ID PESC_HUMAN Reviewed; 588 AA. AC O00541; Q6IC29; DT 20-JUN-2002, integrated into UniProtKB/Swiss-Prot. DT 01-JUL-1997, sequence version 1. DT 27-MAR-2024, entry version 201. DE RecName: Full=Pescadillo homolog {ECO:0000255|HAMAP-Rule:MF_03028}; GN Name=PES1 {ECO:0000255|HAMAP-Rule:MF_03028}; OS Homo sapiens (Human). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia; OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae; OC Homo. OX NCBI_TaxID=9606; RN [1] RP NUCLEOTIDE SEQUENCE [MRNA]. RX PubMed=8985183; DOI=10.1101/gad.10.24.3141; RA Allende M.L., Amsterdam A., Becker T., Kawakami K., Gaiano N., Hopkins N.; RT "Insertional mutagenesis in zebrafish identifies two novel genes, RT pescadillo and dead eye, essential for embryonic development."; RL Genes Dev. 10:3141-3155(1996). RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2). RX PubMed=15461802; DOI=10.1186/gb-2004-5-10-r84; RA Collins J.E., Wright C.L., Edwards C.A., Davis M.P., Grinham J.A., RA Cole C.G., Goward M.E., Aguado B., Mallya M., Mokrab Y., Huckle E.J., RA Beare D.M., Dunham I.; RT "A genome annotation-driven approach to cloning the human ORFeome."; RL Genome Biol. 5:R84.1-R84.11(2004). RN [3] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RX PubMed=10591208; DOI=10.1038/990031; RA Dunham I., Hunt A.R., Collins J.E., Bruskiewich R., Beare D.M., Clamp M., RA Smink L.J., Ainscough R., Almeida J.P., Babbage A.K., Bagguley C., RA Bailey J., Barlow K.F., Bates K.N., Beasley O.P., Bird C.P., Blakey S.E., RA Bridgeman A.M., Buck D., Burgess J., Burrill W.D., Burton J., Carder C., RA Carter N.P., Chen Y., Clark G., Clegg S.M., Cobley V.E., Cole C.G., RA Collier R.E., Connor R., Conroy D., Corby N.R., Coville G.J., Cox A.V., RA Davis J., Dawson E., Dhami P.D., Dockree C., Dodsworth S.J., Durbin R.M., RA Ellington A.G., Evans K.L., Fey J.M., Fleming K., French L., Garner A.A., RA Gilbert J.G.R., Goward M.E., Grafham D.V., Griffiths M.N.D., Hall C., RA Hall R.E., Hall-Tamlyn G., Heathcott R.W., Ho S., Holmes S., Hunt S.E., RA Jones M.C., Kershaw J., Kimberley A.M., King A., Laird G.K., Langford C.F., RA Leversha M.A., Lloyd C., Lloyd D.M., Martyn I.D., Mashreghi-Mohammadi M., RA Matthews L.H., Mccann O.T., Mcclay J., Mclaren S., McMurray A.A., RA Milne S.A., Mortimore B.J., Odell C.N., Pavitt R., Pearce A.V., Pearson D., RA Phillimore B.J.C.T., Phillips S.H., Plumb R.W., Ramsay H., Ramsey Y., RA Rogers L., Ross M.T., Scott C.E., Sehra H.K., Skuce C.D., Smalley S., RA Smith M.L., Soderlund C., Spragon L., Steward C.A., Sulston J.E., RA Swann R.M., Vaudin M., Wall M., Wallis J.M., Whiteley M.N., Willey D.L., RA Williams L., Williams S.A., Williamson H., Wilmer T.E., Wilming L., RA Wright C.L., Hubbard T., Bentley D.R., Beck S., Rogers J., Shimizu N., RA Minoshima S., Kawasaki K., Sasaki T., Asakawa S., Kudoh J., Shintani A., RA Shibuya K., Yoshizaki Y., Aoki N., Mitsuyama S., Roe B.A., Chen F., Chu L., RA Crabtree J., Deschamps S., Do A., Do T., Dorman A., Fang F., Fu Y., Hu P., RA Hua A., Kenton S., Lai H., Lao H.I., Lewis J., Lewis S., Lin S.