CHTOP_BOVIN
ID CHTOP_BOVIN Reviewed; 248 AA.
AC Q3SYW9;
DT 10-JAN-2006, integrated into UniProtKB/Swiss-Prot.
DT 11-OCT-2005, sequence version 1.
DT 03-AUG-2022, entry version 91.
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;
OS Bos taurus (Bovine).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae;
OC Bovinae; Bos.
OX NCBI_TaxID=9913;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=Crossbred X Angus; TISSUE=Ileum;
RG NIH - Mammalian Gene Collection (MGC) project;
RL Submitted (AUG-2005) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Plays an important role in the ligand-dependent activation of
CC estrogen receptor target genes. May play a role in the silencing of
CC fetal globin genes. Recruits the 5FMC complex to ZNF148, leading to
CC desumoylation of ZNF148 and subsequent transactivation of ZNF148 target
CC genes. Required for the tumorigenicity of glioblastoma cells. Binds to
CC 5-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 (By similarity).
CC {ECO:0000250|UniProtKB:Q9CY57, ECO:0000250|UniProtKB:Q9Y3Y2}.
CC -!- SUBUNIT: Interacts with PRMT1 and PRMT5. Interacts with the 5FMC
CC complex; the interaction is methylation-dependent. Interacts with
CC FYTTD1, SET and PRC1 complex members CBX4, RNF2 and PHC2; the
CC interactions are methylation-independent. Interacts with ZNF148.
CC Interacts with WDR77 and ER (By similarity).
CC {ECO:0000250|UniProtKB:Q9CY57, ECO:0000250|UniProtKB:Q9Y3Y2}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:Q9Y3Y2}. Nucleus,
CC nucleolus {ECO:0000250|UniProtKB:Q9Y3Y2}. Nucleus, nucleoplasm
CC {ECO:0000250|UniProtKB:Q9Y3Y2}. Nucleus speckle
CC {ECO:0000250|UniProtKB:Q9Y3Y2}. Note=Mostly associated with facultative
CC heterochromatin (By similarity). Localizes to regions surrounding
CC nuclear speckles known as perispeckles in which TREX complex assembly
CC seems to occur (By similarity). {ECO:0000250|UniProtKB:Q9CY57,
CC ECO:0000250|UniProtKB:Q9Y3Y2}.
CC -!- PTM: Asymmetrically methylated by PRMT1. Symmetrically methylated by
CC PRMT5 (By similarity). {ECO:0000250|UniProtKB:Q9CY57}.
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DR EMBL; BC103347; AAI03348.1; -; mRNA.
DR RefSeq; NP_001030558.1; NM_001035481.2.
DR AlphaFoldDB; Q3SYW9; -.
DR SMR; Q3SYW9; -.
DR STRING; 9913.ENSBTAP00000033800; -.
DR PaxDb; Q3SYW9; -.
DR PRIDE; Q3SYW9; -.
DR GeneID; 616638; -.
DR KEGG; bta:616638; -.
DR CTD; 26097; -.
DR eggNOG; ENOG502QV0X; Eukaryota.
DR HOGENOM; CLU_087638_0_0_1; -.
DR InParanoid; Q3SYW9; -.
DR OrthoDB; 1598721at2759; -.
DR TreeFam; TF331447; -.
DR Proteomes; UP000009136; Unplaced.
DR GO; GO:0016607; C:nuclear speck; IBA:GO_Central.
DR GO; GO:0005730; C:nucleolus; IEA:UniProtKB-SubCell.
DR GO; GO:0005634; C:nucleus; IBA:GO_Central.
DR GO; GO:0008327; F:methyl-CpG binding; ISS:UniProtKB.
DR GO; GO:0003729; F:mRNA binding; IBA:GO_Central.
DR GO; GO:0006406; P:mRNA export from nucleus; IBA:GO_Central.
DR GO; GO:0008284; P:positive regulation of cell population proliferation; ISS:UniProtKB.
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 2: Evidence at transcript level;
KW Acetylation; Isopeptide bond; Methylation; Nucleus; Phosphoprotein;
KW Reference proteome; RNA-binding; Transcription; Transcription regulation;
KW Ubl conjugation.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000250|UniProtKB:Q9Y3Y2"
FT CHAIN 2..248
FT /note="Chromatin target of PRMT1 protein"
FT /id="PRO_0000089262"
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: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 242
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"
SQ SEQUENCE 248 AA; 26427 MW; C2D5ADC78FB0417D CRC64;
MAAQSAPKVV LKSTTKMSLN ERFTNMLKNK QPMPVNIRAS MQQQQQLASA RNRRLAQQME
NRPSVQAALK LKQSLKQRLG KSNIQARLGR PIGALARGAI GGRGLPIIQR GLPRGGLRGG
RATRTLLRGG MSLRGQNLLR GGRAVAPRMG LRRGGVRGRG GPGRGGLGRG AMGRGGIGGR
GRGMIGRGRG GFGGRGRGRG RGRGALARPV LTKEQLDNQL DAYMSKTKGH LDAELDAYMA
QTDPETND
