ID   AROS_HUMAN              Reviewed;         136 AA.
AC   Q86WX3; B0QY96; Q5JZA1;
DT   17-OCT-2006, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-2003, sequence version 1.
DT   05-FEB-2025, entry version 150.
DE   RecName: Full=Active regulator of SIRT1;
DE   AltName: Full=40S ribosomal protein S19-binding protein 1;
DE            Short=RPS19-binding protein 1;
DE            Short=S19BP;
GN   Name=RPS19BP1 {ECO:0000312|HGNC:HGNC:28749};
GN   Synonyms=AROS {ECO:0000303|PubMed:34516797};
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].
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   [2]
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   [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 (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN   [4]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Mammary gland, and Skin;
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   FUNCTION, SUBCELLULAR LOCATION, TISSUE SPECIFICITY, AND INTERACTION WITH
RP   SIRT1.
RX   PubMed=17964266; DOI=10.1016/j.molcel.2007.08.030;
RA   Kim E.-J., Kho J.-H., Kang M.-R., Um S.-J.;
RT   "Active regulator of SIRT1 cooperates with SIRT1 and facilitates
RT   suppression of p53 activity.";
RL   Mol. Cell 28:277-290(2007).
RN   [6]
RP   ERRATUM OF PUBMED:17964266.
RA   Kim E.-J., Kho J.-H., Kang M.-R., Um S.-J.;
RL   Mol. Cell 28:513-513(2007).
RN   [7]
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   [8]
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   [9]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-84, AND IDENTIFICATION BY
RP   MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   TISSUE=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] {ECO:0007744|PDB:7MQA}
RP   STRUCTURE BY ELECTRON MICROSCOPY (2.70 ANGSTROMS), FUNCTION, SUBCELLULAR
RP   LOCATION, AND SUBUNIT.
RX   PubMed=34516797; DOI=10.1126/science.abj5338;
RA   Singh S., Vanden Broeck A., Miller L., Chaker-Margot M., Klinge S.;
RT   "Nucleolar maturation of the human small subunit processome.";
RL   Science 373:eabj5338-eabj5338(2021).
CC   -!- FUNCTION: Part of the small subunit (SSU) processome, first precursor
CC       of the small eukaryotic ribosomal subunit. During the assembly of the
CC       SSU processome in the nucleolus, many ribosome biogenesis factors, an
CC       RNA chaperone and ribosomal proteins associate with the nascent pre-
CC       rRNA and work in concert to generate RNA folding, modifications,
CC       rearrangements and cleavage as well as targeted degradation of pre-
CC       ribosomal RNA by the RNA exosome. Acts as a chaperone that specifically
CC       mediates the integration of RPS19 in state post-A1 (PubMed:34516797).
CC       Direct regulator of SIRT1. Enhances SIRT1-mediated deacetylation of
CC       p53/TP53, thereby participating in inhibition of p53/TP53-mediated
CC       transcriptional activity (PubMed:17964266).
CC       {ECO:0000269|PubMed:17964266, ECO:0000269|PubMed:34516797}.
CC   -!- SUBUNIT: Part of the small subunit (SSU) processome, composed of more
CC       than 70 proteins and the RNA chaperone small nucleolar RNA (snoRNA) U3.
CC       Interacts with RPS19; the interaction is direct and mediates the
CC       integration of RPS19 in state post-A1 (PubMed:34516797). Interacts with
CC       SIRT1 (PubMed:17964266). {ECO:0000269|PubMed:17964266,
CC       ECO:0000269|PubMed:34516797}.
CC   -!- INTERACTION:
CC       Q86WX3; Q6UY14-3: ADAMTSL4; NbExp=3; IntAct=EBI-4479407, EBI-10173507;
CC       Q86WX3; A8MQ03: CYSRT1; NbExp=3; IntAct=EBI-4479407, EBI-3867333;
CC       Q86WX3; Q15323: KRT31; NbExp=3; IntAct=EBI-4479407, EBI-948001;
CC       Q86WX3; Q07627: KRTAP1-1; NbExp=3; IntAct=EBI-4479407, EBI-11959885;
CC       Q86WX3; Q8IUG1: KRTAP1-3; NbExp=3; IntAct=EBI-4479407, EBI-11749135;
CC       Q86WX3; P60410: KRTAP10-8; NbExp=3; IntAct=EBI-4479407, EBI-10171774;
CC       Q86WX3; Q5JR59-3: MTUS2; NbExp=3; IntAct=EBI-4479407, EBI-11522433;
CC       Q86WX3; P0DPK4: NOTCH2NLC; NbExp=3; IntAct=EBI-4479407, EBI-22310682;
CC       Q86WX3; Q8IUQ4: SIAH1; NbExp=3; IntAct=EBI-4479407, EBI-747107;
CC       Q86WX3; Q96EB6: SIRT1; NbExp=11; IntAct=EBI-4479407, EBI-1802965;
CC   -!- SUBCELLULAR LOCATION: Nucleus, nucleolus {ECO:0000269|PubMed:17964266,
CC       ECO:0000269|PubMed:34516797}.
CC   -!- TISSUE SPECIFICITY: Widely expressed (at protein level).
CC       {ECO:0000269|PubMed:17964266}.
CC   -!- PTM: Citrullinated by PADI4. {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the AROS family. {ECO:0000305}.
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DR   EMBL; CR456443; CAG30329.1; -; mRNA.
DR   EMBL; AL022312; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; CH471095; EAW60343.1; -; Genomic_DNA.
DR   EMBL; BC047711; AAH47711.1; -; mRNA.
DR   EMBL; BC037573; AAH37573.1; -; mRNA.