-P., Loh P., RA Malaj E., Nguyen T., Pan H., Phan S., Qi S., Qian Y., Ray L., Ren Q., RA Shaull S., Sloan D., Song L., Wang Q., Wang Y., Wang Z., White J., RA Willingham D., Wu H., Yao Z., Zhan M., Zhang G., Chissoe S., Murray J., RA Miller N., Minx P., Fulton R., Johnson D., Bemis G., Bentley D., RA Bradshaw H., Bourne S., Cordes M., Du Z., Fulton L., Goela D., Graves T., RA Hawkins J., Hinds K., Kemp K., Latreille P., Layman D., Ozersky P., RA Rohlfing T., Scheet P., Walker C., Wamsley A., Wohldmann P., Pepin K., RA Nelson J., Korf I., Bedell J.A., Hillier L.W., Mardis E., Waterston R., RA Wilson R., Emanuel B.S., Shaikh T., Kurahashi H., Saitta S., Budarf M.L., RA McDermid H.E., Johnson A., Wong A.C.C., Morrow B.E., Edelmann L., Kim U.J., RA Shizuya H., Simon M.I., Dumanski J.P., Peyrard M., Kedra D., Seroussi E., RA Fransson I., Tapia I., Bruder C.E., O'Brien K.P., Wilkinson P., RA Bodenteich A., Hartman K., Hu X., Khan A.S., Lane L., Tilahun Y., RA Wright H.; RT "The DNA sequence of human chromosome 22."; RL Nature 402:489-495(1999). RN [4] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1). RC TISSUE=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 [5] RP CHARACTERIZATION. 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 [6] RP SUBCELLULAR LOCATION. RX PubMed=12022229; DOI=10.1017/s1355838202020022; RA Oeffinger M., Leung A., Lamond A., Tollervey D.; RT "Yeast Pescadillo is required for multiple activities during 60S ribosomal RT subunit synthesis."; RL RNA 8:626-636(2002). RN [7] RP ERRATUM OF PUBMED:12022229. RA Oeffinger M., Leung A., Lamond A., Tollervey D.; RL RNA 8:851-851(2002). RN [8] RP SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS]. RC TISSUE=Cervix carcinoma; RX PubMed=12429849; DOI=10.1091/mbc.e02-05-0271; RA Scherl A., Coute Y., Deon C., Calle A., Kindbeiter K., Sanchez J.-C., RA Greco A., Hochstrasser D.F., Diaz J.-J.; RT "Functional proteomic analysis of human nucleolus."; RL Mol. Biol. Cell 13:4100-4109(2002). RN [9] RP INTERACTION WITH BOP1 AND WDR12, AND INDUCTION. RX PubMed=16043514; DOI=10.1083/jcb.200501141; RA Hoelzel M., Rohrmoser M., Schlee M., Grimm T., Harasim T., Malamoussi A., RA Gruber-Eber A., Kremmer E., Hiddemann W., Bornkamm G.W., Eick D.; RT "Mammalian WDR12 is a novel member of the Pes1-Bop1 complex and is required RT for ribosome biogenesis and cell proliferation."; RL J. Cell Biol. 170:367-378(2005). RN [10] RP FUNCTION, INTERACTION WITH BOP1 AND WDR12, AND SUBCELLULAR LOCATION. RX PubMed=16738141; DOI=10.1093/nar/gkl378; RA Grimm T., Hoelzel M., Rohrmoser M., Harasim T., Malamoussi A., RA Gruber-Eber A., Kremmer E., Eick D.; RT "Dominant-negative Pes1 mutants inhibit ribosomal RNA processing and cell RT proliferation via incorporation into the PeBoW-complex."; RL Nucleic Acids Res. 34:3030-3043(2006). RN [11] RP FUNCTION, AND INTERACTION WITH BOP1 AND WDR12. RX PubMed=17353269; DOI=10.1128/mcb.00172-07; RA Rohrmoser M., Hoelzel M., Grimm T., Malamoussi