362EBI-80440,EBI-357253

Protein-protein interaction databases

BioGridi108085. 44 interactions.
IntActiQ92796. 3 interactions.
MINTiMINT-109320.
STRINGi9606.ENSP00000363480.

Structurei

Secondary structure

1
817
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi127 – 1359Combined sources
Beta strandi142 – 1476Combined sources
Beta strandi160 – 1656Combined sources
Helixi170 – 1745Combined sources
Beta strandi182 – 1865Combined sources
Helixi196 – 20510Combined sources
Beta strandi208 – 21710Combined sources
Beta strandi224 – 2307Combined sources
Beta strandi238 – 2425Combined sources
Beta strandi255 – 2606Combined sources
Helixi265 – 2695Combined sources
Beta strandi277 – 2815Combined sources
Helixi291 – 2999Combined sources
Beta strandi303 – 3108Combined sources
Beta strandi383 – 3908Combined sources
Beta strandi396 – 3983Combined sources
Beta strandi416 – 4183Combined sources
Helixi419 – 4224Combined sources
Beta strandi431 – 4377Combined sources
Helixi445 – 4539Combined sources
Beta strandi457 – 4648Combined sources
Helixi467 – 4759Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1UM7NMR-A382-475[»]
2FE5X-ray1.10A223-314[»]
2I1NX-ray1.85A/B126-222[»]
ProteinModelPortaliQ92796.
SMRiQ92796. Positions 61-314, 332-817.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiQ92796.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini130 – 21788PDZ 1PROSITE-ProRule annotationAdd
BLAST
Domaini226 – 31186PDZ 2PROSITE-ProRule annotationAdd
BLAST
Domaini379 – 46587PDZ 3PROSITE-ProRule annotationAdd
BLAST
Domaini503 – 56866SH3PROSITE-ProRule annotationAdd
BLAST
Domaini627 – 802176Guanylate kinase-likePROSITE-ProRule annotationAdd
BLAST

Sequence similaritiesi

Belongs to the MAGUK family.Curated
Contains 1 guanylate kinase-like domain.PROSITE-ProRule annotation
Contains 3 PDZ (DHR) domains.PROSITE-ProRule annotation
Contains 1 SH3 domain.PROSITE-ProRule annotation

Keywords - Domaini

Repeat, SH3 domain

Phylogenomic databases

eggNOGiCOG0194.
GeneTreeiENSGT00760000118866.
HOGENOMiHOG000232102.
HOVERGENiHBG107814.
InParanoidiQ92796.
KOiK12075.
OMAiASQRWAW.
PhylomeDBiQ92796.
TreeFamiTF323171.

Family and domain databases

Gene3Di2.30.42.10. 3 hits.
3.40.50.300. 2 hits.
InterProiIPR016313. 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]
PANTHERiPTHR23119. PTHR23119. 1 hit.
PfamiPF00625. 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]
PIRSFiPIRSF001741. MAGUK_DLGH. 1 hit.
SMARTiSM00072. GuKc. 1 hit.
SM00228. PDZ. 3 hits.
SM00326. SH3. 1 hit.
[Graphical view]
SUPFAMiSSF50044. SSF50044. 2 hits.
SSF50156. SSF50156. 3 hits.
SSF52540. SSF52540. 1 hit.
PROSITEiPS00856. GUANYLATE_KINASE_1. 1 hit.
PS50052. GUANYLATE_KINASE_2. 1 hit.
PS50106. PDZ. 3 hits.
PS50002. SH3. 1 hit.
[Graphical view]

Sequences (3)i

Sequence statusi: Complete.

This entry describes 3 isoformsi produced by alternative splicing. AlignAdd to basket

Isoform 1 (identifier: Q92796-1) [UniParc]FASTAAdd to basket

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.

