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P48678

- LMNA_MOUSE

UniProt

P48678 - LMNA_MOUSE

Protein

Prelamin-A/C

Gene

Lmna

Organism
Mus musculus (Mouse)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 142 (01 Oct 2014)
      Sequence version 2 (24 Jan 2006)
      Previous versions | rss
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    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. Lamin A and C are present in equal amounts in the lamina of mammals. Plays an important role in nuclear assembly, chromatin organization, nuclear membrane and telomere dynamics. Required for normal development of peripheral nervous system and skeletal muscle and for muscle satellite cell proliferation. Required for osteoblastogenesis and bone formation. Also prevents fat infiltration of muscle and bone marrow, helping to maintain the volume and strength of skeletal muscle and bone. Isoform C2 may have a role in determining the organization of nuclear and chromosomal structures during spermatogenesis.6 Publications
    Prelamin-A/C can accelerate smooth muscle cell senescence. It acts to disrupt mitosis and induce DNA damage in vascular smooth muscle cells (VSMCs), leading to mitotic failure, genomic instability, and premature senescence By similarity.By similarity

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sitei266 – 2661Heptad change of phase
    Sitei325 – 3251StutterBy similarity
    Sitei330 – 3301Heptad change of phase
    Sitei647 – 6482Cleavage; by endoproteaseBy similarity

    GO - Molecular functioni

    1. protein binding Source: MGI
    2. structural molecule activity Source: InterPro

    GO - Biological processi

    1. cellular response to hypoxia Source: BHF-UCL
    2. establishment of cell polarity Source: BHF-UCL
    3. establishment or maintenance of microtubule cytoskeleton polarity Source: BHF-UCL
    4. muscle organ development Source: BHF-UCL
    5. negative regulation of extrinsic apoptotic signaling pathway Source: MGI
    6. negative regulation of release of cytochrome c from mitochondria Source: MGI
    7. nuclear envelope organization Source: MGI
    8. nucleus organization Source: MGI
    9. positive regulation of cell aging Source: UniProtKB
    10. protein localization to nucleus Source: UniProtKB
    11. regulation of cell migration Source: BHF-UCL
    12. regulation of protein localization to nucleus Source: MGI
    13. sterol regulatory element binding protein import into nucleus Source: MGI
    14. ventricular cardiac muscle cell development Source: MGI

    Enzyme and pathway databases

    ReactomeiREACT_106572. XBP1(S) activates chaperone genes.
    REACT_198626. Meiotic synapsis.
    REACT_208718. Depolymerisation of the Nuclear Lamina.
    REACT_209025. Breakdown of the nuclear lamina.
    REACT_210180. Initiation of Nuclear Envelope Reformation.
    REACT_221677. Clearance of Nuclear Envelope Membranes from Chromatin.
    REACT_75800. Meiotic Synapsis.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Prelamin-A/C
    Cleaved into the following chain:
    Gene namesi
    Name:Lmna
    Synonyms:Lmn1
    OrganismiMus musculus (Mouse)
    Taxonomic identifieri10090 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
    ProteomesiUP000000589: Chromosome 3

    Organism-specific databases

    MGIiMGI:96794. Lmna.

    Subcellular locationi

    Nucleus. Nucleus envelope. Nucleus lamina By similarity. Nucleusnucleoplasm By similarity
    Note: Farnesylation of prelamin-A/C facilitates nuclear envelope targeting and subsequent cleaveage by ZMPSTE24/FACE1 to remove the farnesyl group produces mature lamin-A/C, which can then be inserted into the nuclear lamina. EMD is required for proper localization of non-farnesylated prelamin-A/C By similarity.By similarity

    GO - Cellular componenti

    1. lamin filament Source: MGI
    2. nuclear envelope Source: UniProtKB
    3. nucleoplasm Source: UniProtKB-SubCell
    4. nucleus Source: BHF-UCL
    5. perinuclear region of cytoplasm Source: BHF-UCL

    Keywords - Cellular componenti

    Intermediate filament, Nucleus

    Pathology & Biotechi

    Disruption phenotypei

    Mutant mice survive postnatally for 6-8 weeks and show skeletal and cardiac myopathy, sarcopenia, osteopenia, decreased bone formation, neuropathy, abnormal neuromuscular junctions, decreased skeletal muscle growth and decreased muscle satellite cell proliferation. Within 2-3 weeks they show a reduction in their growth rate and by week 4 their growth ceases with their mean body weight being half of that of the wild-type or the heterozygous littermates. Simultaneous knockout of Lmna and Lap2 results in partial rescue of the phenotype, with a 30% increase in survival rate and a 25-50% increase in body weight.6 Publications

