Full text data of PPP4C
PPP4C
(PPP4, PPX)
[Confidence: low (only semi-automatic identification from reviews)]
Serine/threonine-protein phosphatase 4 catalytic subunit; PP4C; Pp4; 3.1.3.16 (Protein phosphatase X; PP-X)
Note: presumably soluble (membrane word is not in UniProt keywords or features)
Serine/threonine-protein phosphatase 4 catalytic subunit; PP4C; Pp4; 3.1.3.16 (Protein phosphatase X; PP-X)
Note: presumably soluble (membrane word is not in UniProt keywords or features)
UniProt
P60510
ID PP4C_HUMAN Reviewed; 307 AA.
AC P60510; P33172;
DT 01-MAR-2004, integrated into UniProtKB/Swiss-Prot.
read moreDT 01-MAR-2004, sequence version 1.
DT 22-JAN-2014, entry version 104.
DE RecName: Full=Serine/threonine-protein phosphatase 4 catalytic subunit;
DE Short=PP4C;
DE Short=Pp4;
DE EC=3.1.3.16;
DE AltName: Full=Protein phosphatase X;
DE Short=PP-X;
GN Name=PPP4C; Synonyms=PPP4, PPX;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
OC Catarrhini; Hominidae; Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], INTERACTION WITH REL; NFKB1 AND RELA, AND
RP FUNCTION.
RX PubMed=1336397; DOI=10.1016/0167-4781(92)90129-N;
RA Brewis N.D., Cohen P.T.W.;
RT "Protein phosphatase X has been highly conserved during mammalian
RT evolution.";
RL Biochim. Biophys. Acta 1171:231-233(1992).
RN [2]
RP SEQUENCE REVISION TO 75.
RA Cohen P.T.W.;
RL Submitted (DEC-1998) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [MRNA].
RX PubMed=9837938; DOI=10.1074/jbc.273.50.33561;
RA Hu M.C.-T., Tang-Oxley Q., Qiu W.R., Wang Y.-P.,
RA Mihindukulasuriya K.A., Afshar R., Tan T.-H.;
RT "Protein phosphatase X interacts with c-Rel and stimulates c-
RT Rel/nuclear factor kappaB activity.";
RL J. Biol. Chem. 273:33561-33565(1998).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Placenta;
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
RT project: the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [5]
RP FUNCTION.
RX PubMed=11698396; DOI=10.1074/jbc.M107014200;
RA Zhou G., Mihindukulasuriya K.A., MacCorkle-Chosnek R.A.,
RA Van Hooser A., Hu M.C., Brinkley B.R., Tan T.H.;
RT "Protein phosphatase 4 is involved in tumor necrosis factor-alpha-
RT induced activation of c-Jun N-terminal kinase.";
RL J. Biol. Chem. 277:6391-6398(2002).
RN [6]
RP FUNCTION.
RX PubMed=12934076; DOI=10.1038/sj.cdd.4401274;
RA Mourtada-Maarabouni M., Kirkham L., Jenkins B., Rayner J., Gonda T.J.,
RA Starr R., Trayner I., Farzaneh F., Williams G.T.;
RT "Functional expression cloning reveals proapoptotic role for protein
RT phosphatase 4.";
RL Cell Death Differ. 10:1016-1024(2003).
RN [7]
RP FUNCTION, INTERACTION WITH PPP4R2; SMN1 AND GEMIN4, AND COMPOSITION OF
RP THE PPP4C-PPP4R2 COMPLEX.
RX PubMed=12668731; DOI=10.1242/jcs.00409;
RA Carnegie G.K., Sleeman J.E., Morrice N., Hastie C.J., Peggie M.W.,
RA Philp A., Lamond A.I., Cohen P.T.W.;
RT "Protein phosphatase 4 interacts with the survival of motor neurons
RT complex and enhances the temporal localisation of snRNPs.";
RL J. Cell Sci. 116:1905-1913(2003).
RN [8]
RP INTERACTION WITH IRS4.
RX PubMed=15331607; DOI=10.1074/jbc.M408067200;
RA Mihindukulasuriya K.A., Zhou G., Qin J., Tan T.-H.;
RT "Protein phosphatase 4 interacts with and down-regulates insulin
RT receptor substrate 4 following tumor necrosis factor-alpha
RT stimulation.";
RL J. Biol. Chem. 279:46588-46594(2004).
RN [9]
RP INTERACTION WITH HDAC3, AND FUNCTION OF THE PPP4C-PPP4R1 COMPLEX.
RX PubMed=15805470; DOI=10.1101/gad.1286005;
RA Zhang X., Ozawa Y., Lee H., Wen Y.D., Tan T.H., Wadzinski B.E.,
RA Seto E.;
RT "Histone deacetylase 3 (HDAC3) activity is regulated by interaction
RT with protein serine/threonine phosphatase 4.";
RL Genes Dev. 19:827-839(2005).
RN [10]
RP IDENTIFICATION IN THE PPP4C-PPP4R2-PPP4R3A COMPLEX, INTERACTION WITH
RP SMEK1, AND MASS SPECTROMETRY.
RX PubMed=16085932; DOI=10.1074/mcp.M500231-MCP200;
RA Gingras A.-C., Caballero M., Zarske M., Sanchez A., Hazbun T.R.,
RA Fields S., Sonenberg N., Hafen E., Raught B., Aebersold R.;
RT "A novel, evolutionarily conserved protein phosphatase complex
RT involved in cisplatin sensitivity.";
RL Mol. Cell. Proteomics 4:1725-1740(2005).
RN [11]
RP FUNCTION.
RX PubMed=18758438; DOI=10.1038/embor.2008.162;
RA Nakada S., Chen G.I., Gingras A.C., Durocher D.;
RT "PP4 is a gammaH2AX phosphatase required for recovery from the DNA
RT damage checkpoint.";
RL EMBO Rep. 9:1019-1026(2008).
RN [12]
RP FUNCTION.
RX PubMed=18487071; DOI=10.1016/j.biocel.2008.03.021;
RA Martin-Granados C., Philp A., Oxenham S.K., Prescott A.R.,
RA Cohen P.T.W.;
RT "Depletion of protein phosphatase 4 in human cells reveals essential
RT roles in centrosome maturation, cell migration and the regulation of
RT Rho GTPases.";
RL Int. J. Biochem. Cell Biol. 40:2315-2332(2008).
