CHTOP_HUMAN
ID CHTOP_HUMAN Reviewed; 248 AA.
AC Q9Y3Y2; D3DV55; Q0VAQ8; Q2VPI9; Q5T7Y8; Q5T7Y9; Q5T7Z0; Q6NSM4; Q6PB28;
AC Q8WYT9; Q9BUC5; Q9H034; Q9H2L0;
DT 01-DEC-2000, integrated into UniProtKB/Swiss-Prot.
DT 11-OCT-2004, sequence version 2.
DT 03-AUG-2022, entry version 172.
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=C1orf77, FOP; ORFNames=HT031, PP7704;
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] (ISOFORM 1).
RC TISSUE=Hypothalamus;
RA Xu X., Yang Y., Gao G., Xiao H., Chen Z., Han Z.;
RL Submitted (MAY-2000) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RX PubMed=15498874; DOI=10.1073/pnas.0404089101;
RA Wan D., Gong Y., Qin W., Zhang P., Li J., Wei L., Zhou X., Li H., Qiu X.,
RA Zhong F., He L., Yu J., Yao G., Jiang H., Qian L., Yu Y., Shu H., Chen X.,
RA Xu H., Guo M., Pan Z., Chen Y., Ge C., Yang S., Gu J.;
RT "Large-scale cDNA transfection screening for genes related to cancer
RT development and progression.";
RL Proc. Natl. Acad. Sci. U.S.A. 101:15724-15729(2004).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=16710414; DOI=10.1038/nature04727;
RA Gregory S.G., Barlow K.F., McLay K.E., Kaul R., Swarbreck D., Dunham A.,
RA Scott C.E., Howe K.L., Woodfine K., Spencer C.C.A., Jones M.C., Gillson C.,
RA Searle S., Zhou Y., Kokocinski F., McDonald L., Evans R., Phillips K.,
RA Atkinson A., Cooper R., Jones C., Hall R.E., Andrews T.D., Lloyd C.,
RA Ainscough R., Almeida J.P., Ambrose K.D., Anderson F., Andrew R.W.,
RA Ashwell R.I.S., Aubin K., Babbage A.K., Bagguley C.L., Bailey J.,
RA Beasley H., Bethel G., Bird C.P., Bray-Allen S., Brown J.Y., Brown A.J.,
RA Buckley D., Burton J., Bye J., Carder C., Chapman J.C., Clark S.Y.,
RA Clarke G., Clee C., Cobley V., Collier R.E., Corby N., Coville G.J.,
RA Davies J., Deadman R., Dunn M., Earthrowl M., Ellington A.G., Errington H.,
RA Frankish A., Frankland J., French L., Garner P., Garnett J., Gay L.,
RA Ghori M.R.J., Gibson R., Gilby L.M., Gillett W., Glithero R.J.,
RA Grafham D.V., Griffiths C., Griffiths-Jones S., Grocock R., Hammond S.,
RA Harrison E.S.I., Hart E., Haugen E., Heath P.D., Holmes S., Holt K.,
RA Howden P.J., Hunt A.R., Hunt S.E., Hunter G., Isherwood J., James R.,
RA Johnson C., Johnson D., Joy A., Kay M., Kershaw J.K., Kibukawa M.,
RA Kimberley A.M., King A., Knights A.J., Lad H., Laird G., Lawlor S.,
RA Leongamornlert D.A., Lloyd D.M., Loveland J., Lovell J., Lush M.J.,
RA Lyne R., Martin S., Mashreghi-Mohammadi M., Matthews L., Matthews N.S.W.,
RA McLaren S., Milne S., Mistry S., Moore M.J.F., Nickerson T., O'Dell C.N.,
RA Oliver K., Palmeiri A., Palmer S.A., Parker A., Patel D., Pearce A.V.,
RA Peck A.I., Pelan S., Phelps K., Phillimore B.J., Plumb R., Rajan J.,
RA Raymond C., Rouse G., Saenphimmachak C., Sehra H.K., Sheridan E.,
RA Shownkeen R., Sims S., Skuce C.D., Smith M., Steward C., Subramanian S.,
RA Sycamore N., Tracey A., Tromans A., Van Helmond Z., Wall M., Wallis J.M.,
RA White S., Whitehead S.L., Wilkinson J.E., Willey D.L., Williams H.,
RA Wilming L., Wray P.W., Wu Z., Coulson A., Vaudin M., Sulston J.E.,
RA Durbin R.M., Hubbard T., Wooster R., Dunham I., Carter N.P., McVean G.,
RA Ross M.T., Harrow J., Olson M.V., Beck S., Rogers J., Bentley D.R.;
RT "The DNA sequence and biological annotation of human chromosome 1.";
RL Nature 441:315-321(2006).
