ID   PPM1H_MOUSE             Reviewed;         513 AA.
AC   Q3UYC0; Q3UD05; Q3V3H5; Q3V3Y7; Q571C9; Q7TMU7; Q8BYE6;
DT   15-MAY-2007, integrated into UniProtKB/Swiss-Prot.
DT   11-OCT-2005, sequence version 1.
DT   27-MAR-2024, entry version 134.
DE   RecName: Full=Protein phosphatase 1H;
DE            EC=3.1.3.16;
GN   Name=Ppm1h; Synonyms=Kiaa1157;
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] (ISOFORMS 1 AND 2).
RC   STRAIN=C57BL/6J;
RC   TISSUE=Bone marrow, Head, Medulla oblongata, and Thymus;
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] (ISOFORM 1).
RC   TISSUE=Pancreatic islet;
RA   Okazaki N., Kikuno R.F., Ohara R., Inamoto S., Nagase T., Ohara O.,
RA   Koga H.;
RT   "Prediction of the coding sequences of mouse homologues of KIAA gene. The
RT   complete nucleotide sequences of mouse KIAA-homologous cDNAs identified by
RT   screening of terminal sequences of cDNA clones randomly sampled from size-
RT   fractionated libraries.";
RL   Submitted (FEB-2005) to the EMBL/GenBank/DDBJ databases.
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 90-513 (ISOFORM 1).
RC   STRAIN=C57BL/6NCr; TISSUE=Hematopoietic 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   [4]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-123, AND IDENTIFICATION BY
RP   MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX   PubMed=19144319; DOI=10.1016/j.immuni.2008.11.006;
RA   Trost M., English L., Lemieux S., Courcelles M., Desjardins M.,
RA   Thibault P.;
RT   "The phagosomal proteome in interferon-gamma-activated macrophages.";
RL   Immunity 30:143-154(2009).
RN   [5]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-7; SER-123; SER-220 AND
RP   THR-223, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   TISSUE=Brain, Kidney, and Lung;
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).
RN   [6]
RP   METHYLATION [LARGE SCALE ANALYSIS] AT ARG-212, AND IDENTIFICATION BY MASS
RP   SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   TISSUE=Brain, and Embryo;
RX   PubMed=24129315; DOI=10.1074/mcp.o113.027870;
RA   Guo A., Gu H., Zhou J., Mulhern D., Wang Y., Lee K.A., Yang V., Aguiar M.,
RA   Kornhauser J., Jia X., Ren J., Beausoleil S.A., Silva J.C., Vemulapalli V.,
RA   Bedford M.T., Comb M.J.;
RT   "Immunoaffinity enrichment and mass spectrometry analysis of protein
RT   methylation.";
RL   Mol. Cell. Proteomics 13:372-387(2014).
CC   -!- FUNCTION: Dephosphorylates CDKN1B at 'Thr-187', thus removing a signal
CC       for proteasomal degradation. {ECO:0000250|UniProtKB:Q9ULR3}.
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   -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:Q9ULR3}. Cytoplasm
CC       {ECO:0000250|UniProtKB:Q9ULR3}.
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=2;
CC       Name=1;
CC         IsoId=Q3UYC0-1; Sequence=Displayed;
CC       Name=2;
CC         IsoId=Q3UYC0-2; Sequence=VSP_025121, VSP_025122;
CC   -!- SIMILARITY: Belongs to the PP2C family. {ECO:0000305}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=BAD90185.1; Type=Erroneous initiation; Evidence={ECO:0000305};
CC       Sequence=BAE29457.1; Type=Erroneous initiation; Evidence={ECO:0000305};
CC       Sequence=BAE43270.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR   EMBL; AK029461; BAE43270.1; ALT_INIT; mRNA.
DR   EMBL; AK040194; BAC30536.1; -; mRNA.
DR   EMBL; AK040207; BAE43308.1; -; mRNA.
DR   EMBL; AK134804; BAE22292.1; -; mRNA.
DR   EMBL; AK150309; BAE29457.1; ALT_INIT; mRNA.
DR   EMBL; AK220260; BAD90185.1; ALT_INIT; mRNA.
