PP4R2_PONAB
ID PP4R2_PONAB Reviewed; 417 AA.
AC Q5R9U6;
DT 11-SEP-2007, integrated into UniProtKB/Swiss-Prot.
DT 21-DEC-2004, sequence version 1.
DT 03-AUG-2022, entry version 63.
DE RecName: Full=Serine/threonine-protein phosphatase 4 regulatory subunit 2;
GN Name=PPP4R2;
OS Pongo abelii (Sumatran orangutan) (Pongo pygmaeus abelii).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Pongo.
OX NCBI_TaxID=9601;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Heart;
RG The German cDNA consortium;
RL Submitted (NOV-2004) to the EMBL/GenBank/DDBJ databases.
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 EMBL; CR859286; CAH91464.1; -; mRNA.
DR RefSeq; NP_001125861.1; NM_001132389.1.
DR AlphaFoldDB; Q5R9U6; -.
DR STRING; 9601.ENSPPYP00000015338; -.
DR Ensembl; ENSPPYT00000060241; ENSPPYP00000041300; ENSPPYG00000013715.
DR GeneID; 100172791; -.
DR KEGG; pon:100172791; -.
DR CTD; 151987; -.
DR eggNOG; KOG3175; Eukaryota.
DR GeneTree; ENSGT00940000160975; -.
DR InParanoid; Q5R9U6; -.
DR OrthoDB; 774806at2759; -.
DR Proteomes; UP000001595; Chromosome 3.
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.
DR InterPro; IPR015267; PPP4R2.
DR PANTHER; PTHR16487; PTHR16487; 1.
DR Pfam; PF09184; PPP4R2; 1.
PE 2: Evidence at transcript level;
KW Cytoplasm; Cytoskeleton; mRNA processing; mRNA splicing; Nucleus;
KW Phosphoprotein; Reference proteome.
FT CHAIN 1..417
FT /note="Serine/threonine-protein phosphatase 4 regulatory
FT subunit 2"
FT /id="PRO_0000299367"
FT REGION 140..417
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 140..173
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 183..201
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 202..216
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 228..258
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 259..279
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 280..297
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 298..312
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 313..334
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 349..363
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 381..396
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 398..417
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 159
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9NY27"
FT MOD_RES 226
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9NY27"
SQ SEQUENCE 417 AA; 46850 MW; 7C339D2759B0568F CRC64;
MDVERLQEAL KDFEKRGKKE VCPVLDQFLC HVAKTGETMI QWSQFKGYFI FKLEKVMDDF
RTSAPEPRGP PNPNVEYIPF DEMKERILKI VTGFNGIPFT IQRLCELLTD PRRNYTGTDK
FLRGVEKNVM VVSCVYPSSE KNNSSSLNRM NGVMFPGNSP SYTERSNING PGTPRPLNRP
KVSLSAPMTT NGLPESTDSK EANLQQNEEK SHSDSSTSES EVSSVSPLKN KHPDEDAVEA
EGHEVKRLRF DKEGEVRETA SQTTSSEISS AVVGETETSS SSQDKDKDSR CTRQHCTEED
EEEDEEEEEE SFMTSREMIP ERKNQEKESD DALTVNEETS EENNQMEESD VSQAEKDLLH
SEGSENEGPV SNDSSDCHET EELVGSNSSK TGEILSESSM ENDDEATEVT DEPMEQD
