PPM1K_HUMAN
ID PPM1K_HUMAN Reviewed; 372 AA.
AC Q8N3J5; B2RAZ1; Q05CT5; Q49AB5; Q4W5E6; Q56AN8; Q8IUZ7; Q8IXG7; Q8ND70;
AC Q96NT4;
DT 20-FEB-2007, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2002, sequence version 1.
DT 03-AUG-2022, entry version 157.
DE RecName: Full=Protein phosphatase 1K, mitochondrial;
DE EC=3.1.3.16;
DE AltName: Full=PP2C domain-containing protein phosphatase 1K;
DE AltName: Full=PP2C-like mitochondrial protein;
DE AltName: Full=PP2C-type mitochondrial phosphoprotein phosphatase;
DE Short=PTMP;
DE AltName: Full=Protein phosphatase 2C isoform kappa;
DE Short=PP2C-kappa;
DE Flags: Precursor;
GN Name=PPM1K; Synonyms=PP2CM;
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] (ISOFORM 1), FUNCTION, SUBCELLULAR LOCATION, AND
RP MUTAGENESIS OF ASP-298.
RX PubMed=17374715; DOI=10.1101/gad.1499107;
RA Lu G., Ren S., Korge P., Choi J., Dong Y., Weiss J., Koehler C.,
RA Chen J.-N., Wang Y.;
RT "A novel mitochondrial matrix serine/threonine protein phosphatase
RT regulates the mitochondria permeability transition pore and is essential
RT for cellular survival and development.";
RL Genes Dev. 21:784-796(2007).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1 AND 2).
RA Mao Y., Xie Y., Dai J.;
RT "Cloning and characterization of a novel human PP2C gene from fetal
RT brain.";
RL Submitted (OCT-2002) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), SUBCELLULAR LOCATION, AND
RP BIOPHYSICOCHEMICAL PROPERTIES.
RX PubMed=17336929; DOI=10.1016/j.bbrc.2007.02.108;
RA Joshi M.A., Jeoung N.H., Popov K.M., Harris R.A.;
RT "Identification of a novel PP2C-type mitochondrial phosphatase.";
RL Biochem. Biophys. Res. Commun. 356:38-44(2007).
RN [4]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
RA Xu J., Stagliano N., Deponte J. III, Rodrigue-Way A., Golden S., Katz S.,
RA Jeyaseelan R., Donoghue M., Meyers R., Gottfried S., Wysong D.,
RA McGovern K., Pollman M., Breitbart R.E., Acton S.;
RT "Protein phosphatase 2C kappa is upregulated in heart failure and
RT attenuates agonist-induced cardiomyocyte hypertrophy.";
RL Submitted (OCT-2003) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=Cerebellum, and Testis;
RX PubMed=14702039; DOI=10.1038/ng1285;
RA Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
RA Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
RA Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
RA Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
RA Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H.,
RA Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M.,
RA Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K.,
RA Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T.,
RA Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M.,
RA Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S.,
RA Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H.,
RA Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K.,
RA Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N.,
RA Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
RA Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
RA Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
RA Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
RA Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y.,
RA Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K.,
RA Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T.,
RA Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T.,
RA Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y.,
RA Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H.,
RA Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y.,
RA Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H.,
RA Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O.,
RA Isogai T., Sugano S.;
RT "Complete sequencing and characterization of 21,243 full-length human
RT cDNAs.";
RL Nat. Genet. 36:40-45(2004).
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=Amygdala, and Lymph node;
RX PubMed=17974005; DOI=10.1186/1471-2164-8-399;
RA Bechtel S., Rosenfelder H., Duda A., Schmidt C.P., Ernst U.,
RA Wellenreuther R., Mehrle A., Schuster C., Bahr A., Bloecker H., Heubner D.,
RA Hoerlein A., Michel G., Wedler H., Koehrer K., Ottenwaelder B., Poustka A.,
RA Wiemann S., Schupp I.;
RT "The full-ORF clone resource of the German cDNA consortium.";
RL BMC Genomics 8:399-399(2007).
