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Protein phosphatase 1G (EC 3.1.3.16) (Protein phosphatase 1C) (Protein phosphatase 2C isoform gamma) (PP2C-gamma) (Protein phosphatase magnesium-dependent 1 gamma)

 PPM1G_HUMAN             Reviewed;         546 AA.
O15355;
15-JUL-1998, integrated into UniProtKB/Swiss-Prot.
01-JAN-1998, sequence version 1.
18-JUL-2018, entry version 177.
RecName: Full=Protein phosphatase 1G;
EC=3.1.3.16;
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=PPM1C;
Homo sapiens (Human).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
Catarrhini; Hominidae; Homo.
NCBI_TaxID=9606;
[1]
NUCLEOTIDE SEQUENCE [MRNA].
TISSUE=Skeletal muscle;
PubMed=9276438; DOI=10.1016/S0014-5793(97)00837-5;
Travis S.M., Welsh M.J.;
"PP2C gamma: a human protein phosphatase with a unique acidic
domain.";
FEBS Lett. 412:415-419(1997).
[2]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
TISSUE=Placenta, and Skin;
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]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-183, AND IDENTIFICATION
BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Embryonic kidney;
PubMed=17525332; DOI=10.1126/science.1140321;
Matsuoka S., Ballif B.A., Smogorzewska A., McDonald E.R. III,
Hurov K.E., Luo J., Bakalarski C.E., Zhao Z., Solimini N.,
Lerenthal Y., Shiloh Y., Gygi S.P., Elledge S.J.;
"ATM and ATR substrate analysis reveals extensive protein networks
responsive to DNA damage.";
Science 316:1160-1166(2007).
[4]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Cervix carcinoma;
PubMed=18669648; DOI=10.1073/pnas.0805139105;
Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,
Elledge S.J., Gygi S.P.;
"A quantitative atlas of mitotic phosphorylation.";
Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008).
[5]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Leukemic T-cell;
PubMed=19690332; DOI=10.1126/scisignal.2000007;
Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K.,
Rodionov V., Han D.K.;
"Quantitative phosphoproteomic analysis of T cell receptor signaling
reveals system-wide modulation of protein-protein interactions.";
Sci. Signal. 2:RA46-RA46(2009).
[6]
ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-383, AND IDENTIFICATION BY
MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=19608861; DOI=10.1126/science.1175371;
Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M.,
Walther T.C., Olsen J.V., Mann M.;
"Lysine acetylation targets protein complexes and co-regulates major
cellular functions.";
Science 325:834-840(2009).
[7]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Cervix carcinoma;
PubMed=20068231; DOI=10.1126/scisignal.2000475;
Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L.,
Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S.,
Mann M.;
"Quantitative phosphoproteomics reveals widespread full
phosphorylation site occupancy during mitosis.";
Sci. Signal. 3:RA3-RA3(2010).
[8]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=21269460; DOI=10.1186/1752-0509-5-17;
Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P.,
Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.;
"Initial characterization of the human central proteome.";
BMC Syst. Biol. 5:17-17(2011).
[9]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-527, AND IDENTIFICATION
BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=21406692; DOI=10.1126/scisignal.2001570;
Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J.,
Johansen P.T., Kratchmarova I., Kassem M., Mann M., Olsen J.V.,
Blagoev B.;
"System-wide temporal characterization of the proteome and
phosphoproteome of human embryonic stem cell differentiation.";
Sci. Signal. 4:RS3-RS3(2011).
[10]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-122; SER-183 AND
SER-527, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE
ANALYSIS].
TISSUE=Cervix carcinoma, and Erythroleukemia;
PubMed=23186163; DOI=10.1021/pr300630k;
Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J.,
Mohammed S.;
"Toward a comprehensive characterization of a human cancer cell
phosphoproteome.";
J. Proteome Res. 12:260-271(2013).
[11]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Liver;
PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014;
Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D.,
Wang L., Ye M., Zou H.;
"An enzyme assisted RP-RPLC approach for in-depth analysis of human
liver phosphoproteome.";
J. Proteomics 96:253-262(2014).
[12]
METHYLATION [LARGE SCALE ANALYSIS] AT ARG-22, AND IDENTIFICATION BY
MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Colon carcinoma;
PubMed=24129315; DOI=10.1074/mcp.O113.027870;
Guo A., Gu H., Zhou J., Mulhern D., Wang Y., Lee K.A., Yang V.,
Aguiar M., Kornhauser J., Jia X., Ren J., Beausoleil S.A., Silva J.C.,
Vemulapalli V., Bedford M.T., Comb M.J.;
"Immunoaffinity enrichment and mass spectrometry analysis of protein
methylation.";
Mol. Cell. Proteomics 13:372-387(2014).
