IPP2_HUMAN
ID IPP2_HUMAN Reviewed; 205 AA.
AC P41236;
DT 01-FEB-1995, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 2.
DT 03-AUG-2022, entry version 193.
DE RecName: Full=Protein phosphatase inhibitor 2;
DE Short=IPP-2;
GN Name=PPP1R2; Synonyms=IPP2;
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].
RX PubMed=7949733; DOI=10.1007/bf00369318;
RA Sanseau P., Jackson A., Alderton R.P., Beck S., Senger G., Sheer D.,
RA Kelly A., Trowsdale J.;
RT "Cloning and characterization of human phosphatase inhibitor-2 (IPP-2)
RT sequences.";
RL Mamm. Genome 5:490-496(1994).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA].
RX PubMed=8119416; DOI=10.1016/0014-5793(94)80179-7;
RA Helps N.R., Street A.J., Elledge S.J., Cohen P.T.W.;
RT "Cloning of the complete coding region for human protein phosphatase
RT inhibitor 2 using the two hybrid system and expression of inhibitor 2 in E.
RT coli.";
RL FEBS Lett. 340:93-98(1994).
RN [3]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=9126490; DOI=10.1006/geno.1997.4649;
RA Permana P.A., Mott D.M.;
RT "Genetic analysis of human type 1 protein phosphatase inhibitor 2 in
RT insulin-resistant Pima Indians.";
RL Genomics 41:110-114(1997).
RN [4]
RP NUCLEOTIDE SEQUENCE [MRNA].
RA Croke D.T., McWilliam P.M., Parle-McDermott A., Dunican D., Tighe O.;
RT "Inhibitor 2 of protein phosphatase 1 is differentially expressed between
RT the colon cancer cell lines SW480 and SW620.";
RL Submitted (APR-1999) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC TISSUE=Heart;
RA Mishra S., Tiwari N., Sabbah H.N., Gupta R.C.;
RT "Cloning of inhibitor-2 of protein phosphatase type 1 from human heart.";
RL Submitted (NOV-2001) to the EMBL/GenBank/DDBJ databases.
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Skin;
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 [7]
RP PROTEIN SEQUENCE OF 2-33.
RC TISSUE=Platelet;
RX PubMed=12665801; DOI=10.1038/nbt810;
RA Gevaert K., Goethals M., Martens L., Van Damme J., Staes A., Thomas G.R.,
RA Vandekerckhove J.;
RT "Exploring proteomes and analyzing protein processing by mass spectrometric
RT identification of sorted N-terminal peptides.";
RL Nat. Biotechnol. 21:566-569(2003).
RN [8]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-92, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=18220336; DOI=10.1021/pr0705441;
RA Cantin G.T., Yi W., Lu B., Park S.K., Xu T., Lee J.-D., Yates J.R. III;
RT "Combining protein-based IMAC, peptide-based IMAC, and MudPIT for efficient
RT phosphoproteomic analysis.";
RL J. Proteome Res. 7:1346-1351(2008).
RN [9]
RP PHOSPHORYLATION AT SER-44, AND SUBUNIT.
RX PubMed=18250156; DOI=10.1128/mcb.01711-07;
RA Tang X., Hui Z.G., Cui X.L., Garg R., Kastan M.B., Xu B.;
RT "A novel ATM-dependent pathway regulates protein phosphatase 1 in response
RT to DNA damage.";
RL Mol. Cell. Biol. 28:2559-2566(2008).
RN [10]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-87 AND THR-89, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=18669648; DOI=10.1073/pnas.0805139105;
RA Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,
RA Elledge S.J., Gygi S.P.;
RT "A quantitative atlas of mitotic phosphorylation.";
RL Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008).
RN [11]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-87, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Leukemic T-cell;
RX PubMed=19690332; DOI=10.1126/scisignal.2000007;
RA Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K.,
RA Rodionov V., Han D.K.;
RT "Quantitative phosphoproteomic analysis of T cell receptor signaling
RT reveals system-wide modulation of protein-protein interactions.";
RL Sci. Signal. 2:RA46-RA46(2009).
RN [12]
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 [13]
RP PHOSPHORYLATION AT SER-121; SER-122 AND SER-127.
RC TISSUE=Testis;
RX PubMed=23506001; DOI=10.1186/1471-2121-14-15;
RA Korrodi-Gregorio L., Ferreira M., Vintem A.P., Wu W., Muller T., Marcus K.,
RA Vijayaraghavan S., Brautigan D.L., da Cruz E Silva O.A., Fardilha M.,
RA da Cruz E Silva E.F.;
RT "Identification and characterization of two distinct PPP1R2 isoforms in
RT human spermatozoa.";
RL BMC Cell Biol. 14:15-15(2013).
RN [14]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma, and Erythroleukemia;
RX PubMed=23186163; DOI=10.1021/pr300630k;
RA Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J.,
RA Mohammed S.;
RT "Toward a comprehensive characterization of a human cancer cell
RT phosphoproteome.";
RL J. Proteome Res. 12:260-271(2013).
CC -!- FUNCTION: Inhibitor of protein-phosphatase 1.
CC -!- SUBUNIT: Heterodimer with PP1. {ECO:0000269|PubMed:18250156}.
CC -!- INTERACTION:
CC P41236; P05067: APP; NbExp=3; IntAct=EBI-1056517, EBI-77613;
CC P41236; Q8IWU2: LMTK2; NbExp=3; IntAct=EBI-1056517, EBI-2008933;
CC P41236; P62136: PPP1CA; NbExp=11; IntAct=EBI-1056517, EBI-357253;
CC P41236; P36873: PPP1CC; NbExp=7; IntAct=EBI-1056517, EBI-356283;
CC P41236; Q9BSI4: TINF2; NbExp=2; IntAct=EBI-1056517, EBI-717399;
CC -!- PTM: Phosphorylation on Thr-73 by GSK3 activates PP1 by dissociating
CC the PP1-PPP1R2 complex (By similarity). Phosphorylation on Ser-44 by
CC ATM activates PP1 by dissociating the PP1-PPP1R2 complex. {ECO:0000250,
CC ECO:0000269|PubMed:18250156, ECO:0000269|PubMed:23506001}.
CC -!- SIMILARITY: Belongs to the protein phosphatase inhibitor 2 family.
CC {ECO:0000305}.
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DR EMBL; X78873; CAA55475.1; -; mRNA.
DR EMBL; Z29646; CAA82754.1; -; mRNA.
DR EMBL; U68111; AAC51206.1; -; Genomic_DNA.
DR EMBL; U68106; AAC51206.1; JOINED; Genomic_DNA.
DR EMBL; U68107; AAC51206.1; JOINED; Genomic_DNA.
DR EMBL; U68108; AAC51206.1; JOINED; Genomic_DNA.
DR EMBL; U68109; AAC51206.1; JOINED; Genomic_DNA.
DR EMBL; U68110; AAC51206.1; JOINED; Genomic_DNA.
DR EMBL; AJ133812; CAB41680.1; -; mRNA.
DR EMBL; AY063767; AAL48322.1; -; mRNA.
DR EMBL; BC007655; AAH07655.1; -; mRNA.
DR CCDS; CCDS3309.1; -.
DR PIR; S42406; S42406.
DR RefSeq; NP_001303254.1; NM_001316325.1.
DR RefSeq; NP_006232.1; NM_006241.7.
DR AlphaFoldDB; P41236; -.
DR BMRB; P41236; -.
DR SMR; P41236; -.
DR BioGRID; 111497; 62.
DR DIP; DIP-781N; -.
DR ELM; P41236; -.
DR IntAct; P41236; 18.
DR MINT; P41236; -.
DR STRING; 9606.ENSP00000484580; -.
DR GlyGen; P41236; 1 site, 1 O-linked glycan (1 site).
DR iPTMnet; P41236; -.
DR MetOSite; P41236; -.
DR PhosphoSitePlus; P41236; -.
DR BioMuta; PPP1R2; -.
DR DMDM; 729856; -.
DR EPD; P41236; -.
DR jPOST; P41236; -.
DR MassIVE; P41236; -.
DR MaxQB; P41236; -.
DR PaxDb; P41236; -.
DR PeptideAtlas; P41236; -.
DR PRIDE; P41236; -.
DR ProteomicsDB; 55448; -.
DR TopDownProteomics; P41236; -.
DR Antibodypedia; 33909; 332 antibodies from 29 providers.
DR DNASU; 5504; -.
DR Ensembl; ENST00000618156.5; ENSP00000484580.1; ENSG00000184203.8.
DR GeneID; 5504; -.
DR KEGG; hsa:5504; -.
DR MANE-Select; ENST00000618156.5; ENSP00000484580.1; NM_006241.8; NP_006232.1.
