AROS_HUMAN
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 03-AUG-2022, entry version 137.
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; Synonyms=AROS;
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).
CC -!- FUNCTION: Direct regulator of SIRT1. Enhances SIRT1-mediated
CC deacetylation of p53/TP53, thereby participating in inhibition of
CC p53/TP53-mediated transcriptional activity.
CC {ECO:0000269|PubMed:17964266}.
CC -!- SUBUNIT: Interacts with RPS19 (By similarity). Interacts with SIRT1.
CC {ECO:0000250, ECO:0000269|PubMed:17964266}.
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 -!- 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 PDBsum; 7MQA; -.
DR AlphaFoldDB; Q86WX3; -.
DR SMR; Q86WX3; -.
DR BioGRID; 124848; 86.
DR IntAct; Q86WX3; 31.
DR MINT; Q86WX3; -.
DR STRING; 9606.ENSP00000333948; -.
DR iPTMnet; Q86WX3; -.
DR PhosphoSitePlus; Q86WX3; -.
DR BioMuta; RPS19BP1; -.
DR DMDM; 74727734; -.
DR EPD; Q86WX3; -.
DR jPOST; Q86WX3; -.
DR MassIVE; Q86WX3; -.
DR MaxQB; Q86WX3; -.
DR PaxDb; Q86WX3; -.
DR PeptideAtlas; Q86WX3; -.
DR PRIDE; Q86WX3; -.
DR ProteomicsDB; 70214; -.
DR Antibodypedia; 51530; 139 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 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; 1513987at2759; -.
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; 489 hits in 1082 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 183 other tissues.
DR ExpressionAtlas; Q86WX3; baseline and differential.
DR Genevisible; Q86WX3; HS.
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:0019899; F:enzyme binding; IPI:UniProtKB.
DR GO; GO:0003723; F:RNA binding; HDA:UniProtKB.
DR InterPro; IPR023262; AROS.
DR PANTHER; PTHR31454; PTHR31454; 1.
DR Pfam; PF15684; AROS; 1.
DR PRINTS; PR02029; ACTREGSIRT1.
PE 1: Evidence at protein level;
KW 3D-structure; Citrullination; Nucleus; Phosphoprotein; 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
