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P47930 (FOSL2_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 100. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Alt products·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Fos-related antigen 2

Short name=FRA-2
Gene names
Name:Fosl2
Synonyms:Fra-2, Fra2
OrganismMus musculus (Mouse) [Reference proteome]
Taxonomic identifier10090 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus

Protein attributes

Sequence length326 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Controls osteoclast survival and size. As a dimer with JUN, activates LIF transcription. Activates CEBPB transcription in PGE2-activated osteoblasts By similarity. Ref.4

Subunit structure

Heterodimer; with JUN. Ref.4

Subcellular location

Nucleus.

Disruption phenotype

Mutant pups die within a week after birth. They exhibit severe osteopenia as early as 18.5 dpc, with a 50% decrease in mineralized bone. Osteoblast numbers are not altered. The number, the relative surface covered by osteoclasts and the mean osteoclast surface are increased 3-fold, 5-fold and 2-fold, respectively. Bone resorption activity is increased. This phenotype is due to hypoxia in long bones resulting from placental defects. Ref.4

Sequence similarities

Belongs to the bZIP family. Fos subfamily.

Contains 1 bZIP (basic-leucine zipper) domain.

Ontologies

Keywords
   Biological processTranscription
Transcription regulation
   Cellular componentNucleus
   Coding sequence diversityAlternative splicing
   LigandDNA-binding
   PTMAcetylation
Phosphoprotein
   Technical termComplete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processcellular response to hormone stimulus

Inferred from electronic annotation. Source: Ensembl

female pregnancy

Inferred from electronic annotation. Source: Ensembl

positive regulation of fibroblast proliferation

Inferred from direct assay Ref.1. Source: MGI

response to cAMP

Inferred from electronic annotation. Source: Ensembl

response to corticosterone

Inferred from electronic annotation. Source: Ensembl

response to drug

Inferred from electronic annotation. Source: Ensembl

response to mechanical stimulus

Inferred from electronic annotation. Source: Ensembl

response to morphine

Inferred from electronic annotation. Source: Ensembl

response to progesterone

Inferred from electronic annotation. Source: Ensembl

transcription from RNA polymerase II promoter

Inferred from electronic annotation. Source: Ensembl

   Cellular_componentnucleus

Inferred from electronic annotation. Source: UniProtKB-SubCell

   Molecular_functionRNA polymerase II regulatory region sequence-specific DNA binding

Inferred from direct assay PubMed 19289495. Source: MGI

double-stranded DNA binding

Inferred from electronic annotation. Source: Ensembl

sequence-specific DNA binding transcription factor activity

Inferred from electronic annotation. Source: Ensembl

Complete GO annotation...

Alternative products

This entry describes 2 isoforms produced by alternative splicing. [Align] [Select]
Isoform 1 (identifier: P47930-1)

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.
Isoform 2 (identifier: P47930-2)

The sequence of this isoform differs from the canonical sequence as follows:
     1-33: MYQDYPGNFDTSSRGSSGSPAHAESYSSGGGGQ → MSFSLF
Note: No experimental confirmation available.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 326326Fos-related antigen 2
PRO_0000076484

Regions

Domain124 – 18764bZIP
Region126 – 1283Basic motif By similarity
Region129 – 1368Leucine-zipper By similarity

Amino acid modifications

Modified residue11N-acetylmethionine By similarity
Modified residue1041N6-acetyllysine Ref.6
Modified residue1201Phosphoserine By similarity
Modified residue2001Phosphoserine By similarity
Modified residue2301Phosphoserine By similarity
Modified residue3201Phosphoserine By similarity

Natural variations

Alternative sequence1 – 3333MYQDY…GGGGQ → MSFSLF in isoform 2.
VSP_042084

Experimental info

Sequence conflict1841L → K in CAA58805. Ref.1
Sequence conflict2671V → E in BAE26674. Ref.2

Sequences

Sequence LengthMass (Da)Tools
Isoform 1 [UniParc].

Last modified July 27, 2011. Version 2.
Checksum: 05B0F20D7D0B790A

FASTA32635,298
        10         20         30         40         50         60 
MYQDYPGNFD TSSRGSSGSP AHAESYSSGG GGQQKFRVDM PGSGSAFIPT INAITTSQDL 

        70         80         90        100        110        120 
QWMVQPTVIT SMSNPYPRSH PYSPLPGLAS VPGHMALPRP GVIKTIGTTV GRRRRDEQLS 

       130        140        150        160        170        180 
PEEEEKRRIR RERNKLAAAK CRNRRRELTE KLQAETEELE EEKSGLQKEI AELQKEKEKL 

       190        200        210        220        230        240 
EFMLVAHGPV CKISPEERRS PPTSGLQSLR GTGSAVGPVV VKQEPPEEDS PSSSAGMDKT 

       250        260        270        280        290        300 
QRSVIKPISI AGGGFYGEEP LHTPIVVTST PAITPGTSNL VFTYPNVLEQ ESPSSPSESC 

       310        320 
SKAHRRSSSS GDQSSDSLNS PTLLAL 

« Hide

Isoform 2 [UniParc].