    Mutagenesis

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Mutagenesisi201 – 2011K → L: Decreased sumoylation; aberrant localization with decreased nuclear rim staining and formation of intranuclear foci; associated with increased cell death. 1 Publication
    Mutagenesisi203 – 2031E → G or K: Decreased sumoylation; aberrant localization with decreased nuclear rim staining and formation of intranuclear foci; associated with increased cell death. 1 Publication

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 662662Prelamin-A/CPRO_0000398837Add
    BLAST
    Chaini1 – 647647Lamin-A/CPRO_0000063811Add
    BLAST
    Propeptidei648 – 66215Removed in Lamin-A/C formPRO_0000398838Add
    BLAST
    Propeptidei663 – 6653Removed in Prelamin-A/C form and in Lamin-A/C formPRO_0000403443

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei1 – 11N-acetylmethionineBy similarity
    Modified residuei3 – 31PhosphothreonineBy similarity
    Modified residuei12 – 121PhosphoserineBy similarity
    Modified residuei18 – 181PhosphoserineBy similarity
    Modified residuei19 – 191Phosphothreonine1 Publication
    Modified residuei22 – 221Phosphoserine2 Publications
    Modified residuei32 – 321N6-acetyllysine; alternate1 Publication
    Modified residuei32 – 321N6-succinyllysine; alternate1 Publication
    Modified residuei108 – 1081N6-acetyllysineBy similarity
    Modified residuei123 – 1231N6-acetyllysine1 Publication
    Modified residuei135 – 1351N6-acetyllysine1 Publication
    Modified residuei155 – 1551N6-acetyllysine1 Publication
    Modified residuei171 – 1711N6-acetyllysine; alternate1 Publication
    Modified residuei171 – 1711N6-succinyllysine; alternate1 Publication
    Modified residuei201 – 2011N6-acetyllysine; alternate1 Publication
    Cross-linki201 – 201Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO); alternateBy similarity
    Modified residuei212 – 2121PhosphoserineBy similarity
    Modified residuei260 – 2601N6-acetyllysine1 Publication
    Modified residuei270 – 2701N6-acetyllysine1 Publication
    Modified residuei277 – 2771PhosphoserineBy similarity
    Modified residuei301 – 3011PhosphoserineBy similarity
    Modified residuei311 – 3111N6-acetyllysine1 Publication
    Modified residuei390 – 3901Phosphoserine1 Publication
    Modified residuei392 – 3921Phosphoserine; by CDK12 Publications
    Modified residuei395 – 3951PhosphoserineBy similarity
    Modified residuei404 – 4041PhosphoserineBy similarity
    Modified residuei407 – 4071Phosphoserine1 Publication
    Modified residuei409 – 4091Phosphoserine1 Publication
    Modified residuei414 – 4141PhosphoserineBy similarity
    Modified residuei431 – 4311PhosphoserineBy similarity
    Modified residuei450 – 4501N6-acetyllysine1 Publication
    Modified residuei457 – 4571N6-acetyllysine1 Publication
    Modified residuei458 – 4581PhosphoserineBy similarity
    Modified residuei463 – 4631PhosphoserineBy similarity
    Modified residuei496 – 4961PhosphothreonineBy similarity
    Modified residuei500 – 5001PhosphoserineBy similarity
    Modified residuei505 – 5051PhosphothreonineBy similarity
    Modified residuei510 – 5101PhosphothreonineBy similarity
    Modified residuei546 – 5461Phosphoserine1 Publication
    Modified residuei629 – 6291PhosphoserineBy similarity
    Modified residuei633 – 6331PhosphoserineBy similarity
    Modified residuei637 – 6371PhosphoserineBy similarity
    Modified residuei653 – 6531Phosphoserine1 Publication
    Modified residuei662 – 6621Cysteine methyl esterBy similarity
    Lipidationi662 – 6621S-farnesyl cysteineBy similarity

    Post-translational modificationi

    Proteolytic cleavage of the C-terminal of 18 residues of prelamin-A/C results in the production of lamin-A/C. The prelamin-A/C maturation pathway includes farnesylation of CAAX motif, ZMPSTE24/FACE1 mediated cleavage of the last three amino acids, methylation of the C-terminal cysteine and endoproteolytic removal of the last 15 C-terminal amino acids. Proteolytic cleavage requires prior farnesylation and methylation, and absence of these blocks cleavage By similarity.By similarity
    Sumoylation is necessary for the localization to the nuclear envelope.By similarity
    Farnesylation of prelamin-A/C facilitates nuclear envelope targeting.By similarity
    Increased phosphorylation of the lamins occurs before envelope disintegration and probably plays a role in regulating lamin associations.
    Isoform C is phosphorylated on Ser-392, Ser-407 and Ser-409 at interphase.2 Publications
    The N-terminus is blocked.

