FOSL2_MOUSE
ID FOSL2_MOUSE Reviewed; 326 AA.
AC P47930; Q3UKX7; Q8C231;
DT 01-FEB-1996, integrated into UniProtKB/Swiss-Prot.
DT 27-JUL-2011, sequence version 2.
DT 03-AUG-2022, entry version 151.
DE RecName: Full=Fos-related antigen 2;
DE Short=FRA-2;
GN Name=Fosl2; Synonyms=Fra-2, Fra2;
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 / MRNA] (ISOFORM 1).
RC STRAIN=C57BL/6J; TISSUE=Liver;
RX PubMed=7936655;
RA Foletta V.C., Sonobe M.H., Suzuki T., Endo T., Iba H., Cohen D.R.;
RT "Cloning and characterisation of the mouse fra-2 gene.";
RL Oncogene 9:3305-3311(1994).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
RC STRAIN=C57BL/6J; TISSUE=Dendritic cell, and Placenta;
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 [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC STRAIN=C57BL/6J; TISSUE=Brain;
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 [4]
RP FUNCTION, HETERODIMERIZATION WITH JUN, AND DISRUPTION PHENOTYPE.
RX PubMed=18548006; DOI=10.1038/nature07019;
RA Bozec A., Bakiri L., Hoebertz A., Eferl R., Schilling A.F., Komnenovic V.,
RA Scheuch H., Priemel M., Stewart C.L., Amling M., Wagner E.F.;
RT "Osteoclast size is controlled by Fra-2 through LIF/LIF-receptor signalling
RT and hypoxia.";
RL Nature 454:221-225(2008).
RN [5]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Embryonic fibroblast;
RX PubMed=19131326; DOI=10.1074/mcp.m800451-mcp200;
RA Sweet S.M., Bailey C.M., Cunningham D.L., Heath J.K., Cooper H.J.;
RT "Large scale localization of protein phosphorylation by use of electron
RT capture dissociation mass spectrometry.";
RL Mol. Cell. Proteomics 8:904-912(2009).
RN [6]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Spleen;
RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL Cell 143:1174-1189(2010).
RN [7]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-104, AND IDENTIFICATION BY MASS
RP SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Embryonic fibroblast;
RX PubMed=23806337; DOI=10.1016/j.molcel.2013.06.001;
RA Park J., Chen Y., Tishkoff D.X., Peng C., Tan M., Dai L., Xie Z., Zhang Y.,
RA Zwaans B.M., Skinner M.E., Lombard D.B., Zhao Y.;
RT "SIRT5-mediated lysine desuccinylation impacts diverse metabolic
RT pathways.";
RL Mol. Cell 50:919-930(2013).
RN [8]
RP INTERACTION WITH SMARCB1; SMARCD1; ARID1A AND JUN.
RX PubMed=29272704; DOI=10.1016/j.molcel.2017.11.026;
RA Vierbuchen T., Ling E., Cowley C.J., Couch C.H., Wang X., Harmin D.A.,
RA Roberts C.W.M., Greenberg M.E.;
RT "AP-1 Transcription Factors and the BAF Complex Mediate Signal-Dependent
RT Enhancer Selection.";
RL Mol. Cell 68:1067-1082.e12(2017).
CC -!- FUNCTION: Controls osteoclast survival and size (PubMed:18548006). As a
CC dimer with JUN, activates LIF transcription (PubMed:18548006).
CC Activates CEBPB transcription in PGE2-activated osteoblasts (By
CC similarity). {ECO:0000250|UniProtKB:P51145,
CC ECO:0000269|PubMed:18548006}.
CC -!- SUBUNIT: Heterodimer; with JUN (PubMed:18548006). Interacts with the
CC BAF multiprotein chromatin-remodeling complex subunits SMARCB1 and
CC SMARCD1 (PubMed:29272704). Interacts with ARID1A and JUN
CC (PubMed:29272704). {ECO:0000269|PubMed:18548006,
CC ECO:0000269|PubMed:29272704}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:P51145}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=P47930-1; Sequence=Displayed;
CC Name=2;
CC IsoId=P47930-2; Sequence=VSP_042084;
CC -!- DISRUPTION PHENOTYPE: Mutant pups die within a week after birth. They
CC exhibit severe osteopenia as early as 18.5 dpc, with a 50% decrease in
CC mineralized bone. Osteoblast numbers are not altered. The number, the
CC relative surface covered by osteoclasts and the mean osteoclast surface
CC are increased 3-fold, 5-fold and 2-fold, respectively. Bone resorption
CC activity is increased. This phenotype is due to hypoxia in long bones
CC resulting from placental defects. {ECO:0000269|PubMed:18548006}.
