Q811D0 (DLG1_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Disks large homolog 1

Alternative name(s):
Embryo-dlg/synapse-associated protein 97
Short name=E-dlg/SAP97
Synapse-associated protein 97
Short name=SAP-97
Short name=SAP97

Gene names

Name:	Dlg1
Synonyms:	Dlgh1

Organism

Mus musculus (Mouse) [Reference proteome]

Taxonomic identifier

10090 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Opisthokonta › Metazoa › Eumetazoa › Bilateria › Deuterostomia › Chordata › Craniata › Vertebrata › Gnathostomata › Teleostomi › Euteleostomi › Sarcopterygii › Tetrapoda › Amniota › Mammalia › Theria › Eutheria › Euarchontoglires › Glires › Rodentia › Sciurognathi › Muroidea › Muridae › Murinae › Mus › Mus

Protein attributes

Sequence length	905 AA.
Sequence status	Complete.
Protein existence	Evidence at protein level

General annotation (Comments)

Function	Essential multidomain scaffolding protein required for normal development. Recruits channels, receptors and signaling molecules to discrete plasma membrane domains in polarized cells. Regulates the excitability of cardiac myocytes by modulating the functional expression of Kv4 channels By similarity. Functional regulator of Kv1.5 channel By similarity. May play a role in adherens junction assembly, signal transduction, cell proliferation, synaptogenesis and lymphocyte activation. Ref.6
Subunit structure	Homotetramer Probable. Interacts with KCNF1 and CAMK2 By similarity. Interacts through its PDZ domains with KCND2 and KCND3 By similarity. Interacts with CAMK2 By similarity. Interacts through its PDZ domains with GRIN2A, KCNA1, KCNA2, KCNA3, KCNA4, KCNA5, GRIA1, GPR124 and GPR125. Interacts with cytoskeleton-associated proteins EPB41 and EZR. Found in a complex with KCNA5 and CAV3. Found in a complex with APC and CTNNB1. Interacts with CDH1 through binding to PIK3R1. Forms multiprotein complexes with CASK, LIN7A, LIN7B, LIN7C, APBA1, and KCNJ12. Interacts through its guanylate kinase-like domain with DLGAP1, DLGAP2, DLGAP3, DLGAP4, MAP1A and KIF13B. Interacts with TOPK. Forms a tripartite complex composed of DLG1, MPP7 and LIN7 (LIN7A or LIN7C). May interact with TJAP1 By similarity. May interact with HTR2A. Interacts with LRFN1, LRFN2, LRFN4 and SFPQ By similarity. Interacts with PTEN By similarity. Interacts with FRMPD4 (via C-terminus) By similarity. Ref.4 Ref.5 Ref.7 Ref.8
Subcellular location	Membrane; Peripheral membrane protein By similarity. Basolateral cell membrane By similarity. Endoplasmic reticulum membrane By similarity. Cell junction › synapse › postsynaptic cell membrane › postsynaptic density By similarity. Cell junction › synapse. Note: Colocalizes with EPB41 at regions of intercellular contacts. Basolateral in epithelial cells. May also associate with endoplasmic reticulum membranes. Mainly found in neurons soma, moderately found at postsynaptic densities By similarity.
Tissue specificity	Expressed in epithelial, mesenchymal, neuronal, endothelial and hematopoietic cells during embryogenesis. Expressed in fibroblasts and T-cells. Widely expressed in adult mice. Ref.6
Domain	The PDZ domains may also mediate association to membranes by binding to EPB41 and GPR124 together with the L27 domain that binds CASK and DLG2 By similarity. The L27 domain may regulate DLG1 self-association. The N-terminal alternatively spliced region is capable of binding several SH3 domains and also moderates the level of protein oligomerization By similarity.
Post-translational modification	Phosphorylated by MAPK12 By similarity. Phosphorylation of Ser-232 regulates association with GRIN2A By similarity. Isoform 2 is phosphorylated on Ser-665. Isoform 3 is phosphorylated on Ser-699.
Disruption phenotype	Mice have craniofacial abnormalities as well as a cleft palate. They are smaller than heterozygous littermates, unable to feed and die within 24 hours of birth. Ref.6
Sequence similarities	Belongs to the MAGUK family. Contains 1 guanylate kinase-like domain. Contains 1 L27 domain. Contains 3 PDZ (DHR) domains. Contains 1 SH3 domain.

