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P48678 (LMNA_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 140. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Alt products·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Prelamin-A/C

Cleaved into the following chain:

  1. Lamin-A/C
Gene names
Name:Lmna
Synonyms:Lmn1
OrganismMus musculus (Mouse) [Reference proteome]
Taxonomic identifier10090 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus

Protein attributes

Sequence length665 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
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. 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. Ref.11 Ref.12 Ref.21 Ref.26 Ref.27 Ref.30

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. Ref.11 Ref.12 Ref.21 Ref.26 Ref.27 Ref.30

Subunit structure

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. Ref.13 Ref.14 Ref.15 Ref.19 Ref.22 Ref.24 Ref.25 Ref.29

Subcellular location

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. Ref.11 Ref.18

Tissue specificity

Expressed in liver and in bone marrow (at protein level). Isoform C2 is specifically expressed in germ cells. Ref.11 Ref.27

Post-translational modification

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.

Sumoylation is necessary for the localization to the nuclear envelope By similarity. Ref.18

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. Ref.10

The N-terminus is blocked.

Disruption phenotype

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. Ref.11 Ref.12 Ref.21 Ref.26 Ref.27 Ref.30

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.

Sequence similarities

Belongs to the intermediate filament family.

Sequence caution

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

Ontologies

Keywords
   Cellular componentIntermediate filament
Nucleus
   Coding sequence diversityAlternative splicing
   DomainCoiled coil
   PTMAcetylation
Isopeptide bond
Lipoprotein
Methylation
Phosphoprotein
Prenylation
Ubl conjugation
   Technical term3D-structure
Complete proteome
Direct protein sequencing
Reference proteome
Gene Ontology (GO)
   Biological_processcellular response to hypoxia

Inferred from sequence or structural similarity. Source: BHF-UCL

establishment of cell polarity

Non-traceable author statement PubMed 17631533. Source: BHF-UCL

establishment or maintenance of microtubule cytoskeleton polarity

Inferred from mutant phenotype PubMed 17631533. Source: BHF-UCL

muscle organ development

Inferred from sequence or structural similarity. Source: BHF-UCL

negative regulation of extrinsic apoptotic signaling pathway

Inferred from mutant phenotype PubMed 21151901. Source: MGI

negative regulation of release of cytochrome c from mitochondria

Inferred from mutant phenotype PubMed 21151901. Source: MGI

nuclear envelope organization

Inferred from genetic interaction PubMed 15608054. Source: MGI

nucleus organization

Inferred from mutant phenotype PubMed 14755333. Source: MGI

positive regulation of cell aging

Inferred from sequence or structural similarity. Source: UniProtKB

protein localization to nucleus

Inferred from mutant phenotype Ref.25. Source: UniProtKB

regulation of cell migration

Inferred from mutant phenotype PubMed 17631533. Source: BHF-UCL

regulation of protein localization to nucleus

Inferred from mutant phenotype PubMed 22349700. Source: MGI

sterol regulatory element binding protein import into nucleus

Inferred from mutant phenotype PubMed 14755333. Source: MGI

ventricular cardiac muscle cell development

Inferred from mutant phenotype PubMed 14755333. Source: MGI

   Cellular_componentlamin filament

Inferred from direct assay PubMed 8032679. Source: MGI

nuclear envelope

Inferred from direct assay Ref.18. Source: UniProtKB

nucleoplasm

Inferred from electronic annotation. Source: UniProtKB-SubCell

nucleus

Inferred from direct assay PubMed 18664494. Source: BHF-UCL

perinuclear region of cytoplasm

Inferred from sequence or structural similarity. Source: BHF-UCL

   Molecular_functionprotein binding

Inferred from physical interaction PubMed 11739632Ref.14PubMed 22349700. Source: MGI

structural molecule activity

Inferred from electronic annotation. Source: InterPro

Complete GO annotation...

Alternative products

This entry describes 3 isoforms produced by alternative splicing. [Align] [Select]

Note: Isoform A and isoform C are present in equal amounts in the lamina of mammals.
Isoform A (identifier: P48678-1)

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.
Isoform C (identifier: P48678-2)

The sequence of this isoform differs from the canonical sequence as follows:
     569-574: GSHCSG → VSGSRR
     575-665: Missing.
Isoform C2 (identifier: P48678-3)

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.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 662662Prelamin-A/C
PRO_0000398837
Chain1 – 647647Lamin-A/C
PRO_0000063811
Propeptide648 – 66215Removed in Lamin-A/C form
PRO_0000398838
Propeptide663 – 6653Removed in Prelamin-A/C form and in Lamin-A/C form
PRO_0000403443

Regions

Region1 – 130130Interaction with MLIP By similarity
Region1 – 3333Head
Region34 – 383350Rod
Region34 – 7037Coil 1A
Region71 – 8010Linker 1
Region81 – 218138Coil 1B
Region219 – 24224Linker 2
Region243 – 383141Coil 2
Region384 – 665282Tail
Motif417 – 4226Nuclear localization signal Potential

