CHTOP_MOUSE
ID CHTOP_MOUSE Reviewed; 249 AA.
AC Q9CY57; Q0VBG3; Q3U7V6; Q3UF43; Q3V105; Q5XJG9; Q8C5N4; Q9D7T3; Q9DB03;
AC Q9DC54; Q9JJ95;
DT 11-OCT-2004, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2003, sequence version 2.
DT 03-AUG-2022, entry version 139.
DE RecName: Full=Chromatin target of PRMT1 protein;
DE AltName: Full=Friend of PRMT1 protein;
DE AltName: Full=Small arginine- and glycine-rich protein;
DE Short=SRAG;
GN Name=Chtop; Synonyms=Fop; ORFNames=MNCb-1706;
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 [LARGE SCALE MRNA] (ISOFORM 4).
RC STRAIN=C57BL/6J; TISSUE=Brain;
RA Osada N., Kusuda J., Tanuma R., Ito A., Hirata M., Sugano S., Hashimoto K.;
RT "Isolation of full-length cDNA clones from mouse brain cDNA library made by
RT oligo-capping method.";
RL Submitted (APR-2000) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1; 2; 3 AND 5).
RC STRAIN=C57BL/6J;
RC TISSUE=Bone marrow, Brain, Cerebellum, Embryonic head, Embryonic liver,
RC Lung, Stomach, and Testis;
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 GENOMIC DNA].
RA Mural R.J., Adams M.D., Myers E.W., Smith H.O., Venter J.C.;
RL Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RC STRAIN=C57BL/6J; TISSUE=Brain;
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 ALTERNATIVE SPLICING, SUBCELLULAR LOCATION, TISSUE SPECIFICITY, AND
RP RNA-BINDING.
RX PubMed=19254951; DOI=10.1074/jbc.m809436200;
RA Zullo A.J., Michaud M., Zhang W., Grusby M.J.;
RT "Identification of the small protein rich in arginine and glycine (SRAG): a
RT newly identified nucleolar protein that can regulate cell proliferation.";
RL J. Biol. Chem. 284:12504-12511(2009).
RN [6]
RP FUNCTION, AND TISSUE SPECIFICITY.
RX PubMed=20688955; DOI=10.1182/blood-2010-03-274399;
RA van Dijk T.B., Gillemans N., Pourfarzad F., van Lom K., von Lindern M.,
RA Grosveld F., Philipsen S.;
RT "Fetal globin expression is regulated by Friend of Prmt1.";
RL Blood 116:4349-4352(2010).
RN [7]
RP IDENTIFICATION BY MASS SPECTROMETRY, METHYLATION, INTERACTION WITH PRMT1
RP AND PRMT5, SUBCELLULAR LOCATION, AND DEVELOPMENTAL STAGE.
RX PubMed=19858291; DOI=10.1128/mcb.00645-09;
RA van Dijk T.B., Gillemans N., Stein C., Fanis P., Demmers J.,
RA van de Corput M., Essers J., Grosveld F., Bauer U.M., Philipsen S.;
RT "Friend of Prmt1, a novel chromatin target of protein arginine
RT methyltransferases.";
RL Mol. Cell. Biol. 30:260-272(2010).
RN [8]
RP FUNCTION, SUBCELLULAR LOCATION, AND INTERACTION WITH PRMT1; PRMT5; FYTTD1;
RP SET; CBX4; RNF2; PHC2; ZNF148 AND THE 5FMC COMPLEX.
RX PubMed=22872859; DOI=10.1074/mcp.m112.017194;
RA Fanis P., Gillemans N., Aghajanirefah A., Pourfarzad F., Demmers J.,
RA Esteghamat F., Vadlamudi R.K., Grosveld F., Philipsen S., van Dijk T.B.;
RT "Five friends of methylated chromatin target of protein-arginine-
RT methyltransferase[prmt]-1 (chtop), a complex linking arginine methylation
RT to desumoylation.";
RL Mol. Cell. Proteomics 11:1263-1273(2012).
RN [9]
RP FUNCTION.
RX PubMed=25284789; DOI=10.1016/j.celrep.2014.08.071;
RA Takai H., Masuda K., Sato T., Sakaguchi Y., Suzuki T., Suzuki T.,
RA Koyama-Nasu R., Nasu-Nishimura Y., Katou Y., Ogawa H., Morishita Y.,
RA Kozuka-Hata H., Oyama M., Todo T., Ino Y., Mukasa A., Saito N.,
RA Toyoshima C., Shirahige K., Akiyama T.;
RT "5-Hydroxymethylcytosine plays a critical role in glioblastomagenesis by
RT recruiting the CHTOP-methylosome complex.";
RL Cell Rep. 9:48-60(2014).