A., Harasim T., Orban M., RA Pfisterer I., Gruber-Eber A., Kremmer E., Eick D.; RT "Interdependence of Pes1, Bop1, and WDR12 controls nucleolar localization RT and assembly of the PeBoW complex required for maturation of the 60S RT ribosomal subunit."; RL Mol. Cell. Biol. 27:3682-3694(2007). RN [12] RP FUNCTION, INTERACTION WITH BOP1 AND WDR12, SUBCELLULAR LOCATION, AND RP MUTAGENESIS OF PHE-327; ILE-347; ARG-380 AND TRP-397. RX PubMed=17189298; DOI=10.1093/nar/gkl1058; RA Hoelzel M., Grimm T., Rohrmoser M., Malamoussi A., Harasim T., RA Gruber-Eber A., Kremmer E., Eick D.; RT "The BRCT domain of mammalian Pes1 is crucial for nucleolar localization RT and rRNA processing."; RL Nucleic Acids Res. 35:789-800(2007). RN [13] RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Cervix carcinoma; RX PubMed=18669648; DOI=10.1073/pnas.0805139105; RA Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E., RA Elledge S.J., Gygi S.P.; RT "A quantitative atlas of mitotic phosphorylation."; RL Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008). RN [14] RP ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-98, AND IDENTIFICATION BY MASS RP SPECTROMETRY [LARGE SCALE ANALYSIS]. RX PubMed=19608861; DOI=10.1126/science.1175371; RA Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T.C., RA Olsen J.V., Mann M.; RT "Lysine acetylation targets protein complexes and co-regulates major RT cellular functions."; RL Science 325:834-840(2009). RN [15] RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RX PubMed=21269460; DOI=10.1186/1752-0509-5-17; RA Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T., RA Bennett K.L., Superti-Furga G., Colinge J.; RT "Initial characterization of the human central proteome."; RL BMC Syst. Biol. 5:17-17(2011). RN [16] RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RX PubMed=22814378; DOI=10.1073/pnas.1210303109; RA Van Damme P., Lasa M., Polevoda B., Gazquez C., Elosegui-Artola A., RA Kim D.S., De Juan-Pardo E., Demeyer K., Hole K., Larrea E., Timmerman E., RA Prieto J., Arnesen T., Sherman F., Gevaert K., Aldabe R.; RT "N-terminal acetylome analyses and functional insights of the N-terminal RT acetyltransferase NatB."; RL Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012). RN [17] RP SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-517, AND IDENTIFICATION BY MASS RP SPECTROMETRY [LARGE SCALE ANALYSIS]. RX PubMed=25114211; DOI=10.1073/pnas.1413825111; RA Impens F., Radoshevich L., Cossart P., Ribet D.; RT "Mapping of SUMO sites and analysis of SUMOylation changes induced by RT external stimuli."; RL Proc. Natl. Acad. Sci. U.S.A. 111:12432-12437(2014). RN [18] RP SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-517, AND IDENTIFICATION BY MASS RP SPECTROMETRY [LARGE SCALE ANALYSIS]. RX PubMed=28112733; DOI=10.1038/nsmb.3366; RA Hendriks I.A., Lyon D., Young C., Jensen L.J., Vertegaal A.C., RA Nielsen M.L.; RT "Site-specific mapping of the human SUMO proteome reveals co-modification RT with phosphorylation."; RL Nat. Struct. Mol. Biol. 