    Keywords - PTMi

    Acetylation, Isopeptide bond, Lipoprotein, Methylation, Phosphoprotein, Prenylation, Ubl conjugation

    Proteomic databases

    MaxQBiP48678.
    PaxDbiP48678.
    PRIDEiP48678.

    2D gel databases

    REPRODUCTION-2DPAGEIPI00400300.
    IPI00620256.

    PTM databases

    PhosphoSiteiP48678.

    Expressioni

    Tissue specificityi

    Expressed in liver and in bone marrow (at protein level). Isoform C2 is specifically expressed in germ cells.2 Publications

    Gene expression databases

    ArrayExpressiP48678.
    BgeeiP48678.
    CleanExiMM_LMNA.
    GenevestigatoriP48678.

    Interactioni

    Subunit structurei

    Homodimer of lamin A and lamin C. Interacts with lamin-associated polypeptides IA, IB and TMPO-alpha, RB1 and with emerin. Proteolytically processed isoform A interacts with NARF By similarity. Interacts with SREBF1, SREBF2, SUN1, SUN2 and TMEM43. Prelamin-A/C interacts with EMD. Interacts with DMPK; may regulate nuclear envelope stability By similarity. Interacts with MLIP; may regulate MLIP localization to the nucleus envelope. Interacts with SUV39H1; the interaction increases stability of SUV39H1.By similarity8 Publications

    Protein-protein interaction databases

    BioGridi201176. 60 interactions.
    IntActiP48678. 7 interactions.
    MINTiMINT-1868521.
    STRINGi10090.ENSMUSP00000029699.

    Structurei

    Secondary structure

    1
    665
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Beta strandi417 – 4204
    Beta strandi433 – 4364
    Beta strandi438 – 4458
    Beta strandi449 – 4568
    Beta strandi458 – 4603
    Beta strandi468 – 4736
    Beta strandi479 – 4824
    Beta strandi494 – 50310
    Turni508 – 5103
    Beta strandi511 – 5144
    Beta strandi516 – 5183
    Beta strandi523 – 5319
    Beta strandi533 – 5353
    Beta strandi537 – 5448

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    1UFGNMR-A408-545[»]
    ProteinModelPortaliP48678.
    SMRiP48678. Positions 313-386, 415-546.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiP48678.

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini432 – 544113LTDAdd
    BLAST

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni1 – 130130Interaction with MLIPBy similarityAdd
    BLAST
    Regioni1 – 3333HeadAdd
    BLAST
    Regioni34 – 383350RodAdd
    BLAST
    Regioni34 – 7037Coil 1AAdd
    BLAST
    Regioni71 – 8010Linker 1
    Regioni81 – 218138Coil 1BAdd
    BLAST
    Regioni219 – 24224Linker 2Add
    BLAST
    Regioni243 – 383141Coil 2Add
    BLAST
    Regioni384 – 665282TailAdd
    BLAST

    Motif

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Motifi417 – 4226Nuclear localization signalSequence Analysis

    Sequence similaritiesi

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

    Keywords - Domaini

    Coiled coil

    Phylogenomic databases

    eggNOGiNOG325506.
    GeneTreeiENSGT00750000117244.
    HOVERGENiHBG013015.
    InParanoidiP48678.
    KOiK12641.
    OMAiHCSGSGD.
    OrthoDBiEOG7MD4PW.
    PhylomeDBiP48678.
    TreeFamiTF101181.

    Family and domain databases

    Gene3Di2.60.40.1260. 1 hit.
    InterProiIPR001664. IF.
    IPR018039. Intermediate_filament_CS.
    IPR001322. Lamin_tail_dom.
    [Graphical view]
    PANTHERiPTHR23239. PTHR23239. 1 hit.
    PfamiPF00038. Filament. 1 hit.
    PF00932. LTD. 1 hit.
    [Graphical view]
    SUPFAMiSSF74853. SSF74853. 1 hit.
    PROSITEiPS00226. IF. 1 hit.
    [Graphical view]

    Sequences (3)i

    Sequence statusi: Complete.

