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P48379

- RFX2_MOUSE

UniProt

P48379 - RFX2_MOUSE

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Protein

DNA-binding protein RFX2

Gene

Rfx2

Organism
Mus musculus (Mouse)
Status
Reviewed - 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. DNA binding Source: UniProtKB-KW

GO - Biological processi

  1. regulation of transcription, DNA-templated Source: UniProtKB-KW
  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: UniProtKB-KW
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 .
CCDSi CCDS28915.1. [P48379-2 ]
CCDS50156.1. [P48379-1 ]
PIRi C55926.
RefSeqi NP_033082.1. NM_009056.2. [P48379-2 ]
NP_082063.1. NM_027787.1. [P48379-1 ]
UniGenei Mm.102.

3D structure databases

ProteinModelPortali P48379.
SMRi P48379. Positions 195-268.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 202873. 4 interactions.
IntActi P48379. 1 interaction.
STRINGi 10090.ENSMUSP00000002444.

PTM databases

PhosphoSitei P48379.

Proteomic databases

MaxQBi P48379.
PaxDbi P48379.
PRIDEi P48379.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENSMUST00000002444 ; ENSMUSP00000002444 ; ENSMUSG00000024206 . [P48379-1 ]
ENSMUST00000086801 ; ENSMUSP00000084010 ; ENSMUSG00000024206 . [P48379-2 ]
GeneIDi 19725.
KEGGi mmu:19725.
UCSCi uc008ddf.2. mouse. [P48379-2 ]
uc008ddg.2. mouse. [P48379-1 ]

Organism-specific databases

CTDi 5990.
MGIi MGI:106583. Rfx2.

Phylogenomic databases

eggNOGi NOG264634.
GeneTreei ENSGT00550000074532.
HOGENOMi HOG000294091.
HOVERGENi HBG002753.
InParanoidi P48379.
KOi K09173.
OMAi EAQIYAP.
OrthoDBi EOG7TF793.
PhylomeDBi P48379.
TreeFami TF321340.

Miscellaneous databases

NextBioi 297132.
PROi P48379.
SOURCEi Search...

Gene expression databases

Bgeei P48379.
Genevestigatori P48379.

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

« 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: October 29, 2014
This is version 103 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