PESC_HUMAN
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 03-AUG-2022, entry version 192.
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}.
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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 PDBsum; 2EP8; -.
DR AlphaFoldDB; O00541; -.
DR SMR; O00541; -.
DR BioGRID; 117040; 210.
DR CORUM; O00541; -.
DR IntAct; O00541; 71.
DR MINT; O00541; -.
DR STRING; 9606.ENSP00000346725; -.
DR iPTMnet; O00541; -.
DR PhosphoSitePlus; O00541; -.
DR SwissPalm; O00541; -.
DR BioMuta; PES1; -.
DR SWISS-2DPAGE; O00541; -.
DR CPTAC; CPTAC-1171; -.
DR CPTAC; CPTAC-1193; -.
DR EPD; O00541; -.
DR jPOST; O00541; -.
DR MassIVE; O00541; -.
DR MaxQB; O00541; -.
DR PaxDb; O00541; -.
DR PeptideAtlas; O00541; -.
DR PRIDE; O00541; -.
DR ProteomicsDB; 47963; -. [O00541-1]
DR ProteomicsDB; 47964; -. [O00541-2]
DR Antibodypedia; 10811; 274 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 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; TWIVPHY; -.
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; 770 hits in 1064 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 174 other tissues.
DR ExpressionAtlas; O00541; baseline and differential.
DR Genevisible; O00541; HS.
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:UniProtKB.
DR GO; GO:0005654; C:nucleoplasm; IDA:UniProtKB.
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 Gene3D; 3.40.50.10190; -; 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; PTHR12221; 1.
DR Pfam; PF16589; BRCT_2; 1.
DR Pfam; PF06732; Pescadillo_N; 1.
DR SMART; SM00292; BRCT; 1.
DR SUPFAM; SSF52113; SSF52113; 1.
DR PROSITE; PS50172; BRCT; 1.
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
