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Sep. 10, 2014:
A total of 174 experimentally verified S-nitrosylation sites on 94 S-nitrosylated proteins from individualized human colorectal cancer tissues using a label-free quantitation strategy.

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Protein Name: Serine/threonine-protein phosphatase 2A 65 kDa regulatory subunit A alpha isoform

UniprotKB/SwissProt ID: P30153 (P30153)

Gene Name: PPP2R1A

Organism: Homo sapiens (Human)

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)

Other Modifications: View all modification sites in dbPTM

Protein Subcellular Localization: Cytoplasm. Nucleus. Chromosome. Chromosome, centromere. Lateral cell membrane. Cell projection, dendrite

Graphical Visualization of S-nitrosylation Sites:
InterPro ID Domain Name
IPR011989 ARM-like
IPR016024 ARM-type_fold
IPR000357 HEAT
IPR021133 HEAT_type_2
IPR054573 PP2A/SF3B1-like_HEAT
IPR051023 PP2A_Regulatory_Subunit_A

The S-nitrosylation sites of P30153

No. Position S-nitrosylated Peptide Secondary Structure of S-nitrosylated Peptide Solvent Accessibility of nitrosylated Site PubMed ID
1 148 GDWFTSRTSA C GLFSVCYPRV  CCCCCCCCCH H HHHHHHHHHC  4.95%
2 154 RTSACGLFSV C YPRVSSAVKA  CCCCCCCCCH H HHHHHHHHHC  3.61%
3 174 AELRQYFRNL C SDDTPMVRRA  CCCCCCCCCH H HHHHHHHHHC  4.84%
4 310 AAASHKVKEF C ENLSADCREN  CCCCCCCCCH H HHHHHHHHHC  3.39%
5 317 KEFCENLSAD C RENVIMSQIL  CCCCCCCCCH H HHHHHHHHHC  6.17%
6 329 ENVIMSQILP C IKELVSDANQ  CCCCCCCCCH H HHHHHHHHHC  6.6%
7 377 PLFLAQLKDE C PEVRLNIISN  CCCCCCCCCH H HHHHHHHHHC  5.09%
8 390 VRLNIISNLD C VNEVIGIRQL  CCCCCCCCCH H HHHHHHHHHC  3.89% 19483679