RN [4]
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 (SEP-2005) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2), AND NUCLEOTIDE SEQUENCE
RP [LARGE SCALE MRNA] OF 55-248 (ISOFORM 1).
RC TISSUE=Eye, Liver, Placenta, 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 [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 23-248 (ISOFORM 1).
RC TISSUE=Fetal brain, and Lymph node;
RX PubMed=17974005; DOI=10.1186/1471-2164-8-399;
RA Bechtel S., Rosenfelder H., Duda A., Schmidt C.P., Ernst U.,
RA Wellenreuther R., Mehrle A., Schuster C., Bahr A., Bloecker H., Heubner D.,
RA Hoerlein A., Michel G., Wedler H., Koehrer K., Ottenwaelder B., Poustka A.,
RA Wiemann S., Schupp I.;
RT "The full-ORF clone resource of the German cDNA consortium.";
RL BMC Genomics 8:399-399(2007).
RN [7]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-242, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=17081983; DOI=10.1016/j.cell.2006.09.026;
RA Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P., Mann M.;
RT "Global, in vivo, and site-specific phosphorylation dynamics in signaling
RT networks.";
RL Cell 127:635-648(2006).
RN [8]
RP ALTERNATIVE SPLICING, SUBCELLULAR LOCATION, AND 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 [9]
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 [10]
RP FUNCTION.
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 [11]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-33 AND THR-242, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=20068231; DOI=10.1126/scisignal.2000475;
RA Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L.,
RA Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S., Mann M.;
RT "Quantitative phosphoproteomics reveals widespread full phosphorylation
RT site occupancy during mitosis.";
RL Sci. Signal. 3:RA3-RA3(2010).
RN [12]
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 [13]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, CLEAVAGE OF INITIATOR
RP METHIONINE [LARGE SCALE ANALYSIS], AND IDENTIFICATION BY MASS SPECTROMETRY
RP [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 [14]
RP FUNCTION, IDENTIFICATION IN THE TREX COMPLEX, METHYLATION, SUBCELLULAR
RP LOCATION, AND INTERACTION WITH NXF1; DDX39B AND ALYREF.
RX PubMed=23299939; DOI=10.1038/emboj.2012.342;
RA Chang C.T., Hautbergue G.M., Walsh M.J., Viphakone N., van Dijk T.B.,
RA Philipsen S., Wilson S.A.;
RT "Chtop is a component of the dynamic TREX mRNA export complex.";
RL EMBO J. 32:473-486(2013).
RN [15]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-33; SER-40; SER-49 AND
RP SER-64, AND IDENTIFICATION BY 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 [16]
RP SUBCELLULAR LOCATION, AND INTERACTION WITH ALYREF AND NXF1.
RX PubMed=23826332; DOI=10.1371/journal.pone.0067676;
RA Teng I.F., Wilson S.A.;
RT "Mapping interactions between mRNA export factors in living cells.";
RL PLoS ONE 8:E67676-E67676(2013).
RN [17]
RP FUNCTION, INTERACTION WITH PRMT1; PRMT5; WDR77 AND ERH, METHYLATION, AND
RP MUTAGENESIS OF ARG-195; ARG-197; ARG-199; ARG-201 AND ARG-203.
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).
RN [18]
RP SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-70, AND IDENTIFICATION BY MASS
RP 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: Plays an important role in the ligand-dependent activation of
CC estrogen receptor target genes (PubMed:19858291). May play a role in
CC the silencing of fetal globin genes (PubMed:20688955). Recruits the
CC 5FMC complex to ZNF148, leading to desumoylation of ZNF148 and
CC subsequent transactivation of ZNF148 target genes (By similarity).
CC Plays an important role in the tumorigenicity of glioblastoma cells.
