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Reviewed, UniProtKB/Swiss-Prot P08928 (LAM0_DROME)

Last modified June 16, 2009. Version 91. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data | Customize display text xml rdf/xml gff fasta
Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Binary interactions · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents

Names and origin

Protein namesRecommended name:
    Lamin Dm0
Gene names
Name: Lam
ORF Names: CG6944
OrganismDrosophila melanogaster (Fruit fly) [Complete proteome]
Taxonomic identifier7227 [NCBI]
Taxonomic lineageEukaryotaMetazoaArthropodaHexapodaInsectaPterygotaNeopteraEndopterygotaDipteraBrachyceraMuscomorphaEphydroideaDrosophilidaeDrosophilaSophophora

Protein attributes

Sequence length622 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is not processed.
Protein existenceEvidence at protein level.

General annotation (Comments)

Function

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. Ref.1

Subunit structure

Interacts directly with LBR. Ref.8

Subcellular location

Nucleus. Note: Nuclear periphery. Ref.7

Tissue specificity

Constitutively expressed in all tissues. Ref.7

Developmental stage

Constitutively expressed in all developmental stages, especially during the first 6-9 hours. Ref.7

Post-translational modification

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. Ref.9

Sequence similarities

Belongs to the intermediate filament family.

Binary interactions

With

Entry

#Exp.

IntAct

Notes

OteP202401EBI-188444,EBI-115143

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 622622Lamin Dm0
PRO_0000063828

Regions

Region1 – 5656Head
Region55 – 9137Coil 1A
Region57 – 408352Rod
Region92 – 10312Linker 1
Region104 – 241138Coil 1B
Region242 – 26524Linker 2
Region266 – 408143Coil 2
Region409 – 622214Tail
Motif446 – 4516Nuclear localization signal Potential
Compositional bias28 – 336Poly-Pro

Sites

Site2891Heptad change of phase
Site3531Heptad change of phase

Amino acid modifications

Modified residue101Phosphothreonine Ref.9
Modified residue121Phosphothreonine Ref.9
Modified residue201Phosphothreonine Ref.9
Modified residue251Phosphoserine Ref.9
Modified residue341Phosphoserine Ref.9
Modified residue391Phosphothreonine Ref.9
Modified residue411Phosphoserine Ref.9
Modified residue421Phosphoserine Ref.9
Modified residue451Phosphoserine Ref.9
Modified residue471Phosphothreonine Ref.9
Modified residue2351Phosphoserine Ref.9
Modified residue2491Phosphotyrosine Ref.9
Modified residue2501Phosphoserine Ref.9
Modified residue3111Phosphoserine Ref.9
Modified residue4131Phosphothreonine Ref.9
Modified residue4351Phosphothreonine Ref.9
Modified residue4421Phosphoserine Ref.9
Modified residue4551Phosphoserine Ref.9
Modified residue4591Phosphoserine Ref.9
Modified residue5951Phosphoserine Ref.9
Modified residue5971Phosphothreonine Ref.9
Modified residue6151Phosphoserine Ref.9
Lipidation6191S-farnesyl cysteine By similarity

Experimental info

Sequence conflict1351E → R in CAA30259. Ref.1
Sequence conflict270 – 2712EL → DV in CAA30259. Ref.1
Sequence conflict2901Y → I in CAA30259. Ref.1
Sequence conflict2901Y → I in CAA34351. Ref.1

Sequences

Sequence LengthMass (Da)Tools
P08928-1 [UniParc].

Last modified October 25, 2005. Version 4.
Checksum: B77E48AA5CD9A8BD

FASTA62271,300
        10         20         30         40         50         60 
MSSKSRRAGT ATPQPGNTST PRPPSAGPQP PPPSTHSQTA SSPLSPTRHS RVAEKVELQN 

        70         80         90        100        110        120 
LNDRLATYID RVRNLETENS RLTIEVQTTR DTVTRETTNI KNIFEAELLE TRRLLDDTAR 

       130        140        150        160        170        180 
DRARAEIDIK RLWEENEELK NKLDKKTKEC TTAEGNVRMY ESRANELNNK YNQANADRKK 

       190        200        210        220        230        240 
LNEDLNEALK ELERLRKQFE ETRKNLEQET LSRVDLENTI QSLREELSFK DQIHSQEINE 

       250        260        270        280        290        300 
SRRIKQTEYS EIDGRLSSEY DAKLKQSLQE LRAQYEEQMQ INRDEIQSLY EDKIQRLQEA 

       310        320        330        340        350        360 
AARTSNSTHK SIEELRSTRV RIDALNANIN ELEQANADLN ARIRDLERQL DNDRERHGQE 

       370        380        390        400        410        420 
IDLLEKELIR LREEMTQQLK EYQDLMDIKV SLDLEIAAYD KLLVGEEARL NITPATNTAT 

       430        440        450        460        470        480 
VQSFSQSLRN STRATPSRRT PSAAVKRKRA VVDESEDHSV ADYYVSASAK GNVEIKEIDP 

       490        500        510        520        530        540 
EGKFVRLFNK GSEEVAIGGW QLQRLINEKG PSTTYKFHRS VRIEPNGVIT VWSADTKASH 

       550        560        570        580        590        600 
EPPSSLVMKS QKWVSADNTR TILLNSEGEA VANLDRIKRI VSQHTSSSRL SRRRSVTAVD 