RN [7]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=15815621; DOI=10.1038/nature03466;
RA Hillier L.W., Graves T.A., Fulton R.S., Fulton L.A., Pepin K.H., Minx P.,
RA Wagner-McPherson C., Layman D., Wylie K., Sekhon M., Becker M.C.,
RA Fewell G.A., Delehaunty K.D., Miner T.L., Nash W.E., Kremitzki C., Oddy L.,
RA Du H., Sun H., Bradshaw-Cordum H., Ali J., Carter J., Cordes M., Harris A.,
RA Isak A., van Brunt A., Nguyen C., Du F., Courtney L., Kalicki J.,
RA Ozersky P., Abbott S., Armstrong J., Belter E.A., Caruso L., Cedroni M.,
RA Cotton M., Davidson T., Desai A., Elliott G., Erb T., Fronick C., Gaige T.,
RA Haakenson W., Haglund K., Holmes A., Harkins R., Kim K., Kruchowski S.S.,
RA Strong C.M., Grewal N., Goyea E., Hou S., Levy A., Martinka S., Mead K.,
RA McLellan M.D., Meyer R., Randall-Maher J., Tomlinson C.,
RA Dauphin-Kohlberg S., Kozlowicz-Reilly A., Shah N., Swearengen-Shahid S.,
RA Snider J., Strong J.T., Thompson J., Yoakum M., Leonard S., Pearman C.,
RA Trani L., Radionenko M., Waligorski J.E., Wang C., Rock S.M.,
RA Tin-Wollam A.-M., Maupin R., Latreille P., Wendl M.C., Yang S.-P., Pohl C.,
RA Wallis J.W., Spieth J., Bieri T.A., Berkowicz N., Nelson J.O., Osborne J.,
RA Ding L., Meyer R., Sabo A., Shotland Y., Sinha P., Wohldmann P.E.,
RA Cook L.L., Hickenbotham M.T., Eldred J., Williams D., Jones T.A., She X.,
RA Ciccarelli F.D., Izaurralde E., Taylor J., Schmutz J., Myers R.M.,
RA Cox D.R., Huang X., McPherson J.D., Mardis E.R., Clifton S.W., Warren W.C.,
RA Chinwalla A.T., Eddy S.R., Marra M.A., Ovcharenko I., Furey T.S.,
RA Miller W., Eichler E.E., Bork P., Suyama M., Torrents D., Waterston R.H.,
RA Wilson R.K.;
RT "Generation and annotation of the DNA sequences of human chromosomes 2 and
RT 4.";
RL Nature 434:724-731(2005).
RN [8]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M.,
RA Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J.,
RA Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S.,
RA Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H.,
RA Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K.,
RA Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D.,
RA Hunkapiller M.W., Myers E.W., Venter J.C.;
RL Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN [9]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 3), AND VARIANT
RP LYS-94.
RC TISSUE=Pancreas, and Testis;
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 [10]
RP INVOLVEMENT IN MSUDMV.
RX PubMed=23086801; DOI=10.1002/humu.22242;
RA Oyarzabal A., Martinez-Pardo M., Merinero B., Navarrete R., Desviat L.R.,
RA Ugarte M., Rodriguez-Pombo P.;
RT "A novel regulatory defect in the branched-chain alpha-keto acid
RT dehydrogenase complex due to a mutation in the PPM1K gene causes a mild
RT variant phenotype of maple syrup urine disease.";
RL Hum. Mutat. 34:355-362(2013).
RN [11]
RP X-RAY CRYSTALLOGRAPHY (2.25 ANGSTROMS) OF 89-351, AND MAGNESIUM-BINDING.
RX PubMed=18058037; DOI=10.1007/s10969-007-9036-1;
RA Almo S.C., Bonanno J.B., Sauder J.M., Emtage S., Dilorenzo T.P.,
RA Malashkevich V., Wasserman S.R., Swaminathan S., Eswaramoorthy S.,
RA Agarwal R., Kumaran D., Madegowda M., Ragumani S., Patskovsky Y.,
RA Alvarado J., Ramagopal U.A., Faber-Barata J., Chance M.R., Sali A.,
RA Fiser A., Zhang Z.Y., Lawrence D.S., Burley S.K.;
RT "Structural genomics of protein phosphatases.";
RL J. Struct. Funct. Genomics 8:121-140(2007).
RN [12]
RP VARIANT HIS-26.