CC -!- SIMILARITY: Belongs to the bZIP family. Fos subfamily. {ECO:0000305}.
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DR EMBL; X83971; CAA58805.1; -; mRNA.
DR EMBL; X83970; CAA58804.1; -; Genomic_DNA.
DR EMBL; AK089371; BAC40860.1; -; mRNA.
DR EMBL; AK145822; BAE26674.1; -; mRNA.
DR EMBL; BC065131; AAH65131.1; -; mRNA.
DR CCDS; CCDS19190.1; -. [P47930-1]
DR PIR; I48351; I48351.
DR RefSeq; NP_032063.2; NM_008037.4. [P47930-1]
DR AlphaFoldDB; P47930; -.
DR SMR; P47930; -.
DR BioGRID; 199729; 1.
DR ELM; P47930; -.
DR STRING; 10090.ENSMUSP00000031017; -.
DR iPTMnet; P47930; -.
DR PhosphoSitePlus; P47930; -.
DR EPD; P47930; -.
DR jPOST; P47930; -.
DR MaxQB; P47930; -.
DR PaxDb; P47930; -.
DR PeptideAtlas; P47930; -.
DR PRIDE; P47930; -.
DR ProteomicsDB; 267393; -. [P47930-1]
DR ProteomicsDB; 267394; -. [P47930-2]
DR Antibodypedia; 1415; 592 antibodies from 36 providers.
DR DNASU; 14284; -.
DR Ensembl; ENSMUST00000031017; ENSMUSP00000031017; ENSMUSG00000029135. [P47930-1]
DR GeneID; 14284; -.
DR KEGG; mmu:14284; -.
DR UCSC; uc008wzi.2; mouse. [P47930-1]
DR UCSC; uc008wzj.1; mouse. [P47930-2]
DR CTD; 2355; -.
DR MGI; MGI:102858; Fosl2.
DR VEuPathDB; HostDB:ENSMUSG00000029135; -.
DR eggNOG; KOG1414; Eukaryota.
DR GeneTree; ENSGT00940000158876; -.
DR HOGENOM; CLU_049742_2_1_1; -.
DR InParanoid; P47930; -.
DR OMA; PNMLEPE; -.
DR OrthoDB; 1221590at2759; -.
DR PhylomeDB; P47930; -.
DR TreeFam; TF326301; -.
DR BioGRID-ORCS; 14284; 1 hit in 71 CRISPR screens.
DR ChiTaRS; Fosl2; mouse.
DR PRO; PR:P47930; -.
DR Proteomes; UP000000589; Chromosome 5.
DR RNAct; P47930; protein.
DR Bgee; ENSMUSG00000029135; Expressed in decidua and 248 other tissues.
DR Genevisible; P47930; MM.
DR GO; GO:0005654; C:nucleoplasm; ISO:MGI.
DR GO; GO:0005634; C:nucleus; IDA:MGI.
DR GO; GO:0090575; C:RNA polymerase II transcription regulator complex; ISO:MGI.
DR GO; GO:0003682; F:chromatin binding; IDA:MGI.
DR GO; GO:0003677; F:DNA binding; ISO:MGI.
DR GO; GO:0001228; F:DNA-binding transcription activator activity, RNA polymerase II-specific; ISO: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; IBA:GO_Central.
DR GO; GO:0003690; F:double-stranded DNA binding; ISO:MGI.
DR GO; GO:0000978; F:RNA polymerase II cis-regulatory region sequence-specific DNA binding; IBA:GO_Central.
DR GO; GO:0000977; F:RNA polymerase II transcription regulatory region sequence-specific DNA binding; IDA:MGI.
DR GO; GO:0043565; F:sequence-specific DNA binding; ISO:MGI.
DR GO; GO:0000976; F:transcription cis-regulatory region binding; ISO:MGI.
DR GO; GO:0003334; P:keratinocyte development; IMP:MGI.