DR   EMBL; BC052910; AAH52910.1; -; mRNA.
DR   CCDS; CCDS48705.1; -. [Q3UYC0-1]
DR   CCDS; CCDS48706.1; -. [Q3UYC0-2]
DR   RefSeq; NP_001103688.1; NM_001110218.1. [Q3UYC0-1]
DR   RefSeq; NP_795893.2; NM_176919.4. [Q3UYC0-2]
DR   AlphaFoldDB; Q3UYC0; -.
DR   SMR; Q3UYC0; -.
DR   BioGRID; 235293; 1.
DR   IntAct; Q3UYC0; 1.
DR   STRING; 10090.ENSMUSP00000066561; -.
DR   iPTMnet; Q3UYC0; -.
DR   PhosphoSitePlus; Q3UYC0; -.
DR   SwissPalm; Q3UYC0; -.
DR   EPD; Q3UYC0; -.
DR   jPOST; Q3UYC0; -.
DR   MaxQB; Q3UYC0; -.
DR   PaxDb; 10090-ENSMUSP00000066561; -.
DR   PeptideAtlas; Q3UYC0; -.
DR   ProteomicsDB; 289380; -. [Q3UYC0-1]
DR   ProteomicsDB; 289381; -. [Q3UYC0-2]
DR   Antibodypedia; 53103; 175 antibodies from 22 providers.
DR   DNASU; 319468; -.
DR   Ensembl; ENSMUST00000067918.12; ENSMUSP00000066561.6; ENSMUSG00000034613.13. [Q3UYC0-1]
DR   Ensembl; ENSMUST00000161487.8; ENSMUSP00000124982.2; ENSMUSG00000034613.13. [Q3UYC0-2]
DR   GeneID; 319468; -.
DR   KEGG; mmu:319468; -.
DR   UCSC; uc007hgf.2; mouse. [Q3UYC0-1]
DR   UCSC; uc007hgg.2; mouse. [Q3UYC0-2]
DR   AGR; MGI:2442087; -.
DR   CTD; 57460; -.
DR   MGI; MGI:2442087; Ppm1h.
DR   VEuPathDB; HostDB:ENSMUSG00000034613; -.
DR   eggNOG; KOG1323; Eukaryota.
DR   GeneTree; ENSGT00940000160095; -.
DR   HOGENOM; CLU_029072_1_0_1; -.
DR   InParanoid; Q3UYC0; -.
DR   OMA; YKEHIEW; -.
DR   OrthoDB; 1450097at2759; -.
DR   PhylomeDB; Q3UYC0; -.
DR   TreeFam; TF314700; -.
DR   BioGRID-ORCS; 319468; 2 hits in 76 CRISPR screens.
DR   ChiTaRS; Ppm1h; mouse.
DR   PRO; PR:Q3UYC0; -.
DR   Proteomes; UP000000589; Chromosome 10.
DR   RNAct; Q3UYC0; Protein.
DR   Bgee; ENSMUSG00000034613; Expressed in ciliary body and 210 other cell types or tissues.
DR   ExpressionAtlas; Q3UYC0; baseline and differential.
DR   GO; GO:0005737; C:cytoplasm; ISS:UniProtKB.
DR   GO; GO:0098978; C:glutamatergic synapse; IDA:SynGO.
DR   GO; GO:0005739; C:mitochondrion; IBA:GO_Central.
DR   GO; GO:0005654; C:nucleoplasm; ISO:MGI.
DR   GO; GO:0005634; C:nucleus; ISS:UniProtKB.
DR   GO; GO:0045202; C:synapse; IDA:SynGO.
DR   GO; GO:0004741; F:[pyruvate dehydrogenase (acetyl-transferring)]-phosphatase activity; IBA:GO_Central.
DR   GO; GO:0042802; F:identical protein binding; ISO:MGI.
DR   GO; GO:0017018; F:myosin phosphatase activity; IEA:UniProtKB-EC.
DR   GO; GO:0004721; F:phosphoprotein phosphatase activity; ISS:UniProtKB.
DR   CDD; cd00143; PP2Cc; 1.
DR   Gene3D; 3.60.40.10; PPM-type phosphatase domain; 1.