« Hide

        10         20         30         40         50
MHKHQHCCKC PECYEVTRLA ALRRLEPPGY GDWQVPDPYG PGGGNGASAG
60 70 80 90 100
YGGYSSQTLP SQAGATPTPR TKAKLIPTGR DVGPVPPKPV PGKSTPKLNG
110 120 130 140 150
SGPSWWPECT CTNRDWYEQV NGSDGMFKYE EIVLERGNSG LGFSIAGGID
160 170 180 190 200
NPHVPDDPGI FITKIIPGGA AAMDGRLGVN DCVLRVNEVD VSEVVHSRAV
210 220 230 240 250
EALKEAGPVV RLVVRRRQPP PETIMEVNLL KGPKGLGFSI AGGIGNQHIP
260 270 280 290 300
GDNSIYITKI IEGGAAQKDG RLQIGDRLLA VNNTNLQDVR HEEAVASLKN
310 320 330 340 350
TSDMVYLKVA KPGSLHLNDM YAPPDYASTF TALADNHISH NSSLGYLGAV
360 370 380 390 400
ESKVSYPAPP QVPPTRYSPI PRHMLAEEDF TREPRKIILH KGSTGLGFNI
410 420 430 440 450
VGGEDGEGIF VSFILAGGPA DLSGELRRGD RILSVNGVNL RNATHEQAAA
460 470 480 490 500
ALKRAGQSVT IVAQYRPEEY SRFESKIHDL REQMMNSSMS SGSGSLRTSE
510 520 530 540 550
KRSLYVRALF DYDRTRDSCL PSQGLSFSYG DILHVINASD DEWWQARLVT
560 570 580 590 600
PHGESEQIGV IPSKKRVEKK ERARLKTVKF HARTGMIESN RDFPGLSDDY
610 620 630 640 650
YGAKNLKGQE DAILSYEPVT RQEIHYARPV IILGPMKDRV NDDLISEFPH
660 670 680 690 700
KFGSCVPHTT RPRRDNEVDG QDYHFVVSRE QMEKDIQDNK FIEAGQFNDN
710 720 730 740 750
LYGTSIQSVR AVAERGKHCI LDVSGNAIKR LQQAQLYPIA IFIKPKSIEA
760 770 780 790 800
LMEMNRRQTY EQANKIYDKA MKLEQEFGEY FTAIVQGDSL EEIYNKIKQI
810
IEDQSGHYIW VPSPEKL
Length:817
Mass (Da):90,314
Last modified:December 15, 2008 - v2
Checksum:iCE125E9BEE3EEC66
GO
Isoform 2 (identifier: Q92796-2) [UniParc]FASTAAdd to basket

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.

Show »
Length:512
Mass (Da):57,937
Checksum:i9330A330FF9F8FE5
GO
Isoform 3 (identifier: Q92796-3) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     1-483: Missing.
     592-606: DFPGLSDDYYGAKNL → SIKTKRKKSFRLSRKFPFYKSKENMAQESSIQEQGVTSNTSDSESSS

Note: No experimental confirmation available. Contains a N-acetylmethionine at position 1. Initiator Met-1 is removed. Contains a N-acetylmethionine at position 2.1 Publication

Show »
Length:366
Mass (Da):42,112
Checksum:i91BEFB73D3CA7C8D
GO

Sequence cautioni

The sequence BAA86546.1 differs from that shown. Reason: Erroneous initiation. Curated

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti87 – 871P → L in AAB61453 (PubMed:9188857).Curated
Sequence conflicti190 – 1901D → E in AAB61453 (PubMed:9188857).Curated

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti40 – 401G → R in a colorectal cancer sample; somatic mutation. 1 Publication
VAR_036591

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei1 – 483483Missing in isoform 3. 1 PublicationVSP_043717Add
BLAST
Alternative sequencei1 – 336336Missing in isoform 2. 2 PublicationsVSP_035940Add
BLAST
Alternative sequencei337 – 38145HISHN…EEDFT → MERARKFSGSGLAMGLGSAS ASAWRRASQRWAWPLRSLRP GGDA in isoform 2. 2 PublicationsVSP_035941Add
BLAST
Alternative sequencei592 – 60615DFPGL…GAKNL → SIKTKRKKSFRLSRKFPFYK SKENMAQESSIQEQGVTSNT SDSESSS in isoform 2 and isoform 3. 2 PublicationsVSP_035942Add
BLAST

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
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.
CCDSiCCDS14403.1. [Q92796-1]
CCDS43967.1. [Q92796-2]
CCDS55439.1. [Q92796-3]
RefSeqiNP_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]
UniGeneiHs.721586.

Genome annotation databases

EnsembliENST00000374355; ENSP00000363475; ENSG00000082458. [Q92796-2]
ENST00000374360; ENSP00000363480; ENSG00000082458. [Q92796-1]
ENST00000542398; ENSP00000441393; ENSG00000082458. [Q92796-3]
GeneIDi1741.
KEGGihsa:1741.
UCSCiuc004dyi.2. human. [Q92796-1]
uc004dyj.2. human. [Q92796-2]
uc011mpn.2. human. [Q92796-3]

Polymorphism databases

DMDMi218512007.

Keywords - Coding sequence diversityi

Alternative splicing, Polymorphism

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
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.
CCDSiCCDS14403.1. [Q92796-1]
CCDS43967.1. [Q92796-2]
CCDS55439.1. [Q92796-3]
RefSeqiNP_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]
UniGeneiHs.721586.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1UM7NMR-A382-475[»]
2FE5X-ray1.10A223-314[»]
2I1NX-ray1.85A/B126-222[»]
ProteinModelPortaliQ92796.
SMRiQ92796. Positions 61-314, 332-817.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi108085. 44 interactions.
IntActiQ92796. 3 interactions.
MINTiMINT-109320.
STRINGi9606.ENSP00000363480.

