PP4C_HUMAN
ID PP4C_HUMAN Reviewed; 307 AA.
AC P60510; P33172;
DT 01-MAR-2004, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2004, sequence version 1.
DT 03-AUG-2022, entry version 169.
DE RecName: Full=Serine/threonine-protein phosphatase 4 catalytic subunit;
DE Short=PP4C;
DE Short=Pp4;
DE EC=3.1.3.16 {ECO:0000269|PubMed:18347064, ECO:0000269|PubMed:18614045, ECO:0000269|PubMed:18758438, ECO:0000269|PubMed:20154705};
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; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC 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., Mihindukulasuriya K.A.,
RA Afshar R., Tan T.-H.;
RT "Protein phosphatase X interacts with c-Rel and stimulates c-Rel/nuclear
RT 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 project:
RT 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., Van Hooser A.,
RA Hu M.C., Brinkley B.R., Tan T.H.;
RT "Protein phosphatase 4 is involved in tumor necrosis factor-alpha-induced
RT 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 THE
RP 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 complex
RT 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 receptor
RT substrate 4 following tumor necrosis factor-alpha 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., Seto E.;
RT "Histone deacetylase 3 (HDAC3) activity is regulated by interaction with
RT protein serine/threonine phosphatase 4.";
RL Genes Dev. 19:827-839(2005).
RN [10]
RP IDENTIFICATION IN THE PPP4C-PPP4R2-PPP4R3A COMPLEX, INTERACTION WITH SMEK1,
RP AND IDENTIFICATION BY MASS SPECTROMETRY.
RX PubMed=16085932; DOI=10.1074/mcp.m500231-mcp200;
RA Gingras A.-C., Caballero M., Zarske M., Sanchez A., Hazbun T.R., Fields S.,
RA Sonenberg N., Hafen E., Raught B., Aebersold R.;
RT "A novel, evolutionarily conserved protein phosphatase complex involved in
RT cisplatin sensitivity.";
RL Mol. Cell. Proteomics 4:1725-1740(2005).
RN [11]
RP FUNCTION, AND CATALYTIC ACTIVITY.
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 damage
RT 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., Cohen P.T.W.;
RT "Depletion of protein phosphatase 4 in human cells reveals essential roles
RT in centrosome maturation, cell migration and the regulation of Rho
RT GTPases.";
RL Int. J. Biochem. Cell Biol. 40:2315-2332(2008).
RN [13]
RP INTERACTION WITH PPP4R4, IDENTIFICATION IN THE PPP4C-PPP4R4 COMPLEX, AND
RP 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., Goudreault M.,
RA Gingras A.-C.;
RT "PP4R4/KIAA1622 forms a novel stable cytosolic complex with phosphoprotein
RT phosphatase 4.";
RL J. Biol. Chem. 283:29273-29284(2008).
RN [14]
RP FUNCTION, AND CATALYTIC ACTIVITY.
RX PubMed=18347064; DOI=10.1083/jcb.200705148;
RA Toyo-oka K., Mori D., Yano Y., Shiota M., Iwao H., Goto H., Inagaki M.,
RA Hiraiwa N., Muramatsu M., Wynshaw-Boris A., Yoshiki A., 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 FUNCTION OF THE PPP4C-PPP4R2-PPP4R3A COMPLEX, CATALYTIC ACTIVITY,
RP IDENTIFICATION IN THE PPP4C-PPP4R1 COMPLEX, IDENTIFICATION IN THE
RP PPP4C-PPP4R2-PPP4R3A COMPLEX, AND IDENTIFICATION IN THE
RP PPP4C-PPP4R2-PPP4R3B 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., Dykxhoorn D.M.,
RA Weinstock D.M., Pfeifer G.P., Lieberman J.;
RT "A PP4-phosphatase complex dephosphorylates gamma-H2AX generated during DNA
RT replication.";
RL Mol. Cell 31:33-46(2008).
RN [16]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, CLEAVAGE OF INITIATOR
RP METHIONINE [LARGE SCALE ANALYSIS], AND IDENTIFICATION BY MASS SPECTROMETRY
RP [LARGE SCALE ANALYSIS].