RN [13]
RP INTERACTION WITH PPP4R4, IDENTIFICATION IN THE PPP4C-PPP4R4 COMPLEX,
RP AND MUTAGENESIS OF GLU-39; GLU-64; ASN-76; ARG-107 AND GLU-277.
RX PubMed=18715871; DOI=10.1074/jbc.M803443200;
RA Chen G.I., Tisayakorn S., Jorgensen C., D'Ambrosio L.M.,
RA Goudreault M., Gingras A.-C.;
RT "PP4R4/KIAA1622 forms a novel stable cytosolic complex with
RT phosphoprotein phosphatase 4.";
RL J. Biol. Chem. 283:29273-29284(2008).
RN [14]
RP FUNCTION.
RX PubMed=18347064; DOI=10.1083/jcb.200705148;
RA Toyo-oka K., Mori D., Yano Y., Shiota M., Iwao H., Goto H.,
RA Inagaki M., Hiraiwa N., Muramatsu M., Wynshaw-Boris A., Yoshiki A.,
RA Hirotsune S.;
RT "Protein phosphatase 4 catalytic subunit regulates Cdk1 activity and
RT microtubule organization via NDEL1 dephosphorylation.";
RL J. Cell Biol. 180:1133-1147(2008).
RN [15]
RP IDENTIFICATION IN THE PPP4C-PPP4R1 COMPLEX, IDENTIFICATION IN THE
RP PPP4C-PPP4R2-PPP4R3A COMPLEX, IDENTIFICATION IN THE
RP PPP4C-PPP4R2-PPP4R3B COMPLEX, AND FUNCTION OF THE PPP4C-PPP4R2-PPP4R3A
RP COMPLEX.
RX PubMed=18614045; DOI=10.1016/j.molcel.2008.05.016;
RA Chowdhury D., Xu X., Zhong X., Ahmed F., Zhong J., Liao J.,
RA Dykxhoorn D.M., Weinstock D.M., Pfeifer G.P., Lieberman J.;
RT "A PP4-phosphatase complex dephosphorylates gamma-H2AX generated
RT during DNA replication.";
RL Mol. Cell 31:33-46(2008).
RN [16]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, MASS SPECTROMETRY, AND
RP CLEAVAGE OF INITIATOR METHIONINE.
RX PubMed=19413330; DOI=10.1021/ac9004309;
RA Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J.,
RA Mohammed S.;
RT "Lys-N and trypsin cover complementary parts of the phosphoproteome in
RT a refined SCX-based approach.";
RL Anal. Chem. 81:4493-4501(2009).
RN [17]
RP FUNCTION, AND MUTAGENESIS OF ASP-82.
RX PubMed=20154705; DOI=10.1038/nsmb.1769;
RA Lee D.H., Pan Y., Kanner S., Sung P., Borowiec J.A., Chowdhury D.;
RT "A PP4 phosphatase complex dephosphorylates RPA2 to facilitate DNA
RT repair via homologous recombination.";
RL Nat. Struct. Mol. Biol. 17:365-372(2010).
RN [18]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=21269460; DOI=10.1186/1752-0509-5-17;
RA Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P.,
RA Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.;
RT "Initial characterization of the human central proteome.";
RL BMC Syst. Biol. 5:17-17(2011).
RN [19]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, AND MASS SPECTROMETRY.
RX PubMed=22814378; DOI=10.1073/pnas.1210303109;
RA Van Damme P., Lasa M., Polevoda B., Gazquez C., Elosegui-Artola A.,
RA Kim D.S., De Juan-Pardo E., Demeyer K., Hole K., Larrea E.,
RA Timmerman E., Prieto J., Arnesen T., Sherman F., Gevaert K.,
RA Aldabe R.;
RT "N-terminal acetylome analyses and functional insights of the N-
RT terminal acetyltransferase NatB.";
RL Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012).
CC -!- FUNCTION: Protein phosphatase that is involved in many processes
CC such as microtubule organization at centrosomes, maturation of
CC spliceosomal snRNPs, apoptosis, DNA repair, tumor necrosis factor
CC (TNF)-alpha signaling, activation of c-Jun N-terminal kinase
CC MAPK8, regulation of histone acetylation, DNA damage checkpoint
CC signaling, NF-kappa-B activation and cell migration. The PPP4C-
CC PPP4R1 PP4 complex may play a role in dephosphorylation and
CC regulation of HDAC3. The PPP4C-PPP4R2-PPP4R3A PP4 complex
CC specifically dephosphorylates H2AFX phosphorylated on Ser-140
CC (gamma-H2AFX) generated during DNA replication and required for
CC DNA double strand break repair. Dephosphorylates NDEL1 at CDK1
CC phosphorylation sites and negatively regulates CDK1 activity in
CC interphase (By similarity). In response to DNA damage, catalyzes
CC RPA2 dephosphorylation, an essential step for DNA repair since it
CC allows the efficient RPA2-mediated recruitment of RAD51 to
CC chromatin.
CC -!- CATALYTIC ACTIVITY: A phosphoprotein + H(2)O = a protein +
CC phosphate.
CC -!- COFACTOR: Binds 1 iron ion per subunit (By similarity).
CC -!- COFACTOR: Binds 1 manganese ion per subunit (By similarity).
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-PPP4R1, PPP4C-
CC PPP4R2, PPP4C-PPP4R2-PPP4R3A, PPP4C-PPP4R2-PPP4R3B and PPP4C-
CC PPP4R4. The PPP4C-PPP4R2 complex appears to be a tetramer composed
CC of 2 molecules of PPP4C and 2 molecules of PPP4R2. Interacts with
CC REL, NFKB1/p50 and RELA. Interacts with SMN1 AND GEMIN4. Interacts
CC with IRS4 (phosphorylated). Interacts with SMEK1/PPP4R3A; the
CC interaction requires PP4R2. Interacts with HDAC3.