DR GO; GO:0048146; P:positive regulation of fibroblast proliferation; IDA:MGI.
DR GO; GO:0045944; P:positive regulation of transcription by RNA polymerase II; IDA:MGI.
DR GO; GO:0045893; P:positive regulation of transcription, DNA-templated; IDA:CACAO.
DR GO; GO:0006357; P:regulation of transcription by RNA polymerase II; IBA:GO_Central.
DR GO; GO:0032355; P:response to estradiol; ISO:MGI.
DR GO; GO:0001666; P:response to hypoxia; ISO:MGI.
DR GO; GO:0006366; P:transcription by RNA polymerase II; ISO:MGI.
DR InterPro; IPR000837; AP-1.
DR InterPro; IPR004827; bZIP.
DR InterPro; IPR046347; bZIP_sf.
DR InterPro; IPR029814; Fra2.
DR PANTHER; PTHR23351; PTHR23351; 1.
DR PANTHER; PTHR23351:SF25; PTHR23351:SF25; 1.
DR Pfam; PF00170; bZIP_1; 1.
DR PRINTS; PR00042; LEUZIPPRFOS.
DR SMART; SM00338; BRLZ; 1.
DR SUPFAM; SSF57959; SSF57959; 1.
DR PROSITE; PS50217; BZIP; 1.
DR PROSITE; PS00036; BZIP_BASIC; 1.
PE 1: Evidence at protein level;
KW Acetylation; Alternative splicing; DNA-binding; Isopeptide bond; Nucleus;
KW Phosphoprotein; Reference proteome; Transcription;
KW Transcription regulation; Ubl conjugation.
FT CHAIN 1..326
FT /note="Fos-related antigen 2"
FT /id="PRO_0000076484"
FT DOMAIN 124..187
FT /note="bZIP"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00978"
FT REGION 1..39
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 110..131
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 126..128
FT /note="Basic motif"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00978"
FT REGION 129..136
FT /note="Leucine-zipper"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00978"
FT REGION 193..244
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 285..326
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..32
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 1
FT /note="N-acetylmethionine"
FT /evidence="ECO:0000250|UniProtKB:P15408"
FT MOD_RES 104
FT /note="N6-acetyllysine; alternate"
FT /evidence="ECO:0007744|PubMed:23806337"
FT MOD_RES 120
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P15408"
FT MOD_RES 200
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P15408"
FT MOD_RES 230
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P15408"
FT MOD_RES 308
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P15408"
FT MOD_RES 320
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P15408"
FT CROSSLNK 35
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:P15408"
FT CROSSLNK 104
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2); alternate"
FT /evidence="ECO:0000250|UniProtKB:P15408"
FT CROSSLNK 222
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO1); alternate"
FT /evidence="ECO:0000250|UniProtKB:P15408"
FT CROSSLNK 222
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2); alternate"
FT /evidence="ECO:0000250|UniProtKB:P15408"
FT CROSSLNK 239
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:P15408"
FT VAR_SEQ 1..33
FT /note="MYQDYPGNFDTSSRGSSGSPAHAESYSSGGGGQ -> MSFSLF (in
FT isoform 2)"
FT /evidence="ECO:0000303|PubMed:16141072"
FT /id="VSP_042084"
FT CONFLICT 184
FT /note="L -> K (in Ref. 1; CAA58805)"
FT /evidence="ECO:0000305"
FT CONFLICT 267
FT /note="V -> E (in Ref. 2; BAE26674)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 326 AA; 35298 MW; 05B0F20D7D0B790A CRC64;
MYQDYPGNFD TSSRGSSGSP AHAESYSSGG GGQQKFRVDM PGSGSAFIPT INAITTSQDL
QWMVQPTVIT SMSNPYPRSH PYSPLPGLAS VPGHMALPRP GVIKTIGTTV GRRRRDEQLS
PEEEEKRRIR RERNKLAAAK CRNRRRELTE KLQAETEELE EEKSGLQKEI AELQKEKEKL
EFMLVAHGPV CKISPEERRS PPTSGLQSLR GTGSAVGPVV VKQEPPEEDS PSSSAGMDKT
QRSVIKPISI AGGGFYGEEP LHTPIVVTST PAITPGTSNL VFTYPNVLEQ ESPSSPSESC
SKAHRRSSSS GDQSSDSLNS PTLLAL