RX PubMed=19413330; DOI=10.1021/ac9004309;
RA Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J., Mohammed S.;
RT "Lys-N and trypsin cover complementary parts of the phosphoproteome in a
RT refined SCX-based approach.";
RL Anal. Chem. 81:4493-4501(2009).
RN [17]
RP FUNCTION, CATALYTIC ACTIVITY, 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 repair
RT 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., Buerckstuemmer T.,
RA 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, CLEAVAGE OF INITIATOR
RP METHIONINE [LARGE SCALE ANALYSIS], AND IDENTIFICATION BY MASS SPECTROMETRY
RP [LARGE SCALE ANALYSIS].
RX PubMed=22223895; DOI=10.1074/mcp.m111.015131;
RA Bienvenut W.V., Sumpton D., Martinez A., Lilla S., Espagne C., Meinnel T.,
RA Giglione C.;
RT "Comparative large-scale characterisation of plant vs. mammal proteins
RT reveals similar and idiosyncratic N-alpha acetylation features.";
RL Mol. Cell. Proteomics 11:M111.015131-M111.015131(2012).
RN [20]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, CLEAVAGE OF INITIATOR
RP METHIONINE [LARGE SCALE ANALYSIS], AND IDENTIFICATION BY MASS SPECTROMETRY
RP [LARGE SCALE ANALYSIS].
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., Timmerman E.,
RA Prieto J., Arnesen T., Sherman F., Gevaert K., Aldabe R.;
RT "N-terminal acetylome analyses and functional insights of the N-terminal
RT acetyltransferase NatB.";
RL Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012).
RN [21]
RP METHYLATION AT LEU-307, AND MUTAGENESIS OF LEU-307.
RX PubMed=25130464; DOI=10.1016/j.bbrc.2014.08.045;
RA Lee J., Lee D.H.;
RT "Leucine methylation of protein phosphatase PP4C at C-terminal is critical
RT for its cellular functions.";
RL Biochem. Biophys. Res. Commun. 452:42-47(2014).
CC -!- FUNCTION: Protein phosphatase that is involved in many processes such
CC as microtubule organization at centrosomes, maturation of spliceosomal
CC snRNPs, apoptosis, DNA repair, tumor necrosis factor (TNF)-alpha
CC signaling, activation of c-Jun N-terminal kinase MAPK8, regulation of
CC histone acetylation, DNA damage checkpoint signaling, NF-kappa-B
CC activation and cell migration. The PPP4C-PPP4R1 PP4 complex may play a
CC role in dephosphorylation and regulation of HDAC3. The PPP4C-PPP4R2-
CC PPP4R3A PP4 complex specifically dephosphorylates H2AX phosphorylated
CC on Ser-140 (gamma-H2AX) generated during DNA replication and required
CC for 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 RPA2
CC dephosphorylation, an essential step for DNA repair since it allows the
CC efficient RPA2-mediated recruitment of RAD51 to chromatin.
CC {ECO:0000250, ECO:0000269|PubMed:11698396, ECO:0000269|PubMed:12668731,
CC ECO:0000269|PubMed:12934076, ECO:0000269|PubMed:1336397,
CC ECO:0000269|PubMed:15805470, ECO:0000269|PubMed:18347064,
CC ECO:0000269|PubMed:18487071, ECO:0000269|PubMed:18614045,
CC ECO:0000269|PubMed:18758438, ECO:0000269|PubMed:20154705}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=H2O + O-phospho-L-seryl-[protein] = L-seryl-[protein] +
CC phosphate; Xref=Rhea:RHEA:20629, Rhea:RHEA-COMP:9863, Rhea:RHEA-
CC COMP:11604, ChEBI:CHEBI:15377, ChEBI:CHEBI:29999, ChEBI:CHEBI:43474,
CC ChEBI:CHEBI:83421; EC=3.1.3.16;
CC Evidence={ECO:0000269|PubMed:18347064, ECO:0000269|PubMed:18614045,
CC ECO:0000269|PubMed:18758438, ECO:0000269|PubMed:20154705};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=H2O + O-phospho-L-threonyl-[protein] = L-threonyl-[protein] +
CC phosphate; Xref=Rhea:RHEA:47004, Rhea:RHEA-COMP:11060, Rhea:RHEA-
CC COMP:11605, ChEBI:CHEBI:15377, ChEBI:CHEBI:30013, ChEBI:CHEBI:43474,
CC ChEBI:CHEBI:61977; EC=3.1.3.16;
CC Evidence={ECO:0000269|PubMed:18347064, ECO:0000269|PubMed:18614045,
CC ECO:0000269|PubMed:18758438, ECO:0000269|PubMed:20154705};
CC -!- COFACTOR:
CC Name=Mn(2+); Xref=ChEBI:CHEBI:29035;
CC Evidence={ECO:0000250|UniProtKB:P67775};
CC Note=Binds 2 manganese ions per subunit.
