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Protein

Lethal(2) giant larvae protein

Gene

l(2)gl

Organism
Drosophila melanogaster (Fruit fly)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Essential for the development of polarized epithelia, for cell polarity associated with asymmetric cell division of neuroblasts during development, and for oocyte polarity formation. Promotes the formation of actin-rich projections at the oocyte cortex and the posterior enrichment of par-1 which is required for oocyte polarization. Regulates the localization of axis-specifying morphogens such as stau and grk.
Isoform p78: Has an essential role in control of cell proliferation and differentiation during development and could act as a tumor suppressor.
Isoform p127: Has an accessory function in control of cell proliferation and differentiation during development.

GO - Molecular functioni

  • myosin binding Source: FlyBase
  • myosin II binding Source: FlyBase
  • protein kinase inhibitor activity Source: FlyBase
  • SNARE binding Source: FlyBase

GO - Biological processi

  • actin cytoskeleton organization Source: FlyBase
  • apical protein localization Source: FlyBase
  • asymmetric neuroblast division Source: FlyBase
  • asymmetric protein localization Source: FlyBase
  • asymmetric protein localization involved in cell fate determination Source: FlyBase
  • basal protein localization Source: FlyBase
  • cell competition in a multicellular organism Source: FlyBase
  • cell differentiation Source: FlyBase
  • cell proliferation Source: FlyBase
  • chitin-based larval cuticle pattern formation Source: FlyBase
  • dorsal closure Source: FlyBase
  • ecdysone-mediated induction of salivary gland cell autophagic cell death Source: FlyBase
  • epidermis morphogenesis Source: FlyBase
  • epithelium development Source: FlyBase
  • establishment of epithelial cell planar polarity Source: FlyBase
  • establishment of mitotic spindle orientation Source: FlyBase
  • establishment of neuroblast polarity Source: FlyBase
  • establishment of protein localization Source: FlyBase
  • establishment or maintenance of epithelial cell apical/basal polarity Source: FlyBase
  • establishment or maintenance of neuroblast polarity Source: FlyBase
  • establishment or maintenance of polarity of embryonic epithelium Source: FlyBase
  • establishment or maintenance of polarity of follicular epithelium Source: FlyBase
  • establishment or maintenance of polarity of larval imaginal disc epithelium Source: FlyBase
  • germarium-derived egg chamber formation Source: FlyBase
  • localization within membrane Source: FlyBase
  • morphogenesis of an epithelium Source: FlyBase
  • morphogenesis of a polarized epithelium Source: FlyBase
  • morphogenesis of follicular epithelium Source: FlyBase
  • morphogenesis of larval imaginal disc epithelium Source: FlyBase
  • negative regulation of cell proliferation Source: FlyBase
  • negative regulation of neuroblast proliferation Source: FlyBase
  • negative regulation of Notch signaling pathway Source: FlyBase
  • negative regulation of protein kinase activity Source: FlyBase
  • nervous system development Source: FlyBase
  • neurotransmitter secretion Source: FlyBase
  • oocyte anterior/posterior axis specification Source: FlyBase
  • oocyte microtubule cytoskeleton organization Source: FlyBase
  • protein localization Source: FlyBase
  • protein localization to cell cortex Source: FlyBase
  • regulation of cell cycle Source: FlyBase
  • regulation of cell proliferation Source: FlyBase
  • regulation of cell shape Source: FlyBase
  • salivary gland histolysis Source: FlyBase
  • sensory organ development Source: FlyBase
  • septate junction assembly Source: FlyBase
  • symmetric cell division Source: FlyBase
  • synaptic vesicle priming Source: FlyBase
  • transforming growth factor beta receptor signaling pathway Source: FlyBase
Complete GO annotation...

