P48678 (LMNA_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Prelamin-A/C

Cleaved into the following chain:

1. Lamin-A/C

Gene names

Name:	Lmna
Synonyms:	Lmn1

Organism

Mus musculus (Mouse) [Reference proteome]

Taxonomic identifier

10090 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Opisthokonta › Metazoa › Eumetazoa › Bilateria › Deuterostomia › Chordata › Craniata › Vertebrata › Gnathostomata › Teleostomi › Euteleostomi › Sarcopterygii › Tetrapoda › Amniota › Mammalia › Theria › Eutheria › Euarchontoglires › Glires › Rodentia › Sciurognathi › Muroidea › Muridae › Murinae › Mus › Mus

Protein attributes

Sequence length	665 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Evidence 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 By similarity. 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.
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. Ref.9 Ref.10 Ref.11 Ref.15 Ref.17 Ref.19 Ref.20
Subcellular location	Nucleus By similarity. Nucleus envelope 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.14
Tissue specificity	Isoform C2 is specifically expressed in germ cells. This specific expression and unique structure suggests a role for this isoform in determining the organization of nuclear and chromosomal structures during spermatogenesis.
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.14 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.8 The N-terminus is blocked.
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.

Ontologies

Keywords
Cellular component	Intermediate filament Nucleus
Coding sequence diversity	Alternative splicing
Domain	Coiled coil
PTM	Acetylation Isopeptide bond Lipoprotein Methylation Phosphoprotein Prenylation Ubl conjugation
Technical term	3D-structure Complete proteome Direct protein sequencing Reference proteome
Gene Ontology (GO)
Biological_process	cellular 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 nuclear envelope organization Inferred from genetic interaction PubMed 15608054. Source: MGI positive regulation of cell aging Inferred from sequence or structural similarity. Source: UniProtKB regulation of apoptotic process Inferred from direct assay PubMed 21151901. Source: BHF-UCL regulation of cell migration Inferred from mutant phenotype PubMed 17631533. Source: BHF-UCL 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_component	lamin filament Inferred from direct assay PubMed 8032679. Source: MGI nuclear envelope Inferred from direct assay Ref.14. Source: UniProtKB nucleus Inferred from direct assay PubMed 18664494. Source: BHF-UCL perinuclear region of cytoplasm Inferred from sequence or structural similarity. Source: BHF-UCL
Molecular_function	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 key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 662

