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Protein

Fos-related antigen 2

Gene

Fosl2

Organism
Mus musculus (Mouse)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

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

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Biological processi

Transcription, Transcription regulation

Keywords - Ligandi

DNA-binding

Names & Taxonomyi

Protein namesi
Recommended name:
Fos-related antigen 2
Short name:
FRA-2
Gene namesi
Name:Fosl2
Synonyms:Fra-2, Fra2
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
ProteomesiUP000000589 Componenti: Chromosome 5

Organism-specific databases

MGIiMGI:102858. Fosl2.

Subcellular locationi

GO - Cellular componenti

  • nucleoplasm Source: MGI
  • nucleus Source: MGI
Complete GO annotation...

Keywords - Cellular componenti

Nucleus

Pathology & Biotechi

Disruption phenotypei

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.1 Publication

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 326326Fos-related antigen 2PRO_0000076484Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei1 – 11N-acetylmethionineBy similarity
Modified residuei104 – 1041N6-acetyllysine1 Publication
Modified residuei120 – 1201PhosphoserineBy similarity
Modified residuei200 – 2001PhosphoserineBy similarity
Modified residuei230 – 2301PhosphoserineBy similarity
Modified residuei320 – 3201PhosphoserineBy similarity

Keywords - PTMi

Acetylation, Phosphoprotein

Proteomic databases

MaxQBiP47930.
PRIDEiP47930.

PTM databases

PhosphoSiteiP47930.

Expressioni

Gene expression databases

BgeeiP47930.
CleanExiMM_FOSL2.
GenevisibleiP47930. MM.

Interactioni

Subunit structurei

Heterodimer; with JUN.

Protein-protein interaction databases

STRINGi10090.ENSMUSP00000031017.

Structurei

3D structure databases

ProteinModelPortaliP47930.
SMRiP47930. Positions 125-187.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini124 – 18764bZIPPROSITE-ProRule annotationAdd
BLAST

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni126 – 1283Basic motifPROSITE-ProRule annotation
Regioni129 – 1368Leucine-zipperPROSITE-ProRule annotation

Sequence similaritiesi

Belongs to the bZIP family. Fos subfamily.Curated
Contains 1 bZIP (basic-leucine zipper) domain.PROSITE-ProRule annotation

Phylogenomic databases

eggNOGiNOG301361.
GeneTreeiENSGT00730000110541.
HOGENOMiHOG000234334.
HOVERGENiHBG005743.
InParanoidiP47930.
KOiK09030.
OMAiPYSRSHP.
OrthoDBiEOG761BVN.
TreeFamiTF326301.

Family and domain databases

InterProiIPR000837. AP-1.
IPR004827. bZIP.
IPR029814. Fra2.
[Graphical view]
PANTHERiPTHR23351. PTHR23351. 1 hit.
PTHR23351:SF25. PTHR23351:SF25. 1 hit.
PfamiPF00170. bZIP_1. 1 hit.
[Graphical view]
PRINTSiPR00042. LEUZIPPRFOS.
SMARTiSM00338. BRLZ. 1 hit.
[Graphical view]
PROSITEiPS50217. BZIP. 1 hit.
PS00036. BZIP_BASIC. 1 hit.
[Graphical view]

Sequences (2)i

Sequence statusi: Complete.

This entry describes 2 isoformsi produced by alternative splicing. AlignAdd to basket

Isoform 1 (identifier: P47930-1) [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
MYQDYPGNFD TSSRGSSGSP AHAESYSSGG GGQQKFRVDM PGSGSAFIPT
60 70 80 90 100
INAITTSQDL QWMVQPTVIT SMSNPYPRSH PYSPLPGLAS VPGHMALPRP
110 120 130 140 150
GVIKTIGTTV GRRRRDEQLS PEEEEKRRIR RERNKLAAAK CRNRRRELTE
160 170 180 190 200
KLQAETEELE EEKSGLQKEI AELQKEKEKL EFMLVAHGPV CKISPEERRS
210 220 230 240 250
PPTSGLQSLR GTGSAVGPVV VKQEPPEEDS PSSSAGMDKT QRSVIKPISI
260 270 280 290 300
AGGGFYGEEP LHTPIVVTST PAITPGTSNL VFTYPNVLEQ ESPSSPSESC
310 320
SKAHRRSSSS GDQSSDSLNS PTLLAL
Length:326
Mass (Da):35,298
Last modified:July 27, 2011 - v2
Checksum:i05B0F20D7D0B790A
GO
Isoform 2 (identifier: P47930-2) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     1-33: MYQDYPGNFDTSSRGSSGSPAHAESYSSGGGGQ → MSFSLF

