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Protein

Lamin Dm0

Gene

Lam

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

Functioni

Lamins are components of the nuclear lamina, a fibrous layer on the nucleoplasmic side of the inner nuclear membrane, which is thought to provide a framework for the nuclear envelope and may also interact with chromatin (PubMed:3126192, PubMed:15035436). May have a role in the localization of the LEM domain proteins Ote, bocks and MAN1 to the nuclear membrane (PubMed:15035436, PubMed:16439308).3 Publications

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sitei289Heptad change of phase1
Sitei353Heptad change of phase1

GO - Molecular functioni

  • receptor binding Source: UniProtKB
  • structural molecule activity Source: FlyBase

GO - Biological processi

  • adult locomotory behavior Source: FlyBase
  • cell aging Source: FlyBase
  • central nervous system development Source: FlyBase
  • centrosome organization Source: FlyBase
  • chitin-based cuticle development Source: FlyBase
  • chromatin silencing Source: FlyBase
  • compound eye morphogenesis Source: FlyBase
  • digestive tract morphogenesis Source: FlyBase
  • gonad morphogenesis Source: FlyBase
  • heterochromatin maintenance involved in chromatin silencing Source: FlyBase
  • lateral inhibition Source: FlyBase
  • mitotic nuclear envelope reassembly Source: FlyBase
  • negative regulation of cell proliferation Source: FlyBase
  • negative regulation of immune response Source: FlyBase
  • nuclear envelope organization Source: FlyBase
  • nuclear membrane organization Source: FlyBase
  • nuclear migration Source: FlyBase
  • nuclear pore distribution Source: FlyBase
  • nucleus organization Source: UniProtKB
  • protein localization to nuclear envelope Source: FlyBase
  • spermatogenesis Source: FlyBase
  • terminal branching, open tracheal system Source: FlyBase
Complete GO annotation...

Enzyme and pathway databases

ReactomeiR-DME-352238. Breakdown of the nuclear lamina.
R-DME-4419969. Depolymerisation of the Nuclear Lamina.

Names & Taxonomyi

Protein namesi
Recommended name:
Lamin Dm0
Gene namesi
Name:LamImported
ORF Names:CG6944Imported
OrganismiDrosophila melanogaster (Fruit fly)
Taxonomic identifieri7227 [NCBI]
Taxonomic lineageiEukaryotaMetazoaEcdysozoaArthropodaHexapodaInsectaPterygotaNeopteraEndopterygotaDipteraBrachyceraMuscomorphaEphydroideaDrosophilidaeDrosophilaSophophora
Proteomesi
  • UP000000803 Componenti: Chromosome 2L

Organism-specific databases

FlyBaseiFBgn0002525. Lam.

Subcellular locationi

GO - Cellular componenti

  • centrosome Source: FlyBase
  • cytoplasm Source: UniProtKB-SubCell
  • lamin filament Source: FlyBase
  • lipid particle Source: FlyBase
  • microtubule associated complex Source: FlyBase
  • mitotic spindle Source: FlyBase
  • nuclear envelope Source: FlyBase
  • nuclear inner membrane Source: UniProtKB-SubCell
  • nuclear lamina Source: FlyBase
  • nucleus Source: FlyBase
  • spindle pole Source: UniProtKB-SubCell
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm, Cytoskeleton, Intermediate filament, Membrane, Nucleus

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Initiator methionineiRemovedBy similarity
ChainiPRO_00000638282 – 619Lamin Dm0Add BLAST618
PropeptideiPRO_0000396785620 – 622Removed in mature formBy similarity3

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei2N-acetylserineBy similarity1
Modified residuei10Phosphothreonine2 Publications1
Modified residuei12Phosphothreonine2 Publications1
Modified residuei20Phosphothreonine2 Publications1
Modified residuei25Phosphoserine2 Publications1
Modified residuei34Phosphoserine2 Publications1
Modified residuei39Phosphothreonine2 Publications1
Modified residuei41Phosphoserine2 Publications1
Modified residuei42Phosphoserine2 Publications1
Modified residuei45Phosphoserine2 Publications1
Modified residuei47Phosphothreonine2 Publications1
Modified residuei235Phosphoserine2 Publications1
Modified residuei249Phosphotyrosine2 Publications1
Modified residuei250Phosphoserine2 Publications1
Modified residuei311Phosphoserine2 Publications1
Modified residuei413Phosphothreonine2 Publications1
Modified residuei435Phosphothreonine2 Publications1
Modified residuei442Phosphoserine2 Publications1
Modified residuei455Phosphoserine2 Publications1
Modified residuei459Phosphoserine1 Publication1
Modified residuei595Phosphoserine2 Publications1
Modified residuei597Phosphothreonine1 Publication1
Modified residuei615Phosphoserine2 Publications1
Modified residuei619Cysteine methyl esterBy similarity1
Lipidationi619S-farnesyl cysteineBy similarity1

Post-translational modificationi

Three forms of lamin have been identified in D.melanogaster, lamin Dm0 is rapidly processed to lamin Dm1 in the cytoplasm, Dm1 is then assembled in the nuclear envelope and is then phosphorylated, forming lamin Dm2.2 Publications

Keywords - PTMi

Acetylation, Lipoprotein, Methylation, Phosphoprotein, Prenylation

Proteomic databases

PaxDbiP08928.
PRIDEiP08928.