CC Binds to 5-hydroxymethylcytosine (5hmC) and associates with the
CC methylosome complex containing PRMT1, PRMT5, MEP50 and ERH. The CHTOP-
CC methylosome complex associated with 5hmC is recruited to selective
CC sites on the chromosome, where it methylates H4R3 and activates the
CC transcription of genes involved in glioblastomagenesis
CC (PubMed:25284789). {ECO:0000250|UniProtKB:Q9CY57,
CC ECO:0000269|PubMed:19858291, ECO:0000269|PubMed:20688955,
CC ECO:0000269|PubMed:25284789}.
CC -!- FUNCTION: Required for effective mRNA nuclear export and is a component
CC of the TREX complex which is thought to couple mRNA transcription,
CC processing and nuclear export, and specifically associates with spliced
CC mRNA and not with unspliced pre-mRNA. TREX is recruited to spliced
CC mRNAs by a transcription-independent mechanism, binds to mRNA upstream
CC of the exon-junction complex (EJC) and is recruited in a splicing- and
CC cap-dependent manner to a region near the 5' end of the mRNA where it
CC functions in mRNA export to the cytoplasm via the TAP/NFX1 pathway. The
CC TREX complex is essential for the export of Kaposi's sarcoma-associated
CC herpesvirus (KSHV) intronless mRNAs and infectious virus production.
CC Stimulates DDX39B ATPase and helicase activities. In cooperation with
CC ALYREF/THOC4 enhances NXF1 RNA binding activity (PubMed:23299939).
CC {ECO:0000269|PubMed:23299939}.
CC -!- SUBUNIT: Interacts with PRMT1 and PRMT5 (PubMed:25284789). Interacts
CC with the 5FMC complex; the interaction is methylation-dependent.
CC Interacts with FYTTD1, SET and PRC1 complex members CBX4, RNF2 and
CC PHC2; the interactions are methylation-independent. Interacts with
CC ZNF148 (By similarity). Component of the transcription/export (TREX)
CC complex at least composed of ALYREF/THOC4, DDX39B, SARNP/CIP29, CHTOP
CC and the THO subcomplex; TREX seems to have dynamic structure involving
CC ATP-dependent remodeling; in the complex interacts (methylated) with
CC ALYREF/THOC4 and with DDX39B in a methylation-independent manner.
CC Interacts (methylated) with NXF1; the interaction is mutually exclusive
CC with the NXF1:THOC5 interaction (PubMed:23299939, PubMed:23826332).
CC Interacts with WDR77 and ERH (PubMed:25284789).
CC {ECO:0000250|UniProtKB:Q9CY57, ECO:0000269|PubMed:23299939,
CC ECO:0000269|PubMed:23826332, ECO:0000269|PubMed:25284789}.
CC -!- INTERACTION:
CC Q9Y3Y2; Q86V81: ALYREF; NbExp=8; IntAct=EBI-347794, EBI-347640;
CC Q9Y3Y2; Q13838: DDX39B; NbExp=7; IntAct=EBI-347794, EBI-348622;
CC Q9Y3Y2; P84090: ERH; NbExp=4; IntAct=EBI-347794, EBI-711389;
CC Q9Y3Y2; Q5VWX1: KHDRBS2; NbExp=3; IntAct=EBI-347794, EBI-742808;
CC Q9Y3Y2; Q9UBU9: NXF1; NbExp=9; IntAct=EBI-347794, EBI-398874;
CC Q9Y3Y2; Q99873: PRMT1; NbExp=2; IntAct=EBI-347794, EBI-78738;
CC Q9Y3Y2; Q16637: SMN2; NbExp=3; IntAct=EBI-347794, EBI-395421;
CC Q9Y3Y2; P78362: SRPK2; NbExp=2; IntAct=EBI-347794, EBI-593303;
CC Q9Y3Y2-3; Q9NRW3: APOBEC3C; NbExp=3; IntAct=EBI-11984237, EBI-1044593;
