Q12959 (DLG1_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Disks large homolog 1

Alternative name(s):
Synapse-associated protein 97
Short name=SAP-97
Short name=SAP97
hDlg

Gene names

Name:

DLG1

Organism

Homo sapiens (Human)

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Primates › Haplorrhini › Catarrhini › Hominidae › Homo

Protein attributes

Sequence length	904 AA.
Sequence status	Complete.
Protein existence	Evidence at protein level

General annotation (Comments)

Function	Essential multidomain scaffolding protein required for normal development By similarity. Recruits channels, receptors and signaling molecules to discrete plasma membrane domains in polarized cells. May play a role in adherens junction assembly, signal transduction, cell proliferation, synaptogenesis and lymphocyte activation. Regulates the excitability of cardiac myocytes by modulating the functional expression of Kv4 channels. Functional regulator of Kv1.5 channel. Ref.11 Ref.14 Ref.17 Ref.18 Ref.30 Ref.32
Subunit structure	Homotetramer Probable. Interacts through its guanylate kinase-like domain with DLGAP1, DLGAP2, DLGAP3, DLGAP4 and MAP1A. May interact with HTR2A By similarity. Interacts with LRFN1 By similarity. Interacts through its PDZ domains with GRIN2A, KCNA1, KCNA2, KCNA3, KCNA4, KCNA5, KCND2, KCND3, GRIA1, GPR124 and GPR125. Interacts with KCNF1. Interacts with CAMK2 (by similarity). 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 KIF13B. Forms a tripartite complex composed of DLG1, MPP7 and LIN7 (LIN7A or LIN7C). May interact with TJAP1. Interacts with TOPK and the HTLV-1 viral Tax and HPV-18 E6 papillomavirus (HPV) oncoproteins. Interacts with PTEN By similarity. Interacts with FRMPD4 (via C-terminus). Interacts with LRFN1, LRFN2, LRFN4 and SFPQ. Ref.1 Ref.5 Ref.6 Ref.7 Ref.8 Ref.9 Ref.10 Ref.11 Ref.12 Ref.13 Ref.14 Ref.17 Ref.19 Ref.22 Ref.24 Ref.25 Ref.27 Ref.30 Ref.32
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. Cell membrane › sarcolemma. 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. Ref.1 Ref.6 Ref.10 Ref.14 Ref.15 Ref.16
Tissue specificity	Abundantly expressed in atrial myocardium (at protein level). Expressed in lung fibroblasts, cervical epithelial and B-cells (at protein level). Widely expressed, with isoforms displaying different expression profiles. Ref.1 Ref.14 Ref.30
Domain	The alternatively spliced domain I3 corresponding to amino acids (636-669) of isoform 4 is an EPB41 binding site mediating association to membranes in polarized and non-polarized cells. 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. 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.
Post-translational modification	Phosphorylated by MAPK12. Phosphorylation of Ser-232 regulates association with GRIN2A. Isoform 2 is phosphorylated on Ser-698. Isoform 3 is phosphorylated on Ser-665 By similarity. Ref.21 Ref.23 Ref.26 Ref.28 Ref.29 Ref.31 Ref.32
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
Biological process	Host-virus interaction
Cellular component	Cell junction Cell membrane Endoplasmic reticulum Membrane Postsynaptic cell membrane Synapse
Coding sequence diversity	Alternative splicing Polymorphism
Domain	Repeat SH3 domain
PTM	Phosphoprotein
Technical term	3D-structure Complete proteome Reference proteome
Gene Ontology (GO)
Biological process	actin filament organization Inferred from direct assay Ref.17. Source: UniProtKB axon guidance Traceable author statement. Source: Reactome cell-cell adhesion Inferred from direct assay Ref.17. Source: UniProtKB cortical actin cytoskeleton organization Inferred from direct assay Ref.17. Source: UniProtKB endothelial cell proliferation Inferred from direct assay Ref.17. Source: UniProtKB establishment or maintenance of cell polarity Traceable author statement Ref.20. Source: UniProtKB interspecies interaction between organisms Inferred from electronic annotation. Source: UniProtKB-KW mitotic cell cycle G1/S transition checkpoint Non-traceable author statement Ref.11. Source: UniProtKB negative regulation of mitotic cell cycle Inferred from mutant phenotype Ref.11. Source: UniProtKB protein localization in plasma membrane Inferred from mutant phenotype Ref.25. Source: BHF-UCL synaptic transmission Traceable author statement. Source: Reactome tight junction assembly Inferred from direct assay Ref.25. Source: BHF-UCL
Cellular component	MPP7-DLG1-LIN7 complex Inferred from direct assay Ref.24. Source: BHF-UCL basolateral plasma membrane Inferred from direct assay Ref.6. Source: UniProtKB cytosol Traceable author statement. Source: Reactome endoplasmic reticulum membrane Inferred from electronic annotation. Source: UniProtKB-SubCell immunological synapse Traceable author statement. Source: BHF-UCL nucleus Inferred from direct assay Ref.24. Source: BHF-UCL postsynaptic density Inferred from electronic annotation. Source: UniProtKB-SubCell postsynaptic membrane Inferred from electronic annotation. Source: UniProtKB-KW sarcolemma Inferred from electronic annotation. Source: UniProtKB-SubCell tight junction Inferred from direct assay Ref.25. Source: BHF-UCL
Molecular function	L27 domain binding Inferred from physical interaction Ref.25. Source: BHF-UCL cytoskeletal protein binding Traceable author statement. Source: ProtInc guanylate kinase activity Traceable author statement. Source: ProtInc phosphatase binding Inferred from physical interaction. Source: UniProtKB phosphoprotein phosphatase activity Traceable author statement Ref.21. Source: UniProtKB potassium channel regulator activity Non-traceable author statement Ref.12. Source: UniProtKB protein C-terminus binding Inferred from physical interaction. Source: UniProtKB protein binding Inferred from physical interaction Ref.10. Source: IntAct protein kinase binding Inferred from physical interaction Ref.12Ref.17. Source: UniProtKB
Complete GO annotation...