PTM databases

iPTMnetiP08928.

Expressioni

Tissue specificityi

Constitutively expressed in all tissues.1 Publication

Developmental stagei

Constitutively expressed in all developmental stages, especially during the first 6-9 hours.1 Publication

Gene expression databases

BgeeiFBgn0002525.
ExpressionAtlasiP08928. baseline.
GenevisibleiP08928. DM.

Interactioni

Subunit structurei

Interacts directly with LBR (PubMed:15054108). Interacts with MAN1 (PubMed:16439308). Interacts with Ote (PubMed:22751930).3 Publications

GO - Molecular functioni

  • receptor binding Source: UniProtKB

Protein-protein interaction databases

BioGridi59950. 15 interactors.
DIPiDIP-2663N.
IntActiP08928. 15 interactors.
MINTiMINT-853541.
STRINGi7227.FBpp0078733.

Structurei

3D structure databases

ProteinModelPortaliP08928.
SMRiP08928.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Domaini465 – 578LTDAdd BLAST114

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni2 – 56HeadAdd BLAST55
Regioni55 – 91Coil 1AAdd BLAST37
Regioni57 – 408RodAdd BLAST352
Regioni92 – 103Linker 1Add BLAST12
Regioni104 – 241Coil 1BAdd BLAST138
Regioni242 – 265Linker 2Add BLAST24
Regioni266 – 408Coil 2Add BLAST143
Regioni409 – 619TailAdd BLAST211

Motif

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Motifi446 – 451Nuclear localization signalSequence analysis6

Compositional bias

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Compositional biasi28 – 33Poly-Pro6

Sequence similaritiesi

Belongs to the intermediate filament family.Curated
Contains 1 LTD domain.Curated

Keywords - Domaini

Coiled coil

Phylogenomic databases

eggNOGiKOG0977. Eukaryota.
ENOG410Y2H6. LUCA.
GeneTreeiENSGT00830000128282.
InParanoidiP08928.
KOiK07611.
OMAiSQYEEQM.
OrthoDBiEOG091G05LK.
PhylomeDBiP08928.

Family and domain databases

Gene3Di2.60.40.1260. 1 hit.
InterProiIPR001664. IF.
IPR001322. Lamin_tail_dom.
[Graphical view]
PANTHERiPTHR23239. PTHR23239. 1 hit.
PfamiPF00038. Filament. 1 hit.
PF00932. LTD. 1 hit.
[Graphical view]
SMARTiSM01391. Filament. 1 hit.
[Graphical view]
SUPFAMiSSF74853. SSF74853. 1 hit.

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

P08928-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MSSKSRRAGT ATPQPGNTST PRPPSAGPQP PPPSTHSQTA SSPLSPTRHS
60 70 80 90 100
RVAEKVELQN LNDRLATYID RVRNLETENS RLTIEVQTTR DTVTRETTNI
110 120 130 140 150
KNIFEAELLE TRRLLDDTAR DRARAEIDIK RLWEENEELK NKLDKKTKEC
160 170 180 190 200
TTAEGNVRMY ESRANELNNK YNQANADRKK LNEDLNEALK ELERLRKQFE
210 220 230 240 250
ETRKNLEQET LSRVDLENTI QSLREELSFK DQIHSQEINE SRRIKQTEYS
260 270 280 290 300
EIDGRLSSEY DAKLKQSLQE LRAQYEEQMQ INRDEIQSLY EDKIQRLQEA
310 320 330 340 350
AARTSNSTHK SIEELRSTRV RIDALNANIN ELEQANADLN ARIRDLERQL
360 370 380 390 400
DNDRERHGQE IDLLEKELIR LREEMTQQLK EYQDLMDIKV SLDLEIAAYD
410 420 430 440 450
KLLVGEEARL NITPATNTAT VQSFSQSLRN STRATPSRRT PSAAVKRKRA
460 470 480 490 500
VVDESEDHSV ADYYVSASAK GNVEIKEIDP EGKFVRLFNK GSEEVAIGGW
510 520 530 540 550
QLQRLINEKG PSTTYKFHRS VRIEPNGVIT VWSADTKASH EPPSSLVMKS
560 570 580 590 600
QKWVSADNTR TILLNSEGEA VANLDRIKRI VSQHTSSSRL SRRRSVTAVD
610 620
GNEQLYHQQG DPQQSNEKCA IM
Length:622
Mass (Da):71,300
Last modified:October 25, 2005 - v4
Checksum:iB77E48AA5CD9A8BD
GO

