Search Results

Overview

Uniprot IDQ9UHR5
Protein NameSAP30-binding protein
Gene NameSAP30BP
OrganismHomo sapiens

Kla Sites from experimental identification

Position Flanking peptide
134 CSNHLQDKIQKLYER
137 HLQDKIQKLYERKIK
210 AQKIEMDKLEKAKKE
220 KAKKERTKIEFVTGT
228 IEFVTGTKKGTTTNA
229 EFVTGTKKGTTTNAT
304 SAVGTIVKKAKQ***
305 AVGTIVKKAKQ****

Function

Plays a role in transcriptional repression by promoting histone deacetylase activity, leading to deacetylation of histone H3 (PubMed:21221920). Acts as a regulator of pre-mRNA splicing by facilitating assembly of the cyclin-L-CDK11 cyclin-dependent protein kinase complex, thereby promoting phosphorylation of SF3B1 (PubMed:38059508). May be involved in the regulation of beta-2-microglobulin genes (By similarity)

Protein Sequence

10 MAGKKNVLSS 20 LAVYAEDSEP 30 ESDGEAGIEA 40 VGSAAEEKGG 50 LVSDAYGEDD 60 FSRLGGDEDG 70 YEEEEDENSR 80 QSEDDDSETE 90 KPEADDPKDN 100 TEAEKRDPQE 110 LVASFSERVR 120 NMSPDEIKIP 130 PEPPGRCSNH 140 LQDKIQKLYE 150 RKIKEGMDMN 160 YIIQRKKEFR 170 NPSIYEKLIQ 180 FCAIDELGTN 190 YPKDMFDPHG 200 WSEDSYYEAL 210 AKAQKIEMDK 220 LEKAKKERTK 230 IEFVTGTKKG 240 TTTNATSTTT 250 TTASTAVADA 260 QKRKSKWDSA 270 IPVTTIAQPT 280 ILTTTATLPA 290 VVTVTTSASG 300 SKTTVISAVG TIVKKAKQ

Gene Ontology

Classification GO ID Description
Cellular Component GO:0016607 nuclear speck
Cellular Component GO:0005654 nucleoplasm
Cellular Component GO:0005634 nucleus
Molecular Function GO:0016538 cyclin-dependent protein serine/threonine kinase regulator activity
Biological Process GO:0006351 DNA-templated transcription
Biological Process GO:0006397 mRNA processing
Biological Process GO:0006355 regulation of DNA-templated transcription
Biological Process GO:0048024 regulation of mRNA splicing, via spliceosome
Biological Process GO:0009615 response to virus
Biological Process GO:0008380 RNA splicing

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] 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.

[4] 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.

[5] 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.

[6] 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.

[7] 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.

[8] 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.