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

    This entry describes 3 isoformsi produced by alternative splicing. Align

    Note: Isoform A and isoform C are present in equal amounts in the lamina of mammals.

    Isoform A (identifier: P48678-1) [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

    METPSQRRAT RSGAQASSTP LSPTRITRLQ EKEDLQELND RLAVYIDRVR    50
    SLETENAGLR LRITESEEVV SREVSGIKAA YEAELGDARK TLDSVAKERA 100
    RLQLELSKVR EEFKELKARN TKKEGDLLAA QARLKDLEAL LNSKEAALST 150
    ALSEKRTLEG ELHDLRGQVA KLEAALGEAK KQLQDEMLRR VDAENRLQTL 200
    KEELDFQKNI YSEELRETKR RHETRLVEID NGKQREFESR LADALQELRA 250
    QHEDQVEQYK KELEKTYSAK LDNARQSAER NSNLVGAAHE ELQQSRIRID 300
    SLSAQLSQLQ KQLAAKEAKL RDLEDSLARE RDTSRRLLAE KEREMAEMRA 350
    RMQQQLDEYQ ELLDIKLALD MEIHAYRKLL EGEEERLRLS PSPTSQRSRG 400
    RASSHSSQSQ GGGSVTKKRK LESSESRSSF SQHARTSGRV AVEEVDEEGK 450
    FVRLRNKSNE DQSMGNWQIR RQNGDDPLMT YRFPPKFTLK AGQVVTIWAS 500
    GAGATHSPPT DLVWKAQNTW GCGSSLRTAL INSTGEEVAM RKLVRSLTMV 550
    EDNEDDDEDG EELLHHHRGS HCSGSGDPAE YNLRSRTVLC GTCGQPADKA 600
    AGGAGAQVGG SISSGSSASS VTVTRSFRSV GGSGGGSFGD NLVTRSYLLG 650
    NSSPRSQSSQ NCSIM 665
    Length:665
    Mass (Da):74,238
    Last modified:January 24, 2006 - v2
    Checksum:i5434F574803FCB15
    GO
    Isoform C (identifier: P48678-2) [UniParc] [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         569-574: GSHCSG → VSGSRR
         575-665: Missing.

    Show »
    Length:574
    Mass (Da):65,446
    Checksum:iA736DF1CCEDB65BE
    GO
    Isoform C2 (identifier: P48678-3) [UniParc] [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         1-112: Missing.
         113-118: FKELKA → MGNAEG
         569-574: GSHCSG → VSGSRR
         575-665: Missing.

    Show »
    Length:462
    Mass (Da):52,652
    Checksum:i4A12573CECAA93AA
    GO

    Sequence cautioni

    The sequence BAE31539.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally shortened.

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti4 – 41P → S in BAE31384. (PubMed:16141072)Curated
    Sequence conflicti4 – 41P → S in BAE29519. (PubMed:16141072)Curated
    Sequence conflicti118 – 1192AR → VC in CAA32372. (PubMed:2719959)Curated
    Sequence conflicti118 – 1181A → D in BAE39876. (PubMed:16141072)Curated
    Sequence conflicti340 – 3401E → G in BAE29614. (PubMed:16141072)Curated
    Sequence conflicti401 – 4011R → P in CAA32372. (PubMed:2719959)Curated
    Sequence conflicti439 – 4402RV → WL in CAA32372. (PubMed:2719959)Curated
    Sequence conflicti450 – 4501K → E in BAE31384. (PubMed:16141072)Curated
    Sequence conflicti453 – 4531R → L in BAE36246. (PubMed:16141072)Curated
    Sequence conflicti612 – 6121I → V in BAB23415. (PubMed:16141072)Curated
    Sequence conflicti617 – 6171S → Y in BAB23415. (PubMed:16141072)Curated
    Sequence conflicti623 – 6231V → A in BAA02476. (PubMed:7916626)Curated

    Alternative sequence

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Alternative sequencei1 – 112112Missing in isoform C2. 1 PublicationVSP_002471Add
    BLAST
    Alternative sequencei113 – 1186FKELKA → MGNAEG in isoform C2. 1 PublicationVSP_002472
    Alternative sequencei569 – 5746GSHCSG → VSGSRR in isoform C and isoform C2. 4 PublicationsVSP_017064
    Alternative sequencei575 – 66591Missing in isoform C and isoform C2. 4 PublicationsVSP_017065Add
    BLAST

