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Q92796

- DLG3_HUMAN

UniProt

Q92796 - DLG3_HUMAN

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Protein

Disks large homolog 3

Gene
DLG3, KIAA1232
Organism
Homo sapiens (Human)
Status
Reviewed - 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. phosphatase binding Source: UniProtKB
  2. protein 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: Ensembl
  4. negative regulation of cell proliferation Source: UniProtKB
  5. negative regulation of phosphatase activity Source: UniProtKB
  6. synaptic transmission Source: Reactome
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: 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. cytoplasm Source: Ensembl
  3. dendritic shaft Source: Ensembl
  4. extracellular space Source: UniProt
  5. growth cone Source: Ensembl
  6. neuronal cell body Source: Ensembl
  7. plasma membrane Source: Reactome
  8. synapse Source: Ensembl
  9. tight junction Source: Ensembl
Complete GO annotation...

Pathology & Biotechi

Involvement in diseasei

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.1 Publication

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 – 6731Phosphotyrosine By similarity

Keywords - PTMi

Phosphoprotein

Proteomic databases

MaxQBiQ92796.
PaxDbiQ92796.
PRIDEiQ92796.

PTM databases

PhosphoSiteiQ92796.

Expressioni

Gene expression databases

ArrayExpressiQ92796.
BgeeiQ92796.
CleanExiHS_DLG3.
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 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 LRFN4.5 Publications

Binary interactionsi

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

Protein-protein interaction databases

BioGridi108085. 42 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 – 1359
Beta strandi142 – 1476
Beta strandi160 – 1656
Helixi170 – 1745
Beta strandi182 – 1865
Helixi196 – 20510
Beta strandi208 – 21710
Beta strandi224 – 2307
Beta strandi238 – 2425
Beta strandi255 – 2606
Helixi265 – 2695
Beta strandi277 – 2815
Helixi291 – 2999
Beta strandi303 – 3108
Beta strandi383 – 3908
Beta strandi396 – 3983
Beta strandi416 – 4183
Helixi419 – 4224
Beta strandi431 – 4377
Helixi445 – 4539
Beta strandi457 – 4648
Helixi467 – 4759

3D structure databases

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

Miscellaneous databases

EvolutionaryTraceiQ92796.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini130 – 21788PDZ 1Add
BLAST
Domaini226 – 31186PDZ 2Add
BLAST
Domaini379 – 46587PDZ 3Add
BLAST
Domaini503 – 56866SH3Add
BLAST
Domaini627 – 802176Guanylate kinase-likeAdd
BLAST

Sequence similaritiesi

Belongs to the MAGUK family.
Contains 3 PDZ (DHR) domains.
Contains 1 SH3 domain.

Keywords - Domaini

Repeat, SH3 domain

Phylogenomic databases

eggNOGiCOG0194.
HOGENOMiHOG000232102.
HOVERGENiHBG107814.
KOiK12075.
OMAiRASQRWA.
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. Align

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

MHKHQHCCKC PECYEVTRLA ALRRLEPPGY GDWQVPDPYG PGGGNGASAG    50
YGGYSSQTLP SQAGATPTPR TKAKLIPTGR DVGPVPPKPV PGKSTPKLNG 100
SGPSWWPECT CTNRDWYEQV NGSDGMFKYE EIVLERGNSG LGFSIAGGID 150
NPHVPDDPGI FITKIIPGGA AAMDGRLGVN DCVLRVNEVD VSEVVHSRAV 200
EALKEAGPVV RLVVRRRQPP PETIMEVNLL KGPKGLGFSI AGGIGNQHIP 250
GDNSIYITKI IEGGAAQKDG RLQIGDRLLA VNNTNLQDVR HEEAVASLKN 300
TSDMVYLKVA KPGSLHLNDM YAPPDYASTF TALADNHISH NSSLGYLGAV 350
ESKVSYPAPP QVPPTRYSPI PRHMLAEEDF TREPRKIILH KGSTGLGFNI 400
VGGEDGEGIF VSFILAGGPA DLSGELRRGD RILSVNGVNL RNATHEQAAA 450
ALKRAGQSVT IVAQYRPEEY SRFESKIHDL REQMMNSSMS SGSGSLRTSE 500
KRSLYVRALF DYDRTRDSCL PSQGLSFSYG DILHVINASD DEWWQARLVT 550
PHGESEQIGV IPSKKRVEKK ERARLKTVKF HARTGMIESN RDFPGLSDDY 600
YGAKNLKGQE DAILSYEPVT RQEIHYARPV IILGPMKDRV NDDLISEFPH 650
KFGSCVPHTT RPRRDNEVDG QDYHFVVSRE QMEKDIQDNK FIEAGQFNDN 700
LYGTSIQSVR AVAERGKHCI LDVSGNAIKR LQQAQLYPIA IFIKPKSIEA 750
LMEMNRRQTY EQANKIYDKA MKLEQEFGEY FTAIVQGDSL EEIYNKIKQI 800
IEDQSGHYIW VPSPEKL 817
Length:817
Mass (Da):90,314
Last modified:December 16, 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.

