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Protein

Lamin-B receptor

Gene

LBR

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

Functioni

Anchors the lamina and the heterochromatin to the inner nuclear membrane.1 Publication

GO - Molecular functioni

  • chromatin binding Source: UniProtKB
  • DNA binding Source: UniProtKB-KW
  • lamin binding Source: UniProtKB
  • receptor activity Source: FlyBase

GO - Biological processi

  • nucleus organization Source: UniProtKB
Complete GO annotation...

Keywords - Molecular functioni

Receptor

Keywords - Ligandi

DNA-binding

Enzyme and pathway databases

ReactomeiR-DME-191273. Cholesterol biosynthesis.
R-DME-2426168. Activation of gene expression by SREBF (SREBP).

Names & Taxonomyi

Protein namesi
Recommended name:
Lamin-B receptor
Alternative name(s):
dLBR
Gene namesi
Name:LBRImported
ORF Names:CG17952
OrganismiDrosophila melanogaster (Fruit fly)
Taxonomic identifieri7227 [NCBI]
Taxonomic lineageiEukaryotaMetazoaEcdysozoaArthropodaHexapodaInsectaPterygotaNeopteraEndopterygotaDipteraBrachyceraMuscomorphaEphydroideaDrosophilidaeDrosophilaSophophora
Proteomesi
  • UP000000803 Componenti: Chromosome 2R

Organism-specific databases

FlyBaseiFBgn0034657. LBR.

Subcellular locationi

Topology

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Transmembranei308 – 32821HelicalSequence analysisAdd
BLAST
Transmembranei363 – 38321HelicalSequence analysisAdd
BLAST
Transmembranei402 – 42221HelicalSequence analysisAdd
BLAST
Transmembranei429 – 44921HelicalSequence analysisAdd
BLAST
Transmembranei497 – 51721HelicalSequence analysisAdd
BLAST
Transmembranei543 – 56321HelicalSequence analysisAdd
BLAST
Transmembranei577 – 59923HelicalSequence analysisAdd
BLAST
Transmembranei604 – 62421HelicalSequence analysisAdd
BLAST
Transmembranei687 – 70721HelicalSequence analysisAdd
BLAST

GO - Cellular componenti

  • integral component of nuclear inner membrane Source: UniProtKB
  • nuclear envelope Source: FlyBase
  • nuclear inner membrane Source: FlyBase
Complete GO annotation...

Keywords - Cellular componenti

Membrane, Nucleus

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 741741Lamin-B receptorPRO_0000207512Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei111 – 1111Phosphoserine1 Publication
Modified residuei135 – 1351Phosphothreonine1 Publication
Modified residuei144 – 1441Phosphoserine1 Publication
Modified residuei223 – 2231Phosphoserine1 Publication
Modified residuei225 – 2251Phosphoserine1 Publication
Modified residuei234 – 2341Phosphothreonine1 Publication
Modified residuei237 – 2371Phosphothreonine1 Publication
Modified residuei243 – 2431Phosphoserine1 Publication
Modified residuei246 – 2461Phosphoserine1 Publication
Modified residuei248 – 2481Phosphoserine1 Publication
Modified residuei250 – 2501Phosphoserine1 Publication
Modified residuei263 – 2631Phosphoserine1 Publication
Modified residuei266 – 2661Phosphothreonine1 Publication
Modified residuei284 – 2841Phosphoserine1 Publication
Modified residuei288 – 2881Phosphothreonine1 Publication
Modified residuei291 – 2911Phosphoserine1 Publication
Modified residuei293 – 2931Phosphothreonine1 Publication
Modified residuei298 – 2981Phosphoserine1 Publication
Modified residuei640 – 6401Phosphoserine1 Publication
Modified residuei642 – 6421Phosphoserine1 Publication

Keywords - PTMi

Phosphoprotein

Proteomic databases

PaxDbiQ8MLV1.
PRIDEiQ8MLV1.

PTM databases

iPTMnetiQ8MLV1.

Expressioni

Gene expression databases

BgeeiQ8MLV1.
GenevisibleiQ8MLV1. DM.

Interactioni

Subunit structurei

Interacts directly with LAM.1 Publication

GO - Molecular functioni

  • lamin binding Source: UniProtKB

Protein-protein interaction databases

BioGridi63107. 1 interaction.
IntActiQ8MLV1. 4 interactions.
MINTiMINT-1740287.
STRINGi7227.FBpp0071630.