RX PubMed=23200863; DOI=10.1016/j.ajhg.2012.10.024;
RA Charlesworth G., Plagnol V., Holmstroem K.M., Bras J., Sheerin U.M.,
RA Preza E., Rubio-Agusti I., Ryten M., Schneider S.A., Stamelou M.,
RA Trabzuni D., Abramov A.Y., Bhatia K.P., Wood N.W.;
RT "Mutations in ANO3 cause dominant craniocervical dystonia: ion channel
RT implicated in pathogenesis.";
RL Am. J. Hum. Genet. 91:1041-1050(2012).
CC -!- FUNCTION: Regulates the mitochondrial permeability transition pore and
CC is essential for cellular survival and development.
CC {ECO:0000269|PubMed:17374715}.
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 -!- 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 -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Name=Mn(2+); Xref=ChEBI:CHEBI:29035;
CC Note=Binds 1 Mg(2+) or Mn(2+) ion per subunit.;
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=10.7 mM for p-nitrophenylphosphate {ECO:0000269|PubMed:17336929};
CC Vmax=3.6 umol/min/mg enzyme toward p-nitrophenylphosphate (at 30
CC degrees Celsius) {ECO:0000269|PubMed:17336929};
CC Vmax=4 nmol/min/mg enzyme toward branched-chain alpha-ketoacid
CC dehydrogenase complex (at 37 degrees Celsius)
CC {ECO:0000269|PubMed:17336929};
CC Note=Half maximal activity toward p-nitrophenylphosphate achieved
CC with 3.7 mM of manganese ions.;
CC -!- INTERACTION:
CC Q8N3J5; Q13490: BIRC2; NbExp=6; IntAct=EBI-3923368, EBI-514538;
CC Q8N3J5; A0A024R8L2: hCG_1987119; NbExp=3; IntAct=EBI-3923368, EBI-14103818;
CC Q8N3J5; O75031: HSF2BP; NbExp=3; IntAct=EBI-3923368, EBI-7116203;
CC Q8N3J5; P43364: MAGEA11; NbExp=3; IntAct=EBI-3923368, EBI-739552;
CC Q8N3J5; Q96HA8: NTAQ1; NbExp=3; IntAct=EBI-3923368, EBI-741158;
CC Q8N3J5; Q5T124-6: UBXN11; NbExp=3; IntAct=EBI-3923368, EBI-11524408;
CC Q8N3J5; P98170: XIAP; NbExp=3; IntAct=EBI-3923368, EBI-517127;
CC Q8N3J5; Q86VK4-3: ZNF410; NbExp=3; IntAct=EBI-3923368, EBI-11741890;
CC -!- SUBCELLULAR LOCATION: Mitochondrion matrix
CC {ECO:0000269|PubMed:17336929, ECO:0000269|PubMed:17374715}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=3;
CC Name=1;
CC IsoId=Q8N3J5-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q8N3J5-2; Sequence=VSP_023158, VSP_023159;
CC Name=3;
CC IsoId=Q8N3J5-3; Sequence=VSP_023156, VSP_023157;
CC -!- DISEASE: Maple syrup urine disease, mild variant (MSUDMV) [MIM:615135]:
CC A mild form of maple syrup urine disease, a metabolic disorder due to
CC an enzyme defect in the catabolic pathway of the branched-chain amino
CC acids leucine, isoleucine, and valine. Accumulation of these 3 amino
CC acids and their corresponding keto acids leads to encephalopathy and
CC progressive neurodegeneration. Clinical features include mental and
CC physical retardation, feeding problems, and a maple syrup odor to the
CC urine. The keto acids of the branched-chain amino acids are present in
CC the urine. If untreated, maple syrup urine disease can lead to
CC seizures, coma, and death. The disease is often classified by its
CC pattern of signs and symptoms. The most common and severe form of the
CC disease is the classic type, which becomes apparent soon after birth.
CC Variant forms of the disorder become apparent later in infancy or
CC childhood and are typically milder, but they still involve
CC developmental delay and other medical problems if not treated. MSUDMV
CC is characterized by increased plasma levels of branched-chain amino
CC acids (BCAA) apparent at birth. Treatment with a low-protein diet free
CC of BCAA can result in normal psychomotor development and lack of
CC metabolic episodes. {ECO:0000269|PubMed:23086801}. Note=The gene
CC represented in this entry is involved in disease pathogenesis.
CC -!- SIMILARITY: Belongs to the PP2C family. {ECO:0000305}.
