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P22670 (RFX1_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 141. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (6) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended 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 names
Name:RFX1
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length979 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

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.

Subunit structure

Binds DNA as a homodimer.

Subcellular location

Nucleus.

Sequence similarities

Belongs to the RFX family.

Contains 1 RFX-type winged-helix DNA-binding domain.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 979979MHC class II regulatory factor RFX1
PRO_0000215286

Regions

DNA binding438 – 51376RFX-type winged-helix
Region744 – 979236Necessary for dimerization
Compositional bias381 – 41131Gly-rich
Compositional bias920 – 93617Asp/Glu-rich (acidic)

Amino acid modifications

Modified residue9781Phosphoserine Ref.10
Modified residue9791Phosphoserine Ref.10

Natural variations

Natural variant3701T → A. Ref.1 Ref.3
Corresponds to variant rs2305780 [ dbSNP | Ensembl ].
VAR_059781

Secondary structure

........... 979
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
P22670 [UniParc].

Last modified February 9, 2010. Version 2.
Checksum: 4FD8EA9C4AB1A411

FASTA979104,758
        10         20         30         40         50         60 
MATQAYTELQ AAPPPSQPPQ APPQAQPQPP PPPPPAAPQP PQPPTAAATP QPQYVTELQS 

        70         80         90        100        110        120 
PQPQAQPPGG QKQYVTELPA VPAPSQPTGA PTPSPAPQQY IVVTVSEGAM RASETVSEAS 

       130        140        150        160        170        180 
PGSTASQTGV PTQVVQQVQG TQQRLLVQTS VQAKPGHVSP LQLTNIQVPQ QALPTQRLVV 

       190        200        210        220        230        240 
QSAAPGSKGG QVSLTVHGTQ QVHSPPEQSP VQANSSSSKT AGAPTGTVPQ QLQVHGVQQS 

       250        260        270        280        290        300 
VPVTQERSVV QATPQAPKPG PVQPLTVQGL QPVHVAQEVQ QLQQVPVPHV YSSQVQYVEG 

       310        320        330        340        350        360 
GDASYTASAI RSSTYSYPET PLYTQTASTS YYEAAGTATQ VSTPATSQAV ASSGSMPMYV 

       370        380        390        400        410        420 
SGSQVVASST STGAGASNSS GGGGSGGGGG GGGGGGGGGS GSTGGGGSGA GTYVIQGGYM 

       430        440        450        460        470        480 
LGSASQSYSH TTRASPATVQ WLLDNYETAE GVSLPRSTLY CHYLLHCQEQ KLEPVNAASF 

       490        500        510        520        530        540 
GKLIRSVFMG LRTRRLGTRG NSKYHYYGLR IKASSPLLRL MEDQQHMAMR GQPFSQKQRL 

       550        560        570        580        590        600 
KPIQKMEGMT NGVAVGQQPS TGLSDISAQV QQYQQFLDAS RSLPDFTELD LQGKVLPEGV 

       610        620        630        640        650        660 
GPGDIKAFQV LYREHCEAIV DVMVNLQFTL VETLWKTFWR YNLSQPSEAP PLAVHDEAEK 

       670        680        690        700        710        720 
RLPKAILVLL SKFEPVLQWT KHCDNVLYQG LVEILIPDVL RPIPSALTQA IRNFAKSLES 

       730        740        750        760        770        780 
WLTHAMVNIP EEMLRVKVAA AGAFAQTLRR YTSLNHLAQA ARAVLQNTAQ INQMLSDLNR 

       790        800        810        820        830        840 
VDFANVQEQA SWVCRCEDRV VQRLEQDFKV TLQQQNSLEQ WAAWLDGVVS QVLKPYQGSA 

       850        860        870        880        890        900 
GFPKAAKLFL LKWSFYSSMV IRDLTLRSAA SFGSFHLIRL LYDEYMYYLI EHRVAQAKGE 

       910        920        930        940        950        960 
TPIAVMGEFA NLATSLNPLD PDKDEEEEEE EESEDELPQD ISLAAGGESP ALGPETLEPP 

       970 
AKLARTDARG LFVQALPSS 

« Hide

References

« Hide 'large scale' references
[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. expand/collapse author list , 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]"A quantitative atlas of mitotic phosphorylation."
Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E., Elledge S.J., Gygi S.P.
Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008) [PubMed] [Europe PMC] [Abstract]
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]"Initial characterization of the human central proteome."
Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.
BMC Syst. Biol. 5:17-17(2011) [PubMed] [Europe PMC] [Abstract]
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.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
X58964 mRNA. Translation: CAA41730.1.
AC020916 Genomic DNA. No translation available.
AC022098 Genomic DNA. No translation available.
BC049826 mRNA. Translation: AAH49826.1.
CCDSCCDS12301.1.
PIRA35913.
RefSeqNP_002909.4. NM_002918.4.
XP_006722892.1. XM_006722829.1.
UniGeneHs.655215.

3D structure databases

PDBe
RCSB-PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
1DP7X-ray1.50P438-513[»]
ProteinModelPortalP22670.
SMRP22670. Positions 438-513.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid111921. 15 interactions.
IntActP22670. 8 interactions.
MINTMINT-1186898.
STRING9606.ENSP00000254325.

PTM databases

PhosphoSiteP22670.

Polymorphism databases

DMDM288558824.

Proteomic databases

MaxQBP22670.
PaxDbP22670.
PRIDEP22670.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000254325; ENSP00000254325; ENSG00000132005.
GeneID5989.
KEGGhsa:5989.
UCSCuc002mxv.3. human.

Organism-specific databases

CTD5989.
GeneCardsGC19M014072.
H-InvDBHIX0027643.
HGNCHGNC:9982. RFX1.
HPAHPA048722.
MIM600006. gene.
neXtProtNX_P22670.
PharmGKBPA34352.
GenAtlasSearch...

Phylogenomic databases

eggNOGNOG264634.
HOGENOMHOG000294091.
HOVERGENHBG002753.
InParanoidP22670.
KOK09173.
OMASTYSYPE.
OrthoDBEOG7TF793.
PhylomeDBP22670.
TreeFamTF321340.

Enzyme and pathway databases

SignaLinkP22670.

Gene expression databases

ArrayExpressP22670.
BgeeP22670.
CleanExHS_RFX1.
GenevestigatorP22670.

Family and domain databases

Gene3D1.10.10.10. 1 hit.
InterProIPR003150. DNA-bd_RFX.
IPR007668. RFX1_trans_act.
IPR011991. WHTH_DNA-bd_dom.
[Graphical view]
PfamPF04589. RFX1_trans_act. 1 hit.
PF02257. RFX_DNA_binding. 1 hit.
[Graphical view]
PROSITEPS51526. RFX_DBD. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

EvolutionaryTraceP22670.
GeneWikiRFX1.
GenomeRNAi5989.
NextBio23325.
PROP22670.
SOURCESearch...

Entry information

Entry nameRFX1_HUMAN
AccessionPrimary (citable) accession number: P22670
Entry history
Integrated into UniProtKB/Swiss-Prot: August 1, 1991
Last sequence update: February 9, 2010
Last modified: July 9, 2014
This is version 141 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (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.

Relevant documents

SIMILARITY comments

Index of protein domains and families

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

MIM cross-references

Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot

Human polymorphisms and disease mutations

Index of human polymorphisms and disease mutations

Human entries with polymorphisms or disease mutations

List of human entries with polymorphisms or disease mutations

Human chromosome 19

Human chromosome 19: entries, gene names and cross-references to MIM