RFX1_HUMAN
ID RFX1_HUMAN Reviewed; 979 AA.
AC P22670;
DT 01-AUG-1991, integrated into UniProtKB/Swiss-Prot.
DT 09-FEB-2010, sequence version 2.
DT 03-AUG-2022, entry version 204.
DE RecName: Full=MHC class II regulatory factor RFX1;
DE AltName: Full=Enhancer factor C;
DE Short=EF-C;
DE AltName: Full=Regulatory factor X 1;
DE Short=RFX;
DE AltName: Full=Transcription factor RFX1;
GN Name=RFX1;
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 [MRNA], AND VARIANT ALA-370.
RX PubMed=2253877; DOI=10.1101/gad.4.9.1528;
RA Reith W., Sanchez-Herrero C., Kobr M., Silacci P., Berte C., Barras E.,
RA Mach B.;
RT "MHC class II regulatory factor RFX has a novel DNA-binding domain and a
RT functionally independent dimerization domain.";
RL Genes Dev. 4:1528-1540(1990).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=15057824; DOI=10.1038/nature02399;
RA Grimwood J., Gordon L.A., Olsen A.S., Terry A., Schmutz J., Lamerdin J.E.,
RA Hellsten U., Goodstein D., Couronne O., Tran-Gyamfi M., Aerts A.,
RA Altherr M., Ashworth L., Bajorek E., Black S., Branscomb E., Caenepeel S.,
RA Carrano A.V., Caoile C., Chan Y.M., Christensen M., Cleland C.A.,
RA Copeland A., Dalin E., Dehal P., Denys M., Detter J.C., Escobar J.,
RA Flowers D., Fotopulos D., Garcia C., Georgescu A.M., Glavina T., Gomez M.,
RA Gonzales E., Groza M., Hammon N., Hawkins T., Haydu L., Ho I., Huang W.,
RA Israni S., Jett J., Kadner K., Kimball H., Kobayashi A., Larionov V.,
RA Leem S.-H., Lopez F., Lou Y., Lowry S., Malfatti S., Martinez D.,
RA McCready P.M., Medina C., Morgan J., Nelson K., Nolan M., Ovcharenko I.,
RA Pitluck S., Pollard M., Popkie A.P., Predki P., Quan G., Ramirez L.,
RA Rash S., Retterer J., Rodriguez A., Rogers S., Salamov A., Salazar A.,
RA She X., Smith D., Slezak T., Solovyev V., Thayer N., Tice H., Tsai M.,
RA Ustaszewska A., Vo N., Wagner M., Wheeler J., Wu K., Xie G., Yang J.,
RA Dubchak I., Furey T.S., DeJong P., Dickson M., Gordon D., Eichler E.E.,
RA Pennacchio L.A., Richardson P., Stubbs L., Rokhsar D.S., Myers R.M.,
RA Rubin E.M., Lucas S.M.;
RT "The DNA sequence and biology of human chromosome 19.";
RL Nature 428:529-535(2004).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA], AND VARIANT ALA-370.
RC TISSUE=Testis;
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 [4]
RP IDENTITY OF RFX1 AND EF-C.
RX PubMed=8413236; DOI=10.1128/mcb.13.10.6375-6384.1993;
RA Siegrist C.A., Durand B., Emery P., David E., Hearing P., Mach B.,
RA Reith W.;
RT "RFX1 is identical to enhancer factor C and functions as a transactivator
RT of the hepatitis B virus enhancer.";
RL Mol. Cell. Biol. 13:6375-6384(1993).
RN [5]
RP BINDING TO RPL30 PROMOTER.
RX PubMed=8224874; DOI=10.1016/0378-1119(93)90208-k;
RA Safrany G., Perry R.P.;
RT "Transcription factor RFX1 helps control the promoter of the mouse
RT ribosomal protein-encoding gene rpL30 by binding to its alpha element.";
RL Gene 132:279-283(1993).
RN [6]
RP SUBUNIT.
