P22670 (RFX1_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

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 names

Name:

RFX1

Organism

Homo sapiens (Human) [Reference proteome]

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Opisthokonta › Metazoa › Eumetazoa › Bilateria › Deuterostomia › Chordata › Craniata › Vertebrata › Gnathostomata › Teleostomi › Euteleostomi › Sarcopterygii › Tetrapoda › Amniota › Mammalia › Theria › Eutheria › Euarchontoglires › Primates › Haplorrhini › Simiiformes › Catarrhini › Hominoidea › Hominidae › Homininae › Homo

Protein attributes

Sequence length	979 AA.
Sequence status	Complete.
Protein existence	Evidence 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.

Ontologies

Keywords
Biological process	Transcription Transcription regulation
Cellular component	Nucleus
Coding sequence diversity	Polymorphism
Ligand	DNA-binding
Molecular function	Activator
PTM	Phosphoprotein
Technical term	3D-structure Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	immune response Traceable author statement PubMed 1505960. Source: ProtInc
Cellular_component	nucleus Inferred from electronic annotation. Source: UniProtKB-SubCell
Molecular_function	DNA binding Inferred from electronic annotation. Source: UniProtKB-KW RNA polymerase II distal enhancer sequence-specific DNA binding transcription factor activity Traceable author statement PubMed 8289803. Source: ProtInc
Complete GO annotation...

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 979

979

MHC class II regulatory factor RFX1

PRO_0000215286

Regions

DNA binding

438 – 513

76

RFX-type winged-helix

Region

744 – 979

236

Necessary for dimerization

Compositional bias

381 – 411

31

Gly-rich

Compositional bias

920 – 936

17

Asp/Glu-rich (acidic)

Amino acid modifications

Modified residue

978

1

Phosphoserine Ref.10

Modified residue

979

1

Phosphoserine Ref.10

Natural variations

Natural variant

370

1

T → A. Ref.1 Ref.3
Corresponds to variant rs2305780 [ dbSNP | Ensembl ].

VAR_059781

Secondary structure

1

.

.

.

.

.

.

.

.

.

.

.

979

Helix Strand Turn

Details...

Helix

439 – 445

7

Beta strand

446 – 455

10

Helix

456 – 469

14

Helix

477 – 487

11

Beta strand

492 – 498

7

Beta strand

503 – 511

9

Sequences

	Sequence		Length	Mass (Da)
	P22670 [UniParc]. Last modified February 9, 2010. Version 2. Checksum: 4FD8EA9C4AB1A411	FASTA	979	104,758
	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

References

	« Hide 'large scale' referencesShow '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. , 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, MASS SPECTROMETRY. 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.

IPI

IPI00305337.

PIR

A35913.

RefSeq

NP_002909.4. NM_002918.4.

UniGene

Hs.655215.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
1DP7	X-ray	1.50	P	438-513	[»]

ProteinModelPortal

P22670.

SMR

P22670. Positions 438-513.

ModBase

Search...

Protein-protein interaction databases

IntAct

P22670. 3 interactions.

MINT

MINT-1186898.

STRING

9606.ENSP00000254325.

PTM databases

PhosphoSite

P22670.

Polymorphism databases

DMDM

288558824.

Proteomic databases

PaxDb

P22670.

PRIDE

P22670.

Protocols and materials databases

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

Ensembl

ENST00000254325; ENSP00000254325; ENSG00000132005.

GeneID

5989.

KEGG

hsa:5989.

UCSC

uc002mxv.3. human.

Organism-specific databases

CTD

5989.

GeneCards

GC19M014072.

H-InvDB

HIX0027643.

HGNC

HGNC:9982. RFX1.

HPA

HPA048722.

MIM

600006. gene.

neXtProt

NX_P22670.

PharmGKB

PA34352.

GenAtlas

Search...

Phylogenomic databases

eggNOG

NOG264634.

HOGENOM

HOG000294091.

HOVERGEN

HBG002753.

InParanoid

P22670.

KO

K09173.

OMA

VPVQHVY.

OrthoDB

EOG4TB49X.

PhylomeDB

P22670.

Enzyme and pathway databases

SignaLink

P22670.

Gene expression databases

Bgee

P22670.

CleanEx

HS_RFX1.

Genevestigator

P22670.

GermOnline

ENSG00000132005. Homo sapiens.

Family and domain databases

Gene3D

1.10.10.10. 1 hit.

InterPro

IPR003150. DNA-bd_RFX.
IPR007668. RFX1_trans_act.
IPR011991. WHTH_DNA-bd_dom.
[Graphical view]

Pfam

PF04589. RFX1_trans_act. 1 hit.
PF02257. RFX_DNA_binding. 1 hit.
[Graphical view]

PROSITE

PS51526. RFX_DBD. 1 hit.
[Graphical view]

ProtoNet

Search...

Other

EvolutionaryTrace

P22670.

GenomeRNAi

5989.

NextBio

23325.

SOURCE

Search...

Entry information

Entry name

RFX1_HUMAN

Accession

Primary (citable) accession number: P22670

Entry history

Integrated into UniProtKB/Swiss-Prot:	August 1, 1991
Last sequence update:	February 9, 2010
Last modified:	May 29, 2013
This is version 130 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program

Disclaimer

Any 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.