CC Q9Y3Y2-3; O00148: DDX39A; NbExp=3; IntAct=EBI-11984237, EBI-348253;
CC Q9Y3Y2-3; Q13838: DDX39B; NbExp=5; IntAct=EBI-11984237, EBI-348622;
CC Q9Y3Y2-3; P84090: ERH; NbExp=5; IntAct=EBI-11984237, EBI-711389;
CC Q9Y3Y2-3; Q5VWX1: KHDRBS2; NbExp=3; IntAct=EBI-11984237, EBI-742808;
CC Q9Y3Y2-3; Q6NSJ2-2: PHLDB3; NbExp=3; IntAct=EBI-11984237, EBI-11018958;
CC Q9Y3Y2-3; P98179: RBM3; NbExp=3; IntAct=EBI-11984237, EBI-2949699;
CC Q9Y3Y2-3; Q16637: SMN2; NbExp=3; IntAct=EBI-11984237, EBI-395421;
CC Q9Y3Y2-3; P09012: SNRPA; NbExp=3; IntAct=EBI-11984237, EBI-607085;
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:19254951}. Nucleus,
CC nucleolus {ECO:0000269|PubMed:19254951}. Nucleus, nucleoplasm
CC {ECO:0000269|PubMed:23826332}. Nucleus speckle
CC {ECO:0000269|PubMed:23299939, ECO:0000269|PubMed:23826332}. Note=Mostly
CC associated with facultative heterochromatin (By similarity). Localizes
CC to regions surrounding nuclear speckles known as perispeckles in which
CC TREX complex assembly seems to occur (PubMed:23826332).
CC {ECO:0000250|UniProtKB:Q9CY57, ECO:0000269|PubMed:23826332}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=3;
CC Name=1;
CC IsoId=Q9Y3Y2-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q9Y3Y2-3; Sequence=VSP_017277;
CC Name=3; Synonyms=SRAG-5;
CC IsoId=Q9Y3Y2-4; Sequence=VSP_040496;
CC -!- TISSUE SPECIFICITY: Expressed in an erythroid progenitor cell line
CC derived from peripheral blood. Expressed in glioblastoma cells
CC (PubMed:25284789). {ECO:0000269|PubMed:20688955,
CC ECO:0000269|PubMed:25284789}.
CC -!- PTM: Asymmetrically methylated by PRMT1 (PubMed:25284789).
CC Symmetrically methylated by PRMT5 (By similarity).
CC {ECO:0000250|UniProtKB:Q9CY57, ECO:0000269|PubMed:25284789}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAH02733.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
CC Sequence=AAH70027.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
CC Sequence=AAL55869.1; Type=Frameshift; Evidence={ECO:0000305};
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DR EMBL; AF261137; AAG44673.1; -; mRNA.
DR EMBL; AF318362; AAL55869.1; ALT_FRAME; mRNA.
DR EMBL; AL162258; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH471121; EAW53290.1; -; Genomic_DNA.
DR EMBL; CH471121; EAW53295.1; -; Genomic_DNA.
DR EMBL; BC002733; AAH02733.1; ALT_INIT; mRNA.
DR EMBL; BC059949; AAH59949.1; -; mRNA.
DR EMBL; BC070027; AAH70027.1; ALT_INIT; mRNA.
DR EMBL; BC108721; AAI08722.1; -; mRNA.
DR EMBL; BC120961; AAI20962.1; -; mRNA.
DR EMBL; BC120962; AAI20963.1; -; mRNA.
DR EMBL; AL050260; CAB43362.2; -; mRNA.
DR EMBL; AL512704; CAC21650.2; -; mRNA.
DR CCDS; CCDS1048.1; -. [Q9Y3Y2-1]
DR CCDS; CCDS72917.1; -. [Q9Y3Y2-3]
DR CCDS; CCDS81380.1; -. [Q9Y3Y2-4]
DR PIR; T08660; T08660.
DR RefSeq; NP_001193541.1; NM_001206612.1. [Q9Y3Y2-3]
DR RefSeq; NP_001231593.1; NM_001244664.1.
DR RefSeq; NP_001304006.1; NM_001317077.1. [Q9Y3Y2-4]
DR RefSeq; NP_056422.2; NM_015607.3. [Q9Y3Y2-1]
DR AlphaFoldDB; Q9Y3Y2; -.
DR SMR; Q9Y3Y2; -.
DR BioGRID; 117547; 169.
DR CORUM; Q9Y3Y2; -.
