Search Results

Overview

Uniprot ID	P02545
Protein Name	Prelamin-A/C
Gene Name	LMNA
Organism	Homo sapiens

Kla Sites from experimental identification

Position	Flanking peptide
108	RLQLELSKVREEFKE
114	SKVREEFKELKARNT
123	LKARNTKKEGDLIAA
135	IAAQARLKDLEALLN
144	LEALLNSKEAALSTA
155	LSTALSEKRTLEGEL
171	DLRGQVAKLEAALGE
180	EAALGEAKKQLQDEM
181	AALGEAKKQLQDEML
201	ENRLQTMKEELDFQK
208	KEELDFQKNIYSEEL
233	LVEIDNGKQREFESR
260	EDQVEQYKKELEKTY
261	DQVEQYKKELEKTYS
270	LEKTYSAKLDNARQS
311	AQLSQLQKQLAAKEA
316	LQKQLAAKEAKLRDL
32	RITRLQEKEDLQELN
378	MEIHAYRKLLEGEEE
417	QGGGSVTKKRKLEST
418	GGGSVTKKRKLESTE
420	GSVTKKRKLESTESR
457	KFVRLRNKSNEDQSM
470	SMGNWQIKRQNGDDP
597	TCGQPADKASASGSG
78	SREVSGIKAAYEAEL
90	AELGDARKTLDSVAK
97	KTLDSVAKERARLQL

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:10080180, PubMed:10580070, PubMed:10587585, PubMed:10814726, PubMed:11799477, PubMed:12075506, PubMed:12927431, PubMed:15317753, PubMed:18551513, PubMed:18611980, PubMed:2188730, PubMed:22431096, PubMed:2344612, PubMed:23666920, PubMed:24741066, PubMed:31434876, PubMed:31548606, PubMed:37788673, PubMed:37832547). 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:10080180, PubMed:10580070, PubMed:10587585, PubMed:10814726, PubMed:11799477, PubMed:12075506, PubMed:12927431, PubMed:15317753, PubMed:18551513, PubMed:18611980, PubMed:22431096, PubMed:23666920, PubMed:24741066, PubMed:31548606, PubMed:37788673, PubMed:37832547). Lamin A and C also regulate matrix stiffness by conferring nuclear mechanical properties (PubMed:23990565, PubMed:25127216). 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:2188730, PubMed:2344612). Lamin A and C are present in equal amounts in the lamina of mammals (PubMed:10080180, PubMed:10580070, PubMed:10587585, PubMed:10814726, PubMed:11799477, PubMed:12075506, PubMed:12927431, PubMed:15317753, PubMed:18551513, PubMed:18611980, PubMed:22431096, PubMed:23666920, PubMed:31548606). 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 (PubMed:31548606). Required for normal development of peripheral nervous system and skeletal muscle and for muscle satellite cell proliferation (PubMed:10080180, PubMed:10814726, PubMed:11799477, PubMed:18551513, PubMed:22431096). Required for osteoblastogenesis and bone formation (PubMed:12075506, PubMed:15317753, PubMed:18611980). Also prevents fat infiltration of muscle and bone marrow, helping to maintain the volume and strength of skeletal muscle and bone (PubMed:10587585). Required for cardiac homeostasis (PubMed:10580070, PubMed:12927431, PubMed:18611980, PubMed:23666920)

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 TKKEGDLIAA 140 QARLKDLEAL 150 LNSKEAALST 160 ALSEKRTLEG 170 ELHDLRGQVA 180 KLEAALGEAK 190 KQLQDEMLRR 200 VDAENRLQTM 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 RASSHSSQTQ 420 GGGSVTKKRK 430 LESTESRSSF 440 SQHARTSGRV 450 AVEEVDEEGK 460 FVRLRNKSNE 470 DQSMGNWQIK 480 RQNGDDPLLT 490 YRFPPKFTLK 500 AGQVVTIWAA 510 GAGATHSPPT 520 DLVWKAQNTW 530 GCGNSLRTAL 540 INSTGEEVAM 550 RKLVRSVTVV 560 EDDEDEDGDD 570 LLHHHHGSHC 580 SSSGDPAEYN 590 LRSRTVLCGT 600 CGQPADKASA 610 SGSGAQVGGP 620 ISSGSSASSV 630 TVTRSYRSVG 640 GSGGGSFGDN 650 LVTRSYLLGN 660 SSPRTQSPQN CSIM