Sites

Site2661Heptad change of phase
Site3251Stutter By similarity
Site3301Heptad change of phase
Site647 – 6482Cleavage; by endoprotease By similarity

Amino acid modifications

Modified residue11N-acetylmethionine By similarity
Modified residue31Phosphothreonine By similarity
Modified residue121Phosphoserine By similarity
Modified residue181Phosphoserine By similarity
Modified residue191Phosphothreonine Ref.17
Modified residue221Phosphoserine Ref.17 Ref.20
Modified residue321N6-acetyllysine; alternate Ref.28
Modified residue321N6-succinyllysine; alternate Ref.28
Modified residue1081N6-acetyllysine By similarity
Modified residue1231N6-acetyllysine Ref.28
Modified residue1351N6-acetyllysine Ref.28
Modified residue1551N6-acetyllysine Ref.28
Modified residue1711N6-acetyllysine; alternate Ref.28
Modified residue1711N6-succinyllysine; alternate Ref.28
Modified residue2011N6-acetyllysine; alternate Ref.28
Modified residue2121Phosphoserine By similarity
Modified residue2601N6-acetyllysine Ref.28
Modified residue2701N6-acetyllysine Ref.28
Modified residue2771Phosphoserine By similarity
Modified residue3011Phosphoserine By similarity
Modified residue3111N6-acetyllysine Ref.28
Modified residue3901Phosphoserine Ref.23
Modified residue3921Phosphoserine; by CDK1 Ref.10 Ref.23
Modified residue3951Phosphoserine By similarity
Modified residue4041Phosphoserine By similarity
Modified residue4071Phosphoserine Ref.10
Modified residue4091Phosphoserine Ref.10
Modified residue4141Phosphoserine By similarity
Modified residue4311Phosphoserine By similarity
Modified residue4501N6-acetyllysine Ref.28
Modified residue4571N6-acetyllysine Ref.28
Modified residue4581Phosphoserine By similarity
Modified residue4631Phosphoserine By similarity
Modified residue4961Phosphothreonine By similarity
Modified residue5001Phosphoserine By similarity
Modified residue5051Phosphothreonine By similarity
Modified residue5101Phosphothreonine By similarity
Modified residue5461Phosphoserine Ref.20
Modified residue6291Phosphoserine By similarity
Modified residue6331Phosphoserine By similarity
Modified residue6371Phosphoserine By similarity
Modified residue6531Phosphoserine Ref.17
Modified residue6621Cysteine methyl ester By similarity
Lipidation6621S-farnesyl cysteine By similarity
Cross-link201Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO); alternate By similarity

Natural variations

Alternative sequence1 – 112112Missing in isoform C2.
VSP_002471
Alternative sequence113 – 1186FKELKA → MGNAEG in isoform C2.
VSP_002472
Alternative sequence569 – 5746GSHCSG → VSGSRR in isoform C and isoform C2.
VSP_017064
Alternative sequence575 – 66591Missing in isoform C and isoform C2.
VSP_017065

Experimental info

Mutagenesis2011K → L: Decreased sumoylation; aberrant localization with decreased nuclear rim staining and formation of intranuclear foci; associated with increased cell death. Ref.18
Mutagenesis2031E → G or K: Decreased sumoylation; aberrant localization with decreased nuclear rim staining and formation of intranuclear foci; associated with increased cell death. Ref.18
Sequence conflict41P → S in BAE31384. Ref.5
Sequence conflict41P → S in BAE29519. Ref.5
Sequence conflict118 – 1192AR → VC in CAA32372. Ref.2
Sequence conflict1181A → D in BAE39876. Ref.5
Sequence conflict3401E → G in BAE29614. Ref.5
Sequence conflict4011R → P in CAA32372. Ref.2
Sequence conflict439 – 4402RV → WL in CAA32372. Ref.2
Sequence conflict4501K → E in BAE31384. Ref.5
Sequence conflict4531R → L in BAE36246. Ref.5
Sequence conflict6121I → V in BAB23415. Ref.5
Sequence conflict6171S → Y in BAB23415. Ref.5
Sequence conflict6231V → A in BAA02476. Ref.8

Secondary structure

............................ 665
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
Isoform A [UniParc].

Last modified January 24, 2006. Version 2.
Checksum: 5434F574803FCB15

FASTA66574,238
        10         20         30         40         50         60 
METPSQRRAT RSGAQASSTP LSPTRITRLQ EKEDLQELND RLAVYIDRVR SLETENAGLR 

        70         80         90        100        110        120 
LRITESEEVV SREVSGIKAA YEAELGDARK TLDSVAKERA RLQLELSKVR EEFKELKARN 

       130        140        150        160        170        180 
TKKEGDLLAA QARLKDLEAL LNSKEAALST ALSEKRTLEG ELHDLRGQVA KLEAALGEAK 

       190        200        210        220        230        240 
KQLQDEMLRR VDAENRLQTL KEELDFQKNI YSEELRETKR RHETRLVEID NGKQREFESR 

