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Protein phosphatase 1G (EC 3.1.3.16) (Fibroblast growth factor-inducible protein 13) (FIN13) (Protein phosphatase 1C) (Protein phosphatase 2C isoform gamma) (PP2C-gamma) (Protein phosphatase magnesium-dependent 1 gamma)

 PPM1G_MOUSE             Reviewed;         542 AA.
Q61074;
15-JUL-1998, integrated into UniProtKB/Swiss-Prot.
15-JUL-1999, sequence version 3.
20-DEC-2017, entry version 152.
RecName: Full=Protein phosphatase 1G;
EC=3.1.3.16;
AltName: Full=Fibroblast growth factor-inducible protein 13;
Short=FIN13;
AltName: Full=Protein phosphatase 1C;
AltName: Full=Protein phosphatase 2C isoform gamma;
Short=PP2C-gamma;
AltName: Full=Protein phosphatase magnesium-dependent 1 gamma;
Name=Ppm1g; Synonyms=Fin13, Ppm1c;
Mus musculus (Mouse).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
Muroidea; Muridae; Murinae; Mus; Mus.
NCBI_TaxID=10090;
[1]
NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, AND SUBCELLULAR LOCATION.
PubMed=9271424; DOI=10.1128/MCB.17.9.5485;
Guthridge M.A., Bellosta P., Tavoloni N., Basilico C.;
"FIN13, a novel growth factor-inducible serine-threonine phosphatase
which can inhibit cell cycle progression.";
Mol. Cell. Biol. 17:5485-5498(1997).
[2]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
STRAIN=FVB/N; TISSUE=Mammary gland;
PubMed=15489334; DOI=10.1101/gr.2596504;
The MGC Project Team;
"The status, quality, and expansion of the NIH full-length cDNA
project: the Mammalian Gene Collection (MGC).";
Genome Res. 14:2121-2127(2004).
[3]
NUCLEOTIDE SEQUENCE [MRNA] OF 123-420.
PubMed=8649829;
Guthridge M.A., Seldin M., Basilico C.;
"Induction of expression of growth-related genes by FGF-4 in mouse
fibroblasts.";
Oncogene 12:1267-1278(1996).
[4]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-524, AND IDENTIFICATION
BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Brain, Brown adipose tissue, Heart, Kidney, Liver, Lung,
Pancreas, Spleen, and Testis;
PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
"A tissue-specific atlas of mouse protein phosphorylation and
expression.";
Cell 143:1174-1189(2010).
[5]
ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-380, AND IDENTIFICATION BY
MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Embryonic fibroblast;
PubMed=23806337; DOI=10.1016/j.molcel.2013.06.001;
Park J., Chen Y., Tishkoff D.X., Peng C., Tan M., Dai L., Xie Z.,
Zhang Y., Zwaans B.M., Skinner M.E., Lombard D.B., Zhao Y.;
"SIRT5-mediated lysine desuccinylation impacts diverse metabolic
pathways.";
Mol. Cell 50:919-930(2013).
-!- FUNCTION: May be involved in regulation of cell cycle.
{ECO:0000269|PubMed:9271424}.
-!- CATALYTIC ACTIVITY: [a protein]-serine/threonine phosphate + H(2)O
= [a protein]-serine/threonine + phosphate.
-!- COFACTOR:
Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000250};
Name=Mn(2+); Xref=ChEBI:CHEBI:29035; Evidence={ECO:0000250};
Note=Binds 2 magnesium or manganese ions per subunit.
{ECO:0000250};
-!- SUBUNIT: Interacts with NOL3; may dephosphorylate NOL3.
{ECO:0000250|UniProtKB:F1LNI5}.
-!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:9271424}.
Membrane {ECO:0000250|UniProtKB:O15355}; Lipid-anchor
{ECO:0000250|UniProtKB:O15355}.
-!- TISSUE SPECIFICITY: Highly expressed in testis. Low level of
expression in kidney. Also expressed in a number of tissues
undergoing proliferation including embryo, uterus at pregnancy,
placenta, and ovaries.
-!- INDUCTION: By FGF-4 and serum.
-!- SIMILARITY: Belongs to the PP2C family. {ECO:0000305}.
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EMBL; BC009004; AAH09004.1; -; mRNA.
EMBL; U42383; AAC26322.1; -; mRNA.
CCDS; CCDS19179.1; -.
RefSeq; NP_032040.1; NM_008014.3.
UniGene; Mm.14501; -.
ProteinModelPortal; Q61074; -.
SMR; Q61074; -.
