MCRS1_MOUSE
ID MCRS1_MOUSE Reviewed; 462 AA.
AC Q99L90; O35255; Q32P11;
DT 01-NOV-2002, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2001, sequence version 1.
DT 03-AUG-2022, entry version 157.
DE RecName: Full=Microspherule protein 1;
DE AltName: Full=58 kDa microspherule protein;
GN Name=Mcrs1; Synonyms=Msp58;
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RX PubMed=9654073; DOI=10.1046/j.1432-1327.1998.2530734.x;
RA Ren Y., Busch R.K., Perlaky L., Busch H.;
RT "The 58-kDa microspherule protein (MSP58), a nucleolar protein, interacts
RT with nucleolar protein p120.";
RL Eur. J. Biochem. 253:734-742(1998).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=NOD; TISSUE=Thymus;
RX PubMed=16141072; DOI=10.1126/science.1112014;
RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT "The transcriptional landscape of the mammalian genome.";
RL Science 309:1559-1563(2005).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Eye, Mammary tumor, and Olfactory epithelium;
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 [4]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-282, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Embryonic brain;
RX PubMed=15345747; DOI=10.1074/mcp.m400085-mcp200;
RA Ballif B.A., Villen J., Beausoleil S.A., Schwartz D., Gygi S.P.;
RT "Phosphoproteomic analysis of the developing mouse brain.";
RL Mol. Cell. Proteomics 3:1093-1101(2004).
RN [5]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-282, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=19144319; DOI=10.1016/j.immuni.2008.11.006;
RA Trost M., English L., Lemieux S., Courcelles M., Desjardins M.,
RA Thibault P.;
RT "The phagosomal proteome in interferon-gamma-activated macrophages.";
RL Immunity 30:143-154(2009).
RN [6]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-102; THR-103; SER-108 AND
RP SER-282, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain, Heart, Kidney, Lung, Spleen, and Testis;
RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL Cell 143:1174-1189(2010).
RN [7]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-123 AND LYS-130, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Embryonic fibroblast;
RX PubMed=23806337; DOI=10.1016/j.molcel.2013.06.001;
RA Park J., Chen Y., Tishkoff D.X., Peng C., Tan M., Dai L., Xie Z., Zhang Y.,
RA Zwaans B.M., Skinner M.E., Lombard D.B., Zhao Y.;
RT "SIRT5-mediated lysine desuccinylation impacts diverse metabolic
RT pathways.";
RL Mol. Cell 50:919-930(2013).
CC -!- FUNCTION: Modulates the transcription repressor activity of DAXX by
CC recruiting it to the nucleolus. As part of the NSL complex it may be
CC involved in acetylation of nucleosomal histone H4 on several lysine
CC residues. Putative regulatory component of the chromatin remodeling
CC INO80 complex which is involved in transcriptional regulation, DNA
CC replication and probably DNA repair. May also be an inhibitor of TERT
CC telomerase activity. Binds to G-quadruplex structures in mRNA. Binds to
CC RNA homomer poly(G) and poly(U). {ECO:0000250|UniProtKB:Q96EZ8}.
CC -!- SUBUNIT: Component of the chromatin remodeling INO80 complex;
CC specifically part of a complex module associated with the N-terminus of
CC INO80. Component of some MLL1/MLL complex, at least composed of the
CC core components KMT2A/MLL1, ASH2L, HCFC1, WDR5 and RBBP5, as well as
CC the facultative components BAP18, CHD8, E2F6, HSP70, INO80C, KANSL1,
CC LAS1L, MAX, MCRS1, MGA, KAT8/MOF, PELP1, PHF20, PRP31, RING2,
CC RUVB1/TIP49A, RUVB2/TIP49B, SENP3, TAF1, TAF4, TAF6, TAF7, TAF9 and
CC TEX10. Component of the NSL complex at least composed of MOF/KAT8,
CC KANSL1, KANSL2, KANSL3, MCRS1, PHF20, OGT1/OGT, WDR5 and HCFC1.
CC Interacts with NOP2. Interacts with PINX1. Interacts with TERT.
CC Interacts with CCDC85B. Interacts with DAXX. Interacts (via N-terminus)
CC with FMR1 (via phosphorylated form). Interacts with FXR1 AND FXR2.
CC {ECO:0000250|UniProtKB:Q96EZ8}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:Q96EZ8}. Nucleus,
CC nucleolus {ECO:0000250|UniProtKB:Q96EZ8}. Cytoplasm
CC {ECO:0000250|UniProtKB:Q96EZ8}. Note=In microspherules in the
CC nucleolus. {ECO:0000250|UniProtKB:Q96EZ8}.
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DR EMBL; AF015309; AAC53590.1; -; mRNA.
DR EMBL; AK088116; BAC40155.1; -; mRNA.
DR EMBL; BC003746; AAH03746.1; -; mRNA.
DR EMBL; BC085099; AAH85099.1; -; mRNA.
DR EMBL; BC108340; AAI08341.1; -; mRNA.
DR CCDS; CCDS37199.1; -.
DR RefSeq; NP_001157628.1; NM_001164156.1.
DR RefSeq; NP_058046.2; NM_016766.3.
DR AlphaFoldDB; Q99L90; -.
DR SMR; Q99L90; -.
DR BioGRID; 206187; 1.
DR ComplexPortal; CPX-875; NSL histone acetyltransferase complex.
DR ComplexPortal; CPX-878; INO80 chromatin remodeling complex.
DR STRING; 10090.ENSMUSP00000043901; -.
DR iPTMnet; Q99L90; -.
DR PhosphoSitePlus; Q99L90; -.
DR EPD; Q99L90; -.
DR jPOST; Q99L90; -.
DR MaxQB; Q99L90; -.
DR PaxDb; Q99L90; -.
DR PRIDE; Q99L90; -.
DR ProteomicsDB; 295716; -.
DR Antibodypedia; 25985; 166 antibodies from 25 providers.
DR DNASU; 51812; -.
DR Ensembl; ENSMUST00000041190; ENSMUSP00000043901; ENSMUSG00000037570.
DR GeneID; 51812; -.
DR KEGG; mmu:51812; -.
DR UCSC; uc007xpa.2; mouse.
DR CTD; 10445; -.
DR MGI; MGI:1858420; Mcrs1.
DR VEuPathDB; HostDB:ENSMUSG00000037570; -.
DR eggNOG; KOG2293; Eukaryota.
DR GeneTree; ENSGT00390000005536; -.
DR InParanoid; Q99L90; -.
DR OMA; EIQQRWY; -.
DR OrthoDB; 1091011at2759; -.
DR PhylomeDB; Q99L90; -.
DR TreeFam; TF318119; -.
DR Reactome; R-MMU-3214847; HATs acetylate histones.
DR Reactome; R-MMU-5689603; UCH proteinases.
DR Reactome; R-MMU-5696394; DNA Damage Recognition in GG-NER.
DR BioGRID-ORCS; 51812; 29 hits in 111 CRISPR screens.
DR ChiTaRS; Mcrs1; mouse.
DR PRO; PR:Q99L90; -.
DR Proteomes; UP000000589; Chromosome 15.
DR RNAct; Q99L90; protein.
DR Bgee; ENSMUSG00000037570; Expressed in midbrain and 71 other tissues.
DR ExpressionAtlas; Q99L90; baseline and differential.
DR Genevisible; Q99L90; MM.
DR GO; GO:0005737; C:cytoplasm; ISS:UniProtKB.
DR GO; GO:0030425; C:dendrite; ISS:UniProtKB.
DR GO; GO:0005783; C:endoplasmic reticulum; IEA:Ensembl.
DR GO; GO:0000123; C:histone acetyltransferase complex; ISS:UniProtKB.
DR GO; GO:0031011; C:Ino80 complex; ISO:MGI.
DR GO; GO:0071339; C:MLL1 complex; ISS:UniProtKB.
DR GO; GO:0044545; C:NSL complex; ISO:MGI.
DR GO; GO:0005730; C:nucleolus; ISS:UniProtKB.
DR GO; GO:0005654; C:nucleoplasm; ISO:MGI.
DR GO; GO:0005634; C:nucleus; ISS:UniProtKB.
DR GO; GO:0043204; C:perikaryon; ISS:UniProtKB.
DR GO; GO:0005844; C:polysome; ISS:UniProtKB.
DR GO; GO:0002151; F:G-quadruplex RNA binding; ISS:UniProtKB.
DR GO; GO:0034046; F:poly(G) binding; ISS:UniProtKB.
DR GO; GO:0008266; F:poly(U) RNA binding; ISS:UniProtKB.
DR GO; GO:0010521; F:telomerase inhibitor activity; ISO:MGI.
DR GO; GO:0006338; P:chromatin remodeling; ISO:MGI.
DR GO; GO:0006310; P:DNA recombination; IEA:UniProtKB-KW.
DR GO; GO:0006281; P:DNA repair; IEA:UniProtKB-KW.
DR GO; GO:0043984; P:histone H4-K16 acetylation; ISS:UniProtKB.
DR GO; GO:0043981; P:histone H4-K5 acetylation; ISS:UniProtKB.
DR GO; GO:0043982; P:histone H4-K8 acetylation; ISS:UniProtKB.
DR GO; GO:0051974; P:negative regulation of telomerase activity; ISO:MGI.
DR GO; GO:1904357; P:negative regulation of telomere maintenance via telomere lengthening; ISO:MGI.
DR GO; GO:0045739; P:positive regulation of DNA repair; IDA:ComplexPortal.
DR GO; GO:0051571; P:positive regulation of histone H3-K4 methylation; ISO:MGI.
