ID   IPP2_MOUSE              Reviewed;         206 AA.
AC   Q9DCL8; Q3UD25; Q8C1A6;
DT   16-AUG-2004, integrated into UniProtKB/Swiss-Prot.
DT   23-JAN-2007, sequence version 3.
DT   02-SEP-2026, entry version 154.
DE   RecName: Full=Protein phosphatase inhibitor 2;
DE            Short=IPP-2;
GN   Name=Ppp1r2;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC   Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=C57BL/6J;
RC   TISSUE=Bone marrow, Eye, Kidney, Olfactory bulb, and Skin;
RX   PubMed=16141072; DOI=10.1126/science.1112014;
RA   Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA   Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA   Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA   Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA   Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA   Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA   Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA   Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA   Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA   Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA   Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA   Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA   Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA   Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA   Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA   Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA   Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA   Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA   Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA   Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA   Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA   Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA   Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA   Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA   van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA   Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA   Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA   Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA   Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA   Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA   Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA   Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA   Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT   "The transcriptional landscape of the mammalian genome.";
RL   Science 309:1559-1563(2005).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=FVB/N; TISSUE=Mammary tumor, and Olfactory epithelium;
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   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   TISSUE=Embryonic brain;
RX   PubMed=15345747; DOI=10.1074/mcp.m400085-mcp200;
RA   Ballif B.A., Villen J., Beausoleil S.A., Schwartz D., Gygi S.P.;
RT   "Phosphoproteomic analysis of the developing mouse brain.";
RL   Mol. Cell. Proteomics 3:1093-1101(2004).
RN   [4]
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   TISSUE=Teratocarcinoma;
RX   PubMed=17622165; DOI=10.1021/pr070122r;
RA   Smith J.C., Duchesne M.A., Tozzi P., Ethier M., Figeys D.;
RT   "A differential phosphoproteomic analysis of retinoic acid-treated P19
RT   cells.";
RL   J. Proteome Res. 6:3174-3186(2007).
RN   [5]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-122 AND SER-123, AND
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   TISSUE=Liver;
RX   PubMed=17242355; DOI=10.1073/pnas.0609836104;
RA   Villen J., Beausoleil S.A., Gerber S.A., Gygi S.P.;
RT   "Large-scale phosphorylation analysis of mouse liver.";
RL   Proc. Natl. Acad. Sci. U.S.A. 104:1488-1493(2007).
RN   [6]
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX   PubMed=19144319; DOI=10.1016/j.immuni.2008.11.006;
RA   Trost M., English L., Lemieux S., Courcelles M., Desjardins M.,
RA   Thibault P.;
RT   "The phagosomal proteome in interferon-gamma-activated macrophages.";
RL   Immunity 30:143-154(2009).
RN   [7]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-122 AND SER-123, AND
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   TISSUE=Embryonic fibroblast;
RX   PubMed=19131326; DOI=10.1074/mcp.m800451-mcp200;
RA   Sweet S.M., Bailey C.M., Cunningham D.L., Heath J.K., Cooper H.J.;
RT   "Large scale localization of protein phosphorylation by use of electron
RT   capture dissociation mass spectrometry.";
RL   Mol. Cell. Proteomics 8:904-912(2009).
RN   [8]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-74; SER-88; SER-90; THR-97;
RP   THR-117; SER-122; SER-123 AND SER-131, AND IDENTIFICATION BY MASS
RP   SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   TISSUE=Brain, Brown adipose tissue, Heart, Kidney, Liver, Lung,
RC   Pancreas, Spleen, and Testis;
RX   PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA   Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA   Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT   "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL   Cell 143:1174-1189(2010).
RN   [9]
RP   X-RAY CRYSTALLOGRAPHY (2.5 ANGSTROMS) IN COMPLEX WITH R.NORVEGICUS PPP1CC.
RX   PubMed=17636256; DOI=10.1074/jbc.m703472200;
RA   Hurley T.D., Yang J., Zhang L., Goodwin K.D., Zou Q., Cortese M.,
RA   Dunker A.K., DePaoli-Roach A.A.;
RT   "Structural basis for regulation of protein phosphatase 1 by inhibitor-2.";
RL   J. Biol. Chem. 282:28874-28883(2007).
CC   -!- FUNCTION: Inhibitor of protein-phosphatase 1. {ECO:0000250}.
CC   -!- SUBUNIT: Heterodimer with PP1. {ECO:0000250}.
CC   -!- PTM: Phosphorylation on Ser-45 by ATM activates PP1 by dissociating the
CC       PP1-PPP1R2 complex. Phosphorylation on Thr-74 by GSK3 activates PP1 by
CC       dissociating the PP1-PPP1R2 complex. {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the protein phosphatase inhibitor 2 family.
CC       {ECO:0000305}.
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DR   EMBL; AK002671; BAB22274.1; -; mRNA.
DR   EMBL; AK028603; BAC26028.1; -; mRNA.
DR   EMBL; AK032462; BAC27882.1; -; mRNA.
DR   EMBL; AK053657; BAC35465.1; -; mRNA.
DR   EMBL; AK150281; BAE29437.1; -; mRNA.
DR   EMBL; BC069885; AAH69885.1; -; mRNA.
DR   EMBL; BC069886; AAH69886.1; -; mRNA.
DR   CCDS; CCDS28104.1; -.
DR   RefSeq; NP_080076.1; NM_025800.3.
DR   PDB; 2O8A; X-ray; 2.61 A; I/J=1-206.
DR   PDB; 2O8G; X-ray; 2.50 A; I/J=1-206.
DR   AlphaFoldDB; Q9DCL8; -.
DR   SMR; Q9DCL8; -.
DR   BioGRID; 211762; 27.
DR   ELM; Q9DCL8; -.
DR   FunCoup; Q9DCL8; 566.
DR   IntAct; Q9DCL8; 2.
DR   STRING; 10090.ENSMUSP00000060118; -.
DR   iPTMnet; Q9DCL8; -.
DR   PhosphoSitePlus; Q9DCL8; -.
DR   jPOST; Q9DCL8; -.
DR   PaxDb; 10090-ENSMUSP00000060118; -.
DR   PeptideAtlas; Q9DCL8; -.
DR   ProteomicsDB; 268984; -.
DR   Pumba; Q9DCL8; -.
DR   DNASU; 66849; -.
DR   Ensembl; ENSMUST00000060188.14; ENSMUSP00000060118.8; ENSMUSG00000047714.15.
DR   GeneID; 66849; -.
DR   KEGG; mmu:66849; -.
DR   UCSC; uc007yxd.1; mouse.
DR   AGR; MGI:1914099; -.
DR   CTD; 5504; -.
DR   MGI; MGI:1914099; Ppp1r2.
DR   VEuPathDB; HostDB:ENSMUSG00000047714; -.
DR   eggNOG; KOG4041; Eukaryota.
DR   GeneTree; ENSGT00390000004757; -.
DR   InParanoid; Q9DCL8; -.
DR   OMA; GHYREWH; -.
DR   OrthoDB; 551302at2759; -.
DR   PhylomeDB; Q9DCL8; -.
DR   BioGRID-ORCS; 66849; 15 hits in 78 CRISPR screens.
DR   EvolutionaryTrace; Q9DCL8; -.
DR   PRO; PR:Q9DCL8; -.
DR   Proteomes; UP000000589; Chromosome 16.
DR   RNAct; Q9DCL8; protein.
DR   Bgee; ENSMUSG00000047714; Expressed in granulocyte and 255 other cell types or tissues.
DR   ExpressionAtlas; Q9DCL8; baseline and differential.
DR   GO; GO:0043197; C:dendritic spine; ISO:GO_Central.
DR   GO; GO:0030426; C:growth cone; ISO:GO_Central.
DR   GO; GO:0140678; F:molecular function inhibitor activity; EXP:DisProt.
DR   GO; GO:0019904; F:protein domain specific binding; ISO:GO_Central.
DR   GO; GO:0004864; F:protein phosphatase inhibitor activity; IEA:InterPro.
DR   GO; GO:0035556; P:intracellular signal transduction; IBA:GO_Central.
DR   GO; GO:0009966; P:regulation of signal transduction; IEA:InterPro.
DR   DisProt; DP00815; -.
DR   Gene3D; 6.10.250.1050; -; 2.
DR   InterPro; IPR007062; PPI-2.
DR   PANTHER; PTHR12398; PROTEIN PHOSPHATASE INHIBITOR; 1.
DR   PANTHER; PTHR12398:SF35; PROTEIN PHOSPHATASE INHIBITOR 2-RELATED; 1.
DR   Pfam; PF04979; IPP-2; 1.
DR   PDBsum; 2O8A; -.
DR   PDBsum; 2O8G; -.
PE   1: Evidence at protein level;
KW   3D-structure; Acetylation; Carbohydrate metabolism; Glycogen metabolism;
KW   Phosphoprotein; Protein phosphatase inhibitor; Reference proteome.
FT   INIT_MET        1
FT                   /note="Removed"
FT                   /evidence="ECO:0000250|UniProtKB:P11845"
FT   CHAIN           2..206
FT                   /note="Protein phosphatase inhibitor 2"
FT                   /id="PRO_0000071482"
FT   REGION          1..36
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          12..17
FT                   /note="Required for binding PPP1CC"
FT   REGION          44..56
FT                   /note="Required for binding the 'RVXF' binding groove of
FT                   PPP1CC"
FT   REGION          75..143
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          148..151
FT                   /note="Required for binding PPP1CC catalytic center,
FT                   displacing metal ions and inhibition of PPP1CC catalytic
FT                   activity"
FT   REGION          164..206
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        81..92
FT                   /note="Acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        111..121
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        122..131
FT                   /note="Acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        132..143
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        168..180
FT                   /note="Acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        186..206
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOD_RES         2
FT                   /note="N-acetylalanine"
FT                   /evidence="ECO:0000250|UniProtKB:P11845"
FT   MOD_RES         45
FT                   /note="Phosphoserine; by ATM"
FT                   /evidence="ECO:0000250|UniProtKB:P41236"
FT   MOD_RES         74
FT                   /note="Phosphothreonine"
FT                   /evidence="ECO:0007744|PubMed:21183079"
FT   MOD_RES         88
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:21183079"
FT   MOD_RES         90
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:21183079"
FT   MOD_RES         97
FT                   /note="Phosphothreonine"
FT                   /evidence="ECO:0007744|PubMed:21183079"
FT   MOD_RES         117
FT                   /note="Phosphothreonine"
FT                   /evidence="ECO:0007744|PubMed:21183079"
FT   MOD_RES         122
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:17242355,
FT                   ECO:0007744|PubMed:19131326, ECO:0007744|PubMed:21183079"
FT   MOD_RES         123
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:17242355,
FT                   ECO:0007744|PubMed:19131326, ECO:0007744|PubMed:21183079"
FT   MOD_RES         131
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:21183079"
FT   CONFLICT        193
FT                   /note="S -> C (in Ref. 1; BAC26028)"
FT                   /evidence="ECO:0000305"
FT   HELIX           50..55
FT                   /evidence="ECO:0007829|PDB:2O8G"
FT   HELIX           132..148
FT                   /evidence="ECO:0007829|PDB:2O8G"
FT   HELIX           151..154
FT                   /evidence="ECO:0007829|PDB:2O8G"
FT   HELIX           155..166
FT                   /evidence="ECO:0007829|PDB:2O8G"
SQ   SEQUENCE   206 AA;  23119 MW;  0AE35744A51A523D CRC64;
     MAASTASHRP IKGILKNKTS AASPPVVPSA EQPRPIVEEE LSKKSQKWDE MNILATYHPA
     DKDYGLMKID EPNTPYHNMI GDDEDAYSDS EGNEVMTPDI LAKKLAAAEG SEPKYRTREQ
     ESSGEEDNDL SPEEREKKRQ FEMKRKLHYN EGLNIKLARQ LISKDLHDDD EDEEMAETAD
     GDSMNVEESS QGSTTSDHLQ HKSQSS
//