CC -!- INTERACTION:
CC O15379:HDAC3; NbExp=4; IntAct=EBI-1046072, EBI-607682;
CC P78318:IGBP1; NbExp=7; IntAct=EBI-1046072, EBI-1055954;
CC P30153:PPP2R1A; NbExp=3; IntAct=EBI-1046072, EBI-302388;
CC Q8TF05:PPP4R1; NbExp=5; IntAct=EBI-1046072, EBI-1056262;
CC Q9NY27:PPP4R2; NbExp=8; IntAct=EBI-1046072, EBI-1048740;
CC Q6NUP7:PPP4R4; NbExp=6; IntAct=EBI-1046072, EBI-1774189;
CC O75663:TIPRL; NbExp=3; IntAct=EBI-1046072, EBI-1054735;
CC -!- SUBCELLULAR LOCATION: Cytoplasm. Nucleus. Cytoplasm, cytoskeleton,
CC microtubule organizing center, centrosome.
CC -!- SIMILARITY: Belongs to the PPP phosphatase family. PP-4 (PP-X)
CC subfamily.
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DR EMBL; X70218; CAA49753.1; -; mRNA.
DR EMBL; AF097996; AAC96318.1; -; mRNA.
DR EMBL; BC001416; AAH01416.1; -; mRNA.
DR PIR; S28173; S28173.
DR RefSeq; NP_002711.1; NM_002720.1.
DR RefSeq; XP_005255475.1; XM_005255418.1.
DR UniGene; Hs.534338; -.
DR ProteinModelPortal; P60510; -.
DR SMR; P60510; 6-291.
DR IntAct; P60510; 26.
DR MINT; MINT-5004373; -.
DR STRING; 9606.ENSP00000279387; -.
DR PhosphoSite; P60510; -.
DR DMDM; 44888846; -.
DR PaxDb; P60510; -.
DR PeptideAtlas; P60510; -.
DR PRIDE; P60510; -.
DR DNASU; 5531; -.
DR Ensembl; ENST00000279387; ENSP00000279387; ENSG00000149923.
DR Ensembl; ENST00000561610; ENSP00000455995; ENSG00000149923.
DR GeneID; 5531; -.
DR KEGG; hsa:5531; -.
DR UCSC; uc002dwe.3; human.
DR CTD; 5531; -.
DR GeneCards; GC16P030087; -.
DR HGNC; HGNC:9319; PPP4C.
DR HPA; HPA043837; -.
DR MIM; 602035; gene.
DR neXtProt; NX_P60510; -.
DR PharmGKB; PA33683; -.
DR eggNOG; COG0639; -.
DR HOGENOM; HOG000172696; -.
DR HOVERGEN; HBG000216; -.
DR InParanoid; P60510; -.
DR KO; K15423; -.
DR OMA; VFNHRND; -.
DR OrthoDB; EOG74N5H2; -.
DR PhylomeDB; P60510; -.
DR SignaLink; P60510; -.
DR GeneWiki; PPP4C; -.
DR GenomeRNAi; 5531; -.
DR NextBio; 21426; -.
DR PRO; PR:P60510; -.
DR ArrayExpress; P60510; -.
DR Bgee; P60510; -.
DR CleanEx; HS_PPP4C; -.
DR Genevestigator; P60510; -.
DR GO; GO:0005813; C:centrosome; NAS:UniProtKB.
DR GO; GO:0005737; C:cytoplasm; IDA:HPA.
DR GO; GO:0005634; C:nucleus; NAS:UniProtKB.
DR GO; GO:0005886; C:plasma membrane; IDA:HPA.
DR GO; GO:0030289; C:protein phosphatase 4 complex; IEA:Ensembl.
DR GO; GO:0046872; F:metal ion binding; NAS:UniProtKB.
DR GO; GO:0004704; F:NF-kappaB-inducing kinase activity; NAS:UniProtKB.
DR GO; GO:0004722; F:protein serine/threonine phosphatase activity; IDA:UniProtKB.
DR GO; GO:0000226; P:microtubule cytoskeleton organization; NAS:UniProtKB.
DR GO; GO:0010569; P:regulation of double-strand break repair via homologous recombination; IMP:UniProtKB.
DR InterPro; IPR004843; PEstase_dom.
DR InterPro; IPR006186; Ser/Thr-sp_prot-phosphatase.
DR Pfam; PF00149; Metallophos; 1.
DR PRINTS; PR00114; STPHPHTASE.
DR SMART; SM00156; PP2Ac; 1.
DR PROSITE; PS00125; SER_THR_PHOSPHATASE; 1.
PE 1: Evidence at protein level;
KW Acetylation; Complete proteome; Cytoplasm; Cytoskeleton; Hydrolase;
KW Iron; Manganese; Metal-binding; Methylation; Nucleus;
KW Protein phosphatase; Reference proteome.
FT INIT_MET 1 1 Removed.
FT CHAIN 2 307 Serine/threonine-protein phosphatase 4
FT catalytic subunit.
FT /FTId=PRO_0000058883.
FT ACT_SITE 115 115 Proton donor (By similarity).
FT METAL 54 54 Iron (By similarity).
FT METAL 56 56 Iron (By similarity).
FT METAL 82 82 Iron (By similarity).
FT METAL 82 82 Manganese (By similarity).
FT METAL 114 114 Manganese (By similarity).
FT METAL 164 164 Manganese (By similarity).
FT METAL 238 238 Manganese (By similarity).
FT MOD_RES 2 2 N-acetylalanine.
FT MOD_RES 307 307 Leucine methyl ester (By similarity).
FT MUTAGEN 39 39 E->K: Diminishes interaction with PPP4R4.
FT MUTAGEN 64 64 E->K: Abolishes interaction with PPP4R4.
FT MUTAGEN 76 76 N->D: Diminishes interaction with PPP4R4.
FT MUTAGEN 82 82 D->A: Loss of activity.
FT MUTAGEN 107 107 R->E: Diminishes interaction with PPP4R4.
FT MUTAGEN 277 277 E->K: Abolishes interaction with PPP4R4;
FT no effect on interaction with PPP4R1 and
FT PPP4R2.
SQ SEQUENCE 307 AA; 35080 MW; D6FE470A5C6CBCAC CRC64;
MAEISDLDRQ IEQLRRCELI KESEVKALCA KAREILVEES NVQRVDSPVT VCGDIHGQFY
DLKELFRVGG DVPETNYLFM GDFVDRGFYS VETFLLLLAL KVRYPDRITL IRGNHESRQI
TQVYGFYDEC LRKYGSVTVW RYCTEIFDYL SLSAIIDGKI FCVHGGLSPS IQTLDQIRTI
DRKQEVPHDG PMCDLLWSDP EDTTGWGVSP RGAGYLFGSD VVAQFNAAND IDMICRAHQL
VMEGYKWHFN ETVLTVWSAP NYCYRCGNVA AILELDEHLQ KDFIIFEAAP QETRGIPSKK
PVADYFL
//
ID PP4C_HUMAN Reviewed; 307 AA.