CC -!- CAUTION: PubMed:18058037 has crystallized PPM1K in the presence of
CC magnesium ions. However, PubMed:17336929 reported that no activity
CC toward p-nitrophenylphosphate was seen in the absence of manganese ions
CC and magnesium could not substitute for manganese. {ECO:0000305}.
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DR EMBL; AY157615; AAO17296.1; -; mRNA.
DR EMBL; AF351614; AAN76514.1; -; mRNA.
DR EMBL; AY994097; AAX77016.1; -; mRNA.
DR EMBL; AY435431; AAR06213.1; -; mRNA.
DR EMBL; AK054678; BAB70790.1; -; mRNA.
DR EMBL; AK314417; BAG37038.1; -; mRNA.
DR EMBL; AL834167; CAD38869.2; -; mRNA.
DR EMBL; AL834271; CAD38946.1; -; mRNA.
DR EMBL; AC107067; AAY41021.1; -; Genomic_DNA.
DR EMBL; AC108213; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH471057; EAX06016.1; -; Genomic_DNA.
DR EMBL; BC020850; AAH20850.1; ALT_TERM; mRNA.
DR EMBL; BC037552; AAH37552.1; -; mRNA.
DR EMBL; BC041350; AAH41350.1; -; mRNA.
DR CCDS; CCDS3629.1; -. [Q8N3J5-1]
DR RefSeq; NP_689755.3; NM_152542.4. [Q8N3J5-1]
DR RefSeq; XP_006714174.1; XM_006714111.3. [Q8N3J5-1]
DR RefSeq; XP_016863292.1; XM_017007803.1. [Q8N3J5-1]
DR PDB; 2IQ1; X-ray; 2.25 A; A=89-351.
DR PDB; 4DA1; X-ray; 2.38 A; A=84-360.
DR PDB; 6AK7; X-ray; 2.60 A; A=90-349.
DR PDBsum; 2IQ1; -.
DR PDBsum; 4DA1; -.
DR PDBsum; 6AK7; -.
DR AlphaFoldDB; Q8N3J5; -.
DR SMR; Q8N3J5; -.
DR BioGRID; 127472; 52.
DR IntAct; Q8N3J5; 38.
DR MINT; Q8N3J5; -.
DR STRING; 9606.ENSP00000477341; -.
DR DEPOD; PPM1K; -.
DR iPTMnet; Q8N3J5; -.
DR PhosphoSitePlus; Q8N3J5; -.
DR BioMuta; PPM1K; -.
DR DMDM; 74750962; -.
DR EPD; Q8N3J5; -.
DR MassIVE; Q8N3J5; -.
DR PaxDb; Q8N3J5; -.
DR PeptideAtlas; Q8N3J5; -.
DR PRIDE; Q8N3J5; -.
DR ProteomicsDB; 71811; -. [Q8N3J5-1]
DR ProteomicsDB; 71812; -. [Q8N3J5-2]
DR ProteomicsDB; 71813; -. [Q8N3J5-3]
DR Antibodypedia; 14616; 162 antibodies from 28 providers.
DR DNASU; 152926; -.
DR Ensembl; ENST00000608933.6; ENSP00000477341.1; ENSG00000163644.15. [Q8N3J5-1]
DR GeneID; 152926; -.
DR KEGG; hsa:152926; -.
DR MANE-Select; ENST00000608933.6; ENSP00000477341.1; NM_152542.5; NP_689755.3.
DR UCSC; uc003hrm.6; human. [Q8N3J5-1]
DR CTD; 152926; -.
DR DisGeNET; 152926; -.
DR GeneCards; PPM1K; -.
DR HGNC; HGNC:25415; PPM1K.
DR HPA; ENSG00000163644; Tissue enhanced (heart).
DR MalaCards; PPM1K; -.
DR MIM; 611065; gene.
DR MIM; 615135; phenotype.
DR neXtProt; NX_Q8N3J5; -.
DR OpenTargets; ENSG00000163644; -.
DR Orphanet; 268162; Intermediate maple syrup urine disease.
DR PharmGKB; PA134912083; -.
DR VEuPathDB; HostDB:ENSG00000163644; -.
DR eggNOG; KOG0698; Eukaryota.
DR GeneTree; ENSGT00940000156633; -.
