PPM1G_HUMAN
ID PPM1G_HUMAN Reviewed; 546 AA.
AC O15355;
DT 15-JUL-1998, integrated into UniProtKB/Swiss-Prot.
DT 01-JAN-1998, sequence version 1.
DT 03-AUG-2022, entry version 200.
DE RecName: Full=Protein phosphatase 1G;
DE EC=3.1.3.16;
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=PPM1C;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC TISSUE=Skeletal muscle;
RX PubMed=9276438; DOI=10.1016/s0014-5793(97)00837-5;
RA Travis S.M., Welsh M.J.;
RT "PP2C gamma: a human protein phosphatase with a unique acidic domain.";
RL FEBS Lett. 412:415-419(1997).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Placenta, and Skin;
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 PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-183, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Embryonic kidney;
RX PubMed=17525332; DOI=10.1126/science.1140321;
RA Matsuoka S., Ballif B.A., Smogorzewska A., McDonald E.R. III, Hurov K.E.,
RA Luo J., Bakalarski C.E., Zhao Z., Solimini N., Lerenthal Y., Shiloh Y.,
RA Gygi S.P., Elledge S.J.;
RT "ATM and ATR substrate analysis reveals extensive protein networks
RT responsive to DNA damage.";
RL Science 316:1160-1166(2007).
RN [4]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=18669648; DOI=10.1073/pnas.0805139105;
RA Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,
RA Elledge S.J., Gygi S.P.;
RT "A quantitative atlas of mitotic phosphorylation.";
RL Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008).
RN [5]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Leukemic T-cell;
RX PubMed=19690332; DOI=10.1126/scisignal.2000007;
RA Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K.,
RA Rodionov V., Han D.K.;
RT "Quantitative phosphoproteomic analysis of T cell receptor signaling
RT reveals system-wide modulation of protein-protein interactions.";
RL Sci. Signal. 2:RA46-RA46(2009).
RN [6]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-383, AND IDENTIFICATION BY MASS
RP SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=19608861; DOI=10.1126/science.1175371;
RA Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T.C.,
RA Olsen J.V., Mann M.;
RT "Lysine acetylation targets protein complexes and co-regulates major
RT cellular functions.";
RL Science 325:834-840(2009).
RN [7]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=20068231; DOI=10.1126/scisignal.2000475;
RA Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L.,
RA Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S., Mann M.;
RT "Quantitative phosphoproteomics reveals widespread full phosphorylation
RT site occupancy during mitosis.";
RL Sci. Signal. 3:RA3-RA3(2010).
RN [8]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=21269460; DOI=10.1186/1752-0509-5-17;
RA Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T.,
RA Bennett K.L., Superti-Furga G., Colinge J.;
RT "Initial characterization of the human central proteome.";
RL BMC Syst. Biol. 5:17-17(2011).
RN [9]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-527, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=21406692; DOI=10.1126/scisignal.2001570;
RA Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J., Johansen P.T.,
RA Kratchmarova I., Kassem M., Mann M., Olsen J.V., Blagoev B.;
RT "System-wide temporal characterization of the proteome and phosphoproteome
RT of human embryonic stem cell differentiation.";
RL Sci. Signal. 4:RS3-RS3(2011).
RN [10]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-122; SER-183 AND SER-527, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma, and Erythroleukemia;
RX PubMed=23186163; DOI=10.1021/pr300630k;
RA Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J.,
RA Mohammed S.;
RT "Toward a comprehensive characterization of a human cancer cell
RT phosphoproteome.";
RL J. Proteome Res. 12:260-271(2013).
RN [11]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Liver;
RX PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014;
RA Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., Wang L.,
RA Ye M., Zou H.;
RT "An enzyme assisted RP-RPLC approach for in-depth analysis of human liver
RT phosphoproteome.";
RL J. Proteomics 96:253-262(2014).
RN [12]
RP METHYLATION [LARGE SCALE ANALYSIS] AT ARG-22, AND IDENTIFICATION BY MASS
RP SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Colon carcinoma;
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).
RN [13]
RP MYRISTOYLATION AT GLY-2, CLEAVAGE OF INITIATOR METHIONINE, AND
RP IDENTIFICATION BY MASS SPECTROMETRY.
RX PubMed=25255805; DOI=10.1038/ncomms5919;
RA Thinon E., Serwa R.A., Broncel M., Brannigan J.A., Brassat U., Wright M.H.,
RA Heal W.P., Wilkinson A.J., Mann D.J., Tate E.W.;
RT "Global profiling of co- and post-translationally N-myristoylated proteomes
RT in human cells.";
RL Nat. Commun. 5:4919-4919(2014).
RN [14]
RP MYRISTOYLATION AT GLY-2, CLEAVAGE OF INITIATOR METHIONINE, AND
RP IDENTIFICATION BY MASS SPECTROMETRY.
RX PubMed=25807930; DOI=10.1002/anie.201500342;
RA Broncel M., Serwa R.A., Ciepla P., Krause E., Dallman M.J., Magee A.I.,
RA Tate E.W.;
RT "Multifunctional reagents for quantitative proteome-wide analysis of
RT protein modification in human cells and dynamic profiling of protein
RT lipidation during vertebrate development.";
RL Angew. Chem. Int. Ed. 54:5948-5951(2015).
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 -!- INTERACTION:
CC O15355; P54274: TERF1; NbExp=2; IntAct=EBI-725702, EBI-710997;
CC O15355; P13010: XRCC5; NbExp=3; IntAct=EBI-725702, EBI-357997;
CC O15355; P12956: XRCC6; NbExp=3; IntAct=EBI-725702, EBI-353208;
CC O15355; P67809: YBX1; NbExp=2; IntAct=EBI-725702, EBI-354065;
CC O15355; P04608: tat; Xeno; NbExp=3; IntAct=EBI-725702, EBI-6164389;
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000305}. Membrane {ECO:0000305};
CC Lipid-anchor {ECO:0000305}.