Binary interactions

With	Entry	#Exp.	IntAct	Notes
KIF13B	Q9NQT8	3	EBI-357500,EBI-766408
KIF1B	O60333-3	4	EBI-357481,EBI-465669

Alternative products

This entry describes 7 isoforms produced by alternative splicing. [Align] [Select]

Isoform 1 (identifier: Q12959-1)

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: Q12959-2)

The sequence of this isoform differs from the canonical sequence as follows:
     669-680: EIPDDMGSKGLK → QSFNDKRKKNLFSRKFPFYKNKDQSEQETSDADQ

Note: Phosphorylated on Ser-698 (By similarity).

Isoform 3 (identifier: Q12959-3)

The sequence of this isoform differs from the canonical sequence as follows:
     162-194: Missing.

Isoform 4 (identifier: Q12959-4)

The sequence of this isoform differs from the canonical sequence as follows:
     162-194: Missing.
     669-680: EIPDDMGSKGLK → QSFNDKRKKNLFSRKFPFYKNKDQSEQETSDADQ

Note: Phosphorylated on Ser-665 (By similarity). Ref.4 (AAI44652) sequence is in conflict in position: 636:Q->Missing.

Isoform 5 (identifier: Q12959-5)

The sequence of this isoform differs from the canonical sequence as follows:
     162-194: Missing.
     195-212: Missing.

Isoform 6 (identifier: Q12959-6)

The sequence of this isoform differs from the canonical sequence as follows:
     681-693: Missing.

Isoform 7 (identifier: Q12959-7)

The sequence of this isoform differs from the canonical sequence as follows:
     693-693: Y → YLILITDEYGCSKG

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 904

904

Disks large homolog 1

PRO_0000094548

Regions

Domain

4 – 64

61

L27

Domain

224 – 310

87

PDZ 1

Domain

319 – 405

87

PDZ 2

Domain

466 – 546

81

PDZ 3

Domain

581 – 651

71

SH3

Domain

714 – 889

176

Guanylate kinase-like

Region

162 – 212

51

Interaction with SH3 domains

Amino acid modifications

Modified residue

115

1

Phosphothreonine Ref.29

Modified residue

122

1

Phosphoserine Ref.29

Modified residue

232

1

Phosphoserine By similarity

Modified residue

301

1

Phosphoserine By similarity

Modified residue

399

1

Phosphotyrosine By similarity

Modified residue

575

1

Phosphoserine Ref.29 Ref.31

Modified residue

619

1

Phosphoserine Ref.28

Modified residue

683

1

Phosphothreonine By similarity

Modified residue

684

1

Phosphoserine Ref.21 Ref.29

Modified residue

687

1

Phosphoserine Ref.21 Ref.29

Modified residue

760

1

Phosphotyrosine Ref.23 Ref.26

Natural variations

Alternative sequence

162 – 194

33

Missing in isoform 3, isoform 4 and isoform 5.

VSP_012862

Alternative sequence

195 – 212

18

Missing in isoform 5.

VSP_012863

Alternative sequence

669 – 680

12

EIPDD…SKGLK → QSFNDKRKKNLFSRKFPFYK NKDQSEQETSDADQ in isoform 2 and isoform 4.

VSP_003150

Alternative sequence

681 – 693

13

Missing in isoform 6.

VSP_012864

Alternative sequence

693

1

Y → YLILITDEYGCSKG in isoform 7.

VSP_012865

Natural variant

140

1

K → R.
Corresponds to variant rs1802668 [ dbSNP | Ensembl ].

VAR_054334

Natural variant

278

1

R → Q. Ref.1
Corresponds to variant rs1134986 [ dbSNP | Ensembl ].

VAR_054335

Natural variant

899

1

P → L.
Corresponds to variant rs34492126 [ dbSNP | Ensembl ].

VAR_054336

Experimental info

Mutagenesis

38 – 40

3

INI → ANA: Loss of membrane association and DLG2-binding. Ref.16

Sequence conflict

801

1

E → G in AAA50598. Ref.1

Sequence conflict

801

1

E → G in AAA50599. Ref.1

Secondary structure

1

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904

Helix Strand Turn

Details...

