RRS1_HUMAN
ID RRS1_HUMAN Reviewed; 365 AA.
AC Q15050; Q9BUX8;
DT 15-JUL-1998, integrated into UniProtKB/Swiss-Prot.
DT 06-JUN-2002, sequence version 2.
DT 03-AUG-2022, entry version 186.
DE RecName: Full=Ribosome biogenesis regulatory protein homolog;
GN Name=RRS1; Synonyms=KIAA0112, RRR;
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].
RC TISSUE=Bone marrow;
RX PubMed=7788527; DOI=10.1093/dnares/2.1.37;
RA Nagase T., Miyajima N., Tanaka A., Sazuka T., Seki N., Sato S., Tabata S.,
RA Ishikawa K., Kawarabayasi Y., Kotani H., Nomura N.;
RT "Prediction of the coding sequences of unidentified human genes. III. The
RT coding sequences of 40 new genes (KIAA0081-KIAA0120) deduced by analysis of
RT cDNA clones from human cell line KG-1.";
RL DNA Res. 2:37-43(1995).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Lung, 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 [3]
RP PROTEIN SEQUENCE OF 1-12; 92-98; 129-141; 254-265; 267-273 AND 342-352,
RP ACETYLATION AT MET-1, SUBCELLULAR LOCATION, AND IDENTIFICATION BY MASS
RP SPECTROMETRY.
RC TISSUE=Cervix carcinoma;
RA Bienvenut W.V.;
RL Submitted (AUG-2005) to UniProtKB.
RN [4]
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 [5]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT MET-1, AND IDENTIFICATION BY MASS
RP SPECTROMETRY [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 [6]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT MET-1, AND IDENTIFICATION BY MASS
RP SPECTROMETRY [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 [7]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT MET-1, AND IDENTIFICATION BY MASS
RP 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 [8]
RP FUNCTION.
RX PubMed=24120868; DOI=10.1016/j.celrep.2013.08.049;
RA Sloan K.E., Bohnsack M.T., Watkins N.J.;
RT "The 5S RNP couples p53 homeostasis to ribosome biogenesis and nucleolar
RT stress.";
RL Cell Rep. 5:237-247(2013).
RN [9]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-5, AND IDENTIFICATION BY MASS
RP 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 [10]
RP SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-154; LYS-226 AND LYS-266, AND
RP IDENTIFICATION BY MASS 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).
CC -!- FUNCTION: Involved in ribosomal large subunit assembly. May regulate
CC the localization of the 5S RNP/5S ribonucleoprotein particle to the
CC nucleolus. {ECO:0000269|PubMed:24120868}.
CC -!- INTERACTION:
CC Q15050; Q92624: APPBP2; NbExp=7; IntAct=EBI-749186, EBI-743771;
CC Q15050; Q9H7B2: RPF2; NbExp=2; IntAct=EBI-749186, EBI-1051960;
CC Q15050; O00560: SDCBP; NbExp=3; IntAct=EBI-749186, EBI-727004;
CC -!- SUBCELLULAR LOCATION: Nucleus, nucleolus {ECO:0000269|PubMed:12429849,
CC ECO:0000269|Ref.3}.
CC -!- PTM: Citrullinated by PADI4. {ECO:0000250|UniProtKB:Q9CYH6}.
CC -!- SIMILARITY: Belongs to the RRS1 family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAA04948.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; D25218; BAA04948.1; ALT_INIT; mRNA.
DR EMBL; BC001811; AAH01811.1; -; mRNA.
DR EMBL; BC013043; AAH13043.1; -; mRNA.
DR CCDS; CCDS6189.1; -.
DR RefSeq; NP_055984.1; NM_015169.3.
DR AlphaFoldDB; Q15050; -.
DR SMR; Q15050; -.
DR BioGRID; 116819; 446.
DR IntAct; Q15050; 149.
DR MINT; Q15050; -.
DR STRING; 9606.ENSP00000322396; -.
DR GlyGen; Q15050; 1 site, 1 O-linked glycan (1 site).
DR iPTMnet; Q15050; -.
DR PhosphoSitePlus; Q15050; -.
DR SwissPalm; Q15050; -.
DR BioMuta; RRS1; -.
DR DMDM; 21431847; -.
DR SWISS-2DPAGE; Q15050; -.
DR EPD; Q15050; -.
DR jPOST; Q15050; -.
DR MassIVE; Q15050; -.
DR MaxQB; Q15050; -.
DR PaxDb; Q15050; -.
DR PeptideAtlas; Q15050; -.
DR PRIDE; Q15050; -.
DR ProteomicsDB; 60402; -.
DR TopDownProteomics; Q15050; -.
DR Antibodypedia; 24827; 197 antibodies from 27 providers.
DR DNASU; 23212; -.
DR Ensembl; ENST00000320270.4; ENSP00000322396.2; ENSG00000179041.4.
DR GeneID; 23212; -.
DR KEGG; hsa:23212; -.
DR MANE-Select; ENST00000320270.4; ENSP00000322396.2; NM_015169.4; NP_055984.1.
DR UCSC; uc003xwa.3; human.
DR CTD; 23212; -.
DR DisGeNET; 23212; -.
DR GeneCards; RRS1; -.
DR HGNC; HGNC:17083; RRS1.
DR HPA; ENSG00000179041; Low tissue specificity.