DR HOGENOM; CLU_013173_1_3_1; -.
DR InParanoid; Q8N3J5; -.
DR OMA; MKGADNC; -.
DR OrthoDB; 1044139at2759; -.
DR PhylomeDB; Q8N3J5; -.
DR TreeFam; TF354344; -.
DR BRENDA; 3.1.3.16; 2681.
DR BRENDA; 3.1.3.52; 2681.
DR PathwayCommons; Q8N3J5; -.
DR Reactome; R-HSA-70895; Branched-chain amino acid catabolism.
DR SignaLink; Q8N3J5; -.
DR SIGNOR; Q8N3J5; -.
DR BioGRID-ORCS; 152926; 9 hits in 1078 CRISPR screens.
DR ChiTaRS; PPM1K; human.
DR EvolutionaryTrace; Q8N3J5; -.
DR GeneWiki; PPM1K; -.
DR GenomeRNAi; 152926; -.
DR Pharos; Q8N3J5; Tbio.
DR PRO; PR:Q8N3J5; -.
DR Proteomes; UP000005640; Chromosome 4.
DR RNAct; Q8N3J5; protein.
DR Bgee; ENSG00000163644; Expressed in left ventricle myocardium and 192 other tissues.
DR ExpressionAtlas; Q8N3J5; baseline and differential.
DR Genevisible; Q8N3J5; HS.
DR GO; GO:0005759; C:mitochondrial matrix; TAS:Reactome.
DR GO; GO:0005739; C:mitochondrion; IDA:HPA.
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:0004722; F:protein serine/threonine phosphatase activity; IBA:GO_Central.
DR GO; GO:0035970; P:peptidyl-threonine dephosphorylation; IBA:GO_Central.
DR CDD; cd00143; PP2Cc; 1.
DR Gene3D; 3.60.40.10; -; 1.
DR InterPro; IPR000222; PP2C_BS.
DR InterPro; IPR036457; PPM-type_dom_sf.
DR InterPro; IPR001932; PPM-type_phosphatase_dom.
DR Pfam; PF00481; PP2C; 1.
DR SMART; SM00331; PP2C_SIG; 1.
DR SMART; SM00332; PP2Cc; 1.
DR SUPFAM; SSF81606; SSF81606; 1.
DR PROSITE; PS01032; PPM_1; 1.
DR PROSITE; PS51746; PPM_2; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Alternative splicing; Hydrolase; Magnesium; Manganese;
KW Metal-binding; Mitochondrion; Phosphoprotein; Protein phosphatase;
KW Reference proteome; Transit peptide.
FT TRANSIT 1..29
FT /note="Mitochondrion"
FT /evidence="ECO:0000255"
FT CHAIN 30..372
FT /note="Protein phosphatase 1K, mitochondrial"
FT /id="PRO_0000278208"
FT DOMAIN 94..346
FT /note="PPM-type phosphatase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01082"
FT REGION 34..55
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 34..48
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 127
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT BINDING 128
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT BINDING 337
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT MOD_RES 248
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q8BXN7"
FT VAR_SEQ 148..150
FT /note="DLL -> YVQ (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_023156"
FT VAR_SEQ 151..372
FT /note="Missing (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_023157"
FT VAR_SEQ 181..233
FT /note="ATLLTSGTTATVALLRDGIELVVASVGDSRAILCRKGKPMKLTIDHTPERKD
FT E -> ENCAWSAALDLEPVDTICGASVEREICLILSQVKESSGSYPGLREGSHISLSH
FT (in isoform 2)"
FT /evidence="ECO:0000303|Ref.2"
FT /id="VSP_023158"
FT VAR_SEQ 234..372
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|Ref.2"
FT /id="VSP_023159"
FT VARIANT 26
FT /note="R -> H (in dbSNP:rs369916009)"
FT /evidence="ECO:0000269|PubMed:23200863"
FT /id="VAR_069736"
FT VARIANT 94
FT /note="N -> K (in dbSNP:rs17853762)"
FT /evidence="ECO:0000269|PubMed:15489334"
FT /id="VAR_030691"
FT VARIANT 321
FT /note="E -> K (in dbSNP:rs35523553)"
FT /id="VAR_050621"
FT MUTAGEN 298
FT /note="D->A: Loss of activity."
