ID   PBIR1_MOUSE             Reviewed;         284 AA.
AC   Q9DB52; Q3TA50; Q9D078;
DT   05-JUL-2005, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-2001, sequence version 1.
DT   02-SEP-2026, entry version 138.
DE   RecName: Full=P2R1A-PPP2R2A-interacting phosphatase regulator 1 {ECO:0000250|UniProtKB:Q96E09};
DE   AltName: Full=PABIR family member 1 {ECO:0000250|UniProtKB:Q96E09};
GN   Name=Pabir1 {ECO:0000250|UniProtKB:Q96E09};
GN   Synonyms=Fam122a {ECO:0000312|MGI:MGI:1915284};
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, and NOD;
RC   TISSUE=Cecum, Cerebellum, Embryo, and Spleen;
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   TISSUE=Eye, and Mammary gland;
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-267, AND IDENTIFICATION BY
RP   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   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-140 AND SER-144, 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   [5]
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   TISSUE=Liver;
RX   PubMed=18630941; DOI=10.1021/pr800223m;
RA   Zhou H., Ye M., Dong J., Han G., Jiang X., Wu R., Zou H.;
RT   "Specific phosphopeptide enrichment with immobilized titanium ion affinity
RT   chromatography adsorbent for phosphoproteome analysis.";
RL   J. Proteome Res. 7:3957-3967(2008).
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-73, AND IDENTIFICATION BY
RP   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 SER-45; SER-59; SER-73; SER-140;
RP   SER-144; SER-264; SER-267 AND SER-273, 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).
CC   -!- FUNCTION: Acts as an inhibitor of serine/threonine-protein phosphatase
CC       2A (PP2A) activity (By similarity). Inhibits PP2A activity by blocking
CC       the substrate binding site on PPP2R2A and the active site of PPP2CA (By
CC       similarity). Potentiates ubiquitin-mediated proteasomal degradation of
CC       serine/threonine-protein phosphatase 2A catalytic subunit alpha
CC       (PPP2CA) (By similarity). Inhibits PP2A-mediated dephosphorylation of
CC       WEE1, promoting ubiquitin-mediated proteolysis of WEE1, thereby
CC       releasing G2/M checkpoint (By similarity).
CC       {ECO:0000250|UniProtKB:Q96E09}.
CC   -!- SUBUNIT: Interacts with PPP2CA and PPP2R1A (By similarity). Interacts
CC       (via its N-terminus) with PPP2R2A; the interaction is direct and this
CC       interaction inhibits PP2A activity (By similarity). The CHEK1-mediated
CC       Ser-34 phosphorylated form interacts with 14-3-3 proteins (By
CC       similarity). {ECO:0000250|UniProtKB:Q96E09}.
CC   -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:Q96E09}. Cytoplasm
CC       {ECO:0000250|UniProtKB:Q96E09}. Note=The CHEK1-mediated Ser-34
CC       phosphorylated form is sequestered by 14-3-3 proteins in the cytoplasm
CC       and fails to translocate to the nucleus, where it otherwise inhibits
CC       serine/threonine-protein phosphatase 2A.
CC       {ECO:0000250|UniProtKB:Q96E09}.
CC   -!- PTM: CHEK1-mediated phosphorylation at Ser-34 negatively regulates its
CC       ability to inhibit serine/threonine-protein phosphatase 2A (PP2A)
CC       activity. Phosphorylation leads to its release from the PP2A complex
CC       and its sequestration by 14-3-3 proteins in the cytoplasm resulting in
CC       its inability to translocate to the nucleus, where it otherwise
CC       inhibits PP2A. {ECO:0000250|UniProtKB:Q96E09}.
CC   -!- SIMILARITY: Belongs to the FAM122 family. {ECO:0000305}.
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DR   EMBL; AK005219; BAB23889.1; -; mRNA.
DR   EMBL; AK011741; BAB27811.1; -; mRNA.
DR   EMBL; AK033646; BAC28405.1; -; mRNA.
DR   EMBL; AK077654; BAC36930.1; -; mRNA.
DR   EMBL; AK172089; BAE42820.1; -; mRNA.
DR   EMBL; BC028637; AAH28637.1; -; mRNA.
DR   EMBL; BC083062; AAH83062.1; -; mRNA.
DR   CCDS; CCDS29712.1; -.
DR   RefSeq; NP_080796.1; NM_026520.4.
DR   AlphaFoldDB; Q9DB52; -.
DR   SMR; Q9DB52; -.
DR   FunCoup; Q9DB52; 4215.
DR   STRING; 10090.ENSMUSP00000097152; -.
DR   GlyGen; Q9DB52; 2 sites, 1 N-linked glycan (1 site).
DR   iPTMnet; Q9DB52; -.
DR   PhosphoSitePlus; Q9DB52; -.
DR   jPOST; Q9DB52; -.
DR   PaxDb; 10090-ENSMUSP00000097152; -.
DR   PeptideAtlas; Q9DB52; -.
DR   ProteomicsDB; 271511; -.
DR   Pumba; Q9DB52; -.
DR   Antibodypedia; 26789; 50 antibodies from 13 providers.
DR   Ensembl; ENSMUST00000099556.2; ENSMUSP00000097152.2; ENSMUSG00000074922.2.
DR   GeneID; 68034; -.
DR   KEGG; mmu:68034; -.