Keywords - Molecular functioni

Developmental protein

Keywords - Biological processi

Cell cycle, Exocytosis

Names & Taxonomyi

Protein namesi
Recommended name:
Lethal(2) giant larvae protein
Gene namesi
Name:l(2)gl
ORF Names:CG2671
OrganismiDrosophila melanogaster (Fruit fly)
Taxonomic identifieri7227 [NCBI]
Taxonomic lineageiEukaryotaMetazoaEcdysozoaArthropodaHexapodaInsectaPterygotaNeopteraEndopterygotaDipteraBrachyceraMuscomorphaEphydroideaDrosophilidaeDrosophilaSophophora
Proteomesi
  • UP000000803 Componenti: Chromosome 2L

Organism-specific databases

FlyBaseiFBgn0002121. l(2)gl.

Subcellular locationi

GO - Cellular componenti

  • apicolateral plasma membrane Source: FlyBase
  • basolateral plasma membrane Source: FlyBase
  • cell cortex Source: FlyBase
  • cortical cytoskeleton Source: FlyBase
  • cytoplasm Source: FlyBase
  • cytoskeleton Source: FlyBase
  • cytosol Source: FlyBase
  • interstitial matrix Source: FlyBase
  • plasma membrane Source: FlyBase
  • proteinaceous extracellular matrix Source: FlyBase
  • septate junction Source: FlyBase
  • smooth septate junction Source: FlyBase
  • synaptic vesicle Source: FlyBase
Complete GO annotation...

Keywords - Cellular componenti

Cell membrane, Extracellular matrix, Membrane, Secreted

Pathology & Biotechi

Keywords - Diseasei

Tumor suppressor

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 11611161Lethal(2) giant larvae proteinPRO_0000084345Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei473 – 4731Phosphoserine1 Publication
Modified residuei484 – 4841Phosphoserine1 Publication
Modified residuei679 – 6791Phosphoserine1 Publication
Modified residuei808 – 8081Phosphoserine1 Publication
Modified residuei869 – 8691Phosphoserine1 Publication
Modified residuei876 – 8761Phosphoserine1 Publication
Modified residuei887 – 8871Phosphoserine1 Publication
Modified residuei889 – 8891Phosphoserine1 Publication
Modified residuei893 – 8931Phosphoserine1 Publication
Modified residuei1013 – 10131Phosphoserine1 Publication

Post-translational modificationi

Phosphorylated by aPKC which restricts l2gl activity to the oocyte posterior and is required for oocyte polarity formation.2 Publications

Keywords - PTMi

Phosphoprotein

Proteomic databases

PaxDbiP08111.
PRIDEiP08111.

PTM databases

iPTMnetiP08111.

Expressioni

Tissue specificityi

Expressed in the epithelial cells of the digestive tract and in gonads.

Developmental stagei

Expressed abundantly in early embryogenesis. Moderate expression is found in larval and adult stages.

Gene expression databases

BgeeiP08111.
ExpressionAtlasiP08111. differential.
GenevisibleiP08111. DM.

Interactioni

Subunit structurei

May form multimeric complexes. Interacts with mahj. Interacts with aPKC; the interaction results in phosphorylation of l2gl.2 Publications

GO - Molecular functioni

  • myosin binding Source: FlyBase
  • myosin II binding Source: FlyBase
  • SNARE binding Source: FlyBase

Protein-protein interaction databases

BioGridi59421. 9 interactions.
DIPiDIP-22687N.
IntActiP08111. 5 interactions.
MINTiMINT-778782.
STRINGi7227.FBpp0297544.