DR UCSC; uc032sob.2; human.
DR CTD; 5504; -.
DR DisGeNET; 5504; -.
DR GeneCards; PPP1R2; -.
DR HGNC; HGNC:9288; PPP1R2.
DR HPA; ENSG00000184203; Low tissue specificity.
DR MIM; 601792; gene.
DR neXtProt; NX_P41236; -.
DR OpenTargets; ENSG00000184203; -.
DR PharmGKB; PA33641; -.
DR VEuPathDB; HostDB:ENSG00000184203; -.
DR eggNOG; KOG4041; Eukaryota.
DR GeneTree; ENSGT00390000004757; -.
DR InParanoid; P41236; -.
DR OMA; NYTEPFN; -.
DR OrthoDB; 1321970at2759; -.
DR PhylomeDB; P41236; -.
DR TreeFam; TF105536; -.
DR PathwayCommons; P41236; -.
DR SignaLink; P41236; -.
DR SIGNOR; P41236; -.
DR BioGRID-ORCS; 5504; 610 hits in 1053 CRISPR screens.
DR ChiTaRS; PPP1R2; human.
DR GeneWiki; PPP1R2; -.
DR GenomeRNAi; 5504; -.
DR Pharos; P41236; Tbio.
DR PRO; PR:P41236; -.
DR Proteomes; UP000005640; Chromosome 3.
DR RNAct; P41236; protein.
DR Bgee; ENSG00000184203; Expressed in biceps brachii and 202 other tissues.
DR ExpressionAtlas; P41236; baseline and differential.
DR Genevisible; P41236; HS.
DR GO; GO:0004864; F:protein phosphatase inhibitor activity; IBA:GO_Central.
DR GO; GO:0004865; F:protein serine/threonine phosphatase inhibitor activity; TAS:ProtInc.
DR GO; GO:0006091; P:generation of precursor metabolites and energy; TAS:ProtInc.
DR GO; GO:0005977; P:glycogen metabolic process; IEA:UniProtKB-KW.
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; DP00816; -.
DR InterPro; IPR007062; PPI-2.
DR PANTHER; PTHR12398; PTHR12398; 1.
DR Pfam; PF04979; IPP-2; 1.
PE 1: Evidence at protein level;
KW Acetylation; Carbohydrate metabolism; Direct protein sequencing;
KW Glycogen metabolism; Phosphoprotein; Protein phosphatase inhibitor;
KW Reference proteome.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000250|UniProtKB:P11845,
FT ECO:0000269|PubMed:12665801"
FT CHAIN 2..205
FT /note="Protein phosphatase inhibitor 2"
FT /id="PRO_0000071481"
FT REGION 1..44
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 12..17
FT /note="Required for binding PPP1CC"
FT /evidence="ECO:0000250"
FT REGION 43..55
FT /note="Required for binding PPP1CC"
FT /evidence="ECO:0000250"
FT REGION 111..142
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 147..150
FT /note="Required for binding PPP1CC catalytic center,
FT displacing metal ions and inhibition of PPP1CC catalytic
FT activity"
FT /evidence="ECO:0000250"
FT REGION 163..205
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 14..30
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 166..180
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 181..205
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 44
FT /note="Phosphoserine; by ATM"
FT /evidence="ECO:0000269|PubMed:18250156"
FT MOD_RES 73
FT /note="Phosphothreonine; by GSK3"
FT /evidence="ECO:0000250|UniProtKB:P11845"
FT MOD_RES 87
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648,
FT ECO:0007744|PubMed:19690332"
FT MOD_RES 89
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:18669648"
FT MOD_RES 92
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:18220336"
FT MOD_RES 121
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:23506001"
FT MOD_RES 122
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:23506001"
FT MOD_RES 127
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:23506001"
FT MOD_RES 130
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9DCL8"
SQ SEQUENCE 205 AA; 23015 MW; FFC005B07CD5ABFC CRC64;
MAASTASHRP IKGILKNKTS TTSSMVASAE QPRGNVDEEL SKKSQKWDEM NILATYHPAD
KDYGLMKIDE PSTPYHSMMG DDEDACSDTE ATEAMAPDIL ARKLAAAEGL EPKYRIQEQE
SSGEEDSDLS PEEREKKRQF EMKRKLHYNE GLNIKLARQL ISKDLHDDDE DEEMLETADG
ESMNTEESNQ GSTPSDQQQN KLRSS
