ID RRP5_HUMAN Reviewed; 1871 AA.
AC Q14690; Q2TA92; Q5W093; Q6P2J3; Q86VQ8; Q9H4P1;
DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT 17-APR-2007, sequence version 3.
DT 27-MAR-2024, entry version 206.
DE RecName: Full=Protein RRP5 homolog;
DE AltName: Full=NF-kappa-B-binding protein;
DE Short=NFBP;
DE AltName: Full=Programmed cell death protein 11;
GN Name=PDCD11; Synonyms=KIAA0185;
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 [LARGE SCALE MRNA], AND VARIANT PHE-1216.
RC TISSUE=Bone marrow;
RX PubMed=8724849; DOI=10.1093/dnares/3.1.17;
RA Nagase T., Seki N., Ishikawa K., Tanaka A., Nomura N.;
RT "Prediction of the coding sequences of unidentified human genes. V. The
RT coding sequences of 40 new genes (KIAA0161-KIAA0200) deduced by analysis of
RT cDNA clones from human cell line KG-1.";
RL DNA Res. 3:17-24(1996).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=15164054; DOI=10.1038/nature02462;
RA Deloukas P., Earthrowl M.E., Grafham D.V., Rubenfield M., French L.,
RA Steward C.A., Sims S.K., Jones M.C., Searle S., Scott C., Howe K.,
RA Hunt S.E., Andrews T.D., Gilbert J.G.R., Swarbreck D., Ashurst J.L.,
RA Taylor A., Battles J., Bird C.P., Ainscough R., Almeida J.P.,
RA Ashwell R.I.S., Ambrose K.D., Babbage A.K., Bagguley C.L., Bailey J.,
RA Banerjee R., Bates K., Beasley H., Bray-Allen S., Brown A.J., Brown J.Y.,
RA Burford D.C., Burrill W., Burton J., Cahill P., Camire D., Carter N.P.,
RA Chapman J.C., Clark S.Y., Clarke G., Clee C.M., Clegg S., Corby N.,
RA Coulson A., Dhami P., Dutta I., Dunn M., Faulkner L., Frankish A.,
RA Frankland J.A., Garner P., Garnett J., Gribble S., Griffiths C.,
RA Grocock R., Gustafson E., Hammond S., Harley J.L., Hart E., Heath P.D.,
RA Ho T.P., Hopkins B., Horne J., Howden P.J., Huckle E., Hynds C.,
RA Johnson C., Johnson D., Kana A., Kay M., Kimberley A.M., Kershaw J.K.,
RA Kokkinaki M., Laird G.K., Lawlor S., Lee H.M., Leongamornlert D.A.,
RA Laird G., Lloyd C., Lloyd D.M., Loveland J., Lovell J., McLaren S.,
RA McLay K.E., McMurray A., Mashreghi-Mohammadi M., Matthews L., Milne S.,
RA Nickerson T., Nguyen M., Overton-Larty E., Palmer S.A., Pearce A.V.,
RA Peck A.I., Pelan S., Phillimore B., Porter K., Rice C.M., Rogosin A.,
RA Ross M.T., Sarafidou T., Sehra H.K., Shownkeen R., Skuce C.D., Smith M.,
RA Standring L., Sycamore N., Tester J., Thorpe A., Torcasso W., Tracey A.,
RA Tromans A., Tsolas J., Wall M., Walsh J., Wang H., Weinstock K., West A.P.,
RA Willey D.L., Whitehead S.L., Wilming L., Wray P.W., Young L., Chen Y.,
RA Lovering R.C., Moschonas N.K., Siebert R., Fechtel K., Bentley D.,
RA Durbin R.M., Hubbard T., Doucette-Stamm L., Beck S., Smith D.R., Rogers J.;
RT "The DNA sequence and comparative analysis of human chromosome 10.";
RL Nature 429:375-381(2004).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M.,
RA Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J.,
RA Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S.,
RA Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H.,
RA Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K.,
RA Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D.,
RA Hunkapiller M.W., Myers E.W., Venter J.C.;
RL Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1-1442, AND VARIANT PHE-1216.