24:325-336(2017). RN [19] RP STRUCTURE BY NMR OF 322-414. RG RIKEN structural genomics initiative (RSGI); RT "Solution structure of the BRCT domain from human pescadillo homolog 1."; RL Submitted (OCT-2007) to the PDB data bank. RN [20] RP INTERACTION WITH DDX27. RX PubMed=25825154; DOI=10.1016/j.yexcr.2015.03.017; RA Kellner M., Rohrmoser M., Forne I., Voss K., Burger K., Muehl B., RA Gruber-Eber A., Kremmer E., Imhof A., Eick D.; RT "DEAD-box helicase DDX27 regulates 3' end formation of ribosomal 47S RNA RT and stably associates with the PeBoW-complex."; RL Exp. Cell Res. 334:146-159(2015). 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:16738141, ECO:0000269|PubMed:17189298, CC ECO:0000269|PubMed:17353269}. CC -!- SUBUNIT: Component of the PeBoW complex, composed of BOP1, PES1 and CC WDR12 (PubMed:16043514, PubMed:16738141, PubMed:17189298, CC PubMed:17353269). The complex is held together by BOP1, which interacts CC with PES1 via its N-terminal domain and with WDR12 via a high-affinity CC interaction between the seven-bladed beta-propeller domains of the 2 CC proteins. The PeBoW complex associates with the 66S pre-ribosome (By CC similarity). The PeBoW complex also associates with DDX27, PES1 CC interacts directly with DDX27 (PubMed:25825154). Interacts with IRS1 CC and UBTF. May interact with MAP1B (By similarity). CC {ECO:0000250|UniProtKB:Q9EQ61, ECO:0000255|HAMAP-Rule:MF_03028, CC ECO:0000269|PubMed:16043514, ECO:0000269|PubMed:16738141, CC ECO:0000269|PubMed:17189298, ECO:0000269|PubMed:17353269, CC ECO:0000269|PubMed:25825154}. CC -!- INTERACTION: CC O00541; P54253: ATXN1; NbExp=3; IntAct=EBI-1053271, EBI-930964; CC O00541; Q14137: BOP1; NbExp=4; IntAct=EBI-1053271, EBI-1050828; CC O00541; Q08050: FOXM1; NbExp=2; IntAct=EBI-1053271, EBI-866480; CC O00541; P42858: HTT; NbExp=3; IntAct=EBI-1053271, EBI-466029; CC O00541; Q9GZL7: WDR12; NbExp=4; IntAct=EBI-1053271, EBI-2490660; 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. {ECO:0000255|HAMAP- CC Rule:MF_03028}. CC -!- ALTERNATIVE PRODUCTS: CC Event=Alternative splicing; Named isoforms=2; CC Name=1; CC IsoId=O00541-1; Sequence=Displayed; CC Name=2; CC IsoId=O00541-2; Sequence=VSP_013023; CC -!- TISSUE SPECIFICITY: Significant levels are detected in a variety of CC cancer cell lines, including glioblastoma, breast carcinoma, colon CC carcinoma and cervical carcinoma cells. Levels are abnormally elevated CC in malignant tumors of astrocytic origin. CC -!- INDUCTION: By MYC. {ECO:0000269|PubMed:16043514}. CC -!- PTM: Sumoylated. CC -!- SIMILARITY: Belongs to the pescadillo family. {ECO:0000255|HAMAP- CC Rule:MF_03028}. 