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   05-OCT-2010, entry version 104.
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;
OC   Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
OC   Catarrhini; Hominidae; Homo.
OX   NCBI_TaxID=9606;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA], AND VARIANT ALA-370.
RX   MEDLINE=91071581; PubMed=2253877;
RA   Reith W., Sanchez-Herrero C., Kobr M., Silacci P., Berte C.,
RA   Barras E., Mach B.;
RT   "MHC class II regulatory factor RFX has a novel DNA-binding domain and
RT   a 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.,
RA   Lamerdin J.E., Hellsten U., Goodstein D., Couronne O., Tran-Gyamfi M.,
RA   Aerts A., Altherr M., Ashworth L., Bajorek E., Black S., Branscomb E.,
RA   Caenepeel S., Carrano A.V., Caoile C., Chan Y.M., Christensen M.,
RA   Cleland C.A., Copeland A., Dalin E., Dehal P., Denys M., Detter J.C.,
RA   Escobar J., Flowers D., Fotopulos D., Garcia C., Georgescu A.M.,
RA   Glavina T., Gomez M., Gonzales E., Groza M., Hammon N., Hawkins T.,
RA   Haydu L., Ho I., Huang W., Israni S., Jett J., Kadner K., Kimball H.,
RA   Kobayashi A., Larionov V., Leem S.-H., Lopez F., Lou Y., Lowry S.,
RA   Malfatti S., Martinez D., McCready P.M., Medina C., Morgan J.,
RA   Nelson K., Nolan M., Ovcharenko I., Pitluck S., Pollard M.,
RA   Popkie A.P., Predki P., Quan G., Ramirez L., Rash S., Retterer J.,
RA   Rodriguez A., Rogers S., Salamov A., Salazar A., She X., Smith D.,
RA   Slezak T., Solovyev V., Thayer N., Tice H., Tsai M., Ustaszewska A.,
RA   Vo N., Wagner M., Wheeler J., Wu K., Xie G., Yang J., Dubchak I.,
RA   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
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [4]
RP   IDENTITY OF RFX1 AND EF-C.
RX   MEDLINE=94019311; PubMed=8413236;
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
RT   transactivator of the hepatitis B virus enhancer.";
RL   Mol. Cell. Biol. 13:6375-6384(1993).
RN   [5]
RP   BINDING TO RPL30 PROMOTER.
RX   MEDLINE=94040774; 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
RT   element.";
RL   Gene 132:279-283(1993).
RN   [6]
RP   SHOWS THAT BLS II IS NOT DUE TO RFX1.
RX   MEDLINE=92375076; PubMed=1508204;
RA   Sanchez-Herrero C., Reith W., Silacci P., Mach B.;
RT   "The DNA-binding defect observed in major histocompatibility complex
RT   class II regulatory mutants concerns only one member of a family of
RT   complexes binding to the X boxes of class II promoters.";
RL   Mol. Cell. Biol. 12:4076-4083(1992).
RN   [7]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-120, AND MASS
RP   SPECTROMETRY.
RC   TISSUE=Cervix carcinoma;
RX   PubMed=15302935; DOI=10.1073/pnas.0404720101;
RA   Beausoleil S.A., Jedrychowski M., Schwartz D., Elias J.E., Villen J.,
RA   Li J., Cohn M.A., Cantley L.C., Gygi S.P.;
RT   "Large-scale characterization of HeLa cell nuclear phosphoproteins.";
RL   Proc. Natl. Acad. Sci. U.S.A. 101:12130-12135(2004).
RN   [8]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-159, AND MASS
RP   SPECTROMETRY.
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
RT   the kinome across the cell cycle.";
RL   Mol. Cell 31:438-448(2008).
RN   [9]
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RA   Colinge J., Superti-Furga G., Bennett K.L.;
RL   Submitted (OCT-2008) to UniProtKB.
RN   [10]
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
CC       to 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: Binds DNA as a homodimer.