FT /evidence="ECO:0000269|PubMed:17374715"
FT CONFLICT 17
FT /note="V -> A (in Ref. 3; AAX77016)"
FT /evidence="ECO:0000305"
FT CONFLICT 194
FT /note="L -> I (in Ref. 3; AAX77016)"
FT /evidence="ECO:0000305"
FT CONFLICT 211
FT /note="A -> V (in Ref. 9; AAH20850)"
FT /evidence="ECO:0000305"
FT CONFLICT 264
FT /note="I -> V (in Ref. 5; BAB70790)"
FT /evidence="ECO:0000305"
FT HELIX 92..94
FT /evidence="ECO:0007829|PDB:2IQ1"
FT STRAND 96..100
FT /evidence="ECO:0007829|PDB:2IQ1"
FT STRAND 103..106
FT /evidence="ECO:0007829|PDB:2IQ1"
FT STRAND 109..115
FT /evidence="ECO:0007829|PDB:2IQ1"
FT STRAND 117..131
FT /evidence="ECO:0007829|PDB:2IQ1"
FT HELIX 133..149
FT /evidence="ECO:0007829|PDB:2IQ1"
FT TURN 150..152
FT /evidence="ECO:0007829|PDB:2IQ1"
FT HELIX 156..176
FT /evidence="ECO:0007829|PDB:2IQ1"
FT HELIX 183..185
FT /evidence="ECO:0007829|PDB:2IQ1"
FT STRAND 190..196
FT /evidence="ECO:0007829|PDB:2IQ1"
FT TURN 197..199
FT /evidence="ECO:0007829|PDB:2IQ1"
FT STRAND 200..208
FT /evidence="ECO:0007829|PDB:2IQ1"
FT STRAND 210..215
FT /evidence="ECO:0007829|PDB:2IQ1"
FT STRAND 218..221
FT /evidence="ECO:0007829|PDB:2IQ1"
FT HELIX 231..239
FT /evidence="ECO:0007829|PDB:2IQ1"
FT STRAND 244..246
FT /evidence="ECO:0007829|PDB:2IQ1"
FT STRAND 252..254
FT /evidence="ECO:0007829|PDB:2IQ1"
FT TURN 255..257
FT /evidence="ECO:0007829|PDB:2IQ1"
FT STRAND 258..262
FT /evidence="ECO:0007829|PDB:6AK7"
FT HELIX 267..269
FT /evidence="ECO:0007829|PDB:2IQ1"
FT TURN 270..273
FT /evidence="ECO:0007829|PDB:2IQ1"
FT STRAND 279..284
FT /evidence="ECO:0007829|PDB:2IQ1"
FT TURN 287..289
FT /evidence="ECO:0007829|PDB:2IQ1"
FT STRAND 290..296
FT /evidence="ECO:0007829|PDB:2IQ1"
FT HELIX 298..301
FT /evidence="ECO:0007829|PDB:2IQ1"
FT HELIX 306..314
FT /evidence="ECO:0007829|PDB:2IQ1"
FT STRAND 316..318
FT /evidence="ECO:0007829|PDB:2IQ1"
FT HELIX 319..332
FT /evidence="ECO:0007829|PDB:2IQ1"
FT STRAND 339..345
FT /evidence="ECO:0007829|PDB:2IQ1"
SQ SEQUENCE 372 AA; 40997 MW; 9DD37EEC0EAD3313 CRC64;
MSTAALITLV RSGGNQVRRR VLLSSRLLQD DRRVTPTCHS STSEPRCSRF DPDGSGSPAT
WDNFGIWDNR IDEPILLPPS IKYGKPIPKI SLENVGCASQ IGKRKENEDR FDFAQLTDEV
LYFAVYDGHG GPAAADFCHT HMEKCIMDLL PKEKNLETLL TLAFLEIDKA FSSHARLSAD
ATLLTSGTTA TVALLRDGIE LVVASVGDSR AILCRKGKPM KLTIDHTPER KDEKERIKKC
GGFVAWNSLG QPHVNGRLAM TRSIGDLDLK TSGVIAEPET KRIKLHHADD SFLVLTTDGI
NFMVNSQEIC DFVNQCHDPN EAAHAVTEQA IQYGTEDNST AVVVPFGAWG KYKNSEINFS
FSRSFASSGR WA