RC TISSUE=Lymphoma, and Uterus;
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 PROTEIN SEQUENCE OF 2-10 AND 1343-1352, CLEAVAGE OF INITIATOR METHIONINE,
RP ACETYLATION AT ALA-2, AND IDENTIFICATION BY MASS SPECTROMETRY.
RC TISSUE=Mammary carcinoma;
RA Bienvenut W.V., Matallanas D., Kolch W.;
RL Submitted (JUL-2009) to UniProtKB.
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1508-1871, AND VARIANT ALA-1871.
RC TISSUE=Brain;
RA Zhou J., Yu W., Tang H., Mei G., Tsang Y.T.M., Bouck J., Gibbs R.A.,
RA Margolin J.F.;
RL Submitted (JUL-2000) to the EMBL/GenBank/DDBJ databases.
RN [7]
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 [8]
RP INTERACTION WITH NFKB1 AND RELA, AND SUBCELLULAR LOCATION.
RX PubMed=14624448; DOI=10.1002/jcb.10701;
RA Sweet T., Khalili K., Sawaya B.E., Amini S.;
RT "Identification of a novel protein from glial cells based on its ability to
RT interact with NF-kappaB subunits.";
RL J. Cell. Biochem. 90:884-891(2003).
RN [9]
RP FUNCTION, AND SUBCELLULAR LOCATION.
RX PubMed=17654514; DOI=10.1002/jcp.21204;
RA Sweet T., Yen W., Khalili K., Amini S.;
RT "Evidence for involvement of NFBP in processing of ribosomal RNA.";
RL J. Cell. Physiol. 214:381-388(2008).
RN [10]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1498, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=18691976; DOI=10.1016/j.molcel.2008.07.007;
RA Daub H., Olsen J.V., Bairlein M., Gnad F., Oppermann F.S., Korner R.,
RA Greff Z., Keri G., Stemmann O., Mann M.;
RT "Kinase-selective enrichment enables quantitative phosphoproteomics of the
RT kinome across the cell cycle.";
RL Mol. Cell 31:438-448(2008).
RN [11]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1493 AND SER-1498, AND
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 [12]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, CLEAVAGE OF INITIATOR
RP METHIONINE [LARGE SCALE ANALYSIS], AND IDENTIFICATION BY MASS SPECTROMETRY
RP [LARGE SCALE ANALYSIS].
RX PubMed=19413330; DOI=10.1021/ac9004309;
RA Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J., Mohammed S.;
RT "Lys-N and trypsin cover complementary parts of the phosphoproteome in a
RT refined SCX-based approach.";
RL Anal. Chem. 81:4493-4501(2009).
RN [13]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Leukemic T-cell;
RX PubMed=19690332; DOI=10.1126/scisignal.2000007;
RA Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K.,
RA Rodionov V., Han D.K.;
RT "Quantitative phosphoproteomic analysis of T cell receptor signaling
RT reveals system-wide modulation of protein-protein interactions.";
RL Sci. Signal. 2:RA46-RA46(2009).
RN [14]
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 [15]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1360 AND SER-1362, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=21406692; DOI=10.1126/scisignal.2001570;
RA Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J., Johansen P.T.,
RA Kratchmarova I., Kassem M., Mann M., Olsen J.V., Blagoev B.;
RT "System-wide temporal characterization of the proteome and phosphoproteome
RT of human embryonic stem cell differentiation.";
RL Sci. Signal. 4:RS3-RS3(2011).
RN [16]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, CLEAVAGE OF INITIATOR
RP METHIONINE [LARGE SCALE ANALYSIS], AND IDENTIFICATION BY MASS SPECTROMETRY
RP [LARGE SCALE ANALYSIS].