Structurei

3D structure databases

ProteinModelPortaliQ8MLV1.
SMRiQ8MLV1. Positions 554-741.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Belongs to the ERG4/ERG24 family.Sequence analysis

Keywords - Domaini

Transmembrane, Transmembrane helix

Phylogenomic databases

eggNOGiKOG1435. Eukaryota.
ENOG410XP67. LUCA.
GeneTreeiENSGT00390000000417.
InParanoidiQ8MLV1.
KOiK19532.
OMAiAEMKIHN.
OrthoDBiEOG75B85C.
PhylomeDBiQ8MLV1.

Family and domain databases

InterProiIPR001171. Ergosterol_biosynth_ERG4_ERG24.
[Graphical view]
PfamiPF01222. ERG4_ERG24. 2 hits.
[Graphical view]

Sequences (2)i

Sequence statusi: Complete.

This entry describes 2 isoformsi produced by alternative splicing. AlignAdd to basket

Isoform C1 Publication (identifier: Q8MLV1-1) [UniParc]FASTAAdd to basket

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

« Hide

        10         20         30         40         50
MQHSPSTTTD HIHFAARFFD RNSYTMDRRL RRPRRTEDVS SGPLLAQSKQ
60 70 80 90 100
PSLLPVTRRT GSVTAAGATA TATATAGPAT RTRASPSRNK VVAPPSPDLG
110 120 130 140 150
PRTRRSSRPR SSVGPLTGSG SGSSLPIKAA IKARTPIPEV SEVSSPIRLS
160 170 180 190 200
TSNLPMTLTT NTSSGAPNKA FNTSSVNSGN SFSRTTTSST TTTTERIEIR
210 220 230 240 250
AEGDGEVDTD SIRKRITERL RRSVSKTISN LAGTPVTNTE EGSRYSRSVS
260 270 280 290 300
RSVYDDEKSS KRSYSTGEED IDEEDELEED QFRSFNVTRK SATPAEISCR
310 320 330 340 350
QLKAPREFGG WLGAFLFLLL LPTAVYYLTW SCTARNACQF KHLNLGILLD
360 370 380 390 400
VNYLTRQVFQ PRVVGAFAAY QVVVFLLVAL LPGRRVHLTR ETYKFNCLAV
410 420 430 440 450
SLTLLIASGV AEYLKYPVVT FVLRHYLRFC IFGLVGAFVA AAWSYWLVDT
460 470 480 490 500
AKYNVLRQTL TNDYGRTGSF VVDFALGRQL NPKWLGRVDW KQFQYRLSLV
510 520 530 540 550
TTLIYATCYI YQTLVWPQKP QLGEQEGYLY QAKYYWNNVN YDPATLFSAS
560 570 580 590 600
CLLFYVLDAI IFEHHLSSSF ELQHEGYGCL LLLRYAATPY LLTAVTKYFY
610 620 630 640 650
EQRVPISCWY APLAVAALLS LGLLVKRFSC AYKYKYRLNS QSPIFANIET
660 670 680 690 700
IHTYQGSRLL LSGMWGWVRQ PNYLGDIVAL LALAAPMALR PAWPPVLGLS
710 720 730 740
LIILLLLHRA TRANARNQAR YHSSWQRYST QVRSYILPRV Y
Length:741
Mass (Da):83,185
Last modified:October 1, 2002 - v1
Checksum:i679CD09855F07963
GO
Isoform A1 Publication (identifier: Q8MLV1-2) [UniParc]FASTAAdd to basket

Also known as: B1 Publication

The sequence of this isoform differs from the canonical sequence as follows:
     1-25: Missing.

Note: No experimental confirmation available.Curated
Show »
Length:716
Mass (Da):80,235
Checksum:iA38DF82126E131E0
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti52 – 521S → T (PubMed:15054108).Curated
Sequence conflicti52 – 521S → T (Ref. 5) Curated
Sequence conflicti67 – 671G → A (PubMed:15054108).Curated
Sequence conflicti67 – 671G → A (Ref. 5) Curated
Sequence conflicti317 – 3171F → L (PubMed:15054108).Curated
Sequence conflicti317 – 3171F → L (Ref. 5) Curated
Sequence conflicti408 – 4081S → G (PubMed:15054108).Curated
Sequence conflicti408 – 4081S → G (Ref. 5) Curated

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei1 – 2525Missing in isoform A. 2 PublicationsVSP_051851Add
BLAST

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AJ606680 mRNA. Translation: CAE54809.1.
AE013599 Genomic DNA. Translation: AAM71015.1.
AE013599 Genomic DNA. Translation: AAF46760.2.
AY070562 mRNA. Translation: AAL48033.1.
BT023819 mRNA. Translation: AAZ86740.1.
RefSeqiNP_611608.1. NM_137764.3. [Q8MLV1-2]
NP_726114.1. NM_166484.2. [Q8MLV1-1]
NP_726115.1. NM_166485.2. [Q8MLV1-2]
UniGeneiDm.6462.