CC -!- FUNCTION: Plays an important role in the ligand-dependent activation of
CC estrogen receptor target genes (By similarity). May play a role in the
CC silencing of fetal globin genes (PubMed:20688955). Recruits the 5FMC
CC complex to ZNF148, leading to desumoylation of ZNF148 and subsequent
CC transactivation of ZNF148 target genes (PubMed:22872859). Required for
CC the tumorigenicity of glioblastoma cells. Binds to 5-
CC hydroxymethylcytosine (5hmC) and associates with the methylosome
CC complex containing PRMT1, PRMT5, MEP50 and ERH. The CHTOP-methylosome
CC complex associated with 5hmC methylates H4R3 and transactivates genes
CC involved in glioblastomagenesis (PubMed:25284789).
CC {ECO:0000250|UniProtKB:Q9Y3Y2, ECO:0000269|PubMed:20688955,
CC ECO:0000269|PubMed:22872859, ECO:0000269|PubMed:25284789}.
CC -!- SUBUNIT: Interacts with PRMT1 and PRMT5 (PubMed:19858291,
CC PubMed:22872859). Interacts with the 5FMC complex; the interaction is
CC methylation-dependent. Interacts with FYTTD1, SET and PRC1 complex
CC members CBX4, RNF2 and PHC2; the interactions are methylation-
CC independent. Interacts with ZNF148 (PubMed:22872859). Interacts with
CC WDR77 and ERH (By similarity). {ECO:0000250|UniProtKB:Q9Y3Y2,
CC ECO:0000269|PubMed:19858291, ECO:0000269|PubMed:22872859}.
CC -!- INTERACTION:
CC Q9CY57; Q9JIF0: Prmt1; NbExp=8; IntAct=EBI-6393116, EBI-519055;
CC Q9CY57; Q8CIG8: Prmt5; NbExp=4; IntAct=EBI-6393116, EBI-2527009;
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:19254951}. Nucleus,
CC nucleolus {ECO:0000269|PubMed:19254951}. Nucleus, nucleoplasm
CC {ECO:0000269|PubMed:19858291, ECO:0000269|PubMed:22872859}. Nucleus
CC speckle {ECO:0000269|PubMed:19858291}. Note=Mostly associated with
CC facultative heterochromatin. Localizes to regions surrounding nuclear
CC speckles known as perispeckles in which TREX complex assembly seems to
CC occur (By similarity). {ECO:0000250|UniProtKB:Q9Y3Y2,
CC ECO:0000269|PubMed:19858291}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=5;
CC Name=1;
CC IsoId=Q9CY57-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q9CY57-2; Sequence=VSP_011743;
CC Name=3;
CC IsoId=Q9CY57-3; Sequence=VSP_011744, VSP_011745;
CC Name=4;
CC IsoId=Q9CY57-4; Sequence=VSP_011743, VSP_011745;
CC Name=5;
CC IsoId=Q9CY57-5; Sequence=VSP_011743, VSP_011744, VSP_011745;
CC -!- TISSUE SPECIFICITY: Broadly expressed with highest levels found in
CC thymus, spleen, and lymph nodes. Expressed in an erythroid progenitor
CC cell line derived from fetal liver. {ECO:0000269|PubMed:19254951,
CC ECO:0000269|PubMed:20688955}.
CC -!- DEVELOPMENTAL STAGE: Broadly expressed at 16.5 dpc.
CC {ECO:0000269|PubMed:19858291}.
CC -!- PTM: Asymmetrically methylated by PRMT1. Symmetrically methylated by
CC PRMT5. {ECO:0000269|PubMed:19858291}.
CC -!- MISCELLANEOUS: [Isoform 2]: May be due to an intron retention.
CC {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAA95102.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
CC Sequence=BAB25951.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
CC Sequence=BAC37084.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; AB041654; BAA95102.1; ALT_INIT; mRNA.
DR EMBL; AK004558; BAB23371.1; -; mRNA.
DR EMBL; AK005377; BAB23984.2; -; mRNA.
DR EMBL; AK008885; BAB25951.1; ALT_INIT; mRNA.
DR EMBL; AK010866; BAB27232.2; -; mRNA.
DR EMBL; AK047914; BAC33189.1; -; mRNA.