AC P60510; P33172;
DT 01-MAR-2004, integrated into UniProtKB/Swiss-Prot.
read moreDT 01-MAR-2004, sequence version 1.
DT 22-JAN-2014, entry version 104.
DE RecName: Full=Serine/threonine-protein phosphatase 4 catalytic subunit;
DE Short=PP4C;
DE Short=Pp4;
DE EC=3.1.3.16;
DE AltName: Full=Protein phosphatase X;
DE Short=PP-X;
GN Name=PPP4C; Synonyms=PPP4, PPX;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
OC Catarrhini; Hominidae; Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], INTERACTION WITH REL; NFKB1 AND RELA, AND
RP FUNCTION.
RX PubMed=1336397; DOI=10.1016/0167-4781(92)90129-N;
RA Brewis N.D., Cohen P.T.W.;
RT "Protein phosphatase X has been highly conserved during mammalian
RT evolution.";
RL Biochim. Biophys. Acta 1171:231-233(1992).
RN [2]
RP SEQUENCE REVISION TO 75.
RA Cohen P.T.W.;
RL Submitted (DEC-1998) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [MRNA].
RX PubMed=9837938; DOI=10.1074/jbc.273.50.33561;
RA Hu M.C.-T., Tang-Oxley Q., Qiu W.R., Wang Y.-P.,
RA Mihindukulasuriya K.A., Afshar R., Tan T.-H.;
RT "Protein phosphatase X interacts with c-Rel and stimulates c-
RT Rel/nuclear factor kappaB activity.";
RL J. Biol. Chem. 273:33561-33565(1998).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Placenta;
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
RT project: the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [5]
RP FUNCTION.
RX PubMed=11698396; DOI=10.1074/jbc.M107014200;
RA Zhou G., Mihindukulasuriya K.A., MacCorkle-Chosnek R.A.,
RA Van Hooser A., Hu M.C., Brinkley B.R., Tan T.H.;
RT "Protein phosphatase 4 is involved in tumor necrosis factor-alpha-
RT induced activation of c-Jun N-terminal kinase.";
RL J. Biol. Chem. 277:6391-6398(2002).
RN [6]
RP FUNCTION.
RX PubMed=12934076; DOI=10.1038/sj.cdd.4401274;
RA Mourtada-Maarabouni M., Kirkham L., Jenkins B., Rayner J., Gonda T.J.,
RA Starr R., Trayner I., Farzaneh F., Williams G.T.;
RT "Functional expression cloning reveals proapoptotic role for protein
RT phosphatase 4.";
RL Cell Death Differ. 10:1016-1024(2003).
RN [7]
RP FUNCTION, INTERACTION WITH PPP4R2; SMN1 AND GEMIN4, AND COMPOSITION OF
RP THE PPP4C-PPP4R2 COMPLEX.
RX PubMed=12668731; DOI=10.1242/jcs.00409;
RA Carnegie G.K., Sleeman J.E., Morrice N., Hastie C.J., Peggie M.W.,
RA Philp A., Lamond A.I., Cohen P.T.W.;
RT "Protein phosphatase 4 interacts with the survival of motor neurons
RT complex and enhances the temporal localisation of snRNPs.";
RL J. Cell Sci. 116:1905-1913(2003).
RN [8]
RP INTERACTION WITH IRS4.
RX PubMed=15331607; DOI=10.1074/jbc.M408067200;
RA Mihindukulasuriya K.A., Zhou G., Qin J., Tan T.-H.;
RT "Protein phosphatase 4 interacts with and down-regulates insulin
RT receptor substrate 4 following tumor necrosis factor-alpha
RT stimulation.";
RL J. Biol. Chem. 279:46588-46594(2004).
RN [9]
RP INTERACTION WITH HDAC3, AND FUNCTION OF THE PPP4C-PPP4R1 COMPLEX.
RX PubMed=15805470; DOI=10.1101/gad.1286005;
RA Zhang X., Ozawa Y., Lee H., Wen Y.D., Tan T.H., Wadzinski B.E.,
RA Seto E.;
RT "Histone deacetylase 3 (HDAC3) activity is regulated by interaction
RT with protein serine/threonine phosphatase 4.";
RL Genes Dev. 19:827-839(2005).
RN [10]
RP IDENTIFICATION IN THE PPP4C-PPP4R2-PPP4R3A COMPLEX, INTERACTION WITH
RP SMEK1, AND MASS SPECTROMETRY.
RX PubMed=16085932; DOI=10.1074/mcp.M500231-MCP200;
RA Gingras A.-C., Caballero M., Zarske M., Sanchez A., Hazbun T.R.,
RA Fields S., Sonenberg N., Hafen E., Raught B., Aebersold R.;
RT "A novel, evolutionarily conserved protein phosphatase complex
RT involved in cisplatin sensitivity.";
RL Mol. Cell. Proteomics 4:1725-1740(2005).
RN [11]
RP FUNCTION.
RX PubMed=18758438; DOI=10.1038/embor.2008.162;
RA Nakada S., Chen G.I., Gingras A.C., Durocher D.;
RT "PP4 is a gammaH2AX phosphatase required for recovery from the DNA
RT damage checkpoint.";
RL EMBO Rep. 9:1019-1026(2008).
RN [12]
RP FUNCTION.
RX PubMed=18487071; DOI=10.1016/j.biocel.2008.03.021;
RA Martin-Granados C., Philp A., Oxenham S.K., Prescott A.R.,
RA Cohen P.T.W.;
RT "Depletion of protein phosphatase 4 in human cells reveals essential
RT roles in centrosome maturation, cell migration and the regulation of
RT Rho GTPases.";
RL Int. J. Biochem. Cell Biol. 40:2315-2332(2008).
RN [13]
RP INTERACTION WITH PPP4R4, IDENTIFICATION IN THE PPP4C-PPP4R4 COMPLEX,
RP AND MUTAGENESIS OF GLU-39; GLU-64; ASN-76; ARG-107 AND GLU-277.