Genome annotation databases

EnsemblMetazoaiFBtr0071713; FBpp0071630; FBgn0034657. [Q8MLV1-1]
GeneIDi37482.
KEGGidme:Dmel_CG17952.

Keywords - Coding sequence diversityi

Alternative splicing

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AJ606680 mRNA. Translation: CAE54809.1.
AE013599 Genomic DNA. Translation: AAM71015.1.
AE013599 Genomic DNA. Translation: AAF46760.2.
AY070562 mRNA. Translation: AAL48033.1.
BT023819 mRNA. Translation: AAZ86740.1.
RefSeqiNP_611608.1. NM_137764.3. [Q8MLV1-2]
NP_726114.1. NM_166484.2. [Q8MLV1-1]
NP_726115.1. NM_166485.2. [Q8MLV1-2]
UniGeneiDm.6462.

3D structure databases

ProteinModelPortaliQ8MLV1.
SMRiQ8MLV1. Positions 554-741.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi63107. 1 interaction.
IntActiQ8MLV1. 4 interactions.
MINTiMINT-1740287.
STRINGi7227.FBpp0071630.

PTM databases

iPTMnetiQ8MLV1.

Proteomic databases

PaxDbiQ8MLV1.
PRIDEiQ8MLV1.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblMetazoaiFBtr0071713; FBpp0071630; FBgn0034657. [Q8MLV1-1]
GeneIDi37482.
KEGGidme:Dmel_CG17952.

Organism-specific databases

CTDi3930.
FlyBaseiFBgn0034657. LBR.

Phylogenomic databases

eggNOGiKOG1435. Eukaryota.
ENOG410XP67. LUCA.
GeneTreeiENSGT00390000000417.
InParanoidiQ8MLV1.
KOiK19532.
OMAiAEMKIHN.
OrthoDBiEOG75B85C.
PhylomeDBiQ8MLV1.

Enzyme and pathway databases

ReactomeiR-DME-191273. Cholesterol biosynthesis.
R-DME-2426168. Activation of gene expression by SREBF (SREBP).

Miscellaneous databases

ChiTaRSiLBR. fly.
GenomeRNAii37482.
NextBioi803872.
PROiQ8MLV1.

Gene expression databases

BgeeiQ8MLV1.
GenevisibleiQ8MLV1. DM.

Family and domain databases

InterProiIPR001171. Ergosterol_biosynth_ERG4_ERG24.
[Graphical view]
PfamiPF01222. ERG4_ERG24. 2 hits.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "The lamin B receptor of Drosophila melanogaster."
    Wagner N., Weber D., Seitz S., Krohne G.
    J. Cell Sci. 117:2015-2028(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM C), FUNCTION, SUBCELLULAR LOCATION, INTERACTION WITH LAM.
  2. "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: Berkeley1 Publication.
  3. Cited for: GENOME REANNOTATION, ALTERNATIVE SPLICING.
    Strain: Berkeley.
  4. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM A).
    Strain: Berkeley1 Publication.
    Tissue: Embryo1 Publication.
  5. Stapleton M., Carlson J.W., Chavez C., Frise E., George R.A., Pacleb J.M., Park S., Wan K.H., Yu C., Celniker S.E.
    Submitted (AUG-2005) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM C).
    Strain: Berkeley1 Publication.
    Tissue: Embryo1 Publication.
  6. "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-111; THR-135; SER-144; SER-223; SER-225; THR-234; THR-237; SER-243; SER-246; SER-248; SER-250; SER-263; THR-266; SER-284; THR-288; SER-291; THR-293; SER-298; SER-640 AND SER-642, IDENTIFICATION BY MASS SPECTROMETRY.
    Tissue: Embryo.

Entry informationi

Entry nameiLBR_DROME
AccessioniPrimary (citable) accession number: Q8MLV1
Secondary accession number(s): Q0E8Z1, Q709R7, Q9W2D2
Entry historyi
Integrated into UniProtKB/Swiss-Prot: October 25, 2005
Last sequence update: October 1, 2002
Last modified: May 11, 2016
This is version 97 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programDrosophila annotation project

Miscellaneousi

Caution

Unlike other members of this family, it does not possess sterol C14 reductase activity.Curated

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.