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    D49733 Genomic DNA. Translation: BAA08569.1.
    D49733 Genomic DNA. Translation: BAA08570.1.
    D49733 Genomic DNA. Translation: BAA08571.1.
    X14170 mRNA. Translation: CAA32372.1.
    D14850 mRNA. Translation: BAA03578.1.
    DQ832702 mRNA. Translation: ABI16251.1.
    DQ832703 mRNA. Translation: ABI16252.1.
    AK004619 mRNA. Translation: BAB23415.1.
    AK147150 mRNA. Translation: BAE27717.1.
    AK149998 mRNA. Translation: BAE29226.1.
    AK150391 mRNA. Translation: BAE29519.1.
    AK150501 mRNA. Translation: BAE29614.1.
    AK150624 mRNA. Translation: BAE29714.1.
    AK152539 mRNA. Translation: BAE31294.1.
    AK152646 mRNA. Translation: BAE31384.1.
    AK152846 mRNA. Translation: BAE31539.1. Different initiation.
    AK161221 mRNA. Translation: BAE36246.1.
    AK167858 mRNA. Translation: BAE39876.1.
    CH466547 Genomic DNA. Translation: EDL15275.1.
    BC015302 mRNA. Translation: AAH15302.1.
    BC094020 mRNA. Translation: AAH94020.1.
    D13181 mRNA. Translation: BAA02476.1.
    CCDSiCCDS38482.1. [P48678-1]
    CCDS38483.1. [P48678-3]
    CCDS50951.1. [P48678-2]
    PIRiI53414.
    S04333.
    S18324.
    S28182.
    RefSeqiNP_001002011.2. NM_001002011.3. [P48678-1]
    NP_001104572.1. NM_001111102.2. [P48678-2]
    NP_062263.1. NM_019390.3. [P48678-3]
    XP_006501136.1. XM_006501073.1. [P48678-1]
    UniGeneiMm.243014.
    Mm.471227.

    Genome annotation databases

    EnsembliENSMUST00000029699; ENSMUSP00000029699; ENSMUSG00000028063. [P48678-1]
    ENSMUST00000036252; ENSMUSP00000040265; ENSMUSG00000028063. [P48678-3]
    ENSMUST00000120377; ENSMUSP00000113093; ENSMUSG00000028063. [P48678-2]
    GeneIDi16905.
    KEGGimmu:16905.
    UCSCiuc008pvj.2. mouse. [P48678-1]
    uc008pvk.2. mouse. [P48678-3]

    Keywords - Coding sequence diversityi

    Alternative splicing

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    D49733 Genomic DNA. Translation: BAA08569.1 .
    D49733 Genomic DNA. Translation: BAA08570.1 .
    D49733 Genomic DNA. Translation: BAA08571.1 .
    X14170 mRNA. Translation: CAA32372.1 .
    D14850 mRNA. Translation: BAA03578.1 .
    DQ832702 mRNA. Translation: ABI16251.1 .
    DQ832703 mRNA. Translation: ABI16252.1 .
    AK004619 mRNA. Translation: BAB23415.1 .
    AK147150 mRNA. Translation: BAE27717.1 .
    AK149998 mRNA. Translation: BAE29226.1 .
    AK150391 mRNA. Translation: BAE29519.1 .
    AK150501 mRNA. Translation: BAE29614.1 .
    AK150624 mRNA. Translation: BAE29714.1 .
    AK152539 mRNA. Translation: BAE31294.1 .
    AK152646 mRNA. Translation: BAE31384.1 .
    AK152846 mRNA. Translation: BAE31539.1 . Different initiation.
    AK161221 mRNA. Translation: BAE36246.1 .
    AK167858 mRNA. Translation: BAE39876.1 .
    CH466547 Genomic DNA. Translation: EDL15275.1 .
    BC015302 mRNA. Translation: AAH15302.1 .
    BC094020 mRNA. Translation: AAH94020.1 .
    D13181 mRNA. Translation: BAA02476.1 .
    CCDSi CCDS38482.1. [P48678-1 ]
    CCDS38483.1. [P48678-3 ]
    CCDS50951.1. [P48678-2 ]
    PIRi I53414.
    S04333.
    S18324.
    S28182.
    RefSeqi NP_001002011.2. NM_001002011.3. [P48678-1 ]
    NP_001104572.1. NM_001111102.2. [P48678-2 ]
    NP_062263.1. NM_019390.3. [P48678-3 ]
    XP_006501136.1. XM_006501073.1. [P48678-1 ]
    UniGenei Mm.243014.
    Mm.471227.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    1UFG NMR - A 408-545 [» ]
    ProteinModelPortali P48678.
    SMRi P48678. Positions 313-386, 415-546.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 201176. 60 interactions.
    IntActi P48678. 7 interactions.
    MINTi MINT-1868521.
    STRINGi 10090.ENSMUSP00000029699.