Beta strand

319 – 323

5

Beta strand

331 – 334

4

Beta strand

347 – 349

3

Helix

358 – 362

5

Beta strand

370 – 374

5

Beta strand

377 – 382

6

Helix

384 – 392

9

Beta strand

395 – 403

9

Beta strand

465 – 470

6

Beta strand

472 – 474

3

Beta strand

477 – 482

6

Beta strand

484 – 487

4

Beta strand

489 – 494

6

Helix

499 – 503

5

Beta strand

510 – 515

6

Helix

525 – 533

9

Beta strand

537 – 545

9

Helix

547 – 552

6

Sequences

	Sequence		Length	Mass (Da)
	Isoform 1 [UniParc]. Last modified February 10, 2009. Version 2. Checksum: 6722993A84D0F761	FASTA	904	100,455
	10 20 30 40 50 60 MPVRKQDTQR ALHLLEEYRS KLSQTEDRQL RSSIERVINI FQSNLFQALI DIQEFYEVTL 70 80 90 100 110 120 LDNPKCIDRS KPSEPIQPVN TWEISSLPSS TVTSETLPSS LSPSVEKYRY QDEDTPPQEH 130 140 150 160 170 180 ISPQITNEVI GPELVHVSEK NLSEIENVHG FVSHSHISPI KPTEAVLPSP PTVPVIPVLP 190 200 210 220 230 240 VPAENTVILP TIPQANPPPV LVNTDSLETP TYVNGTDADY EYEEITLERG NSGLGFSIAG 250 260 270 280 290 300 GTDNPHIGDD SSIFITKIIT GGAAAQDGRL RVNDCILRVN EVDVRDVTHS KAVEALKEAG 310 320 330 340 350 360 SIVRLYVKRR KPVSEKIMEI KLIKGPKGLG FSIAGGVGNQ HIPGDNSIYV TKIIEGGAAH 370 380 390 400 410 420 KDGKLQIGDK LLAVNNVCLE EVTHEEAVTA LKNTSDFVYL KVAKPTSMYM NDGYAPPDIT 430 440 450 460 470 480 NSSSQPVDNH VSPSSFLGQT PASPARYSPV SKAVLGDDEI TREPRKVVLH RGSTGLGFNI 490 500 510 520 530 540 VGGEDGEGIF ISFILAGGPA DLSGELRKGD RIISVNSVDL RAASHEQAAA ALKNAGQAVT 550 560 570 580 590 600 IVAQYRPEEY SRFEAKIHDL REQMMNSSIS SGSGSLRTSQ KRSLYVRALF DYDKTKDSGL 610 620 630 640 650 660 PSQGLNFKFG DILHVINASD DEWWQARQVT PDGESDEVGV IPSKRRVEKK ERARLKTVKF 670 680 690 700 710 720 NSKTRDKGEI PDDMGSKGLK HVTSNASDSE SSYRGQEEYV LSYEPVNQQE VNYTRPVIIL 730 740 750 760 770 780 GPMKDRINDD LISEFPDKFG SCVPHTTRPK RDYEVDGRDY HFVTSREQME KDIQEHKFIE 790 800 810 820 830 840 AGQYNNHLYG TSVQSVREVA EKGKHCILDV SGNAIKRLQI AQLYPISIFI KPKSMENIME 850 860 870 880 890 900 MNKRLTEEQA RKTFERAMKL EQEFTEHFTA IVQGDTLEDI YNQVKQIIEE QSGSYIWVPA KEKL
	Isoform 2 [UniParc]. Checksum: 85BD4E93A17D74C4	FASTA	926	103,321
	10 20 30 40 50 60 MPVRKQDTQR ALHLLEEYRS KLSQTEDRQL RSSIERVINI FQSNLFQALI DIQEFYEVTL 70 80 90 100 110 120 LDNPKCIDRS KPSEPIQPVN TWEISSLPSS TVTSETLPSS LSPSVEKYRY QDEDTPPQEH 130 140 150 160 170 180 ISPQITNEVI GPELVHVSEK NLSEIENVHG FVSHSHISPI KPTEAVLPSP PTVPVIPVLP 190 200 210 220 230 240 VPAENTVILP TIPQANPPPV LVNTDSLETP TYVNGTDADY EYEEITLERG NSGLGFSIAG 250 260 270 280 290 300 GTDNPHIGDD SSIFITKIIT GGAAAQDGRL RVNDCILRVN EVDVRDVTHS KAVEALKEAG 310 320 330 340 350 360 SIVRLYVKRR KPVSEKIMEI KLIKGPKGLG FSIAGGVGNQ HIPGDNSIYV TKIIEGGAAH 370 380 390 400 410 420 KDGKLQIGDK LLAVNNVCLE EVTHEEAVTA LKNTSDFVYL KVAKPTSMYM NDGYAPPDIT 430 440 450 460 470 480 NSSSQPVDNH VSPSSFLGQT PASPARYSPV SKAVLGDDEI TREPRKVVLH RGSTGLGFNI 490 500 510 520 530 540 VGGEDGEGIF ISFILAGGPA DLSGELRKGD RIISVNSVDL RAASHEQAAA ALKNAGQAVT 550 560 570 580 590 600 IVAQYRPEEY SRFEAKIHDL REQMMNSSIS SGSGSLRTSQ KRSLYVRALF DYDKTKDSGL 610 620 630 640 650 660 PSQGLNFKFG DILHVINASD DEWWQARQVT PDGESDEVGV IPSKRRVEKK ERARLKTVKF 670 680 690 700 710 720 NSKTRDKGQS FNDKRKKNLF SRKFPFYKNK DQSEQETSDA DQHVTSNASD SESSYRGQEE 730 740 750 760 770 780 YVLSYEPVNQ QEVNYTRPVI ILGPMKDRIN DDLISEFPDK FGSCVPHTTR PKRDYEVDGR 790 800 810 820 830 840 DYHFVTSREQ MEKDIQEHKF IEAGQYNNHL YGTSVQSVRE VAEKGKHCIL DVSGNAIKRL 850 860 870 880 890 900 QIAQLYPISI FIKPKSMENI MEMNKRLTEE QARKTFERAM KLEQEFTEHF TAIVQGDTLE 910 920 DIYNQVKQII EEQSGSYIWV PAKEKL
	Isoform 3 [UniParc]. Checksum: 78CB64FC6DE66BB1	FASTA	871	97,076