RX PubMed=22223895; DOI=10.1074/mcp.m111.015131;
RA Bienvenut W.V., Sumpton D., Martinez A., Lilla S., Espagne C., Meinnel T.,
RA Giglione C.;
RT "Comparative large-scale characterisation of plant vs. mammal proteins
RT reveals similar and idiosyncratic N-alpha acetylation features.";
RL Mol. Cell. Proteomics 11:M111.015131-M111.015131(2012).
RN [17]
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 [18]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-7; SER-438 AND SER-1498, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma, and Erythroleukemia;
RX PubMed=23186163; DOI=10.1021/pr300630k;
RA Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J.,
RA Mohammed S.;
RT "Toward a comprehensive characterization of a human cancer cell
RT phosphoproteome.";
RL J. Proteome Res. 12:260-271(2013).
RN [19]
RP SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-1030, 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 [20]
RP SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-1416, 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 [21]
RP STRUCTURE BY NMR OF 173-278.
RG RIKEN structural genomics initiative (RSGI);
RT "Solution structure of the S1 RNA binding domain from human hypothetical
RT protein BAA11502.";
RL Submitted (NOV-2004) to the PDB data bank.
RN [22]
RP VARIANT GLU-45.
RX PubMed=26566883; DOI=10.1136/jmedgenet-2015-103179;
RA Rafiullah R., Aslamkhan M., Paramasivam N., Thiel C., Mustafa G.,
RA Wiemann S., Schlesner M., Wade R.C., Rappold G.A., Berkel S.;
RT "Homozygous missense mutation in the LMAN2L gene segregates with
RT intellectual disability in a large consanguineous Pakistani family.";
RL J. Med. Genet. 53:138-144(2016).
CC -!- FUNCTION: Essential for the generation of mature 18S rRNA, specifically
CC necessary for cleavages at sites A0, 1 and 2 of the 47S precursor.
CC Directly interacts with U3 snoRNA. {ECO:0000269|PubMed:17654514}.
CC -!- FUNCTION: Involved in the biogenesis of rRNA. {ECO:0000250}.
CC -!- SUBUNIT: Interacts with NF-kappa-B p50/NFKB1 and NF-kappa-B p65/RELA.
CC {ECO:0000269|PubMed:14624448}.
CC -!- INTERACTION:
CC Q14690; P19838: NFKB1; NbExp=2; IntAct=EBI-300028, EBI-300010;
CC -!- SUBCELLULAR LOCATION: Nucleus, nucleolus {ECO:0000269|PubMed:12429849,
CC ECO:0000269|PubMed:14624448, ECO:0000269|PubMed:17654514}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAG01992.1; Type=Erroneous translation; Note=Wrong choice of frame.; Evidence={ECO:0000305};
CC Sequence=AAH49838.1; Type=Miscellaneous discrepancy; Note=Contaminating sequence. Potential poly-A sequence.; Evidence={ECO:0000305};
CC Sequence=AAH64486.1; Type=Miscellaneous discrepancy; Note=Contaminating sequence. Potential poly-A sequence.; Evidence={ECO:0000305};
CC Sequence=AAH80560.1; Type=Miscellaneous discrepancy; Note=Contaminating sequence. Potential poly-A sequence.; Evidence={ECO:0000305};
CC Sequence=AAI11041.1; Type=Miscellaneous discrepancy; Note=Contaminating sequence. Potential poly-A sequence.; Evidence={ECO:0000305};
CC Sequence=BAA11502.1; Type=Erroneous initiation; Evidence={ECO:0000305};
CC Sequence=BAA11502.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
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DR EMBL; D80007; BAA11502.1; ALT_INIT; mRNA.
DR EMBL; AL139339; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AL591408; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AL603983; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH471066; EAW49641.1; -; Genomic_DNA.
DR EMBL; BC049838; AAH49838.1; ALT_SEQ; mRNA.
DR EMBL; BC064486; AAH64486.1; ALT_SEQ; mRNA.
DR EMBL; BC080560; AAH80560.1; ALT_SEQ; mRNA.
DR EMBL; BC111040; AAI11041.1; ALT_SEQ; mRNA.
