Search Results

Overview

Uniprot IDQ9UHB6
Protein NameLIM domain and actin-binding protein 1
Gene NameLIMA1
OrganismHomo sapiens

Kla Sites from experimental identification

Position Flanking peptide
189 DASGKIEKYNVPLNR
210 KGEPTQTKILRAQSR
268 RLSETSIKDRMAKYQ
273 SIKDRMAKYQAAVSK
280 KYQAAVSKQSSSTNY
381 SPPKAMKKFQAPARE
439 LHGRIYCKPHFNQLF
614 TVSPPIRKGWSMSEQ

Function

Actin-binding protein involved in actin cytoskeleton regulation and dynamics. Increases the number and size of actin stress fibers and inhibits membrane ruffling. Inhibits actin filament depolymerization. Bundles actin filaments, delays filament nucleation and reduces formation of branched filaments (PubMed:12566430, PubMed:33999101). Acts as a negative regulator of primary cilium formation (PubMed:32496561). Plays a role in cholesterol homeostasis. Influences plasma cholesterol levels through regulation of intestinal cholesterol absorption. May act as a scaffold protein by regulating NPC1L1 transportation, an essential protein for cholesterol absorption, to the plasma membrane by recruiting MYO5B to NPC1L1, and thus facilitates cholesterol uptake (By similarity)

Protein Sequence

10 MESSPFNRRQ 20 WTSLSLRVTA 30 KELSLVNKNK 40 SSAIVEIFSK 50 YQKAAEETNM 60 EKKRSNTENL 70 SQHFRKGTLT 80 VLKKKWENPG 90 LGAESHTDSL 100 RNSSTEIRHR 110 ADHPPAEVTS 120 HAASGAKADQ 130 EEQIHPRSRL 140 RSPPEALVQG 150 RYPHIKDGED 160 LKDHSTESKK 170 MENCLGESRH 180 EVEKSEISEN 190 TDASGKIEKY 200 NVPLNRLKMM 210 FEKGEPTQTK 220 ILRAQSRSAS 230 GRKISENSYS 240 LDDLEIGPGQ 250 LSSSTFDSEK 260 NESRRNLELP 270 RLSETSIKDR 280 MAKYQAAVSK 290 QSSSTNYTNE 300 LKASGGEIKI 310 HKMEQKENVP 320 PGPEVCITHQ 330 EGEKISANEN 340 SLAVRSTPAE 350 DDSRDSQVKS 360 EVQQPVHPKP 370 LSPDSRASSL 380 SESSPPKAMK 390 KFQAPARETC 400 VECQKTVYPM 410 ERLLANQQVF 420 HISCFRCSYC 430 NNKLSLGTYA 440 SLHGRIYCKP 450 HFNQLFKSKG 460 NYDEGFGHRP 470 HKDLWASKNE 480 NEEILERPAQ 490 LANARETPHS 500 PGVEDAPIAK 510 VGVLAASMEA 520 KASSQQEKED 530 KPAETKKLRI 540 AWPPPTELGS 550 SGSALEEGIK 560 MSKPKWPPED 570 EISKPEVPED 580 VDLDLKKLRR 590 SSSLKERSRP 600 FTVAASFQST 610 SVKSPKTVSP 620 PIRKGWSMSE 630 QSEESVGGRV 640 AERKQVENAK 650 ASKKNGNVGK 660 TTWQNKESKG 670 ETGKRSKEGH 680 SLEMENENLV 690 ENGADSDEDD 700 NSFLKQQSPQ 710 EPKSLNWSSF 720 VDNTFAEEFT 730 TQNQKSQDVE 740 LWEGEVVKEL 750 SVEEQIKRNR YYDEDEDEE

Gene Ontology

Classification GO ID Description
Cellular Component GO:0015629 actin cytoskeleton
Cellular Component GO:0005884 actin filament
Cellular Component GO:0031526 brush border membrane
Cellular Component GO:0032154 cleavage furrow
Cellular Component GO:0005829 cytosol
Cellular Component GO:0005925 focal adhesion
Cellular Component GO:0030027 lamellipodium
Cellular Component GO:0005886 plasma membrane
Cellular Component GO:0001726 ruffle
Cellular Component GO:0001725 stress fiber
Molecular Function GO:0051015 actin filament binding
Molecular Function GO:0003785 actin monomer binding
Molecular Function GO:0045296 cadherin binding
Molecular Function GO:0046872 metal ion binding
Molecular Function GO:0140778 microtubule stabilizing activity
Biological Process GO:0051017 actin filament bundle assembly
Biological Process GO:0016477 cell migration
Biological Process GO:0042632 cholesterol homeostasis
Biological Process GO:0008203 cholesterol metabolic process
Biological Process GO:0030299 intestinal cholesterol absorption
Biological Process GO:0030835 negative regulation of actin filament depolymerization
Biological Process GO:0030336 negative regulation of cell migration
Biological Process GO:1902018 negative regulation of cilium assembly
Biological Process GO:0032233 positive regulation of actin filament bundle assembly
Biological Process GO:1902743 regulation of lamellipodium organization
Biological Process GO:0031529 ruffle organization

Reference

[1] 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.

[2] 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.

[3] 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.