PPM1G_MOUSE
ID PPM1G_MOUSE Reviewed; 542 AA.
AC Q61074;
DT 15-JUL-1998, integrated into UniProtKB/Swiss-Prot.
DT 15-JUL-1999, sequence version 3.
DT 03-AUG-2022, entry version 175.
DE RecName: Full=Protein phosphatase 1G;
DE EC=3.1.3.16;
DE AltName: Full=Fibroblast growth factor-inducible protein 13;
DE Short=FIN13;
DE AltName: Full=Protein phosphatase 1C;
DE AltName: Full=Protein phosphatase 2C isoform gamma;
DE Short=PP2C-gamma;
DE AltName: Full=Protein phosphatase magnesium-dependent 1 gamma;
GN Name=Ppm1g; Synonyms=Fin13, Ppm1c;
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 [MRNA], FUNCTION, AND SUBCELLULAR LOCATION.
RX PubMed=9271424; DOI=10.1128/mcb.17.9.5485;
RA Guthridge M.A., Bellosta P., Tavoloni N., Basilico C.;
RT "FIN13, a novel growth factor-inducible serine-threonine phosphatase which
RT can inhibit cell cycle progression.";
RL Mol. Cell. Biol. 17:5485-5498(1997).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=FVB/N; TISSUE=Mammary gland;
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 [3]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 123-420.
RX PubMed=8649829;
RA Guthridge M.A., Seldin M., Basilico C.;
RT "Induction of expression of growth-related genes by FGF-4 in mouse
RT fibroblasts.";
RL Oncogene 12:1267-1278(1996).
RN [4]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-524, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain, Brown adipose tissue, Heart, Kidney, Liver, Lung, Pancreas,
RC Spleen, and Testis;
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 [5]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-380, AND IDENTIFICATION BY MASS
RP SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Embryonic fibroblast;
RX PubMed=23806337; DOI=10.1016/j.molcel.2013.06.001;
RA Park J., Chen Y., Tishkoff D.X., Peng C., Tan M., Dai L., Xie Z., Zhang Y.,
RA Zwaans B.M., Skinner M.E., Lombard D.B., Zhao Y.;
RT "SIRT5-mediated lysine desuccinylation impacts diverse metabolic
RT pathways.";
RL Mol. Cell 50:919-930(2013).
CC -!- FUNCTION: May be involved in regulation of cell cycle.
CC {ECO:0000269|PubMed:9271424}.
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; Evidence={ECO:0000250};
CC Name=Mn(2+); Xref=ChEBI:CHEBI:29035; Evidence={ECO:0000250};
CC Note=Binds 2 magnesium or manganese ions per subunit. {ECO:0000250};
CC -!- SUBUNIT: Interacts with NOL3; may dephosphorylate NOL3.
CC {ECO:0000250|UniProtKB:F1LNI5}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:9271424}. Membrane
CC {ECO:0000250|UniProtKB:O15355}; Lipid-anchor
CC {ECO:0000250|UniProtKB:O15355}.
CC -!- TISSUE SPECIFICITY: Highly expressed in testis. Low level of expression
CC in kidney. Also expressed in a number of tissues undergoing
CC proliferation including embryo, uterus at pregnancy, placenta, and
CC ovaries.
CC -!- INDUCTION: By FGF-4 and serum.
CC -!- SIMILARITY: Belongs to the PP2C family. {ECO:0000305}.
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DR EMBL; BC009004; AAH09004.1; -; mRNA.
DR EMBL; U42383; AAC26322.1; -; mRNA.
DR CCDS; CCDS19179.1; -.
DR RefSeq; NP_032040.1; NM_008014.3.
DR AlphaFoldDB; Q61074; -.
DR SMR; Q61074; -.
DR BioGRID; 199674; 14.
DR IntAct; Q61074; 6.
DR MINT; Q61074; -.
DR STRING; 10090.ENSMUSP00000031032; -.
DR iPTMnet; Q61074; -.
DR PhosphoSitePlus; Q61074; -.
DR SwissPalm; Q61074; -.
DR EPD; Q61074; -.
DR jPOST; Q61074; -.
DR MaxQB; Q61074; -.
DR PaxDb; Q61074; -.
DR PeptideAtlas; Q61074; -.
DR PRIDE; Q61074; -.
DR ProteomicsDB; 291714; -.
DR Antibodypedia; 28474; 412 antibodies from 31 providers.
DR DNASU; 14208; -.
DR Ensembl; ENSMUST00000031032; ENSMUSP00000031032; ENSMUSG00000029147.
DR GeneID; 14208; -.
DR KEGG; mmu:14208; -.
DR UCSC; uc008wxr.1; mouse.
DR CTD; 5496; -.
DR MGI; MGI:106065; Ppm1g.