       250        260        270        280        290        300 
LADALQELRA QHEDQVEQYK KELEKTYSAK LDNARQSAER NSNLVGAAHE ELQQSRIRID 

       310        320        330        340        350        360 
SLSAQLSQLQ KQLAAKEAKL RDLEDSLARE RDTSRRLLAE KEREMAEMRA RMQQQLDEYQ 

       370        380        390        400        410        420 
ELLDIKLALD MEIHAYRKLL EGEEERLRLS PSPTSQRSRG RASSHSSQSQ GGGSVTKKRK 

       430        440        450        460        470        480 
LESSESRSSF SQHARTSGRV AVEEVDEEGK FVRLRNKSNE DQSMGNWQIR RQNGDDPLMT 

       490        500        510        520        530        540 
YRFPPKFTLK AGQVVTIWAS GAGATHSPPT DLVWKAQNTW GCGSSLRTAL INSTGEEVAM 

       550        560        570        580        590        600 
RKLVRSLTMV EDNEDDDEDG EELLHHHRGS HCSGSGDPAE YNLRSRTVLC GTCGQPADKA 

       610        620        630        640        650        660 
AGGAGAQVGG SISSGSSASS VTVTRSFRSV GGSGGGSFGD NLVTRSYLLG NSSPRSQSSQ 


NCSIM 

« Hide

Isoform C [UniParc] [UniParc].

Checksum: A736DF1CCEDB65BE
Show »

FASTA57465,446
Isoform C2 [UniParc] [UniParc].

Checksum: 4A12573CECAA93AA
Show »

FASTA46252,652

References

« Hide 'large scale' references
[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. expand/collapse author list , 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]"Large-scale phosphorylation analysis of mouse liver."
Villen J., Beausoleil S.A., Gerber S.A., Gygi S.P.
Proc. Natl. Acad. Sci. U.S.A. 104:1488-1493(2007) [PubMed] [Europe PMC] [Abstract]
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.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
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.
CCDSCCDS38482.1. [P48678-1]
CCDS38483.1. [P48678-3]
CCDS50951.1. [P48678-2]
PIRI53414.
S04333.
S18324.
S28182.
RefSeqNP_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]
UniGeneMm.243014.
Mm.471227.

3D structure databases

PDBe
RCSB-PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
1UFGNMR-A408-545[»]
ProteinModelPortalP48678.
SMRP48678. Positions 313-386, 415-546.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid201176. 60 interactions.
IntActP48678. 7 interactions.
MINTMINT-1868521.
STRING10090.ENSMUSP00000029699.

PTM databases

PhosphoSiteP48678.

2D gel databases

REPRODUCTION-2DPAGEIPI00400300.
IPI00620256.

Proteomic databases

MaxQBP48678.
PaxDbP48678.
PRIDEP48678.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENSMUST00000029699; ENSMUSP00000029699; ENSMUSG00000028063. [P48678-1]
ENSMUST00000036252; ENSMUSP00000040265; ENSMUSG00000028063. [P48678-3]
ENSMUST00000120377; ENSMUSP00000113093; ENSMUSG00000028063. [P48678-2]
GeneID16905.
KEGGmmu:16905.
UCSCuc008pvj.2. mouse. [P48678-1]
uc008pvk.2. mouse. [P48678-3]

Organism-specific databases

CTD4000.
MGIMGI:96794. Lmna.

Phylogenomic databases

eggNOGNOG325506.
GeneTreeENSGT00750000117244.
HOVERGENHBG013015.
InParanoidP48678.
KOK12641.
OMAHCSGSGD.
OrthoDBEOG7MD4PW.
PhylomeDBP48678.
TreeFamTF101181.

Enzyme and pathway databases

ReactomeREACT_188804. Cell Cycle.
REACT_200794. Mus musculus biological processes.

Gene expression databases

ArrayExpressP48678.
BgeeP48678.
CleanExMM_LMNA.
GenevestigatorP48678.

Family and domain databases

Gene3D2.60.40.1260. 1 hit.
InterProIPR001664. IF.
IPR018039. Intermediate_filament_CS.
IPR001322. Lamin_tail_dom.
[Graphical view]
PANTHERPTHR23239. PTHR23239. 1 hit.
PfamPF00038. Filament. 1 hit.
PF00932. LTD. 1 hit.
[Graphical view]
SUPFAMSSF74853. SSF74853. 1 hit.
PROSITEPS00226. IF. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

EvolutionaryTraceP48678.
NextBio290934.
PROP48678.
SOURCESearch...

Entry information

Entry nameLMNA_MOUSE
AccessionPrimary (citable) accession number: P48678
Secondary accession number(s): B3RH23 expand/collapse secondary AC list , B3RH24, P11516, P97859, Q3TIH0, Q3TTS8, Q3U733, Q3U7I5, Q3UCA0, Q3UCJ8, Q3UCU3, Q91WF2, Q9DC21
Entry history
Integrated into UniProtKB/Swiss-Prot: February 1, 1996
Last sequence update: January 24, 2006
Last modified: July 9, 2014
This is version 140 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

MGD cross-references

Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot