IPP2_RAT
ID IPP2_RAT Reviewed; 205 AA.
AC P50411; Q56A32;
DT 01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 2.
DT 03-AUG-2022, entry version 131.
DE RecName: Full=Protein phosphatase inhibitor 2;
DE Short=IPP-2;
GN Name=Ppp1r2; Synonyms=Ipp2;
OS Rattus norvegicus (Rat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Rattus.
OX NCBI_TaxID=10116;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC TISSUE=Brain;
RX PubMed=7669271; DOI=10.1016/0891-0618(95)00051-8;
RA Sakagami H., Kondo H.;
RT "Molecular cloning of the cDNA for rat phosphatase inhibitor-2 and its wide
RT gene expression in the central nervous system.";
RL J. Chem. Neuroanat. 8:259-266(1995).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Brain;
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 PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-121; SER-122 AND SER-130, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=22673903; DOI=10.1038/ncomms1871;
RA Lundby A., Secher A., Lage K., Nordsborg N.B., Dmytriyev A., Lundby C.,
RA Olsen J.V.;
RT "Quantitative maps of protein phosphorylation sites across 14 different rat
RT organs and tissues.";
RL Nat. Commun. 3:876-876(2012).
CC -!- FUNCTION: Inhibitor of protein-phosphatase 1.
CC -!- SUBUNIT: Heterodimer with PP1. {ECO:0000250}.
CC -!- TISSUE SPECIFICITY: Central nervous system.
CC -!- PTM: Phosphorylation on Ser-44 by ATM activates PP1 by dissociating the
CC PP1-PPP1R2 complex. Phosphorylation on Thr-73 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; S79213; AAB35244.1; -; mRNA.
DR EMBL; BC092194; AAH92194.1; -; mRNA.
DR RefSeq; NP_620178.1; NM_138823.2.
DR AlphaFoldDB; P50411; -.
DR SMR; P50411; -.
DR ELM; P50411; -.
DR STRING; 10116.ENSRNOP00000002361; -.
DR iPTMnet; P50411; -.
DR PhosphoSitePlus; P50411; -.
DR jPOST; P50411; -.
DR PaxDb; P50411; -.
DR PRIDE; P50411; -.
DR Ensembl; ENSRNOT00000002361; ENSRNOP00000002361; ENSRNOG00000001733.
DR GeneID; 192361; -.
DR KEGG; rno:192361; -.
DR UCSC; RGD:621099; rat.
DR CTD; 5504; -.
DR RGD; 621099; Ppp1r2.
DR eggNOG; KOG4041; Eukaryota.
DR GeneTree; ENSGT00390000004757; -.
DR HOGENOM; CLU_084310_2_0_1; -.
DR InParanoid; P50411; -.
DR OrthoDB; 1321970at2759; -.
DR PhylomeDB; P50411; -.
DR TreeFam; TF105536; -.
DR PRO; PR:P50411; -.
DR Proteomes; UP000002494; Chromosome 11.
DR Genevisible; P50411; RN.
DR GO; GO:0005737; C:cytoplasm; IDA:RGD.
DR GO; GO:0043197; C:dendritic spine; IDA:RGD.
DR GO; GO:0030426; C:growth cone; IDA:RGD.
DR GO; GO:0019904; F:protein domain specific binding; IPI:RGD.
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; IDA:RGD.
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 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; Glycogen metabolism; Phosphoprotein;
KW Protein phosphatase inhibitor; Reference proteome.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000250|UniProtKB:P11845"
FT CHAIN 2..205
FT /note="Protein phosphatase inhibitor 2"
FT /id="PRO_0000071484"
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 104..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 108..142
FT /note="Basic and acidic 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:0000250|UniProtKB:P41236"
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:0000250|UniProtKB:P41236"
FT MOD_RES 89
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9DCL8"
FT MOD_RES 96
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q9DCL8"
FT MOD_RES 116
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q9DCL8"
FT MOD_RES 121
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 122
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 130
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
SQ SEQUENCE 205 AA; 23071 MW; 5D58BC9435A2A5CE CRC64;
MAASTASHRP IKGILKNKTS TTSSVVASAE QPRRTVEEEL SKKSQKWDEM NILATYHPAD
KDYGLMKIDE PDTPYHNMIG DDEDVCSDSE GNEVMTPEIL AKKLAAAEGS EPKFRTREQE
SSGEEDNDLS PEEREKKRQF EMKRKLHYNE GLNIKLARQL ISKDLHDDDE DEEMSETADA
DSMNIEESNQ GSTAGDHLQH KSQSS