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; U78310; AAB61140.1; -; mRNA. DR EMBL; CR456539; CAG30425.1; -; mRNA. DR EMBL; AC005006; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; BC032489; AAH32489.1; -; mRNA. DR CCDS; CCDS13880.1; -. [O00541-1] DR CCDS; CCDS58802.1; -. [O00541-2] DR RefSeq; NP_001230154.1; NM_001243225.1. [O00541-2] DR RefSeq; NP_055118.1; NM_014303.3. [O00541-1] DR PDB; 2EP8; NMR; -; A=322-414. DR PDB; 8FKP; EM; 2.85 A; SM=1-588. DR PDB; 8FKQ; EM; 2.76 A; SM=1-588. DR PDB; 8FKR; EM; 2.89 A; SM=1-588. DR PDB; 8FKS; EM; 2.88 A; SM=1-588. DR PDB; 8FKT; EM; 2.81 A; SM=1-588. DR PDB; 8FKU; EM; 2.82 A; SM=1-588. DR PDB; 8FKV; EM; 2.47 A; SM=1-588. DR PDB; 8FKW; EM; 2.50 A; SM=1-588. DR PDB; 8FKX; EM; 2.59 A; SM=1-588. DR PDB; 8FKY; EM; 2.67 A; SM=1-588. DR PDB; 8FKZ; EM; 3.04 A; SM=1-588. DR PDB; 8FL2; EM; 2.67 A; SM=1-588. DR PDB; 8FL3; EM; 2.53 A; SM=1-588. DR PDB; 8FL4; EM; 2.89 A; SM=1-588. DR PDB; 8FL6; EM; 2.62 A; SM=1-588. DR PDB; 8FL7; EM; 2.55 A; SM=1-588. DR PDB; 8FLA; EM; 2.63 A; SM=1-588. DR PDB; 8FLB; EM; 2.55 A; SM=1-588. DR PDB; 8FLD; EM; 2.58 A; SM=1-588. DR PDB; 8FLE; EM; 2.48 A; SM=1-588. DR PDB; 8INE; EM; 3.20 A; v=1-588. DR PDB; 8INF; EM; 3.00 A; v=1-588. DR PDB; 8IPX; EM; 4.30 A; q=1-588. DR PDB; 8IPY; EM; 3.20 A; q=1-588. DR PDB; 8IR3; EM; 3.50 A; q=1-588. DR PDBsum; 2EP8; -. DR PDBsum; 8FKP; -. DR PDBsum; 8FKQ; -. DR PDBsum; 8FKR; -. DR PDBsum; 8FKS; -. DR PDBsum; 8FKT; -. DR PDBsum; 8FKU; -. DR PDBsum; 8FKV; -. DR PDBsum; 8FKW; -. DR PDBsum; 8FKX; -. DR PDBsum; 8FKY; -. DR PDBsum; 8FKZ; -. DR PDBsum; 8FL2; -. DR PDBsum; 8FL3; -. DR PDBsum; 8FL4; -. DR PDBsum; 8FL6; -. DR PDBsum; 8FL7; -. DR PDBsum; 8FLA; -. DR PDBsum; 8FLB; -. DR PDBsum; 8FLD; -. DR PDBsum; 8FLE; -. DR PDBsum; 8INE; -. DR PDBsum; 8INF; -. DR PDBsum; 8IPX; -. DR PDBsum; 8IPY; -. DR PDBsum; 8IR3; -. DR AlphaFoldDB; O00541; -. DR EMDB; EMD-29252; -. DR EMDB; EMD-29253; -. DR EMDB; EMD-29254; -. DR EMDB; EMD-29255; -. DR EMDB; EMD-29256; -. DR EMDB; EMD-29257; -. DR EMDB; EMD-29258; -. DR EMDB; EMD-29259; -. DR EMDB; EMD-29260; -. DR EMDB; EMD-29261; -. DR EMDB; EMD-29262; -. DR EMDB; EMD-29265; -. DR EMDB; EMD-29266; -. DR EMDB; EMD-29267; -. DR EMDB; EMD-29268; -. DR EMDB; EMD-29269; -. DR EMDB; EMD-29272; -. DR EMDB; EMD-29273; -. DR EMDB; EMD-29275; -. DR EMDB; EMD-29276; -. DR EMDB; EMD-35596; -. DR EMDB; EMD-35597; -. DR EMDB; EMD-35649; -. DR EMDB; EMD-35651; -. DR EMDB; EMD-35673; -. DR SMR; O00541; -. DR BioGRID; 117040; 250. DR ComplexPortal; CPX-2846; PeBoW complex. DR CORUM; O00541; -. DR IntAct; O00541; 76. DR MINT; O00541; -. DR STRING; 9606.ENSP00000346725; -. DR GlyGen; O00541; 1 site, 1 O-linked glycan (1 site). DR iPTMnet; O00541; -. DR PhosphoSitePlus; O00541; -. DR SwissPalm; O00541; -. DR BioMuta; PES1; -. DR CPTAC; CPTAC-1171; -. DR CPTAC; CPTAC-1193; -. DR EPD; O00541; -. DR jPOST; O00541; -. DR MassIVE; O00541; -. DR MaxQB; O00541; -. DR PaxDb; 9606-ENSP00000346725; -. DR PeptideAtlas; O00541; -. DR ProteomicsDB; 47963; -. [O00541-1] DR ProteomicsDB; 47964; -. [O00541-2] DR Pumba; O00541; -. DR Antibodypedia; 10811; 288 antibodies from 33 providers. DR DNASU; 23481; -. DR Ensembl; ENST00000335214.8; ENSP00000334612.6; ENSG00000100029.18. [O00541-2] DR Ensembl; ENST00000354694.12; ENSP00000346725.6; ENSG00000100029.18. [O00541-1] DR GeneID; 23481; -. DR KEGG; hsa:23481; -. DR