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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
 
 
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