662

Prelamin-A/C

PRO_0000398837

Chain

1 – 647

647

Lamin-A/C

PRO_0000063811

Propeptide

648 – 662

15

Removed in Lamin-A/C form

PRO_0000398838

Propeptide

663 – 665

3

Removed in Prelamin-A/C form and in Lamin-A/C form

PRO_0000403443

Regions

Region

1 – 130

130

Interaction with MLIP By similarity

Region

1 – 33

33

Head

Region

34 – 383

350

Rod

Region

34 – 70

37

Coil 1A

Region

71 – 80

10

Linker 1

Region

81 – 218

138

Coil 1B

Region

219 – 242

24

Linker 2

Region

243 – 383

141

Coil 2

Region

384 – 665

282

Tail

Motif

417 – 422

6

Nuclear localization signal Potential

Sites

Site

266

1

Heptad change of phase

Site

325

1

Stutter By similarity

Site

330

1

Heptad change of phase

Site

647 – 648

2

Cleavage; by endoprotease By similarity

Amino acid modifications

Modified residue

1

1

N-acetylmethionine By similarity

Modified residue

3

1

Phosphothreonine By similarity

Modified residue

12

1

Phosphoserine Ref.13

Modified residue

18

1

Phosphoserine By similarity

Modified residue

19

1

Phosphothreonine Ref.13

Modified residue

22

1

Phosphoserine Ref.13 Ref.18

Modified residue

108

1

N6-acetyllysine By similarity

Modified residue

212

1

Phosphoserine By similarity

Modified residue

270

1

N6-acetyllysine By similarity

Modified residue

277

1

Phosphoserine By similarity

Modified residue

301

1

Phosphoserine Ref.16

Modified residue

311

1

N6-acetyllysine By similarity

Modified residue

390

1

Phosphoserine Ref.12 Ref.16 Ref.18

Modified residue

392

1

Phosphoserine; by CDK1 Ref.8 Ref.12 Ref.16 Ref.18

Modified residue

395

1

Phosphoserine By similarity

Modified residue

398

1

Phosphoserine Ref.16

Modified residue

404

1

Phosphoserine By similarity

Modified residue

406

1

Phosphoserine Ref.16

Modified residue

407

1

Phosphoserine Ref.8 Ref.16

Modified residue

409

1

Phosphoserine Ref.8 Ref.16

Modified residue

414

1

Phosphoserine Ref.16

Modified residue

431

1

Phosphoserine By similarity

Modified residue

450

1

N6-acetyllysine By similarity

Modified residue

458

1

Phosphoserine By similarity

Modified residue

463

1

Phosphoserine By similarity

Modified residue

496

1

Phosphothreonine By similarity

Modified residue

505

1

Phosphothreonine By similarity

Modified residue

507

1

Phosphoserine By similarity

Modified residue

510

1

Phosphothreonine By similarity

Modified residue

573

1

Phosphoserine Ref.16

Modified residue

575

1

Phosphoserine Ref.16

Modified residue

629

1

Phosphoserine Ref.16

Modified residue

633

1

Phosphoserine Ref.13 Ref.16

Modified residue

637

1

Phosphoserine Ref.13

Modified residue

653

1

Phosphoserine By similarity

Modified residue

662

1

Cysteine methyl ester By similarity

Lipidation

662

1

S-farnesyl cysteine By similarity

Cross-link

201

Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO) By similarity

Natural variations

Alternative sequence

1 – 112

112

Missing in isoform C2.

VSP_002471

Alternative sequence

113 – 118

6

FKELKA → MGNAEG in isoform C2.

VSP_002472

Alternative sequence

569 – 574

6

GSHCSG → VSGSRR in isoform C and isoform C2.

VSP_017064

Alternative sequence

575 – 665

91

Missing in isoform C and isoform C2.

VSP_017065

Experimental info

Mutagenesis

201

1

K → L: Decreased sumoylation; aberrant localization with decreased nuclear rim staining and formation of intranuclear foci; associated with increased cell death. Ref.14

Mutagenesis

203

1

E → G or K: Decreased sumoylation; aberrant localization with decreased nuclear rim staining and formation of intranuclear foci; associated with increased cell death. Ref.14

Sequence conflict

118 – 119

2

AR → VC in CAA32372. Ref.2

Sequence conflict

118

1

A → D in BAE39876. Ref.4

Sequence conflict

340

1

E → G in BAE29614. Ref.4

Sequence conflict

401

1

R → P in CAA32372. Ref.2

Sequence conflict

439 – 440

2

RV → WL in CAA32372. Ref.2

Sequence conflict

453

1

R → L in BAE36246. Ref.4

Sequence conflict

612

1

I → V in BAB23415. Ref.4

Sequence conflict

617

1

S → Y in BAB23415. Ref.4

Sequence conflict

623

1

V → A in BAA02476. Ref.6

Secondary structure

1

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

665

Helix Strand Turn

Details...

Beta strand

417 – 420

4

Beta strand

433 – 436

4

Beta strand

438 – 445

8

Beta strand

449 – 456

8

Beta strand

458 – 460

3

Beta strand

468 – 473

6

Beta strand

479 – 482

4

Beta strand

494 – 503

10

Turn

508 – 510

3

Beta strand

511 – 514

4

Beta strand

516 – 518

3

Beta strand

523 – 531

9

Beta strand

533 – 535

3

Beta strand

537 – 544

8

Sequences

	Sequence		Length	Mass (Da)
	Isoform A [UniParc]. Last modified January 24, 2006. Version 2. Checksum: 5434F574803FCB15	FASTA	665	74,238
	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
	Isoform C [UniParc] [UniParc]. Checksum: A736DF1CCEDB65BE	FASTA	574	65,446
	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 RKLVRSLTMV EDNEDDDEDG EELLHHHRVS GSRR
	Isoform C2 [UniParc] [UniParc]. Checksum: 4A12573CECAA93AA	FASTA	462	52,652
	10 20 30 40 50 60 MGNAEGRNTK KEGDLLAAQA RLKDLEALLN SKEAALSTAL SEKRTLEGEL HDLRGQVAKL 70 80 90 100 110 120 EAALGEAKKQ LQDEMLRRVD AENRLQTLKE ELDFQKNIYS EELRETKRRH ETRLVEIDNG 130 140 150 160 170 180 KQREFESRLA DALQELRAQH EDQVEQYKKE LEKTYSAKLD NARQSAERNS NLVGAAHEEL 190 200 210 220 230 240 QQSRIRIDSL SAQLSQLQKQ LAAKEAKLRD LEDSLARERD TSRRLLAEKE REMAEMRARM 250 260 270 280 290 300 QQQLDEYQEL LDIKLALDME IHAYRKLLEG EEERLRLSPS PTSQRSRGRA SSHSSQSQGG 310 320 330 340 350 360 GSVTKKRKLE SSESRSSFSQ HARTSGRVAV EEVDEEGKFV RLRNKSNEDQ SMGNWQIRRQ 370 380 390 400 410 420 NGDDPLMTYR FPPKFTLKAG QVVTIWASGA GATHSPPTDL VWKAQNTWGC GSSLRTALIN 430 440 450 460 STGEEVAMRK LVRSLTMVED NEDDDEDGEE LLHHHRVSGS RR

