USF2_MOUSE
ID USF2_MOUSE Reviewed; 346 AA.
AC Q64705; Q3UIL2; Q8VE59;
DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1996, sequence version 1.
DT 03-AUG-2022, entry version 166.
DE RecName: Full=Upstream stimulatory factor 2;
DE AltName: Full=Major late transcription factor 2;
DE AltName: Full=Upstream transcription factor 2;
GN Name=Usf2;
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=129/Sv; TISSUE=Kidney, and Spleen;
RX PubMed=7523363; DOI=10.1016/s0021-9258(19)51023-7;
RA Lin Q., Luo X., Sawadogo M.;
RT "Archaic structure of the gene encoding transcription factor USF.";
RL J. Biol. Chem. 269:23894-23903(1994).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS USF2A AND USF2B).
RX PubMed=8127680; DOI=10.1093/nar/22.3.427;
RA Sirito M., Lin Q., Maity T., Sawadogo M.;
RT "Ubiquitous expression of the 43- and 44-kDa forms of transcription factor
RT USF in mammalian cells.";
RL Nucleic Acids Res. 22:427-433(1994).
RN [3]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=129;
RX PubMed=7774954; DOI=10.1016/0888-7543(95)80107-w;
RA Henrion A.A., Martinez A., Mattei M.-G., Kahn A., Raymondjean M.;
RT "Structure, sequence, and chromosomal location of the gene for USF2
RT transcription factors in mouse.";
RL Genomics 25:36-43(1995).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM USF2A).
RC STRAIN=FVB/N, and FVB/N-3; TISSUE=Mammary tumor;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 4-346 (ISOFORM USF2A).
RC STRAIN=C57BL/6J; TISSUE=Amnion;
RX PubMed=16141072; DOI=10.1126/science.1112014;
RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT "The transcriptional landscape of the mammalian genome.";
RL Science 309:1559-1563(2005).
RN [6]
RP INTERACTION WITH MAF.
RX PubMed=9070273; DOI=10.1006/bbrc.1997.6097;
RA Kurschner C., Morgan J.I.;
RT "USF2/FIP associates with the b-Zip transcription factor, c-Maf, via its
RT bHLH domain and inhibits c-Maf DNA binding activity.";
RL Biochem. Biophys. Res. Commun. 231:333-339(1997).
CC -!- FUNCTION: Transcription factor that binds to a symmetrical DNA sequence
CC (E-boxes) (5'-CACGTG-3') that is found in a variety of viral and
CC cellular promoters.
CC -!- SUBUNIT: Efficient DNA binding requires dimerization with another bHLH
CC protein. Binds DNA as a homodimer or a heterodimer (USF1/USF2).
CC Interacts with MAF. {ECO:0000269|PubMed:9070273}.
CC -!- INTERACTION:
CC Q64705; P42225: Stat1; NbExp=3; IntAct=EBI-647583, EBI-647118;
CC -!- SUBCELLULAR LOCATION: Nucleus.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Comment=Additional isoforms seem to exist.;
CC Name=USF2A;
CC IsoId=Q64705-1; Sequence=Displayed;
CC Name=USF2B;
CC IsoId=Q64705-2; Sequence=VSP_002166;
CC -!- SEQUENCE CAUTION:
CC Sequence=AAA20493.1; Type=Erroneous initiation; Evidence={ECO:0000305};
CC Sequence=AAH19729.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; U12283; AAB60674.1; -; Genomic_DNA.
DR EMBL; U12282; AAB60674.1; JOINED; Genomic_DNA.
DR EMBL; U01662; AAA20492.1; -; mRNA.
DR EMBL; U01663; AAA20493.1; ALT_INIT; mRNA.
DR EMBL; X77602; CAA54697.1; -; Genomic_DNA.
DR EMBL; X77605; CAA54697.1; JOINED; Genomic_DNA.
DR EMBL; BC019729; AAH19729.1; ALT_INIT; mRNA.
DR EMBL; BC082995; AAH82995.1; -; mRNA.
DR EMBL; AK146871; BAE27494.1; -; mRNA.
DR CCDS; CCDS21118.1; -. [Q64705-1]
DR PIR; A55111; A55111.
DR RefSeq; NP_035810.1; NM_011680.2. [Q64705-1]
DR RefSeq; XP_006539796.1; XM_006539733.3. [Q64705-2]
DR RefSeq; XP_006539797.1; XM_006539734.3.
DR RefSeq; XP_006539798.1; XM_006539735.3.
DR AlphaFoldDB; Q64705; -.
DR ComplexPortal; CPX-3084; USF2 upstream stimulatory factor complex.
DR ComplexPortal; CPX-3086; USF1-USF2 upstream stimulatory factor complex.
DR IntAct; Q64705; 2.
DR STRING; 10090.ENSMUSP00000132256; -.
DR iPTMnet; Q64705; -.
DR PhosphoSitePlus; Q64705; -.
DR EPD; Q64705; -.
DR MaxQB; Q64705; -.
DR PaxDb; Q64705; -.
DR PRIDE; Q64705; -.
DR ProteomicsDB; 299646; -. [Q64705-1]
DR ProteomicsDB; 299647; -. [Q64705-2]
DR Antibodypedia; 15859; 390 antibodies from 34 providers.
DR DNASU; 22282; -.
DR Ensembl; ENSMUST00000058860; ENSMUSP00000132256; ENSMUSG00000058239. [Q64705-1]
DR Ensembl; ENSMUST00000108119; ENSMUSP00000132021; ENSMUSG00000058239. [Q64705-2]
DR GeneID; 22282; -.
