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 27-MAR-2024, entry version 209. 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; O96017: CHEK2; NbExp=2; IntAct=EBI-725702, EBI-1180783; 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}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- 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; 326. DR CORUM; O15355; -. DR DIP; DIP-29404N; -. DR IntAct; O15355; 104. DR MINT; O15355; -. DR STRING; 9606.ENSP00000342778; -. DR BindingDB; O15355; -. DR ChEMBL; CHEMBL3351199; -. DR DEPOD; PPM1G; -. DR GlyGen; O15355; 2 sites, 1 O-linked glycan (2 sites). DR iPTMnet; O15355; -. DR PhosphoSitePlus; O15355; -. DR SwissPalm; O15355; -. DR BioMuta; PPM1G; -. DR EPD; O15355; -. DR jPOST; O15355; -. DR MassIVE; O15355; -. DR PaxDb; 9606-ENSP00000342778; -. DR PeptideAtlas; O15355; -. DR ProteomicsDB; 48608; -. DR Pumba; O15355; -. DR Antibodypedia; 28474; 449 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 AGR; HGNC:9278; -. 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; RYGQNCI; -. DR OrthoDB; 11028at2759; -. DR PhylomeDB; O15355; -. DR TreeFam; TF354280; -. DR PathwayCommons; O15355; -. DR SignaLink; O15355; -. DR SIGNOR; O15355; -. DR BioGRID-ORCS; 5496; 94 hits in 1185 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 200 other cell types or tissues. DR ExpressionAtlas; O15355; baseline and differential. 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; TAS:ProtInc. DR GO; GO:0051726; P:regulation of cell cycle; TAS:ProtInc. DR CDD; cd00143; PP2Cc; 2. DR Gene3D; 3.60.40.10; PPM-type phosphatase domain; 2. DR InterPro; IPR015655; PP2C. DR InterPro; IPR000222; PP2C_BS. DR InterPro; IPR036457; PPM-type-like_dom_sf. DR InterPro; IPR001932; PPM-type_phosphatase-like_dom. DR PANTHER; PTHR13832:SF876; PROTEIN PHOSPHATASE 1G; 1. DR PANTHER; PTHR13832; PROTEIN PHOSPHATASE 2C; 1. DR Pfam; PF00481; PP2C; 2. DR SMART; SM00332; PP2Cc; 1. DR SUPFAM; SSF81606; PP2C-like; 1. DR PROSITE; PS01032; PPM_1; 1. DR PROSITE; PS51746; PPM_2; 1. DR Genevisible; O15355; HS. 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 //