DR IntAct; Q9Y3Y2; 92.
DR MINT; Q9Y3Y2; -.
DR STRING; 9606.ENSP00000357679; -.
DR iPTMnet; Q9Y3Y2; -.
DR MetOSite; Q9Y3Y2; -.
DR PhosphoSitePlus; Q9Y3Y2; -.
DR BioMuta; CHTOP; -.
DR EPD; Q9Y3Y2; -.
DR jPOST; Q9Y3Y2; -.
DR MassIVE; Q9Y3Y2; -.
DR MaxQB; Q9Y3Y2; -.
DR PaxDb; Q9Y3Y2; -.
DR PeptideAtlas; Q9Y3Y2; -.
DR PRIDE; Q9Y3Y2; -.
DR ProteomicsDB; 86084; -. [Q9Y3Y2-1]
DR ProteomicsDB; 86085; -. [Q9Y3Y2-3]
DR ProteomicsDB; 86086; -. [Q9Y3Y2-4]
DR Antibodypedia; 34133; 155 antibodies from 25 providers.
DR DNASU; 26097; -.
DR Ensembl; ENST00000368690.7; ENSP00000357679.4; ENSG00000160679.13. [Q9Y3Y2-3]
DR Ensembl; ENST00000368694.8; ENSP00000357683.3; ENSG00000160679.13. [Q9Y3Y2-1]
DR Ensembl; ENST00000403433.5; ENSP00000385228.1; ENSG00000160679.13. [Q9Y3Y2-4]
DR GeneID; 26097; -.
DR KEGG; hsa:26097; -.
DR MANE-Select; ENST00000368694.8; ENSP00000357683.3; NM_015607.4; NP_056422.2.
DR UCSC; uc001fcm.3; human. [Q9Y3Y2-1]
DR CTD; 26097; -.
DR DisGeNET; 26097; -.
DR GeneCards; CHTOP; -.
DR HGNC; HGNC:24511; CHTOP.
DR HPA; ENSG00000160679; Low tissue specificity.
DR MIM; 614206; gene.
DR neXtProt; NX_Q9Y3Y2; -.
DR OpenTargets; ENSG00000160679; -.
DR PharmGKB; PA142672526; -.
DR VEuPathDB; HostDB:ENSG00000160679; -.
DR eggNOG; ENOG502QV0X; Eukaryota.
DR GeneTree; ENSGT00390000002869; -.
DR HOGENOM; CLU_087638_0_0_1; -.
DR InParanoid; Q9Y3Y2; -.
DR OMA; AMQMENR; -.
DR OrthoDB; 1598721at2759; -.
DR PhylomeDB; Q9Y3Y2; -.
DR TreeFam; TF331447; -.
DR PathwayCommons; Q9Y3Y2; -.
DR Reactome; R-HSA-159236; Transport of Mature mRNA derived from an Intron-Containing Transcript.
DR Reactome; R-HSA-72187; mRNA 3'-end processing.
DR Reactome; R-HSA-73856; RNA Polymerase II Transcription Termination.
DR SignaLink; Q9Y3Y2; -.
DR BioGRID-ORCS; 26097; 150 hits in 1088 CRISPR screens.
DR ChiTaRS; CHTOP; human.
DR GenomeRNAi; 26097; -.
DR Pharos; Q9Y3Y2; Tbio.
DR PRO; PR:Q9Y3Y2; -.
DR Proteomes; UP000005640; Chromosome 1.
DR RNAct; Q9Y3Y2; protein.
DR Bgee; ENSG00000160679; Expressed in tendon of biceps brachii and 209 other tissues.
DR ExpressionAtlas; Q9Y3Y2; baseline and differential.
DR Genevisible; Q9Y3Y2; HS.
DR GO; GO:0036464; C:cytoplasmic ribonucleoprotein granule; IDA:HPA.
DR GO; GO:0016607; C:nuclear speck; IDA:UniProtKB.
DR GO; GO:0005730; C:nucleolus; IEA:UniProtKB-SubCell.
DR GO; GO:0005654; C:nucleoplasm; TAS:Reactome.
DR GO; GO:0005634; C:nucleus; IBA:GO_Central.