Structurei

3D structure databases

ProteinModelPortaliP08111.
SMRiP08111. Positions 512-538.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Repeati39 – 7234WD 1Add
BLAST
Repeati82 – 12847WD 2Add
BLAST
Repeati131 – 16737WD 3Add
BLAST
Repeati189 – 22335WD 4Add
BLAST
Repeati231 – 26333WD 5Add
BLAST
Repeati278 – 32043WD 6Add
BLAST
Repeati328 – 35831WD 7Add
BLAST
Repeati380 – 46485WD 8Add
BLAST
Repeati513 – 59482WD 9Add
BLAST
Repeati603 – 66462WD 10Add
BLAST
Repeati708 – 77871WD 11Add
BLAST
Repeati787 – 83246WD 12Add
BLAST
Repeati837 – 92791WD 13Add
BLAST
Repeati941 – 96424WD 14Add
BLAST

Sequence similaritiesi

Belongs to the WD repeat L(2)GL family.Curated
Contains 14 WD repeats.Curated

Keywords - Domaini

Repeat, WD repeat

Phylogenomic databases

eggNOGiKOG1983. Eukaryota.
ENOG410XS6Z. LUCA.
GeneTreeiENSGT00390000000018.
InParanoidiP08111.
KOiK06094.
OMAiGHLRDPT.
OrthoDBiEOG79W94C.
PhylomeDBiP08111.

Family and domain databases

Gene3Di2.130.10.10. 4 hits.
InterProiIPR000664. Lethal2_giant.
IPR013905. Lgl_C_dom.
IPR013577. LLGL2.
IPR015943. WD40/YVTN_repeat-like_dom.
IPR017986. WD40_repeat_dom.
[Graphical view]
PfamiPF08596. Lgl_C. 1 hit.
PF08366. LLGL. 1 hit.
[Graphical view]
PRINTSiPR00962. LETHAL2GIANT.
SUPFAMiSSF50978. SSF50978. 8 hits.
PROSITEiPS00678. WD_REPEATS_1. 1 hit.
[Graphical view]

Sequences (4)i

Sequence statusi: Complete.

This entry describes 4 isoformsi produced by alternative splicing. AlignAdd to basket

Isoform p127 (identifier: P08111-1) [UniParc]FASTAAdd to basket

Also known as: A, C

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
MLKFIRGKGQ QPSADRHRLQ KDLFAYRKTA QHGFPHKPSA LAYDPVLKLM
60 70 80 90 100
AIGTQTGALK VFGQPGVELY GQHTLLNNSA SELNVQLLEW VYGTGRILSL
110 120 130 140 150
TAANQLILWE PVGATLLPIK TLPFDGKLKK VSSLCCSLSK DLLWIGTEGG
160 170 180 190 200
NIYQLDLHTF TIKEPVIYHD VVLEQVPPAY KLNPGAIESI RQLPNSPSKL
210 220 230 240 250
LVAYNRGLCV LWDFESASVQ RAYIAPGHGQ SVGLTVNFEG SEFTWYHADG
260 270 280 290 300
SYATWSIDNP EPPSNVNYVP YGPDPCKSIN RLYKGKRRSN DVIVFSGGMP
310 320 330 340 350
RSAYGDHNCV SVHASDGHKV CLDFTSKVID FFVTFENNRD VAEVLVVLLE
360 370 380 390 400
EELCAYDLTD PNICAIKAPY LHSVHASAVT CNYLASEVVQ SVYESILRAG
410 420 430 440 450
DEQDIDYSNI SWPITGGTLP DNLEESVEED ATKLYEILLT GHEDGSVKFW
460 470 480 490 500
DCTGVLLKPI YNFKTSSIFG SESDFRDDAA ADMSAEQVDE GEPPFRKSGL
510 520 530 540 550
FDPYSDDPRL AVKKIAFCPK TGQLIVGGTA GQIVIADFID LPEKVSLKYI
560 570 580 590 600
SMNLVSDRDG FVWKGHDQLN VRSNLLDGEA IPTTERGVNI SGVLQVLPPA
610 620 630 640 650
SITCMALEAS WGLVSGGTAH GLVLFDFKNF VPVFHRCTLN PNDLTGAGEQ
660 670 680 690 700
LSRRKSFKKS LRESFRKLRK GRSTRTNQSN QVPTTLEARP VERQIEARCA
710 720 730 740 750
DDGLGSMVRC LLFAKTYVTN VNITSPTLWS ATNASTVSVF LLHLPPAQTA
760 770 780 790 800
ATAVPSASGN APPHMPRRIS AQLAKEIQLK HRAPVVGISI FDQAGSPVDQ
810 820 830 840 850
LNAGENGSPP HRVLIASEEQ FKVFSLPQLK PINKYKLTAN EGARIRRIHF
860 870 880 890 900
GSFSCRISPE TLQSMHGCSP TKSTRSHGDG EADPNISGSL AVSRGDVYNE
910 920 930 940 950
TALICLTNMG DIMVLSVPEL KRQLNAAAVR REDINGVSSL CFTNSGEALY
960 970 980 990 1000
MMSSSELQRI ALATSRVVQP TGVVPVEPLE NEESVLEEND AENNKETYAC
1010 1020 1030 1040 1050
DEVVNTYEIK NPSGISICTR PAEENVGRNS VQQVNGVNIS NSPNQANETI
1060 1070 1080 1090 1100
SSSIGDITVD SVRDHLNMTT TTLCSINTEE TIGRLSVLST QTNKASTTVN
1110 1120 1130 1140 1150
MSEIPNINIS NLEDLESKRN TTETSTSSVV IKSIITNISH EKTNGDNKIG
1160
TPKTAPEESQ F
Length:1,161
Mass (Da):126,892
Last modified:February 1, 1995 - v2
Checksum:i979F73A01DA62A1A
GO
Isoform p78 (identifier: P08111-2) [UniParc]FASTAAdd to basket

