ID   PESC_MOUSE              Reviewed;         584 AA.
AC   Q9EQ61; Q542F0;
DT   20-JUN-2002, integrated into UniProtKB/Swiss-Prot.
DT   01-MAR-2001, sequence version 1.
DT   24-JAN-2024, entry version 149.
DE   RecName: Full=Pescadillo homolog {ECO:0000255|HAMAP-Rule:MF_03028};
GN   Name=Pes1; Synonyms=Pes;
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 [MRNA], SUBCELLULAR LOCATION, AND TISSUE SPECIFICITY.
RC   STRAIN=C57BL/6J;
RX   PubMed=11112348; DOI=10.1006/geno.2000.6375;
RA   Haque J., Boger S., Li J., Duncan S.A.;
RT   "The murine Pes1 gene encodes a nuclear protein containing a BRCT domain.";
RL   Genomics 70:201-210(2000).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=C57BL/6J, and NOD; TISSUE=Skin, and Thymus;
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   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Colon, 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   [4]
RP   INDUCTION, AND DEVELOPMENTAL STAGE.
RX   PubMed=11071894; DOI=10.1074/jbc.m008536200;
RA   Kinoshita Y., Jarell A.D., Flaman J.-M., Foltz G., Schuster J.,
RA   Sopher B.L., Irvin D.K., Kanning K., Kornblum H.I., Nelson P.S., Hieter P.,
RA   Morrison R.S.;
RT   "Pescadillo, a novel cell cycle regulatory protein abnormally expressed in
RT   malignant cells.";
RL   J. Biol. Chem. 276:6656-6665(2001).
RN   [5]
RP   SUBCELLULAR LOCATION, TISSUE SPECIFICITY, DEVELOPMENTAL STAGE, INDUCTION,
RP   AND DISRUPTION PHENOTYPE.
RX   PubMed=12237316; DOI=10.1074/jbc.m208338200;
RA   Lerch-Gaggl A.F., Haque J., Li J., Ning G., Traktman P., Duncan S.A.;
RT   "Pescadillo is essential for nucleolar assembly, ribosome biogenesis, and
RT   mammalian cell proliferation.";
RL   J. Biol. Chem. 277:45347-45355(2002).
RN   [6]
RP   FUNCTION, INTERACTION WITH BOP1, AND SUBCELLULAR LOCATION.
RX   PubMed=15225545; DOI=10.1016/j.molcel.2004.05.020;
RA   Lapik Y.R., Fernandes C.J., Lau L.F., Pestov D.G.;
RT   "Physical and functional interaction between Pes1 and Bop1 in mammalian
RT   ribosome biogenesis.";
RL   Mol. Cell 15:17-29(2004).
RN   [7]
RP   INTERACTION WITH IRS1 AND UBTF, AND SUBCELLULAR LOCATION.
RX   PubMed=15169904; DOI=10.1128/mcb.24.12.5421-5433.2004;
RA   Prisco M., Maiorana A., Guerzoni C., Calin G., Calabretta B., Voit R.,
RA   Grummt I., Baserga R.;
RT   "Role of pescadillo and upstream binding factor in the proliferation and
RT   differentiation of murine myeloid cells.";
RL   Mol. Cell. Biol. 24:5421-5433(2004).
RN   [8]
RP   FUNCTION, INTERACTION WITH MAP1B, AND SUBCELLULAR LOCATION.
RX   PubMed=17308336; DOI=10.1074/jbc.m610977200;
RA   Lerch-Gaggl A.F., Sun K., Duncan S.A.;
RT   "Light chain 1 of microtubule-associated protein 1B can negatively regulate
RT   the action of Pes1.";
RL   J. Biol. Chem. 282:11308-11316(2007).
RN   [9]
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   TISSUE=Spleen;
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: Component of the PeBoW complex, which is required for
CC       maturation of 28S and 5.8S ribosomal RNAs and formation of the 60S
CC       ribosome. {ECO:0000255|HAMAP-Rule:MF_03028,
CC       ECO:0000269|PubMed:15225545, ECO:0000269|PubMed:17308336}.
CC   -!- SUBUNIT: Component of the PeBoW complex, composed of BOP1, PES1 and
CC       WDR12 (PubMed:15225545). The complex is held together by BOP1, which
CC       interacts with PES1 via its N-terminal domain and with WDR12 via a
CC       high-affinity interaction between the seven-bladed beta-propeller
CC       domains of the 2 proteins. The PeBoW complex associates with the 66S
CC       pre-ribosome (By similarity). The PeBoW complex also associates with
CC       DDX27, PES1 interacts directly with DDX27 (By similarity). Interacts
CC       with IRS1 and UBTF (PubMed:15169904). May interact with MAP1B
CC       (PubMed:17308336). {ECO:0000255|HAMAP-Rule:MF_03028,
CC       ECO:0000269|PubMed:15169904, ECO:0000269|PubMed:15225545,
CC       ECO:0000269|PubMed:17308336}.
CC   -!- SUBCELLULAR LOCATION: Nucleus, nucleolus. Nucleus, nucleoplasm.
CC       Chromosome. Note=Appears to localize to the periphery of metaphase
CC       chromosomes during mitosis and to the prenucleolar bodies that form in
CC       mitotic cells prior to the actual nucleoli.
CC   -!- TISSUE SPECIFICITY: Ubiquitous. Highest levels appear to be found in
CC       tissues that contain a population of proliferating cells, such as ovary
CC       and testis. Also appears to be highly expressed in kidney and liver. In
CC       the brain expression is restricted to neural progenitor cells and
CC       postmitotic neurons. Highly expressed in malignant astrocytes.
CC       {ECO:0000269|PubMed:11112348, ECO:0000269|PubMed:12237316}.
CC   -!- DEVELOPMENTAL STAGE: In 2-cell and 4-cell stage interphase blastomeres
CC       expression is restricted to a sub-nuclear band that encircles one or
CC       more large vacuoles within the nucleus. These vacuoles may give rise to
CC       the mature nucleolus. Later in embryogenesis high levels are detected
CC       in developing liver. Is also widely and highly expressed throughout the
CC       developing brain and spinal cord at embryonic day 13.
CC       {ECO:0000269|PubMed:11071894, ECO:0000269|PubMed:12237316}.
CC   -!- INDUCTION: Induced in malignant astrocytes following the loss of p53.
CC       Induced in hepatocytes following partial hepatectomy.
CC       {ECO:0000269|PubMed:11071894, ECO:0000269|PubMed:12237316}.
CC   -!- PTM: Sumoylated. {ECO:0000255|HAMAP-Rule:MF_03028}.
CC   -!- DISRUPTION PHENOTYPE: Embryos die during preimplantation stages of
CC       development, with blastomeres failing to progress past morula stages.
CC       Within blastocysts the nucleoli fail to form correctly and the number
CC       of ribosomes appears dramatically reduced.
CC       {ECO:0000269|PubMed:12237316}.
CC   -!- SIMILARITY: Belongs to the pescadillo family. {ECO:0000255|HAMAP-
CC       Rule:MF_03028}.
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DR   EMBL; AF289539; AAG40734.1; -; mRNA.
DR   EMBL; AK029075; BAC26278.1; -; mRNA.
DR   EMBL; AK088831; BAC40599.1; -; mRNA.
DR   EMBL; BC004844; AAH04844.1; -; mRNA.
DR   EMBL; BC011142; AAH11142.1; -; mRNA.
DR   CCDS; CCDS24372.1; -.
DR   RefSeq; NP_075027.1; NM_022889.3.
DR   AlphaFoldDB; Q9EQ61; -.
DR   SMR; Q9EQ61; -.
DR   BioGRID; 211118; 6.
DR   CORUM; Q9EQ61; -.
DR   STRING; 10090.ENSMUSP00000020705; -.
DR   GlyGen; Q9EQ61; 1 site, 1 O-linked glycan (1 site).
DR   iPTMnet; Q9EQ61; -.
DR   PhosphoSitePlus; Q9EQ61; -.
DR   SwissPalm; Q9EQ61; -.
DR   EPD; Q9EQ61; -.
DR   MaxQB; Q9EQ61; -.
DR   PaxDb; 10090-ENSMUSP00000105612; -.
DR   ProteomicsDB; 288036; -.
DR   Pumba; Q9EQ61; -.
DR   Antibodypedia; 10811; 288 antibodies from 33 providers.
DR   DNASU; 64934; -.
DR   Ensembl; ENSMUST00000020705.5; ENSMUSP00000020705.5; ENSMUSG00000020430.13.
DR   GeneID; 64934; -.
DR   KEGG; mmu:64934; -.
DR   UCSC; uc007hua.1; mouse.
DR   AGR; MGI:1890613; -.
DR   CTD; 23481; -.
DR   MGI; MGI:1890613; Pes1.
DR   VEuPathDB; HostDB:ENSMUSG00000020430; -.
DR   eggNOG; KOG2481; Eukaryota.
DR   GeneTree; ENSGT00390000002626; -.
DR   HOGENOM; CLU_019619_0_0_1; -.
DR   InParanoid; Q9EQ61; -.
DR   OrthoDB; 169151at2759; -.
DR   Reactome; R-MMU-6791226; Major pathway of rRNA processing in the nucleolus and cytosol.
DR   BioGRID-ORCS; 64934; 29 hits in 73 CRISPR screens.
DR   ChiTaRS; Pes1; mouse.
DR   PRO; PR:Q9EQ61; -.
DR   Proteomes; UP000000589; Chromosome 11.
DR   RNAct; Q9EQ61; Protein.
DR   Bgee; ENSMUSG00000020430; Expressed in dorsal pancreas and 233 other cell types or tissues.
DR   ExpressionAtlas; Q9EQ61; baseline and differential.
DR   GO; GO:0005694; C:chromosome; ISO:MGI.
DR   GO; GO:0000793; C:condensed chromosome; IDA:MGI.
DR   GO; GO:0005829; C:cytosol; ISO:MGI.
DR   GO; GO:0005730; C:nucleolus; IDA:MGI.
DR   GO; GO:0005654; C:nucleoplasm; ISS:UniProtKB.
DR   GO; GO:0005634; C:nucleus; IDA:MGI.
DR   GO; GO:0070545; C:PeBoW complex; IDA:MGI.
DR   GO; GO:0030687; C:preribosome, large subunit precursor; ISS:UniProtKB.
DR   GO; GO:0043021; F:ribonucleoprotein complex binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0003723; F:RNA binding; IBA:GO_Central.
DR   GO; GO:0048144; P:fibroblast proliferation; ISO:MGI.
DR   GO; GO:0000466; P:maturation of 5.8S rRNA from tricistronic rRNA transcript (SSU-rRNA, 5.8S rRNA, LSU-rRNA); ISS:UniProtKB.
DR   GO; GO:0000463; P:maturation of LSU-rRNA from tricistronic rRNA transcript (SSU-rRNA, 5.8S rRNA, LSU-rRNA); IMP:MGI.
DR   GO; GO:0007000; P:nucleolus organization; IMP:MGI.
DR   GO; GO:0033365; P:protein localization to organelle; IMP:MGI.
DR   GO; GO:0051726; P:regulation of cell cycle; ISS:UniProtKB.
DR   GO; GO:0042254; P:ribosome biogenesis; IMP:MGI.
DR   GO; GO:0006364; P:rRNA processing; IMP:MGI.
DR   CDD; cd17709; BRCT_pescadillo_like; 1.
DR   Gene3D; 3.40.50.10190; BRCT domain; 1.
