RFXAP_MOUSE
ID RFXAP_MOUSE Reviewed; 231 AA.
AC Q8VCG9; Q91Y54;
DT 11-SEP-2007, integrated into UniProtKB/Swiss-Prot.
DT 05-SEP-2006, sequence version 2.
DT 03-AUG-2022, entry version 104.
DE RecName: Full=Regulatory factor X-associated protein;
DE Short=RFX-associated protein;
GN Name=Rfxap;
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], AND USE OF A NON-AUG INITIATOR START CODON.
RC TISSUE=Spleen;
RX PubMed=11486010; DOI=10.1128/mcb.21.17.5699-5709.2001;
RA Peretti M., Villard J., Barras E., Zufferey M., Reith W.;
RT "Expression of the three human major histocompatibility complex class II
RT isotypes exhibits a differential dependence on the transcription factor
RT RFXAP.";
RL Mol. Cell. Biol. 21:5699-5709(2001).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=FVB/N; TISSUE=Kidney;
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).
CC -!- FUNCTION: Part of the RFX complex that binds to the X-box of MHC II
CC promoters. {ECO:0000250}.
CC -!- SUBUNIT: RFX consists of at least 3 different subunits; RFXAP, RFX5 and
CC RFX-B/RFXANK; with each subunit representing a separate complementation
CC group. RFX forms cooperative DNA binding complexes with X2BP and
CC CBF/NF-Y. RFX associates with CIITA to form an active transcriptional
CC complex (By similarity). {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250}.
CC -!- PTM: Phosphorylated. {ECO:0000250}.
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DR EMBL; AF335512; AAK38586.1; -; mRNA.
DR EMBL; BC019935; AAH19935.2; -; mRNA.
DR CCDS; CCDS50907.1; -.
DR RefSeq; NP_573494.1; NM_133231.2.
DR AlphaFoldDB; Q8VCG9; -.
DR SMR; Q8VCG9; -.
DR BioGRID; 228427; 1.
DR IntAct; Q8VCG9; 1.
DR STRING; 10090.ENSMUSP00000040917; -.
DR PhosphoSitePlus; Q8VCG9; -.
DR EPD; Q8VCG9; -.
DR MaxQB; Q8VCG9; -.
DR PaxDb; Q8VCG9; -.
DR PRIDE; Q8VCG9; -.
DR ProteomicsDB; 253120; -.
DR Antibodypedia; 8059; 184 antibodies from 25 providers.
DR DNASU; 170767; -.
DR Ensembl; ENSMUST00000044373; ENSMUSP00000040917; ENSMUSG00000036615.
DR GeneID; 170767; -.
DR KEGG; mmu:170767; -.
DR UCSC; uc008pfw.1; mouse.
DR CTD; 5994; -.
DR MGI; MGI:2180854; Rfxap.
DR eggNOG; ENOG502RYED; Eukaryota.
DR GeneTree; ENSGT00390000006573; -.
DR InParanoid; Q8VCG9; -.
DR OMA; HPCGGQD; -.
DR OrthoDB; 1504851at2759; -.
DR PhylomeDB; Q8VCG9; -.
DR BioGRID-ORCS; 170767; 3 hits in 71 CRISPR screens.
DR ChiTaRS; Rfxap; mouse.
DR PRO; PR:Q8VCG9; -.
DR Proteomes; UP000000589; Chromosome 3.
DR RNAct; Q8VCG9; protein.
DR Bgee; ENSMUSG00000036615; Expressed in spermatocyte and 241 other tissues.
DR ExpressionAtlas; Q8VCG9; baseline and differential.
DR GO; GO:0016607; C:nuclear speck; ISO:MGI.
DR GO; GO:0005634; C:nucleus; IDA:MGI.
DR GO; GO:0090575; C:RNA polymerase II transcription regulator complex; ISO:MGI.
DR GO; GO:0003677; F:DNA binding; IDA:MGI.
DR GO; GO:0001228; F:DNA-binding transcription activator activity, RNA polymerase II-specific; ISO:MGI.
DR GO; GO:0000977; F:RNA polymerase II transcription regulatory region sequence-specific DNA binding; ISO:MGI.
DR GO; GO:0045944; P:positive regulation of transcription by RNA polymerase II; ISO:MGI.
DR GO; GO:0045893; P:positive regulation of transcription, DNA-templated; IDA:MGI.
DR GO; GO:0006357; P:regulation of transcription by RNA polymerase II; IBA:GO_Central.
DR Gene3D; 6.10.290.30; -; 1.
DR InterPro; IPR038308; RFXAP_C_sf.
DR InterPro; IPR029316; RFXAP_RFXANK-bd.
DR PANTHER; PTHR15110; PTHR15110; 1.
DR Pfam; PF15289; RFXA_RFXANK_bdg; 1.
PE 2: Evidence at transcript level;
KW DNA-binding; Isopeptide bond; Nucleus; Phosphoprotein; Reference proteome;
KW Ubl conjugation.
FT CHAIN 1..231
FT /note="Regulatory factor X-associated protein"
FT /id="PRO_0000300252"
FT REGION 1..163
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 123..138
FT /note="Nuclear localization signal"
FT /evidence="ECO:0000255"
FT COMPBIAS 51..65
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 118..133
FT /note="Basic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 145..163
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT CROSSLNK 157
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:O00287"
SQ SEQUENCE 231 AA; 24787 MW; 4BB22676F5A4FA55 CRC64;
MEAQAVPEGS GPSTASPRTA PPVTVLVMRQ DEAEADGALR PGLAGSEAAA DAEDEAGDDD
ADLLDTSDPA GGGESAASPE ELEDEDAEGG GAARRRGSKT CTYEGCRETT SQVAKQRKPW
MCKKHRNKMY KDKYKKKKSD QALGSGGPSA ASTGNVKLEE STDNILSIVK QRTGSFGDRP
ARPTLLEQVL NQKRLSLLRS PEVVQFLQKQ QQLLNQQVLE QRQQHFPGAP V