Also known as: EC371

The sequence of this isoform differs from the canonical sequence as follows:
     708-708: V → F
     709-1161: Missing.

Show »
Length:708
Mass (Da):78,112
Checksum:i830226D7396A8CC5
GO
Isoform B (identifier: P08111-3) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     17-28: HRLQKDLFAYRK → QRYI

Note: No experimental confirmation available.
Show »
Length:1,153
Mass (Da):125,896
Checksum:i577E34DFAE48539C
GO
Isoform D (identifier: P08111-4) [UniParc]FASTAAdd to basket

Also known as: E, F

The sequence of this isoform differs from the canonical sequence as follows:
     1-49: Missing.

Note: No experimental confirmation available.
Show »
Length:1,112
Mass (Da):121,249
Checksum:i524F615010E8B775
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti2 – 21L → F in AAA28671 (PubMed:3036370).Curated
Sequence conflicti2 – 21L → F in AAA28672 (PubMed:3036370).Curated
Sequence conflicti37 – 382KP → A in CAA29007 (PubMed:16453778).Curated
Sequence conflicti58 – 581A → V in ACY56896 (Ref. 6) Curated
Sequence conflicti185 – 1851G → S in CAA29007 (PubMed:16453778).Curated
Sequence conflicti227 – 2271G → R in CAA29007 (PubMed:16453778).Curated
Sequence conflicti243 – 2453FTW → RYL in CAA29007 (PubMed:16453778).Curated
Sequence conflicti304 – 3041Y → N in CAA29007 (PubMed:16453778).Curated
Sequence conflicti331 – 3311F → I in CAA29007 (PubMed:16453778).Curated
Sequence conflicti338 – 3381N → S in CAA29007 (PubMed:16453778).Curated
Sequence conflicti366 – 3661I → T in CAA29007 (PubMed:16453778).Curated
Sequence conflicti388 – 3881V → L in CAA29007 (PubMed:16453778).Curated
Sequence conflicti512 – 5154VKKI → SEEN in CAA29007 (PubMed:16453778).Curated
Sequence conflicti667 – 6759KLRKGRSTR → SFARVDQTK in CAA29007 (PubMed:16453778).Curated
Sequence conflicti727 – 7271T → S in CAA29007 (PubMed:16453778).Curated
Sequence conflicti857 – 8571I → V in ACY56896 (Ref. 6) Curated
Sequence conflicti959 – 9591R → G in AAA28671 (PubMed:3036370).Curated
Sequence conflicti1095 – 10951A → G in CAA29007 (PubMed:16453778).Curated

