Search Results

Overview

Uniprot ID	P63151
Protein Name	Serine/threonine-protein phosphatase 2A 55 kDa regulatory subunit B alpha isoform
Gene Name	PPP2R2A
Organism	Homo sapiens

Kla Sites from experimental identification

Position	Flanking peptide
405	CASGKRKKDEISVDS

Function

Substrate-recognition subunit of protein phosphatase 2A (PP2A) that plays a key role in cell cycle by controlling mitosis entry and exit (PubMed:1849734, PubMed:33108758). Involved in chromosome clustering during late mitosis by mediating dephosphorylation of MKI67 (By similarity). Essential for serine/threonine-protein phosphatase 2A-mediated dephosphorylation of WEE1, preventing its ubiquitin-mediated proteolysis, increasing WEE1 protein levels, and promoting the G2/M checkpoint (PubMed:33108758)

Protein Sequence

10 MAGAGGGNDI 20 QWCFSQVKGA 30 VDDDVAEADI 40 ISTVEFNHSG 50 ELLATGDKGG 60 RVVIFQQEQE 70 NKIQSHSRGE 80 YNVYSTFQSH 90 EPEFDYLKSL 100 EIEEKINKIR 110 WLPQKNAAQF 120 LLSTNDKTIK 130 LWKISERDKR 140 PEGYNLKEED 150 GRYRDPTTVT 160 TLRVPVFRPM 170 DLMVEASPRR 180 IFANAHTYHI 190 NSISINSDYE 200 TYLSADDLRI 210 NLWHLEITDR 220 SFNIVDIKPA 230 NMEELTEVIT 240 AAEFHPNSCN 250 TFVYSSSKGT 260 IRLCDMRASA 270 LCDRHSKLFE 280 EPEDPSNRSF 290 FSEIISSISD 300 VKFSHSGRYM 310 MTRDYLSVKI 320 WDLNMENRPV 330 ETYQVHEYLR 340 SKLCSLYEND 350 CIFDKFECCW 360 NGSDSVVMTG 370 SYNNFFRMFD 380 RNTKRDITLE 390 ASRENNKPRT 400 VLKPRKVCAS 410 GKRKKDEISV 420 DSLDFNKKIL 430 HTAWHPKENI 440 IAVATTNNLY IFQDKVN

Gene Ontology

Classification	GO ID	Description
Cellular Component	GO:0005829	cytosol
Cellular Component	GO:0098978	glutamatergic synapse
Cellular Component	GO:0005654	nucleoplasm
Cellular Component	GO:0000159	protein phosphatase type 2A complex
Molecular Function	GO:0140767	enzyme-substrate adaptor activity
Molecular Function	GO:0051721	protein phosphatase 2A binding
Molecular Function	GO:0019888	protein phosphatase regulator activity
Molecular Function	GO:0044877	protein-containing complex binding
Molecular Function	GO:0048156	tau protein binding
Biological Process	GO:0006470	protein dephosphorylation
Biological Process	GO:0051983	regulation of chromosome segregation

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] Shi CM, Wang QC, Li XL, Yang YH, Tang XY et al.. Global Profiling of Protein Lactylation in Human Hippocampi.. Proteomics Clin Appl 19(2):e202400061. 2025 Mar. PMID: 39610256.

[4] 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.

[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] 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.

[7] 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.