IPP2_MOUSE
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 03-AUG-2022, entry version 137.
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; 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, Pancreas,
RC 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 PDBsum; 2O8A; -.
DR PDBsum; 2O8G; -.
DR AlphaFoldDB; Q9DCL8; -.
DR SMR; Q9DCL8; -.
DR BioGRID; 211762; 23.
DR ELM; Q9DCL8; -.
DR IntAct; Q9DCL8; 2.
DR STRING; 10090.ENSMUSP00000060118; -.
DR iPTMnet; Q9DCL8; -.
DR PhosphoSitePlus; Q9DCL8; -.
DR EPD; Q9DCL8; -.
DR jPOST; Q9DCL8; -.
DR MaxQB; Q9DCL8; -.
DR PaxDb; Q9DCL8; -.
DR PeptideAtlas; Q9DCL8; -.
DR PRIDE; Q9DCL8; -.
DR ProteomicsDB; 268984; -.
DR DNASU; 66849; -.
DR Ensembl; ENSMUST00000060188; ENSMUSP00000060118; ENSMUSG00000047714.
DR GeneID; 66849; -.
DR KEGG; mmu:66849; -.
DR UCSC; uc007yxd.1; mouse.
DR CTD; 5504; -.
DR MGI; MGI:1914099; Ppp1r2.
DR VEuPathDB; HostDB:ENSMUSG00000047714; -.
DR eggNOG; KOG4041; Eukaryota.
DR GeneTree; ENSGT00390000004757; -.
DR InParanoid; Q9DCL8; -.
DR OMA; NYTEPFN; -.
DR OrthoDB; 1321970at2759; -.
DR PhylomeDB; Q9DCL8; -.
DR TreeFam; TF105536; -.
DR BioGRID-ORCS; 66849; 15 hits in 73 CRISPR screens.
DR ChiTaRS; Ppp1r2; mouse.
DR EvolutionaryTrace; Q9DCL8; -.
DR PRO; PR:Q9DCL8; -.
DR Proteomes; UP000000589; Chromosome 16.
DR RNAct; Q9DCL8; protein.
DR Bgee; ENSMUSG00000047714; Expressed in granulocyte and 251 other tissues.
DR ExpressionAtlas; Q9DCL8; baseline and differential.
DR Genevisible; Q9DCL8; MM.
DR GO; GO:0005737; C:cytoplasm; ISO:MGI.
DR GO; GO:0043197; C:dendritic spine; ISO:MGI.
DR GO; GO:0030426; C:growth cone; ISO:MGI.
DR GO; GO:0019904; F:protein domain specific binding; ISO:MGI.
DR GO; GO:0004864; F:protein phosphatase inhibitor activity; IBA:GO_Central.
DR GO; GO:0005977; P:glycogen metabolic process; IEA:UniProtKB-KW.
DR GO; GO:0032091; P:negative regulation of protein binding; ISO:MGI.
DR GO; GO:0043666; P:regulation of phosphoprotein phosphatase activity; IBA:GO_Central.
DR GO; GO:0009966; P:regulation of signal transduction; IEA:InterPro.
DR DisProt; DP00815; -.
DR InterPro; IPR007062; PPI-2.
DR PANTHER; PTHR12398; PTHR12398; 1.
DR Pfam; PF04979; IPP-2; 1.
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 109..143
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 167..181
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 183..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
