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P22670

- RFX1_HUMAN

UniProt

P22670 - RFX1_HUMAN

Protein

MHC class II regulatory factor RFX1

Gene

RFX1

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 142 (01 Oct 2014)
      Sequence version 2 (09 Feb 2010)
      Previous versions | rss
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    Functioni

    Regulatory factor essential for MHC class II genes expression. Binds to the X boxes of MHC class II genes. Also binds to an inverted repeat (ENH1) required for hepatitis B virus genes expression and to the most upstream element (alpha) of the RPL30 promoter.

    Regions

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    DNA bindingi438 – 51376RFX-type winged-helixPROSITE-ProRule annotationAdd
    BLAST

    GO - Molecular functioni

    1. DNA binding Source: UniProtKB-KW
    2. protein binding Source: BHF-UCL
    3. RNA polymerase II distal enhancer sequence-specific DNA binding transcription factor activity Source: ProtInc

    GO - Biological processi

    1. immune response Source: ProtInc
    2. regulation of transcription from RNA polymerase II promoter Source: GOC
    3. transcription from RNA polymerase II promoter Source: GOC

    Keywords - Molecular functioni

    Activator

    Keywords - Biological processi

    Transcription, Transcription regulation

    Keywords - Ligandi

    DNA-binding

    Enzyme and pathway databases

    SignaLinkiP22670.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    MHC class II regulatory factor RFX1
    Alternative name(s):
    Enhancer factor C
    Short name:
    EF-C
    Regulatory factor X 1
    Short name:
    RFX
    Transcription factor RFX1
    Gene namesi
    Name:RFX1
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 19

    Organism-specific databases

    HGNCiHGNC:9982. RFX1.

    Subcellular locationi

    GO - Cellular componenti

    1. nucleus Source: UniProtKB-SubCell

    Keywords - Cellular componenti

    Nucleus

    Pathology & Biotechi

    Organism-specific databases

    PharmGKBiPA34352.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 979979MHC class II regulatory factor RFX1PRO_0000215286Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei978 – 9781Phosphoserine1 Publication
    Modified residuei979 – 9791Phosphoserine1 Publication

    Keywords - PTMi

    Phosphoprotein

    Proteomic databases

    MaxQBiP22670.
    PaxDbiP22670.
    PRIDEiP22670.

    PTM databases

    PhosphoSiteiP22670.

    Expressioni

    Gene expression databases

    ArrayExpressiP22670.
    BgeeiP22670.
    CleanExiHS_RFX1.
    GenevestigatoriP22670.

    Organism-specific databases

    HPAiHPA048722.

    Interactioni

    Subunit structurei

    Binds DNA as a homodimer.1 Publication

    Protein-protein interaction databases

    BioGridi111921. 15 interactions.
    IntActiP22670. 8 interactions.
    MINTiMINT-1186898.
    STRINGi9606.ENSP00000254325.

    Structurei

    Secondary structure

    1
    979
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Helixi439 – 4457
    Beta strandi446 – 45510
    Helixi456 – 46914
    Helixi477 – 48711
    Beta strandi492 – 4987
    Beta strandi503 – 5119

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    1DP7X-ray1.50P438-513[»]
    ProteinModelPortaliP22670.
    SMRiP22670. Positions 438-513.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiP22670.

    Family & Domainsi

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni744 – 979236Necessary for dimerizationAdd
    BLAST

    Compositional bias

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Compositional biasi381 – 41131Gly-richAdd
    BLAST
    Compositional biasi920 – 93617Asp/Glu-rich (acidic)Add
    BLAST

    Sequence similaritiesi

    Belongs to the RFX family.PROSITE-ProRule annotation
    Contains 1 RFX-type winged-helix DNA-binding domain.PROSITE-ProRule annotation

    Phylogenomic databases

    eggNOGiNOG264634.
    HOGENOMiHOG000294091.
    HOVERGENiHBG002753.
    InParanoidiP22670.
    KOiK09173.
    OMAiSTYSYPE.
    OrthoDBiEOG7TF793.
    PhylomeDBiP22670.
    TreeFamiTF321340.