BioGrid; 199674; 2.
IntAct; Q61074; 2.
MINT; MINT-1675839; -.
STRING; 10090.ENSMUSP00000031032; -.
iPTMnet; Q61074; -.
PhosphoSitePlus; Q61074; -.
EPD; Q61074; -.
MaxQB; Q61074; -.
PaxDb; Q61074; -.
PeptideAtlas; Q61074; -.
PRIDE; Q61074; -.
Ensembl; ENSMUST00000031032; ENSMUSP00000031032; ENSMUSG00000029147.
GeneID; 14208; -.
KEGG; mmu:14208; -.
UCSC; uc008wxr.1; mouse.
CTD; 5496; -.
MGI; MGI:106065; Ppm1g.
eggNOG; KOG0699; Eukaryota.
eggNOG; COG0631; LUCA.
GeneTree; ENSGT00900000140981; -.
HOGENOM; HOG000233896; -.
HOVERGEN; HBG053647; -.
InParanoid; Q61074; -.
KO; K17499; -.
OMA; GWRNSQE; -.
OrthoDB; EOG091G0D0W; -.
PhylomeDB; Q61074; -.
TreeFam; TF354280; -.
ChiTaRS; Ppm1g; mouse.
PRO; PR:Q61074; -.
Proteomes; UP000000589; Chromosome 5.
Bgee; ENSMUSG00000029147; -.
ExpressionAtlas; Q61074; baseline and differential.
Genevisible; Q61074; MM.
GO; GO:0016020; C:membrane; IEA:UniProtKB-SubCell.
GO; GO:0005654; C:nucleoplasm; ISO:MGI.
GO; GO:0005634; C:nucleus; IDA:MGI.
GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
GO; GO:0004721; F:phosphoprotein phosphatase activity; IDA:MGI.
GO; GO:0004722; F:protein serine/threonine phosphatase activity; ISO:MGI.
GO; GO:0007050; P:cell cycle arrest; IDA:MGI.
GO; GO:0035970; P:peptidyl-threonine dephosphorylation; ISO:MGI.
GO; GO:0006470; P:protein dephosphorylation; IDA:MGI.
CDD; cd00143; PP2Cc; 1.
Gene3D; 3.60.40.10; -; 2.
InterPro; IPR015655; PP2C.
InterPro; IPR000222; PP2C_BS.
InterPro; IPR036457; PPM-type_dom_sf.
InterPro; IPR001932; PPM-type_phosphatase_dom.
PANTHER; PTHR13832; PTHR13832; 1.
Pfam; PF00481; PP2C; 2.
SMART; SM00332; PP2Cc; 1.
SUPFAM; SSF81606; SSF81606; 2.
PROSITE; PS01032; PPM_1; 1.
PROSITE; PS51746; PPM_2; 1.
1: Evidence at protein level;
Acetylation; Cell cycle; Complete proteome; Hydrolase; Lipoprotein;
Magnesium; Manganese; Membrane; Metal-binding; Methylation; Myristate;
Nucleus; Phosphoprotein; Protein phosphatase; Reference proteome;
Repeat.
INIT_MET 1 1 Removed. {ECO:0000250|UniProtKB:O15355}.
CHAIN 2 542 Protein phosphatase 1G.
/FTId=PRO_0000057751.
DOMAIN 26 502 PPM-type phosphatase.
{ECO:0000255|PROSITE-ProRule:PRU01082}.
COMPBIAS 258 319 Glu-rich. {ECO:0000255|PROSITE-
ProRule:PRU00007}.
METAL 60 60 Manganese 1. {ECO:0000250}.
METAL 60 60 Manganese 2. {ECO:0000250}.
METAL 61 61 Manganese 1; via carbonyl oxygen.
{ECO:0000250}.
METAL 438 438 Manganese 2. {ECO:0000250}.
METAL 493 493 Manganese 2. {ECO:0000250}.
MOD_RES 22 22 Omega-N-methylarginine.
{ECO:0000250|UniProtKB:O15355}.
MOD_RES 122 122 Phosphothreonine.
{ECO:0000250|UniProtKB:O15355}.
MOD_RES 380 380 N6-acetyllysine.
{ECO:0000244|PubMed:23806337}.
MOD_RES 524 524 Phosphoserine.
{ECO:0000244|PubMed:21183079}.
LIPID 2 2 N-myristoyl glycine.
{ECO:0000250|UniProtKB:O15355}.
CONFLICT 123 126 EDED -> NSAR (in Ref. 3). {ECO:0000305}.
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


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