	10 20 30 40 50 60 MPVRKQDTQR ALHLLEEYRS KLSQTEDRQL RSSIERVINI FQSNLFQALI DIQEFYEVTL 70 80 90 100 110 120 LDNPKCIDRS KPSEPIQPVN TWEISSLPSS TVTSETLPSS LSPSVEKYRY QDEDTPPQEH 130 140 150 160 170 180 ISPQITNEVI GPELVHVSEK NLSEIENVHG FVSHSHISPI KANPPPVLVN TDSLETPTYV 190 200 210 220 230 240 NGTDADYEYE EITLERGNSG LGFSIAGGTD NPHIGDDSSI FITKIITGGA AAQDGRLRVN 250 260 270 280 290 300 DCILRVNEVD VRDVTHSKAV EALKEAGSIV RLYVKRRKPV SEKIMEIKLI KGPKGLGFSI 310 320 330 340 350 360 AGGVGNQHIP GDNSIYVTKI IEGGAAHKDG KLQIGDKLLA VNNVCLEEVT HEEAVTALKN 370 380 390 400 410 420 TSDFVYLKVA KPTSMYMNDG YAPPDITNSS SQPVDNHVSP SSFLGQTPAS PARYSPVSKA 430 440 450 460 470 480 VLGDDEITRE PRKVVLHRGS TGLGFNIVGG EDGEGIFISF ILAGGPADLS GELRKGDRII 490 500 510 520 530 540 SVNSVDLRAA SHEQAAAALK NAGQAVTIVA QYRPEEYSRF EAKIHDLREQ MMNSSISSGS 550 560 570 580 590 600 GSLRTSQKRS LYVRALFDYD KTKDSGLPSQ GLNFKFGDIL HVINASDDEW WQARQVTPDG 610 620 630 640 650 660 ESDEVGVIPS KRRVEKKERA RLKTVKFNSK TRDKGEIPDD MGSKGLKHVT SNASDSESSY 670 680 690 700 710 720 RGQEEYVLSY EPVNQQEVNY TRPVIILGPM KDRINDDLIS EFPDKFGSCV PHTTRPKRDY 730 740 750 760 770 780 EVDGRDYHFV TSREQMEKDI QEHKFIEAGQ YNNHLYGTSV QSVREVAEKG KHCILDVSGN 790 800 810 820 830 840 AIKRLQIAQL YPISIFIKPK SMENIMEMNK RLTEEQARKT FERAMKLEQE FTEHFTAIVQ 850 860 870 GDTLEDIYNQ VKQIIEEQSG SYIWVPAKEK L
	Isoform 4 [UniParc]. Checksum: 3A026E9BAA62FFB7	FASTA	893	99,942
	10 20 30 40 50 60 MPVRKQDTQR ALHLLEEYRS KLSQTEDRQL RSSIERVINI FQSNLFQALI DIQEFYEVTL 70 80 90 100 110 120 LDNPKCIDRS KPSEPIQPVN TWEISSLPSS TVTSETLPSS LSPSVEKYRY QDEDTPPQEH 130 140 150 160 170 180 ISPQITNEVI GPELVHVSEK NLSEIENVHG FVSHSHISPI KANPPPVLVN TDSLETPTYV 190 200 210 220 230 240 NGTDADYEYE EITLERGNSG LGFSIAGGTD NPHIGDDSSI FITKIITGGA AAQDGRLRVN 250 260 270 280 290 300 DCILRVNEVD VRDVTHSKAV EALKEAGSIV RLYVKRRKPV SEKIMEIKLI KGPKGLGFSI 310 320 330 340 350 360 AGGVGNQHIP GDNSIYVTKI IEGGAAHKDG KLQIGDKLLA VNNVCLEEVT HEEAVTALKN 370 380 390 400 410 420 TSDFVYLKVA KPTSMYMNDG YAPPDITNSS SQPVDNHVSP SSFLGQTPAS PARYSPVSKA 430 440 450 460 470 480 VLGDDEITRE PRKVVLHRGS TGLGFNIVGG EDGEGIFISF ILAGGPADLS GELRKGDRII 490 500 510 520 530 540 SVNSVDLRAA SHEQAAAALK NAGQAVTIVA QYRPEEYSRF EAKIHDLREQ MMNSSISSGS 550 560 570 580 590 600 GSLRTSQKRS LYVRALFDYD KTKDSGLPSQ GLNFKFGDIL HVINASDDEW WQARQVTPDG 610 620 630 640 650 660 ESDEVGVIPS KRRVEKKERA RLKTVKFNSK TRDKGQSFND KRKKNLFSRK FPFYKNKDQS 670 680 690 700 710 720 EQETSDADQH VTSNASDSES SYRGQEEYVL SYEPVNQQEV NYTRPVIILG PMKDRINDDL 730 740 750 760 770 780 ISEFPDKFGS CVPHTTRPKR DYEVDGRDYH FVTSREQMEK DIQEHKFIEA GQYNNHLYGT 790 800 810 820 830 840 SVQSVREVAE KGKHCILDVS GNAIKRLQIA QLYPISIFIK PKSMENIMEM NKRLTEEQAR 850 860 870 880 890 KTFERAMKLE QEFTEHFTAI VQGDTLEDIY NQVKQIIEEQ SGSYIWVPAK EKL
	Isoform 5 [UniParc]. Checksum: 2E7EE3F5954BA3E0	FASTA	853	95,166
	10 20 30 40 50 60 MPVRKQDTQR ALHLLEEYRS KLSQTEDRQL RSSIERVINI FQSNLFQALI DIQEFYEVTL 70 80 90 100 110 120 LDNPKCIDRS KPSEPIQPVN TWEISSLPSS TVTSETLPSS LSPSVEKYRY QDEDTPPQEH 130 140 150 160 170 180 ISPQITNEVI GPELVHVSEK NLSEIENVHG FVSHSHISPI KVNGTDADYE YEEITLERGN 190 200 210 220 230 240 SGLGFSIAGG TDNPHIGDDS SIFITKIITG GAAAQDGRLR VNDCILRVNE VDVRDVTHSK 250 260 270 280 290 300 AVEALKEAGS IVRLYVKRRK PVSEKIMEIK LIKGPKGLGF SIAGGVGNQH IPGDNSIYVT 310 320 330 340 350 360 KIIEGGAAHK DGKLQIGDKL LAVNNVCLEE VTHEEAVTAL KNTSDFVYLK VAKPTSMYMN 370 380 390 400 410 420 DGYAPPDITN SSSQPVDNHV SPSSFLGQTP ASPARYSPVS KAVLGDDEIT REPRKVVLHR 430 440 450 460 470 480 GSTGLGFNIV