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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
 
 
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