RX PubMed=10330134; DOI=10.1128/mcb.19.6.3940;
RA Iwama A., Pan J., Zhang P., Reith W., Mach B., Tenen D.G., Sun Z.;
RT "Dimeric RFX proteins contribute to the activity and lineage specificity of
RT the interleukin-5 receptor alpha promoter through activation and repression
RT domains.";
RL Mol. Cell. Biol. 19:3940-3950(1999).
RN [7]
RP SHOWS THAT BLS II IS NOT DUE TO RFX1.
RX PubMed=1508204; DOI=10.1128/mcb.12.9.4076-4083.1992;
RA Sanchez-Herrero C., Reith W., Silacci P., Mach B.;
RT "The DNA-binding defect observed in major histocompatibility complex class
RT II regulatory mutants concerns only one member of a family of complexes
RT binding to the X boxes of class II promoters.";
RL Mol. Cell. Biol. 12:4076-4083(1992).
RN [8]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=18691976; DOI=10.1016/j.molcel.2008.07.007;
RA Daub H., Olsen J.V., Bairlein M., Gnad F., Oppermann F.S., Korner R.,
RA Greff Z., Keri G., Stemmann O., Mann M.;
RT "Kinase-selective enrichment enables quantitative phosphoproteomics of the
RT kinome across the cell cycle.";
RL Mol. Cell 31:438-448(2008).
RN [9]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=18669648; DOI=10.1073/pnas.0805139105;
RA Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,
RA Elledge S.J., Gygi S.P.;
RT "A quantitative atlas of mitotic phosphorylation.";
RL Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008).
RN [10]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Leukemic T-cell;
RX PubMed=19690332; DOI=10.1126/scisignal.2000007;
RA Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K.,
RA Rodionov V., Han D.K.;
RT "Quantitative phosphoproteomic analysis of T cell receptor signaling
RT reveals system-wide modulation of protein-protein interactions.";
RL Sci. Signal. 2:RA46-RA46(2009).
RN [11]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-978 AND SER-979, 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 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 [14]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-60, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Liver;
RX PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014;
RA Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., Wang L.,
RA Ye M., Zou H.;
RT "An enzyme assisted RP-RPLC approach for in-depth analysis of human liver
RT phosphoproteome.";
RL J. Proteomics 96:253-262(2014).
RN [15]
RP X-RAY CRYSTALLOGRAPHY (1.5 ANGSTROMS) OF 438-513 IN COMPLEX WITH DNA.
RX PubMed=10706293; DOI=10.1038/35002634;
RA Gajiwala K.S., Chen H., Cornille F., Roques B.P., Reith W., Mach B.,
RA Burley S.K.;
RT "Structure of the winged-helix protein hRFX1 reveals a new mode of DNA
RT binding.";
RL Nature 403:916-921(2000).
CC -!- FUNCTION: Regulatory factor essential for MHC class II genes
CC expression. Binds to the X boxes of MHC class II genes. Also binds to
CC an inverted repeat (ENH1) required for hepatitis B virus genes
CC expression and to the most upstream element (alpha) of the RPL30
CC promoter.
CC -!- SUBUNIT: Homodimer; binds DNA as a homodimer (PubMed:10706293).
CC Heterodimer; heterodimerizes with RFX2 and RFX3 (PubMed:10330134).
CC {ECO:0000269|PubMed:10330134, ECO:0000269|PubMed:10706293}.
CC -!- INTERACTION:
CC P22670; P32314: FOXN2; NbExp=3; IntAct=EBI-716037, EBI-10706164;
CC -!- SUBCELLULAR LOCATION: Nucleus.
CC -!- SIMILARITY: Belongs to the RFX family. {ECO:0000255|PROSITE-
CC ProRule:PRU00858}.
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; X58964; CAA41730.1; -; mRNA.
DR EMBL; AC020916; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AC022098; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC049826; AAH49826.1; -; mRNA.
DR CCDS; CCDS12301.1; -.
DR PIR; A35913; A35913.
DR RefSeq; NP_002909.4; NM_002918.4.
DR PDB; 1DP7; X-ray; 1.50 A; P=438-513.
DR PDBsum; 1DP7; -.
DR AlphaFoldDB; P22670; -.
DR SMR; P22670; -.
DR BioGRID; 111921; 58.
DR IntAct; P22670; 25.
DR MINT; P22670; -.