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

Sequence cautioni

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

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. VSP_043717Add
BLAST
Alternative sequencei1 – 336336Missing in isoform 2. VSP_035940Add
BLAST
Alternative sequencei337 – 38145HISHN…EEDFT → MERARKFSGSGLAMGLGSAS ASAWRRASQRWAWPLRSLRP GGDA in isoform 2. VSP_035941Add
BLAST
Alternative sequencei592 – 60615DFPGL…GAKNL → SIKTKRKKSFRLSRKFPFYK SKENMAQESSIQEQGVTSNT SDSESSS in isoform 2 and isoform 3. VSP_035942Add
BLAST

Sequence conflict

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti87 – 871P → L in AAB61453. 1 Publication
Sequence conflicti190 – 1901D → E in AAB61453. 1 Publication

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
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:
EMBL
GenBank
DDBJ
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 .
CCDSi CCDS14403.1. [Q92796-1 ]
CCDS43967.1. [Q92796-2 ]
CCDS55439.1. [Q92796-3 ]
RefSeqi NP_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 ]
UniGenei Hs.721586.

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
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 [» ]
ProteinModelPortali Q92796.
SMRi Q92796. Positions 61-314, 332-817.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 108085. 42 interactions.
IntActi Q92796. 3 interactions.
MINTi MINT-109320.
STRINGi 9606.ENSP00000363480.

PTM databases

PhosphoSitei Q92796.

Polymorphism databases

DMDMi 218512007.

Proteomic databases

MaxQBi Q92796.
PaxDbi Q92796.
PRIDEi Q92796.

Protocols and materials databases

DNASUi 1741.
Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENST00000374355 ; ENSP00000363475 ; ENSG00000082458 . [Q92796-2 ]
ENST00000374360 ; ENSP00000363480 ; ENSG00000082458 . [Q92796-1 ]
ENST00000542398 ; ENSP00000441393 ; ENSG00000082458 . [Q92796-3 ]
GeneIDi 1741.
KEGGi hsa:1741.
UCSCi uc004dyi.2. human. [Q92796-1 ]
uc004dyj.2. human. [Q92796-2 ]
uc011mpn.2. human. [Q92796-3 ]

Organism-specific databases

CTDi 1741.
GeneCardsi GC0XP069664.
H-InvDB HIX0016853.
HGNCi HGNC:2902. DLG3.
HPAi HPA001733.
MIMi 300189. gene.
300850. phenotype.
neXtProti NX_Q92796.
Orphaneti 777. X-linked non-syndromic intellectual disability.
PharmGKBi PA164741439.
HUGEi Search...
GenAtlasi Search...

Phylogenomic databases

eggNOGi COG0194.
HOGENOMi HOG000232102.
HOVERGENi HBG107814.
KOi K12075.
OMAi RASQRWA.
PhylomeDBi Q92796.
TreeFami TF323171.

Enzyme and pathway databases

Reactomei REACT_21346. Activation of Ca-permeable Kainate Receptor.
REACT_22329. NrCAM interactions.

Miscellaneous databases

ChiTaRSi DLG3. human.
EvolutionaryTracei Q92796.
GenomeRNAii 1741.
NextBioi 7061.
PROi Q92796.
SOURCEi Search...

Gene expression databases

ArrayExpressi Q92796.
Bgeei Q92796.
CleanExi HS_DLG3.
Genevestigatori Q92796.

Family and domain databases

Gene3Di 2.30.42.10. 3 hits.
3.40.50.300. 2 hits.
InterProi IPR016313. 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 ]
PANTHERi PTHR23119. PTHR23119. 1 hit.
Pfami 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 ]
PIRSFi PIRSF001741. MAGUK_DLGH. 1 hit.
SMARTi SM00072. GuKc. 1 hit.
SM00228. PDZ. 3 hits.
SM00326. SH3. 1 hit.
[Graphical view ]
SUPFAMi SSF50044. SSF50044. 2 hits.
SSF50156. SSF50156. 3 hits.
SSF52540. SSF52540. 1 hit.
PROSITEi PS00856. GUANYLATE_KINASE_1. 1 hit.
PS50052. GUANYLATE_KINASE_2. 1 hit.
PS50106. PDZ. 3 hits.
PS50002. SH3. 1 hit.
[Graphical view ]
ProtoNeti Search...

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(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.
    , 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.
    , 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. 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. 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. 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. 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. 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: November 1, 1997
Last sequence update: December 16, 2008
Last modified: September 3, 2014
This is version 150 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

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