CC {ECO:0000250|UniProtKB:P67775};
CC -!- SUBUNIT: Serine/threonine-protein phosphatase 4 (PP4) occurs in
CC different assemblies of the catalytic and one or more regulatory
CC subunits (PubMed:12668731, PubMed:18715871, PubMed:16085932,
CC PubMed:18614045). Component of the PP4 complexes PPP4C-PPP4R1, PPP4C-
CC PPP4R2, PPP4C-PPP4R2-PPP4R3A, PPP4C-PPP4R2-PPP4R3B and PPP4C-PPP4R4
CC (PubMed:12668731, PubMed:18715871, PubMed:16085932, PubMed:18614045).
CC The PPP4C-PPP4R2 complex appears to be a tetramer composed of 2
CC molecules of PPP4C and 2 molecules of PPP4R2 (PubMed:12668731).
CC Interacts with REL, NFKB1/p50 and RELA (PubMed:1336397). Interacts with
CC SMN1 and GEMIN4 (PubMed:12668731). Interacts with IRS4 (phosphorylated)
CC (PubMed:15331607). Interacts with SMEK1/PPP4R3A; the interaction
CC requires PP4R2 (PubMed:16085932). Interacts with HDAC3
CC (PubMed:15805470). {ECO:0000269|PubMed:12668731,
CC ECO:0000269|PubMed:1336397, ECO:0000269|PubMed:15331607,
CC ECO:0000269|PubMed:15805470, ECO:0000269|PubMed:16085932,
CC ECO:0000269|PubMed:18614045, ECO:0000269|PubMed:18715871}.
CC -!- INTERACTION:
CC P60510; O95872: GPANK1; NbExp=3; IntAct=EBI-1046072, EBI-751540;
CC P60510; O15379: HDAC3; NbExp=2; IntAct=EBI-1046072, EBI-607682;
CC P60510; P78318: IGBP1; NbExp=15; IntAct=EBI-1046072, EBI-1055954;
CC P60510; P30153: PPP2R1A; NbExp=6; IntAct=EBI-1046072, EBI-302388;
CC P60510; Q8TF05: PPP4R1; NbExp=8; IntAct=EBI-1046072, EBI-1056262;
CC P60510; Q9NY27: PPP4R2; NbExp=14; IntAct=EBI-1046072, EBI-1048740;
CC P60510; Q6NUP7: PPP4R4; NbExp=8; IntAct=EBI-1046072, EBI-1774189;
CC P60510; O75663: TIPRL; NbExp=5; IntAct=EBI-1046072, EBI-1054735;
CC -!- SUBCELLULAR LOCATION: Cytoplasm. Nucleus. Cytoplasm, cytoskeleton,
CC microtubule organizing center, centrosome.
CC -!- PTM: Methylation at the C-terminal Leu-307 is critical for interactions
CC with regulatory subunits and functions in DNA repair.
CC {ECO:0000269|PubMed:25130464}.
CC -!- SIMILARITY: Belongs to the PPP phosphatase family. PP-4 (PP-X)
CC subfamily. {ECO:0000305}.
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DR EMBL; X70218; CAA49753.1; -; mRNA.
DR EMBL; AF097996; AAC96318.1; -; mRNA.
DR EMBL; BC001416; AAH01416.1; -; mRNA.
DR CCDS; CCDS10669.1; -.