DR EMBL; AY007124; AAG01992.1; ALT_SEQ; mRNA.
DR CCDS; CCDS31276.1; -.
DR RefSeq; NP_055791.1; NM_014976.1.
DR RefSeq; XP_011537841.1; XM_011539539.2.
DR PDB; 1WI5; NMR; -; A=173-278.
DR PDBsum; 1WI5; -.
DR AlphaFoldDB; Q14690; -.
DR SMR; Q14690; -.
DR BioGRID; 116633; 396.
DR IntAct; Q14690; 83.
DR MINT; Q14690; -.
DR STRING; 9606.ENSP00000358812; -.
DR GlyGen; Q14690; 1 site, 1 O-linked glycan (1 site).
DR iPTMnet; Q14690; -.
DR PhosphoSitePlus; Q14690; -.
DR SwissPalm; Q14690; -.
DR BioMuta; PDCD11; -.
DR DMDM; 145559523; -.
DR SWISS-2DPAGE; Q14690; -.
DR CPTAC; CPTAC-1635; -.
DR EPD; Q14690; -.
DR jPOST; Q14690; -.
DR MassIVE; Q14690; -.
DR MaxQB; Q14690; -.
DR PaxDb; 9606-ENSP00000358812; -.
DR PeptideAtlas; Q14690; -.
DR ProteomicsDB; 60128; -.
DR Pumba; Q14690; -.
DR Antibodypedia; 31534; 50 antibodies from 16 providers.
DR DNASU; 22984; -.
DR Ensembl; ENST00000369797.8; ENSP00000358812.3; ENSG00000148843.15.
DR GeneID; 22984; -.
DR KEGG; hsa:22984; -.
DR MANE-Select; ENST00000369797.8; ENSP00000358812.3; NM_014976.2; NP_055791.1.
DR UCSC; uc001kwy.2; human.
DR AGR; HGNC:13408; -.
DR CTD; 22984; -.
DR DisGeNET; 22984; -.
DR GeneCards; PDCD11; -.
DR HGNC; HGNC:13408; PDCD11.
DR HPA; ENSG00000148843; Low tissue specificity.
DR MIM; 612333; gene.
DR neXtProt; NX_Q14690; -.
DR OpenTargets; ENSG00000148843; -.
DR PharmGKB; PA134909758; -.
DR VEuPathDB; HostDB:ENSG00000148843; -.
DR eggNOG; KOG1070; Eukaryota.
DR GeneTree; ENSGT00390000012228; -.
DR HOGENOM; CLU_000845_1_1_1; -.
DR InParanoid; Q14690; -.
DR OrthoDB; 167902at2759; -.
DR PhylomeDB; Q14690; -.
DR TreeFam; TF105697; -.
DR PathwayCommons; Q14690; -.
DR Reactome; R-HSA-6790901; rRNA modification in the nucleus and cytosol.
DR Reactome; R-HSA-6791226; Major pathway of rRNA processing in the nucleolus and cytosol.
DR SignaLink; Q14690; -.
DR BioGRID-ORCS; 22984; 749 hits in 1165 CRISPR screens.
DR ChiTaRS; PDCD11; human.
DR EvolutionaryTrace; Q14690; -.
DR GenomeRNAi; 22984; -.
DR Pharos; Q14690; Tbio.
DR PRO; PR:Q14690; -.
DR Proteomes; UP000005640; Chromosome 10.
DR RNAct; Q14690; Protein.
DR Bgee; ENSG00000148843; Expressed in primordial germ cell in gonad and 188 other cell types or tissues.
DR ExpressionAtlas; Q14690; baseline and differential.
DR Genevisible; Q14690; HS.
DR GO; GO:0005829; C:cytosol; IEA:Ensembl.
DR GO; GO:0005730; C:nucleolus; IBA:GO_Central.
DR GO; GO:0005654; C:nucleoplasm; TAS:Reactome.
DR GO; GO:0005634; C:nucleus; IDA:UniProtKB.
DR GO; GO:0032040; C:small-subunit processome; IBA:GO_Central.
