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 29-MAY-2013, entry version 138.
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 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 [11]
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 [12]
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.
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.
CC -!- INTERACTION:
CC P49407:ARRB1; NbExp=4; IntAct=EBI-1047039, EBI-743313;
CC P32121:ARRB2; NbExp=3; IntAct=EBI-1047039, EBI-714559;
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 -!- 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 IPI; IPI00026612; -.
DR IPI; IPI00219537; -.
DR IPI; IPI00651725; -.
DR IPI; IPI00743802; -.
DR IPI; IPI00917979; -.
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 IntAct; O75688; 7.
DR MINT; MINT-2841839; -.
DR STRING; 9606.ENSP00000282412; -.
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; uc002rts.3; human.
DR UCSC; uc002rtt.3; human.
DR UCSC; uc002rtu.3; human.
DR UCSC; uc002rtv.3; human.
DR UCSC; uc002rtw.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 BindingDB; O75688; -.
DR ChEMBL; CHEMBL2845; -.
DR EvolutionaryTrace; O75688; -.
DR GenomeRNAi; 5495; -.
DR NextBio; 21250; -.
DR ArrayExpress; O75688; -.
DR Bgee; O75688; -.
DR CleanEx; HS_PPM1B; -.
DR Genevestigator; O75688; -.
DR GermOnline; ENSG00000138032; Homo sapiens.
DR GO; GO:0005829; C:cytosol; TAS:Reactome.
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: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.
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; SSF81606; PP2C-related; 1.
DR SUPFAM; SSF81601; PP2C_C; 1.
DR PROSITE; PS01032; PP2C; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Alternative splicing; Complete proteome; Hydrolase;
KW Magnesium; Manganese; Metal-binding; Protein phosphatase;
KW Reference proteome.
FT CHAIN 1 479 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 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
//