DR GO; GO:1904751; P:positive regulation of protein localization to nucleolus; ISS:UniProtKB.
DR GO; GO:1904507; P:positive regulation of telomere maintenance in response to DNA damage; IMP:ComplexPortal.
DR GO; GO:0045944; P:positive regulation of transcription by RNA polymerase II; IBA:GO_Central.
DR GO; GO:0045893; P:positive regulation of transcription, DNA-templated; ISO:MGI.
DR GO; GO:0051726; P:regulation of cell cycle; ISO:MGI.
DR GO; GO:0033044; P:regulation of chromosome organization; ISO:MGI.
DR GO; GO:0006282; P:regulation of DNA repair; IDA:ComplexPortal.
DR GO; GO:0006275; P:regulation of DNA replication; ISO:MGI.
DR GO; GO:0060382; P:regulation of DNA strand elongation; ISO:MGI.
DR GO; GO:1900095; P:regulation of dosage compensation by inactivation of X chromosome; IDA:ComplexPortal.
DR GO; GO:0045995; P:regulation of embryonic development; IMP:ComplexPortal.
DR GO; GO:0000723; P:telomere maintenance; IMP:ComplexPortal.
DR CDD; cd00060; FHA; 1.
DR InterPro; IPR000253; FHA_dom.
DR InterPro; IPR037912; MCRS1.
DR InterPro; IPR025999; MCRS_N.
DR InterPro; IPR008984; SMAD_FHA_dom_sf.
DR PANTHER; PTHR13233; PTHR13233; 1.
DR Pfam; PF00498; FHA; 1.
DR Pfam; PF13325; MCRS_N; 1.
DR SMART; SM00240; FHA; 1.
DR SUPFAM; SSF49879; SSF49879; 1.
DR PROSITE; PS50006; FHA_DOMAIN; 1.
PE 1: Evidence at protein level;
KW Acetylation; Chromatin regulator; Coiled coil; Cytoplasm; DNA damage;
KW DNA recombination; DNA repair; Nucleus; Phosphoprotein; Reference proteome;
KW Transcription; Transcription regulation.
FT CHAIN 1..462
FT /note="Microspherule protein 1"
FT /id="PRO_0000096306"
FT DOMAIN 363..419
FT /note="FHA"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00086"
FT REGION 1..130
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 301..335
FT /evidence="ECO:0000255"
FT MOTIF 113..123
FT /note="Nuclear localization signal"
FT /evidence="ECO:0000255"
FT COMPBIAS 9..24
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 1
FT /note="N-acetylmethionine"
FT /evidence="ECO:0000250|UniProtKB:Q96EZ8"
FT MOD_RES 22
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q96EZ8"
FT MOD_RES 102
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 103
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 108
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 123
FT /note="N6-acetyllysine"
FT /evidence="ECO:0007744|PubMed:23806337"
FT MOD_RES 130
FT /note="N6-acetyllysine"
FT /evidence="ECO:0007744|PubMed:23806337"
FT MOD_RES 282
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:15345747,
FT ECO:0007744|PubMed:19144319, ECO:0007744|PubMed:21183079"
FT CONFLICT 193
FT /note="R -> K (in Ref. 1; AAC53590)"
FT /evidence="ECO:0000305"
FT CONFLICT 274
FT /note="K -> R (in Ref. 1; AAC53590)"
FT /evidence="ECO:0000305"
FT CONFLICT 298
FT /note="D -> N (in Ref. 1; AAC53590)"
FT /evidence="ECO:0000305"
FT CONFLICT 314..315
FT /note="RE -> QK (in Ref. 1; AAC53590)"
FT /evidence="ECO:0000305"
FT CONFLICT 368
FT /note="A -> T (in Ref. 1; AAC53590)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 462 AA; 51692 MW; 47A73672270E2014 CRC64;
MDKDSQGLLD SSLMASGTAS RSEDEESLAG QKRASSQALG TIPKRRSSSR FIKRKKFDDE
LVESSLAKSS TRVKGAGGVE SGRCSGSEPS SSEKKKVSKA PSTPVPPSPA PTPGLTKRVK
KSKQPLQVTK DLGRWKPADD LLLINAVLQT NDLTSVHLGV KFSCRFTLRE VQERWYALLY
DPVISKLACQ AMRQLHPEAI AAIQSKALFS KAEEQLLSKV GSSSQPTLET FQDLLHTHPD
AFYLARTAKA LQAHWQLMKQ YYLLEDQTVQ PLPKGDQVLN FSDAEDLIDD SKLKDMRDEV
LEHELTVADR RQKREIRQLE QELHKWQVLV DSITGMGSPD FDNQTLAVLR GRMVRYLMRS
REITLGRATK DNQIDVDLSL EGPAWKISRK QGVIKLKNNG DFFIANEGRR PIYIDGRPVL
CGSKWRLSNN SVVEIASLRF VFLINQDLIA LIRAEAAKIT PQ
