Search Results

Overview

Uniprot IDP30153
Protein NameSerine/threonine-protein phosphatase 2A 65 kDa regulatory subunit A alpha isoform
Gene NamePPP2R1A
OrganismHomo sapiens

Kla Sites from experimental identification

Position Flanking peptide
107 EETVVRDKAVESLRA
133 AHFVPLVKRLAGGDW
163 PRVSSAVKAELRQYF
188 VRRAAASKLGEFAKV
266 VRYMVADKFTELQKA
34 LRLNSIKKLSTIALA

Function

The PR65 subunit of protein phosphatase 2A serves as a scaffolding molecule to coordinate the assembly of the catalytic subunit and a variable regulatory B subunit (PubMed:15525651, PubMed:16580887, PubMed:33243860, PubMed:33633399, PubMed:34004147, PubMed:8694763). Upon interaction with GNA12 promotes dephosphorylation of microtubule associated protein TAU/MAPT (PubMed:15525651). Required for proper chromosome segregation and for centromeric localization of SGO1 in mitosis (PubMed:16580887). Together with RACK1 adapter, mediates dephosphorylation of AKT1 at 'Ser-473', preventing AKT1 activation and AKT-mTOR signaling pathway (By similarity). Dephosphorylation of AKT1 is essential for regulatory T-cells (Treg) homeostasis and stability (By similarity). Part of the striatin-interacting phosphatase and kinase (STRIPAK) complexes (PubMed:18782753, PubMed:33633399). STRIPAK complexes have critical roles in protein (de)phosphorylation and are regulators of multiple signaling pathways including Hippo, MAPK, nuclear receptor and cytoskeleton remodeling (PubMed:18782753, PubMed:33633399). Different types of STRIPAK complexes are involved in a variety of biological processes such as cell growth, differentiation, apoptosis, metabolism and immune regulation (PubMed:18782753, PubMed:33633399). Key mediator of a quality checkpoint during transcription elongation as part of the Integrator-PP2A (INTAC) complex (PubMed:33243860, PubMed:34004147). The INTAC complex drives premature transcription termination of transcripts that are unfavorably configured for transcriptional elongation: within the INTAC complex, acts as a scaffolding subunit for PPP2CA, which catalyzes dephosphorylation of the C-terminal domain (CTD) of Pol II subunit POLR2A/RPB1 and SUPT5H/SPT5, thereby preventing transcriptional elongation (PubMed:33243860, PubMed:34004147). Regulates the recruitment of the SKA complex to kinetochores (PubMed:28982702)

Protein Sequence

10 MAAADGDDSL 20 YPIAVLIDEL 30 RNEDVQLRLN 40 SIKKLSTIAL 50 ALGVERTRSE 60 LLPFLTDTIY 70 DEDEVLLALA 80 EQLGTFTTLV 90 GGPEYVHCLL 100 PPLESLATVE 110 ETVVRDKAVE 120 SLRAISHEHS 130 PSDLEAHFVP 140 LVKRLAGGDW 150 FTSRTSACGL 160 FSVCYPRVSS 170 AVKAELRQYF 180 RNLCSDDTPM 190 VRRAAASKLG 200 EFAKVLELDN 210 VKSEIIPMFS 220 NLASDEQDSV 230 RLLAVEACVN 240 IAQLLPQEDL 250 EALVMPTLRQ 260 AAEDKSWRVR 270 YMVADKFTEL 280 QKAVGPEITK 290 TDLVPAFQNL 300 MKDCEAEVRA 310 AASHKVKEFC 320 ENLSADCREN 330 VIMSQILPCI 340 KELVSDANQH 350 VKSALASVIM 360 GLSPILGKDN 370 TIEHLLPLFL 380 AQLKDECPEV 390 RLNIISNLDC 400 VNEVIGIRQL 410 SQSLLPAIVE 420 LAEDAKWRVR 430 LAIIEYMPLL 440 AGQLGVEFFD 450 EKLNSLCMAW 460 LVDHVYAIRE 470 AATSNLKKLV 480 EKFGKEWAHA 490 TIIPKVLAMS 500 GDPNYLHRMT 510 TLFCINVLSE 520 VCGQDITTKH 530 MLPTVLRMAG 540 DPVANVRFNV 550 AKSLQKIGPI 560 LDNSTLQSEV 570 KPILEKLTQD 580 QDVDVKYFAQ EALTVLSLA

Gene Ontology

Classification GO ID Description
Molecular Function GO:0019888 protein phosphatase regulator activity
Cellular Component GO:0000785 chromatin
Cellular Component GO:0000775 chromosome, centromeric region
Cellular Component GO:0005737 cytoplasm
Cellular Component GO:0005829 cytosol
Cellular Component GO:0030425 dendrite
Cellular Component GO:0070062 extracellular exosome
Cellular Component GO:0090443 FAR/SIN/STRIPAK complex
Cellular Component GO:0098978 glutamatergic synapse
Cellular Component GO:0160232 INTAC complex
Cellular Component GO:0016328 lateral plasma membrane
Cellular Component GO:0016020 membrane
Cellular Component GO:0015630 microtubule cytoskeleton
Cellular Component GO:0005739 mitochondrion
Cellular Component GO:0043005 neuron projection
Cellular Component GO:0043025 neuronal cell body
Cellular Component GO:0005634 nucleus
Cellular Component GO:0000159 protein phosphatase type 2A complex
Molecular Function GO:1990405 protein antigen binding
Molecular Function GO:0046982 protein heterodimerization activity
Molecular Function GO:0004722 protein serine/threonine phosphatase activity
Biological Process GO:0007059 chromosome segregation
Biological Process GO:0035556 intracellular signal transduction
Biological Process GO:0051754 meiotic sister chromatid cohesion, centromeric
Biological Process GO:0035331 negative regulation of hippo signaling
Biological Process GO:0051898 negative regulation of phosphatidylinositol 3-kinase/protein kinase B signal transduction
Biological Process GO:0065003 protein-containing complex assembly
Biological Process GO:0045595 regulation of cell differentiation
Biological Process GO:0040008 regulation of growth
Biological Process GO:0035330 regulation of hippo signaling
Biological Process GO:0034243 regulation of transcription elongation by RNA polymerase II
Biological Process GO:0160240 RNA polymerase II transcription initiation surveillance
Biological Process GO:0016180 snRNA processing
Biological Process GO:0051225 spindle assembly
Biological Process GO:0043029 T cell homeostasis

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] 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.

[3] 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.