GGEDGEGIFI SFILAGGPAD LSGELRKGDR IISVNSVDLR AASHEQAAAA 490 500 510 520 530 540 LKNAGQAVTI VAQYRPEEYS RFEAKIHDLR EQMMNSSISS GSGSLRTSQK RSLYVRALFD 550 560 570 580 590 600 YDKTKDSGLP SQGLNFKFGD ILHVINASDD EWWQARQVTP DGESDEVGVI PSKRRVEKKE 610 620 630 640 650 660 RARLKTVKFN SKTRDKGEIP DDMGSKGLKH VTSNASDSES SYRGQEEYVL SYEPVNQQEV 670 680 690 700 710 720 NYTRPVIILG PMKDRINDDL ISEFPDKFGS CVPHTTRPKR DYEVDGRDYH FVTSREQMEK 730 740 750 760 770 780 DIQEHKFIEA GQYNNHLYGT SVQSVREVAE KGKHCILDVS GNAIKRLQIA QLYPISIFIK 790 800 810 820 830 840 PKSMENIMEM NKRLTEEQAR KTFERAMKLE QEFTEHFTAI VQGDTLEDIY NQVKQIIEEQ 850 SGSYIWVPAK EKL
	Isoform 6 [UniParc]. Checksum: 5DB5256100623D0B	FASTA	891	99,090
	10 20 30 40 50 60 MPVRKQDTQR ALHLLEEYRS KLSQTEDRQL RSSIERVINI FQSNLFQALI DIQEFYEVTL 70 80 90 100 110 120 LDNPKCIDRS KPSEPIQPVN TWEISSLPSS TVTSETLPSS LSPSVEKYRY QDEDTPPQEH 130 140 150 160 170 180 ISPQITNEVI GPELVHVSEK NLSEIENVHG FVSHSHISPI KPTEAVLPSP PTVPVIPVLP 190 200 210 220 230 240 VPAENTVILP TIPQANPPPV LVNTDSLETP TYVNGTDADY EYEEITLERG NSGLGFSIAG 250 260 270 280 290 300 GTDNPHIGDD SSIFITKIIT GGAAAQDGRL RVNDCILRVN EVDVRDVTHS KAVEALKEAG 310 320 330 340 350 360 SIVRLYVKRR KPVSEKIMEI KLIKGPKGLG FSIAGGVGNQ HIPGDNSIYV TKIIEGGAAH 370 380 390 400 410 420 KDGKLQIGDK LLAVNNVCLE EVTHEEAVTA LKNTSDFVYL KVAKPTSMYM NDGYAPPDIT 430 440 450 460 470 480 NSSSQPVDNH VSPSSFLGQT PASPARYSPV SKAVLGDDEI TREPRKVVLH RGSTGLGFNI 490 500 510 520 530 540 VGGEDGEGIF ISFILAGGPA DLSGELRKGD RIISVNSVDL RAASHEQAAA ALKNAGQAVT 550 560 570 580 590 600 IVAQYRPEEY SRFEAKIHDL REQMMNSSIS SGSGSLRTSQ KRSLYVRALF DYDKTKDSGL 610 620 630 640 650 660 PSQGLNFKFG DILHVINASD DEWWQARQVT PDGESDEVGV IPSKRRVEKK ERARLKTVKF 670 680 690 700 710 720 NSKTRDKGEI PDDMGSKGLK RGQEEYVLSY EPVNQQEVNY TRPVIILGPM KDRINDDLIS 730 740 750 760 770 780 EFPDKFGSCV PHTTRPKRDY EVDGRDYHFV TSREQMEKDI QEHKFIEAGQ YNNHLYGTSV 790 800 810 820 830 840 QSVREVAEKG KHCILDVSGN AIKRLQIAQL YPISIFIKPK SMENIMEMNK RLTEEQARKT 850 860 870 880 890 FERAMKLEQE FTEHFTAIVQ GDTLEDIYNQ VKQIIEEQSG SYIWVPAKEK L
	Isoform 7 [UniParc]. Checksum: FE8911BB05B03211	FASTA	917	101,849
	10 20 30 40 50 60 MPVRKQDTQR ALHLLEEYRS KLSQTEDRQL RSSIERVINI FQSNLFQALI DIQEFYEVTL 70 80 90 100 110 120 LDNPKCIDRS KPSEPIQPVN TWEISSLPSS TVTSETLPSS LSPSVEKYRY QDEDTPPQEH 130 140 150 160 170 180 ISPQITNEVI GPELVHVSEK NLSEIENVHG FVSHSHISPI KPTEAVLPSP PTVPVIPVLP 190 200 210 220 230 240 VPAENTVILP TIPQANPPPV LVNTDSLETP TYVNGTDADY EYEEITLERG NSGLGFSIAG 250 260 270 280 290 300 GTDNPHIGDD SSIFITKIIT GGAAAQDGRL RVNDCILRVN EVDVRDVTHS KAVEALKEAG 310 320 330 340 350 360 SIVRLYVKRR KPVSEKIMEI KLIKGPKGLG FSIAGGVGNQ HIPGDNSIYV TKIIEGGAAH 370 380 390 400 410 420 KDGKLQIGDK LLAVNNVCLE EVTHEEAVTA LKNTSDFVYL KVAKPTSMYM NDGYAPPDIT 430 440 450 460 470 480 NSSSQPVDNH VSPSSFLGQT PASPARYSPV SKAVLGDDEI TREPRKVVLH RGSTGLGFNI 490 500 510 520 530 540 VGGEDGEGIF ISFILAGGPA DLSGELRKGD RIISVNSVDL RAASHEQAAA ALKNAGQAVT 550 560 570 580 590 600 IVAQYRPEEY SRFEAKIHDL REQMMNSSIS SGSGSLRTSQ KRSLYVRALF DYDKTKDSGL 610 620 630 640 650 660 PSQGLNFKFG DILHVINASD DEWWQARQVT PDGESDEVGV IPSKRRVEKK ERARLKTVKF 670 680 690 700 710 720 NSKTRDKGEI PDDMGSKGLK HVTSNASDSE SSYLILITDE YGCSKGRGQE EYVLSYEPVN 730 740 750 760 770 780 QQEVNYTRPV IILGPMKDRI NDDLISEFPD KFGSCVPHTT RPKRDYEVDG RDYHFVTSRE 790 800 810 820 830 840 QMEKDIQEHK FIEAGQYNNH LYGTSVQSVR EVAEKGKHCI LDVSGNAIKR LQIAQLYPIS 850 860 870 880 890 900 IFIKPKSMEN IMEMNKRLTE EQARKTFERA MKLEQEFTEH FTAIVQGDTL EDIYNQVKQI 910 IEEQSGSYIW VPAKEKL