DR EMBL; AK077960; BAC37084.1; ALT_INIT; mRNA.
DR EMBL; AK132769; BAE21348.1; -; mRNA.
DR EMBL; AK149010; BAE28718.1; -; mRNA.
DR EMBL; AK152492; BAE31263.1; -; mRNA.
DR EMBL; CH466547; EDL15130.1; -; Genomic_DNA.
DR EMBL; BC083333; AAH83333.1; -; mRNA.
DR EMBL; BC120651; AAI20652.1; -; mRNA.
DR CCDS; CCDS17532.1; -. [Q9CY57-2]
DR CCDS; CCDS79964.1; -. [Q9CY57-5]
DR CCDS; CCDS79965.1; -. [Q9CY57-4]
DR CCDS; CCDS79966.1; -. [Q9CY57-3]
DR CCDS; CCDS79968.1; -. [Q9CY57-1]
DR RefSeq; NP_001280705.1; NM_001293776.1. [Q9CY57-1]
DR RefSeq; NP_001280706.1; NM_001293777.1.
DR RefSeq; NP_001280707.1; NM_001293778.1.
DR RefSeq; NP_001280708.1; NM_001293779.1. [Q9CY57-3]
DR RefSeq; NP_001280710.1; NM_001293781.1. [Q9CY57-5]
DR RefSeq; NP_001280711.1; NM_001293782.1. [Q9CY57-2]
DR RefSeq; NP_075704.2; NM_023215.6. [Q9CY57-2]
DR AlphaFoldDB; Q9CY57; -.
DR SMR; Q9CY57; -.
DR BioGRID; 211527; 5.
DR IntAct; Q9CY57; 11.
DR STRING; 10090.ENSMUSP00000001043; -.
DR iPTMnet; Q9CY57; -.
DR PhosphoSitePlus; Q9CY57; -.
DR SwissPalm; Q9CY57; -.
DR EPD; Q9CY57; -.
DR jPOST; Q9CY57; -.
DR MaxQB; Q9CY57; -.
DR PaxDb; Q9CY57; -.
DR PRIDE; Q9CY57; -.
DR ProteomicsDB; 283913; -. [Q9CY57-1]
DR ProteomicsDB; 283914; -. [Q9CY57-2]
DR ProteomicsDB; 283915; -. [Q9CY57-3]
DR ProteomicsDB; 283916; -. [Q9CY57-4]
DR ProteomicsDB; 283917; -. [Q9CY57-5]
DR Antibodypedia; 34133; 155 antibodies from 25 providers.
DR DNASU; 66511; -.
DR Ensembl; ENSMUST00000001043; ENSMUSP00000001043; ENSMUSG00000001017. [Q9CY57-2]
DR Ensembl; ENSMUST00000049937; ENSMUSP00000061800; ENSMUSG00000001017. [Q9CY57-1]
DR Ensembl; ENSMUST00000076639; ENSMUSP00000075936; ENSMUSG00000001017. [Q9CY57-3]
DR Ensembl; ENSMUST00000107342; ENSMUSP00000102965; ENSMUSG00000001017. [Q9CY57-5]
DR Ensembl; ENSMUST00000107343; ENSMUSP00000102966; ENSMUSG00000001017. [Q9CY57-4]
DR Ensembl; ENSMUST00000107344; ENSMUSP00000102967; ENSMUSG00000001017. [Q9CY57-2]
DR GeneID; 66511; -.
DR KEGG; mmu:66511; -.
DR UCSC; uc008qco.2; mouse. [Q9CY57-1]
DR UCSC; uc008qcr.2; mouse. [Q9CY57-3]
DR UCSC; uc056ztp.1; mouse. [Q9CY57-5]
DR CTD; 26097; -.
DR MGI; MGI:1913761; Chtop.
DR VEuPathDB; HostDB:ENSMUSG00000001017; -.
DR eggNOG; ENOG502QV0X; Eukaryota.
DR GeneTree; ENSGT00390000002869; -.
DR HOGENOM; CLU_087638_0_0_1; -.
DR InParanoid; Q9CY57; -.
DR OMA; AMQMENR; -.
DR OrthoDB; 1598721at2759; -.
DR PhylomeDB; Q9CY57; -.
DR TreeFam; TF331447; -.
DR Reactome; R-MMU-159236; Transport of Mature mRNA derived from an Intron-Containing Transcript.
DR Reactome; R-MMU-72187; mRNA 3'-end processing.
DR Reactome; R-MMU-73856; RNA Polymerase II Transcription Termination.