CC   -!- INTERACTION:
CC       Q13547:HDAC1; NbExp=1; IntAct=EBI-716037, EBI-301834;
CC   -!- SUBCELLULAR LOCATION: Nucleus.
CC   -!- SIMILARITY: Belongs to the RFX family.
CC   -!- SIMILARITY: Contains 1 H-T-H motif winged-type DNA-binding domain.
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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   IPI; IPI00305337; -.
DR   PIR; A35913; A35913.
DR   RefSeq; NP_002909.4; -.
DR   UniGene; Hs.655215; -.
DR   PDB; 1DP7; X-ray; 1.50 A; P=438-513.
DR   PDBsum; 1DP7; -.
DR   ProteinModelPortal; P22670; -.
DR   IntAct; P22670; 4.
DR   MINT; MINT-1186898; -.
DR   STRING; P22670; -.
DR   PhosphoSite; P22670; -.
DR   Ensembl; ENST00000254325; ENSP00000254325; ENSG00000132005.
DR   GeneID; 5989; -.
DR   KEGG; hsa:5989; -.
DR   UCSC; uc002mxv.1; human.
DR   CTD; 5989; -.
DR   GeneCards; GC19M014072; -.
DR   H-InvDB; HIX0027643; -.
DR   HGNC; HGNC:9982; RFX1.
DR   MIM; 600006; gene.
DR   PharmGKB; PA34352; -.
DR   eggNOG; prNOG04314; -.
DR   HOGENOM; HBG714364; -.
DR   HOVERGEN; HBG002753; -.
DR   InParanoid; P22670; -.
DR   OMA; SYPETPL; -.
DR   NextBio; 23325; -.
DR   ArrayExpress; P22670; -.
DR   Bgee; P22670; -.
DR   CleanEx; HS_RFX1; -.
DR   Genevestigator; P22670; -.
DR   GermOnline; ENSG00000132005; Homo sapiens.
DR   GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR   GO; GO:0005515; F:protein binding; IPI:IntAct.
DR   GO; GO:0003705; F:RNA polymerase II transcription factor acti...; TAS:ProtInc.
DR   GO; GO:0006955; P:immune response; TAS:ProtInc.
DR   GO; GO:0006355; P:regulation of transcription, DNA-dependent; IEA:InterPro.
DR   GO; GO:0006350; P:transcription; IEA:UniProtKB-KW.
DR   InterPro; IPR007668; RFX1_trans_act.
DR   InterPro; IPR003150; RFX_DNA-bd.
DR   InterPro; IPR011991; WHTH_trsnscrt_rep_DNA-bd.
DR   Gene3D; G3DSA:1.10.10.10; Wing_hlx_DNA_bd; 1.
DR   Pfam; PF04589; RFX1_trans_act; 1.
DR   Pfam; PF02257; RFX_DNA_binding; 1.
PE   1: Evidence at protein level;
KW   3D-structure; Activator; Complete proteome; DNA-binding; Nucleus;
KW   Phosphoprotein; Polymorphism; Transcription; Transcription regulation.
FT   CHAIN         1    979       MHC class II regulatory factor RFX1.
FT                                /FTId=PRO_0000215286.
FT   DNA_BIND    441    512       H-T-H motif winged-type.
FT   REGION      744    979       Necessary for dimerization.
FT   COMPBIAS    381    411       Gly-rich.
FT   COMPBIAS    920    936       Asp/Glu-rich (acidic).
FT   MOD_RES     120    120       Phosphoserine.
FT   MOD_RES     159    159       Phosphoserine.
FT   VARIANT     370    370       T -> A (in dbSNP:rs2305780).
FT                                /FTId=VAR_059781.
FT   HELIX       439    445
FT   STRAND      446    455
FT   HELIX       456    469
FT   HELIX       477    487
FT   STRAND      492    498
FT   STRAND      503    511
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
//