PPM1B_HUMAN
ID PPM1B_HUMAN Reviewed; 479 AA.
AC O75688; Q461Q2; Q4J6C1; Q4J6C2; Q658R4; Q96ER6; Q9HAY8;
DT 01-DEC-2000, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1998, sequence version 1.
DT 03-AUG-2022, entry version 211.
DE RecName: Full=Protein phosphatase 1B;
DE EC=3.1.3.16;
DE AltName: Full=Protein phosphatase 2C isoform beta;
DE Short=PP2C-beta;
GN Name=PPM1B; Synonyms=PP2CB;
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] (ISOFORM BETA-1).
RC TISSUE=Liver;
RX PubMed=9684878; DOI=10.1016/s0014-5793(98)00708-x;
RA Marely A.E., Kline A., Crabtree G., Sullivan J.E., Beri R.K.;
RT "The cloning expression and tissue distribution of human PP2Cbeta.";
RL FEBS Lett. 431:121-124(1998).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM BETA-2).
RX PubMed=10934208; DOI=10.1074/jbc.m006210200;
RA Cheng A., Kaldis P., Solomon M.J.;
RT "Dephosphorylation of human cyclin-dependent kinases by protein phosphatase
RT type 2Calpha and beta2 isoforms.";
RL J. Biol. Chem. 275:34744-34749(2000).
RN [3]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS BETA-1 AND BETA-2).
RA Seroussi E., Shani N., Hayut A., Faier S., Ben-Meir D., Divinski I.,
RA Smorodinsky N.I., Lavi S.;
RT "Protein phosphatase 1B. Cloning and characterization of two major
RT transcripts generated by alternative use of 3' exons.";
RL Submitted (FEB-2000) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS BETA-2; 4 AND 5).
RX PubMed=15913950; DOI=10.1016/j.ygeno.2005.04.001;
RA Parvari R., Gonen Y., Alshafee I., Buriakovsky S., Regev K.,
RA Hershkovitz E.;
RT "The 2p21 deletion syndrome: characterization of the transcription
RT content.";
RL Genomics 86:195-211(2005).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM BETA-2).
RC TISSUE=Adrenal gland;
RX PubMed=10931946; DOI=10.1073/pnas.160270997;
RA Hu R.-M., Han Z.-G., Song H.-D., Peng Y.-D., Huang Q.-H., Ren S.-X.,
RA Gu Y.-J., Huang C.-H., Li Y.-B., Jiang C.-L., Fu G., Zhang Q.-H., Gu B.-W.,
RA Dai M., Mao Y.-F., Gao G.-F., Rong R., Ye M., Zhou J., Xu S.-H., Gu J.,
RA Shi J.-X., Jin W.-R., Zhang C.-K., Wu T.-M., Huang G.-Y., Chen Z.,
RA Chen M.-D., Chen J.-L.;
RT "Gene expression profiling in the human hypothalamus-pituitary-adrenal axis
RT and full-length cDNA cloning.";
RL Proc. Natl. Acad. Sci. U.S.A. 97:9543-9548(2000).
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM BETA-1).
RC TISSUE=Stomach;
RX PubMed=17974005; DOI=10.1186/1471-2164-8-399;
RA Bechtel S., Rosenfelder H., Duda A., Schmidt C.P., Ernst U.,
RA Wellenreuther R., Mehrle A., Schuster C., Bahr A., Bloecker H., Heubner D.,
RA Hoerlein A., Michel G., Wedler H., Koehrer K., Ottenwaelder B., Poustka A.,
RA Wiemann S., Schupp I.;
RT "The full-ORF clone resource of the German cDNA consortium.";
RL BMC Genomics 8:399-399(2007).
RN [7]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=15815621; DOI=10.1038/nature03466;
RA Hillier L.W., Graves T.A., Fulton R.S., Fulton L.A., Pepin K.H., Minx P.,
RA Wagner-McPherson C., Layman D., Wylie K., Sekhon M., Becker M.C.,
RA Fewell G.A., Delehaunty K.D., Miner T.L., Nash W.E., Kremitzki C., Oddy L.,
RA Du H., Sun H., Bradshaw-Cordum H., Ali J., Carter J., Cordes M., Harris A.,
RA Isak A., van Brunt A., Nguyen C., Du F., Courtney L., Kalicki J.,
RA Ozersky P., Abbott S., Armstrong J., Belter E.A., Caruso L., Cedroni M.,
RA Cotton M., Davidson T., Desai A., Elliott G., Erb T., Fronick C., Gaige T.,
RA Haakenson W., Haglund K., Holmes A., Harkins R., Kim K., Kruchowski S.S.,
RA Strong C.M., Grewal N., Goyea E., Hou S., Levy A., Martinka S., Mead K.,
RA McLellan M.D., Meyer R., Randall-Maher J., Tomlinson C.,
RA Dauphin-Kohlberg S., Kozlowicz-Reilly A., Shah N., Swearengen-Shahid S.,
RA Snider J., Strong J.T., Thompson J., Yoakum M., Leonard S., Pearman C.,
RA Trani L., Radionenko M., Waligorski J.E., Wang C., Rock S.M.,
RA Tin-Wollam A.-M., Maupin R., Latreille P., Wendl M.C., Yang S.-P., Pohl C.,
RA Wallis J.W., Spieth J., Bieri T.A., Berkowicz N., Nelson J.O., Osborne J.,
RA Ding L., Meyer R., Sabo A., Shotland Y., Sinha P., Wohldmann P.E.,
RA Cook L.L., Hickenbotham M.T., Eldred J., Williams D., Jones T.A., She X.,
RA Ciccarelli F.D., Izaurralde E., Taylor J., Schmutz J., Myers R.M.,
RA Cox D.R., Huang X., McPherson J.D., Mardis E.R., Clifton S.W., Warren W.C.,
RA Chinwalla A.T., Eddy S.R., Marra M.A., Ovcharenko I., Furey T.S.,
RA Miller W., Eichler E.E., Bork P., Suyama M., Torrents D., Waterston R.H.,
RA Wilson R.K.;
RT "Generation and annotation of the DNA sequences of human chromosomes 2 and
RT 4.";
RL Nature 434:724-731(2005).
RN [8]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M.,
RA Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J.,
RA Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S.,
RA Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H.,
RA Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K.,
RA Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D.,
RA Hunkapiller M.W., Myers E.W., Venter J.C.;
RL Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
RN [9]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS BETA-1 AND BETA-X).
RC TISSUE=Brain, and Urinary bladder;
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 [10]
RP ISGYLATION AT LYS-12 AND LYS-142.
RX PubMed=16872604; DOI=10.1016/j.febslet.2006.07.032;
RA Takeuchi T., Kobayashi T., Tamura S., Yokosawa H.;
RT "Negative regulation of protein phosphatase 2Cbeta by ISG15 conjugation.";
RL FEBS Lett. 580:4521-4526(2006).
RN [11]
RP INTERACTION WITH PAK6.
RX PubMed=18642328; DOI=10.1002/pros.20787;
RA Kaur R., Yuan X., Lu M.L., Balk S.P.;
RT "Increased PAK6 expression in prostate cancer and identification of PAK6
RT associated proteins.";
RL Prostate 68:1510-1516(2008).
RN [12]
RP FUNCTION, AND INTERACTION WITH IKBKB.
RX PubMed=18930133; DOI=10.1016/j.cellsig.2008.09.012;
RA Sun W., Yu Y., Dotti G., Shen T., Tan X., Savoldo B., Pass A.K., Chu M.,
RA Zhang D., Lu X., Fu S., Lin X., Yang J.;
RT "PPM1A and PPM1B act as IKKbeta phosphatases to terminate TNFalpha-induced
RT IKKbeta-NF-kappaB activation.";
RL Cell. Signal. 21:95-102(2009).
RN [13]
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 [14]
RP SUBCELLULAR LOCATION.
RX PubMed=22781750; DOI=10.1016/j.cellsig.2012.07.003;
RA Bruce D.L., Macartney T., Yong W., Shou W., Sapkota G.P.;
RT "Protein phosphatase 5 modulates SMAD3 function in the transforming growth
RT factor-beta pathway.";
RL Cell. Signal. 24:1999-2006(2012).
RN [15]
RP FUNCTION.
RX PubMed=22750291; DOI=10.1016/j.cellsig.2012.06.017;
RA Zhao Y., Liang L., Fan Y., Sun S., An L., Shi Z., Cheng J., Jia W., Sun W.,
RA Mori-Akiyama Y., Zhang H., Fu S., Yang J.;
RT "PPM1B negatively regulates antiviral response via dephosphorylating
RT TBK1.";
RL Cell. Signal. 24:2197-2204(2012).
RN [16]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-386, AND IDENTIFICATION BY
RP 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 [17]
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 [18]
RP X-RAY CRYSTALLOGRAPHY (1.82 ANGSTROMS) OF 2-297 IN COMPLEX WITH MAGNESIUM.
RX PubMed=18058037; DOI=10.1007/s10969-007-9036-1;
RA Almo S.C., Bonanno J.B., Sauder J.M., Emtage S., Dilorenzo T.P.,
RA Malashkevich V., Wasserman S.R., Swaminathan S., Eswaramoorthy S.,
RA Agarwal R., Kumaran D., Madegowda M., Ragumani S., Patskovsky Y.,
RA Alvarado J., Ramagopal U.A., Faber-Barata J., Chance M.R., Sali A.,
RA Fiser A., Zhang Z.Y., Lawrence D.S., Burley S.K.;
RT "Structural genomics of protein phosphatases.";
RL J. Struct. Funct. Genomics 8:121-140(2007).
CC -!- FUNCTION: Enzyme with a broad specificity. Dephosphorylates CDK2 and
CC CDK6 in vitro. Dephosphorylates PRKAA1 and PRKAA2. Inhibits TBK1-
CC mediated antiviral signaling by dephosphorylating it at 'Ser-172'.
CC Plays an important role in the termination of TNF-alpha-mediated NF-
CC kappa-B activation through dephosphorylating and inactivating
CC IKBKB/IKKB. {ECO:0000269|PubMed:18930133, ECO:0000269|PubMed:22750291}.
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: Monomer (By similarity). Interacts with PAK6. Interacts with
CC the phosphorylated form of IKBKB/IKKB. {ECO:0000250,
CC ECO:0000269|PubMed:18642328, ECO:0000269|PubMed:18930133}.
CC -!- INTERACTION:
CC O75688; P49407: ARRB1; NbExp=4; IntAct=EBI-1047039, EBI-743313;
CC O75688; P32121: ARRB2; NbExp=4; IntAct=EBI-1047039, EBI-714559;
CC O75688; P05161: ISG15; NbExp=2; IntAct=EBI-1047039, EBI-746466;
CC O75688-3; Q9UI95: MAD2L2; NbExp=3; IntAct=EBI-17715099, EBI-77889;
CC O75688-3; Q01449: MYL7; NbExp=3; IntAct=EBI-17715099, EBI-10222416;
CC -!- SUBCELLULAR LOCATION: Cytoplasm, cytosol {ECO:0000269|PubMed:22781750}.
CC Membrane {ECO:0000250|UniProtKB:P36993}; Lipid-anchor
CC {ECO:0000250|UniProtKB:P36993}. Note=Weakly associates at the membrane
CC and N-myristoylation mediates the membrane localization.
CC {ECO:0000250|UniProtKB:P36993}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=5;
CC Comment=Additional isoforms seem to exist.;
CC Name=Beta-1; Synonyms=Beta-X, PPM1B2;
CC IsoId=O75688-1; Sequence=Displayed;
CC Name=Beta-2; Synonyms=PPM1B1;
CC IsoId=O75688-2; Sequence=VSP_005087, VSP_005088;
CC Name=Beta-X;
CC IsoId=O75688-3; Sequence=VSP_041085;
CC Name=4;
CC IsoId=O75688-4; Sequence=VSP_043643, VSP_043644, VSP_005088;
CC Name=5;
CC IsoId=O75688-5; Sequence=VSP_043641, VSP_043642, VSP_043644,
CC VSP_005088;
CC -!- TISSUE SPECIFICITY: Highly expressed in heart and skeletal muscle.
CC -!- PTM: Isgylation negatively regulates its activity.
CC {ECO:0000269|PubMed:16872604}.
CC -!- PTM: N-myristoylation is essential for the recognition of its
CC substrates for dephosphorylation. {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the PP2C family. {ECO:0000305}.
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DR EMBL; AJ005801; CAA06704.1; -; mRNA.
DR EMBL; AF294792; AAG02232.1; -; mRNA.
DR EMBL; AJ271832; CAC27992.1; -; mRNA.
DR EMBL; AJ271835; CAC27993.1; -; mRNA.
DR EMBL; DQ023508; AAY89639.1; -; mRNA.
DR EMBL; DQ023509; AAY89640.1; -; mRNA.
DR EMBL; DQ023510; AAY89641.1; -; mRNA.
DR EMBL; AF136972; AAG49433.1; -; mRNA.
DR EMBL; AL833035; CAH56319.1; -; mRNA.
DR EMBL; AC013717; AAX88954.1; -; Genomic_DNA.
DR EMBL; AC019129; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH471053; EAX00282.1; -; Genomic_DNA.
DR EMBL; CH471053; EAX00283.1; -; Genomic_DNA.
DR EMBL; BC012002; AAH12002.1; -; mRNA.
DR EMBL; BC064381; AAH64381.1; -; mRNA.
DR CCDS; CCDS1816.1; -. [O75688-2]
DR CCDS; CCDS1817.1; -. [O75688-1]
DR CCDS; CCDS1818.1; -. [O75688-3]
DR CCDS; CCDS46271.1; -. [O75688-4]
DR RefSeq; NP_001028729.1; NM_001033557.2. [O75688-4]
DR RefSeq; NP_002697.1; NM_002706.5. [O75688-1]
DR RefSeq; NP_808907.1; NM_177968.3. [O75688-2]
DR RefSeq; NP_808908.1; NM_177969.3. [O75688-3]
DR PDB; 2P8E; X-ray; 1.82 A; A/B=2-297.
DR PDBsum; 2P8E; -.
DR AlphaFoldDB; O75688; -.
DR SMR; O75688; -.
DR BioGRID; 111490; 174.
DR IntAct; O75688; 78.
DR MINT; O75688; -.
DR STRING; 9606.ENSP00000282412; -.
DR BindingDB; O75688; -.
DR ChEMBL; CHEMBL2845; -.
DR DEPOD; PPM1B; -.
DR iPTMnet; O75688; -.
DR MetOSite; O75688; -.
DR PhosphoSitePlus; O75688; -.
DR BioMuta; PPM1B; -.
DR EPD; O75688; -.
DR jPOST; O75688; -.
DR MassIVE; O75688; -.
DR MaxQB; O75688; -.
DR PaxDb; O75688; -.
DR PeptideAtlas; O75688; -.
DR PRIDE; O75688; -.
DR ProteomicsDB; 50157; -. [O75688-1]
DR ProteomicsDB; 50158; -. [O75688-2]
DR ProteomicsDB; 50159; -. [O75688-3]
DR ProteomicsDB; 50160; -. [O75688-4]
DR ProteomicsDB; 50161; -. [O75688-5]
DR Antibodypedia; 14962; 387 antibodies from 29 providers.
DR DNASU; 5495; -.
DR Ensembl; ENST00000282412.9; ENSP00000282412.4; ENSG00000138032.21. [O75688-1]
DR Ensembl; ENST00000345249.8; ENSP00000326089.4; ENSG00000138032.21. [O75688-3]
DR Ensembl; ENST00000378551.6; ENSP00000367813.2; ENSG00000138032.21. [O75688-2]
DR Ensembl; ENST00000409432.7; ENSP00000387287.3; ENSG00000138032.21. [O75688-4]
DR GeneID; 5495; -.
DR KEGG; hsa:5495; -.
DR MANE-Select; ENST00000282412.9; ENSP00000282412.4; NM_002706.6; NP_002697.1.
DR UCSC; uc002rtt.4; human. [O75688-1]
DR CTD; 5495; -.
DR DisGeNET; 5495; -.
DR GeneCards; PPM1B; -.
DR HGNC; HGNC:9276; PPM1B.
DR HPA; ENSG00000138032; Low tissue specificity.
DR MalaCards; PPM1B; -.
DR MIM; 603770; gene.
DR neXtProt; NX_O75688; -.
DR OpenTargets; ENSG00000138032; -.
DR Orphanet; 163693; 2p21 microdeletion syndrome.
DR PharmGKB; PA33604; -.
DR VEuPathDB; HostDB:ENSG00000138032; -.
DR eggNOG; KOG0697; Eukaryota.
DR GeneTree; ENSGT00940000156070; -.
DR HOGENOM; CLU_121979_0_0_1; -.
DR InParanoid; O75688; -.
DR OMA; KRMAINI; -.
DR OrthoDB; 957254at2759; -.
DR PhylomeDB; O75688; -.
DR TreeFam; TF313590; -.
DR PathwayCommons; O75688; -.
DR Reactome; R-HSA-1169408; ISG15 antiviral mechanism.
DR Reactome; R-HSA-9700645; ALK mutants bind TKIs.
DR Reactome; R-HSA-9725370; Signaling by ALK fusions and activated point mutants.
DR SignaLink; O75688; -.
DR SIGNOR; O75688; -.
DR BioGRID-ORCS; 5495; 8 hits in 1080 CRISPR screens.
DR ChiTaRS; PPM1B; human.
DR EvolutionaryTrace; O75688; -.
DR GeneWiki; PPM1B; -.
DR GenomeRNAi; 5495; -.
DR Pharos; O75688; Tchem.
DR PRO; PR:O75688; -.
DR Proteomes; UP000005640; Chromosome 2.
DR RNAct; O75688; protein.
DR Bgee; ENSG00000138032; Expressed in secondary oocyte and 208 other tissues.
DR ExpressionAtlas; O75688; baseline and differential.
DR Genevisible; O75688; HS.
DR GO; GO:0005829; C:cytosol; IDA:HPA.
DR GO; GO:0016020; C:membrane; ISS:UniProtKB.
DR GO; GO:0005730; C:nucleolus; IDA:HPA.
DR GO; GO:0005634; C:nucleus; IBA:GO_Central.
DR GO; GO:0000287; F:magnesium ion binding; IEA:InterPro.
DR GO; GO:0030145; F:manganese ion binding; IEA:InterPro.
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:0006499; P:N-terminal protein myristoylation; ISS:UniProtKB.
DR GO; GO:0050687; P:negative regulation of defense response to virus; IMP:UniProtKB.
DR GO; GO:0043124; P:negative regulation of I-kappaB kinase/NF-kappaB signaling; IMP:UniProtKB.
DR GO; GO:0032688; P:negative regulation of interferon-beta production; IMP:UniProtKB.
DR GO; GO:1901223; P:negative regulation of NIK/NF-kappaB signaling; IMP:UniProtKB.
DR GO; GO:0035970; P:peptidyl-threonine dephosphorylation; IDA:UniProtKB.
DR GO; GO:0090263; P:positive regulation of canonical Wnt signaling pathway; IBA:GO_Central.
DR GO; GO:0006470; P:protein dephosphorylation; IMP:UniProtKB.
DR CDD; cd00143; PP2Cc; 1.
DR Gene3D; 1.10.10.430; -; 1.
DR Gene3D; 3.60.40.10; -; 1.
DR InterPro; IPR000222; PP2C_BS.
DR InterPro; IPR012911; PP2C_C.
DR InterPro; IPR036580; PP2C_C_sf.
DR InterPro; IPR036457; PPM-type_dom_sf.
DR InterPro; IPR001932; PPM-type_phosphatase_dom.
DR Pfam; PF00481; PP2C; 1.
DR Pfam; PF07830; PP2C_C; 1.
DR SMART; SM00332; PP2Cc; 1.
DR SUPFAM; SSF81601; SSF81601; 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 3D-structure; Alternative splicing; Cytoplasm; Hydrolase; Isopeptide bond;
KW Lipoprotein; Magnesium; Manganese; Membrane; Metal-binding; Myristate;
KW Phosphoprotein; Protein phosphatase; Reference proteome; Ubl conjugation.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000269|PubMed:25255805"
FT CHAIN 2..479
FT /note="Protein phosphatase 1B"
FT /id="PRO_0000057746"
FT DOMAIN 23..295
FT /note="PPM-type phosphatase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01082"
FT REGION 1..20
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 423..479
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..16
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 432..470
FT /note="Polar 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:0000269|PubMed:18058037,
FT ECO:0007744|PDB:2P8E"
FT BINDING 61
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
FT BINDING 243
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="2"
FT /evidence="ECO:0000269|PubMed:18058037,
FT ECO:0007744|PDB:2P8E"
FT BINDING 286
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="2"
FT /evidence="ECO:0000269|PubMed:18058037,
FT ECO:0007744|PDB:2P8E"
FT MOD_RES 386
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:24275569"
FT LIPID 2
FT /note="N-myristoyl glycine"
FT /evidence="ECO:0000269|PubMed:25255805"
FT CROSSLNK 12
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in ISG15)"
FT CROSSLNK 142
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in ISG15)"
FT VAR_SEQ 1..287
FT /note="Missing (in isoform Beta-X)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_041085"
FT VAR_SEQ 322..327
FT /note="EIMEKS -> GKTNAF (in isoform 5)"
FT /evidence="ECO:0000303|PubMed:15913950"
FT /id="VSP_043641"
FT VAR_SEQ 328..380
FT /note="Missing (in isoform 5)"
FT /evidence="ECO:0000303|PubMed:15913950"
FT /id="VSP_043642"
FT VAR_SEQ 379..387
FT /note="ASDEAEESG -> GAGDLEDPW (in isoform Beta-2)"
FT /evidence="ECO:0000303|PubMed:10931946,
FT ECO:0000303|PubMed:10934208, ECO:0000303|PubMed:15913950,
FT ECO:0000303|Ref.3"
FT /id="VSP_005087"
FT VAR_SEQ 379..380
FT /note="AS -> QK (in isoform 4)"
FT /evidence="ECO:0000303|PubMed:15913950"
FT /id="VSP_043643"
FT VAR_SEQ 381..387
FT /note="Missing (in isoform 4 and isoform 5)"
FT /evidence="ECO:0000303|PubMed:15913950"
FT /id="VSP_043644"
FT VAR_SEQ 388..479
FT /note="Missing (in isoform Beta-2, isoform 4 and isoform
FT 5)"
FT /evidence="ECO:0000303|PubMed:10931946,
FT ECO:0000303|PubMed:10934208, ECO:0000303|PubMed:15913950,
FT ECO:0000303|Ref.3"
FT /id="VSP_005088"
FT STRAND 9..19
FT /evidence="ECO:0007829|PDB:2P8E"
FT STRAND 22..31
FT /evidence="ECO:0007829|PDB:2P8E"
FT STRAND 33..35
FT /evidence="ECO:0007829|PDB:2P8E"
FT STRAND 38..46
FT /evidence="ECO:0007829|PDB:2P8E"
FT TURN 47..49
FT /evidence="ECO:0007829|PDB:2P8E"
FT STRAND 50..63
FT /evidence="ECO:0007829|PDB:2P8E"
FT HELIX 66..80
FT /evidence="ECO:0007829|PDB:2P8E"
FT TURN 83..85
FT /evidence="ECO:0007829|PDB:2P8E"
FT HELIX 99..118
FT /evidence="ECO:0007829|PDB:2P8E"
FT TURN 121..123
FT /evidence="ECO:0007829|PDB:2P8E"
FT STRAND 134..139
FT /evidence="ECO:0007829|PDB:2P8E"
FT STRAND 141..151
FT /evidence="ECO:0007829|PDB:2P8E"
FT STRAND 153..158
FT /evidence="ECO:0007829|PDB:2P8E"
FT STRAND 161..165
FT /evidence="ECO:0007829|PDB:2P8E"
FT HELIX 174..182
FT /evidence="ECO:0007829|PDB:2P8E"
FT TURN 193..195
FT /evidence="ECO:0007829|PDB:2P8E"
FT HELIX 205..207
FT /evidence="ECO:0007829|PDB:2P8E"
FT HELIX 215..217
FT /evidence="ECO:0007829|PDB:2P8E"
FT STRAND 218..221
FT /evidence="ECO:0007829|PDB:2P8E"
FT STRAND 225..230
FT /evidence="ECO:0007829|PDB:2P8E"
FT STRAND 235..241
FT /evidence="ECO:0007829|PDB:2P8E"
FT HELIX 243..246
FT /evidence="ECO:0007829|PDB:2P8E"
FT HELIX 251..262
FT /evidence="ECO:0007829|PDB:2P8E"
FT HELIX 268..281
FT /evidence="ECO:0007829|PDB:2P8E"
FT STRAND 288..294
FT /evidence="ECO:0007829|PDB:2P8E"
SQ SEQUENCE 479 AA; 52643 MW; A3A5797AD263DFBD CRC64;
MGAFLDKPKT EKHNAHGAGN GLRYGLSSMQ GWRVEMEDAH TAVVGIPHGL EDWSFFAVYD
GHAGSRVANY CSTHLLEHIT TNEDFRAAGK SGSALELSVE NVKNGIRTGF LKIDEYMRNF
SDLRNGMDRS GSTAVGVMIS PKHIYFINCG DSRAVLYRNG QVCFSTQDHK PCNPREKERI
QNAGGSVMIQ RVNGSLAVSR ALGDYDYKCV DGKGPTEQLV SPEPEVYEIL RAEEDEFIIL
ACDGIWDVMS NEELCEYVKS RLEVSDDLEN VCNWVVDTCL HKGSRDNMSI VLVCFSNAPK
VSDEAVKKDS ELDKHLESRV EEIMEKSGEE GMPDLAHVMR ILSAENIPNL PPGGGLAGKR
NVIEAVYSRL NPHRESDGAS DEAEESGSQG KLVEALRQMR INHRGNYRQL LEEMLTSYRL
AKVEGEESPA EPAATATSSN SDAGNPVTMQ ESHTESESGL AELDSSNEDA GTKMSGEKI