DR BioGRID-ORCS; 66511; 5 hits in 60 CRISPR screens.
DR ChiTaRS; Chtop; mouse.
DR PRO; PR:Q9CY57; -.
DR Proteomes; UP000000589; Chromosome 3.
DR RNAct; Q9CY57; protein.
DR Bgee; ENSMUSG00000001017; Expressed in saccule of membranous labyrinth and 259 other tissues.
DR ExpressionAtlas; Q9CY57; baseline and differential.
DR Genevisible; Q9CY57; MM.
DR GO; GO:0036464; C:cytoplasmic ribonucleoprotein granule; ISO:MGI.
DR GO; GO:0016607; C:nuclear speck; ISO:MGI.
DR GO; GO:0005730; C:nucleolus; IEA:UniProtKB-SubCell.
DR GO; GO:0005634; C:nucleus; IBA:GO_Central.
DR GO; GO:0000346; C:transcription export complex; ISO:MGI.
DR GO; GO:0008327; F:methyl-CpG binding; ISS:UniProtKB.
DR GO; GO:0003729; F:mRNA binding; IBA:GO_Central.
DR GO; GO:0001701; P:in utero embryonic development; IMP:MGI.
DR GO; GO:0006406; P:mRNA export from nucleus; ISO:MGI.
DR GO; GO:0032781; P:positive regulation of ATP-dependent activity; ISO:MGI.
DR GO; GO:0008284; P:positive regulation of cell population proliferation; ISS:UniProtKB.
DR GO; GO:0051096; P:positive regulation of helicase activity; ISO:MGI.
DR GO; GO:0031062; P:positive regulation of histone methylation; ISS:UniProtKB.
DR InterPro; IPR025715; FoP_C.
DR Pfam; PF13865; FoP_duplication; 1.
DR SMART; SM01218; FoP_duplication; 1.
PE 1: Evidence at protein level;
KW Acetylation; Alternative splicing; Isopeptide bond; Methylation; Nucleus;
KW Phosphoprotein; Reference proteome; RNA-binding; Transcription;
KW Transcription regulation; Ubl conjugation.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000250|UniProtKB:Q9Y3Y2"
FT CHAIN 2..249
FT /note="Chromatin target of PRMT1 protein"
FT /id="PRO_0000089264"
FT REGION 152..205
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 154..207
FT /note="Interaction with PRMT1"
FT MOTIF 195..204
FT /note="GAR motif; involved in 5hmC binding"
FT /evidence="ECO:0000250|UniProtKB:Q9Y3Y2"
FT MOD_RES 2
FT /note="N-acetylalanine"
FT /evidence="ECO:0000250|UniProtKB:Q9Y3Y2"
FT MOD_RES 40
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9Y3Y2"
FT MOD_RES 49
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9Y3Y2"
FT MOD_RES 64
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9Y3Y2"
FT MOD_RES 243
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q9Y3Y2"
FT CROSSLNK 70
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:Q9Y3Y2"
FT VAR_SEQ 1..25
FT /note="Missing (in isoform 2, isoform 4 and isoform 5)"
FT /evidence="ECO:0000303|PubMed:15489334,
FT ECO:0000303|PubMed:16141072, ECO:0000303|Ref.1"
FT /id="VSP_011743"
FT VAR_SEQ 74
FT /note="Missing (in isoform 3 and isoform 5)"
FT /evidence="ECO:0000303|PubMed:16141072"
FT /id="VSP_011744"
FT VAR_SEQ 137..182
FT /note="Missing (in isoform 3, isoform 4 and isoform 5)"
FT /evidence="ECO:0000303|PubMed:16141072, ECO:0000303|Ref.1"
FT /id="VSP_011745"
FT CONFLICT 96
FT /note="L -> Q (in Ref. 2; BAE31263)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 249 AA; 26585 MW; 5F3E44A53ED0645F CRC64;
MAAQSAPKVV LKSTTKMSLN ERFTNMLKNK QPMPVNIRAS MQQQQQLASA RNRRLAQQME
NRPSVQAALK LKQKSLKQRL GKSNIQARLG RPIGALARGA IGGRGLPIIQ RGLPRGGLRG
GRATRTLLRG GMSLRGQNLL RGGRAVAPRM GLRRGGVRGR GGPGRGGLGR GAMGRGGIGG
RGRGMIGRGR GGFGGRGRGR GRGRGALTRP VLTKEQLDNQ LDAYMSKTKG HLDAELDAYM
AQTDPETND