DR PIR; S28173; S28173.
DR RefSeq; NP_001290432.1; NM_001303503.1.
DR RefSeq; NP_001290433.1; NM_001303504.1.
DR RefSeq; NP_001290435.1; NM_001303506.1.
DR RefSeq; NP_001290436.1; NM_001303507.1.
DR RefSeq; NP_002711.1; NM_002720.2.
DR AlphaFoldDB; P60510; -.
DR SMR; P60510; -.
DR BioGRID; 111523; 107.
DR ComplexPortal; CPX-156; PPP4C-PPP4R2 protein phosphatase 4 complex.
DR ComplexPortal; CPX-1842; PPP4C-PPP4R1 protein phosphatase 4 complex.
DR ComplexPortal; CPX-1843; PPP4C-PPP4R2-PPP4R3A protein phosphatase 4 complex.
DR ComplexPortal; CPX-1844; PPP4C-PPP4R2-PPP4R3B protein phosphatase 4 complex.
DR ComplexPortal; CPX-1845; PPP4C-PPP4R4 protein phosphatase 4 complex.
DR CORUM; P60510; -.
DR IntAct; P60510; 50.
DR MINT; P60510; -.
DR STRING; 9606.ENSP00000279387; -.
DR DEPOD; PPP4C; -.
DR iPTMnet; P60510; -.
DR MetOSite; P60510; -.
DR PhosphoSitePlus; P60510; -.
DR BioMuta; PPP4C; -.
DR DMDM; 44888846; -.
DR EPD; P60510; -.
DR jPOST; P60510; -.
DR MassIVE; P60510; -.
DR MaxQB; P60510; -.
DR PaxDb; P60510; -.
DR PeptideAtlas; P60510; -.
DR PRIDE; P60510; -.
DR ProteomicsDB; 57213; -.
DR Antibodypedia; 26991; 440 antibodies from 40 providers.
DR DNASU; 5531; -.
DR Ensembl; ENST00000279387.12; ENSP00000279387.7; ENSG00000149923.14.
DR Ensembl; ENST00000561610.1; ENSP00000455995.1; ENSG00000149923.14.
DR GeneID; 5531; -.
DR KEGG; hsa:5531; -.
DR MANE-Select; ENST00000279387.12; ENSP00000279387.7; NM_002720.3; NP_002711.1.
DR UCSC; uc002dwf.4; human.
DR CTD; 5531; -.
DR DisGeNET; 5531; -.
DR GeneCards; PPP4C; -.
DR HGNC; HGNC:9319; PPP4C.
DR HPA; ENSG00000149923; Low tissue specificity.
DR MIM; 602035; gene.
DR neXtProt; NX_P60510; -.
DR OpenTargets; ENSG00000149923; -.
DR PharmGKB; PA33683; -.
DR VEuPathDB; HostDB:ENSG00000149923; -.
DR eggNOG; KOG0372; Eukaryota.
DR GeneTree; ENSGT00930000151040; -.
DR HOGENOM; CLU_004962_8_1_1; -.
DR InParanoid; P60510; -.
DR OMA; HGQFWDM; -.
DR OrthoDB; 808922at2759; -.
DR PhylomeDB; P60510; -.
DR TreeFam; TF105559; -.
DR PathwayCommons; P60510; -.
DR Reactome; R-HSA-5693607; Processing of DNA double-strand break ends.
DR SignaLink; P60510; -.
DR SIGNOR; P60510; -.
DR BioGRID-ORCS; 5531; 750 hits in 1098 CRISPR screens.
DR ChiTaRS; PPP4C; human.
DR GeneWiki; PPP4C; -.
DR GenomeRNAi; 5531; -.
DR Pharos; P60510; Tbio.
DR PRO; PR:P60510; -.
DR Proteomes; UP000005640; Chromosome 16.
DR RNAct; P60510; protein.
DR Bgee; ENSG00000149923; Expressed in lower esophagus mucosa and 200 other tissues.
DR ExpressionAtlas; P60510; baseline and differential.
DR Genevisible; P60510; HS.
DR GO; GO:0000785; C:chromatin; IDA:ComplexPortal.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0005829; C:cytosol; IDA:HPA.