    Family and domain databases

    Gene3Di1.10.10.10. 1 hit.
    InterProiIPR003150. DNA-bd_RFX.
    IPR007668. RFX1_trans_act.
    IPR011991. WHTH_DNA-bd_dom.
    [Graphical view]
    PfamiPF04589. RFX1_trans_act. 1 hit.
    PF02257. RFX_DNA_binding. 1 hit.
    [Graphical view]
    PROSITEiPS51526. RFX_DBD. 1 hit.
    [Graphical view]

    Sequencei

    Sequence statusi: Complete.

    P22670-1 [UniParc]FASTAAdd to Basket

    « Hide

    MATQAYTELQ AAPPPSQPPQ APPQAQPQPP PPPPPAAPQP PQPPTAAATP    50
    QPQYVTELQS PQPQAQPPGG QKQYVTELPA VPAPSQPTGA PTPSPAPQQY 100
    IVVTVSEGAM RASETVSEAS PGSTASQTGV PTQVVQQVQG TQQRLLVQTS 150
    VQAKPGHVSP LQLTNIQVPQ QALPTQRLVV QSAAPGSKGG QVSLTVHGTQ 200
    QVHSPPEQSP VQANSSSSKT AGAPTGTVPQ QLQVHGVQQS VPVTQERSVV 250
    QATPQAPKPG PVQPLTVQGL QPVHVAQEVQ QLQQVPVPHV YSSQVQYVEG 300
    GDASYTASAI RSSTYSYPET PLYTQTASTS YYEAAGTATQ VSTPATSQAV 350
    ASSGSMPMYV SGSQVVASST STGAGASNSS GGGGSGGGGG GGGGGGGGGS 400
    GSTGGGGSGA GTYVIQGGYM LGSASQSYSH TTRASPATVQ WLLDNYETAE 450
    GVSLPRSTLY CHYLLHCQEQ KLEPVNAASF GKLIRSVFMG LRTRRLGTRG 500
    NSKYHYYGLR IKASSPLLRL MEDQQHMAMR GQPFSQKQRL KPIQKMEGMT 550
    NGVAVGQQPS TGLSDISAQV QQYQQFLDAS RSLPDFTELD LQGKVLPEGV 600
    GPGDIKAFQV LYREHCEAIV DVMVNLQFTL VETLWKTFWR YNLSQPSEAP 650
    PLAVHDEAEK RLPKAILVLL SKFEPVLQWT KHCDNVLYQG LVEILIPDVL 700
    RPIPSALTQA IRNFAKSLES WLTHAMVNIP EEMLRVKVAA AGAFAQTLRR 750
    YTSLNHLAQA ARAVLQNTAQ INQMLSDLNR VDFANVQEQA SWVCRCEDRV 800
    VQRLEQDFKV TLQQQNSLEQ WAAWLDGVVS QVLKPYQGSA GFPKAAKLFL 850
    LKWSFYSSMV IRDLTLRSAA SFGSFHLIRL LYDEYMYYLI EHRVAQAKGE 900
    TPIAVMGEFA NLATSLNPLD PDKDEEEEEE EESEDELPQD ISLAAGGESP 950
    ALGPETLEPP AKLARTDARG LFVQALPSS 979
    Length:979
    Mass (Da):104,758
    Last modified:February 9, 2010 - v2
    Checksum:i4FD8EA9C4AB1A411
    GO

    Natural variant

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti370 – 3701T → A.2 Publications
    Corresponds to variant rs2305780 [ dbSNP | Ensembl ].
    VAR_059781

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    X58964 mRNA. Translation: CAA41730.1.
    AC020916 Genomic DNA. No translation available.
    AC022098 Genomic DNA. No translation available.
    BC049826 mRNA. Translation: AAH49826.1.
    CCDSiCCDS12301.1.
    PIRiA35913.
    RefSeqiNP_002909.4. NM_002918.4.
    XP_006722892.1. XM_006722829.1.
    UniGeneiHs.655215.

    Genome annotation databases

    EnsembliENST00000254325; ENSP00000254325; ENSG00000132005.
    GeneIDi5989.
    KEGGihsa:5989.
    UCSCiuc002mxv.3. human.