DR   CCDS; CCDS13997.1; -.
DR   RefSeq; NP_919307.1; NM_194326.3.
DR   PDB; 7MQA; EM; 2.70 A; LY=1-136.
DR   PDB; 8BBK; X-ray; 3.27 A; G/H/I/J/K/L=1-136.
DR   PDBsum; 7MQA; -.
DR   PDBsum; 8BBK; -.
DR   AlphaFoldDB; Q86WX3; -.
DR   EMDB; EMD-23938; -.
DR   SMR; Q86WX3; -.
DR   BioGRID; 124848; 98.
DR   IntAct; Q86WX3; 53.
DR   MINT; Q86WX3; -.
DR   STRING; 9606.ENSP00000333948; -.
DR   GlyGen; Q86WX3; 1 site, 1 O-linked glycan (1 site).
DR   iPTMnet; Q86WX3; -.
DR   PhosphoSitePlus; Q86WX3; -.
DR   BioMuta; RPS19BP1; -.
DR   DMDM; 74727734; -.
DR   jPOST; Q86WX3; -.
DR   MassIVE; Q86WX3; -.
DR   PaxDb; 9606-ENSP00000333948; -.
DR   PeptideAtlas; Q86WX3; -.
DR   ProteomicsDB; 70214; -.
DR   Pumba; Q86WX3; -.
DR   Antibodypedia; 51530; 148 antibodies from 25 providers.
DR   DNASU; 91582; -.
DR   Ensembl; ENST00000334678.8; ENSP00000333948.3; ENSG00000187051.9.
DR   GeneID; 91582; -.
DR   KEGG; hsa:91582; -.
DR   MANE-Select; ENST00000334678.8; ENSP00000333948.3; NM_194326.4; NP_919307.1.
DR   UCSC; uc003ayb.3; human.
DR   AGR; HGNC:28749; -.
DR   CTD; 91582; -.
DR   DisGeNET; 91582; -.
DR   GeneCards; RPS19BP1; -.
DR   HGNC; HGNC:28749; RPS19BP1.
DR   HPA; ENSG00000187051; Low tissue specificity.
DR   MIM; 610225; gene.
DR   neXtProt; NX_Q86WX3; -.
DR   OpenTargets; ENSG00000187051; -.
DR   PharmGKB; PA143485599; -.
DR   VEuPathDB; HostDB:ENSG00000187051; -.
DR   eggNOG; ENOG502S1CM; Eukaryota.
DR   GeneTree; ENSGT00390000016774; -.
DR   HOGENOM; CLU_152637_0_0_1; -.
DR   InParanoid; Q86WX3; -.
DR   OMA; KFQREYF; -.
DR   OrthoDB; 6493910at2759; -.
DR   PhylomeDB; Q86WX3; -.
DR   TreeFam; TF333429; -.
DR   PathwayCommons; Q86WX3; -.
DR   Reactome; R-HSA-3371453; Regulation of HSF1-mediated heat shock response.
DR   SignaLink; Q86WX3; -.
DR   BioGRID-ORCS; 91582; 519 hits in 1162 CRISPR screens.
DR   ChiTaRS; RPS19BP1; human.
DR   GenomeRNAi; 91582; -.
DR   Pharos; Q86WX3; Tbio.
DR   PRO; PR:Q86WX3; -.
DR   Proteomes; UP000005640; Chromosome 22.
DR   RNAct; Q86WX3; protein.
DR   Bgee; ENSG00000187051; Expressed in muscle layer of sigmoid colon and 185 other cell types or tissues.
DR   ExpressionAtlas; Q86WX3; baseline and differential.
DR   GO; GO:0005829; C:cytosol; IDA:HPA.
DR   GO; GO:0005730; C:nucleolus; IDA:HPA.
DR   GO; GO:0005654; C:nucleoplasm; IDA:HPA.
DR   GO; GO:0032040; C:small-subunit processome; IDA:UniProtKB.
DR   GO; GO:0019899; F:enzyme binding; IPI:UniProtKB.
DR   GO; GO:0003723; F:RNA binding; HDA:UniProtKB.
DR   GO; GO:0042274; P:ribosomal small subunit biogenesis; IDA:UniProtKB.
DR   InterPro; IPR023262; AROS.
DR   PANTHER; PTHR31454; ACTIVE REGULATOR OF SIRT1; 1.
DR   PANTHER; PTHR31454:SF2; ACTIVE REGULATOR OF SIRT1; 1.
DR   Pfam; PF15684; AROS; 1.
DR   PRINTS; PR02029; ACTREGSIRT1.
PE   1: Evidence at protein level;
KW   3D-structure; Citrullination; Nucleus; Phosphoprotein;
KW   Proteomics identification; Reference proteome.
FT   CHAIN           1..136
FT                   /note="Active regulator of SIRT1"
FT                   /id="PRO_0000252393"
FT   REGION          13..58
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOD_RES         7
FT                   /note="Citrulline"
FT                   /evidence="ECO:0000250"
FT   MOD_RES         84
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:23186163"
FT   VARIANT         124
FT                   /note="E -> A (in dbSNP:rs17001278)"
FT                   /id="VAR_051330"
SQ   SEQUENCE   136 AA;  15434 MW;  F7CE798D68CC0941 CRC64;
     MSAALLRRGL ELLAASEAPR DPPGQAKPRG APVKRPRKTK AIQAQKLRNS AKGKVPKSAL
     DEYRKRECRD HLRVNLKFLT RTRSTVAESV SQQILRQNRG RKACDRPVAK TKKKKAEGTV
     FTEEDFQKFQ QEYFGS
//