DR GO; GO:0005815; C:microtubule organizing center; IEA:UniProtKB-SubCell.
DR GO; GO:0005654; C:nucleoplasm; IDA:HPA.
DR GO; GO:0005634; C:nucleus; IBA:GO_Central.
DR GO; GO:0005886; C:plasma membrane; IDA:HPA.
DR GO; GO:0030289; C:protein phosphatase 4 complex; IPI:ComplexPortal.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0017018; F:myosin phosphatase activity; IEA:UniProtKB-EC.
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:0000724; P:double-strand break repair via homologous recombination; IBA:GO_Central.
DR GO; GO:0033128; P:negative regulation of histone phosphorylation; IMP:ComplexPortal.
DR GO; GO:0006470; P:protein dephosphorylation; IEA:UniProt.
DR GO; GO:2000779; P:regulation of double-strand break repair; IMP:ComplexPortal.
DR GO; GO:0010569; P:regulation of double-strand break repair via homologous recombination; IMP:UniProtKB.
DR Gene3D; 3.60.21.10; -; 1.
DR InterPro; IPR004843; Calcineurin-like_PHP_ApaH.
DR InterPro; IPR029052; Metallo-depent_PP-like.
DR InterPro; IPR006186; Ser/Thr-sp_prot-phosphatase.
DR Pfam; PF00149; Metallophos; 1.
DR PRINTS; PR00114; STPHPHTASE.
DR SMART; SM00156; PP2Ac; 1.
DR SUPFAM; SSF56300; SSF56300; 1.
DR PROSITE; PS00125; SER_THR_PHOSPHATASE; 1.
PE 1: Evidence at protein level;
KW Acetylation; Cytoplasm; Cytoskeleton; Hydrolase; Manganese; Metal-binding;
KW Methylation; Nucleus; Protein phosphatase; Reference proteome.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0007744|PubMed:19413330,
FT ECO:0007744|PubMed:22223895, ECO:0007744|PubMed:22814378"
FT CHAIN 2..307
FT /note="Serine/threonine-protein phosphatase 4 catalytic
FT subunit"
FT /id="PRO_0000058883"
FT ACT_SITE 115
FT /note="Proton donor"
FT /evidence="ECO:0000250|UniProtKB:P36873"
FT BINDING 54
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:P67775"
FT BINDING 56
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:P67775"
FT BINDING 82
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:P67775"
FT BINDING 82
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:P67775"
FT BINDING 114
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:P67775"
FT BINDING 164
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:P67775"
FT BINDING 238
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:P67775"
FT MOD_RES 2
FT /note="N-acetylalanine"
FT /evidence="ECO:0007744|PubMed:19413330,
FT ECO:0007744|PubMed:22223895, ECO:0007744|PubMed:22814378"
FT MOD_RES 307
FT /note="Leucine methyl ester"
FT /evidence="ECO:0000269|PubMed:25130464"
FT MUTAGEN 39
FT /note="E->K: Diminishes interaction with PPP4R4."
FT /evidence="ECO:0000269|PubMed:18715871"
FT MUTAGEN 64
FT /note="E->K: Abolishes interaction with PPP4R4."
FT /evidence="ECO:0000269|PubMed:18715871"
FT MUTAGEN 76
FT /note="N->D: Diminishes interaction with PPP4R4."
FT /evidence="ECO:0000269|PubMed:18715871"
FT MUTAGEN 82
FT /note="D->A: Loss of activity."
FT /evidence="ECO:0000269|PubMed:20154705"
FT MUTAGEN 107
FT /note="R->E: Diminishes interaction with PPP4R4."
FT /evidence="ECO:0000269|PubMed:18715871"
FT MUTAGEN 277
FT /note="E->K: Abolishes interaction with PPP4R4; no effect
FT on interaction with PPP4R1 and PPP4R2."
FT /evidence="ECO:0000269|PubMed:18715871"
FT MUTAGEN 307
FT /note="L->A: Unable to dephosphorylate 53BP1 and KAR1, loss
FT of DSB repair activity."
FT /evidence="ECO:0000269|PubMed:25130464"
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
