PBIR1_MOUSE
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 03-AUG-2022, entry version 120.
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; 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, 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).
CC -!- FUNCTION: Acts as an inhibitor of serine/threonine-protein phosphatase
CC 2A (PP2A) activity. Potentiates ubiquitin-mediated proteasomal
CC degradation of serine/threonine-protein phosphatase 2A catalytic
CC subunit alpha (PPP2CA) (By similarity). Inhibits PP2A-mediated
CC dephosphorylation of WEE1, promoting ubiquitin-mediated proteolysis of
CC WEE1, thereby releasing G2/M checkpoint (By similarity).
CC {ECO:0000250|UniProtKB:Q96E09}.
CC -!- SUBUNIT: Interacts with PPP2CA, PPP2R2A and PPP2R1A (By similarity).
CC The CHEK1-mediated Ser-34 phosphorylated form interacts with 14-3-3
CC proteins (By 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_026520.3.
DR AlphaFoldDB; Q9DB52; -.
DR STRING; 10090.ENSMUSP00000097152; -.
DR iPTMnet; Q9DB52; -.
DR PhosphoSitePlus; Q9DB52; -.
DR EPD; Q9DB52; -.
DR jPOST; Q9DB52; -.
DR MaxQB; Q9DB52; -.
DR PaxDb; Q9DB52; -.
DR PeptideAtlas; Q9DB52; -.
DR PRIDE; Q9DB52; -.
DR ProteomicsDB; 271511; -.
DR Antibodypedia; 26789; 54 antibodies from 14 providers.
DR Ensembl; ENSMUST00000099556; ENSMUSP00000097152; ENSMUSG00000074922.
DR GeneID; 68034; -.
DR KEGG; mmu:68034; -.
DR UCSC; uc008haq.1; mouse.
DR CTD; 68034; -.
DR MGI; MGI:1915284; Fam122a.
DR VEuPathDB; HostDB:ENSMUSG00000074922; -.
DR eggNOG; ENOG502QTCH; Eukaryota.
DR GeneTree; ENSGT00390000015476; -.
DR HOGENOM; CLU_083344_0_0_1; -.
DR InParanoid; Q9DB52; -.
DR OMA; MNLMNRE; -.
DR OrthoDB; 1406067at2759; -.
DR PhylomeDB; Q9DB52; -.
DR TreeFam; TF330808; -.
DR BioGRID-ORCS; 68034; 12 hits in 75 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 252 other tissues.
DR Genevisible; Q9DB52; MM.
DR GO; GO:0005737; C:cytoplasm; ISS:UniProtKB.
DR GO; GO:0005634; C:nucleus; ISS:UniProtKB.
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; IPR026716; PBIR1/2/3.
DR PANTHER; PTHR22227; PTHR22227; 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 47..65
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 233..269
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