Ontologies

Keywords
Cellular component	Cell junction Cell membrane Endoplasmic reticulum Membrane Postsynaptic cell membrane Synapse
Coding sequence diversity	Alternative splicing
Domain	Repeat SH3 domain
PTM	Phosphoprotein
Technical term	Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	T cell activation Inferred from mutant phenotype PubMed 15699074PubMed 17187070. Source: MGI T cell cytokine production Inferred from mutant phenotype PubMed 15699074. Source: MGI actin filament organization Inferred from sequence or structural similarity. Source: UniProtKB activation of protein kinase activity Inferred from mutant phenotype PubMed 17187070. Source: MGI amyloid precursor protein metabolic process Inferred from genetic interaction PubMed 17301176. Source: MGI branching involved in ureteric bud morphogenesis Inferred from mutant phenotype PubMed 16105026PubMed 17172448PubMed 17435047. Source: MGI cell-cell adhesion Inferred from sequence or structural similarity. Source: UniProtKB cortical actin cytoskeleton organization Inferred from sequence or structural similarity. Source: UniProtKB embryonic skeletal system morphogenesis Inferred from mutant phenotype Ref.6. Source: MGI endothelial cell proliferation Inferred from sequence or structural similarity. Source: UniProtKB hard palate development Inferred from mutant phenotype Ref.6PubMed 17435047. Source: MGI immunological synapse formation Inferred from mutant phenotype PubMed 15699074. Source: MGI lens development in camera-type eye Inferred from mutant phenotype PubMed 14645510. Source: MGI membrane raft organization Inferred from mutant phenotype PubMed 15699074. Source: MGI negative regulation of T cell proliferation Inferred from mutant phenotype PubMed 17724087. Source: MGI negative regulation of epithelial cell proliferation Inferred from mutant phenotype PubMed 14645510. Source: MGI negative regulation of mitotic cell cycle Inferred from sequence or structural similarity. Source: UniProtKB peristalsis Inferred from mutant phenotype PubMed 17172448. Source: MGI positive regulation of actin filament polymerization Inferred from mutant phenotype PubMed 15699074. Source: MGI positive regulation of cell proliferation Inferred from mutant phenotype PubMed 17435047. Source: MGI positive regulation of developmental growth Traceable author statement PubMed 12766944. Source: UniProtKB positive regulation of establishment of protein localization to plasma membrane Inferred from electronic annotation. Source: Compara positive regulation of multicellular organism growth Traceable author statement PubMed 12766944. Source: UniProtKB positive regulation of potassium ion transport Inferred from electronic annotation. Source: Compara protein localization Inferred from mutant phenotype PubMed 17301176. Source: MGI protein localization to plasma membrane Inferred from electronic annotation. Source: Compara regulation of membrane potential Inferred from genetic interaction Ref.7. Source: MGI reproductive structure development Inferred from mutant phenotype PubMed 17435047. Source: MGI smooth muscle tissue development Inferred from mutant phenotype PubMed 17172448. Source: MGI tight junction assembly Inferred from electronic annotation. Source: Compara
Cellular_component	Golgi apparatus Inferred from electronic annotation. Source: Compara MPP7-DLG1-LIN7 complex Inferred from electronic annotation. Source: Compara basolateral plasma membrane Inferred from sequence or structural similarity. Source: UniProtKB cell projection membrane Inferred from direct assay PubMed 16621792. Source: MGI cell-cell adherens junction Traceable author statement PubMed 12766944. Source: UniProtKB endoplasmic reticulum membrane Inferred from electronic annotation. Source: UniProtKB-SubCell immunological synapse Inferred from direct assay PubMed 15699074. Source: MGI internal side of plasma membrane Inferred from electronic annotation. Source: Compara lateral loop Inferred from direct assay PubMed 20237282. Source: BHF-UCL lateral plasma membrane Inferred from direct assay PubMed 16105026. Source: MGI membrane raft Inferred from direct assay PubMed 15699074. Source: MGI microtubule Inferred from electronic annotation. Source: Compara myelin sheath abaxonal region Inferred from direct assay PubMed 20237282. Source: BHF-UCL neuromuscular junction Inferred from direct assay PubMed 9674605. Source: MGI node of Ranvier Inferred from direct assay PubMed 20237282. Source: BHF-UCL nucleus Inferred from electronic annotation. Source: Compara perinuclear region of cytoplasm Inferred from electronic annotation. Source: Compara postsynaptic density Inferred from direct assay PubMed 17301176. Source: MGI postsynaptic membrane Inferred from electronic annotation. Source: UniProtKB-KW tight junction Inferred from electronic annotation. Source: Compara
Molecular_function	phosphatase binding Inferred from sequence or structural similarity. Source: UniProtKB protein complex scaffold Inferred from mutant phenotype PubMed 15699074. Source: MGI protein kinase binding Inferred from sequence or structural similarity. Source: UniProtKB
Complete GO annotation...

Binary interactions

With	Entry	#Exp.	IntAct	Notes
Dlg4	Q62108	3	EBI-514290,EBI-300895
Lrfn2	Q80TG9	3	EBI-514290,EBI-877092

Alternative products

This entry describes 3 isoforms produced by alternative splicing. [Align] [Select]

Isoform 1 (identifier: Q811D0-1)

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: Q811D0-2)

The sequence of this isoform differs from the canonical sequence as follows:
     162-194: Missing.
     670-681: EIPDDMGSKGLK → SFNDKRKKNLFSRKFPFYKNKDQSEQETSDADQ

Note: Contains a phosphoserine at position 665.

Isoform 3 (identifier: Q811D0-3)

The sequence of this isoform differs from the canonical sequence as follows:
     670-681: EIPDDMGSKGLK → QSFNDKRKKNLFSRKFPFYKNKDQSEQETSDADQ

Note: Contains a phosphoserine at position 699.

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 905	905	Disks large homolog 1		PRO_0000094549
Regions
	Domain	4 – 64	61	L27
	Domain	224 – 311	88	PDZ 1
	Domain	319 – 406	88	PDZ 2
	Domain	466 – 547	82	PDZ 3
	Domain	581 – 651	71	SH3
	Domain	715 – 890	176	Guanylate kinase-like
	Region	162 – 212	51	Interaction with SH3 domains By similarity
Amino acid modifications
	Modified residue	122	1	Phosphoserine By similarity
	Modified residue	158	1	Phosphoserine By similarity
	Modified residue	232	1	Phosphoserine By similarity
	Modified residue	301	1	Phosphoserine Ref.9
	Modified residue	399	1	Phosphotyrosine Ref.10
	Modified residue	568	1	Phosphoserine By similarity
	Modified residue	575	1	Phosphoserine By similarity
	Modified residue	619	1	Phosphoserine By similarity
	Modified residue	684	1	Phosphothreonine Ref.11
	Modified residue	685	1	Phosphoserine By similarity
	Modified residue	688	1	Phosphoserine Ref.12
Natural variations
	Alternative sequence	162 – 194	33	Missing in isoform 2.		VSP_012866
	Alternative sequence	670 – 681	12	EIPDD…SKGLK → SFNDKRKKNLFSRKFPFYKN KDQSEQETSDADQ in isoform 2.		VSP_012867
	Alternative sequence	670 – 681	12	EIPDD…SKGLK → QSFNDKRKKNLFSRKFPFYK NKDQSEQETSDADQ in isoform 3.		VSP_012868
Experimental info
	Sequence conflict	263	1	A → R in AAC31653. Ref.1
	Sequence conflict	276	1	I → V in AAC31653. Ref.1
	Sequence conflict	312	1	P → L in AAC31653. Ref.1
	Sequence conflict	337	1	V → I in AAC31653. Ref.1
	Sequence conflict	470	1	H → R in AAN87264. Ref.2
	Sequence conflict	482	1	G → A in AAC31653. Ref.1
	Sequence conflict	550 – 551	2	YS → SR in AAC31653. Ref.1
	Sequence conflict	568	1	S → R in AAC31653. Ref.1
	Sequence conflict	576	1	L → P in AAC31653. Ref.1
	Sequence conflict	647	1	V → A in AAC31653. Ref.1
	Sequence conflict	700	1	Y → C in AAC31653. Ref.1
	Sequence conflict	754	1	Y → I in AAC31653. Ref.1
	Sequence conflict	769 – 770	2	QM → RV in AAC31653. Ref.1
	Sequence conflict	900	1	P → L in AAC31653. Ref.1