    PTM databases

    PhosphoSitei P48678.

    2D gel databases

    REPRODUCTION-2DPAGE IPI00400300.
    IPI00620256.

    Proteomic databases

    MaxQBi P48678.
    PaxDbi P48678.
    PRIDEi P48678.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENSMUST00000029699 ; ENSMUSP00000029699 ; ENSMUSG00000028063 . [P48678-1 ]
    ENSMUST00000036252 ; ENSMUSP00000040265 ; ENSMUSG00000028063 . [P48678-3 ]
    ENSMUST00000120377 ; ENSMUSP00000113093 ; ENSMUSG00000028063 . [P48678-2 ]
    GeneIDi 16905.
    KEGGi mmu:16905.
    UCSCi uc008pvj.2. mouse. [P48678-1 ]
    uc008pvk.2. mouse. [P48678-3 ]

    Organism-specific databases

    CTDi 4000.
    MGIi MGI:96794. Lmna.

    Phylogenomic databases

    eggNOGi NOG325506.
    GeneTreei ENSGT00750000117244.
    HOVERGENi HBG013015.
    InParanoidi P48678.
    KOi K12641.
    OMAi HCSGSGD.
    OrthoDBi EOG7MD4PW.
    PhylomeDBi P48678.
    TreeFami TF101181.

    Enzyme and pathway databases

    Reactomei REACT_106572. XBP1(S) activates chaperone genes.
    REACT_198626. Meiotic synapsis.
    REACT_208718. Depolymerisation of the Nuclear Lamina.
    REACT_209025. Breakdown of the nuclear lamina.
    REACT_210180. Initiation of Nuclear Envelope Reformation.
    REACT_221677. Clearance of Nuclear Envelope Membranes from Chromatin.
    REACT_75800. Meiotic Synapsis.

    Miscellaneous databases

    EvolutionaryTracei P48678.
    NextBioi 290934.
    PROi P48678.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi P48678.
    Bgeei P48678.
    CleanExi MM_LMNA.
    Genevestigatori P48678.