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei1 – 4949Missing in isoform D. CuratedVSP_021793Add
BLAST
Alternative sequencei17 – 2812HRLQK…FAYRK → QRYI in isoform B. 1 PublicationVSP_021794Add
BLAST
Alternative sequencei708 – 7081V → F in isoform p78. CuratedVSP_004299
Alternative sequencei709 – 1161453Missing in isoform p78. CuratedVSP_004300Add
BLAST

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X05426 mRNA. Translation: CAA29007.1.
M17022 Genomic DNA. Translation: AAA28671.1.
M17022 Genomic DNA. Translation: AAA28672.1.
AE014134 Genomic DNA. Translation: AAG22255.1.
AE014134 Genomic DNA. Translation: AAG22256.2.
AE014134 Genomic DNA. Translation: AAN10501.1.
AE014134 Genomic DNA. Translation: AAN10502.1.
AE014134 Genomic DNA. Translation: AAN10503.1.
AY051654 mRNA. Translation: AAK93078.1.
BT100129 mRNA. Translation: ACX85650.1.
BT100228 mRNA. Translation: ACY56896.1.
PIRiA27069.
A27868.
RefSeqiNP_001245801.1. NM_001258872.2. [P08111-1]
NP_001245802.1. NM_001258873.2. [P08111-1]
NP_001245803.1. NM_001258874.2. [P08111-1]
NP_001245804.1. NM_001258875.2. [P08111-1]
NP_523439.2. NM_078715.4. [P08111-1]
NP_722583.1. NM_164348.3. [P08111-3]
NP_722584.1. NM_164349.3. [P08111-1]
NP_722585.1. NM_164350.3. [P08111-4]
NP_722586.1. NM_164351.3. [P08111-4]
NP_722587.1. NM_164352.3. [P08111-4]
UniGeneiDm.2784.

Genome annotation databases

EnsemblMetazoaiFBtr0078170; FBpp0077828; FBgn0002121. [P08111-1]
FBtr0078171; FBpp0077829; FBgn0002121. [P08111-1]
FBtr0306589; FBpp0297544; FBgn0002121. [P08111-1]
FBtr0306590; FBpp0297545; FBgn0002121. [P08111-1]
FBtr0306591; FBpp0297546; FBgn0002121. [P08111-1]
FBtr0306592; FBpp0297547; FBgn0002121. [P08111-1]
GeneIDi33156.
KEGGidme:Dmel_CG2671.
UCSCiCG2671-RE. d. melanogaster.

Keywords - Coding sequence diversityi

Alternative splicing

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X05426 mRNA. Translation: CAA29007.1.
M17022 Genomic DNA. Translation: AAA28671.1.
M17022 Genomic DNA. Translation: AAA28672.1.
AE014134 Genomic DNA. Translation: AAG22255.1.
AE014134 Genomic DNA. Translation: AAG22256.2.
AE014134 Genomic DNA. Translation: AAN10501.1.
AE014134 Genomic DNA. Translation: AAN10502.1.
AE014134 Genomic DNA. Translation: AAN10503.1.
AY051654 mRNA. Translation: AAK93078.1.
BT100129 mRNA. Translation: ACX85650.1.
BT100228 mRNA. Translation: ACY56896.1.
PIRiA27069.
A27868.
RefSeqiNP_001245801.1. NM_001258872.2. [P08111-1]
NP_001245802.1. NM_001258873.2. [P08111-1]
NP_001245803.1. NM_001258874.2. [P08111-1]
NP_001245804.1. NM_001258875.2. [P08111-1]
NP_523439.2. NM_078715.4. [P08111-1]
NP_722583.1. NM_164348.3. [P08111-3]
NP_722584.1. NM_164349.3. [P08111-1]
NP_722585.1. NM_164350.3. [P08111-4]
NP_722586.1. NM_164351.3. [P08111-4]
NP_722587.1. NM_164352.3. [P08111-4]
UniGeneiDm.2784.

