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Overview

Uniprot IDQ9NX58
Protein NameCell growth-regulating nucleolar protein
Gene NameLYAR
OrganismHomo sapiens

Kla Sites from experimental identification

Position Flanking peptide
14 NACGESVKKIQVEKH
168 PHAEISTKVPASKVK
175 KVPASKVKDAVEQQG
186 EQQGEVKKNKRERKE
207 KREKKELKLENHQEN
247 EANGSAGKRSKKKKQ
288 DSKKKKMKLPEHPEG
57 KCISEDQKYGGKGYE
61 EDQKYGGKGYEGKTH
66 GGKGYEGKTHKGDIK

Function

Plays a role in the maintenance of the appropriate processing of 47S/45S pre-rRNA to 32S/30S pre-rRNAs and their subsequent processing to produce 18S and 28S rRNAs (PubMed:24495227). Also acts at the level of transcription regulation. Along with PRMT5, binds the gamma-globin (HBG1/HBG2) promoter and represses its expression (PubMed:25092918). In neuroblastoma cells, may also repress the expression of oxidative stress genes, including CHAC1, HMOX1, SLC7A11, ULBP1 and SNORD41 that encodes a small nucleolar RNA (PubMed:28686580). Preferentially binds to a DNA motif containing 5'-GGTTAT-3' (PubMed:25092918). Negatively regulates the antiviral innate immune response by targeting IRF3 and impairing its DNA-binding activity (PubMed:31413131). In addition, inhibits NF-kappa-B-mediated expression of pro-inflammatory cytokines (PubMed:31413131). Stimulates phagocytosis of photoreceptor outer segments by retinal pigment epithelial cells (By similarity). Prevents nucleolin/NCL self-cleavage, maintaining a normal steady-state level of NCL protein in undifferentiated embryonic stem cells (ESCs), which in turn is essential for ESC self-renewal (By similarity)

Protein Sequence

10 MVFFTCNACG 20 ESVKKIQVEK 30 HVSVCRNCEC 40 LSCIDCGKDF 50 WGDDYKNHVK 60 CISEDQKYGG 70 KGYEGKTHKG 80 DIKQQAWIQK 90 ISELIKRPNV 100 SPKVRELLEQ 110 ISAFDNVPRK 120 KAKFQNWMKN 130 SLKVHNESIL 140 DQVWNIFSEA 150 SNSEPVNKEQ 160 DQRPLHPVAN 170 PHAEISTKVP 180 ASKVKDAVEQ 190 QGEVKKNKRE 200 RKEERQKKRK 210 REKKELKLEN 220 HQENSRNQKP 230 KKRKKGQEAD 240 LEAGGEEVPE 250 ANGSAGKRSK 260 KKKQRKDSAS 270 EEEARVGAGK 280 RKRRHSEVET 290 DSKKKKMKLP 300 EHPEGGEPED 310 DEAPAKGKFN 320 WKGTIKAILK 330 QAPDNEITIK 340 KLRKKVLAQY 350 YTVTDEHHRS 360 EEELLVIFNK 370 KISKNPTFKL LKDKVKLVK

Gene Ontology

Classification GO ID Description
Cellular Component GO:0005737 cytoplasm
Cellular Component GO:0005730 nucleolus
Cellular Component GO:0005654 nucleoplasm
Cellular Component GO:0005634 nucleus
Cellular Component GO:0001750 photoreceptor outer segment
Molecular Function GO:0003677 DNA binding
Molecular Function GO:0140297 DNA-binding transcription factor binding
Molecular Function GO:0042802 identical protein binding
Molecular Function GO:0003723 RNA binding
Molecular Function GO:0140416 transcription regulator inhibitor activity
Molecular Function GO:0008270 zinc ion binding
Biological Process GO:0006351 DNA-templated transcription
Biological Process GO:0048821 erythrocyte development
Biological Process GO:0045087 innate immune response
Biological Process GO:0045824 negative regulation of innate immune response
Biological Process GO:0000122 negative regulation of transcription by RNA polymerase II
Biological Process GO:0050766 positive regulation of phagocytosis
Biological Process GO:0045943 positive regulation of transcription by RNA polymerase I
Biological Process GO:0006364 rRNA processing

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] 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.

[3] 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.