DR GO; GO:0051059; F:NF-kappaB binding; IPI:UniProtKB.
DR GO; GO:0003723; F:RNA binding; HDA:UniProtKB.
DR GO; GO:0006364; P:rRNA processing; IEA:UniProtKB-KW.
DR CDD; cd05701; S1_Rrp5_repeat_hs10; 1.
DR CDD; cd05702; S1_Rrp5_repeat_hs11_sc8; 1.
DR CDD; cd05703; S1_Rrp5_repeat_hs12_sc9; 1.
DR CDD; cd05704; S1_Rrp5_repeat_hs13; 1.
DR CDD; cd05705; S1_Rrp5_repeat_hs14; 1.
DR CDD; cd05693; S1_Rrp5_repeat_hs1_sc1; 1.
DR CDD; cd05694; S1_Rrp5_repeat_hs2_sc2; 1.
DR CDD; cd05695; S1_Rrp5_repeat_hs3; 1.
DR CDD; cd05696; S1_Rrp5_repeat_hs4; 1.
DR CDD; cd05697; S1_Rrp5_repeat_hs5; 1.
DR CDD; cd05698; S1_Rrp5_repeat_hs6_sc5; 1.
DR CDD; cd05699; S1_Rrp5_repeat_hs7; 1.
DR CDD; cd04461; S1_Rrp5_repeat_hs8_sc7; 1.
DR Gene3D; 2.40.50.140; Nucleic acid-binding proteins; 8.
DR Gene3D; 1.25.40.10; Tetratricopeptide repeat domain; 1.
DR InterPro; IPR003107; HAT.
DR InterPro; IPR012340; NA-bd_OB-fold.
DR InterPro; IPR045209; Rrp5.
DR InterPro; IPR048058; Rrp5_S1_rpt_hs11_sc8.
DR InterPro; IPR048059; Rrp5_S1_rpt_hs1_sc1.
DR InterPro; IPR003029; S1_domain.
DR InterPro; IPR008847; Suf.
DR InterPro; IPR011990; TPR-like_helical_dom_sf.
DR PANTHER; PTHR23270; PROGRAMMED CELL DEATH PROTEIN 11 PRE-RRNA PROCESSING PROTEIN RRP5; 1.
DR PANTHER; PTHR23270:SF10; PROTEIN RRP5 HOMOLOG; 1.
DR Pfam; PF00575; S1; 4.
DR Pfam; PF05843; Suf; 1.
DR SMART; SM00386; HAT; 7.
DR SMART; SM00316; S1; 13.
DR SUPFAM; SSF50249; Nucleic acid-binding proteins; 11.
DR SUPFAM; SSF48452; TPR-like; 2.
DR PROSITE; PS50126; S1; 12.
PE 1: Evidence at protein level;
KW 3D-structure; Acetylation; Direct protein sequencing; Isopeptide bond;
KW Nucleus; Phosphoprotein; Reference proteome; Repeat; rRNA processing;
KW Ubl conjugation.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000269|Ref.5, ECO:0007744|PubMed:19413330,
FT ECO:0007744|PubMed:22223895"
FT CHAIN 2..1871
FT /note="Protein RRP5 homolog"
FT /id="PRO_0000205762"
FT DOMAIN 83..171
FT /note="S1 motif 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00180"
FT DOMAIN 187..258
FT /note="S1 motif 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00180"
FT DOMAIN 281..346
FT /note="S1 motif 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00180"
FT DOMAIN 365..436
FT /note="S1 motif 4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00180"
FT DOMAIN 453..522
FT /note="S1 motif 5"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00180"
FT DOMAIN 542..611
FT /note="S1 motif 6"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00180"
FT DOMAIN 636..707
FT /note="S1 motif 7"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00180"
FT DOMAIN 729..798
FT /note="S1 motif 8"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00180"