CC -!- TISSUE SPECIFICITY: Widely expressed. Most abundant in testis, skeletal
CC muscle, and heart.
CC -!- SIMILARITY: Belongs to the PP2C family. {ECO:0000305}.
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DR EMBL; Y13936; CAA74245.1; -; mRNA.
DR EMBL; BC022061; AAH22061.1; -; mRNA.
DR EMBL; BC000057; AAH00057.1; -; mRNA.
DR CCDS; CCDS1752.1; -.
DR RefSeq; NP_817092.1; NM_177983.2.
DR AlphaFoldDB; O15355; -.
DR SMR; O15355; -.
DR BioGRID; 111491; 255.
DR CORUM; O15355; -.
DR DIP; DIP-29404N; -.
DR IntAct; O15355; 102.
DR MINT; O15355; -.
DR STRING; 9606.ENSP00000342778; -.
DR BindingDB; O15355; -.
DR ChEMBL; CHEMBL3351199; -.
DR DEPOD; PPM1G; -.
DR GlyGen; O15355; 1 site, 1 O-linked glycan (1 site).
DR iPTMnet; O15355; -.
DR PhosphoSitePlus; O15355; -.
DR SwissPalm; O15355; -.
DR BioMuta; PPM1G; -.
DR EPD; O15355; -.
DR jPOST; O15355; -.
DR MassIVE; O15355; -.
DR PaxDb; O15355; -.
DR PeptideAtlas; O15355; -.
DR PRIDE; O15355; -.
DR ProteomicsDB; 48608; -.
DR Antibodypedia; 28474; 412 antibodies from 31 providers.
DR DNASU; 5496; -.
DR Ensembl; ENST00000344034.5; ENSP00000342778.4; ENSG00000115241.11.
DR GeneID; 5496; -.
DR KEGG; hsa:5496; -.
DR MANE-Select; ENST00000344034.5; ENSP00000342778.4; NM_177983.3; NP_817092.1.
DR CTD; 5496; -.
DR DisGeNET; 5496; -.
DR GeneCards; PPM1G; -.
DR HGNC; HGNC:9278; PPM1G.
DR HPA; ENSG00000115241; Tissue enhanced (testis).
DR MIM; 605119; gene.
DR neXtProt; NX_O15355; -.
DR OpenTargets; ENSG00000115241; -.
DR PharmGKB; PA33606; -.
DR VEuPathDB; HostDB:ENSG00000115241; -.
DR eggNOG; KOG0699; Eukaryota.
DR GeneTree; ENSGT00940000158427; -.
DR HOGENOM; CLU_013173_13_1_1; -.
DR InParanoid; O15355; -.
DR OMA; TPEDEFM; -.
DR OrthoDB; 957254at2759; -.
DR PhylomeDB; O15355; -.
DR TreeFam; TF354280; -.
DR PathwayCommons; O15355; -.
DR SignaLink; O15355; -.
DR SIGNOR; O15355; -.
DR BioGRID-ORCS; 5496; 88 hits in 1091 CRISPR screens.
DR ChiTaRS; PPM1G; human.
DR GeneWiki; PPM1G; -.
DR GenomeRNAi; 5496; -.
DR Pharos; O15355; Tbio.
DR PRO; PR:O15355; -.
DR Proteomes; UP000005640; Chromosome 2.
DR RNAct; O15355; protein.
DR Bgee; ENSG00000115241; Expressed in left testis and 198 other tissues.
DR ExpressionAtlas; O15355; baseline and differential.
DR Genevisible; O15355; HS.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005654; C:nucleoplasm; IDA:HPA.
DR GO; GO:0005634; C:nucleus; TAS:ProtInc.
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:0004722; F:protein serine/threonine phosphatase activity; IDA:UniProtKB.
DR GO; GO:0035970; P:peptidyl-threonine dephosphorylation; IDA:UniProtKB.
DR GO; GO:0006470; P:protein dephosphorylation; IBA:GO_Central.
DR GO; GO:0051726; P:regulation of cell cycle; TAS:ProtInc.
DR CDD; cd00143; PP2Cc; 2.
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; Cytoplasm; Hydrolase; Lipoprotein; Magnesium; Manganese;
KW Membrane; Metal-binding; Methylation; Myristate; Phosphoprotein;
KW Protein phosphatase; Reference proteome; Repeat.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000269|PubMed:25255805,
FT ECO:0000269|PubMed:25807930"
FT CHAIN 2..546
FT /note="Protein phosphatase 1G"
FT /id="PRO_0000057750"
FT DOMAIN 26..505
FT /note="PPM-type phosphatase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01082"
FT REGION 116..139
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 161..328
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 512..546
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 194..223
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 261..315
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 513..540
FT /note="Basic and 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 441
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
FT BINDING 496
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:0007744|PubMed:24129315"
FT MOD_RES 122
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 183
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17525332,
FT ECO:0007744|PubMed:23186163"
FT MOD_RES 383
FT /note="N6-acetyllysine"
FT /evidence="ECO:0007744|PubMed:19608861"
FT MOD_RES 527
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21406692,
FT ECO:0007744|PubMed:23186163"
FT LIPID 2
FT /note="N-myristoyl glycine"
FT /evidence="ECO:0000269|PubMed:25255805,
FT ECO:0000269|PubMed:25807930"
SQ 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