RX PubMed=18715871; DOI=10.1074/jbc.M803443200;
RA Chen G.I., Tisayakorn S., Jorgensen C., D'Ambrosio L.M.,
RA Goudreault M., Gingras A.-C.;
RT "PP4R4/KIAA1622 forms a novel stable cytosolic complex with
RT phosphoprotein phosphatase 4.";
RL J. Biol. Chem. 283:29273-29284(2008).
RN [14]
RP FUNCTION.
RX PubMed=18347064; DOI=10.1083/jcb.200705148;
RA Toyo-oka K., Mori D., Yano Y., Shiota M., Iwao H., Goto H.,
RA Inagaki M., Hiraiwa N., Muramatsu M., Wynshaw-Boris A., Yoshiki A.,
RA Hirotsune S.;
RT "Protein phosphatase 4 catalytic subunit regulates Cdk1 activity and
RT microtubule organization via NDEL1 dephosphorylation.";
RL J. Cell Biol. 180:1133-1147(2008).
RN [15]
RP IDENTIFICATION IN THE PPP4C-PPP4R1 COMPLEX, IDENTIFICATION IN THE
RP PPP4C-PPP4R2-PPP4R3A COMPLEX, IDENTIFICATION IN THE
RP PPP4C-PPP4R2-PPP4R3B COMPLEX, AND FUNCTION OF THE PPP4C-PPP4R2-PPP4R3A
RP COMPLEX.
RX PubMed=18614045; DOI=10.1016/j.molcel.2008.05.016;
RA Chowdhury D., Xu X., Zhong X., Ahmed F., Zhong J., Liao J.,
RA Dykxhoorn D.M., Weinstock D.M., Pfeifer G.P., Lieberman J.;
RT "A PP4-phosphatase complex dephosphorylates gamma-H2AX generated
RT during DNA replication.";
RL Mol. Cell 31:33-46(2008).
RN [16]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, MASS SPECTROMETRY, AND
RP CLEAVAGE OF INITIATOR METHIONINE.
RX PubMed=19413330; DOI=10.1021/ac9004309;
RA Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J.,
RA Mohammed S.;
RT "Lys-N and trypsin cover complementary parts of the phosphoproteome in
RT a refined SCX-based approach.";
RL Anal. Chem. 81:4493-4501(2009).
RN [17]
RP FUNCTION, AND MUTAGENESIS OF ASP-82.
RX PubMed=20154705; DOI=10.1038/nsmb.1769;
RA Lee D.H., Pan Y., Kanner S., Sung P., Borowiec J.A., Chowdhury D.;
RT "A PP4 phosphatase complex dephosphorylates RPA2 to facilitate DNA
RT repair via homologous recombination.";
RL Nat. Struct. Mol. Biol. 17:365-372(2010).
RN [18]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=21269460; DOI=10.1186/1752-0509-5-17;
RA Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P.,
RA Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.;
RT "Initial characterization of the human central proteome.";
RL BMC Syst. Biol. 5:17-17(2011).
RN [19]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, AND MASS SPECTROMETRY.
RX PubMed=22814378; DOI=10.1073/pnas.1210303109;
RA Van Damme P., Lasa M., Polevoda B., Gazquez C., Elosegui-Artola A.,
RA Kim D.S., De Juan-Pardo E., Demeyer K., Hole K., Larrea E.,
RA Timmerman E., Prieto J., Arnesen T., Sherman F., Gevaert K.,
RA Aldabe R.;
RT "N-terminal acetylome analyses and functional insights of the N-
RT terminal acetyltransferase NatB.";
RL Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012).
CC -!- FUNCTION: Protein phosphatase that is involved in many processes
CC such as microtubule organization at centrosomes, maturation of
CC spliceosomal snRNPs, apoptosis, DNA repair, tumor necrosis factor
CC (TNF)-alpha signaling, activation of c-Jun N-terminal kinase
CC MAPK8, regulation of histone acetylation, DNA damage checkpoint
CC signaling, NF-kappa-B activation and cell migration. The PPP4C-
CC PPP4R1 PP4 complex may play a role in dephosphorylation and
CC regulation of HDAC3. The PPP4C-PPP4R2-PPP4R3A PP4 complex
CC specifically dephosphorylates H2AFX phosphorylated on Ser-140
CC (gamma-H2AFX) generated during DNA replication and required for
CC DNA double strand break repair. Dephosphorylates NDEL1 at CDK1
CC phosphorylation sites and negatively regulates CDK1 activity in
CC interphase (By similarity). In response to DNA damage, catalyzes
CC RPA2 dephosphorylation, an essential step for DNA repair since it
CC allows the efficient RPA2-mediated recruitment of RAD51 to
CC chromatin.
CC -!- CATALYTIC ACTIVITY: A phosphoprotein + H(2)O = a protein +
CC phosphate.
CC -!- COFACTOR: Binds 1 iron ion per subunit (By similarity).
CC -!- COFACTOR: Binds 1 manganese ion per subunit (By similarity).
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-PPP4R1, PPP4C-
CC PPP4R2, PPP4C-PPP4R2-PPP4R3A, PPP4C-PPP4R2-PPP4R3B and PPP4C-
CC PPP4R4. The PPP4C-PPP4R2 complex appears to be a tetramer composed
CC of 2 molecules of PPP4C and 2 molecules of PPP4R2. Interacts with
CC REL, NFKB1/p50 and RELA. Interacts with SMN1 AND GEMIN4. Interacts
CC with IRS4 (phosphorylated). Interacts with SMEK1/PPP4R3A; the
CC interaction requires PP4R2. Interacts with HDAC3.
CC -!- INTERACTION:
CC O15379:HDAC3; NbExp=4; IntAct=EBI-1046072, EBI-607682;
CC P78318:IGBP1; NbExp=7; IntAct=EBI-1046072, EBI-1055954;
CC P30153:PPP2R1A; NbExp=3; IntAct=EBI-1046072, EBI-302388;
CC Q8TF05:PPP4R1; NbExp=5; IntAct=EBI-1046072, EBI-1056262;
CC Q9NY27:PPP4R2; NbExp=8; IntAct=EBI-1046072, EBI-1048740;
CC Q6NUP7:PPP4R4; NbExp=6; IntAct=EBI-1046072, EBI-1774189;
CC O75663:TIPRL; NbExp=3; IntAct=EBI-1046072, EBI-1054735;
CC -!- SUBCELLULAR LOCATION: Cytoplasm. Nucleus. Cytoplasm, cytoskeleton,
CC microtubule organizing center, centrosome.
