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RFX5_HUMAN
ID   RFX5_HUMAN              Reviewed;         616 AA.
AC   P48382; B7Z848; D3DV19; E9PFU4; Q5VWC3;
DT   01-FEB-1996, integrated into UniProtKB/Swiss-Prot.
DT   01-FEB-1996, sequence version 1.
DT   03-AUG-2022, entry version 185.
DE   RecName: Full=DNA-binding protein RFX5;
DE   AltName: Full=Regulatory factor X 5;
GN   Name=RFX5;
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] (ISOFORM 1).
RX   PubMed=7744245; DOI=10.1101/gad.9.9.1021;
RA   Steimle V., Durand B., Barras E., Zufferey M., Hadam M.R., Mach B.,
RA   Reith W.;
RT   "A novel DNA-binding regulatory factor is mutated in primary MHC class II
RT   deficiency (bare lymphocyte syndrome).";
RL   Genes Dev. 9:1021-1032(1995).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RC   TISSUE=Testis;
RX   PubMed=14702039; DOI=10.1038/ng1285;
RA   Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
RA   Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
RA   Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
RA   Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
RA   Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H.,
RA   Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M.,
RA   Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K.,
RA   Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T.,
RA   Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M.,
RA   Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S.,
RA   Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H.,
RA   Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K.,
RA   Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N.,
RA   Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
RA   Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
RA   Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
RA   Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
RA   Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y.,
RA   Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K.,
RA   Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T.,
RA   Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T.,
RA   Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y.,
RA   Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H.,
RA   Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y.,
RA   Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H.,
RA   Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O.,
RA   Isogai T., Sugano S.;
RT   "Complete sequencing and characterization of 21,243 full-length human
RT   cDNAs.";
RL   Nat. Genet. 36:40-45(2004).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=16710414; DOI=10.1038/nature04727;
RA   Gregory S.G., Barlow K.F., McLay K.E., Kaul R., Swarbreck D., Dunham A.,
RA   Scott C.E., Howe K.L., Woodfine K., Spencer C.C.A., Jones M.C., Gillson C.,
RA   Searle S., Zhou Y., Kokocinski F., McDonald L., Evans R., Phillips K.,
RA   Atkinson A., Cooper R., Jones C., Hall R.E., Andrews T.D., Lloyd C.,
RA   Ainscough R., Almeida J.P., Ambrose K.D., Anderson F., Andrew R.W.,
RA   Ashwell R.I.S., Aubin K., Babbage A.K., Bagguley C.L., Bailey J.,
RA   Beasley H., Bethel G., Bird C.P., Bray-Allen S., Brown J.Y., Brown A.J.,
RA   Buckley D., Burton J., Bye J., Carder C., Chapman J.C., Clark S.Y.,
RA   Clarke G., Clee C., Cobley V., Collier R.E., Corby N., Coville G.J.,
RA   Davies J., Deadman R., Dunn M., Earthrowl M., Ellington A.G., Errington H.,
RA   Frankish A., Frankland J., French L., Garner P., Garnett J., Gay L.,
RA   Ghori M.R.J., Gibson R., Gilby L.M., Gillett W., Glithero R.J.,
RA   Grafham D.V., Griffiths C., Griffiths-Jones S., Grocock R., Hammond S.,
RA   Harrison E.S.I., Hart E., Haugen E., Heath P.D., Holmes S., Holt K.,
RA   Howden P.J., Hunt A.R., Hunt S.E., Hunter G., Isherwood J., James R.,
RA   Johnson C., Johnson D., Joy A., Kay M., Kershaw J.K., Kibukawa M.,
RA   Kimberley A.M., King A., Knights A.J., Lad H., Laird G., Lawlor S.,
RA   Leongamornlert D.A., Lloyd D.M., Loveland J., Lovell J., Lush M.J.,
RA   Lyne R., Martin S., Mashreghi-Mohammadi M., Matthews L., Matthews N.S.W.,
RA   McLaren S., Milne S., Mistry S., Moore M.J.F., Nickerson T., O'Dell C.N.,
RA   Oliver K., Palmeiri A., Palmer S.A., Parker A., Patel D., Pearce A.V.,
RA   Peck A.I., Pelan S., Phelps K., Phillimore B.J., Plumb R., Rajan J.,
RA   Raymond C., Rouse G., Saenphimmachak C., Sehra H.K., Sheridan E.,
RA   Shownkeen R., Sims S., Skuce C.D., Smith M., Steward C., Subramanian S.,
RA   Sycamore N., Tracey A., Tromans A., Van Helmond Z., Wall M., Wallis J.M.,
RA   White S., Whitehead S.L., Wilkinson J.E., Willey D.L., Williams H.,
RA   Wilming L., Wray P.W., Wu Z., Coulson A., Vaudin M., Sulston J.E.,
RA   Durbin R.M., Hubbard T., Wooster R., Dunham I., Carter N.P., McVean G.,
RA   Ross M.T., Harrow J., Olson M.V., Beck S., Rogers J., Bentley D.R.;
RT   "The DNA sequence and biological annotation of human chromosome 1.";
RL   Nature 441:315-321(2006).
RN   [4]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA   Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M.,
RA   Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J.,
RA   Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S.,
RA   Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H.,
RA   Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K.,
RA   Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D.,
RA   Hunkapiller M.W., Myers E.W., Venter J.C.;
RL   Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
RN   [5]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC   TISSUE=Uterus;
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   [6]
RP   PARTIAL PROTEIN SEQUENCE.
RC   TISSUE=Lymphoblast;
RX   PubMed=10072068; DOI=10.1016/s1074-7613(00)80016-3;
RA   Nagarajan U.M., Louis-Plence P., DeSandro A., Nilsen R., Bushey A.,
RA   Boss J.M.;
RT   "RFX-B is the gene responsible for the most common cause of the bare
RT   lymphocyte syndrome, an MHC class II immunodeficiency.";
RL   Immunity 10:153-162(1999).
RN   [7]
RP   ERRATUM OF PUBMED:10072068.
RA   Nagarajan U.M., Louis-Plence P., DeSandro A., Nilsen R., Bushey A.,
RA   Boss J.M.;
RL   Immunity 10:399-399(1999).
RN   [8]
RP   CHARACTERIZATION.
RX   PubMed=10779326; DOI=10.1128/mcb.20.10.3364-3376.2000;
RA   Villard J., Peretti M., Masternak K., Barras E., Caretti G., Mantovani R.,
RA   Reith W.;
RT   "A functionally essential domain of RFX5 mediates activation of major
RT   histocompatibility complex class II promoters by promoting cooperative
RT   binding between RFX and NF-Y.";
RL   Mol. Cell. Biol. 20:3364-3376(2000).
RN   [9]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-185, AND IDENTIFICATION BY
RP   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   [10]
RP   ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, CLEAVAGE OF INITIATOR
RP   METHIONINE [LARGE SCALE ANALYSIS], AND IDENTIFICATION BY MASS SPECTROMETRY
RP   [LARGE SCALE ANALYSIS].
RX   PubMed=22814378; DOI=10.1073/pnas.1210303109;
RA   Van Damme P., Lasa M., Polevoda B., Gazquez C., Elosegui-Artola A.,
RA   Kim D.S., De Juan-Pardo E., Demeyer K., Hole K., Larrea E., Timmerman E.,
RA   Prieto J., Arnesen T., Sherman F., Gevaert K., Aldabe R.;
RT   "N-terminal acetylome analyses and functional insights of the N-terminal
RT   acetyltransferase NatB.";
RL   Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012).
RN   [11]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-10, AND IDENTIFICATION BY
RP   MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   TISSUE=Cervix carcinoma, and 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   [12]
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   TISSUE=Colon carcinoma;
RX   PubMed=24129315; DOI=10.1074/mcp.o113.027870;
RA   Guo A., Gu H., Zhou J., Mulhern D., Wang Y., Lee K.A., Yang V., Aguiar M.,
RA   Kornhauser J., Jia X., Ren J., Beausoleil S.A., Silva J.C., Vemulapalli V.,
RA   Bedford M.T., Comb M.J.;
RT   "Immunoaffinity enrichment and mass spectrometry analysis of protein
RT   methylation.";
RL   Mol. Cell. Proteomics 13:372-387(2014).
RN   [13]
RP   STRUCTURE BY NMR OF 24-90, SUBUNIT, AND DOMAIN N-TERMINAL.
RX   PubMed=20732328; DOI=10.1016/j.jmb.2010.08.025;
RA   Laird K.M., Briggs L.L., Boss J.M., Summers M.F., Garvie C.W.;
RT   "Solution structure of the heterotrimeric complex between the interaction
RT   domains of RFX5 and RFXAP from the RFX gene regulatory complex.";
RL   J. Mol. Biol. 403:40-51(2010).
RN   [14]
RP   X-RAY CRYSTALLOGRAPHY (1.57 ANGSTROMS) OF 167-183 IN COMPLEX WITH RFXANK,
RP   AND MOTIF.
RX   PubMed=22649097; DOI=10.1126/scisignal.2002979;
RA   Xu C., Jin J., Bian C., Lam R., Tian R., Weist R., You L., Nie J.,
RA   Bochkarev A., Tempel W., Tan C.S., Wasney G.A., Vedadi M., Gish G.D.,
RA   Arrowsmith C.H., Pawson T., Yang X.J., Min J.;
RT   "Sequence-specific recognition of a PxLPxI/L motif by an ankyrin repeat
RT   tumbler lock.";
RL   Sci. Signal. 5:RA39-RA39(2012).
RN   [15]
RP   VARIANT BLS2 GLN-149.
RX   PubMed=10825209; DOI=10.1128/mcb.20.12.4455-4461.2000;
RA   Nekrep N., Jabrane-Ferrat N., Peterlin B.M.;
RT   "Mutations in the bare lymphocyte syndrome define critical steps in the
RT   assembly of the regulatory factor X complex.";
RL   Mol. Cell. Biol. 20:4455-4461(2000).
CC   -!- FUNCTION: Activates transcription from class II MHC promoters.
CC       Recognizes X-boxes. Mediates cooperative binding between RFX and NF-Y.
CC       RFX binds the X1 box of MHC-II promoters.
CC   -!- SUBUNIT: Homodimer. The RFX heterotetrameric complex consists of 2
CC       molecules of RFX5 and one each of RFXAP and RFX-B/RFXANK; with each
CC       subunit representing a separate complementation group. Interacts (via
CC       PxLPxI/L motif) with RFXANK (via ankyrin repeats); the interaction is
CC       direct. RFX forms cooperative DNA binding complexes with X2BP and
CC       CBF/NF-Y. RFX associates with CIITA to form an active transcriptional
CC       complex. {ECO:0000269|PubMed:20732328, ECO:0000269|PubMed:22649097}.
CC   -!- INTERACTION:
CC       P48382; P33076: CIITA; NbExp=2; IntAct=EBI-923266, EBI-1538819;
CC       P48382; Q92769: HDAC2; NbExp=4; IntAct=EBI-923266, EBI-301821;
CC       P48382; O14593: RFXANK; NbExp=8; IntAct=EBI-923266, EBI-1057665;
CC       P48382; O00287: RFXAP; NbExp=11; IntAct=EBI-923266, EBI-3929296;
CC   -!- SUBCELLULAR LOCATION: Nucleus.
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=2;
CC       Name=1;
CC         IsoId=P48382-1; Sequence=Displayed;
CC       Name=2;
CC         IsoId=P48382-2; Sequence=VSP_055864;
CC   -!- TISSUE SPECIFICITY: Ubiquitous.
CC   -!- DOMAIN: The N-terminus is required for dimer formation, association
CC       with RFXANK and RFXAP, assembly of the RFX complex, and for binding of
CC       this complex to its X box target site in the MHC-II promoter. The C-
CC       terminus mediates cooperative binding between the RFX complex and NF-Y.
CC       {ECO:0000269|PubMed:20732328}.
CC   -!- DOMAIN: The PxLPxI/L motif mediates interaction with ankyrin repeats of
CC       RFXANK. {ECO:0000269|PubMed:22649097}.
CC   -!- PTM: Phosphorylated.
CC   -!- DISEASE: Bare lymphocyte syndrome 2 (BLS2) [MIM:209920]: A severe
CC       combined immunodeficiency disease with early onset. It is characterized
CC       by a profound defect in constitutive and interferon-gamma induced MHC
CC       II expression, absence of cellular and humoral T-cell response to
CC       antigen challenge, hypogammaglobulinemia and impaired antibody
CC       production. The consequence include extreme susceptibility to viral,
CC       bacterial and fungal infections. {ECO:0000269|PubMed:10825209}.
CC       Note=The disease is caused by variants affecting the gene represented
CC       in this entry.
CC   -!- SIMILARITY: Belongs to the RFX family. {ECO:0000255|PROSITE-
CC       ProRule:PRU00858}.
CC   -!- WEB RESOURCE: Name=RFX5base; Note=RFX5 mutation db;
CC       URL="http://structure.bmc.lu.se/idbase/RFX5base/";
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DR   EMBL; X85786; CAA59771.1; -; mRNA.
DR   EMBL; AK302891; BAH13834.1; -; mRNA.
DR   EMBL; AL391069; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; CH471121; EAW53446.1; -; Genomic_DNA.
DR   EMBL; CH471121; EAW53447.1; -; Genomic_DNA.
DR   EMBL; CH471121; EAW53448.1; -; Genomic_DNA.
DR   EMBL; BC017471; AAH17471.1; -; mRNA.
DR   CCDS; CCDS994.1; -. [P48382-1]
DR   PIR; I38155; I38155.
DR   RefSeq; NP_000440.1; NM_000449.3. [P48382-1]
DR   RefSeq; NP_001020774.1; NM_001025603.1. [P48382-1]
DR   RefSeq; XP_005245462.1; XM_005245405.1.
DR   RefSeq; XP_005245463.1; XM_005245406.3.
DR   RefSeq; XP_011508149.1; XM_011509847.1.
DR   RefSeq; XP_011508150.1; XM_011509848.1.
DR   RefSeq; XP_011508151.1; XM_011509849.1.
DR   RefSeq; XP_011508152.1; XM_011509850.1.
DR   PDB; 2KW3; NMR; -; A/B=24-90.
DR   PDB; 3V30; X-ray; 1.57 A; B=167-183.
DR   PDBsum; 2KW3; -.
DR   PDBsum; 3V30; -.
DR   AlphaFoldDB; P48382; -.
DR   SMR; P48382; -.
DR   BioGRID; 111925; 42.
DR   ComplexPortal; CPX-6461; RFX gene regulatory complex.
DR   CORUM; P48382; -.
DR   ELM; P48382; -.
DR   IntAct; P48382; 22.
DR   MINT; P48382; -.
DR   STRING; 9606.ENSP00000290524; -.
DR   GlyGen; P48382; 2 sites, 1 O-linked glycan (2 sites).
DR   iPTMnet; P48382; -.
DR   MetOSite; P48382; -.
DR   PhosphoSitePlus; P48382; -.
DR   BioMuta; RFX5; -.
DR   DMDM; 1350587; -.
DR   EPD; P48382; -.
DR   jPOST; P48382; -.
DR   MassIVE; P48382; -.
DR   MaxQB; P48382; -.
DR   PaxDb; P48382; -.
DR   PeptideAtlas; P48382; -.
DR   PRIDE; P48382; -.
DR   ProteomicsDB; 55886; -. [P48382-1]
DR   ProteomicsDB; 6925; -.
DR   Antibodypedia; 683; 299 antibodies from 34 providers.
DR   DNASU; 5993; -.
DR   Ensembl; ENST00000290524.8; ENSP00000290524.4; ENSG00000143390.18. [P48382-1]
DR   Ensembl; ENST00000368870.6; ENSP00000357864.2; ENSG00000143390.18. [P48382-1]
DR   Ensembl; ENST00000452671.7; ENSP00000389130.2; ENSG00000143390.18. [P48382-1]
DR   GeneID; 5993; -.
DR   KEGG; hsa:5993; -.
DR   MANE-Select; ENST00000452671.7; ENSP00000389130.2; NM_001025603.2; NP_001020774.1.
DR   UCSC; uc001exv.2; human. [P48382-1]
DR   CTD; 5993; -.
DR   DisGeNET; 5993; -.
DR   GeneCards; RFX5; -.
DR   HGNC; HGNC:9986; RFX5.
DR   HPA; ENSG00000143390; Low tissue specificity.
DR   MalaCards; RFX5; -.
DR   MIM; 209920; phenotype.
DR   MIM; 601863; gene.
DR   neXtProt; NX_P48382; -.
DR   OpenTargets; ENSG00000143390; -.
DR   Orphanet; 572; Immunodeficiency by defective expression of MHC class II.
DR   PharmGKB; PA34356; -.
DR   VEuPathDB; HostDB:ENSG00000143390; -.
DR   eggNOG; KOG3712; Eukaryota.
DR   GeneTree; ENSGT01050000244970; -.
DR   InParanoid; P48382; -.
DR   OMA; INMILPA; -.
DR   OrthoDB; 67697at2759; -.
DR   PhylomeDB; P48382; -.
DR   TreeFam; TF321340; -.
DR   PathwayCommons; P48382; -.
DR   SignaLink; P48382; -.
DR   SIGNOR; P48382; -.
DR   BioGRID-ORCS; 5993; 38 hits in 1102 CRISPR screens.
DR   ChiTaRS; RFX5; human.
DR   EvolutionaryTrace; P48382; -.
DR   GeneWiki; RFX5; -.
DR   GenomeRNAi; 5993; -.
DR   Pharos; P48382; Tbio.
DR   PRO; PR:P48382; -.
DR   Proteomes; UP000005640; Chromosome 1.
DR   RNAct; P48382; protein.
DR   Bgee; ENSG00000143390; Expressed in epithelium of nasopharynx and 200 other tissues.
DR   ExpressionAtlas; P48382; baseline and differential.
DR   Genevisible; P48382; 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:0005634; C:nucleus; IDA:ComplexPortal.
DR   GO; GO:0090575; C:RNA polymerase II transcription regulator complex; IPI:ARUK-UCL.
DR   GO; GO:0001228; F:DNA-binding transcription activator activity, RNA polymerase II-specific; IDA:NTNU_SB.
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:0000977; F:RNA polymerase II transcription regulatory region sequence-specific DNA binding; IDA:GO_Central.
DR   GO; GO:0043565; F:sequence-specific DNA binding; IDA:NTNU_SB.
DR   GO; GO:1990837; F:sequence-specific double-stranded DNA binding; IDA:ARUK-UCL.
DR   GO; GO:0000122; P:negative regulation of transcription by RNA polymerase II; IEA:Ensembl.
DR   GO; GO:0045348; P:positive regulation of MHC class II biosynthetic process; IC:ComplexPortal.
DR   GO; GO:0045944; P:positive regulation of transcription by RNA polymerase II; IDA:NTNU_SB.
DR   GO; GO:0006357; P:regulation of transcription by RNA polymerase II; IBA:GO_Central.
DR   Gene3D; 1.10.10.10; -; 1.
DR   IDEAL; IID00452; -.
DR   InterPro; IPR003150; DNA-bd_RFX.
DR   InterPro; IPR039779; RFX-like.
DR   InterPro; IPR033486; RFX5.
DR   InterPro; IPR029298; RFX5_C.
DR   InterPro; IPR040889; RFX5_N.
DR   InterPro; IPR036388; WH-like_DNA-bd_sf.
DR   InterPro; IPR036390; WH_DNA-bd_sf.
DR   PANTHER; PTHR12619; PTHR12619; 1.
DR   PANTHER; PTHR12619:SF18; PTHR12619:SF18; 1.
DR   Pfam; PF14621; RFX5_DNA_bdg; 1.
DR   Pfam; PF18326; RFX5_N; 1.
DR   Pfam; PF02257; RFX_DNA_binding; 1.
DR   SMART; SM01306; RFX5_DNA_bdg; 1.
DR   SUPFAM; SSF46785; SSF46785; 1.
DR   PROSITE; PS51526; RFX_DBD; 1.
PE   1: Evidence at protein level;
KW   3D-structure; Acetylation; Activator; Alternative splicing;
KW   Direct protein sequencing; Disease variant; DNA-binding; Nucleus;
KW   Phosphoprotein; Reference proteome; SCID; Transcription;
KW   Transcription regulation.
FT   INIT_MET        1
FT                   /note="Removed"
FT                   /evidence="ECO:0007744|PubMed:22814378"
FT   CHAIN           2..616
FT                   /note="DNA-binding protein RFX5"
FT                   /id="PRO_0000215292"
FT   DNA_BIND        92..168
FT                   /note="RFX-type winged-helix"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00858"
FT   REGION          1..29
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          25..90
FT                   /note="N-terminal domain"
FT   REGION          62..66
FT                   /note="Leucine-rich region; critical for dimer formation
FT                   and for interaction with RFXAP"
FT   REGION          252..314
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          391..616
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOTIF           173..178
FT                   /note="PxLPxI/L motif; mediates interaction with RFXANK"
FT                   /evidence="ECO:0000269|PubMed:22649097"
FT   COMPBIAS        252..289
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        420..434
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        476..501
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOD_RES         2
FT                   /note="N-acetylalanine"
FT                   /evidence="ECO:0007744|PubMed:22814378"
FT   MOD_RES         10
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:23186163"
FT   MOD_RES         185
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:20068231"
FT   VAR_SEQ         78..117
FT                   /note="Missing (in isoform 2)"
FT                   /evidence="ECO:0000303|PubMed:14702039"
FT                   /id="VSP_055864"
FT   VARIANT         149
FT                   /note="R -> Q (in BLS2; dbSNP:rs137853099)"
FT                   /evidence="ECO:0000269|PubMed:10825209"
FT                   /id="VAR_015550"
FT   VARIANT         197
FT                   /note="R -> Q (in dbSNP:rs2233851)"
FT                   /id="VAR_034448"
FT   VARIANT         409
FT                   /note="P -> R (in dbSNP:rs2233854)"
FT                   /id="VAR_034449"
FT   VARIANT         499
FT                   /note="P -> S (in dbSNP:rs2233855)"
FT                   /id="VAR_034450"
FT   HELIX           30..36
FT                   /evidence="ECO:0007829|PDB:2KW3"
FT   HELIX           40..54
FT                   /evidence="ECO:0007829|PDB:2KW3"
FT   HELIX           58..66
FT                   /evidence="ECO:0007829|PDB:2KW3"
FT   HELIX           74..78
FT                   /evidence="ECO:0007829|PDB:2KW3"
FT   STRAND          82..86
FT                   /evidence="ECO:0007829|PDB:2KW3"
FT   STRAND          178..180
FT                   /evidence="ECO:0007829|PDB:3V30"
SQ   SEQUENCE   616 AA;  65323 MW;  5EBB33C677BB717F CRC64;
     MAEDEPDAKS PKTGGRAPPG GAEAGEPTTL LQRLRGTISK AVQNKVEGIL QDVQKFSDND
     KLYLYLQLPS GPTTGDKSSE PSTLSNEEYM YAYRWIRNHL EEHTDTCLPK QSVYDAYRKY
     CESLACCRPL STANFGKIIR EIFPDIKARR LGGRGQSKYC YSGIRRKTLV SMPPLPGLDL
     KGSESPEMGP EVTPAPRDEL VEAACALTCD WAERILKRSF SSIVEVARFL LQQHLISARS
     AHAHVLKAMG LAEEDEHAPR ERSSKPKNGL ENPEGGAHKK PERLAQPPKD LEARTGAGPL
     ARGERKKSVV ESSAPGANNL QVNALVARLP LLLPRAPRSL IPPIPVSPPI LAPRLSSGAL
     KVATLPLSSR AGAPPAAVPI INMILPTVPA LPGPGPGPGR APPGGLTQPR GTENREVGIG
     GDQGPHDKGV KRTAEVPVSE ASGQAPPAKA AKQDIEDTAS DAKRKRGRPR KKSGGSGERN
     STPLKSAAAM ESAQSSRLPW ETWGSGGEGN SAGGAERPGP MGEAEKGAVL AQGQGDGTVS
     KGGRGPGSQH TKEAEDKIPL VPSKVSVIKG SRSQKEAFPL AKGEVDTAPQ GNKDLKEHVL
     QSSLSQEHKD PKATPP
 
 
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