PR15B_MOUSE
ID PR15B_MOUSE Reviewed; 697 AA.
AC Q8BFW3; Q3TC78; Q8C390;
DT 26-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2003, sequence version 1.
DT 03-AUG-2022, entry version 116.
DE RecName: Full=Protein phosphatase 1 regulatory subunit 15B;
DE AltName: Full=Constitutive repressor of eIF2alpha phosphorylation;
DE Short=CReP;
GN Name=Ppp1r15b;
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] (ISOFORMS 1 AND 2).
RC STRAIN=C57BL/6J, and NOD;
RC TISSUE=Cerebellum, Head, Liver, Lung, Placenta, and Spinal cord;
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 FUNCTION, AND INTERACTION WITH PP1.
RX PubMed=14638860; DOI=10.1083/jcb.200308075;
RA Jousse C., Oyadomari S., Novoa I., Lu P., Zhang Y., Harding H.P., Ron D.;
RT "Inhibition of a constitutive translation initiation factor 2alpha
RT phosphatase, CReP, promotes survival of stressed cells.";
RL J. Cell Biol. 163:767-775(2003).
RN [3]
RP IDENTIFICATION IN COMPLEX WITH PP1 AND NCK1.
RX PubMed=16835242; DOI=10.1074/jbc.m513556200;
RA Latreille M., Larose L.;
RT "Nck in a complex containing the catalytic subunit of protein phosphatase 1
RT regulates eukaryotic initiation factor 2alpha signaling and cell survival
RT to endoplasmic reticulum stress.";
RL J. Biol. Chem. 281:26633-26644(2006).
RN [4]
RP FUNCTION, AND DISRUPTION PHENOTYPE.
RX PubMed=19181853; DOI=10.1073/pnas.0809632106;
RA Harding H.P., Zhang Y., Scheuner D., Chen J.J., Kaufman R.J., Ron D.;
RT "Ppp1r15 gene knockout reveals an essential role for translation initiation
RT factor 2 alpha (eIF2alpha) dephosphorylation in mammalian development.";
RL Proc. Natl. Acad. Sci. U.S.A. 106:1832-1837(2009).
CC -!- FUNCTION: Maintains low levels of EIF2S1 phosphorylation in unstressed
CC cells by promoting its dephosphorylation by PP1.
CC {ECO:0000269|PubMed:14638860, ECO:0000269|PubMed:19181853}.
CC -!- SUBUNIT: Interacts with PP1. Part of a complex containing PPP1R15B, PP1
CC and NCK1/2. {ECO:0000269|PubMed:14638860, ECO:0000269|PubMed:16835242}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q8BFW3-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q8BFW3-2; Sequence=VSP_031652;
CC -!- DISRUPTION PHENOTYPE: Mice are born at the expected Mendelian ratio,
CC but exhibit severe growth retardation and impaired erythropoiesis. None
CC survive the first day of postnatal life. PPP1R15A-PPP1R15B double-
CC knockout embryos do not develop past the preimplantation period.
CC {ECO:0000269|PubMed:19181853}.
CC -!- SIMILARITY: Belongs to the PPP1R15 family. {ECO:0000305}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; AK049028; BAC33517.1; -; mRNA.
DR EMBL; AK082957; BAC38708.1; -; mRNA.
DR EMBL; AK086606; BAC39701.1; -; mRNA.
DR EMBL; AK144678; BAE26007.1; -; mRNA.
DR EMBL; AK146089; BAE26892.1; -; mRNA.
DR EMBL; AK167565; BAE39628.1; -; mRNA.
DR EMBL; AK170862; BAE42079.1; -; mRNA.
DR CCDS; CCDS15291.1; -. [Q8BFW3-1]
DR RefSeq; NP_598580.1; NM_133819.3. [Q8BFW3-1]
DR AlphaFoldDB; Q8BFW3; -.
DR SMR; Q8BFW3; -.
DR BioGRID; 224491; 3.
DR STRING; 10090.ENSMUSP00000057062; -.
DR iPTMnet; Q8BFW3; -.
DR PhosphoSitePlus; Q8BFW3; -.
DR EPD; Q8BFW3; -.
DR PaxDb; Q8BFW3; -.
DR PeptideAtlas; Q8BFW3; -.
DR PRIDE; Q8BFW3; -.
DR ProteomicsDB; 291850; -. [Q8BFW3-1]
DR ProteomicsDB; 291851; -. [Q8BFW3-2]
DR Antibodypedia; 34557; 111 antibodies from 25 providers.
DR Ensembl; ENSMUST00000052529; ENSMUSP00000057062; ENSMUSG00000046062. [Q8BFW3-1]
DR GeneID; 108954; -.
DR KEGG; mmu:108954; -.
DR UCSC; uc007cpt.2; mouse. [Q8BFW3-1]
DR CTD; 84919; -.
DR MGI; MGI:2444211; Ppp1r15b.
DR VEuPathDB; HostDB:ENSMUSG00000046062; -.
DR eggNOG; ENOG502QV9K; Eukaryota.
DR GeneTree; ENSGT00940000154404; -.
DR HOGENOM; CLU_014797_0_0_1; -.
DR InParanoid; Q8BFW3; -.
DR OMA; QTSGKNW; -.
DR OrthoDB; 391948at2759; -.
DR PhylomeDB; Q8BFW3; -.
DR TreeFam; TF105548; -.
DR BioGRID-ORCS; 108954; 24 hits in 70 CRISPR screens.
DR ChiTaRS; Ppp1r15b; mouse.
DR PRO; PR:Q8BFW3; -.
DR Proteomes; UP000000589; Chromosome 1.
DR RNAct; Q8BFW3; protein.
DR Bgee; ENSMUSG00000046062; Expressed in lacrimal gland and 255 other tissues.
DR Genevisible; Q8BFW3; MM.
DR GO; GO:0005783; C:endoplasmic reticulum; IBA:GO_Central.
DR GO; GO:0000164; C:protein phosphatase type 1 complex; IDA:ParkinsonsUK-UCL.
DR GO; GO:0019888; F:protein phosphatase regulator activity; IDA:MGI.
DR GO; GO:0006983; P:ER overload response; IDA:MGI.
DR GO; GO:1903912; P:negative regulation of endoplasmic reticulum stress-induced eIF2 alpha phosphorylation; IDA:ParkinsonsUK-UCL.
DR GO; GO:0001933; P:negative regulation of protein phosphorylation; ISO:MGI.
DR GO; GO:0070262; P:peptidyl-serine dephosphorylation; IDA:ParkinsonsUK-UCL.
DR GO; GO:0032516; P:positive regulation of phosphoprotein phosphatase activity; IBA:GO_Central.
DR GO; GO:0006446; P:regulation of translational initiation; IC:MGI.
DR GO; GO:0034976; P:response to endoplasmic reticulum stress; IMP:MGI.
DR GO; GO:0042542; P:response to hydrogen peroxide; IMP:MGI.
DR GO; GO:0006979; P:response to oxidative stress; IDA:MGI.
DR InterPro; IPR019523; Prot_Pase1_reg-su15A/B_C.
DR InterPro; IPR019512; Prot_Pase1_reg-su15B_N.
DR Pfam; PF10472; CReP_N; 1.
DR Pfam; PF10488; PP1c_bdg; 1.
PE 1: Evidence at protein level;
KW Alternative splicing; Phosphoprotein; Reference proteome;
KW Translation regulation.
FT CHAIN 1..697
FT /note="Protein phosphatase 1 regulatory subunit 15B"
FT /id="PRO_0000320521"
FT REGION 328..354
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 417..456
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 486..531
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 424..451
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 197
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q5SWA1"
FT MOD_RES 199
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q5SWA1"
FT MOD_RES 492
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q5SWA1"
FT VAR_SEQ 336..353
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:16141072"
FT /id="VSP_031652"
SQ SEQUENCE 697 AA; 77712 MW; E439B12615F33737 CRC64;
METGTHRARK RPGPRLGSWF RLPFLRRSHA CSSEFPPPSS RQNPGNSALP ERRTRYWTKL
LSQLLALLPS LFQKLLLWSQ LFGGLIPTRW LDFAASYSAL RALRGREESA APTVQKSLSS
LRLDSSEDLV VSSLDWLEEG LQWQCSSSDL ELKLKAQERA LDSAAPTFLL EQQLWGVELL
PSSLQAGLVS HRELDSSSSG PLSVQSLGNF KVVSYLLNPS YLDYLPQLGL RCQSSAGGGQ
FVGFRTLTPE SCYLSEDGCH PQPLRAEMSA TAWRRCPPLS TEGLPEIHHL RMKRLEFLQA
NKGQELPTPD QDNGYHSLEE EHNLLRMDPQ HCTDNPAQAV SPAADRPEPT EKKPELVIQE
VSQSPQGSSL FCELPVEKEC EEDHTNATDL SDRGESLPVS TRPVCSNKLI DYILGGAPSD
LEASSDSESE DWGEEPEDDG FDSDGSLSES DVEQDSEGLH LWNSFHSVDP YNPQNFTATI
QTAARIAPRD PSDSGTSWSG SCGVGSCQEG PLPETPDHSS GEEDDWEPSA DEAENLKLWN
SFCHSEDPYN LLNFKAPFQP SGKNWKGRQD SKASSEATVA FSGHHTLLSC KAQLLESQED
NCPGCGLGEA LAGERYTHIK RKKVTFLEEV TEYYISGDED RKGPWEEFAR DGCRFQKRIQ
ETEVAIGYCL AFEHREKMFN RLRIESKDLL LYSNVKK