3D structure databases

ProteinModelPortaliP08111.
SMRiP08111. Positions 512-538.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi59421. 9 interactions.
DIPiDIP-22687N.
IntActiP08111. 5 interactions.
MINTiMINT-778782.
STRINGi7227.FBpp0297544.

PTM databases

iPTMnetiP08111.

Proteomic databases

PaxDbiP08111.
PRIDEiP08111.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblMetazoaiFBtr0078170; FBpp0077828; FBgn0002121. [P08111-1]
FBtr0078171; FBpp0077829; FBgn0002121. [P08111-1]
FBtr0306589; FBpp0297544; FBgn0002121. [P08111-1]
FBtr0306590; FBpp0297545; FBgn0002121. [P08111-1]
FBtr0306591; FBpp0297546; FBgn0002121. [P08111-1]
FBtr0306592; FBpp0297547; FBgn0002121. [P08111-1]
GeneIDi33156.
KEGGidme:Dmel_CG2671.
UCSCiCG2671-RE. d. melanogaster.

Organism-specific databases

FlyBaseiFBgn0002121. l(2)gl.

Phylogenomic databases

eggNOGiKOG1983. Eukaryota.
ENOG410XS6Z. LUCA.
GeneTreeiENSGT00390000000018.
InParanoidiP08111.
KOiK06094.
OMAiGHLRDPT.
OrthoDBiEOG79W94C.
PhylomeDBiP08111.

Miscellaneous databases

ChiTaRSil(2)gl. fly.
GenomeRNAii33156.
NextBioi782168.
PROiP08111.

Gene expression databases

BgeeiP08111.
ExpressionAtlasiP08111. differential.
GenevisibleiP08111. DM.

