Search Results

Overview

Uniprot IDQ9Y3A5
Protein NameRibosome maturation protein SBDS
Gene NameSBDS
OrganismHomo sapiens

Kla Sites from experimental identification

Position Flanking peptide
151 VKTNKSTKQQALEVI
231 IKKETKGKGSLEVLN
98 GEVQVSDKERHTQLE

Function

Required for the assembly of mature ribosomes and ribosome biogenesis. Together with EFL1, triggers the GTP-dependent release of EIF6 from 60S pre-ribosomes in the cytoplasm, thereby activating ribosomes for translation competence by allowing 80S ribosome assembly and facilitating EIF6 recycling to the nucleus, where it is required for 60S rRNA processing and nuclear export. Required for normal levels of protein synthesis. May play a role in cellular stress resistance. May play a role in cellular response to DNA damage. May play a role in cell proliferation

Protein Sequence

10 MSIFTPTNQI 20 RLTNVAVVRM 30 KRAGKRFEIA 40 CYKNKVVGWR 50 SGVEKDLDEV 60 LQTHSVFVNV 70 SKGQVAKKED 80 LISAFGTDDQ 90 TEICKQILTK 100 GEVQVSDKER 110 HTQLEQMFRD 120 IATIVADKCV 130 NPETKRPYTV 140 ILIERAMKDI 150 HYSVKTNKST 160 KQQALEVIKQ 170 LKEKMKIERA 180 HMRLRFILPV 190 NEGKKLKEKL 200 KPLIKVIESE 210 DYGQQLEIVC 220 LIDPGCFREI 230 DELIKKETKG 240 KGSLEVLNLK 250 DVEEGDEKFE

Gene Ontology

Classification GO ID Description
Cellular Component GO:0005737 cytoplasm
Cellular Component GO:0005829 cytosol
Cellular Component GO:0005730 nucleolus
Cellular Component GO:0005654 nucleoplasm
Cellular Component GO:0005634 nucleus
Cellular Component GO:0000922 spindle pole
Molecular Function GO:0008017 microtubule binding
Molecular Function GO:0043022 ribosome binding
Molecular Function GO:0003723 RNA binding
Molecular Function GO:0019843 rRNA binding
Biological Process GO:0048539 bone marrow development
Biological Process GO:0030282 bone mineralization
Biological Process GO:0042256 cytosolic ribosome assembly
Biological Process GO:0002244 hematopoietic progenitor cell differentiation
Biological Process GO:0030595 leukocyte chemotaxis
Biological Process GO:0007052 mitotic spindle organization
Biological Process GO:0006364 rRNA processing

Reference

[1] Yang D, Yin J, Shan L, Yi X, Zhang W et al.. Identification of lysine-lactylated substrates in gastric cancer cells.. iScience 25(7):104630. 2022 Jul 15. PMID: 35800753.

[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] 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.

[4] 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.

[5] 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.

[6] 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.