[13]
MYRISTOYLATION AT GLY-2, CLEAVAGE OF INITIATOR METHIONINE, AND
IDENTIFICATION BY MASS SPECTROMETRY.
PubMed=25255805; DOI=10.1038/ncomms5919;
Thinon E., Serwa R.A., Broncel M., Brannigan J.A., Brassat U.,
Wright M.H., Heal W.P., Wilkinson A.J., Mann D.J., Tate E.W.;
"Global profiling of co- and post-translationally N-myristoylated
proteomes in human cells.";
Nat. Commun. 5:4919-4919(2014).
[14]
MYRISTOYLATION AT GLY-2, CLEAVAGE OF INITIATOR METHIONINE, AND
IDENTIFICATION BY MASS SPECTROMETRY.
PubMed=25807930; DOI=10.1002/anie.201500342;
Broncel M., Serwa R.A., Ciepla P., Krause E., Dallman M.J.,
Magee A.I., Tate E.W.;
"Multifunctional reagents for quantitative proteome-wide analysis of
protein modification in human cells and dynamic profiling of protein
lipidation during vertebrate development.";
Angew. Chem. Int. Ed. 54:5948-5951(2015).
-!- 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}.
-!- INTERACTION:
P04608:tat (xeno); NbExp=3; IntAct=EBI-725702, EBI-6164389;
P54274:TERF1; NbExp=2; IntAct=EBI-725702, EBI-710997;
P13010:XRCC5; NbExp=3; IntAct=EBI-725702, EBI-357997;
P12956:XRCC6; NbExp=3; IntAct=EBI-725702, EBI-353208;
P67809:YBX1; NbExp=2; IntAct=EBI-725702, EBI-354065;
-!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000305}. Membrane
{ECO:0000305}; Lipid-anchor {ECO:0000305}.
-!- TISSUE SPECIFICITY: Widely expressed. Most abundant in testis,
skeletal muscle, and heart.
-!- SIMILARITY: Belongs to the PP2C family. {ECO:0000305}.
-----------------------------------------------------------------------
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EMBL; Y13936; CAA74245.1; -; mRNA.
EMBL; BC022061; AAH22061.1; -; mRNA.
EMBL; BC000057; AAH00057.1; -; mRNA.
CCDS; CCDS1752.1; -.
RefSeq; NP_817092.1; NM_177983.2.
UniGene; Hs.643951; -.
ProteinModelPortal; O15355; -.
SMR; O15355; -.
BioGrid; 111491; 112.
CORUM; O15355; -.
DIP; DIP-29404N; -.
IntAct; O15355; 61.
MINT; O15355; -.
STRING; 9606.ENSP00000264714; -.
BindingDB; O15355; -.
ChEMBL; CHEMBL3351199; -.
DEPOD; O15355; -.
iPTMnet; O15355; -.
PhosphoSitePlus; O15355; -.
SwissPalm; O15355; -.
BioMuta; PPM1G; -.
EPD; O15355; -.
PaxDb; O15355; -.
PeptideAtlas; O15355; -.
PRIDE; O15355; -.
ProteomicsDB; 48608; -.
DNASU; 5496; -.
Ensembl; ENST00000344034; ENSP00000342778; ENSG00000115241.
GeneID; 5496; -.
KEGG; hsa:5496; -.
CTD; 5496; -.
DisGeNET; 5496; -.
EuPathDB; HostDB:ENSG00000115241.10; -.
GeneCards; PPM1G; -.
HGNC; HGNC:9278; PPM1G.
HPA; HPA035530; -.
HPA; HPA035531; -.
MIM; 605119; gene.
neXtProt; NX_O15355; -.
OpenTargets; ENSG00000115241; -.
PharmGKB; PA33606; -.
eggNOG; KOG0699; Eukaryota.
eggNOG; COG0631; LUCA.
GeneTree; ENSGT00920000149079; -.
HOGENOM; HOG000233896; -.