Gene Ontology

Classification	GO ID	Description
Cellular Component	GO:0005829	cytosol
Cellular Component	GO:0005882	intermediate filament
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:0005200	structural constituent of cytoskeleton
Molecular Function	GO:0160123	structural constituent of nuclear lamina
Molecular Function	GO:0005198	structural molecule activity
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: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:1903243	negative regulation of cardiac muscle hypertrophy in response to stress
Biological Process	GO:0008285	negative regulation of cell population proliferation
Biological Process	GO:0006998	nuclear envelope organization
Biological Process	GO:0007097	nuclear migration
Biological Process	GO:0051664	nuclear pore localization
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:0032204	regulation of telomere maintenance

Reference

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[2] Yang Z, Yan C, Ma J, Peng P, Ren X et al.. Lactylome analysis suggests lactylation-dependent mechanisms of metabolic adaptation in hepatocellular carcinoma.. Nat Metab 5(1):61-79. 2023 Jan. PMID: 36593272.

[3] Hong H, Chen X, Wang H, Gu X, Yuan Y et al.. Global profiling of protein lysine lactylation and potential target modified protein analysis in hepatocellular carcinoma.. Proteomics 23(9):e2200432. 2023 May. PMID: 36625413.

[4] Lin Y, Chen M, Wang D, Yu Y, Chen R et al.. Multi-Proteomic Analysis Reveals the Effect of Protein Lactylation on Matrix and Cholesterol Metabolism in Tendinopathy.. J Proteome Res 22(6):1712-1722. 2023 Jun 2. PMID: 37159428.

[5] Yang YH, Wang QC, Kong J, Yang JT, Liu JF. Global profiling of lysine lactylation in human lungs.. Proteomics 23(15):e2200437. 2023 Aug. PMID: 37170646.

[6] Cheng Z, Huang H, Li M, Chen Y. Proteomic analysis identifies PFKP lactylation in SW480 colon cancer cells.. iScience 27(1):108645. 2024 Jan 19. PMID: 38155775.

[7] He C, Zhang J, Bai X, Lu C, Zhang K. Lysine lactylation-based insight to understanding the characterization of cervical cancer.. Biochim Biophys Acta Mol Basis Dis 1870(7):167356. 2024 Oct. PMID: 39025375.

[8] Bao Q, Wan N, He Z, Cao J, Yuan W et al.. Subcellular Proteomic Mapping of Lysine Lactylation.. J Am Soc Mass Spectrom 35(12):3221-3232. 2024 Dec 4. PMID: 39569522.

[9] Shi CM, Wang QC, Li XL, Yang YH, Tang XY et al.. Global Profiling of Protein Lactylation in Human Hippocampi.. Proteomics Clin Appl 19(2):e202400061. 2025 Mar. PMID: 39610256.

[10] Hu J, Jin Z, Gao Y, Liu Q, Yu Y et al.. Global Profiling of Lactylation Proteomics and Specific Lactylated Site Validation in Rheumatoid Arthritis Patients.. J Proteome Res 24(4):1732-1744. 2025 Apr 4. PMID: 40112136.

[11] He J, Lai T, Zhou Z, Yang H, Lei Z et al.. Multiomics profiling reveals the involvement of protein lactylation in nonhomologous end joining pathway conferring radioresistance in lung adenocarcinoma cell.. Sci Rep 15(1):24651. 2025 Jul 9. PMID: 40634431.

[12] Chao L, Xu Y, Yang Y, Ao X, Liang J. Identification of lactylation-related biomarkers for diagnosis, prognosis, and treatment responsiveness in triple-negative breast cancer.. World J Surg Oncol 24(1):77. 2026 Jan 22. PMID: 41566505.

[13] Wu Q, Li Z, Gong T, Zheng X, Zhou X et al.. Porphyromonas gingivalis infection induces lysine lactylation reprogramming in human umbilical vein endothelial cells.. Front Cell Infect Microbiol 16:1706727. 2026. PMID: 41696360.