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Cloning and characterization of hdlg: the human homologue of the Drosophila discs large tumor suppressor binds to protein 4.1." Lue R.A., Marfatia S.M., Branton D., Chishti A.H. Proc. Natl. Acad. Sci. U.S.A. 91:9818-9822(1994) [PubMed: 7937897] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1; 2; 3 AND 4), TISSUE SPECIFICITY, SUBCELLULAR LOCATION, INTERACTION WITH EPB41, VARIANT GLN-278.
[2]	"The full-ORF clone resource of the German cDNA consortium." Bechtel S., Rosenfelder H., Duda A., Schmidt C.P., Ernst U., Wellenreuther R., Mehrle A., Schuster C., Bahr A., Bloecker H., Heubner D., Hoerlein A., Michel G., Wedler H., Koehrer K., Ottenwaelder B., Poustka A., Wiemann S., Schupp I. BMC Genomics 8:399-399(2007) [PubMed: 17974005] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1). Tissue: Liver.
[3]	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. , Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W., Venter J.C. Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[4]	"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] (ISOFORMS 2 AND 4). Tissue: Brain.
[5]	"Clustering of Shaker-type K+ channels by interaction with a family of membrane-associated guanylate kinases." Kim E., Niethammer M., Rothschild A., Jan Y.N., Sheng M. Nature 378:85-88(1995) [PubMed: 7477295] [Abstract] Cited for: INTERACTION WITH KCNA1; KCNA2; KCNA3 AND KCNA4.
[6]	"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: 8922391] [Abstract] Cited for: INTERACTION WITH EPB41, SUBCELLULAR LOCATION.
[7]	"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: 8638125] [Abstract] Cited for: INTERACTION WITH APC.
[8]	"Binding of human virus oncoproteins to hDlg/SAP97, a mammalian homolog of the Drosophila discs large tumor suppressor protein." Lee S.S., Weiss R.S., Javier R.T. Proc. Natl. Acad. Sci. U.S.A. 94:6670-6675(1997) [PubMed: 9192623] [Abstract] Cited for: INTERACTION WITH VIRAL ONCOPROTEIN TAX AND HPV-18 E6.
[9]	"Tax oncoprotein of HTLV-1 binds to the human homologue of Drosophila discs large tumor suppressor protein, hDLG, and perturbs its function in cell growth control." Suzuki T., Ohsugi Y., Uchida-Toita M., Akiyama T., Yoshida M. Oncogene 18:5967-5972(1999) [PubMed: 10557085] [Abstract] Cited for: INTERACTION WITH HTLV-1 TAX-1.
[10]	"GAKIN, a novel kinesin-like protein associates with the human homologue of the Drosophila discs large tumor suppressor in T lymphocytes." Hanada T., Lin L., Tibaldi E.V., Reinherz E.L., Chishti A.H. J. Biol. Chem. 275:28774-28784(2000) [PubMed: 10859302] [Abstract] Cited for: INTERACTION WITH KIF13B, SUBCELLULAR LOCATION.
[11]	"The APC-hDLG complex negatively regulates cell cycle progression from the G0/G1 to S phase." Ishidate T., Matsumine A., Toyoshima K., Akiyama T. Oncogene 19:365-372(2000) [PubMed: 10656683] [Abstract] Cited for: INTERACTION WITH APC, FUNCTION IN CELL PROLIFERATION.
[12]	"Characterization of PDZ-binding kinase, a mitotic kinase." Gaudet S., Branton D., Lue R.A. Proc. Natl. Acad. Sci. U.S.A. 97:5167-5172(2000) [PubMed: 10779557] [Abstract] Cited for: INTERACTION WITH TOPK.
[13]	"Pilt, a novel peripheral membrane protein at tight junctions in epithelial cells." Kawabe H., Nakanishi H., Asada M., Fukuhara A., Morimoto K., Takeuchi M., Takai Y. J. Biol. Chem. 276:48350-48355(2001) [PubMed: 11602598] [Abstract] Cited for: POSSIBLE INTERACTION WITH TJAP1.
[14]	"Expression, regulation and role of the MAGUK protein SAP-97 in human atrial myocardium." Godreau D., Vranckx R., Maguy A., Rucker-Martin C., Goyenvalle C., Abdelshafy S., Tessier S., Couetil J.P., Hatem S.N. Cardiovasc. Res. 56:433-442(2002) [PubMed: 12445884] [Abstract] Cited for: FUNCTION, TISSUE SPECIFICITY, SUBCELLULAR LOCATION, INTERACTION WITH KCNF1.
[15]	"The distribution and function of alternatively spliced insertions in hDlg." McLaughlin M., Hale R., Ellston D., Gaudet S., Lue R.A., Viel A. J. Biol. Chem. 277:6406-6412(2002) [PubMed: 11723125] [Abstract] Cited for: ALTERNATIVE SPLICING (ISOFORMS 5; 6 AND 7), SUBCELLULAR LOCATION.
[16]	"Protein 4.1-mediated membrane targeting of human discs large in epithelial cells." Hanada T., Takeuchi A., Sondarva G., Chishti A.H. J. Biol. Chem. 278:34445-34450(2003) [PubMed: 12807908] [Abstract] Cited for: SUBCELLULAR LOCATION, MUTAGENESIS OF 38-ILE--ILE-40.
[17]	"Human homolog of disc-large is required for adherens junction assembly and differentiation of human intestinal epithelial cells." Laprise P., Viel A., Rivard N. J. Biol. Chem. 279:10157-10166(2004) [PubMed: 14699157] [Abstract] Cited for: INTERACTION WITH PIK3R1 AND CDH1, FUNCTION IN ADHERENS JUNCTION ASSEMBLY.