Checksum: 4879B6E93597B61E
Show »

FASTA29932,687

References

« Hide 'large scale' references
[1]"Cloning and characterisation of the mouse fra-2 gene."
Foletta V.C., Sonobe M.H., Suzuki T., Endo T., Iba H., Cohen D.R.
Oncogene 9:3305-3311(1994) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA] (ISOFORM 1).
Strain: C57BL/6.
Tissue: Liver.
[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. expand/collapse author list , 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] (ISOFORMS 1 AND 2).
Strain: C57BL/6J.
Tissue: Dendritic cell and Placenta.
[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 1).
Strain: C57BL/6.
Tissue: Brain.
[4]"Osteoclast size is controlled by Fra-2 through LIF/LIF-receptor signalling and hypoxia."
Bozec A., Bakiri L., Hoebertz A., Eferl R., Schilling A.F., Komnenovic V., Scheuch H., Priemel M., Stewart C.L., Amling M., Wagner E.F.
Nature 454:221-225(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, HETERODIMERIZATION WITH JUN, DISRUPTION PHENOTYPE.
[5]"Large scale localization of protein phosphorylation by use of electron capture dissociation mass spectrometry."
Sweet S.M., Bailey C.M., Cunningham D.L., Heath J.K., Cooper H.J.
Mol. Cell. Proteomics 8:904-912(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Embryonic fibroblast.
[6]"SIRT5-mediated lysine desuccinylation impacts diverse metabolic pathways."
Park J., Chen Y., Tishkoff D.X., Peng C., Tan M., Dai L., Xie Z., Zhang Y., Zwaans B.M., Skinner M.E., Lombard D.B., Zhao Y.
Mol. Cell 50:919-930(2013) [PubMed] [Europe PMC] [Abstract]
Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-104, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Embryonic fibroblast.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
X83971 mRNA. Translation: CAA58805.1.
X83970 Genomic DNA. Translation: CAA58804.1.
AK089371 mRNA. Translation: BAC40860.1.
AK145822 mRNA. Translation: BAE26674.1.
BC065131 mRNA. Translation: AAH65131.1.
CCDSCCDS19190.1. [P47930-1]
PIRI48351.
RefSeqNP_032063.2. NM_008037.4. [P47930-1]
UniGeneMm.24684.

3D structure databases

ProteinModelPortalP47930.
SMRP47930. Positions 125-187.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING10090.ENSMUSP00000031017.

PTM databases

PhosphoSiteP47930.

Proteomic databases

PRIDEP47930.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENSMUST00000031017; ENSMUSP00000031017; ENSMUSG00000029135. [P47930-1]
GeneID14284.
KEGGmmu:14284.
UCSCuc008wzi.2. mouse. [P47930-1]
uc008wzj.1. mouse. [P47930-2]

Organism-specific databases

CTD2355.
MGIMGI:102858. Fosl2.

Phylogenomic databases

eggNOGNOG301361.
GeneTreeENSGT00730000110541.
HOGENOMHOG000234334.
HOVERGENHBG005743.
InParanoidQ8C231.
KOK09030.
OMAIKPICLG.
OrthoDBEOG761BVN.
TreeFamTF326301.

Gene expression databases

BgeeP47930.
CleanExMM_FOSL2.
GenevestigatorP47930.

Family and domain databases

InterProIPR004827. bZIP.
IPR000837. Leuzip_Fos.
[Graphical view]
PfamPF00170. bZIP_1. 1 hit.
[Graphical view]
PRINTSPR00042. LEUZIPPRFOS.
SMARTSM00338. BRLZ. 1 hit.
[Graphical view]
PROSITEPS50217. BZIP. 1 hit.
PS00036. BZIP_BASIC. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

NextBio285669.
PROP47930.
SOURCESearch...

Entry information

Entry nameFOSL2_MOUSE
AccessionPrimary (citable) accession number: P47930
Secondary accession number(s): Q3UKX7, Q8C231
Entry history
Integrated into UniProtKB/Swiss-Prot: February 1, 1996
Last sequence update: July 27, 2011
Last modified: July 9, 2014
This is version 100 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

MGD cross-references

Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot