Full text data of PPM1B
PPM1B
(PP2CB)
[Confidence: low (only semi-automatic identification from reviews)]
Protein phosphatase 1B; 3.1.3.16 (Protein phosphatase 2C isoform beta; PP2C-beta)
Protein phosphatase 1B; 3.1.3.16 (Protein phosphatase 2C isoform beta; PP2C-beta)
UniProt
O75688
ID PPM1B_HUMAN Reviewed; 479 AA.
AC O75688; Q461Q2; Q4J6C1; Q4J6C2; Q658R4; Q96ER6; Q9HAY8;
DT 01-DEC-2000, integrated into UniProtKB/Swiss-Prot.
read moreDT 01-NOV-1998, sequence version 1.
DT 22-JAN-2014, entry version 144.
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;
OC Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
OC Catarrhini; Hominidae; 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
RT phosphatase 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.,
RA Gu B.-W., Dai M., Mao Y.-F., Gao G.-F., Rong R., Ye M., Zhou J.,
RA Xu S.-H., Gu J., Shi J.-X., Jin W.-R., Zhang C.-K., Wu T.-M.,
RA Huang G.-Y., Chen Z., Chen M.-D., Chen J.-L.;
RT "Gene expression profiling in the human hypothalamus-pituitary-adrenal
RT axis 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.,
RA Heubner D., Hoerlein A., Michel G., Wedler H., Koehrer K.,
RA Ottenwaelder B., Poustka A., 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.,
RA Minx P., Wagner-McPherson C., Layman D., Wylie K., Sekhon M.,
RA Becker M.C., Fewell G.A., Delehaunty K.D., Miner T.L., Nash W.E.,
RA Kremitzki C., Oddy L., Du H., Sun H., Bradshaw-Cordum H., Ali J.,
RA Carter J., Cordes M., Harris A., Isak A., van Brunt A., Nguyen C.,
RA Du F., Courtney L., Kalicki J., Ozersky P., Abbott S., Armstrong J.,
RA Belter E.A., Caruso L., Cedroni M., Cotton M., Davidson T., Desai A.,
RA Elliott G., Erb T., Fronick C., Gaige T., Haakenson W., Haglund K.,
RA Holmes A., Harkins R., Kim K., Kruchowski S.S., Strong C.M.,
RA 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.,
RA Swearengen-Shahid S., Snider J., Strong J.T., Thompson J., Yoakum M.,
RA Leonard S., Pearman C., Trani L., Radionenko M., Waligorski J.E.,
RA Wang C., Rock S.M., Tin-Wollam A.-M., Maupin R., Latreille P.,
RA Wendl M.C., Yang S.-P., Pohl C., Wallis J.W., Spieth J., Bieri T.A.,
RA Berkowicz N., Nelson J.O., Osborne J., Ding L., Meyer R., Sabo A.,
RA Shotland Y., Sinha P., Wohldmann P.E., Cook L.L., Hickenbotham M.T.,
RA Eldred J., Williams D., Jones T.A., She X., Ciccarelli F.D.,
RA Izaurralde E., Taylor J., Schmutz J., Myers R.M., Cox D.R., Huang X.,
RA 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.,
RA Waterston R.H., Wilson R.K.;
RT "Generation and annotation of the DNA sequences of human chromosomes 2
RT and 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.,
RA Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R.,
RA Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V.,
RA Hannenhalli S., Turner R., Yooseph S., Lu F., Nusskern D.R.,
RA Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H.,
RA Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G.,
RA Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W.,
RA 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
RT project: 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
RT 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
RT PAK6 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.,
RA Chu M., Zhang D., Lu X., Fu S., Lin X., Yang J.;
RT "PPM1A and PPM1B act as IKKbeta phosphatases to terminate TNFalpha-
RT induced 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.,
RA Buerckstuemmer T., 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
RT growth factor-? 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.,
RA Sun W., 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 X-RAY CRYSTALLOGRAPHY (1.82 ANGSTROMS) OF 2-297.
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
CC and CDK6 in vitro. Dephosphorylates PRKAA1 and PRKAA2. Inhibits
CC TBK1-mediated antiviral signaling by dephosphorylating it at 'Ser-
CC 172'. Plays an important role in the termination of TNF-alpha-
CC mediated NF-kappa-B activation through dephosphorylating and
CC inactivating IKBKB/IKKB.
CC -!- CATALYTIC ACTIVITY: A phosphoprotein + H(2)O = a protein +
CC phosphate.
CC -!- COFACTOR: Binds 2 magnesium or manganese ions per subunit (By
CC similarity).
CC -!- SUBUNIT: Monomer (By similarity). Interacts with PAK6. Interacts
CC with the phosphorylated form of IKBKB/IKKB.
CC -!- INTERACTION:
CC P49407:ARRB1; NbExp=4; IntAct=EBI-1047039, EBI-743313;
CC P32121:ARRB2; NbExp=3; IntAct=EBI-1047039, EBI-714559;
CC P05161:ISG15; NbExp=2; IntAct=EBI-1047039, EBI-746466;
CC -!- SUBCELLULAR LOCATION: Cytoplasm, cytosol. Membrane (By
CC similarity). Note=Weakly associates at the membrane and N-
CC myristoylation mediates the membrane localization (By similarity).
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 -!- PTM: N-myristoylation is essential for the recognition of its
CC substrates for dephosphorylation (By similarity).
CC -!- SIMILARITY: Belongs to the PP2C family.
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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 RefSeq; NP_001028728.1; NM_001033556.1.
DR RefSeq; NP_001028729.1; NM_001033557.1.
DR RefSeq; NP_002697.1; NM_002706.4.
DR RefSeq; NP_808907.1; NM_177968.2.
DR RefSeq; NP_808908.1; NM_177969.2.
DR UniGene; Hs.416769; -.
DR PDB; 2P8E; X-ray; 1.82 A; A/B=2-297.
DR PDBsum; 2P8E; -.
DR ProteinModelPortal; O75688; -.
DR SMR; O75688; 4-295.
DR IntAct; O75688; 11.
DR MINT; MINT-2841839; -.
DR STRING; 9606.ENSP00000282412; -.
DR BindingDB; O75688; -.
DR ChEMBL; CHEMBL2845; -.
DR PhosphoSite; O75688; -.
DR PaxDb; O75688; -.
DR PRIDE; O75688; -.
DR DNASU; 5495; -.
DR Ensembl; ENST00000282412; ENSP00000282412; ENSG00000138032.
DR Ensembl; ENST00000345249; ENSP00000326089; ENSG00000138032.
DR Ensembl; ENST00000378551; ENSP00000367813; ENSG00000138032.
DR Ensembl; ENST00000409432; ENSP00000387287; ENSG00000138032.
DR Ensembl; ENST00000409895; ENSP00000387341; ENSG00000138032.
DR GeneID; 5495; -.
DR KEGG; hsa:5495; -.
DR UCSC; uc002rtt.3; human.
DR CTD; 5495; -.
DR GeneCards; GC02P044307; -.
DR HGNC; HGNC:9276; PPM1B.
DR HPA; HPA016745; -.
DR MIM; 603770; gene.
DR neXtProt; NX_O75688; -.
DR Orphanet; 163693; 2p21 microdeletion syndrome.
DR PharmGKB; PA33604; -.
DR eggNOG; COG0631; -.
DR HOGENOM; HOG000233895; -.
DR HOVERGEN; HBG053647; -.
DR InParanoid; O75688; -.
DR KO; K04461; -.
DR OMA; VMISPEH; -.
DR PhylomeDB; O75688; -.
DR Reactome; REACT_6900; Immune System.
DR EvolutionaryTrace; O75688; -.
DR GeneWiki; PPM1B; -.
DR GenomeRNAi; 5495; -.
DR NextBio; 21250; -.
DR PRO; PR:O75688; -.
DR ArrayExpress; O75688; -.
DR Bgee; O75688; -.
DR CleanEx; HS_PPM1B; -.
DR Genevestigator; O75688; -.
DR GO; GO:0005829; C:cytosol; ISS:UniProtKB.
DR GO; GO:0016020; C:membrane; ISS:UniProtKB.
DR GO; GO:0000287; F:magnesium ion binding; IEA:InterPro.
DR GO; GO:0030145; F:manganese ion binding; IEA:InterPro.
DR GO; GO:0004722; F:protein serine/threonine phosphatase activity; IDA:UniProtKB.
DR GO; GO:0019221; P:cytokine-mediated signaling pathway; TAS:Reactome.
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 cascade; IMP:UniProtKB.
DR GO; GO:0032688; P:negative regulation of interferon-beta production; IMP:UniProtKB.
DR GO; GO:0042347; P:negative regulation of NF-kappaB import into nucleus; IMP:UniProtKB.
DR GO; GO:0035970; P:peptidyl-threonine dephosphorylation; IDA:UniProtKB.
DR Gene3D; 1.10.10.430; -; 1.
DR Gene3D; 3.60.40.10; -; 1.
DR InterPro; IPR001932; PP2C-like_dom.
DR InterPro; IPR012911; PP2C_C.
DR InterPro; IPR000222; PP2C_Mn2_Asp60_BS.
DR InterPro; IPR015655; Protein_Pase_2C.
DR PANTHER; PTHR13832; PTHR13832; 1.
DR Pfam; PF00481; PP2C; 1.
DR Pfam; PF07830; PP2C_C; 1.
DR SMART; SM00331; PP2C_SIG; 1.
DR SMART; SM00332; PP2Cc; 1.
DR SUPFAM; SSF81601; SSF81601; 1.
DR SUPFAM; SSF81606; SSF81606; 1.
DR PROSITE; PS01032; PP2C; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Alternative splicing; Complete proteome; Cytoplasm;
KW Hydrolase; Isopeptide bond; Lipoprotein; Magnesium; Manganese;
KW Membrane; Metal-binding; Myristate; Protein phosphatase;
KW Reference proteome; Ubl conjugation.
FT INIT_MET 1 1 Removed (By similarity).
FT CHAIN 2 479 Protein phosphatase 1B.
FT /FTId=PRO_0000057746.
FT METAL 60 60 Manganese 1 (By similarity).
FT METAL 60 60 Manganese 2 (By similarity).
FT METAL 61 61 Manganese 1; via carbonyl oxygen (By
FT similarity).
FT METAL 243 243 Manganese 2 (By similarity).
FT METAL 286 286 Manganese 2 (By similarity).
FT LIPID 2 2 N-myristoyl glycine (By similarity).
FT CROSSLNK 12 12 Glycyl lysine isopeptide (Lys-Gly)
FT (interchain with G-Cter in ISG15).
FT CROSSLNK 142 142 Glycyl lysine isopeptide (Lys-Gly)
FT (interchain with G-Cter in ISG15).
FT VAR_SEQ 1 287 Missing (in isoform Beta-X).
FT /FTId=VSP_041085.
FT VAR_SEQ 322 327 EIMEKS -> GKTNAF (in isoform 5).
FT /FTId=VSP_043641.
FT VAR_SEQ 328 380 Missing (in isoform 5).
FT /FTId=VSP_043642.
FT VAR_SEQ 379 387 ASDEAEESG -> GAGDLEDPW (in isoform Beta-
FT 2).
FT /FTId=VSP_005087.
FT VAR_SEQ 379 380 AS -> QK (in isoform 4).
FT /FTId=VSP_043643.
FT VAR_SEQ 381 387 Missing (in isoform 4 and isoform 5).
FT /FTId=VSP_043644.
FT VAR_SEQ 388 479 Missing (in isoform Beta-2, isoform 4 and
FT isoform 5).
FT /FTId=VSP_005088.
FT STRAND 9 19
FT STRAND 22 31
FT STRAND 33 35
FT STRAND 38 46
FT TURN 47 49
FT STRAND 50 63
FT HELIX 66 80
FT TURN 83 85
FT HELIX 99 118
FT TURN 121 123
FT STRAND 134 139
FT STRAND 141 151
FT STRAND 153 158
FT STRAND 161 165
FT HELIX 174 182
FT TURN 193 195
FT HELIX 205 207
FT HELIX 215 217
FT STRAND 218 221
FT STRAND 225 230
FT STRAND 235 241
FT HELIX 243 246
FT HELIX 251 262
FT HELIX 268 281
FT STRAND 288 294
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
//
ID PPM1B_HUMAN Reviewed; 479 AA.
AC O75688; Q461Q2; Q4J6C1; Q4J6C2; Q658R4; Q96ER6; Q9HAY8;
DT 01-DEC-2000, integrated into UniProtKB/Swiss-Prot.
read moreDT 01-NOV-1998, sequence version 1.
DT 22-JAN-2014, entry version 144.
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;
OC Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
OC Catarrhini; Hominidae; 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
RT phosphatase 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.,
RA Gu B.-W., Dai M., Mao Y.-F., Gao G.-F., Rong R., Ye M., Zhou J.,
RA Xu S.-H., Gu J., Shi J.-X., Jin W.-R., Zhang C.-K., Wu T.-M.,
RA Huang G.-Y., Chen Z., Chen M.-D., Chen J.-L.;
RT "Gene expression profiling in the human hypothalamus-pituitary-adrenal
RT axis 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.,
RA Heubner D., Hoerlein A., Michel G., Wedler H., Koehrer K.,
RA Ottenwaelder B., Poustka A., 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.,
RA Minx P., Wagner-McPherson C., Layman D., Wylie K., Sekhon M.,
RA Becker M.C., Fewell G.A., Delehaunty K.D., Miner T.L., Nash W.E.,
RA Kremitzki C., Oddy L., Du H., Sun H., Bradshaw-Cordum H., Ali J.,
RA Carter J., Cordes M., Harris A., Isak A., van Brunt A., Nguyen C.,
RA Du F., Courtney L., Kalicki J., Ozersky P., Abbott S., Armstrong J.,
RA Belter E.A., Caruso L., Cedroni M., Cotton M., Davidson T., Desai A.,
RA Elliott G., Erb T., Fronick C., Gaige T., Haakenson W., Haglund K.,
RA Holmes A., Harkins R., Kim K., Kruchowski S.S., Strong C.M.,
RA 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.,
RA Swearengen-Shahid S., Snider J., Strong J.T., Thompson J., Yoakum M.,
RA Leonard S., Pearman C., Trani L., Radionenko M., Waligorski J.E.,
RA Wang C., Rock S.M., Tin-Wollam A.-M., Maupin R., Latreille P.,
RA Wendl M.C., Yang S.-P., Pohl C., Wallis J.W., Spieth J., Bieri T.A.,
RA Berkowicz N., Nelson J.O., Osborne J., Ding L., Meyer R., Sabo A.,
RA Shotland Y., Sinha P., Wohldmann P.E., Cook L.L., Hickenbotham M.T.,
RA Eldred J., Williams D., Jones T.A., She X., Ciccarelli F.D.,
RA Izaurralde E., Taylor J., Schmutz J., Myers R.M., Cox D.R., Huang X.,
RA 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.,
RA Waterston R.H., Wilson R.K.;
RT "Generation and annotation of the DNA sequences of human chromosomes 2
RT and 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.,
RA Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R.,
RA Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V.,
RA Hannenhalli S., Turner R., Yooseph S., Lu F., Nusskern D.R.,
RA Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H.,
RA Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G.,
RA Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W.,
RA 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
RT project: 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
RT 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
RT PAK6 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.,
RA Chu M., Zhang D., Lu X., Fu S., Lin X., Yang J.;
RT "PPM1A and PPM1B act as IKKbeta phosphatases to terminate TNFalpha-
RT induced 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.,
RA Buerckstuemmer T., 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
RT growth factor-? 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.,
RA Sun W., 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 X-RAY CRYSTALLOGRAPHY (1.82 ANGSTROMS) OF 2-297.
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
CC and CDK6 in vitro. Dephosphorylates PRKAA1 and PRKAA2. Inhibits
CC TBK1-mediated antiviral signaling by dephosphorylating it at 'Ser-
CC 172'. Plays an important role in the termination of TNF-alpha-
CC mediated NF-kappa-B activation through dephosphorylating and
CC inactivating IKBKB/IKKB.
CC -!- CATALYTIC ACTIVITY: A phosphoprotein + H(2)O = a protein +
CC phosphate.
CC -!- COFACTOR: Binds 2 magnesium or manganese ions per subunit (By
CC similarity).
CC -!- SUBUNIT: Monomer (By similarity). Interacts with PAK6. Interacts
CC with the phosphorylated form of IKBKB/IKKB.
CC -!- INTERACTION:
CC P49407:ARRB1; NbExp=4; IntAct=EBI-1047039, EBI-743313;
CC P32121:ARRB2; NbExp=3; IntAct=EBI-1047039, EBI-714559;
CC P05161:ISG15; NbExp=2; IntAct=EBI-1047039, EBI-746466;
CC -!- SUBCELLULAR LOCATION: Cytoplasm, cytosol. Membrane (By
CC similarity). Note=Weakly associates at the membrane and N-
CC myristoylation mediates the membrane localization (By similarity).
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 -!- PTM: N-myristoylation is essential for the recognition of its
CC substrates for dephosphorylation (By similarity).
CC -!- SIMILARITY: Belongs to the PP2C family.
CC -----------------------------------------------------------------------
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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 RefSeq; NP_001028728.1; NM_001033556.1.
DR RefSeq; NP_001028729.1; NM_001033557.1.
DR RefSeq; NP_002697.1; NM_002706.4.
DR RefSeq; NP_808907.1; NM_177968.2.
DR RefSeq; NP_808908.1; NM_177969.2.
DR UniGene; Hs.416769; -.
DR PDB; 2P8E; X-ray; 1.82 A; A/B=2-297.
DR PDBsum; 2P8E; -.
DR ProteinModelPortal; O75688; -.
DR SMR; O75688; 4-295.
DR IntAct; O75688; 11.
DR MINT; MINT-2841839; -.
DR STRING; 9606.ENSP00000282412; -.
DR BindingDB; O75688; -.
DR ChEMBL; CHEMBL2845; -.
DR PhosphoSite; O75688; -.
DR PaxDb; O75688; -.
DR PRIDE; O75688; -.
DR DNASU; 5495; -.
DR Ensembl; ENST00000282412; ENSP00000282412; ENSG00000138032.
DR Ensembl; ENST00000345249; ENSP00000326089; ENSG00000138032.
DR Ensembl; ENST00000378551; ENSP00000367813; ENSG00000138032.
DR Ensembl; ENST00000409432; ENSP00000387287; ENSG00000138032.
DR Ensembl; ENST00000409895; ENSP00000387341; ENSG00000138032.
DR GeneID; 5495; -.
DR KEGG; hsa:5495; -.
DR UCSC; uc002rtt.3; human.
DR CTD; 5495; -.
DR GeneCards; GC02P044307; -.
DR HGNC; HGNC:9276; PPM1B.
DR HPA; HPA016745; -.
DR MIM; 603770; gene.
DR neXtProt; NX_O75688; -.
DR Orphanet; 163693; 2p21 microdeletion syndrome.
DR PharmGKB; PA33604; -.
DR eggNOG; COG0631; -.
DR HOGENOM; HOG000233895; -.
DR HOVERGEN; HBG053647; -.
DR InParanoid; O75688; -.
DR KO; K04461; -.
DR OMA; VMISPEH; -.
DR PhylomeDB; O75688; -.
DR Reactome; REACT_6900; Immune System.
DR EvolutionaryTrace; O75688; -.
DR GeneWiki; PPM1B; -.
DR GenomeRNAi; 5495; -.
DR NextBio; 21250; -.
DR PRO; PR:O75688; -.
DR ArrayExpress; O75688; -.
DR Bgee; O75688; -.
DR CleanEx; HS_PPM1B; -.
DR Genevestigator; O75688; -.
DR GO; GO:0005829; C:cytosol; ISS:UniProtKB.
DR GO; GO:0016020; C:membrane; ISS:UniProtKB.
DR GO; GO:0000287; F:magnesium ion binding; IEA:InterPro.
DR GO; GO:0030145; F:manganese ion binding; IEA:InterPro.
DR GO; GO:0004722; F:protein serine/threonine phosphatase activity; IDA:UniProtKB.
DR GO; GO:0019221; P:cytokine-mediated signaling pathway; TAS:Reactome.
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 cascade; IMP:UniProtKB.
DR GO; GO:0032688; P:negative regulation of interferon-beta production; IMP:UniProtKB.
DR GO; GO:0042347; P:negative regulation of NF-kappaB import into nucleus; IMP:UniProtKB.
DR GO; GO:0035970; P:peptidyl-threonine dephosphorylation; IDA:UniProtKB.
DR Gene3D; 1.10.10.430; -; 1.
DR Gene3D; 3.60.40.10; -; 1.
DR InterPro; IPR001932; PP2C-like_dom.
DR InterPro; IPR012911; PP2C_C.
DR InterPro; IPR000222; PP2C_Mn2_Asp60_BS.
DR InterPro; IPR015655; Protein_Pase_2C.
DR PANTHER; PTHR13832; PTHR13832; 1.
DR Pfam; PF00481; PP2C; 1.
DR Pfam; PF07830; PP2C_C; 1.
DR SMART; SM00331; PP2C_SIG; 1.
DR SMART; SM00332; PP2Cc; 1.
DR SUPFAM; SSF81601; SSF81601; 1.
DR SUPFAM; SSF81606; SSF81606; 1.
DR PROSITE; PS01032; PP2C; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Alternative splicing; Complete proteome; Cytoplasm;
KW Hydrolase; Isopeptide bond; Lipoprotein; Magnesium; Manganese;
KW Membrane; Metal-binding; Myristate; Protein phosphatase;
KW Reference proteome; Ubl conjugation.
FT INIT_MET 1 1 Removed (By similarity).
FT CHAIN 2 479 Protein phosphatase 1B.
FT /FTId=PRO_0000057746.
FT METAL 60 60 Manganese 1 (By similarity).
FT METAL 60 60 Manganese 2 (By similarity).
FT METAL 61 61 Manganese 1; via carbonyl oxygen (By
FT similarity).
FT METAL 243 243 Manganese 2 (By similarity).
FT METAL 286 286 Manganese 2 (By similarity).
FT LIPID 2 2 N-myristoyl glycine (By similarity).
FT CROSSLNK 12 12 Glycyl lysine isopeptide (Lys-Gly)
FT (interchain with G-Cter in ISG15).
FT CROSSLNK 142 142 Glycyl lysine isopeptide (Lys-Gly)
FT (interchain with G-Cter in ISG15).
FT VAR_SEQ 1 287 Missing (in isoform Beta-X).
FT /FTId=VSP_041085.
FT VAR_SEQ 322 327 EIMEKS -> GKTNAF (in isoform 5).
FT /FTId=VSP_043641.
FT VAR_SEQ 328 380 Missing (in isoform 5).
FT /FTId=VSP_043642.
FT VAR_SEQ 379 387 ASDEAEESG -> GAGDLEDPW (in isoform Beta-
FT 2).
FT /FTId=VSP_005087.
FT VAR_SEQ 379 380 AS -> QK (in isoform 4).
FT /FTId=VSP_043643.
FT VAR_SEQ 381 387 Missing (in isoform 4 and isoform 5).
FT /FTId=VSP_043644.
FT VAR_SEQ 388 479 Missing (in isoform Beta-2, isoform 4 and
FT isoform 5).
FT /FTId=VSP_005088.
FT STRAND 9 19
FT STRAND 22 31
FT STRAND 33 35
FT STRAND 38 46
FT TURN 47 49
FT STRAND 50 63
FT HELIX 66 80
FT TURN 83 85
FT HELIX 99 118
FT TURN 121 123
FT STRAND 134 139
FT STRAND 141 151
FT STRAND 153 158
FT STRAND 161 165
FT HELIX 174 182
FT TURN 193 195
FT HELIX 205 207
FT HELIX 215 217
FT STRAND 218 221
FT STRAND 225 230
FT STRAND 235 241
FT HELIX 243 246
FT HELIX 251 262
FT HELIX 268 281
FT STRAND 288 294
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
//
MIM
603770
*RECORD*
*FIELD* NO
603770
*FIELD* TI
*603770 PROTEIN PHOSPHATASE, MAGNESIUM-DEPENDENT, 1B; PPM1B
;;PROTEIN PHOSPHATASE, MAGNESIUM-DEPENDENT, 1, BETA ISOFORM;;
read morePROTEIN PHOSPHATASE 2C, BETA ISOFORM, FORMERLY; PP2CB, FORMERLY
*FIELD* TX
CLONING
Protein phosphorylation/dephosphorylation is a major mechanism for
regulating cellular functions. PP2C, 1 of 4 major groups of
serine/threonine phosphatases in eukaryotic cells, is distinguished from
the other groups by its absolute requirement for magnesium or manganese
and its insensitivity to the tumor promoter okadaic acid. Marley et al.
(1998) cloned human liver cDNAs encoding a novel PP2C-beta isoform,
which they named PP2C-beta-X. The deduced 479-amino acid protein shows
high sequence similarity to other mammalian PP2C-beta isoforms but has
an extended and unique C-terminal portion. Recombinant PP2C-beta-X
expressed in bacteria is indistinguishable from recombinant human
PP2C-alpha (PPM1A; 606108) in its cation dependence and its
insensitivity to okadaic acid. By Northern blot analysis, the authors
demonstrated that both PP2C-beta-X and PP2C-alpha are widely expressed,
with the most abundant expression detected in heart and skeletal muscle.
Parvari et al. (2001) identified PPM1B as one of the genes affected by a
homozygous deletion of 179 kb on chromosome 2, which results in the 2p21
deletion syndrome (606407). By EST database analysis, Parvari et al.
(2005) identified 7 PPM1B splice variants, some of which differ only in
noncoding regions. The longest deduced protein contains 479 amino acids,
and its N-terminal half has a phosphatase catalytic domain. RT-PCR
showed that expression of each variant was tissue specific.
GENE STRUCTURE
Parvari et al. (2005) determined that the PPM1B gene contains 6 exons,
the first of which is noncoding.
MAPPING
By genomic sequence analysis, Parvari et al. (2001) mapped the PPM1B
gene to chromosome 2p16. Parvari et al. (2005) refined the mapping to
chromosome 2p21.
MOLECULAR GENETICS
Parvari et al. (2001, 2005) identified PPM1B as one of the genes deleted
in the homozygous 2p21 deletion syndrome (606407).
NOMENCLATURE
The symbol PP2CB, formerly used for PPM1B, now refers to a gene that
maps to chromosome 8p21 (see 176916).
*FIELD* RF
1. Marley, A. E.; Kline, A.; Crabtree, G.; Sullivan, J. E.; Beri,
R. K.: The cloning expression and tissue distribution of human PP2C-beta. FEBS
Lett. 431: 121-124, 1998.
2. Parvari, R.; Brodyansky, I.; Elpeleg, O.; Moses, S.; Landau, D.;
Hershkovitz, E.: A recessive contiguous gene deletion of chromosome
2p16 associated with cystinuria and a mitochondrial disease. Am.
J. Hum. Genet. 69: 869-875, 2001.
3. Parvari, R.; Gonen, Y.; Alshafee, I.; Buriakovsky, S.; Regev, K.;
Hershkovitz, E.: The 2p21 deletion syndrome: characterization of
the transcription content. Genomics 86: 195-211, 2005.
*FIELD* CN
Patricia A. Hartz - updated: 8/30/2005
Victor A. McKusick - updated: 11/5/2001
Carol A. Bocchini - updated: 10/19/2001
*FIELD* CD
Sheryl A. Jankowski: 4/23/1999
*FIELD* ED
mgross: 06/12/2006
mgross: 3/15/2006
mgross: 8/30/2005
carol: 11/15/2001
terry: 11/5/2001
carol: 10/24/2001
carol: 10/19/2001
mgross: 7/13/2001
psherman: 6/30/2000
psherman: 4/23/1999
*RECORD*
*FIELD* NO
603770
*FIELD* TI
*603770 PROTEIN PHOSPHATASE, MAGNESIUM-DEPENDENT, 1B; PPM1B
;;PROTEIN PHOSPHATASE, MAGNESIUM-DEPENDENT, 1, BETA ISOFORM;;
read morePROTEIN PHOSPHATASE 2C, BETA ISOFORM, FORMERLY; PP2CB, FORMERLY
*FIELD* TX
CLONING
Protein phosphorylation/dephosphorylation is a major mechanism for
regulating cellular functions. PP2C, 1 of 4 major groups of
serine/threonine phosphatases in eukaryotic cells, is distinguished from
the other groups by its absolute requirement for magnesium or manganese
and its insensitivity to the tumor promoter okadaic acid. Marley et al.
(1998) cloned human liver cDNAs encoding a novel PP2C-beta isoform,
which they named PP2C-beta-X. The deduced 479-amino acid protein shows
high sequence similarity to other mammalian PP2C-beta isoforms but has
an extended and unique C-terminal portion. Recombinant PP2C-beta-X
expressed in bacteria is indistinguishable from recombinant human
PP2C-alpha (PPM1A; 606108) in its cation dependence and its
insensitivity to okadaic acid. By Northern blot analysis, the authors
demonstrated that both PP2C-beta-X and PP2C-alpha are widely expressed,
with the most abundant expression detected in heart and skeletal muscle.
Parvari et al. (2001) identified PPM1B as one of the genes affected by a
homozygous deletion of 179 kb on chromosome 2, which results in the 2p21
deletion syndrome (606407). By EST database analysis, Parvari et al.
(2005) identified 7 PPM1B splice variants, some of which differ only in
noncoding regions. The longest deduced protein contains 479 amino acids,
and its N-terminal half has a phosphatase catalytic domain. RT-PCR
showed that expression of each variant was tissue specific.
GENE STRUCTURE
Parvari et al. (2005) determined that the PPM1B gene contains 6 exons,
the first of which is noncoding.
MAPPING
By genomic sequence analysis, Parvari et al. (2001) mapped the PPM1B
gene to chromosome 2p16. Parvari et al. (2005) refined the mapping to
chromosome 2p21.
MOLECULAR GENETICS
Parvari et al. (2001, 2005) identified PPM1B as one of the genes deleted
in the homozygous 2p21 deletion syndrome (606407).
NOMENCLATURE
The symbol PP2CB, formerly used for PPM1B, now refers to a gene that
maps to chromosome 8p21 (see 176916).
*FIELD* RF
1. Marley, A. E.; Kline, A.; Crabtree, G.; Sullivan, J. E.; Beri,
R. K.: The cloning expression and tissue distribution of human PP2C-beta. FEBS
Lett. 431: 121-124, 1998.
2. Parvari, R.; Brodyansky, I.; Elpeleg, O.; Moses, S.; Landau, D.;
Hershkovitz, E.: A recessive contiguous gene deletion of chromosome
2p16 associated with cystinuria and a mitochondrial disease. Am.
J. Hum. Genet. 69: 869-875, 2001.
3. Parvari, R.; Gonen, Y.; Alshafee, I.; Buriakovsky, S.; Regev, K.;
Hershkovitz, E.: The 2p21 deletion syndrome: characterization of
the transcription content. Genomics 86: 195-211, 2005.
*FIELD* CN
Patricia A. Hartz - updated: 8/30/2005
Victor A. McKusick - updated: 11/5/2001
Carol A. Bocchini - updated: 10/19/2001
*FIELD* CD
Sheryl A. Jankowski: 4/23/1999
*FIELD* ED
mgross: 06/12/2006
mgross: 3/15/2006
mgross: 8/30/2005
carol: 11/15/2001
terry: 11/5/2001
carol: 10/24/2001
carol: 10/19/2001
mgross: 7/13/2001
psherman: 6/30/2000
psherman: 4/23/1999