Search Results

Overview

Uniprot IDP48678
Protein NamePrelamin-A/C
Gene NameLmna
OrganismMus musculus

Kla Sites from experimental identification

Position Flanking peptide
270 LEKTYSAKLDNARQS
378 MEIHAYRKLLEGEEE

Function

Lamins are intermediate filament proteins that assemble into a filamentous meshwork, and which constitute the major components of the nuclear lamina, a fibrous layer on the nucleoplasmic side of the inner nuclear membrane (PubMed:10579712, PubMed:28241138, PubMed:31576060). Lamins provide a framework for the nuclear envelope, bridging the nuclear envelope and chromatin, thereby playing an important role in nuclear assembly, chromatin organization, nuclear membrane and telomere dynamics (PubMed:10579712, PubMed:28241138). Lamin A and C also regulate matrix stiffness by conferring nuclear mechanical properties (By similarity). 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 (PubMed:10579712, PubMed:28241138). Lamin A and C are present in equal amounts in the lamina of mammals (By similarity). Also involved in DNA repair: recruited by DNA repair proteins XRCC4 and IFFO1 to the DNA double-strand breaks (DSBs) to prevent chromosome translocation by immobilizing broken DNA ends (By similarity). Required for normal development of peripheral nervous system and skeletal muscle and for muscle satellite cell proliferation (PubMed:11799477, PubMed:19124654, PubMed:23535822). Required for osteoblastogenesis and bone formation (By similarity). Also prevents fat infiltration of muscle and bone marrow, helping to maintain the volume and strength of skeletal muscle and bone (PubMed:21547077, PubMed:21982926). Required for cardiac homeostasis (PubMed:26436652)

Protein Sequence

10 METPSQRRAT 20 RSGAQASSTP 30 LSPTRITRLQ 40 EKEDLQELND 50 RLAVYIDRVR 60 SLETENAGLR 70 LRITESEEVV 80 SREVSGIKAA 90 YEAELGDARK 100 TLDSVAKERA 110 RLQLELSKVR 120 EEFKELKARN 130 TKKEGDLLAA 140 QARLKDLEAL 150 LNSKEAALST 160 ALSEKRTLEG 170 ELHDLRGQVA 180 KLEAALGEAK 190 KQLQDEMLRR 200 VDAENRLQTL 210 KEELDFQKNI 220 YSEELRETKR 230 RHETRLVEID 240 NGKQREFESR 250 LADALQELRA 260 QHEDQVEQYK 270 KELEKTYSAK 280 LDNARQSAER 290 NSNLVGAAHE 300 ELQQSRIRID 310 SLSAQLSQLQ 320 KQLAAKEAKL 330 RDLEDSLARE 340 RDTSRRLLAE 350 KEREMAEMRA 360 RMQQQLDEYQ 370 ELLDIKLALD 380 MEIHAYRKLL 390 EGEEERLRLS 400 PSPTSQRSRG 410 RASSHSSQSQ 420 GGGSVTKKRK 430 LESSESRSSF 440 SQHARTSGRV 450 AVEEVDEEGK 460 FVRLRNKSNE 470 DQSMGNWQIR 480 RQNGDDPLMT 490 YRFPPKFTLK 500 AGQVVTIWAS 510 GAGATHSPPT 520 DLVWKAQNTW 530 GCGSSLRTAL 540 INSTGEEVAM 550 RKLVRSLTMV 560 EDNEDDDEDG 570 EELLHHHRGS 580 HCSGSGDPAE 590 YNLRSRTVLC 600 GTCGQPADKA 610 AGGAGAQVGG 620 SISSGSSASS 630 VTVTRSFRSV 640 GGSGGGSFGD 650 NLVTRSYLLG 660 NSSPRSQSSQ NCSIM

Gene Ontology

Classification GO ID Description
Cellular Component GO:0005638 lamin filament
Cellular Component GO:0005635 nuclear envelope
Cellular Component GO:0005652 nuclear lamina
Cellular Component GO:0016363 nuclear matrix
Cellular Component GO:0031965 nuclear membrane
Cellular Component GO:0016607 nuclear speck
Cellular Component GO:0005654 nucleoplasm
Cellular Component GO:0005634 nucleus
Cellular Component GO:0048471 perinuclear region of cytoplasm
Cellular Component GO:0035861 site of double-strand break
Molecular Function GO:0042802 identical protein binding
Molecular Function GO:0008157 protein phosphatase 1 binding
Molecular Function GO:0005200 structural constituent of cytoskeleton
Molecular Function GO:0160123 structural constituent of nuclear lamina
Biological Process GO:0071456 cellular response to hypoxia
Biological Process GO:0090398 cellular senescence
Biological Process GO:1990683 DNA double-strand break attachment to nuclear envelope
Biological Process GO:0006303 double-strand break repair via nonhomologous end joining
Biological Process GO:0030010 establishment of cell polarity
Biological Process GO:0030951 establishment or maintenance of microtubule cytoskeleton polarity
Biological Process GO:0031507 heterochromatin formation
Biological Process GO:0008104 intracellular protein localization
Biological Process GO:0007517 muscle organ development
Biological Process GO:1904178 negative regulation of adipose tissue development
Biological Process GO:1903243 negative regulation of cardiac muscle hypertrophy in response to stress
Biological Process GO:0008285 negative regulation of cell population proliferation
Biological Process GO:2001237 negative regulation of extrinsic apoptotic signaling pathway
Biological Process GO:0072201 negative regulation of mesenchymal cell proliferation
Biological Process GO:0090201 negative regulation of release of cytochrome c from mitochondria
Biological Process GO:0006998 nuclear envelope organization
Biological Process GO:0007097 nuclear migration
Biological Process GO:0051664 nuclear pore localization
Biological Process GO:0006997 nucleus organization
Biological Process GO:0010628 positive regulation of gene expression
Biological Process GO:0045669 positive regulation of osteoblast differentiation
Biological Process GO:0006606 protein import into nucleus
Biological Process GO:0090435 protein localization to nuclear envelope
Biological Process GO:0034504 protein localization to nucleus
Biological Process GO:0030334 regulation of cell migration
Biological Process GO:1900180 regulation of protein localization to nucleus
Biological Process GO:0031647 regulation of protein stability
Biological Process GO:0032204 regulation of telomere maintenance
Biological Process GO:0055015 ventricular cardiac muscle cell development

Reference

[1] Wu D, Tang Y, Li X, Xiong S, Zhang Z et al.. Characterization of protein lactylation in healthy and ischemic mouse hearts.. Front Cardiovasc Med 12:1644886. 2025. PMID: 41089239.