PBIR1_RAT
ID PBIR1_RAT Reviewed; 286 AA.
AC Q6AYT4;
DT 05-JUL-2005, integrated into UniProtKB/Swiss-Prot.
DT 13-SEP-2004, sequence version 1.
DT 03-AUG-2022, entry version 95.
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|RGD:1310316};
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 [LARGE SCALE MRNA].
RC TISSUE=Kidney;
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 [2]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-61; SER-75; SER-142; SER-146;
RP SER-188 AND SER-269, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE
RP 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: 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-36 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-36
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-36 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; BC078922; AAH78922.1; -; mRNA.
DR RefSeq; NP_001014051.1; NM_001014029.1.
DR AlphaFoldDB; Q6AYT4; -.
DR STRING; 10116.ENSRNOP00000068087; -.
DR iPTMnet; Q6AYT4; -.
DR PhosphoSitePlus; Q6AYT4; -.
DR PRIDE; Q6AYT4; -.
DR Ensembl; ENSRNOT00000076544; ENSRNOP00000068087; ENSRNOG00000051051.
DR GeneID; 309420; -.
DR KEGG; rno:309420; -.
DR UCSC; RGD:1310316; rat.
DR CTD; 116224; -.
DR RGD; 1310316; Fam122a.
DR eggNOG; ENOG502QTCH; Eukaryota.
DR GeneTree; ENSGT00390000015476; -.
DR HOGENOM; CLU_083344_0_0_1; -.
DR InParanoid; Q6AYT4; -.
DR OMA; MNLMNRE; -.
DR OrthoDB; 1406067at2759; -.
DR PhylomeDB; Q6AYT4; -.
DR PRO; PR:Q6AYT4; -.
DR Proteomes; UP000002494; Chromosome 1.
DR Bgee; ENSRNOG00000051051; Expressed in heart and 19 other tissues.
DR Genevisible; Q6AYT4; RN.
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..286
FT /note="P2R1A-PPP2R2A-interacting phosphatase regulator 1"
FT /id="PRO_0000089691"
FT REGION 1..46
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 166..187
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 238..286
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 238..271
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 34
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q96E09"
FT MOD_RES 36
FT /note="Phosphoserine; by CHEK1"
FT /evidence="ECO:0000250|UniProtKB:Q96E09"
FT MOD_RES 44
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q96E09"
FT MOD_RES 47
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q96E09"
FT MOD_RES 61
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 75
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 142
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 146
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 148
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q96E09"
FT MOD_RES 186
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q96E09"
FT MOD_RES 188
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 266
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9DB52"
FT MOD_RES 269
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 275
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q96E09"
FT CROSSLNK 88
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO1)"
FT /evidence="ECO:0000250|UniProtKB:Q96E09"
SQ SEQUENCE 286 AA; 30472 MW; 14A2B674623D2688 CRC64;
MAQEKMELDL ELPAGTGASP AEGGGPGSGG LRRSNSAPLI HGLSDSSPVF QAEAPSARRN
STTFPSRHGL LLPASPVRMH SSRLHQIKQE EGMDLINRET VHEREVQTAM QISHSWEESF
SLSDNDVEKS ASPKRIDFIP VSPAPSPTRG IGKQCFSPSL QSFVSSNGLP PSPIPSPTTR
FTTRRSQSPI NCIRPSVLGP LKRKCEMETD YQPKRFFQGI TNMLSSDVAQ LSEPGVCVSS
DTLDGNSSSA GSSCNSPAKV STTTDSPVSP AQAASPFIPV DELSSK