Note: No experimental confirmation available.
Show »
Length:299
Mass (Da):32,687
Checksum:i4879B6E93597B61E
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti184 – 1841L → K in CAA58805 (PubMed:7936655).Curated
Sequence conflicti267 – 2671V → E in BAE26674 (PubMed:16141072).Curated

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei1 – 3333MYQDY…GGGGQ → MSFSLF in isoform 2. 1 PublicationVSP_042084Add
BLAST

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
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.
CCDSiCCDS19190.1. [P47930-1]
PIRiI48351.
RefSeqiNP_032063.2. NM_008037.4. [P47930-1]
UniGeneiMm.24684.

Genome annotation databases

EnsembliENSMUST00000031017; ENSMUSP00000031017; ENSMUSG00000029135. [P47930-1]
GeneIDi14284.
KEGGimmu:14284.
UCSCiuc008wzi.2. mouse. [P47930-1]
uc008wzj.1. mouse. [P47930-2]

Keywords - Coding sequence diversityi

Alternative splicing

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
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.
CCDSiCCDS19190.1. [P47930-1]
PIRiI48351.
RefSeqiNP_032063.2. NM_008037.4. [P47930-1]
UniGeneiMm.24684.

3D structure databases

ProteinModelPortaliP47930.
SMRiP47930. Positions 125-187.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi10090.ENSMUSP00000031017.

PTM databases

PhosphoSiteiP47930.

Proteomic databases

MaxQBiP47930.
PRIDEiP47930.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSMUST00000031017; ENSMUSP00000031017; ENSMUSG00000029135. [P47930-1]
GeneIDi14284.
KEGGimmu:14284.
UCSCiuc008wzi.2. mouse. [P47930-1]
uc008wzj.1. mouse. [P47930-2]

Organism-specific databases

CTDi2355.
MGIiMGI:102858. Fosl2.

Phylogenomic databases

eggNOGiNOG301361.
GeneTreeiENSGT00730000110541.
HOGENOMiHOG000234334.
HOVERGENiHBG005743.
InParanoidiP47930.
KOiK09030.
OMAiPYSRSHP.
OrthoDBiEOG761BVN.
TreeFamiTF326301.

Miscellaneous databases

NextBioi285669.
PROiP47930.
SOURCEiSearch...

Gene expression databases

BgeeiP47930.
CleanExiMM_FOSL2.
GenevisibleiP47930. MM.

Family and domain databases

InterProiIPR000837. AP-1.
IPR004827. bZIP.
IPR029814. Fra2.
[Graphical view]
PANTHERiPTHR23351. PTHR23351. 1 hit.
PTHR23351:SF25. PTHR23351:SF25. 1 hit.
PfamiPF00170. bZIP_1. 1 hit.
[Graphical view]
PRINTSiPR00042. LEUZIPPRFOS.
SMARTiSM00338. BRLZ. 1 hit.
[Graphical view]
PROSITEiPS50217. BZIP. 1 hit.
PS00036. BZIP_BASIC. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  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.
    , 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.

Entry informationi

Entry nameiFOSL2_MOUSE
AccessioniPrimary (citable) accession number: P47930
Secondary accession number(s): Q3UKX7, Q8C231
Entry historyi
Integrated into UniProtKB/Swiss-Prot: February 1, 1996
Last sequence update: July 27, 2011
Last modified: June 24, 2015
This is version 108 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

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into Uniref entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.