FT DOMAIN 1036..1109
FT /note="S1 motif 9"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00180"
FT DOMAIN 1149..1222
FT /note="S1 motif 10"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00180"
FT DOMAIN 1230..1298
FT /note="S1 motif 11"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00180"
FT DOMAIN 1324..1396
FT /note="S1 motif 12"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00180"
FT REPEAT 1599..1631
FT /note="HAT 1"
FT REPEAT 1705..1737
FT /note="HAT 2"
FT REPEAT 1775..1807
FT /note="HAT 3"
FT REPEAT 1809..1844
FT /note="HAT 4"
FT REGION 1..62
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 998..1018
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1395..1531
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1549..1586
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 10..24
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1414..1456
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1467..1526
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1557..1586
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 2
FT /note="N-acetylalanine"
FT /evidence="ECO:0000269|Ref.5, ECO:0007744|PubMed:19413330,
FT ECO:0007744|PubMed:22223895"
FT MOD_RES 7
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 438
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 1360
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21406692"
FT MOD_RES 1362
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21406692"
FT MOD_RES 1476
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q6NS46"
FT MOD_RES 1493
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648"
FT MOD_RES 1498
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648,
FT ECO:0007744|PubMed:18691976, ECO:0007744|PubMed:23186163"
FT CROSSLNK 1030
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO1)"
FT /evidence="ECO:0007744|PubMed:25114211"
FT CROSSLNK 1416
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:28112733"
FT VARIANT 45
FT /note="K -> E (in dbSNP:rs150893869)"
FT /evidence="ECO:0000269|PubMed:26566883"
FT /id="VAR_076436"
FT VARIANT 397
FT /note="S -> N (in dbSNP:rs7074814)"
FT /id="VAR_054485"
FT VARIANT 623
FT /note="A -> S (in dbSNP:rs11598673)"
FT /id="VAR_031669"
FT VARIANT 780
FT /note="A -> S (in dbSNP:rs11591914)"
FT /id="VAR_054486"
FT VARIANT 1216
FT /note="L -> F (in dbSNP:rs2986014)"
FT /evidence="ECO:0000269|PubMed:15489334,
FT ECO:0000269|PubMed:8724849"
FT /id="VAR_031670"
FT VARIANT 1453
FT /note="P -> S (in dbSNP:rs2274289)"
FT /id="VAR_054487"
FT VARIANT 1871
FT /note="D -> A (in dbSNP:rs7831)"
FT /evidence="ECO:0000269|Ref.6"