Sequences

	Sequence		Length	Mass (Da)
	Isoform 1 [UniParc]. Last modified June 1, 2003. Version 1. Checksum: 950A465824AE3210	FASTA	905	100,120
	10 20 30 40 50 60 MPVRKQDTQR ALHLLEEYRS KLSQTEDRQL RSSIERVINI FQSNLFQALI DIQEFYEVTL 70 80 90 100 110 120 LDNPKCVDHS KQCEPVQPVT TWEIASLPST AVTSETLPGS LSPPVEKYRY QDEEVLPPEH 130 140 150 160 170 180 ISPQVTNEVL GPELVHVSEK NLSEIENVHG FVSHSHISPI KPTEAVPPSS PIVPVTPALP 190 200 210 220 230 240 VPAESTVVLP SAPQANPPPV LVNTDSLETP TYVNGTDADY EYEEITLERG NSGLGFSIAG 250 260 270 280 290 300 GTDNPHIGDD SSIFITKIIT GGAAAQDGRL RVNDCILRVN EADVRDVTHS KAVEALKEAG 310 320 330 340 350 360 SIVRLYVKRR KPASEKIMEI KLIKGPKGLG FSIAGGVGNQ HIPGDNSIYV TKIIEGGAAH 370 380 390 400 410 420 KDGKLQIGDK LLAVNSVCLE EVTHEEAVTA LKNTSDFVYL KVAKPTSMYI NDGYAPPDIT 430 440 450 460 470 480 NSSSQSVDNH VSPSSCLGQT PTSPARYSPI SKAVLGDDEI TREPRKVVLH RGSTGLGFNI 490 500 510 520 530 540 VGGEDGEGIF ISFILAGGPA DLSGELRKGD RIISVNSVDL RAASHEQAAA ALKNAGQAVT 550 560 570 580 590 600 IVAQYRPEEY SRFEAKIHDL REQMMNSSVS SGSGSLRTSQ KRSLYVRALF DYDKTKDSGL 610 620 630 640 650 660 PSQGLNFRFG DILHVINASD DEWWQARQVT PDGESDEVGV IPSKRRVEKK ERARLKTVKF 670 680 690 700 710 720 NSKTRGDKGE IPDDMGSKGL KHVTSNASDS ESSYRGQEEY VLSYEPVNQQ EVNYTRPVII 730 740 750 760 770 780 LGPMKDRVND DLISEFPDKF GSCVPHTTRP KRDYEVDGRD YHFVTSREQM EKDIQEHKFI 790 800 810 820 830 840 EAGQYNNHLY GTSVQSVRAV AEKGKHCILD VSGNAIKRLQ IAQLYPISIF IKPKSMENIM 850 860 870 880 890 900 EMNKRLTEEQ ARKTFERAMK LEQEFTEHFT AIVQGDTLED IYNQVKQIIE EQSGPYIWVP AKEKL
	Isoform 2 [UniParc]. Checksum: 085DFCCCC2067FEB	FASTA	893	99,630
	10 20 30 40 50 60 MPVRKQDTQR ALHLLEEYRS KLSQTEDRQL RSSIERVINI FQSNLFQALI DIQEFYEVTL 70 80 90 100 110 120 LDNPKCVDHS KQCEPVQPVT TWEIASLPST AVTSETLPGS LSPPVEKYRY QDEEVLPPEH 130 140 150 160 170 180 ISPQVTNEVL GPELVHVSEK NLSEIENVHG FVSHSHISPI KANPPPVLVN TDSLETPTYV 190 200 210 220 230 240 NGTDADYEYE EITLERGNSG LGFSIAGGTD NPHIGDDSSI FITKIITGGA AAQDGRLRVN 250 260 270 280 290 300 DCILRVNEAD VRDVTHSKAV EALKEAGSIV RLYVKRRKPA SEKIMEIKLI KGPKGLGFSI 310 320 330 340 350 360 AGGVGNQHIP GDNSIYVTKI IEGGAAHKDG KLQIGDKLLA VNSVCLEEVT HEEAVTALKN 370 380 390 400 410 420 TSDFVYLKVA KPTSMYINDG YAPPDITNSS SQSVDNHVSP SSCLGQTPTS