UniProt functional annotation for Q13362



	UniProt functional annotation for Q13362

UniProt code: Q13362.

Organism: Homo sapiens (Human).

Taxonomy: Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae; Homo.

Function: The B regulatory subunit might modulate substrate selectivity and catalytic activity, and also might direct the localization of the catalytic enzyme to a particular subcellular compartment. The PP2A- PPP2R5C holoenzyme may specifically dephosphorylate and activate TP53 and play a role in DNA damage-induced inhibition of cell proliferation. PP2A-PPP2R5C may also regulate the ERK signaling pathway through ERK dephosphorylation. {ECO:0000269|PubMed:16456541, ECO:0000269|PubMed:17245430}.

Subunit: PP2A consists of a common heterodimeric core enzyme, composed of PPP2CA a 36 kDa catalytic subunit (subunit C) and PPP2R1A a 65 kDa constant regulatory subunit (PR65 or subunit A), that associates with a variety of regulatory subunits. Proteins that associate with the core dimer include three families of regulatory subunits B (the R2/B/PR55/B55, R3/B''/PR72/PR130/PR59 and R5/B'/B56 families), the 48 kDa variable regulatory subunit, viral proteins, and cell signaling molecules. Interacts with PPP2CA AND PPP2R1A; the interaction is direct. Interacts with SGO1; the interaction is direct. Isoform 1 and isoform 2 interact with TP53 (phosphorylated at Ser-15 by ATM); increased upon DNA damage it drives PP2A-mediated dephosphorylation of TP53 at Thr-55. Interacts with IER3 and/or ERK kinases; regulates ERK dephosphorylation. Interacts with CIP2A; this interaction stabilizes CIP2A (PubMed:28174209). {ECO:0000269|PubMed:16456541, ECO:0000269|PubMed:16541025, ECO:0000269|PubMed:16580887, ECO:0000269|PubMed:17086192, ECO:0000269|PubMed:17174897, ECO:0000269|PubMed:17245430, ECO:0000269|PubMed:17967874, ECO:0000269|PubMed:19716788, ECO:0000269|PubMed:28174209}.

Subcellular location: Nucleus. Chromosome, centromere.

Tissue specificity: Highest levels in heart, skeletal muscle and brain. Lower levels in pancreas, kidney, lung and placenta. Very low levels in liver.

Induction: Up-regulated upon DNA damage. {ECO:0000269|PubMed:17245430}.

Ptm: Isoform Gamma-3 is phosphorylated on serine residues. Isoform Gamma-1 phosphorylation by ERK2 is IER3-dependent and inhibits ERK dephosphorylation by PP2A-PPP2R5C. {ECO:0000269|PubMed:16456541, ECO:0000269|PubMed:8703017}.

Similarity: Belongs to the phosphatase 2A regulatory subunit B56 family. {ECO:0000305}.

Sequence caution: Sequence=AAC50387.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305}; Sequence=BAG63760.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};

Annotations taken from UniProtKB at the EBI.


Organism:		Homo sapiens (Human).
Taxonomy:		Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae; Homo.



Function:		The B regulatory subunit might modulate substrate selectivity and catalytic activity, and also might direct the localization of the catalytic enzyme to a particular subcellular compartment. The PP2A- PPP2R5C holoenzyme may specifically dephosphorylate and activate TP53 and play a role in DNA damage-induced inhibition of cell proliferation. PP2A-PPP2R5C may also regulate the ERK signaling pathway through ERK dephosphorylation. {ECO:0000269\|PubMed:16456541, ECO:0000269\|PubMed:17245430}.


Subunit:		PP2A consists of a common heterodimeric core enzyme, composed of PPP2CA a 36 kDa catalytic subunit (subunit C) and PPP2R1A a 65 kDa constant regulatory subunit (PR65 or subunit A), that associates with a variety of regulatory subunits. Proteins that associate with the core dimer include three families of regulatory subunits B (the R2/B/PR55/B55, R3/B''/PR72/PR130/PR59 and R5/B'/B56 families), the 48 kDa variable regulatory subunit, viral proteins, and cell signaling molecules. Interacts with PPP2CA AND PPP2R1A; the interaction is direct. Interacts with SGO1; the interaction is direct. Isoform 1 and isoform 2 interact with TP53 (phosphorylated at Ser-15 by ATM); increased upon DNA damage it drives PP2A-mediated dephosphorylation of TP53 at Thr-55. Interacts with IER3 and/or ERK kinases; regulates ERK dephosphorylation. Interacts with CIP2A; this interaction stabilizes CIP2A (PubMed:28174209). {ECO:0000269\|PubMed:16456541, ECO:0000269\|PubMed:16541025, ECO:0000269\|PubMed:16580887, ECO:0000269\|PubMed:17086192, ECO:0000269\|PubMed:17174897, ECO:0000269\|PubMed:17245430, ECO:0000269\|PubMed:17967874, ECO:0000269\|PubMed:19716788, ECO:0000269\|PubMed:28174209}.
Subcellular location:		Nucleus. Chromosome, centromere.
Tissue specificity:		Highest levels in heart, skeletal muscle and brain. Lower levels in pancreas, kidney, lung and placenta. Very low levels in liver.
Induction:		Up-regulated upon DNA damage. {ECO:0000269\|PubMed:17245430}.
Ptm:		Isoform Gamma-3 is phosphorylated on serine residues. Isoform Gamma-1 phosphorylation by ERK2 is IER3-dependent and inhibits ERK dephosphorylation by PP2A-PPP2R5C. {ECO:0000269\|PubMed:16456541, ECO:0000269\|PubMed:8703017}.
Similarity:		Belongs to the phosphatase 2A regulatory subunit B56 family. {ECO:0000305}.
Sequence caution:		Sequence=AAC50387.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305}; Sequence=BAG63760.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};