Family and domain databases

Gene3Di2.130.10.10. 4 hits.
InterProiIPR000664. Lethal2_giant.
IPR013905. Lgl_C_dom.
IPR013577. LLGL2.
IPR015943. WD40/YVTN_repeat-like_dom.
IPR017986. WD40_repeat_dom.
[Graphical view]
PfamiPF08596. Lgl_C. 1 hit.
PF08366. LLGL. 1 hit.
[Graphical view]
PRINTSiPR00962. LETHAL2GIANT.
SUPFAMiSSF50978. SSF50978. 8 hits.
PROSITEiPS00678. WD_REPEATS_1. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "A protein product of the Drosophila recessive tumor gene, l(2) giant gl, potentially has cell adhesion properties."
    Luetzelschwab R., Klaembt C., Rossa R., Schmidt O.
    EMBO J. 6:1791-1797(1987) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM P127).
  2. "Structure of the l(2)gl gene of Drosophila and delimitation of its tumor suppressor domain."
    Jacob L., Opper M., Metzroth B., Phannavong B., Mechler B.M.
    Cell 50:215-225(1987) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION, ALTERNATIVE SPLICING (ISOFORMS P127 AND P78).
    Tissue: Embryo.
  3. "The genome sequence of Drosophila melanogaster."
    Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D., Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F., George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N., Sutton G.G., Wortman J.R., Yandell M.D.
    , Zhang Q., Chen L.X., Brandon R.C., Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D., Wan K.H., Doyle C., Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G., Abril J.F., Agbayani A., An H.-J., Andrews-Pfannkoch C., Baldwin D., Ballew R.M., Basu A., Baxendale J., Bayraktaroglu L., Beasley E.M., Beeson K.Y., Benos P.V., Berman B.P., Bhandari D., Bolshakov S., Borkova D., Botchan M.R., Bouck J., Brokstein P., Brottier P., Burtis K.C., Busam D.A., Butler H., Cadieu E., Center A., Chandra I., Cherry J.M., Cawley S., Dahlke C., Davenport L.B., Davies P., de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I., Dietz S.M., Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C., Dunn P., Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S., Fleischmann W., Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M., Glasser K., Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M., Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J., Hostin D., Houston K.A., Howland T.J., Wei M.-H., Ibegwam C., Jalali M., Kalush F., Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A., Kimmel B.E., Kodira C.D., Kraft C.L., Kravitz S., Kulp D., Lai Z., Lasko P., Lei Y., Levitsky A.A., Li J.H., Li Z., Liang Y., Lin X., Liu X., Mattei B., McIntosh T.C., McLeod M.P., McPherson D., Merkulov G., Milshina N.V., Mobarry C., Morris J., Moshrefi A., Mount S.M., Moy M., Murphy B., Murphy L., Muzny D.M., Nelson D.L., Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R., Pacleb J.M., Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V., Reese M.G., Reinert K., Remington K., Saunders R.D.C., Scheeler F., Shen H., Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T.J., Spier E., Spradling A.C., Stapleton M., Strong R., Sun E., Svirskas R., Tector C., Turner R., Venter E., Wang A.H., Wang X., Wang Z.-Y., Wassarman D.A., Weinstock G.M., Weissenbach J., Williams S.M., Woodage T., Worley K.C., Wu D., Yang S., Yao Q.A., Ye J., Yeh R.-F., Zaveri J.S., Zhan M., Zhang G., Zhao Q., Zheng L., Zheng X.H., Zhong F.N., Zhong W., Zhou X., Zhu S.C., Zhu X., Smith H.O., Gibbs R.A., Myers E.W., Rubin G.M., Venter J.C.
    Science 287:2185-2195(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: Berkeley.
  4. Cited for: GENOME REANNOTATION, ALTERNATIVE SPLICING.
    Strain: Berkeley.
  5. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM P127).
    Strain: Berkeley.
    Tissue: Embryo.
  6. Carlson J.W., Booth B., Frise E., Park S., Wan K.H., Yu C., Celniker S.E.
    Submitted (NOV-2009) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS B AND P127).
    Strain: Berkeley.
    Tissue: Embryo.
  7. "Dlg, Scrib and Lgl regulate neuroblast cell size and mitotic spindle asymmetry."
    Albertson R., Doe C.Q.
    Nat. Cell Biol. 5:166-170(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION.
  8. "Lgl and its phosphorylation by aPKC regulate oocyte polarity formation in Drosophila."
    Tian A.G., Deng W.M.
    Development 135:463-471(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, INTERACTION WITH APKC, PHOSPHORYLATION BY APKC.
  9. "Phosphoproteome analysis of Drosophila melanogaster embryos."
    Zhai B., Villen J., Beausoleil S.A., Mintseris J., Gygi S.P.
    J. Proteome Res. 7:1675-1682(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-473; SER-484; SER-679; SER-808; SER-869; SER-876; SER-887; SER-889; SER-893 AND SER-1013, IDENTIFICATION BY MASS SPECTROMETRY.
    Tissue: Embryo.
  10. Cited for: INTERACTION WITH MAHJ.

Entry informationi

Entry nameiL2GL_DROME
AccessioniPrimary (citable) accession number: P08111
Secondary accession number(s): A4UZW0
, D0IQ91, D0IQJ0, Q0E8V5, Q24377, Q8IPV4, Q8IPV5, Q9VPI1
Entry historyi
Integrated into UniProtKB/Swiss-Prot: August 1, 1988
Last sequence update: February 1, 1995
Last modified: May 11, 2016
This is version 164 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programDrosophila annotation project

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. Drosophila
    Drosophila: entries, gene names and cross-references to FlyBase
  2. SIMILARITY comments
    Index of protein domains and families

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 one 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.