MANE-Select; ENST00000354694.12; ENSP00000346725.6; NM_014303.4; NP_055118.1. DR UCSC; uc003aij.2; human. [O00541-1] DR AGR; HGNC:8848; -. DR CTD; 23481; -. DR DisGeNET; 23481; -. DR GeneCards; PES1; -. DR HGNC; HGNC:8848; PES1. DR HPA; ENSG00000100029; Low tissue specificity. DR MIM; 605819; gene. DR neXtProt; NX_O00541; -. DR OpenTargets; ENSG00000100029; -. DR PharmGKB; PA33190; -. DR VEuPathDB; HostDB:ENSG00000100029; -. DR eggNOG; KOG2481; Eukaryota. DR GeneTree; ENSGT00390000002626; -. DR HOGENOM; CLU_019619_0_0_1; -. DR InParanoid; O00541; -. DR OMA; QKVTWIV; -. DR OrthoDB; 169151at2759; -. DR PhylomeDB; O00541; -. DR TreeFam; TF300671; -. DR PathwayCommons; O00541; -. DR Reactome; R-HSA-6791226; Major pathway of rRNA processing in the nucleolus and cytosol. DR SignaLink; O00541; -. DR SIGNOR; O00541; -. DR BioGRID-ORCS; 23481; 807 hits in 1156 CRISPR screens. DR ChiTaRS; PES1; human. DR EvolutionaryTrace; O00541; -. DR GeneWiki; PES1; -. DR GenomeRNAi; 23481; -. DR Pharos; O00541; Tbio. DR PRO; PR:O00541; -. DR Proteomes; UP000005640; Chromosome 22. DR RNAct; O00541; Protein. DR Bgee; ENSG00000100029; Expressed in sural nerve and 176 other cell types or tissues. DR ExpressionAtlas; O00541; baseline and differential. DR GO; GO:0005694; C:chromosome; IDA:HPA. DR GO; GO:0005829; C:cytosol; IDA:HPA. DR GO; GO:0016020; C:membrane; HDA:UniProtKB. DR GO; GO:0005730; C:nucleolus; IDA:HPA. DR GO; GO:0005654; C:nucleoplasm; IDA:HPA. DR GO; GO:0070545; C:PeBoW complex; IDA:UniProtKB. DR GO; GO:0030687; C:preribosome, large subunit precursor; IDA:UniProtKB. DR GO; GO:0043021; F:ribonucleoprotein complex binding; IEA:UniProtKB-UniRule. DR GO; GO:0003723; F:RNA binding; HDA:UniProtKB. DR GO; GO:0008283; P:cell population proliferation; IMP:MGI. DR GO; GO:0000466; P:maturation of 5.8S rRNA from tricistronic rRNA transcript (SSU-rRNA, 5.8S rRNA, LSU-rRNA); IMP:UniProtKB. DR GO; GO:0000463; P:maturation of LSU-rRNA from tricistronic rRNA transcript (SSU-rRNA, 5.8S rRNA, LSU-rRNA); IMP:UniProtKB. DR GO; GO:0051726; P:regulation of cell cycle; IMP:UniProtKB. DR GO; GO:0042273; P:ribosomal large subunit biogenesis; IC:UniProtKB. 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:SF8; 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 SWISS-2DPAGE; O00541; -. DR Genevisible; O00541; HS. PE 1: Evidence at protein level; KW 3D-structure; Acetylation; Alternative splicing; Chromosome; KW Isopeptide bond; Nucleus; Reference proteome; Ribosome biogenesis; KW rRNA processing; Ubl conjugation. FT CHAIN 1..588 FT /note="Pescadillo homolog" FT /id="PRO_0000186188" FT DOMAIN 322..415 FT /note="BRCT" FT /evidence="ECO:0000255|HAMAP-Rule:MF_03028" FT REGION 1..257 FT /note="Sufficient for nucleolar localization" FT REGION 1..54 FT /note="Required for 28S ribosomal RNA processing" FT REGION 294..314 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 306..415 FT /note="Sufficient for interaction with MAP1B" FT /evidence="ECO:0000250" FT REGION 448..515 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 