DR KEGG; mmu:22282; -.
DR UCSC; uc009ghg.2; mouse. [Q64705-2]
DR UCSC; uc009ghh.2; mouse. [Q64705-1]
DR CTD; 7392; -.
DR MGI; MGI:99961; Usf2.
DR VEuPathDB; HostDB:ENSMUSG00000058239; -.
DR eggNOG; KOG1318; Eukaryota.
DR GeneTree; ENSGT00940000160704; -.
DR InParanoid; Q64705; -.
DR OMA; SWKMDGP; -.
DR OrthoDB; 1345445at2759; -.
DR PhylomeDB; Q64705; -.
DR TreeFam; TF323338; -.
DR Reactome; R-MMU-9018519; Estrogen-dependent gene expression.
DR BioGRID-ORCS; 22282; 0 hits in 74 CRISPR screens.
DR ChiTaRS; Usf2; mouse.
DR PRO; PR:Q64705; -.
DR Proteomes; UP000000589; Chromosome 7.
DR RNAct; Q64705; protein.
DR Bgee; ENSMUSG00000058239; Expressed in retinal neural layer and 252 other tissues.
DR ExpressionAtlas; Q64705; baseline and differential.
DR Genevisible; Q64705; MM.
DR GO; GO:0043231; C:intracellular membrane-bounded organelle; ISO:MGI.
DR GO; GO:0005654; C:nucleoplasm; ISO:MGI.
DR GO; GO:0005634; C:nucleus; IDA:MGI.
DR GO; GO:0043425; F:bHLH transcription factor binding; ISO:MGI.
DR GO; GO:0003677; F:DNA binding; IDA:MGI.
DR GO; GO:0003700; F:DNA-binding transcription factor activity; ISO:MGI.
DR GO; GO:0000981; F:DNA-binding transcription factor activity, RNA polymerase II-specific; ISO:MGI.
DR GO; GO:0003690; F:double-stranded DNA binding; ISO:MGI.
DR GO; GO:0042802; F:identical protein binding; ISO:MGI.
DR GO; GO:0046982; F:protein heterodimerization activity; ISO:MGI.
DR GO; GO:0042803; F:protein homodimerization activity; ISO:MGI.
DR GO; GO:0044877; F:protein-containing complex binding; ISO:MGI.
DR GO; GO:0000978; F:RNA polymerase II cis-regulatory region sequence-specific DNA binding; ISO:MGI.
DR GO; GO:0043565; F:sequence-specific DNA binding; ISO:MGI.
DR GO; GO:1990837; F:sequence-specific double-stranded DNA binding; ISO:MGI.
DR GO; GO:0007595; P:lactation; IMP:MGI.
DR GO; GO:0055088; P:lipid homeostasis; IMP:BHF-UCL.
DR GO; GO:0045944; P:positive regulation of transcription by RNA polymerase II; ISO:MGI.
DR GO; GO:0000432; P:positive regulation of transcription from RNA polymerase II promoter by glucose; IMP:BHF-UCL.
DR GO; GO:0045893; P:positive regulation of transcription, DNA-templated; IDA:MGI.
DR GO; GO:0006357; P:regulation of transcription by RNA polymerase II; IDA:MGI.
DR Gene3D; 4.10.280.10; -; 1.
DR InterPro; IPR011598; bHLH_dom.
DR InterPro; IPR036638; HLH_DNA-bd_sf.
DR Pfam; PF00010; HLH; 1.
DR SMART; SM00353; HLH; 1.
DR SUPFAM; SSF47459; SSF47459; 1.
DR PROSITE; PS50888; BHLH; 1.
PE 1: Evidence at protein level;
KW Alternative splicing; DNA-binding; Nucleus; Reference proteome;
KW Transcription; Transcription regulation.
FT CHAIN 1..346
FT /note="Upstream stimulatory factor 2"
FT /id="PRO_0000127501"
FT DOMAIN 235..290
FT /note="bHLH"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00981"
FT REGION 1..44
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 215..244
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 307..328
FT /note="Leucine-zipper"
FT COMPBIAS 226..244
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT VAR_SEQ 77..143
FT /note="Missing (in isoform USF2B)"
FT /evidence="ECO:0000303|PubMed:8127680"
FT /id="VSP_002166"
FT CONFLICT 240..243
FT /note="Missing (in Ref. 3; CAA54697)"
FT /evidence="ECO:0000305"
FT CONFLICT 326
FT /note="A -> S (in Ref. 3; CAA54697)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 346 AA; 36954 MW; E9D216BC25F9447B CRC64;
MDMLDPGLDP ASSATAAAAA SHDKGPEAEE GVELQEGGDG PGAEEQTAVA IASVQQAAFG
DHNIQYQFRT ESNGGQVTYR VVQVTDGQLD GQGDAAGAVS VVSTAAFAGG QQAVTQVGVD
GAAQRPGPAA ASVPTGPAAP FPLAVIQNPF SNGGSPAAEA VSGEARFAYF PASSVGDTTA
VSVQTTDQSL QAGGQFYVMM TPQDVLQTGT QRTIAPRTHP YSPKIDGTRT PRDERRRAQH
NEVERRRRDK INNWIVQLSK IIPDCHADNS KTGASKGGIL SKACDYIREL RQTNQRMQET
FKEAERLQMD NELLRQQIEE LKNENALLRA QLQQHNLEMV GESTRQ
