PP4R2_RABIT
ID PP4R2_RABIT Reviewed; 78 AA.
AC P0C5B7;
DT 11-SEP-2007, integrated into UniProtKB/Swiss-Prot.
DT 11-SEP-2007, sequence version 1.
DT 25-MAY-2022, entry version 29.
DE RecName: Full=Serine/threonine-protein phosphatase 4 regulatory subunit 2;
DE Flags: Fragments;
GN Name=PPP4R2;
OS Oryctolagus cuniculus (Rabbit).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Lagomorpha; Leporidae; Oryctolagus.
OX NCBI_TaxID=9986;
RN [1]
RP PROTEIN SEQUENCE, AND INTERACTION WITH PPP4C.
RX PubMed=10769191; DOI=10.1042/bj3470845;
RA Hastie C.J., Carnegie G.K., Morrice N., Cohen P.T.W.;
RT "A novel 50 kDa protein forms complexes with protein phosphatase 4 and is
RT located at centrosomal microtubule organizing centres.";
RL Biochem. J. 347:845-855(2000).
CC -!- FUNCTION: Regulatory subunit of serine/threonine-protein phosphatase 4
CC (PP4). May regulate the activity of PPP4C at centrosomal microtubule
CC organizing centers. Its interaction with the SMN complex leads to
CC enhance the temporal localization of snRNPs, suggesting a role of PPP4C
CC in maturation of spliceosomal snRNPs. The PPP4C-PPP4R2-PPP4R3A PP4
CC complex specifically dephosphorylates H2AX phosphorylated on 'Ser-140'
CC (gamma-H2AX) generated during DNA replication and required for DNA
CC double strand break repair (By similarity). Mediates RPA2
CC dephosphorylation by recruiting PPP4C to RPA2 in a DNA damage-dependent
CC manner. RPA2 dephosphorylation is required for the efficient RPA2-
CC mediated recruitment of RAD51 to chromatin following double strand
CC breaks, an essential step for DNA repair (By similarity).
CC {ECO:0000250}.
CC -!- SUBUNIT: Serine/threonine-protein phosphatase 4 (PP4) occurs in
CC different assemblies of the catalytic and one or more regulatory
CC subunits. Component of the PP4 complexes PPP4C-PPP4R2, PPP4C-PPP4R2-
CC PPP4R3A and PPP4C-PPP4R2-PPP4R3B. The PPP4C-PPP4R2 complex appears to
CC be a tetramer composed of 2 molecules of PPP4C and 2 molecules of
CC PPP4R2. Interacts with DDX20/GEMIN3 and GEMIN4 (By similarity).
CC Interacts with RPA2; this DNA damage-dependent interaction recruits
CC PPP4C leading to RPA2 dephosphorylation (By similarity). {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton, microtubule organizing
CC center, centrosome {ECO:0000250}. Nucleus {ECO:0000250}. Note=Ionizing
CC radiation induces relocalization to nuclear foci and colocalization
CC with RPA2. {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the PPP4R2 family. {ECO:0000305}.
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DR AlphaFoldDB; P0C5B7; -.
DR InParanoid; P0C5B7; -.
DR Proteomes; UP000001811; Unplaced.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-KW.
DR GO; GO:0005815; C:microtubule organizing center; IEA:UniProtKB-SubCell.
DR GO; GO:0005634; C:nucleus; ISS:UniProtKB.
DR GO; GO:0030289; C:protein phosphatase 4 complex; ISS:UniProtKB.
DR GO; GO:0019888; F:protein phosphatase regulator activity; ISS:UniProtKB.
DR GO; GO:0006397; P:mRNA processing; IEA:UniProtKB-KW.
DR GO; GO:0010569; P:regulation of double-strand break repair via homologous recombination; ISS:UniProtKB.
DR GO; GO:0008380; P:RNA splicing; IEA:UniProtKB-KW.
PE 1: Evidence at protein level;
KW Cytoplasm; Cytoskeleton; Direct protein sequencing; mRNA processing;
KW mRNA splicing; Nucleus; Reference proteome.
FT CHAIN <1..>78
FT /note="Serine/threonine-protein phosphatase 4 regulatory
FT subunit 2"
FT /id="PRO_0000299368"
FT REGION 53..78
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT NON_CONS 11..12
FT /evidence="ECO:0000305"
FT NON_CONS 23..24
FT /evidence="ECO:0000305"
FT NON_CONS 39..40
FT /evidence="ECO:0000305"
FT NON_CONS 44..45
FT /evidence="ECO:0000305"
FT NON_CONS 51..52
FT /evidence="ECO:0000305"
FT NON_CONS 64..65
FT /evidence="ECO:0000305"
FT NON_TER 1
FT NON_TER 78
SQ SEQUENCE 78 AA; 9047 MW; 59F30142E559A070 CRC64;
LQEALKDFEK RTGETMIQWS QFKGPPNPNV EYIPFDEMKN VMVVMNGVMF PINGPGTPRP
LNRPNLQQNE EKNHHPDE