       610        620 
GNEQLYHQQG DPQQSNEKCA IM 

« Hide

References

« Hide 'large scale' references
[1]"Drosophila nuclear lamin precursor Dm0 is translated from either of two developmentally regulated mRNA species apparently encoded by a single gene."
Gruenbaum Y., Landesman Y., Drees B., Bare J.W., Saumweber H., Paddy M.R., Sedat J.W., Smith D.E., Benton B.M., Fisher P.A.
J. Cell Biol. 106:585-596(1988) [PubMed: 3126192] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, POST-TRANSLATIONAL MODIFICATION.
Tissue: Embryo.
[2]Stuurman N., Maus N., Fisher P.A.
Submitted (JAN-1994) to the EMBL/GenBank/DDBJ databases
Cited for: SEQUENCE REVISION TO 24-39 AND 254-263.
[3]"Molecular analysis of the Drosophila nuclear lamin gene."
Osman M., Paz M., Landesman Y., Fainsod A., Gruenbaum Y.
Genomics 8:217-224(1990) [PubMed: 2123469] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[4]"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. expand/collapse author list , 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: 10731132] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: Berkeley.
[5]"Annotation of the Drosophila melanogaster euchromatic genome: a systematic review."
Misra S., Crosby M.A., Mungall C.J., Matthews B.B., Campbell K.S., Hradecky P., Huang Y., Kaminker J.S., Millburn G.H., Prochnik S.E., Smith C.D., Tupy J.L., Whitfield E.J., Bayraktaroglu L., Berman B.P., Bettencourt B.R., Celniker S.E., de Grey A.D.N.J. expand/collapse author list , Drysdale R.A., Harris N.L., Richter J., Russo S., Schroeder A.J., Shu S.Q., Stapleton M., Yamada C., Ashburner M., Gelbart W.M., Rubin G.M., Lewis S.E.
Genome Biol. 3:RESEARCH0083.1-RESEARCH0083.22(2002) [PubMed: 12537572] [Abstract]
Cited for: GENOME REANNOTATION.
[6]"A Drosophila full-length cDNA resource."
Stapleton M., Carlson J.W., Brokstein P., Yu C., Champe M., George R.A., Guarin H., Kronmiller B., Pacleb J.M., Park S., Wan K.H., Rubin G.M., Celniker S.E.
Genome Biol. 3:RESEARCH0080.1-RESEARCH0080.8(2002) [PubMed: 12537569] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Strain: Berkeley.
Tissue: Embryo.
[7]"Expression of Drosophila lamin C is developmentally regulated: analogies with vertebrate A-type lamins."
Riemer D., Stuurman N., Berrios M., Hunter C., Fisher P.A., Weber K.
J. Cell Sci. 108:3189-3198(1995) [PubMed: 7593280] [Abstract]
Cited for: SUBCELLULAR LOCATION, TISSUE SPECIFICITY, DEVELOPMENTAL STAGE.
[8]"The lamin B receptor of Drosophila melanogaster."
Wagner N., Weber D., Seitz S., Krohne G.
J. Cell Sci. 117:2015-2028(2004) [PubMed: 15054108] [Abstract]
Cited for: SUBUNIT, INTERACTION WITH LBR.
[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: 18327897] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-10; THR-12; THR-20; SER-25; SER-34; THR-39; SER-41; SER-42; SER-45; THR-47; SER-235; TYR-249; SER-250; SER-311; THR-413; THR-435; SER-442; SER-455; SER-459; SER-595; THR-597 AND SER-615, MASS SPECTROMETRY.
Tissue: Embryo.
+Additional computationally mapped references.

Cross-references

Sequence databases

X07278 mRNA. Translation: CAA30259.1.
X16275 Genomic DNA. Translation: CAA34351.1.
AE014134 Genomic DNA. Translation: AAF52262.1.
BT001506 mRNA. Translation: AAN71261.1.
PIRA29965.
A37103.
RefSeqNP_476616.1.
UniGeneDm.312

3D structure databases

HSSPHSSP built from PDB template 1GK7 based on UniProtKB P08670.
ModBaseSearch...

Protein-protein interaction databases

DIPDIP:2663N.
IntActP08928. 11 interactions.

Genome annotation databases

EnsemblFBgn0002525. Drosophila melanogaster. [Contig view]
GeneID33782.
KEGGdme:Dmel_CG6944.
NMPDRfig|7227.3.peg.902.

Organism-specific databases

FlyBaseFBgn0002525. Lam.

Phylogenomic databases

HOGENOMP08928.
OMAP08928. INDEYQS.

Gene expression databases

ArrayExpressP08928.
GermOnlineCG6944. Drosophila melanogaster.

Family and domain databases

InterProIPR016044. F.
IPR001664. IF.
IPR001322. IF_tail_C.
IPR018039. Intermediate_filament_CS.
[Graphical view]
PANTHERPTHR23239. IF. 1 hit.
PfamPF00038. Filament. 1 hit.
PF00932. IF_tail. 1 hit.
[Graphical view]
PROSITEPS00226. IF. False negative.
[Graphical view]
ProtoNetSearch...

Other Resources

NextBio785227.

Entry information

Entry nameLAM0_DROME
AccessionPrimary (citable) accession number: P08928
Secondary accession number(s): Q9VMQ0
Entry history
Integrated into UniProtKB/Swiss-Prot: November 1, 1988
Last sequence update: October 25, 2005
Last modified: June 16, 2009
This is version 91 of the entry and version 4 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation projectDrosophila annotation project

Relevant documents

Drosophila

Drosophila: entries, gene names and cross-references to FlyBase

SIMILARITY comments

Index of protein domains and families

Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Binary interactions · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents