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 24-JAN-2024, entry version 211. 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; 64. DR IntAct; P22670; 26. DR MINT; P22670; -. DR STRING; 9606.ENSP00000254325; -. DR GlyCosmos; P22670; 1 site, 1 glycan. DR GlyGen; P22670; 4 sites, 1 O-linked glycan (4 sites). 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; 9606-ENSP00000254325; -. DR PeptideAtlas; P22670; -. DR ProteomicsDB; 54012; -. DR Pumba; P22670; -. DR Antibodypedia; 26599; 200 antibodies from 26 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 AGR; HGNC:9982; -. 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; CCLEDER; -. DR OrthoDB; 2915941at2759; -. DR PhylomeDB; P22670; -. DR TreeFam; TF321340; -. DR PathwayCommons; P22670; -. DR SignaLink; P22670; -. DR SIGNOR; P22670; -. DR BioGRID-ORCS; 5989; 13 hits in 1185 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 95 other cell types or tissues. DR ExpressionAtlas; P22670; baseline and differential. 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; Winged helix-like DNA-binding domain superfamily/Winged helix DNA-binding domain; 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:SF23; MHC CLASS II REGULATORY FACTOR RFX1; 1. DR PANTHER; PTHR12619; RFX TRANSCRIPTION FACTOR FAMILY; 1. DR Pfam; PF04589; RFX1_trans_act; 1. DR Pfam; PF02257; RFX_DNA_binding; 1. DR SUPFAM; SSF46785; Winged helix' DNA-binding domain; 1. DR PROSITE; PS51526; RFX_DBD; 1. DR Genevisible; P22670; HS. 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 //