PARYSPISKA 430 440 450 460 470 480 VLGDDEITRE PRKVVLHRGS TGLGFNIVGG EDGEGIFISF ILAGGPADLS GELRKGDRII 490 500 510 520 530 540 SVNSVDLRAA SHEQAAAALK NAGQAVTIVA QYRPEEYSRF EAKIHDLREQ MMNSSVSSGS 550 560 570 580 590 600 GSLRTSQKRS LYVRALFDYD KTKDSGLPSQ GLNFRFGDIL HVINASDDEW WQARQVTPDG 610 620 630 640 650 660 ESDEVGVIPS KRRVEKKERA RLKTVKFNSK TRGDKGSFND KRKKNLFSRK FPFYKNKDQS 670 680 690 700 710 720 EQETSDADQH VTSNASDSES SYRGQEEYVL SYEPVNQQEV NYTRPVIILG PMKDRVNDDL 730 740 750 760 770 780 ISEFPDKFGS CVPHTTRPKR DYEVDGRDYH FVTSREQMEK DIQEHKFIEA GQYNNHLYGT 790 800 810 820 830 840 SVQSVRAVAE KGKHCILDVS GNAIKRLQIA QLYPISIFIK PKSMENIMEM NKRLTEEQAR 850 860 870 880 890 KTFERAMKLE QEFTEHFTAI VQGDTLEDIY NQVKQIIEEQ SGPYIWVPAK EKL
	Isoform 3 [UniParc]. Checksum: 885671B7DACA7CD3	FASTA	927	102,986
	10 20 30 40 50 60 MPVRKQDTQR ALHLLEEYRS KLSQTEDRQL RSSIERVINI FQSNLFQALI DIQEFYEVTL 70 80 90 100 110 120 LDNPKCVDHS KQCEPVQPVT TWEIASLPST AVTSETLPGS LSPPVEKYRY QDEEVLPPEH 130 140 150 160 170 180 ISPQVTNEVL GPELVHVSEK NLSEIENVHG FVSHSHISPI KPTEAVPPSS PIVPVTPALP 190 200 210 220 230 240 VPAESTVVLP SAPQANPPPV LVNTDSLETP TYVNGTDADY EYEEITLERG NSGLGFSIAG 250 260 270 280 290 300 GTDNPHIGDD SSIFITKIIT GGAAAQDGRL RVNDCILRVN EADVRDVTHS KAVEALKEAG 310 320 330 340 350 360 SIVRLYVKRR KPASEKIMEI KLIKGPKGLG FSIAGGVGNQ HIPGDNSIYV TKIIEGGAAH 370 380 390 400 410 420 KDGKLQIGDK LLAVNSVCLE EVTHEEAVTA LKNTSDFVYL KVAKPTSMYI NDGYAPPDIT 430 440 450 460 470 480 NSSSQSVDNH VSPSSCLGQT PTSPARYSPI SKAVLGDDEI TREPRKVVLH RGSTGLGFNI 490 500 510 520 530 540 VGGEDGEGIF ISFILAGGPA DLSGELRKGD RIISVNSVDL RAASHEQAAA ALKNAGQAVT 550 560 570 580 590 600 IVAQYRPEEY SRFEAKIHDL REQMMNSSVS SGSGSLRTSQ KRSLYVRALF DYDKTKDSGL 610 620 630 640 650 660 PSQGLNFRFG DILHVINASD DEWWQARQVT PDGESDEVGV IPSKRRVEKK ERARLKTVKF 670 680 690 700 710 720 NSKTRGDKGQ SFNDKRKKNL FSRKFPFYKN KDQSEQETSD ADQHVTSNAS DSESSYRGQE 730 740 750 760 770 780 EYVLSYEPVN QQEVNYTRPV IILGPMKDRV NDDLISEFPD KFGSCVPHTT RPKRDYEVDG 790 800 810 820 830 840 RDYHFVTSRE QMEKDIQEHK FIEAGQYNNH LYGTSVQSVR AVAEKGKHCI LDVSGNAIKR 850 860 870 880 890 900 LQIAQLYPIS IFIKPKSMEN IMEMNKRLTE EQARKTFERA MKLEQEFTEH FTAIVQGDTL 910 920 EDIYNQVKQI IEEQSGPYIW VPAKEKL