References

	« Hide 'large scale' referencesShow '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]	"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.
[5]	"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.
[6]	"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).
[7]	"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.
[8]	"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.
[9]	"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.
[10]	"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.
[11]	"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.
[12]	"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: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-390 AND SER-392, MASS SPECTROMETRY. Tissue: Brain.
[13]	"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 SER-12; THR-19; SER-22; SER-633 AND SER-637, MASS SPECTROMETRY. Tissue: Liver.
[14]	"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.
[15]	"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.
[16]	"Solid tumor proteome and phosphoproteome analysis by high resolution mass spectrometry." Zanivan S., Gnad F., Wickstroem S.A., Geiger T., Macek B., Cox J., Faessler R., Mann M. J. Proteome Res. 7:5314-5326(2008) [PubMed] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-301; SER-390; SER-392; SER-398; SER-406; SER-407; SER-409; SER-414; SER-573; SER-575; SER-629 AND SER-633, MASS SPECTROMETRY. Tissue: Melanoma.
[17]	"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.
[18]	"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-22; SER-390 AND SER-392, MASS SPECTROMETRY. Tissue: Embryonic fibroblast.
[19]	"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.
[20]	"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.
[21]	"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.
AK004619 mRNA. Translation: BAB23415.1.
AK147150 mRNA. Translation: BAE27717.1.
AK149998 mRNA. Translation: BAE29226.1.
AK150501 mRNA. Translation: BAE29614.1.
AK150624 mRNA. Translation: BAE29714.1.
AK152539 mRNA. Translation: BAE31294.1.
AK161221 mRNA. Translation: BAE36246.1.
AK167858 mRNA. Translation: BAE39876.1.
BC015302 mRNA. Translation: AAH15302.1.
BC094020 mRNA. Translation: AAH94020.1.
D13181 mRNA. Translation: BAA02476.1.

IPI

IPI00230435.
IPI00400300.
IPI00620256.

PIR

I53414.
S04333.
S18324.
S28182.

RefSeq

NP_001002011.2. NM_001002011.2.
NP_001104572.1. NM_001111102.1.
NP_062263.1. NM_019390.2.

UniGene

Mm.243014.
Mm.471227.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
1UFG	NMR	-	A	408-545	[»]

ProteinModelPortal

P48678.

SMR

P48678. Positions 313-386, 415-546.

ModBase

Search...

Protein-protein interaction databases

IntAct

P48678. 5 interactions.

MINT

MINT-1868521.

STRING

10090.ENSMUSP00000029699.

PTM databases

PhosphoSite

P48678.

2D gel databases

REPRODUCTION-2DPAGE

IPI00400300.
IPI00620256.

Proteomic databases

PaxDb

P48678.

PRIDE

P48678.

Protocols and materials databases

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

Ensembl

ENSMUST00000029699; ENSMUSP00000029699; ENSMUSG00000028063.
ENSMUST00000036252; ENSMUSP00000040265; ENSMUSG00000028063.
ENSMUST00000120377; ENSMUSP00000113093; ENSMUSG00000028063.

GeneID

16905.

KEGG

mmu:16905.

UCSC

uc008pvk.2. mouse.

Organism-specific databases

CTD

4000.

MGI

MGI:96794. Lmna.

Phylogenomic databases

eggNOG

NOG325506.

GeneTree

ENSGT00560000076873.

HOVERGEN

HBG013015.

InParanoid

P48678.

KO

K12641.

OMA

HCSGSGD.

OrthoDB

EOG4S4PG2.

Enzyme and pathway databases

Reactome

REACT_118161. Cell Cycle.
REACT_120463. Meiosis.
REACT_75800. Meiotic Synapsis (mouse).

Gene expression databases

ArrayExpress

P48678.

Bgee

P48678.

CleanEx

MM_LMNA.

Genevestigator

P48678.

GermOnline

ENSMUSG00000028063. Mus musculus.

Family and domain databases

InterPro

IPR016044. F.
IPR001664. IF.
IPR018039. Intermediate_filament_CS.
IPR001322. Lamin_tail_dom.
[Graphical view]

PANTHER

PTHR23239. PTHR23239. 1 hit.

Pfam

PF00038. Filament. 1 hit.
PF00932. LTD. 1 hit.
[Graphical view]

PROSITE

PS00226. IF. 1 hit.
[Graphical view]

ProtoNet

Search...

Other

EvolutionaryTrace

P48678.

NextBio

290934.

SOURCE

Search...

Entry information

Entry name

LMNA_MOUSE

Accession

Primary (citable) accession number: P48678
Secondary accession number(s): P11516 , P97859, Q3TIH0, Q3TTS8, Q3UCA0, Q3UCJ8, Q91WF2, Q9DC21

Entry history

Integrated into UniProtKB/Swiss-Prot:	February 1, 1996
Last sequence update:	January 24, 2006
Last modified:	May 1, 2013
This is version 126 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program