DR MIM; 618311; gene.
DR neXtProt; NX_Q15050; -.
DR OpenTargets; ENSG00000179041; -.
DR PharmGKB; PA134993138; -.
DR VEuPathDB; HostDB:ENSG00000179041; -.
DR eggNOG; KOG1765; Eukaryota.
DR GeneTree; ENSGT00390000005213; -.
DR HOGENOM; CLU_065163_1_0_1; -.
DR InParanoid; Q15050; -.
DR OMA; LLINEIW; -.
DR OrthoDB; 1264304at2759; -.
DR PhylomeDB; Q15050; -.
DR TreeFam; TF313067; -.
DR PathwayCommons; Q15050; -.
DR SignaLink; Q15050; -.
DR BioGRID-ORCS; 23212; 748 hits in 1082 CRISPR screens.
DR GeneWiki; RRS1; -.
DR GenomeRNAi; 23212; -.
DR Pharos; Q15050; Tbio.
DR PRO; PR:Q15050; -.
DR Proteomes; UP000005640; Chromosome 8.
DR RNAct; Q15050; protein.
DR Bgee; ENSG00000179041; Expressed in gastrocnemius and 114 other tissues.
DR Genevisible; Q15050; HS.
DR GO; GO:0000794; C:condensed nuclear chromosome; IDA:UniProtKB.
DR GO; GO:0005783; C:endoplasmic reticulum; IEA:Ensembl.
DR GO; GO:0005730; C:nucleolus; IDA:UniProtKB.
DR GO; GO:0005654; C:nucleoplasm; IDA:HPA.
DR GO; GO:0030687; C:preribosome, large subunit precursor; IBA:GO_Central.
DR GO; GO:0008097; F:5S rRNA binding; IDA:UniProtKB.
DR GO; GO:0003723; F:RNA binding; HDA:UniProtKB.
DR GO; GO:0000447; P:endonucleolytic cleavage in ITS1 to separate SSU-rRNA from 5.8S rRNA and LSU-rRNA from tricistronic rRNA transcript (SSU-rRNA, 5.8S rRNA, LSU-rRNA); IBA:GO_Central.
DR GO; GO:0002244; P:hematopoietic progenitor cell differentiation; IEA:Ensembl.
DR GO; GO:0007080; P:mitotic metaphase plate congression; IMP:UniProtKB.
DR GO; GO:1902570; P:protein localization to nucleolus; IMP:UniProtKB.
DR GO; GO:1901796; P:regulation of signal transduction by p53 class mediator; IMP:UniProtKB.
DR GO; GO:0000027; P:ribosomal large subunit assembly; IMP:UniProtKB.
DR GO; GO:0042273; P:ribosomal large subunit biogenesis; IMP:UniProtKB.
DR GO; GO:0000055; P:ribosomal large subunit export from nucleus; IBA:GO_Central.
DR InterPro; IPR007023; Ribosom_reg.
DR PANTHER; PTHR17602; PTHR17602; 1.
DR Pfam; PF04939; RRS1; 1.
PE 1: Evidence at protein level;
KW Acetylation; Citrullination; Direct protein sequencing; Isopeptide bond;
KW Nucleus; Phosphoprotein; Reference proteome; Ribosome biogenesis;
KW Ubl conjugation.
FT CHAIN 1..365
FT /note="Ribosome biogenesis regulatory protein homolog"
FT /id="PRO_0000185374"
FT REGION 233..253
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 280..365
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 288..305
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 1
FT /note="N-acetylmethionine"
FT /evidence="ECO:0000269|Ref.3, ECO:0007744|PubMed:19413330,
FT ECO:0007744|PubMed:22223895, ECO:0007744|PubMed:22814378"
FT MOD_RES 5
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 273
FT /note="Citrulline"
FT /evidence="ECO:0000250|UniProtKB:Q9CYH6"
FT CROSSLNK 154
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:28112733"
FT CROSSLNK 226
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:28112733"
FT CROSSLNK 266
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:28112733"
FT VARIANT 116
FT /note="Q -> H (in dbSNP:rs34077648)"
FT /id="VAR_051887"
FT VARIANT 126
FT /note="K -> R (in dbSNP:rs3739335)"
FT /id="VAR_051888"
FT VARIANT 191
FT /note="R -> L (in dbSNP:rs3739336)"
FT /id="VAR_020484"
SQ SEQUENCE 365 AA; 41193 MW; 061C3A6174C2E7C2 CRC64;
MEGQSVEELL AKAEQDEAEK LQRITVHKEL ELQFDLGNLL ASDRNPPTGL RCAGPTPEAE
LQALARDNTQ LLINQLWQLP TERVEEAIVA RLPEPTTRLP REKPLPRPRP LTRWQQFARL
KGIRPKKKTN LVWDEVSGQW RRRWGYQRAR DDTKEWLIEV PGNADPLEDQ FAKRIQAKKE
RVAKNELNRL RNLARAHKMQ LPSAAGLHPT GHQSKEELGR AMQVAKVSTA SVGRFQERLP
KEKVPRGSGK KRKFQPLFGD FAAEKKNQLE LLRVMNSKKP QLDVTRATNK QMREEDQEEA
AKRRKMSQKG KRKGGRQGPG GKRKGGPPSQ GGKRKGGLGG KMNSGPPGLG GKRKGGQRPG
GKRRK