    Family and domain databases

    Gene3Di 2.60.40.1260. 1 hit.
    InterProi IPR001664. IF.
    IPR018039. Intermediate_filament_CS.
    IPR001322. Lamin_tail_dom.
    [Graphical view ]
    PANTHERi PTHR23239. PTHR23239. 1 hit.
    Pfami PF00038. Filament. 1 hit.
    PF00932. LTD. 1 hit.
    [Graphical view ]
    SUPFAMi SSF74853. SSF74853. 1 hit.
    PROSITEi PS00226. IF. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "Genomic structure of the mouse A-type lamin gene locus encoding somatic and germ cell-specific lamins."
      Nakajima N., Abe K.
      FEBS Lett. 365:108-114(1995) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    2. "Nucleotide sequence of the full-length mouse lamin C cDNA and its deduced amino-acid sequence."
      Riedel W., Werner D.
      Biochim. Biophys. Acta 1008:119-122(1989) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM C).
    3. "Identification and cloning of an mRNA coding for a germ cell-specific A-type lamin in mice."
      Furukawa K., Inagaki H., Hotta Y.
      Exp. Cell Res. 212:426-430(1994) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM C2).
      Strain: ddY.
      Tissue: Testis.
    4. "Lamin A binds to Runx2."
      Fujita T.
      Submitted (JUN-2006) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS A AND C).
    5. "The transcriptional landscape of the mammalian genome."
      Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.
      , Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.
      Science 309:1559-1563(2005) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS A AND C).
      Strain: BALB/c and C57BL/6J.
      Tissue: Amnion, Bone marrow, Head and Lung.
    6. Mural R.J., Adams M.D., Myers E.W., Smith H.O., Venter J.C.
      Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    7. "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] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
      Strain: FVB/N.
      Tissue: Kidney and Salivary gland.
    8. "Nucleotide sequence of a mouse lamin A cDNA and its deduced amino acid sequence."
      Nakajima N., Sado T.
      Biochim. Biophys. Acta 1171:311-314(1993) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 235-665 (ISOFORM A).
    9. "Maturation of nuclear lamin A involves a specific carboxy-terminal trimming, which removes the polyisoprenylation site from the precursor; implications for the structure of the nuclear lamina."
      Weber K., Plessmann U., Traub P.
      FEBS Lett. 257:411-414(1989) [PubMed] [Europe PMC] [Abstract]
      Cited for: PROTEIN SEQUENCE OF 521-574, C-TERMINAL PROCESSING OF ISOFORM A.
    10. "Identification of phosphorylation sites on murine nuclear lamin C by RP-HPLC and microsequencing."
      Eggert M., Radomski N., Tripier D., Traub P., Jost E.
      FEBS Lett. 292:205-209(1991) [PubMed] [Europe PMC] [Abstract]
      Cited for: PARTIAL PROTEIN SEQUENCE, PHOSPHORYLATION AT SER-392; SER-407 AND SER-409.
    11. "Loss of A-type lamin expression compromises nuclear envelope integrity leading to muscular dystrophy."
      Sullivan T., Escalante-Alcalde D., Bhatt H., Anver M., Bhat N., Nagashima K., Stewart C.L., Burke B.
      J. Cell Biol. 147:913-920(1999) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, SUBCELLULAR LOCATION, TISSUE SPECIFICITY, DISRUPTION PHENOTYPE.
    12. "Homozygous defects in LMNA, encoding lamin A/C nuclear-envelope proteins, cause autosomal recessive axonal neuropathy in human (Charcot-Marie-Tooth disorder type 2) and mouse."
      De Sandre-Giovannoli A., Chaouch M., Kozlov S., Vallat J.-M., Tazir M., Kassouri N., Szepetowski P., Hammadouche T., Vandenberghe A., Stewart C.L., Grid D., Levy N.
      Am. J. Hum. Genet. 70:726-736(2002) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, DISRUPTION PHENOTYPE.
    13. "A novel interaction between lamin A and SREBP1: implications for partial lipodystrophy and other laminopathies."
      Lloyd D.J., Trembath R.C., Shackleton S.
      Hum. Mol. Genet. 11:769-777(2002) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH SREBF1 AND SREBF2.
    14. "Coupling of the nucleus and cytoplasm: role of the LINC complex."
      Crisp M., Liu Q., Roux K., Rattner J.B., Shanahan C., Burke B., Stahl P.D., Hodzic D.
      J. Cell Biol. 172:41-53(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH SUN1.
    15. "SUN1 interacts with nuclear lamin A and cytoplasmic nesprins to provide a physical connection between the nuclear lamina and the cytoskeleton."
      Haque F., Lloyd D.J., Smallwood D.T., Dent C.L., Shanahan C.M., Fry A.M., Trembath R.C., Shackleton S.
      Mol. Cell. Biol. 26:3738-3751(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH SUN1.
    16. "Comprehensive identification of phosphorylation sites in postsynaptic density preparations."
      Trinidad J.C., Specht C.G., Thalhammer A., Schoepfer R., Burlingame A.L.
      Mol. Cell. Proteomics 5:914-922(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Brain.
    17. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-19; SER-22 AND SER-653, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Liver.
    18. "Sumoylation regulates lamin A function and is lost in lamin A mutants associated with familial cardiomyopathies."
      Zhang Y.Q., Sarge K.D.
      J. Cell Biol. 182:35-39(2008) [PubMed] [Europe PMC] [Abstract]