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Identification of the mouse homologue of human discs large and rat SAP97 genes." Lin L., Sahr K.E., Chishti A.H. Biochim. Biophys. Acta 1362:1-5(1997) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 3). Tissue: Bone marrow.
[2]	"Cloning and characterization of a novel mouse homolog E-dlg/SAP97 of the Drosophila discs large tumor suppressor binds to SAP102." Mao P., Tao Y.-X., Levine C., Tao F., Li D., Johns R.A. Submitted (OCT-2002) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2). Strain: C57BL/6J.
[3]	"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] (ISOFORMS 1 AND 3). Strain: C57BL/6. Tissue: Brain and Colon.
[4]	"Two independent domains of hDlg are sufficient for subcellular targeting: the PDZ1-2 conformational unit and an alternatively spliced domain." Lue R.A., Brandin E., Chan E.P., Branton D. J. Cell Biol. 135:1125-1137(1996) [PubMed] [Europe PMC] [Abstract] Cited for: INTERACTION WITH EZR.
[5]	"Binding of APC to the human homolog of the Drosophila discs large tumor suppressor protein." Matsumine A., Ogai A., Senda T., Okumura N., Satoh K., Baeg G.-H., Kawahara T., Kobayashi S., Okada M., Toyoshima K., Akiyama T. Science 272:1020-1023(1996) [PubMed] [Europe PMC] [Abstract] Cited for: INTERACTION WITH APC AND CTNNB1.
[6]	"Craniofacial dysmorphogenesis including cleft palate in mice with an insertional mutation in the discs large gene." Caruana G., Bernstein A. Mol. Cell. Biol. 21:1475-1483(2001) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION, TISSUE SPECIFICITY, DISRUPTION PHENOTYPE.
[7]	"Caveolin-3 and SAP97 form a scaffolding protein complex that regulates the voltage-gated potassium channel Kv1.5." Folco E.J., Liu G.-X., Koren G. Am. J. Physiol. 287:H681-H690(2004) [PubMed] [Europe PMC] [Abstract] Cited for: INTERACTION WITH KCNA5 AND CAV3.
[8]	"The serotonin 5-HT2A and 5-HT2C receptors interact with specific sets of PDZ proteins." Becamel C., Gavarini S., Chanrion B., Alonso G., Galeotti N., Dumuis A., Bockaert J., Marin P. J. Biol. Chem. 279:20257-20266(2004) [PubMed] [Europe PMC] [Abstract] Cited for: INTERACTION WITH HTR2A.
[9]	"Comprehensive identification of phosphorylation sites in postsynaptic density preparations." Trinidad J.C., Specht C.G., Thalhammer A., Schoepfer R., Burlingame A.L. Mol. Cell. Proteomics 5:914-922(2006) [PubMed] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-301, MASS SPECTROMETRY. Tissue: Brain.
[10]	"Large-scale identification and evolution indexing of tyrosine phosphorylation sites from murine brain." Ballif B.A., Carey G.R., Sunyaev S.R., Gygi S.P. J. Proteome Res. 7:311-318(2008) [PubMed] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-399, MASS SPECTROMETRY. Tissue: Brain.
[11]	"Large-scale phosphorylation analysis of mouse liver." Villen J., Beausoleil S.A., Gerber S.A., Gygi S.P. Proc. Natl. Acad. Sci. U.S.A. 104:1488-1493(2007) [PubMed] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-684, PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-665 (ISOFORM 2), MASS SPECTROMETRY. Tissue: Liver.
[12]	"Solid tumor proteome and phosphoproteome analysis by high resolution mass spectrometry." Zanivan S., Gnad F., Wickstroem S.A., Geiger T., Macek B., Cox J., Faessler R., Mann M. J. Proteome Res. 7:5314-5326(2008) [PubMed] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-688, MASS SPECTROMETRY. Tissue: Melanoma.
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBL GenBank DDBJ	U93309 mRNA. Translation: AAC31653.1. AY159380 mRNA. Translation: AAN87264.1. BC047142 mRNA. Translation: AAH47142.1. BC057118 mRNA. Translation: AAH57118.1.
IPI	IPI00125861. IPI00408668. IPI00553807.
RefSeq	NP_001239362.1. NM_001252433.1. NP_001239363.1. NM_001252434.1. NP_001239364.1. NM_001252435.1. NP_031888.2. NM_007862.3.
UniGene	Mm.382.
3D structure databases
ProteinModelPortal	Q811D0.
SMR	Q811D0. Positions 2-65, 221-902.
ModBase	Search...
Protein-protein interaction databases
IntAct	Q811D0. 6 interactions.
MINT	MINT-136497.
PTM databases
PhosphoSite	Q811D0.
Proteomic databases
PaxDb	Q811D0.
PRIDE	Q811D0.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
Ensembl	ENSMUST00000064477; ENSMUSP00000064280; ENSMUSG00000022770. ENSMUST00000100001; ENSMUSP00000097581; ENSMUSG00000022770. ENSMUST00000115205; ENSMUSP00000110859; ENSMUSG00000022770.
GeneID	13383.
KEGG	mmu:13383.
UCSC	uc007yxo.1. mouse. uc007yxp.1. mouse. uc007yxs.1. mouse.
Organism-specific databases
CTD	1739.
MGI	MGI:107231. Dlg1.
Phylogenomic databases
eggNOG	COG0194.
GeneTree	ENSGT00660000095130.
HOGENOM	HOG000232102.
HOVERGEN	HBG107814.
KO	K12076.
OrthoDB	EOG447FSN.
Enzyme and pathway databases
Reactome	REACT_127416. Developmental Biology.
Gene expression databases
ArrayExpress	Q811D0.
Bgee	Q811D0.
CleanEx	MM_DLG1.
Genevestigator	Q811D0.
GermOnline	ENSMUSG00000022770. Mus musculus.
Family and domain databases
InterPro	IPR008144. Guanylate_kin. IPR008145. Guanylate_kin/L-typ_Ca_channel. IPR020590. Guanylate_kinase_CS. IPR004172. L27. IPR015143. L27_1. IPR016313. M-assoc_guanylate_kinase. IPR019590. MAGUK_PEST_N. IPR001478. PDZ. IPR019583. PDZ_assoc. IPR011511. SH3_2. IPR001452. SH3_domain. [Graphical view]
Pfam	PF00625. Guanylate_kin. 1 hit. PF09058. L27_1. 1 hit. PF10608. MAGUK_N_PEST. 1 hit. PF00595. PDZ. 3 hits. PF10600. PDZ_assoc. 1 hit. PF07653. SH3_2. 1 hit. [Graphical view]
PIRSF	PIRSF001741. MAGUK_DLGH. 1 hit.
SMART	SM00072. GuKc. 1 hit. SM00569. L27. 1 hit. SM00228. PDZ. 3 hits. SM00326. SH3. 1 hit. [Graphical view]
SUPFAM	SSF50156. PDZ. 3 hits. SSF50044. SH3. 1 hit.
PROSITE	PS00856. GUANYLATE_KINASE_1. 1 hit. PS50052. GUANYLATE_KINASE_2. 1 hit. PS51022. L27. 1 hit. PS50106. PDZ. 3 hits. PS50002. SH3. 1 hit. [Graphical view]
ProtoNet	Search...
Other
ChiTaRS	dlg1. mouse.
NextBio	283732.
SOURCE	Search...

Entry information

Entry name

DLG1_MOUSE

Accession

Primary (citable) accession number: Q811D0
Secondary accession number(s): Q62402, Q6PGB5, Q8CGN7

Entry history

Integrated into UniProtKB/Swiss-Prot:	February 15, 2005
Last sequence update:	June 1, 2003
Last modified:	April 3, 2013
This is version 114 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program