DR GO; GO:0000346; C:transcription export complex; IDA:UniProtKB.
DR GO; GO:0008327; F:methyl-CpG binding; IDA:UniProtKB.
DR GO; GO:0003729; F:mRNA binding; IBA:GO_Central.
DR GO; GO:0003723; F:RNA binding; HDA:UniProtKB.
DR GO; GO:0001701; P:in utero embryonic development; IEA:Ensembl.
DR GO; GO:0006406; P:mRNA export from nucleus; IDA:UniProtKB.
DR GO; GO:0032781; P:positive regulation of ATP-dependent activity; IDA:UniProtKB.
DR GO; GO:0008284; P:positive regulation of cell population proliferation; IMP:UniProtKB.
DR GO; GO:0051096; P:positive regulation of helicase activity; IDA:UniProtKB.
DR GO; GO:0031062; P:positive regulation of histone methylation; IMP: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;
KW mRNA transport; Nucleus; Phosphoprotein; Reference proteome; RNA-binding;
KW Transcription; Transcription regulation; Transport; Ubl conjugation.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0007744|PubMed:22814378"
FT CHAIN 2..248
FT /note="Chromatin target of PRMT1 protein"
FT /id="PRO_0000089263"
FT REGION 151..204
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 153..206
FT /note="Interaction with PRMT1"
FT /evidence="ECO:0000250"
FT MOTIF 194..203
FT /note="GAR motif; involved in 5hmC binding"
FT /evidence="ECO:0000269|PubMed:25284789"
FT MOD_RES 2
FT /note="N-acetylalanine"
FT /evidence="ECO:0007744|PubMed:22814378"
FT MOD_RES 33
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:20068231,
FT ECO:0007744|PubMed:23186163"
FT MOD_RES 40
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 49
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 64
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 242
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:17081983,
FT ECO:0007744|PubMed:20068231"
FT CROSSLNK 70
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:28112733"
FT VAR_SEQ 73
FT /note="Q -> QK (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_017277"
FT VAR_SEQ 134..179
FT /note="Missing (in isoform 3)"
FT /evidence="ECO:0000305"
FT /id="VSP_040496"
FT MUTAGEN 195
FT /note="R->A: Loss of 5hmc binding; when associated with A-
FT 197; A-199; A-201 and A-203."
FT /evidence="ECO:0000269|PubMed:25284789"
FT MUTAGEN 197
FT /note="R->A: Loss of 5hmc binding; when associated with A-
FT 195; A-199; A-201 and A-203."
FT /evidence="ECO:0000269|PubMed:25284789"
FT MUTAGEN 199
FT /note="R->A: Loss of 5hmc binding; when associated with A-
FT 195; A-197; A-201 and A-203."
FT /evidence="ECO:0000269|PubMed:25284789"
FT MUTAGEN 201
FT /note="R->A: Loss of 5hmc binding; when associated with A-
FT 195; A-197; A-199 and A-203."
FT /evidence="ECO:0000269|PubMed:25284789"
FT MUTAGEN 203
FT /note="R->A: Loss of 5hmc binding; when associated with A-
FT 195; A-197; A-199 and A-201."
FT /evidence="ECO:0000269|PubMed:25284789"
FT CONFLICT 72
FT /note="K -> N (in Ref. 5; AAH59949)"
FT /evidence="ECO:0000305"
FT CONFLICT 180
FT /note="R -> P (in Ref. 6; CAB43362)"
FT /evidence="ECO:0000305"
FT CONFLICT 238
FT /note="Y -> H (in Ref. 6; CAB43362)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 248 AA; 26397 MW; 3D97D16610FCE0E6 CRC64;
MAAQSAPKVV LKSTTKMSLN ERFTNMLKNK QPTPVNIRAS MQQQQQLASA RNRRLAQQME
NRPSVQAALK LKQSLKQRLG KSNIQARLGR PIGALARGAI GGRGLPIIQR GLPRGGLRGG
RATRTLLRGG MSLRGQNLLR GGRAVAPRMG LRRGGVRGRG GPGRGGLGRG AMGRGGIGGR
GRGMIGRGRG GFGGRGRGRG RGRGALARPV LTKEQLDNQL DAYMSKTKGH LDAELDAYMA
QTDPETND