HOVERGEN; HBG053647; -.
InParanoid; O15355; -.
KO; K17499; -.
OMA; GWRNSQE; -.
OrthoDB; EOG091G0D0W; -.
PhylomeDB; O15355; -.
TreeFam; TF354280; -.
SIGNOR; O15355; -.
ChiTaRS; PPM1G; human.
GeneWiki; PPM1G; -.
GenomeRNAi; 5496; -.
PRO; PR:O15355; -.
Proteomes; UP000005640; Chromosome 2.
Bgee; ENSG00000115241; -.
CleanEx; HS_PPM1G; -.
ExpressionAtlas; O15355; baseline and differential.
Genevisible; O15355; HS.
GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
GO; GO:0016020; C:membrane; IEA:UniProtKB-SubCell.
GO; GO:0005654; C:nucleoplasm; IDA:HPA.
GO; GO:0005634; C:nucleus; TAS:ProtInc.
GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
GO; GO:0004722; F:protein serine/threonine phosphatase activity; IDA:UniProtKB.
GO; GO:0007050; P:cell cycle arrest; TAS:ProtInc.
GO; GO:0035970; P:peptidyl-threonine dephosphorylation; IDA:UniProtKB.
GO; GO:0006470; P:protein dephosphorylation; TAS:ProtInc.
CDD; cd00143; PP2Cc; 2.
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; Complete proteome; Cytoplasm; Hydrolase; Lipoprotein;
Magnesium; Manganese; Membrane; Metal-binding; Methylation; Myristate;
Phosphoprotein; Protein phosphatase; Reference proteome; Repeat.
INIT_MET 1 1 Removed. {ECO:0000269|PubMed:25255805,
ECO:0000269|PubMed:25807930}.
CHAIN 2 546 Protein phosphatase 1G.
/FTId=PRO_0000057750.
DOMAIN 26 505 PPM-type phosphatase.
{ECO:0000255|PROSITE-ProRule:PRU01082}.
COMPBIAS 258 322 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 441 441 Manganese 2. {ECO:0000250}.
METAL 496 496 Manganese 2. {ECO:0000250}.
MOD_RES 22 22 Omega-N-methylarginine.
{ECO:0000244|PubMed:24129315}.
MOD_RES 122 122 Phosphothreonine.
{ECO:0000244|PubMed:23186163}.
MOD_RES 183 183 Phosphoserine.
{ECO:0000244|PubMed:17525332,
ECO:0000244|PubMed:23186163}.
MOD_RES 383 383 N6-acetyllysine.
{ECO:0000244|PubMed:19608861}.
MOD_RES 527 527 Phosphoserine.
{ECO:0000244|PubMed:21406692,
ECO:0000244|PubMed:23186163}.
LIPID 2 2 N-myristoyl glycine.
{ECO:0000269|PubMed:25255805,
ECO:0000269|PubMed:25807930}.
SEQUENCE 546 AA; 59272 MW; 084C16F8252330D9 CRC64;
MGAYLSQPNT VKCSGDGVGA PRLPLPYGFS AMQGWRVSME DAHNCIPELD SETAMFSVYD
GHGGEEVALY CAKYLPDIIK DQKAYKEGKL QKALEDAFLA IDAKLTTEEV IKELAQIAGR
PTEDEDEKEK VADEDDVDNE EAALLHEEAT MTIEELLTRY GQNCHKGPPH SKSGGGTGEE
PGSQGLNGEA GPEDSTRETP SQENGPTAKA YTGFSSNSER GTEAGQVGEP GIPTGEAGPS
CSSASDKLPR VAKSKFFEDS EDESDEAEEE EEDSEECSEE EDGYSSEEAE NEEDEDDTEE
AEEDDEEEEE EMMVPGMEGK EEPGSDSGTT AVVALIRGKQ LIVANAGDSR CVVSEAGKAL
DMSYDHKPED EVELARIKNA GGKVTMDGRV NGGLNLSRAI GDHFYKRNKN LPPEEQMISA
LPDIKVLTLT DDHEFMVIAC DGIWNVMSSQ EVVDFIQSKI SQRDENGELR LLSSIVEELL
DQCLAPDTSG DGTGCDNMTC IIICFKPRNT AELQPESGKR KLEEVLSTEG AEENGNSDKK
KKAKRD


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