Search Results

Overview

Uniprot IDQ9UGP4
Protein NameLIM domain-containing protein 1
Gene NameLIMD1
OrganismHomo sapiens

Kla Sites from experimental identification

Position Flanking peptide
33 DGLFRVDKGAGNNPE
465 REMDAHPKADYFGAC
54 VFATKMAKIHLQQQQ

Function

Adapter or scaffold protein which participates in the assembly of numerous protein complexes and is involved in several cellular processes such as cell fate determination, cytoskeletal organization, repression of gene transcription, cell-cell adhesion, cell differentiation, proliferation and migration. Positively regulates microRNA (miRNA)-mediated gene silencing and is essential for P-body formation and integrity. Acts as a hypoxic regulator by bridging an association between the prolyl hydroxylases and VHL enabling efficient degradation of HIF1A. Acts as a transcriptional corepressor for SNAI1- and SNAI2/SLUG-dependent repression of E-cadherin transcription. Negatively regulates the Hippo signaling pathway and antagonizes phosphorylation of YAP1. Inhibits E2F-mediated transcription, and suppresses the expression of the majority of genes with E2F1-responsive elements. Regulates osteoblast development, function, differentiation and stress osteoclastogenesis. Enhances the ability of TRAF6 to activate adapter protein complex 1 (AP-1) and negatively regulates the canonical Wnt receptor signaling pathway in osteoblasts. May act as a tumor suppressor by inhibiting cell proliferation

Protein Sequence

10 MDKYDDLGLE 20 ASKFIEDLNM 30 YEASKDGLFR 40 VDKGAGNNPE 50 FEETRRVFAT 60 KMAKIHLQQQ 70 QQQLLQEETL 80 PRGSRGPVNG 90 GGRLGPQARW 100 EVVGSKLTVD 110 GAAKPPLAAS 120 TGAPGAVTTL 130 AAGQPPYPPQ 140 EQRSRPYLHG 150 TRHGSQDCGS 160 RESLATSEMS 170 AFHQPGPCED 180 PSCLTHGDYY 190 DNLSLASPKW 200 GDKPGVSPSI 210 GLSVGSGWPS 220 SPGSDPPLPK 230 PCGDHPLNHR 240 QLSLSSSRSS 250 EGSLGGQNSG 260 IGGRSSEKPT 270 GLWSTASSQR 280 VSPGLPSPNL 290 ENGAPAVGPV 300 QPRTPSVSAP 310 LALSCPRQGG 320 LPRSNSGLGG 330 EVSGVMSKPN 340 VDPQPWFQDG 350 PKSYLSSSAP 360 SSSPAGLDGS 370 QQGAVPGLGP 380 KPGCTDLGTG 390 PKLSPTSLVH 400 PVMSTLPELS 410 CKEGPLGWSS 420 DGSLGSVLLD 430 SPSSPRVRLP 440 CQPLVPGPEL 450 RPSAAELKLE 460 ALTQRLEREM 470 DAHPKADYFG 480 ACVKCSKGVF 490 GAGQACQAMG 500 NLYHDTCFTC 510 AACSRKLRGK 520 AFYFVNGKVF 530 CEEDFLYSGF 540 QQSADRCFLC 550 GHLIMDMILQ 560 ALGKSYHPGC 570 FRCVICNECL 580 DGVPFTVDSE 590 NKIYCVRDYH 600 KVLAPKCAAC 610 GLPILPPEGS 620 DETIRVVSMD 630 RDYHVECYHC 640 EDCGLELNDE 650 DGHRCYPLED 660 HLFCHSCHVK 670 RLEKRPSSTA LHQHHF

Gene Ontology

Classification GO ID Description
Cellular Component GO:0005912 adherens junction
Cellular Component GO:0005737 cytoplasm
Cellular Component GO:0005829 cytosol
Cellular Component GO:0005925 focal adhesion
Cellular Component GO:0005654 nucleoplasm
Cellular Component GO:0005634 nucleus
Cellular Component GO:0000932 P-body
Cellular Component GO:0016442 RISC complex
Cellular Component GO:0005667 transcription regulator complex
Molecular Function GO:0046872 metal ion binding
Molecular Function GO:0003714 transcription corepressor activity
Biological Process GO:0007010 cytoskeleton organization
Biological Process GO:0006351 DNA-templated transcription
Biological Process GO:0035278 miRNA-mediated gene silencing by inhibition of translation
Biological Process GO:0035195 miRNA-mediated post-transcriptional gene silencing
Biological Process GO:0090090 negative regulation of canonical Wnt signaling pathway
Biological Process GO:0045892 negative regulation of DNA-templated transcription
Biological Process GO:0035331 negative regulation of hippo signaling
Biological Process GO:0045668 negative regulation of osteoblast differentiation
Biological Process GO:0002076 osteoblast development
Biological Process GO:0033962 P-body assembly
Biological Process GO:0016310 phosphorylation
Biological Process GO:0006355 regulation of DNA-templated transcription
Biological Process GO:0001666 response to hypoxia

Reference

[1] 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.

[2] 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.

[3] Guo X, Ren X, Yan C, Huang H. Quantitative Proteomics Reveals the Role of Lysine Lactylation in Lenalidomide-Resistance in Multiple Myeloma Cells.. ACS Chem Biol 20(7):1728-1738. 2025 Jul 18. PMID: 40590393.

[4] 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.