DR VEuPathDB; HostDB:ENSMUSG00000029147; -.
DR eggNOG; KOG0699; Eukaryota.
DR GeneTree; ENSGT00940000158427; -.
DR InParanoid; Q61074; -.
DR OMA; TPEDEFM; -.
DR OrthoDB; 957254at2759; -.
DR PhylomeDB; Q61074; -.
DR TreeFam; TF354280; -.
DR BioGRID-ORCS; 14208; 12 hits in 72 CRISPR screens.
DR ChiTaRS; Ppm1g; mouse.
DR PRO; PR:Q61074; -.
DR Proteomes; UP000000589; Chromosome 5.
DR RNAct; Q61074; protein.
DR Bgee; ENSMUSG00000029147; Expressed in fetal liver hematopoietic progenitor cell and 268 other tissues.
DR ExpressionAtlas; Q61074; baseline and differential.
DR Genevisible; Q61074; MM.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005654; C:nucleoplasm; ISO:MGI.
DR GO; GO:0005634; C:nucleus; IDA:MGI.
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:0004721; F:phosphoprotein phosphatase activity; IDA:MGI.
DR GO; GO:0004722; F:protein serine/threonine phosphatase activity; ISO:MGI.
DR GO; GO:0007049; P:cell cycle; IEA:UniProtKB-KW.
DR GO; GO:0035970; P:peptidyl-threonine dephosphorylation; ISO:MGI.
DR GO; GO:0006470; P:protein dephosphorylation; IDA:MGI.
DR GO; GO:0051726; P:regulation of cell cycle; IDA:MGI.
DR CDD; cd00143; PP2Cc; 1.
DR Gene3D; 3.60.40.10; -; 2.
DR InterPro; IPR015655; PP2C.
DR InterPro; IPR000222; PP2C_BS.
DR InterPro; IPR036457; PPM-type_dom_sf.
DR InterPro; IPR001932; PPM-type_phosphatase_dom.
DR PANTHER; PTHR13832; PTHR13832; 2.
DR Pfam; PF00481; PP2C; 2.
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 Acetylation; Cell cycle; Hydrolase; Lipoprotein; Magnesium; Manganese;
KW Membrane; Metal-binding; Methylation; Myristate; Nucleus; Phosphoprotein;
KW Protein phosphatase; Reference proteome; Repeat.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000250|UniProtKB:O15355"
FT CHAIN 2..542
FT /note="Protein phosphatase 1G"
FT /id="PRO_0000057751"
FT DOMAIN 26..502
FT /note="PPM-type phosphatase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01082"
FT REGION 117..136
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 164..325
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 513..542
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 197..241
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 261..312
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 60
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
FT BINDING 60
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
FT BINDING 61
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
FT BINDING 438
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
FT BINDING 493
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
FT MOD_RES 22
FT /note="Omega-N-methylarginine"
FT /evidence="ECO:0000250|UniProtKB:O15355"
FT MOD_RES 122
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:O15355"
FT MOD_RES 380
FT /note="N6-acetyllysine"
FT /evidence="ECO:0007744|PubMed:23806337"
FT MOD_RES 524
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT LIPID 2
FT /note="N-myristoyl glycine"
FT /evidence="ECO:0000250|UniProtKB:O15355"
FT CONFLICT 123..126
FT /note="EDED -> NSAR (in Ref. 3)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 542 AA; 58728 MW; 1DC72E7A66E71453 CRC64;
MGAYLSQPNT VKCSGDGVGA PRLPLPYGFS AMQGWRVSME DAHNCIPELD NETAMFSVYD
GHGGEEVALY CAKYLPDIIK DQKAYKEGKL QKALQDAFLA IDAKLTTEEV IKELAQIAGR
PTEDEDDKDK VADEDDVDNE EAALLHEEAT MTIEELLTRY GQNCQKVPPH TKSGIGTGDE
PGPQGLNGEA GPEDPSRETP SQENGPTAKG HTGFSSNSEH GTEAGQISEP GTATGEAGPS
CSSASDKLPR VAKSKFFEDS EDESDEVEEE EDDSEECSED EDGYSSEEAE NEEDEDDTEE
AEEDDDEEMM VPGMEGKEEP GSDSGTTAVV ALIRGKQLIV ANAGDSRCVV SEAGKALDMS
YDHKPEDEVE LARIKNAGGK VTMDGRVNGG LNLSRAIGDH FYKRNKNLPP QEQMISALPD
IKVLTLTDDH EFMVIACDGI WNVMSSQEVV DFIQSKISQR DENGELRLLS SIVEELLDQC
LAPDTSGDGT GCDNMTCIII CFKPRNTVEL QAESGKRKLE EALSTEGAED TGNSDKKKAK
RD