    Polymorphism databases

    DMDMi288558824.

    Keywords - Coding sequence diversityi

    Polymorphism

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    X58964 mRNA. Translation: CAA41730.1 .
    AC020916 Genomic DNA. No translation available.
    AC022098 Genomic DNA. No translation available.
    BC049826 mRNA. Translation: AAH49826.1 .
    CCDSi CCDS12301.1.
    PIRi A35913.
    RefSeqi NP_002909.4. NM_002918.4.
    XP_006722892.1. XM_006722829.1.
    UniGenei Hs.655215.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    1DP7 X-ray 1.50 P 438-513 [» ]
    ProteinModelPortali P22670.
    SMRi P22670. Positions 438-513.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 111921. 15 interactions.
    IntActi P22670. 8 interactions.
    MINTi MINT-1186898.
    STRINGi 9606.ENSP00000254325.

    PTM databases

    PhosphoSitei P22670.

    Polymorphism databases

    DMDMi 288558824.

    Proteomic databases

    MaxQBi P22670.
    PaxDbi P22670.
    PRIDEi P22670.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000254325 ; ENSP00000254325 ; ENSG00000132005 .
    GeneIDi 5989.
    KEGGi hsa:5989.
    UCSCi uc002mxv.3. human.

    Organism-specific databases

    CTDi 5989.
    GeneCardsi GC19M014072.
    H-InvDB HIX0027643.
    HGNCi HGNC:9982. RFX1.
    HPAi HPA048722.
    MIMi 600006. gene.
    neXtProti NX_P22670.
    PharmGKBi PA34352.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi NOG264634.
    HOGENOMi HOG000294091.
    HOVERGENi HBG002753.
    InParanoidi P22670.
    KOi K09173.
    OMAi STYSYPE.
    OrthoDBi EOG7TF793.
    PhylomeDBi P22670.
    TreeFami TF321340.

    Enzyme and pathway databases

    SignaLinki P22670.

    Miscellaneous databases

    EvolutionaryTracei P22670.
    GeneWikii RFX1.
    GenomeRNAii 5989.
    NextBioi 23325.
    PROi P22670.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi P22670.
    Bgeei P22670.
    CleanExi HS_RFX1.
    Genevestigatori P22670.