DR STRING; 9606.ENSP00000254325; -.
DR GlyGen; P22670; 1 site, 1 O-linked glycan (1 site).
DR iPTMnet; P22670; -.
DR PhosphoSitePlus; P22670; -.
DR SwissPalm; P22670; -.
DR BioMuta; RFX1; -.
DR DMDM; 288558824; -.
DR EPD; P22670; -.
DR jPOST; P22670; -.
DR MassIVE; P22670; -.
DR MaxQB; P22670; -.
DR PaxDb; P22670; -.
DR PeptideAtlas; P22670; -.
DR PRIDE; P22670; -.
DR ProteomicsDB; 54012; -.
DR Antibodypedia; 26599; 185 antibodies from 25 providers.
DR DNASU; 5989; -.
DR Ensembl; ENST00000254325.9; ENSP00000254325.3; ENSG00000132005.9.
DR Ensembl; ENST00000672295.1; ENSP00000500760.1; ENSG00000288283.1.
DR GeneID; 5989; -.
DR KEGG; hsa:5989; -.
DR MANE-Select; ENST00000254325.9; ENSP00000254325.3; NM_002918.5; NP_002909.4.
DR UCSC; uc002mxv.4; human.
DR CTD; 5989; -.
DR DisGeNET; 5989; -.
DR GeneCards; RFX1; -.
DR HGNC; HGNC:9982; RFX1.
DR HPA; ENSG00000132005; Low tissue specificity.
DR MIM; 600006; gene.
DR neXtProt; NX_P22670; -.
DR OpenTargets; ENSG00000132005; -.
DR PharmGKB; PA34352; -.
DR VEuPathDB; HostDB:ENSG00000132005; -.
DR eggNOG; KOG3712; Eukaryota.
DR GeneTree; ENSGT01050000244879; -.
DR HOGENOM; CLU_010393_1_0_1; -.
DR InParanoid; P22670; -.
DR OMA; QVHSVQA; -.
DR OrthoDB; 346630at2759; -.
DR PhylomeDB; P22670; -.
DR TreeFam; TF321340; -.
DR PathwayCommons; P22670; -.
DR SignaLink; P22670; -.
DR SIGNOR; P22670; -.
DR BioGRID-ORCS; 5989; 12 hits in 1104 CRISPR screens.
DR ChiTaRS; RFX1; human.
DR EvolutionaryTrace; P22670; -.
DR GeneWiki; RFX1; -.
DR GenomeRNAi; 5989; -.
DR Pharos; P22670; Tbio.
DR PRO; PR:P22670; -.
DR Proteomes; UP000005640; Chromosome 19.
DR RNAct; P22670; protein.
DR Bgee; ENSG00000132005; Expressed in right testis and 93 other tissues.
DR ExpressionAtlas; P22670; baseline and differential.
DR Genevisible; P22670; HS.
DR GO; GO:0000785; C:chromatin; ISA:NTNU_SB.
DR GO; GO:0043231; C:intracellular membrane-bounded organelle; IDA:HPA.
DR GO; GO:0005654; C:nucleoplasm; IDA:HPA.
DR GO; GO:0000981; F:DNA-binding transcription factor activity, RNA polymerase II-specific; ISA:NTNU_SB.
DR GO; GO:0000978; F:RNA polymerase II cis-regulatory region sequence-specific DNA binding; IBA:GO_Central.
DR GO; GO:1990837; F:sequence-specific double-stranded DNA binding; IDA:ARUK-UCL.
DR GO; GO:0006955; P:immune response; TAS:ProtInc.
DR GO; GO:0006357; P:regulation of transcription by RNA polymerase II; IBA:GO_Central.
DR Gene3D; 1.10.10.10; -; 1.
DR InterPro; IPR003150; DNA-bd_RFX.
DR InterPro; IPR039779; RFX-like.
DR InterPro; IPR007668; RFX1_trans_act.
DR InterPro; IPR036388; WH-like_DNA-bd_sf.
DR InterPro; IPR036390; WH_DNA-bd_sf.
DR PANTHER; PTHR12619; PTHR12619; 1.
DR Pfam; PF04589; RFX1_trans_act; 1.