      Cited for: SUBCELLULAR LOCATION, SUMOYLATION AT LYS-201, MUTAGENESIS OF LYS-201 AND GLU-203.
    19. "LUMA interacts with emerin and influences its distribution at the inner nuclear membrane."
      Bengtsson L., Otto H.
      J. Cell Sci. 121:536-548(2008) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH TMEM43.
    20. "The phagosomal proteome in interferon-gamma-activated macrophages."
      Trost M., English L., Lemieux S., Courcelles M., Desjardins M., Thibault P.
      Immunity 30:143-154(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-22 AND SER-546, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    21. "Lamin A/C-mediated neuromuscular junction defects in Emery-Dreifuss muscular dystrophy."
      Mejat A., Decostre V., Li J., Renou L., Kesari A., Hantai D., Stewart C.L., Xiao X., Hoffman E., Bonne G., Misteli T.
      J. Cell Biol. 184:31-44(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, DISRUPTION PHENOTYPE.
    22. "Dynamics and molecular interactions of linker of nucleoskeleton and cytoskeleton (LINC) complex proteins."
      Ostlund C., Folker E.S., Choi J.C., Gomes E.R., Gundersen G.G., Worman H.J.
      J. Cell Sci. 122:4099-4108(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH SUN1 AND SUN2.
    23. "Large scale localization of protein phosphorylation by use of electron capture dissociation mass spectrometry."
      Sweet S.M., Bailey C.M., Cunningham D.L., Heath J.K., Cooper H.J.
      Mol. Cell. Proteomics 8:904-912(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-390 AND SER-392, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Embryonic fibroblast.
    24. "Mammalian SUN protein interaction networks at the inner nuclear membrane and their role in laminopathy disease processes."
      Haque F., Mazzeo D., Patel J.T., Smallwood D.T., Ellis J.A., Shanahan C.M., Shackleton S.
      J. Biol. Chem. 285:3487-3498(2010) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH SUN2.
    25. "Identification of a novel muscle enriched A-type Lamin interacting protein (MLIP)."
      Ahmady E., Deeke S.A., Rabaa S., Kouri L., Kenney L., Stewart A.F., Burgon P.G.
      J. Biol. Chem. 286:19702-19713(2011) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH MLIP.
    26. "Lamin A/C deficiency is associated with fat infiltration of muscle and bone."
      Tong J., Li W., Vidal C., Yeo L.S., Fatkin D., Duque G.
      Mech. Ageing Dev. 132:552-559(2011) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, DISRUPTION PHENOTYPE.
    27. "Decreased bone formation and osteopenia in lamin a/c-deficient mice."
      Li W., Yeo L.S., Vidal C., McCorquodale T., Herrmann M., Fatkin D., Duque G.
      PLoS ONE 6:E19313-E19313(2011) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, TISSUE SPECIFICITY, DISRUPTION PHENOTYPE.
    28. "SIRT5-mediated lysine desuccinylation impacts diverse metabolic pathways."
      Park J., Chen Y., Tishkoff D.X., Peng C., Tan M., Dai L., Xie Z., Zhang Y., Zwaans B.M., Skinner M.E., Lombard D.B., Zhao Y.
      Mol. Cell 50:919-930(2013) [PubMed] [Europe PMC] [Abstract]
      Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-32; LYS-123; LYS-135; LYS-155; LYS-171; LYS-201; LYS-260; LYS-270; LYS-311; LYS-450 AND LYS-457, SUCCINYLATION [LARGE SCALE ANALYSIS] AT LYS-32 AND LYS-171, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Embryonic fibroblast.
    29. "Depleting the methyltransferase Suv39h1 improves DNA repair and extends lifespan in a progeria mouse model."
      Liu B., Wang Z., Zhang L., Ghosh S., Zheng H., Zhou Z.
      Nat. Commun. 4:1868-1868(2013) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH SUV39H1.
    30. "Defective skeletal muscle growth in lamin A/C-deficient mice is rescued by loss of Lap2alpha."
      Cohen T.V., Gnocchi V.F., Cohen J.E., Phadke A., Liu H., Ellis J.A., Foisner R., Stewart C.L., Zammit P.S., Partridge T.A.
      Hum. Mol. Genet. 22:2852-2869(2013) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, DISRUPTION PHENOTYPE.
    31. "Solution structure of immunoglobulin-like domain of mouse nuclear lamin."
      RIKEN structural genomics initiative (RSGI)
      Submitted (JUN-2004) to the PDB data bank
      Cited for: STRUCTURE BY NMR OF 406-546.

    Entry informationi

    Entry nameiLMNA_MOUSE
    AccessioniPrimary (citable) accession number: P48678
    Secondary accession number(s): B3RH23
    , B3RH24, P11516, P97859, Q3TIH0, Q3TTS8, Q3U733, Q3U7I5, Q3UCA0, Q3UCJ8, Q3UCU3, Q91WF2, Q9DC21
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: February 1, 1996
    Last sequence update: January 24, 2006
    Last modified: October 1, 2014
    This is version 142 of the entry and version 2 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programChordata Protein Annotation Program

    Miscellaneousi

    Miscellaneous

    The structural integrity of the lamina is strictly controlled by the cell cycle, as seen by the disintegration and formation of the nuclear envelope in prophase and telophase, respectively.

    Keywords - Technical termi

    3D-structure, Complete proteome, Direct protein sequencing, Reference proteome

    Documents

    1. MGD cross-references
      Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
    2. PDB cross-references
      Index of Protein Data Bank (PDB) cross-references
    3. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3