539..588 FT /note="Required for 28S ribosomal RNA processing" FT REGION 565..588 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 454..488 FT /note="Acidic residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 489..515 FT /note="Basic and acidic residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT MOD_RES 98 FT /note="N6-acetyllysine" FT /evidence="ECO:0007744|PubMed:19608861" FT CROSSLNK 517 FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with FT G-Cter in SUMO1); alternate" FT /evidence="ECO:0007744|PubMed:25114211" FT CROSSLNK 517 FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with FT G-Cter in SUMO2); alternate" FT /evidence="ECO:0007744|PubMed:25114211, FT ECO:0007744|PubMed:28112733" FT VAR_SEQ 306..310 FT /note="Missing (in isoform 2)" FT /evidence="ECO:0000303|PubMed:15461802" FT /id="VSP_013023" FT VARIANT 264 FT /note="T -> S (in dbSNP:rs42942)" FT /id="VAR_034375" FT VARIANT 370 FT /note="D -> H (in dbSNP:rs11541876)" FT /id="VAR_053570" FT VARIANT 411 FT /note="A -> T (in dbSNP:rs34123894)" FT /id="VAR_053571" FT MUTAGEN 327 FT /note="F->R: Reduces incorporation into the PeBoW complex FT and nucleolar localization and impairs maturation of 28S FT ribosomal RNA." FT /evidence="ECO:0000269|PubMed:17189298" FT MUTAGEN 347 FT /note="I->R: Reduces incorporation into the PeBoW complex FT and nucleolar localization and impairs maturation of 28S FT ribosomal RNA." FT /evidence="ECO:0000269|PubMed:17189298" FT MUTAGEN 380 FT /note="R->W: Slightly impairs nucleolar localization." FT /evidence="ECO:0000269|PubMed:17189298" FT MUTAGEN 397 FT /note="W->R: Reduces incorporation into the PeBoW complex FT and nucleolar localization and impairs maturation of 28S FT ribosomal RNA." FT /evidence="ECO:0000269|PubMed:17189298" FT STRAND 331..333 FT /evidence="ECO:0007829|PDB:2EP8" FT STRAND 336..338 FT /evidence="ECO:0007829|PDB:2EP8" FT HELIX 340..349 FT /evidence="ECO:0007829|PDB:2EP8" FT STRAND 353..355 FT /evidence="ECO:0007829|PDB:2EP8" FT TURN 358..360 FT /evidence="ECO:0007829|PDB:2EP8" FT STRAND 375..377 FT /evidence="ECO:0007829|PDB:2EP8" FT TURN 381..383 FT /evidence="ECO:0007829|PDB:2EP8" FT STRAND 390..393 FT /evidence="ECO:0007829|PDB:2EP8" FT HELIX 396..404 FT /evidence="ECO:0007829|PDB:2EP8" FT TURN 410..412 FT /evidence="ECO:0007829|PDB:2EP8" SQ SEQUENCE 588 AA; 68003 MW; CB6201D6E34D82B1 CRC64; MGGLEKKKYE RGSATNYITR NKARKKLQLS LADFRRLCIL KGIYPHEPKH KKKVNKGSTA ARTFYLIKDI RFLLHEPIVN KFREYKVFVR KLRKAYGKSE WNTVERLKDN KPNYKLDHII KERYPTFIDA LRDLDDALSM CFLFSTFPRT GKCHVQTIQL CRRLTVEFMH YIIAARALRK VFLSIKGIYY QAEVLGQPIV WITPYAFSHD HPTDVDYRVM ATFTEFYTTL LGFVNFRLYQ LLNLHYPPKL EGQAQAEAKA GEGTYALDSE SCMEKLAALS ASLARVVVPA TEEEAEVDEF PTDGEMSAQE EDRRKELEAQ EKHKKLFEGL KFFLNREVPR EALAFIIRSF GGEVSWDKSL CIGATYDVTD SRITHQIVDR PGQQTSVIGR CYVQPQWVFD SVNARLLLPV AEYFSGVQLP PHLSPFVTEK EGDYVPPEKL KLLALQRGED PGNLNESEEE EEEDDNNEGD GDEEGENEEE EEDAEAGSEK EEEARLAALE EQRMEGKKPR VMAGTLKLED KQRLAQEEES EAKRLAIMMM KKREKYLYQK IMFGKRRKIR EANKLAEKRK AHDEAVRSEK KAKKARPE //