CC -!- SIMILARITY: Belongs to the PPP phosphatase family. PP-4 (PP-X)
CC subfamily.
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DR EMBL; X70218; CAA49753.1; -; mRNA.
DR EMBL; AF097996; AAC96318.1; -; mRNA.
DR EMBL; BC001416; AAH01416.1; -; mRNA.
DR PIR; S28173; S28173.
DR RefSeq; NP_002711.1; NM_002720.1.
DR RefSeq; XP_005255475.1; XM_005255418.1.
DR UniGene; Hs.534338; -.
DR ProteinModelPortal; P60510; -.
DR SMR; P60510; 6-291.
DR IntAct; P60510; 26.
DR MINT; MINT-5004373; -.
DR STRING; 9606.ENSP00000279387; -.
DR PhosphoSite; P60510; -.
DR DMDM; 44888846; -.
DR PaxDb; P60510; -.
DR PeptideAtlas; P60510; -.
DR PRIDE; P60510; -.
DR DNASU; 5531; -.
DR Ensembl; ENST00000279387; ENSP00000279387; ENSG00000149923.
DR Ensembl; ENST00000561610; ENSP00000455995; ENSG00000149923.
DR GeneID; 5531; -.
DR KEGG; hsa:5531; -.
DR UCSC; uc002dwe.3; human.
DR CTD; 5531; -.
DR GeneCards; GC16P030087; -.
DR HGNC; HGNC:9319; PPP4C.
DR HPA; HPA043837; -.
DR MIM; 602035; gene.
DR neXtProt; NX_P60510; -.
DR PharmGKB; PA33683; -.
DR eggNOG; COG0639; -.
DR HOGENOM; HOG000172696; -.
DR HOVERGEN; HBG000216; -.
DR InParanoid; P60510; -.
DR KO; K15423; -.
DR OMA; VFNHRND; -.
DR OrthoDB; EOG74N5H2; -.
DR PhylomeDB; P60510; -.
DR SignaLink; P60510; -.
DR GeneWiki; PPP4C; -.
DR GenomeRNAi; 5531; -.
DR NextBio; 21426; -.
DR PRO; PR:P60510; -.
DR ArrayExpress; P60510; -.
DR Bgee; P60510; -.
DR CleanEx; HS_PPP4C; -.
DR Genevestigator; P60510; -.
DR GO; GO:0005813; C:centrosome; NAS:UniProtKB.
DR GO; GO:0005737; C:cytoplasm; IDA:HPA.
DR GO; GO:0005634; C:nucleus; NAS:UniProtKB.
DR GO; GO:0005886; C:plasma membrane; IDA:HPA.
DR GO; GO:0030289; C:protein phosphatase 4 complex; IEA:Ensembl.
DR GO; GO:0046872; F:metal ion binding; NAS:UniProtKB.
DR GO; GO:0004704; F:NF-kappaB-inducing kinase activity; NAS:UniProtKB.
DR GO; GO:0004722; F:protein serine/threonine phosphatase activity; IDA:UniProtKB.
DR GO; GO:0000226; P:microtubule cytoskeleton organization; NAS:UniProtKB.
DR GO; GO:0010569; P:regulation of double-strand break repair via homologous recombination; IMP:UniProtKB.
DR InterPro; IPR004843; PEstase_dom.
DR InterPro; IPR006186; Ser/Thr-sp_prot-phosphatase.
DR Pfam; PF00149; Metallophos; 1.
DR PRINTS; PR00114; STPHPHTASE.
DR SMART; SM00156; PP2Ac; 1.
DR PROSITE; PS00125; SER_THR_PHOSPHATASE; 1.
PE 1: Evidence at protein level;
KW Acetylation; Complete proteome; Cytoplasm; Cytoskeleton; Hydrolase;
KW Iron; Manganese; Metal-binding; Methylation; Nucleus;
KW Protein phosphatase; Reference proteome.
FT INIT_MET 1 1 Removed.
FT CHAIN 2 307 Serine/threonine-protein phosphatase 4
FT catalytic subunit.
FT /FTId=PRO_0000058883.
FT ACT_SITE 115 115 Proton donor (By similarity).
FT METAL 54 54 Iron (By similarity).
FT METAL 56 56 Iron (By similarity).
FT METAL 82 82 Iron (By similarity).
FT METAL 82 82 Manganese (By similarity).
FT METAL 114 114 Manganese (By similarity).
FT METAL 164 164 Manganese (By similarity).
FT METAL 238 238 Manganese (By similarity).
FT MOD_RES 2 2 N-acetylalanine.
FT MOD_RES 307 307 Leucine methyl ester (By similarity).
FT MUTAGEN 39 39 E->K: Diminishes interaction with PPP4R4.
FT MUTAGEN 64 64 E->K: Abolishes interaction with PPP4R4.
FT MUTAGEN 76 76 N->D: Diminishes interaction with PPP4R4.
FT MUTAGEN 82 82 D->A: Loss of activity.
FT MUTAGEN 107 107 R->E: Diminishes interaction with PPP4R4.
FT MUTAGEN 277 277 E->K: Abolishes interaction with PPP4R4;
FT no effect on interaction with PPP4R1 and
FT PPP4R2.