    Family and domain databases

    Gene3Di 1.10.10.10. 1 hit.
    InterProi IPR003150. DNA-bd_RFX.
    IPR007668. RFX1_trans_act.
    IPR011991. WHTH_DNA-bd_dom.
    [Graphical view ]
    Pfami PF04589. RFX1_trans_act. 1 hit.
    PF02257. RFX_DNA_binding. 1 hit.
    [Graphical view ]
    PROSITEi PS51526. RFX_DBD. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "MHC class II regulatory factor RFX has a novel DNA-binding domain and a functionally independent dimerization domain."
      Reith W., Sanchez-Herrero C., Kobr M., Silacci P., Berte C., Barras E., Mach B.
      Genes Dev. 4:1528-1540(1990) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA], VARIANT ALA-370.
    2. "The DNA sequence and biology of human chromosome 19."
      Grimwood J., Gordon L.A., Olsen A.S., Terry A., Schmutz J., Lamerdin J.E., Hellsten U., Goodstein D., Couronne O., Tran-Gyamfi M., Aerts A., Altherr M., Ashworth L., Bajorek E., Black S., Branscomb E., Caenepeel S., Carrano A.V.
      , Caoile C., Chan Y.M., Christensen M., Cleland C.A., Copeland A., Dalin E., Dehal P., Denys M., Detter J.C., Escobar J., Flowers D., Fotopulos D., Garcia C., Georgescu A.M., Glavina T., Gomez M., Gonzales E., Groza M., Hammon N., Hawkins T., Haydu L., Ho I., Huang W., Israni S., Jett J., Kadner K., Kimball H., Kobayashi A., Larionov V., Leem S.-H., Lopez F., Lou Y., Lowry S., Malfatti S., Martinez D., McCready P.M., Medina C., Morgan J., Nelson K., Nolan M., Ovcharenko I., Pitluck S., Pollard M., Popkie A.P., Predki P., Quan G., Ramirez L., Rash S., Retterer J., Rodriguez A., Rogers S., Salamov A., Salazar A., She X., Smith D., Slezak T., Solovyev V., Thayer N., Tice H., Tsai M., Ustaszewska A., Vo N., Wagner M., Wheeler J., Wu K., Xie G., Yang J., Dubchak I., Furey T.S., DeJong P., Dickson M., Gordon D., Eichler E.E., Pennacchio L.A., Richardson P., Stubbs L., Rokhsar D.S., Myers R.M., Rubin E.M., Lucas S.M.
      Nature 428:529-535(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    3. "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
      The MGC Project Team
      Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA], VARIANT ALA-370.
      Tissue: Testis.
    4. "RFX1 is identical to enhancer factor C and functions as a transactivator of the hepatitis B virus enhancer."
      Siegrist C.A., Durand B., Emery P., David E., Hearing P., Mach B., Reith W.
      Mol. Cell. Biol. 13:6375-6384(1993) [PubMed] [Europe PMC] [Abstract]
      Cited for: IDENTITY OF RFX1 AND EF-C.
    5. "Transcription factor RFX1 helps control the promoter of the mouse ribosomal protein-encoding gene rpL30 by binding to its alpha element."
      Safrany G., Perry R.P.
      Gene 132:279-283(1993) [PubMed] [Europe PMC] [Abstract]
      Cited for: BINDING TO RPL30 PROMOTER.
    6. "The DNA-binding defect observed in major histocompatibility complex class II regulatory mutants concerns only one member of a family of complexes binding to the X boxes of class II promoters."
      Sanchez-Herrero C., Reith W., Silacci P., Mach B.
      Mol. Cell. Biol. 12:4076-4083(1992) [PubMed] [Europe PMC] [Abstract]
      Cited for: SHOWS THAT BLS II IS NOT DUE TO RFX1.
    7. "Kinase-selective enrichment enables quantitative phosphoproteomics of the kinome across the cell cycle."
      Daub H., Olsen J.V., Bairlein M., Gnad F., Oppermann F.S., Korner R., Greff Z., Keri G., Stemmann O., Mann M.
      Mol. Cell 31:438-448(2008) [PubMed] [Europe PMC] [Abstract]
      Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    8. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    9. "Quantitative phosphoproteomic analysis of T cell receptor signaling reveals system-wide modulation of protein-protein interactions."
      Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K., Rodionov V., Han D.K.
      Sci. Signal. 2:RA46-RA46(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Leukemic T-cell.
    10. "Quantitative phosphoproteomics reveals widespread full phosphorylation site occupancy during mitosis."
      Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L., Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S., Mann M.
      Sci. Signal. 3:RA3-RA3(2010) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-978 AND SER-979, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    11. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    12. "Structure of the winged-helix protein hRFX1 reveals a new mode of DNA binding."
      Gajiwala K.S., Chen H., Cornille F., Roques B.P., Reith W., Mach B., Burley S.K.
      Nature 403:916-921(2000) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (1.5 ANGSTROMS) OF 438-513 IN COMPLEX WITH DNA.

    Entry informationi

    Entry nameiRFX1_HUMAN
    AccessioniPrimary (citable) accession number: P22670
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: August 1, 1991
    Last sequence update: February 9, 2010
    Last modified: October 1, 2014
    This is version 142 of the entry and version 2 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programChordata Protein Annotation Program
    DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

    Miscellaneousi

    Keywords - Technical termi

    3D-structure, Complete proteome, Reference proteome

    Documents

    1. Human chromosome 19
      Human chromosome 19: entries, gene names and cross-references to MIM
    2. Human entries with polymorphisms or disease mutations
      List of human entries with polymorphisms or disease mutations
    3. Human polymorphisms and disease mutations
      Index of human polymorphisms and disease mutations
    4. MIM cross-references
      Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
    5. PDB cross-references
      Index of Protein Data Bank (PDB) cross-references
    6. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3