PTM databases

PhosphoSiteiQ92796.

Polymorphism databases

DMDMi218512007.

Proteomic databases

MaxQBiQ92796.
PaxDbiQ92796.
PRIDEiQ92796.

Protocols and materials databases

DNASUi1741.
Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000374355; ENSP00000363475; ENSG00000082458. [Q92796-2]
ENST00000374360; ENSP00000363480; ENSG00000082458. [Q92796-1]
ENST00000542398; ENSP00000441393; ENSG00000082458. [Q92796-3]
GeneIDi1741.
KEGGihsa:1741.
UCSCiuc004dyi.2. human. [Q92796-1]
uc004dyj.2. human. [Q92796-2]
uc011mpn.2. human. [Q92796-3]

Organism-specific databases

CTDi1741.
GeneCardsiGC0XP069664.
H-InvDBHIX0016853.
HGNCiHGNC:2902. DLG3.
HPAiHPA001733.
MIMi300189. gene.
300850. phenotype.
neXtProtiNX_Q92796.
Orphaneti777. X-linked non-syndromic intellectual disability.
PharmGKBiPA164741439.
HUGEiSearch...
GenAtlasiSearch...

Phylogenomic databases

eggNOGiCOG0194.
GeneTreeiENSGT00760000118866.
HOGENOMiHOG000232102.
HOVERGENiHBG107814.
InParanoidiQ92796.
KOiK12075.
OMAiASQRWAW.
PhylomeDBiQ92796.
TreeFamiTF323171.

Enzyme and pathway databases

ReactomeiREACT_21346. Activation of Ca-permeable Kainate Receptor.
REACT_22329. NrCAM interactions.

Miscellaneous databases

ChiTaRSiDLG3. human.
EvolutionaryTraceiQ92796.
GenomeRNAii1741.
NextBioi7061.
PROiQ92796.
SOURCEiSearch...

Gene expression databases

BgeeiQ92796.
CleanExiHS_DLG3.
ExpressionAtlasiQ92796. baseline and differential.
GenevestigatoriQ92796.

Family and domain databases

Gene3Di2.30.42.10. 3 hits.
3.40.50.300. 2 hits.
InterProiIPR016313. 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]
PANTHERiPTHR23119. PTHR23119. 1 hit.
PfamiPF00625. 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]
PIRSFiPIRSF001741. MAGUK_DLGH. 1 hit.
SMARTiSM00072. GuKc. 1 hit.
SM00228. PDZ. 3 hits.
SM00326. SH3. 1 hit.
[Graphical view]
SUPFAMiSSF50044. SSF50044. 2 hits.
SSF50156. SSF50156. 3 hits.
SSF52540. SSF52540. 1 hit.
PROSITEiPS00856. GUANYLATE_KINASE_1. 1 hit.
PS50052. GUANYLATE_KINASE_2. 1 hit.
PS50106. PDZ. 3 hits.
PS50002. SH3. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  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(1996) [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(1998) [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.
    , 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(2003) [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.
    , 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(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  5. 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(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
    Tissue: Brain.
  7. 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(1999) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH ERBB4.
  9. 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(2005) [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(2007) [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(2010) [PubMed] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  13. Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT MET-1 AND MET-2 (ISOFORM 3), IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS], CLEAVAGE OF INITIATOR METHIONINE [LARGE SCALE ANALYSIS] (ISOFORM 3).
  14. "Solution structure of the third PDZ domain of synapse-associated protein 102."
    RIKEN structural genomics initiative (RSGI)
    Submitted (FEB-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 (NOV-2005) to the PDB data bank
    Cited for: X-RAY CRYSTALLOGRAPHY (1.1 ANGSTROMS) OF 223-314.
  16. Cited for: VARIANT [LARGE SCALE ANALYSIS] ARG-40.

Entry informationi

Entry nameiDLG3_HUMAN
AccessioniPrimary (citable) accession number: Q92796
Secondary accession number(s): B4E0H1
, D3DVU5, Q5JUW6, Q5JUW7, Q9ULI8
Entry historyi
Integrated into UniProtKB/Swiss-Prot: October 31, 1997
Last sequence update: December 15, 2008
Last modified: March 31, 2015
This is version 157 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (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.

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

Documents

  1. Human chromosome X
    Human chromosome X: entries, gene names and cross-references to MIM
  2. Human entries with polymorphisms or disease mutations
    List of human entries with polymorphisms or disease mutations
  3. Human polymorphisms and disease mutations
    Index of human polymorphisms and disease mutations
  4. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  5. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  6. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into Uniref entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.