SQ SEQUENCE 307 AA; 35080 MW; D6FE470A5C6CBCAC CRC64;
MAEISDLDRQ IEQLRRCELI KESEVKALCA KAREILVEES NVQRVDSPVT VCGDIHGQFY
DLKELFRVGG DVPETNYLFM GDFVDRGFYS VETFLLLLAL KVRYPDRITL IRGNHESRQI
TQVYGFYDEC LRKYGSVTVW RYCTEIFDYL SLSAIIDGKI FCVHGGLSPS IQTLDQIRTI
DRKQEVPHDG PMCDLLWSDP EDTTGWGVSP RGAGYLFGSD VVAQFNAAND IDMICRAHQL
VMEGYKWHFN ETVLTVWSAP NYCYRCGNVA AILELDEHLQ KDFIIFEAAP QETRGIPSKK
PVADYFL
//
MIM
602035
*RECORD*
*FIELD* NO
602035
*FIELD* TI
*602035 PROTEIN PHOSPHATASE 4, CATALYTIC SUBUNIT; PPP4C
;;SERINE/THREONINE PROTEIN PHOSPHATASE 4; PP4;;
read morePROTEIN PHOSPHATASE X; PPX
*FIELD* TX
CLONING
Protein phosphatases are involved in determining the phosphorylation
state of many regulatory proteins. Other members of this family include
PP1 (see 176875), PP2A (see 176915), and PP5 (see 600658). Brewis and
Cohen (1992) cloned a cDNA that they termed PPX from a human
teratocarcinoma library. The sequence predicted a protein of 307 amino
acids with a mass of 35 kD. Brewis and Cohen (1992) found that PPX
shares 66% identity with the human PP2 isoforms PP2A-alpha and PP2A-beta
(176916).
GENE FUNCTION
Hastie et al. (2000) identified Ppp4r2 (613822) and Ppp4c as the sole
components of a 450-kD PPP4 complex purified from rabbit skeletal muscle
and pig testis. Ppp4r2 and Ppp4c were also present in a 600-kD PPP4
complex that could be converted to a 450-kD species. Protein pull-down
and coimmunoprecipitation analyses showed that recombinant human PPP4R2
interacted specifically with purified pig Ppp4c and not with related
protein phosphatases. Gel filtration and sediment analyses suggested
that recombinant human PPP4R2 formed dimers. Ppp4r2 and Ppp4c were
present in a 1:1 ratio in the purified rabbit and pig PPP4 complexes,
suggesting that the PPP4 complex is a tetramer comprised of 2 PPP4R2
molecules and 2 PPP4C molecules. The 450-kD and 600-kD PPP4 complexes
showed very little phosphatase activity, but they could be activated by
exposure to a basic protein, such as protamine (PRM1; 182880).
Zhang et al. (2005) found that in HeLa cells HDAC3 (605166) was
activated by the phosphorylation of ser424 by casein kinase II (see
CSNK2A1; 115440) and was deactivated by dephosphorylation of ser424 by
protein phosphatase-4. HDAC3 copurified with PPP4C and its regulatory
subunit, PPP4R1 (604908), in an HDAC3 complex that showed phosphatase
activity. Both PP4 proteins interacted directly with HDAC3, and mutation
analysis indicated that the N terminus of HDAC3 was necessary and
sufficient for HDAC3-PPP4C interaction. Both overexpression and RNA
interference experiments indicated that HDAC3 activity was inversely
proportional to the cellular abundance of PPP4C.
Using protein pull-down assays, Gingras et al. (2005) showed that
PP4R3-alpha (SMEK1; 610351), PPP4C, and PPP4R2 interacted in a complex.
Lee et al. (2010) stated that PPP4C, PPP4R2, and PPP4R3-beta (SMEK2;
610352) form a heterotrimeric complex involved in DNA double-strand
break repair. They found that a dimeric PPP4 complex containing PPP4C
and PPP4R2 dephosphorylated replication protein A2 (RPA2; 179836),
regulating its role in the DNA double-stranded break response. PPP4C
efficiently dephosphorylated phospho-RPA2 in vitro. Silencing PPP4R2 in
human cell lines, or introduction of a PPP4R2 mutant unable to interact
with PPP4C, altered the kinetics and pattern of RPA2 phosphorylation.
Depletion of PPP4R2 impeded homologous recombination via inefficient
loading of the essential factor RAD51 (179617), causing an extended G2-M
checkpoint and hypersensitivity to DNA damage. Cells expressing
phosphomimetic RPA2 mutants had a comparable phenotype, suggesting that
PPP4-mediated dephosphorylation of RPA2 is necessary for efficient DNA
damage response.
MAPPING
Bastians et al. (1997) used fluorescence in situ hybridization to map
the PPP4C gene to chromosome 16p12-p11. They noted that several
translocations associated with acute leukemias have been mapped to this
region of chromosome 16p.
*FIELD* RF
1. Bastians, H.; Krebber, H.; Hoheisel, J.; Ohl, S.; Lichter, P.;
Ponstingl, H.; Joos, S.: Assignment of the human serine/threonine
protein phosphatase 4 gene (PPP4C) to chromosome 16p11-p12 by fluorescence
in situ hybridization. Genomics 42: 181-182, 1997.
2. Brewis, N. D.; Cohen, P. T. W.: Protein phosphatase X has been
highly conserved during mammalian evolution. Biochim. Biophys. Acta 1171:
231-233, 1992.
3. Gingras, A.-C.; Caballero, M.; Zarske, M.; Sanchez, A.; Hazbun,
T. R.; Fields, S.; Sonenberg, N.; Hafen, E.; Raught, B.; Aebersold,
R.: A novel, evolutionarily conserved protein phosphatase complex
involved in cisplatin sensitivity. Molec. Cell. Proteomics 4: 1725-1740,
2005.
4. Hastie, C. J.; Carnegie, G. K.; Morrice, N.; Cohen, P. T. W.:
A novel 50 kDa protein forms complexes with protein phosphatase 4
and is located at centrosomal microtubule organizing centres. Biochem.
J. 347: 845-855, 2000.
5. Lee, D.-H.; Pan, Y.; Kanner, S.; Sung, P.; Borowiec, J. A.; Chowdhury,
D.: A PP4 phosphatase complex dephosphorylates RPA2 to facilitate
DNA repair via homologous recombination. Nature Struct. Molec. Biol. 17:
365-372, 2010.
6. Zhang, X.; Ozawa, Y.; Lee, H.; Wen, Y.-D.; Tan, T.-H.; Wadzinski,
B. E.; Seto, E.: Histone deacetylase 3 (HDAC3) activity is regulated
by interaction with protein serine/threonine phosphatase 4. Genes
Dev. 19: 827-839, 2005.