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sequence conflicti135E → R in CAA30259 (PubMed:3126192).Curated1
Sequence conflicti270 – 271EL → DV in CAA30259 (PubMed:3126192).Curated2
Sequence conflicti290Y → I in CAA30259 (PubMed:3126192).Curated1
Sequence conflicti290Y → I in CAA34351 (PubMed:3126192).Curated1

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X07278 mRNA. Translation: CAA30259.1.
X16275 Genomic DNA. Translation: CAA34351.1.
AE014134 Genomic DNA. Translation: AAF52262.1.
BT001506 mRNA. Translation: AAN71261.1.
PIRiA29965.
A37103.
RefSeqiNP_001245892.1. NM_001258963.2.
NP_001245893.1. NM_001258964.2.
NP_001285629.1. NM_001298700.1.
NP_476616.1. NM_057268.5.
UniGeneiDm.312.

Genome annotation databases

EnsemblMetazoaiFBtr0079100; FBpp0078733; FBgn0002525.
FBtr0307058; FBpp0297901; FBgn0002525.
FBtr0307059; FBpp0297902; FBgn0002525.
FBtr0346460; FBpp0312110; FBgn0002525.
GeneIDi33782.
KEGGidme:Dmel_CG6944.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X07278 mRNA. Translation: CAA30259.1.
X16275 Genomic DNA. Translation: CAA34351.1.
AE014134 Genomic DNA. Translation: AAF52262.1.
BT001506 mRNA. Translation: AAN71261.1.
PIRiA29965.
A37103.
RefSeqiNP_001245892.1. NM_001258963.2.
NP_001245893.1. NM_001258964.2.
NP_001285629.1. NM_001298700.1.
NP_476616.1. NM_057268.5.
UniGeneiDm.312.

3D structure databases

ProteinModelPortaliP08928.
SMRiP08928.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi59950. 15 interactors.
DIPiDIP-2663N.
IntActiP08928. 15 interactors.
MINTiMINT-853541.
STRINGi7227.FBpp0078733.

PTM databases

iPTMnetiP08928.

Proteomic databases

PaxDbiP08928.
PRIDEiP08928.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblMetazoaiFBtr0079100; FBpp0078733; FBgn0002525.
FBtr0307058; FBpp0297901; FBgn0002525.
FBtr0307059; FBpp0297902; FBgn0002525.
FBtr0346460; FBpp0312110; FBgn0002525.
GeneIDi33782.
KEGGidme:Dmel_CG6944.

Organism-specific databases

CTDi33782.
FlyBaseiFBgn0002525. Lam.

Phylogenomic databases

eggNOGiKOG0977. Eukaryota.
ENOG410Y2H6. LUCA.
GeneTreeiENSGT00830000128282.
InParanoidiP08928.
KOiK07611.
OMAiSQYEEQM.
OrthoDBiEOG091G05LK.
PhylomeDBiP08928.

Enzyme and pathway databases

ReactomeiR-DME-352238. Breakdown of the nuclear lamina.
R-DME-4419969. Depolymerisation of the Nuclear Lamina.

Miscellaneous databases

GenomeRNAii33782.
PROiP08928.

Gene expression databases

BgeeiFBgn0002525.
ExpressionAtlasiP08928. baseline.
GenevisibleiP08928. DM.

Family and domain databases

Gene3Di2.60.40.1260. 1 hit.
InterProiIPR001664. IF.
IPR001322. Lamin_tail_dom.
[Graphical view]
PANTHERiPTHR23239. PTHR23239. 1 hit.
PfamiPF00038. Filament. 1 hit.
PF00932. LTD. 1 hit.
[Graphical view]
SMARTiSM01391. Filament. 1 hit.
[Graphical view]
SUPFAMiSSF74853. SSF74853. 1 hit.
ProtoNetiSearch...

Entry informationi

Entry nameiLAM0_DROME
AccessioniPrimary (citable) accession number: P08928
Secondary accession number(s): Q9VMQ0
Entry historyi
Integrated into UniProtKB/Swiss-Prot: November 1, 1988
Last sequence update: October 25, 2005
Last modified: November 30, 2016
This is version 154 of the entry and version 4 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.