[18]	"Discs large (Dlg1) complexes in lymphocyte activation." Xavier R., Rabizadeh S., Ishiguro K., Andre N., Ortiz J.B., Wachtel H., Morris D.G., Lopez-Ilasaca M., Shaw A.C., Swat W., Seed B. J. Cell Biol. 166:173-178(2004) [PubMed: 15263016] [Abstract] Cited for: FUNCTION IN T-CELL ACTIVATION.
[19]	"Direct binding of the human homologue of the Drosophila disc large tumor suppressor gene to seven-pass transmembrane proteins, tumor endothelial marker 5 (TEM5), and a novel TEM5-like protein." Yamamoto Y., Irie K., Asada M., Mino A., Mandai K., Takai Y. Oncogene 23:3889-3897(2004) [PubMed: 15021905] [Abstract] Cited for: INTERACTION WITH GPR124 AND GPR125.
[20]	"Dlg, Scribble and Lgl in cell polarity, cell proliferation and cancer." Humbert P., Russell S., Richardson H. Bioessays 25:542-553(2003) [PubMed: 12766944] [Abstract] Cited for: REVIEW.
[21]	"Large-scale characterization of HeLa cell nuclear phosphoproteins." Beausoleil S.A., Jedrychowski M., Schwartz D., Elias J.E., Villen J., Li J., Cohn M.A., Cantley L.C., Gygi S.P. Proc. Natl. Acad. Sci. U.S.A. 101:12130-12135(2004) [PubMed: 15302935] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-684 AND SER-687, MASS SPECTROMETRY. Tissue: Cervix carcinoma.
[22]	"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: 16630835] [Abstract] Cited for: INTERACTION WITH LRFN1; LRFN2 AND LRFN4.
[23]	"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. , Yuan J., Bakalarski C.E., Villen J., Kornhauser J.M., Smith B., Li D., Zhou X., Gygi S.P., Gu T.-L., Polakiewicz R.D., Rush J., Comb M.J. Cell 131:1190-1203(2007) [PubMed: 18083107] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-760, MASS SPECTROMETRY. Tissue: Lung carcinoma.
[24]	"The stardust family protein MPP7 forms a tripartite complex with LIN7 and DLG1 that regulates the stability and localization of DLG1 to cell junctions." Bohl J., Brimer N., Lyons C., Vande Pol S.B. J. Biol. Chem. 282:9392-9400(2007) [PubMed: 17237226] [Abstract] Cited for: INTERACTION WITH LIN7A; LIN7C AND MPP7.
[25]	"The MAGUK protein MPP7 binds to the polarity protein hDlg1 and facilitates epithelial tight junction formation." Stucke V.M., Timmerman E., Vandekerckhove J., Gevaert K., Hall A. Mol. Biol. Cell 18:1744-1755(2007) [PubMed: 17332497] [Abstract] Cited for: INTERACTION WITH MPP7.
[26]	"Multiple reaction monitoring for robust quantitative proteomic analysis of cellular signaling networks." Wolf-Yadlin A., Hautaniemi S., Lauffenburger D.A., White F.M. Proc. Natl. Acad. Sci. U.S.A. 104:5860-5865(2007) [PubMed: 17389395] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-760, MASS SPECTROMETRY. Tissue: Mammary epithelium.
[27]	"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.
[28]	"Combining protein-based IMAC, peptide-based IMAC, and MudPIT for efficient phosphoproteomic analysis." Cantin G.T., Yi W., Lu B., Park S.K., Xu T., Lee J.-D., Yates J.R. III J. Proteome Res. 7:1346-1351(2008) [PubMed: 18220336] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-619, MASS SPECTROMETRY. Tissue: Cervix carcinoma.
[29]	"A quantitative atlas of mitotic phosphorylation." Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E., Elledge S.J., Gygi S.P. Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008) [PubMed: 18669648] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-115; SER-122; SER-575; SER-684 AND SER-687, MASS SPECTROMETRY. Tissue: Cervix carcinoma.
[30]	"Kv4 potassium channels form a tripartite complex with the anchoring protein SAP97 and CaMKII in cardiac myocytes." El-Haou S., Balse E., Neyroud N., Dilanian G., Gavillet B., Abriel H., Coulombe A., Jeromin A., Hatem S.N. Circ. Res. 104:758-769(2009) [PubMed: 19213956] [Abstract] Cited for: FUNCTION, TISSUE SPECIFICITY, INTERACTION WITH KCND2 AND KCND3.
[31]	"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 SER-575, MASS SPECTROMETRY. Tissue: Leukemic T-cell.
[32]	"p38gamma regulates interaction of nuclear PSF and RNA with the tumour-suppressor hDlg in response to osmotic shock." Sabio G., Cerezo-Guisado M.I., Del Reino P., Inesta-Vaquera F.A., Rousseau S., Arthur J.S., Campbell D.G., Centeno F., Cuenda A. J. Cell Sci. 123:2596-2604(2010) [PubMed: 20605917] [Abstract] Cited for: PHOSPHORYLATION BY MAPK12, INTERACTION WITH SFPQ, FUNCTION.
[33]	"Crystal structure of a PDZ domain." Cabral J.H., Petosa C., Sutcliffe M.J., Raza S., Byron O., Poy F., Marfatia S.M., Chishti A.H., Liddington R.C. Nature 382:649-652(1996) [PubMed: 8757139] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (2.8 ANGSTROMS) OF 460-555.
+	Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ

U13896 mRNA. Translation: AAA50598.1.
U13897 mRNA. Translation: AAA50599.1.
EF553524 mRNA. Translation: ABQ66269.1.
CH471191 Genomic DNA. Translation: EAW53610.1.
CH471191 Genomic DNA. Translation: EAW53611.1.
CH471191 Genomic DNA. Translation: EAW53612.1.
CH471191 Genomic DNA. Translation: EAW53614.1.
BC140841 mRNA. Translation: AAI40842.1.
BC144651 mRNA. Translation: AAI44652.1.

IPI

IPI00030351.
IPI00218729.
IPI00552213.
IPI00552376.
IPI00552511.
IPI00552682.
IPI00553029.

PIR

I38756.
I38757.

RefSeq

NP_001091894.1. NM_001098424.1.
NP_001191315.1. NM_001204386.1.
NP_001191316.1. NM_001204387.1.
NP_001191317.1. NM_001204388.1.
NP_004078.2. NM_004087.2.

UniGene

Hs.292549.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
1PDR	X-ray	2.80	A	457-552	[»]
2OQS	NMR	-	A	318-405	[»]
2X7Z	X-ray	2.00	A	311-407	[»]
3LRA	X-ray	2.95	A	2-65	[»]

ProteinModelPortal

Q12959.

SMR

Q12959. Positions 2-65, 221-904.

ModBase

Search...

Protein-protein interaction databases

IntAct

Q12959. 8 interactions.

MINT

MINT-107690.

STRING

Q12959.

PTM databases

PhosphoSite

Q12959.

Polymorphism databases

DMDM

223590196.

Proteomic databases

PRIDE

Q12959.

Protocols and materials databases

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

Ensembl

ENST00000419354; ENSP00000407531; ENSG00000075711.
ENST00000448528; ENSP00000391732; ENSG00000075711.

GeneID

1739.

KEGG

hsa:1739.

UCSC

uc003fxn.2. human.

Organism-specific databases

CTD

1739.

GeneCards

GC03M196769.

HGNC

HGNC:2900. DLG1.

HPA

CAB016307.

MIM

601014. gene.

neXtProt

NX_Q12959.

PharmGKB

PA27356.

GenAtlas

Search...

Phylogenomic databases

eggNOG

prNOG11698.

HOVERGEN

HBG107814.

Enzyme and pathway databases

Reactome

REACT_111045. Developmental Biology.
REACT_13685. Neuronal System.

Gene expression databases

ArrayExpress

Q12959.

Bgee

Q12959.

CleanEx

HS_DLG1.

Genevestigator

Q12959.

GermOnline

ENSG00000075711. Homo sapiens.

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/DHR/GLGF.
IPR019583. PDZ_assoc.
IPR011511. SH3_2.
IPR001452. SH3_domain.
[Graphical view]

KO

K12076.

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

NextBio

7051.

SOURCE

Search...

Entry information

Entry name

DLG1_HUMAN

Accession

Primary (citable) accession number: Q12959
Secondary accession number(s): A5YKK7 , B7ZMM0, B9EIQ5, D3DXB8, D3DXB9, Q12958

Entry history

Integrated into UniProtKB/Swiss-Prot:	November 1, 1997
Last sequence update:	February 10, 2009
Last modified:	January 25, 2012
This is version 139 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program

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.