PP4R2_MOUSE
ID PP4R2_MOUSE Reviewed; 417 AA.
AC Q0VGB7; Q4G0D4; Q6P6N7; Q6PHU6; Q8BUU5;
DT 11-SEP-2007, integrated into UniProtKB/Swiss-Prot.
DT 05-SEP-2006, sequence version 1.
DT 03-AUG-2022, entry version 97.
DE RecName: Full=Serine/threonine-protein phosphatase 4 regulatory subunit 2;
GN Name=Ppp4r2;
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J; TISSUE=Cerebellum;
RX PubMed=16141072; DOI=10.1126/science.1112014;
RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT "The transcriptional landscape of the mammalian genome.";
RL Science 309:1559-1563(2005).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J, CD-1, and NMRI;
RC TISSUE=Brain, Mammary tumor, and Neural stem cell;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [3]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-159, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Liver;
RX PubMed=17242355; DOI=10.1073/pnas.0609836104;
RA Villen J., Beausoleil S.A., Gerber S.A., Gygi S.P.;
RT "Large-scale phosphorylation analysis of mouse liver.";
RL Proc. Natl. Acad. Sci. U.S.A. 104:1488-1493(2007).
RN [4]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-159 AND SER-226, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain, Kidney, Liver, Lung, Pancreas, Spleen, and Testis;
RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL Cell 143:1174-1189(2010).
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; AK082539; BAC38523.1; -; mRNA.
DR EMBL; BC056340; AAH56340.2; -; mRNA.
DR EMBL; BC062117; AAH62117.1; -; mRNA.
DR EMBL; BC098464; AAH98464.1; -; mRNA.
DR EMBL; BC110429; AAI10430.1; -; mRNA.
DR CCDS; CCDS20391.1; -.
DR RefSeq; NP_891984.1; NM_182939.4.
DR AlphaFoldDB; Q0VGB7; -.
DR BioGRID; 231238; 9.
DR ComplexPortal; CPX-158; PPP4C-PPP4R2-PPP4R3A protein phosphatase 4 complex.
DR ComplexPortal; CPX-163; PPP4C-PPP4R2 protein phosphatase 4 complex.
DR ComplexPortal; CPX-164; PPP4C-PPP4R2-PPP4R3B protein phosphatase 4 complex.
DR IntAct; Q0VGB7; 1.
DR MINT; Q0VGB7; -.
DR STRING; 10090.ENSMUSP00000066314; -.
DR iPTMnet; Q0VGB7; -.
DR PhosphoSitePlus; Q0VGB7; -.
DR EPD; Q0VGB7; -.
DR jPOST; Q0VGB7; -.
DR MaxQB; Q0VGB7; -.
DR PaxDb; Q0VGB7; -.
DR PeptideAtlas; Q0VGB7; -.
DR PRIDE; Q0VGB7; -.
DR ProteomicsDB; 289722; -.
DR DNASU; 232314; -.
DR GeneID; 232314; -.
DR KEGG; mmu:232314; -.
DR UCSC; uc009dcb.1; mouse.
DR CTD; 151987; -.
DR MGI; MGI:3027896; Ppp4r2.
DR eggNOG; KOG3175; Eukaryota.
DR InParanoid; Q0VGB7; -.
DR OrthoDB; 774806at2759; -.
DR PhylomeDB; Q0VGB7; -.
DR TreeFam; TF105561; -.
DR Reactome; R-MMU-5693607; Processing of DNA double-strand break ends.
DR BioGRID-ORCS; 232314; 23 hits in 111 CRISPR screens.
DR ChiTaRS; Ppp4r2; mouse.
DR PRO; PR:Q0VGB7; -.
DR Proteomes; UP000000589; Unplaced.
DR RNAct; Q0VGB7; protein.
DR GO; GO:0000785; C:chromatin; ISO:MGI.
DR GO; GO:0005737; C:cytoplasm; IDA:MGI.
DR GO; GO:0005815; C:microtubule organizing center; IEA:UniProtKB-SubCell.
DR GO; GO:0005654; C:nucleoplasm; ISO:MGI.
DR GO; GO:0005634; C:nucleus; IDA:MGI.
DR GO; GO:0030289; C:protein phosphatase 4 complex; IDA:MGI.
DR GO; GO:0019888; F:protein phosphatase regulator activity; ISS:UniProtKB.
DR GO; GO:0030674; F:protein-macromolecule adaptor activity; ISO:MGI.
DR GO; GO:0002244; P:hematopoietic progenitor cell differentiation; IMP:MGI.
DR GO; GO:0006397; P:mRNA processing; IEA:UniProtKB-KW.
DR GO; GO:0033128; P:negative regulation of histone phosphorylation; ISO:MGI.
DR GO; GO:0006470; P:protein dephosphorylation; IBA:GO_Central.
DR GO; GO:2000779; P:regulation of double-strand break repair; ISO:MGI.
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 1: Evidence at protein 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_0000299366"
FT REGION 141..417
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 141..173
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 183..200
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 201..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 278..297
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 298..314
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 315..346
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 347..404
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 159
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17242355,
FT ECO:0007744|PubMed:21183079"
FT MOD_RES 226
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT CONFLICT 77
FT /note="Y -> C (in Ref. 2; AAH98464)"
FT /evidence="ECO:0000305"
FT CONFLICT 297
FT /note="Missing (in Ref. 2; AAH98464)"
FT /evidence="ECO:0000305"
FT CONFLICT 407
FT /note="T -> A (in Ref. 1; BAC38523 and 2; AAH56340/
FT AAH62117)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 417 AA; 46479 MW; 3E23DFFD74B72EF4 CRC64;
MDVERLQEAL KDFEKRGKKE VCPVLDQFLC HVAKTGETMI QWSQFKGYFI FKLEKVMDDF
RTSAPEPRGP PNPNVEYIPF DEMKERILKI VTGFNGIPFT IQRLCELLTD PRRNYTGTDK
FLRGVEKNVM VVSCVCPSSE KNNSNSLNRM NGVMFPGNSP NYTDRSNING PGTPRPLNRP
KLSLSAPLTT NGLPESTDSK DSELQLSEEK GHSDSSASES EVSLLSPVKN KHPDEDAVES
EEHEVKRLKF DKEGDVRETA SQTVSGEVSS VRAEETETAA PPPDKDRESR TRQHCTEEEE
EEEEEEEEEE EESFMTPREM VPERKNQEKE SDDALTVNEE TSEESHQMEG SGVSPAQTDS
TSERSDSAGA SRSGSDCLET QESGGPPSSK TGESVSVPSS MESEEATEVT DDPMEQD
