PPM1H_MOUSE
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 03-AUG-2022, entry version 125.
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; 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; Q3UYC0; -.
DR PeptideAtlas; Q3UYC0; -.
DR PRIDE; Q3UYC0; -.
DR ProteomicsDB; 289380; -. [Q3UYC0-1]
DR ProteomicsDB; 289381; -. [Q3UYC0-2]
DR Antibodypedia; 53103; 157 antibodies from 22 providers.
DR DNASU; 319468; -.
DR Ensembl; ENSMUST00000067918; ENSMUSP00000066561; ENSMUSG00000034613. [Q3UYC0-1]
DR Ensembl; ENSMUST00000161487; ENSMUSP00000124982; ENSMUSG00000034613. [Q3UYC0-2]
DR GeneID; 319468; -.
DR KEGG; mmu:319468; -.
DR UCSC; uc007hgf.2; mouse. [Q3UYC0-1]
DR UCSC; uc007hgg.2; mouse. [Q3UYC0-2]
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; KEHVEWT; -.
DR OrthoDB; 601888at2759; -.
DR PhylomeDB; Q3UYC0; -.
DR TreeFam; TF314700; -.
DR BioGRID-ORCS; 319468; 1 hit in 71 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 208 other tissues.
DR ExpressionAtlas; Q3UYC0; baseline and differential.
DR Genevisible; Q3UYC0; MM.
DR GO; GO:0005737; C:cytoplasm; ISS:UniProtKB.
DR GO; GO:0098978; C:glutamatergic synapse; IDA:SynGO.
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: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 GO; GO:0006470; P:protein dephosphorylation; IBA:GO_Central.
DR CDD; cd00143; PP2Cc; 1.
DR Gene3D; 3.60.40.10; -; 1.
DR InterPro; IPR015655; PP2C.
DR InterPro; IPR036457; PPM-type_dom_sf.
DR InterPro; IPR001932; PPM-type_phosphatase_dom.
DR PANTHER; PTHR13832; PTHR13832; 1.
DR Pfam; PF00481; PP2C; 2.
DR SMART; SM00332; PP2Cc; 1.
DR SUPFAM; SSF81606; SSF81606; 1.
DR PROSITE; PS51746; PPM_2; 1.
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