DR   HAMAP; MF_03028; Pescadillo; 1.
DR   InterPro; IPR001357; BRCT_dom.
DR   InterPro; IPR036420; BRCT_dom_sf.
DR   InterPro; IPR010613; PES.
DR   PANTHER; PTHR12221; PESCADILLO - RELATED; 1.
DR   PANTHER; PTHR12221:SF6; PESCADILLO HOMOLOG; 1.
DR   Pfam; PF16589; BRCT_2; 1.
DR   Pfam; PF06732; Pescadillo_N; 1.
DR   SMART; SM00292; BRCT; 1.
DR   SUPFAM; SSF52113; BRCT domain; 1.
DR   PROSITE; PS50172; BRCT; 1.
DR   Genevisible; Q9EQ61; MM.
PE   1: Evidence at protein level;
KW   Acetylation; Chromosome; Isopeptide bond; Nucleus; Reference proteome;
KW   Ribosome biogenesis; rRNA processing; Ubl conjugation.
FT   CHAIN           1..584
FT                   /note="Pescadillo homolog"
FT                   /id="PRO_0000186189"
FT   DOMAIN          321..414
FT                   /note="BRCT"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_03028"
FT   REGION          1..257
FT                   /note="Sufficient for nucleolar localization"
FT                   /evidence="ECO:0000250"
FT   REGION          1..54
FT                   /note="Required for 28S ribosomal RNA processing"
FT                   /evidence="ECO:0000250"
FT   REGION          312..414
FT                   /note="Sufficient for interaction with MAP1B"
FT                   /evidence="ECO:0000269|PubMed:17308336"
FT   REGION          449..510
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          535..584
FT                   /note="Required for 28S ribosomal RNA processing"
FT                   /evidence="ECO:0000250"
FT   REGION          560..584
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        452..490
FT                   /note="Acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        491..510
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        560..578
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOD_RES         98
FT                   /note="N6-acetyllysine"
FT                   /evidence="ECO:0000250|UniProtKB:O00541"
FT   CROSSLNK        513
FT                   /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT                   G-Cter in SUMO1); alternate"
FT                   /evidence="ECO:0000250|UniProtKB:O00541"
FT   CROSSLNK        513
FT                   /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT                   G-Cter in SUMO2); alternate"
FT                   /evidence="ECO:0000250|UniProtKB:O00541"
SQ   SEQUENCE   584 AA;  67796 MW;  63D3C352DF5E9893 CRC64;
     MGGLEKKKYE RGSATNYITR NKARKKLQLS LPDFRRLCIL KGIYPHEPKH KKKVNKGSTA
     ARTFYLIKDI KFLLHEPIVN KFREYKVFVR KLRKAYGKSE WNAVERLKDN KPCYKLDHIV
     KERYPTFIDA LRDLDDALSM CFLFSTFPRT GKCHVQTIQL CRRLTVEFLH YVITARALRK
     VFLSIKGIYY QAEVLGQPIV WIAPYAFSHD HPTDVDYRVM ATFTEFYTTL LGFVNFRLYQ
     SLNLHYPPKL EGQAQAETKI SEDTYALDSE SSMEKLAALS ASLARVVVPA IEEAEADEFP
     TDGEVTAQEE DRKKELEAQE KHKKLFEGLK FFLNREVPRE ALAFIIRSFG GDVSWDKSLC
     IGATYDVTDS CITHQIVDRP GQQTPIIGRY YVQPQWVFDC VNARLLLPVA EYFPGMQLPP
     HLSPFVSEKE GDYIPPEKLK LLALQRGEDP GHLEEEEEED EDDDNEGDVA AENEEEDVEV
     ESEEEEEEEV HLSALEQHRL EEKKPQVMAG TVKLEDKQRL AQEEESEAKR LAIMMMKKRE
     KYLYQKIMFG KRRKIREANK LAEKRKAHDD AVRSEKKAKR TRPV
//