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Protein

DNA-binding protein RFX2

Gene

Rfx2

Organism
Mus musculus (Mouse)
Status
Reviewed-Annotation score: Annotation score: 2 out of 5-Experimental evidence at transcript leveli

Functioni

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
DNA bindingi194 – 26976RFX-type winged-helixPROSITE-ProRule annotationAdd
BLAST

GO - Molecular functioni

  1. RNA polymerase II core promoter proximal region sequence-specific DNA binding Source: GO_Central
  2. sequence-specific DNA binding transcription factor activity Source: GO_Central

GO - Biological processi

  1. regulation of transcription from RNA polymerase II promoter Source: GO_Central
  2. transcription, DNA-templated Source: UniProtKB-KW
Complete GO annotation...

Keywords - Biological processi

Transcription, Transcription regulation

Keywords - Ligandi

DNA-binding

Names & Taxonomyi

Protein namesi
Recommended name:
DNA-binding protein RFX2
Alternative name(s):
Regulatory factor X 2
Gene namesi
Name:Rfx2
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
ProteomesiUP000000589: Chromosome 17

Organism-specific databases

MGIiMGI:106583. Rfx2.

Subcellular locationi

Nucleus Curated

GO - Cellular componenti

  1. nucleus Source: GO_Central
Complete GO annotation...

Keywords - Cellular componenti

Nucleus

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 717717DNA-binding protein RFX2PRO_0000215289Add
BLAST

Proteomic databases

MaxQBiP48379.
PaxDbiP48379.
PRIDEiP48379.

PTM databases

PhosphoSiteiP48379.

Expressioni

Gene expression databases

BgeeiP48379.
GenevestigatoriP48379.

Interactioni

Protein-protein interaction databases

BioGridi202873. 4 interactions.
IntActiP48379. 1 interaction.
STRINGi10090.ENSMUSP00000002444.

Structurei

3D structure databases

ProteinModelPortaliP48379.
SMRiP48379. Positions 195-268.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

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.
GeneTreeiENSGT00550000074532.
HOGENOMiHOG000294091.
HOVERGENiHBG002753.
InParanoidiP48379.
KOiK09173.
OMAiEAQIYAP.
OrthoDBiEOG7TF793.
PhylomeDBiP48379.
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]

Sequences (2)i

Sequence statusi: Complete.

This entry describes 2 isoformsi produced by alternative splicing. Align

Isoform 1 (identifier: P48379-1) [UniParc]FASTAAdd to Basket

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

« Hide

        10         20         30         40         50
MQNSEGGADS PASVALRPAA QPMPASPQRV LVQAAGSTPK GTPMQTLTLP
60 70 80 90 100
RVQPVPPQVQ HVYPAQVQYV EGGDAVYANG AIRAAYAYNP DPQLYAPSSA
110 120 130 140 150
ASYFETPGGT QVTVAASSPP AVPSHGMVGI TMDVSGTPIV SGAGAYLIHG
160 170 180 190 200
GMDGTRHSLA HTARSSPATL EMAIETLQKS EGLAPHKGGL LNSHLQWLLD
210 220 230 240 250
NYETAEGVSL PRSSLYNHYL RHCQEHKLEP VNAASFGKLI RSVFMGLRTR
260 270 280 290 300
RLGTRGNSKY HYYGIRLKPD SPLNRLQEDT QYMAMRQQPT HQKPRYRPAQ
310 320 330 340 350
KSDSLGDGSA HSNMHGMPDQ AMATQGQHHQ QYIDVSHVFP EFPAPDLGST
360 370 380 390 400
LLQESVTLHD VKALQLVYRR HCEATLDVVM NLQFQYIEKL WLSFWNCKAT
410 420 430 440 450
SSDSCASLPA SDEDPEVTLL PKEKLISLCK CEPILQWMRS CDHILYQTLV
460 470 480 490 500
ETLIPDVLRP VPSSLTQAIR NFAKSLEGWL INAMSGFPQQ VIQTKVGVVS
510 520 530 540 550
AFAQTLRRYT SLNHLAQAAR AVLQNTSQIN QMLSDLNRVD FANVQEQASW
560 570 580 590 600
VCQCEESLVQ RLEHDFKVTL QQQSSLDQWA SWLDNVVTQV LKQHSGSPSF
610 620 630 640 650
PKAARQFLLK WSFYSSMVIR DLTLRSAASF GSFHLIRLLY DEYMFYLVEH
660 670 680 690 700
RVAQATGETP IAVMGEFNDL ASLSLTLLDK EDIGDGHSSE ADVDGRSLGE
710
PLVKRERSDP SHPLQGI
Length:717
Mass (Da):79,190
Last modified:July 28, 2009 - v2
Checksum:i3A0EBF008ECD8B61
GO
Isoform 2 (identifier: P48379-2) [UniParc]FASTAAdd to Basket

The sequence of this isoform differs from the canonical sequence as follows:
     170-194: Missing.

Show »
Length:692
Mass (Da):76,534
Checksum:iE4A187A90CD88F81
GO

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei170 – 19425Missing in isoform 2. 2 PublicationsVSP_037812Add
BLAST

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X76089 mRNA. Translation: CAA53703.1.
AK044439 mRNA. Translation: BAC31919.1.
BC004654 mRNA. Translation: AAH04654.1.
CCDSiCCDS28915.1. [P48379-2]
CCDS50156.1. [P48379-1]
PIRiC55926.
RefSeqiNP_033082.1. NM_009056.2. [P48379-2]
NP_082063.1. NM_027787.1. [P48379-1]
UniGeneiMm.102.

Genome annotation databases

EnsembliENSMUST00000002444; ENSMUSP00000002444; ENSMUSG00000024206. [P48379-1]
ENSMUST00000086801; ENSMUSP00000084010; ENSMUSG00000024206. [P48379-2]
GeneIDi19725.
KEGGimmu:19725.
UCSCiuc008ddf.2. mouse. [P48379-2]
uc008ddg.2. mouse. [P48379-1]

Keywords - Coding sequence diversityi

Alternative splicing

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X76089 mRNA. Translation: CAA53703.1.
AK044439 mRNA. Translation: BAC31919.1.
BC004654 mRNA. Translation: AAH04654.1.
CCDSiCCDS28915.1. [P48379-2]
CCDS50156.1. [P48379-1]
PIRiC55926.
RefSeqiNP_033082.1. NM_009056.2. [P48379-2]
NP_082063.1. NM_027787.1. [P48379-1]
UniGeneiMm.102.

3D structure databases

ProteinModelPortaliP48379.
SMRiP48379. Positions 195-268.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi202873. 4 interactions.
IntActiP48379. 1 interaction.
STRINGi10090.ENSMUSP00000002444.

PTM databases

PhosphoSiteiP48379.

Proteomic databases

MaxQBiP48379.
PaxDbiP48379.
PRIDEiP48379.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSMUST00000002444; ENSMUSP00000002444; ENSMUSG00000024206. [P48379-1]
ENSMUST00000086801; ENSMUSP00000084010; ENSMUSG00000024206. [P48379-2]
GeneIDi19725.
KEGGimmu:19725.
UCSCiuc008ddf.2. mouse. [P48379-2]
uc008ddg.2. mouse. [P48379-1]

Organism-specific databases

CTDi5990.
MGIiMGI:106583. Rfx2.

Phylogenomic databases

eggNOGiNOG264634.
GeneTreeiENSGT00550000074532.
HOGENOMiHOG000294091.
HOVERGENiHBG002753.
InParanoidiP48379.
KOiK09173.
OMAiEAQIYAP.
OrthoDBiEOG7TF793.
PhylomeDBiP48379.
TreeFamiTF321340.

Miscellaneous databases

NextBioi297132.
PROiP48379.
SOURCEiSearch...

Gene expression databases

BgeeiP48379.
GenevestigatoriP48379.

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]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "RFX1, a transactivator of hepatitis B virus enhancer I, belongs to a novel family of homodimeric and heterodimeric DNA-binding proteins."
    Reith W., Ucla C., Barras E., Gaud A., Durand B., Herrero-Sanchez C., Kobr M., Mach B.
    Mol. Cell. Biol. 14:1230-1244(1994) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2).
    Strain: BALB/c.
    Tissue: Spleen.
  2. "The transcriptional landscape of the mammalian genome."
    Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.
    , Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.
    Science 309:1559-1563(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
    Strain: C57BL/6J.
    Tissue: Retina.
  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] (ISOFORM 2).
    Strain: FVB/N.
    Tissue: Mammary gland.

Entry informationi

Entry nameiRFX2_MOUSE
AccessioniPrimary (citable) accession number: P48379
Secondary accession number(s): Q8BXR3
Entry historyi
Integrated into UniProtKB/Swiss-Prot: February 1, 1996
Last sequence update: July 28, 2009
Last modified: February 4, 2015
This is version 105 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. MGD cross-references
    Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
  2. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into Uniref entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.