DR Pfam; PF02257; RFX_DNA_binding; 1.
DR SUPFAM; SSF46785; SSF46785; 1.
DR PROSITE; PS51526; RFX_DBD; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Activator; DNA-binding; Nucleus; Phosphoprotein;
KW Reference proteome; Transcription; Transcription regulation.
FT CHAIN 1..979
FT /note="MHC class II regulatory factor RFX1"
FT /id="PRO_0000215286"
FT DNA_BIND 438..513
FT /note="RFX-type winged-helix"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00858"
FT REGION 1..136
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 181..227
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 370..405
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 744..979
FT /note="Necessary for dimerization"
FT REGION 915..960
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 12..48
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 49..71
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 110..136
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 370..384
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 921..938
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 60
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:24275569"
FT MOD_RES 978
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:20068231"
FT MOD_RES 979
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:20068231"
FT VARIANT 370
FT /note="T -> A (in dbSNP:rs2305780)"
FT /evidence="ECO:0000269|PubMed:15489334,
FT ECO:0000269|PubMed:2253877"
FT /id="VAR_059781"
FT HELIX 439..445
FT /evidence="ECO:0007829|PDB:1DP7"
FT STRAND 446..455
FT /evidence="ECO:0007829|PDB:1DP7"
FT HELIX 456..469
FT /evidence="ECO:0007829|PDB:1DP7"
FT HELIX 477..487
FT /evidence="ECO:0007829|PDB:1DP7"
FT STRAND 492..498
FT /evidence="ECO:0007829|PDB:1DP7"
FT STRAND 503..511
FT /evidence="ECO:0007829|PDB:1DP7"
SQ SEQUENCE 979 AA; 104758 MW; 4FD8EA9C4AB1A411 CRC64;
MATQAYTELQ AAPPPSQPPQ APPQAQPQPP PPPPPAAPQP PQPPTAAATP QPQYVTELQS
PQPQAQPPGG QKQYVTELPA VPAPSQPTGA PTPSPAPQQY IVVTVSEGAM RASETVSEAS
PGSTASQTGV PTQVVQQVQG TQQRLLVQTS VQAKPGHVSP LQLTNIQVPQ QALPTQRLVV
QSAAPGSKGG QVSLTVHGTQ QVHSPPEQSP VQANSSSSKT AGAPTGTVPQ QLQVHGVQQS
VPVTQERSVV QATPQAPKPG PVQPLTVQGL QPVHVAQEVQ QLQQVPVPHV YSSQVQYVEG
GDASYTASAI RSSTYSYPET PLYTQTASTS YYEAAGTATQ VSTPATSQAV ASSGSMPMYV
SGSQVVASST STGAGASNSS GGGGSGGGGG GGGGGGGGGS GSTGGGGSGA GTYVIQGGYM
LGSASQSYSH TTRASPATVQ WLLDNYETAE GVSLPRSTLY CHYLLHCQEQ KLEPVNAASF
GKLIRSVFMG LRTRRLGTRG NSKYHYYGLR IKASSPLLRL MEDQQHMAMR GQPFSQKQRL
KPIQKMEGMT NGVAVGQQPS TGLSDISAQV QQYQQFLDAS RSLPDFTELD LQGKVLPEGV
GPGDIKAFQV LYREHCEAIV DVMVNLQFTL VETLWKTFWR YNLSQPSEAP PLAVHDEAEK
RLPKAILVLL SKFEPVLQWT KHCDNVLYQG LVEILIPDVL RPIPSALTQA IRNFAKSLES
WLTHAMVNIP EEMLRVKVAA AGAFAQTLRR YTSLNHLAQA ARAVLQNTAQ INQMLSDLNR
VDFANVQEQA SWVCRCEDRV VQRLEQDFKV TLQQQNSLEQ WAAWLDGVVS QVLKPYQGSA
GFPKAAKLFL LKWSFYSSMV IRDLTLRSAA SFGSFHLIRL LYDEYMYYLI EHRVAQAKGE
TPIAVMGEFA NLATSLNPLD PDKDEEEEEE EESEDELPQD ISLAAGGESP ALGPETLEPP
AKLARTDARG LFVQALPSS