DR   UCSC; uc008haq.1; mouse.
DR   AGR; MGI:1915284; -.
DR   CTD; 116224; -.
DR   MGI; MGI:1915284; Pabir1.
DR   VEuPathDB; HostDB:ENSMUSG00000074922; -.
DR   eggNOG; ENOG502QTCH; Eukaryota.
DR   GeneTree; ENSGT00390000015476; -.
DR   HOGENOM; CLU_083344_0_0_1; -.
DR   InParanoid; Q9DB52; -.
DR   OMA; ISHHTDS; -.
DR   OrthoDB; 10036177at2759; -.
DR   PhylomeDB; Q9DB52; -.
DR   BioGRID-ORCS; 68034; 12 hits in 80 CRISPR screens.
DR   PRO; PR:Q9DB52; -.
DR   Proteomes; UP000000589; Chromosome 19.
DR   RNAct; Q9DB52; protein.
DR   Bgee; ENSMUSG00000074922; Expressed in pigmented layer of retina and 255 other cell types or tissues.
DR   GO; GO:0005737; C:cytoplasm; ISS:UniProtKB.
DR   GO; GO:0016604; C:nuclear body; ISO:GO_Central.
DR   GO; GO:0005654; C:nucleoplasm; ISO:GO_Central.
DR   GO; GO:0005634; C:nucleus; ISS:UniProtKB.
DR   GO; GO:0051721; F:protein phosphatase 2A binding; ISO:GO_Central.
DR   GO; GO:0004864; F:protein phosphatase inhibitor activity; ISO:GO_Central.
DR   GO; GO:0004865; F:protein serine/threonine phosphatase inhibitor activity; ISS:UniProtKB.
DR   GO; GO:0044818; P:mitotic G2/M transition checkpoint; ISS:UniProtKB.
DR   GO; GO:0030307; P:positive regulation of cell growth; ISS:UniProtKB.
DR   GO; GO:0032436; P:positive regulation of proteasomal ubiquitin-dependent protein catabolic process; ISS:UniProtKB.
DR   InterPro; IPR060392; PABIR_helical.
DR   InterPro; IPR026716; PBIR1/2/3.
DR   PANTHER; PTHR22227; FAMILY WITH SEQUENCE SIMILARITY 122B ISOFORM X1; 1.
DR   PANTHER; PTHR22227:SF14; PPP2R1A-PPP2R2A-INTERACTING PHOSPHATASE REGULATOR 1; 1.
DR   Pfam; PF27638; PABIR_N; 1.
PE   1: Evidence at protein level;
KW   Cytoplasm; Isopeptide bond; Nucleus; Phosphoprotein;
KW   Protein phosphatase inhibitor; Reference proteome; Ubl conjugation.
FT   CHAIN           1..284
FT                   /note="P2R1A-PPP2R2A-interacting phosphatase regulator 1"
FT                   /id="PRO_0000089690"
FT   REGION          1..65
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          164..185
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          233..284
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        20..29
FT                   /note="Gly residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        175..185
FT                   /note="Low complexity"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        243..254
FT                   /note="Low complexity"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        256..267
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOD_RES         32
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q96E09"
FT   MOD_RES         34
FT                   /note="Phosphoserine; by CHEK1"
FT                   /evidence="ECO:0000250|UniProtKB:Q96E09"
FT   MOD_RES         42
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q96E09"
FT   MOD_RES         45
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:21183079"
FT   MOD_RES         59
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:21183079"
FT   MOD_RES         73
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:19131326,
FT                   ECO:0007744|PubMed:21183079"
FT   MOD_RES         140
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:17242355,
FT                   ECO:0007744|PubMed:21183079"
FT   MOD_RES         144
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:17242355,
FT                   ECO:0007744|PubMed:21183079"
FT   MOD_RES         146
FT                   /note="Phosphothreonine"
FT                   /evidence="ECO:0000250|UniProtKB:Q96E09"
FT   MOD_RES         184
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q96E09"
FT   MOD_RES         186
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q96E09"
FT   MOD_RES         264
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:21183079"
FT   MOD_RES         267
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:15345747,
FT                   ECO:0007744|PubMed:21183079"
FT   MOD_RES         273
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:21183079"
FT   CROSSLNK        86
FT                   /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT                   G-Cter in SUMO1)"
FT                   /evidence="ECO:0000250|UniProtKB:Q96E09"
FT   CONFLICT        18..20
FT                   /note="PAE -> RRR (in Ref. 1; BAB27811)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        37
FT                   /note="L -> P (in Ref. 1; BAB27811)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   284 AA;  30270 MW;  F099612EB932120B CRC64;
     MAQEKMELDL ELPAGASPAE GGGPGGGGLR RSNSAPLIHG LSDSSPVFQA EAPSARRNST
     TFPSRHGLLL PASPVRMHSS RLHQIKQEEG MDLINRETVH EREVQTAMQI SHSWEESFSL
     SDNDVEKSAS PKRIDFIPVS PAPSPTRGIG KQCFSPSLQS FVSSNGLPPS PIPSPTTRFT
     TRRSQSPINC IRPSVLGPLK RKCEMETDYQ PKRFFQGITN MLSSDVAQLS DPGVCVSSDT
     LDGNSSSAGS SCNSPAKVST TTDSPVSPAQ AASPFIPVDE LSSK
//