FT /id="VAR_014930"
FT CONFLICT 1431
FT /note="Missing (in Ref. 4; AAH49838)"
FT /evidence="ECO:0000305"
FT TURN 181..183
FT /evidence="ECO:0007829|PDB:1WI5"
FT STRAND 189..197
FT /evidence="ECO:0007829|PDB:1WI5"
FT STRAND 199..205
FT /evidence="ECO:0007829|PDB:1WI5"
FT STRAND 212..216
FT /evidence="ECO:0007829|PDB:1WI5"
FT HELIX 217..227
FT /evidence="ECO:0007829|PDB:1WI5"
FT STRAND 228..230
FT /evidence="ECO:0007829|PDB:1WI5"
FT STRAND 238..245
FT /evidence="ECO:0007829|PDB:1WI5"
FT STRAND 252..256
FT /evidence="ECO:0007829|PDB:1WI5"
SQ SEQUENCE 1871 AA; 208701 MW; 8ED3665EB503CBB0 CRC64;
MANLEESFPR GGTRKIHKPE KAFQQSVEQD NLFDISTEEG STKRKKSQKG PAKTKKLKIE
KRESSKSARE KFEILSVESL CEGMRILGCV KEVNELELVI SLPNGLQGFV QVTEICDAYT
KKLNEQVTQE QPLKDLLHLP ELFSPGMLVR CVVSSLGITD RGKKSVKLSL NPKNVNRVLS
AEALKPGMLL TGTVSSLEDH GYLVDIGVDG TRAFLPLLKA QEYIRQKNKG AKLKVGQYLN
CIVEKVKGNG GVVSLSVGHS EVSTAIATEQ QSWNLNNLLP GLVVKAQVQK VTPFGLTLNF
LTFFTGVVDF MHLDPKKAGT YFSNQAVRAC ILCVHPRTRV VHLSLRPIFL QPGRPLTRLS
CQNLGAVLDD VPVQGFFKKA GATFRLKDGV LAYARLSHLS DSKNVFNPEA FKPGNTHKCR
IIDYSQMDEL ALLSLRTSII EAQYLRYHDI EPGAVVKGTV LTIKSYGMLV KVGEQMRGLV
PPMHLADILM KNPEKKYHIG DEVKCRVLLC DPEAKKLMMT LKKTLIESKL PVITCYADAK
PGLQTHGFII RVKDYGCIVK FYNNVQGLVP KHELSTEYIP DPERVFYTGQ VVKVVVLNCE
PSKERMLLSF KLSSDPEPKK EPAGHSQKKG KAINIGQLVD VKVLEKTKDG LEVAVLPHNI
RAFLPTSHLS DHVANGPLLH HWLQAGDILH RVLCLSQSEG RVLLCRKPAL VSTVEGGQDP
KNFSEIHPGM LLIGFVKSIK DYGVFIQFPS GLSGLAPKAI MSDKFVTSTS DHFVEGQTVA
AKVTNVDEEK QRMLLSLRLS DCGLGDLAIT SLLLLNQCLE ELQGVRSLMS NRDSVLIQTL
AEMTPGMFLD LVVQEVLEDG SVVFSGGPVP DLVLKASRYH RAGQEVESGQ KKKVVILNVD
LLKLEVHVSL HQDLVNRKAR KLRKGSEHQA IVQHLEKSFA IASLVETGHL AAFSLTSHLN
DTFRFDSEKL QVGQGVSLTL KTTEPGVTGL LLAVEGPAAK RTMRPTQKDS ETVDEDEEVD
PALTVGTIKK HTLSIGDMVT GTVKSIKPTH VVVTLEDGII GCIHASHILD DVPEGTSPTT
KLKVGKTVTA RVIGGRDMKT FKYLPISHPR FVRTIPELSV RPSELEDGHT ALNTHSVSPM
EKIKQYQAGQ TVTCFLKKYN VVKKWLEVEI APDIRGRIPL LLTSLSFKVL KHPDKKFRVG
QALRATVVGP DSSKTLLCLS LTGPHKLEEG EVAMGRVVKV TPNEGLTVSF PFGKIGTVSI
FHMSDSYSET PLEDFVPQKV VRCYILSTAD NVLTLSLRSS RTNPETKSKV EDPEINSIQD
IKEGQLLRGY VGSIQPHGVF FRLGPSVVGL ARYSHVSQHS PSKKALYNKH LPEGKLLTAR
VLRLNHQKNL VELSFLPGDT GKPDVLSASL EGQLTKQEER KTEAEERDQK GEKKNQKRNE
KKNQKGQEEV EMPSKEKQQP QKPQAQKRGG RECRESGSEQ ERVSKKPKKA GLSEEDDSLV
DVYYREGKEE AEETNVLPKE KQTKPAEAPR LQLSSGFAWN VGLDSLTPAL PPLAESSDSE
EDEKPHQATI KKSKKERELE KQKAEKELSR IEEALMDPGR QPESADDFDR LVLSSPNSSI
LWLQYMAFHL QATEIEKARA VAERALKTIS FREEQEKLNV WVALLNLENM YGSQESLTKV
FERAVQYNEP LKVFLHLADI YAKSEKFQEA GELYNRMLKR FRQEKAVWIK YGAFLLRRSQ
AAASHRVLQR ALECLPSKEH VDVIAKFAQL EFQLGDAERA KAIFENTLST YPKRTDVWSV
YIDMTIKHGS QKDVRDIFER VIHLSLAPKR MKFFFKRYLD YEKQHGTEKD VQAVKAKALE
YVEAKSSVLE D
//