*FIELD* CN
Patricia A. Hartz - updated: 03/21/2011
Patricia A. Hartz - updated: 11/9/2005
*FIELD* CD
Jennifer P. Macke: 10/8/1997
*FIELD* ED
mgross: 03/21/2011
wwang: 11/29/2005
terry: 11/9/2005
alopez: 10/10/1997
alopez: 10/8/1997
*RECORD*
*FIELD* NO
602035
*FIELD* TI
*602035 PROTEIN PHOSPHATASE 4, CATALYTIC SUBUNIT; PPP4C
;;SERINE/THREONINE PROTEIN PHOSPHATASE 4; PP4;;
read morePROTEIN PHOSPHATASE X; PPX
*FIELD* TX
CLONING
Protein phosphatases are involved in determining the phosphorylation
state of many regulatory proteins. Other members of this family include
PP1 (see 176875), PP2A (see 176915), and PP5 (see 600658). Brewis and
Cohen (1992) cloned a cDNA that they termed PPX from a human
teratocarcinoma library. The sequence predicted a protein of 307 amino
acids with a mass of 35 kD. Brewis and Cohen (1992) found that PPX
shares 66% identity with the human PP2 isoforms PP2A-alpha and PP2A-beta
(176916).
GENE FUNCTION
Hastie et al. (2000) identified Ppp4r2 (613822) and Ppp4c as the sole
components of a 450-kD PPP4 complex purified from rabbit skeletal muscle
and pig testis. Ppp4r2 and Ppp4c were also present in a 600-kD PPP4
complex that could be converted to a 450-kD species. Protein pull-down
and coimmunoprecipitation analyses showed that recombinant human PPP4R2
interacted specifically with purified pig Ppp4c and not with related
protein phosphatases. Gel filtration and sediment analyses suggested
that recombinant human PPP4R2 formed dimers. Ppp4r2 and Ppp4c were
present in a 1:1 ratio in the purified rabbit and pig PPP4 complexes,
suggesting that the PPP4 complex is a tetramer comprised of 2 PPP4R2
molecules and 2 PPP4C molecules. The 450-kD and 600-kD PPP4 complexes
showed very little phosphatase activity, but they could be activated by
exposure to a basic protein, such as protamine (PRM1; 182880).
Zhang et al. (2005) found that in HeLa cells HDAC3 (605166) was
activated by the phosphorylation of ser424 by casein kinase II (see
CSNK2A1; 115440) and was deactivated by dephosphorylation of ser424 by
protein phosphatase-4. HDAC3 copurified with PPP4C and its regulatory
subunit, PPP4R1 (604908), in an HDAC3 complex that showed phosphatase
activity. Both PP4 proteins interacted directly with HDAC3, and mutation
analysis indicated that the N terminus of HDAC3 was necessary and
sufficient for HDAC3-PPP4C interaction. Both overexpression and RNA
interference experiments indicated that HDAC3 activity was inversely
proportional to the cellular abundance of PPP4C.
Using protein pull-down assays, Gingras et al. (2005) showed that
PP4R3-alpha (SMEK1; 610351), PPP4C, and PPP4R2 interacted in a complex.
Lee et al. (2010) stated that PPP4C, PPP4R2, and PPP4R3-beta (SMEK2;
610352) form a heterotrimeric complex involved in DNA double-strand
break repair. They found that a dimeric PPP4 complex containing PPP4C
and PPP4R2 dephosphorylated replication protein A2 (RPA2; 179836),
regulating its role in the DNA double-stranded break response. PPP4C
efficiently dephosphorylated phospho-RPA2 in vitro. Silencing PPP4R2 in
human cell lines, or introduction of a PPP4R2 mutant unable to interact
with PPP4C, altered the kinetics and pattern of RPA2 phosphorylation.
Depletion of PPP4R2 impeded homologous recombination via inefficient
loading of the essential factor RAD51 (179617), causing an extended G2-M
checkpoint and hypersensitivity to DNA damage. Cells expressing
phosphomimetic RPA2 mutants had a comparable phenotype, suggesting that
PPP4-mediated dephosphorylation of RPA2 is necessary for efficient DNA
damage response.
MAPPING
Bastians et al. (1997) used fluorescence in situ hybridization to map
the PPP4C gene to chromosome 16p12-p11. They noted that several
translocations associated with acute leukemias have been mapped to this
region of chromosome 16p.
*FIELD* RF
1. Bastians, H.; Krebber, H.; Hoheisel, J.; Ohl, S.; Lichter, P.;
Ponstingl, H.; Joos, S.: Assignment of the human serine/threonine
protein phosphatase 4 gene (PPP4C) to chromosome 16p11-p12 by fluorescence
in situ hybridization. Genomics 42: 181-182, 1997.
2. Brewis, N. D.; Cohen, P. T. W.: Protein phosphatase X has been
highly conserved during mammalian evolution. Biochim. Biophys. Acta 1171:
231-233, 1992.
3. Gingras, A.-C.; Caballero, M.; Zarske, M.; Sanchez, A.; Hazbun,
T. R.; Fields, S.; Sonenberg, N.; Hafen, E.; Raught, B.; Aebersold,
R.: A novel, evolutionarily conserved protein phosphatase complex
involved in cisplatin sensitivity. Molec. Cell. Proteomics 4: 1725-1740,
2005.
4. Hastie, C. J.; Carnegie, G. K.; Morrice, N.; Cohen, P. T. W.:
A novel 50 kDa protein forms complexes with protein phosphatase 4
and is located at centrosomal microtubule organizing centres. Biochem.
J. 347: 845-855, 2000.
5. Lee, D.-H.; Pan, Y.; Kanner, S.; Sung, P.; Borowiec, J. A.; Chowdhury,
D.: A PP4 phosphatase complex dephosphorylates RPA2 to facilitate
DNA repair via homologous recombination. Nature Struct. Molec. Biol. 17:
365-372, 2010.
6. Zhang, X.; Ozawa, Y.; Lee, H.; Wen, Y.-D.; Tan, T.-H.; Wadzinski,
B. E.; Seto, E.: Histone deacetylase 3 (HDAC3) activity is regulated
by interaction with protein serine/threonine phosphatase 4. Genes
Dev. 19: 827-839, 2005.
*FIELD* CN
Patricia A. Hartz - updated: 03/21/2011
Patricia A. Hartz - updated: 11/9/2005
*FIELD* CD
Jennifer P. Macke: 10/8/1997
*FIELD* ED
mgross: 03/21/2011
wwang: 11/29/2005
terry: 11/9/2005
alopez: 10/10/1997
alopez: 10/8/1997