DR   InterPro; IPR015655; PP2C.
DR   InterPro; IPR036457; PPM-type-like_dom_sf.
DR   InterPro; IPR001932; PPM-type_phosphatase-like_dom.
DR   PANTHER; PTHR13832:SF287; PROTEIN PHOSPHATASE 1H; 1.
DR   PANTHER; PTHR13832; PROTEIN PHOSPHATASE 2C; 1.
DR   Pfam; PF00481; PP2C; 2.
DR   SMART; SM00332; PP2Cc; 1.
DR   SUPFAM; SSF81606; PP2C-like; 1.
DR   PROSITE; PS51746; PPM_2; 1.
DR   Genevisible; Q3UYC0; MM.
PE   1: Evidence at protein level;
KW   Alternative splicing; Cytoplasm; Hydrolase; Methylation; Nucleus;
KW   Phosphoprotein; Protein phosphatase; Reference proteome.
FT   CHAIN           1..513
FT                   /note="Protein phosphatase 1H"
FT                   /id="PRO_0000286604"
FT   DOMAIN          77..506
FT                   /note="PPM-type phosphatase"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01082"
FT   REGION          109..133
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOD_RES         7
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:21183079"
FT   MOD_RES         113
FT                   /note="Phosphothreonine"
FT                   /evidence="ECO:0000250|UniProtKB:Q5M821"
FT   MOD_RES         123
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:19144319,
FT                   ECO:0007744|PubMed:21183079"
FT   MOD_RES         210
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q9ULR3"
FT   MOD_RES         212
FT                   /note="Omega-N-methylarginine"
FT                   /evidence="ECO:0007744|PubMed:24129315"
FT   MOD_RES         220
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:21183079"
FT   MOD_RES         223
FT                   /note="Phosphothreonine"
FT                   /evidence="ECO:0007744|PubMed:21183079"
FT   MOD_RES         421
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q9ULR3"
FT   VAR_SEQ         466..469
FT                   /note="YTLA -> FVPL (in isoform 2)"
FT                   /evidence="ECO:0000303|PubMed:16141072"
FT                   /id="VSP_025121"
FT   VAR_SEQ         470..513
FT                   /note="Missing (in isoform 2)"
FT                   /evidence="ECO:0000303|PubMed:16141072"
FT                   /id="VSP_025122"
FT   CONFLICT        90..93
FT                   /note="THNE -> EVIP (in Ref. 3; AAH52910)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        130
FT                   /note="L -> R (in Ref. 2; BAD90185)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        168
FT                   /note="H -> P (in Ref. 3; AAH52910)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        198
FT                   /note="T -> A (in Ref. 1; BAE43308)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        260
FT                   /note="S -> G (in Ref. 1; BAE29457)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        456
FT                   /note="P -> L (in Ref. 3; AAH52910)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   513 AA;  56380 MW;  27885A4519A0F0DB CRC64;
     MLTRVKSAVA NFMGGIMAGS SGSEHGGSGC GGSDLPLRFP YGRPEFLGLS QDEVECSADH
     IARPILILKE TRRLPWATGY AEVINAGKST HNEDQASCEV LTVKKKAGTI TSTPNRNSKR
     RSSLPNGEGL QLKENSESEG ISCHYWSLFD GHAGSGAAVV ASRLLQHHIT QQLQDIVEIL
     KNSAILPPTC LGEEPESTPA HGRTLTRAAS LRGGVGAPGS PSTPPTRFFT EKKIPHECLV
     IGALESAFKE MDLQIERERS AYNISGGCTA LIVVCLLGKL YVANAGDSRA IIIRNGEIIP
     MSSEFTPETE RQRLQYLAFM QPHLLGNEFT HLEFPRRVQR KELGKKMLYR DFNMTGWAYK
     TIEDDDLKFP LIYGEGKKAR VMATIGVTRG LGDHDLKVHD SNIYIKPFLS SAPEVRVYDL
     SRYEHGADDV LILATDGLWD VLSNEEVAEA ITQFLPNCDP DDPHRYTLAA QDLVMRARGV
     LKDRGWRISN DRLGSGDDIS VYVIPLIHGN KLS
//