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Protein

Fos-related antigen 2

Gene

Fosl2

Organism
Rattus norvegicus (Rat)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Controls osteoclast survival and size (By similarity). As a dimer with JUN, activates LIF transcription (By similarity). Activates CEBPB transcription in PGE2-activated osteoblasts.By similarity1 Publication

GO - Molecular functioni

  • DNA binding Source: RGD
  • double-stranded DNA binding Source: RGD
  • sequence-specific DNA binding Source: RGD
  • transcription factor activity, sequence-specific DNA binding Source: RGD
  • transcription regulatory region DNA binding Source: RGD

GO - Biological processi

  • aging Source: RGD
  • circadian rhythm Source: RGD
  • conditioned taste aversion Source: RGD
  • female pregnancy Source: RGD
  • photoperiodism Source: RGD
  • positive regulation of transcription, DNA-templated Source: RGD
  • regulation of transcription from RNA polymerase II promoter Source: InterPro
  • response to cAMP Source: RGD
  • response to cold Source: RGD
  • response to cytokine Source: RGD
  • response to estradiol Source: RGD
  • response to hypoxia Source: RGD
  • response to immobilization stress Source: RGD
  • response to light stimulus Source: RGD
  • response to mechanical stimulus Source: RGD
  • response to organic cyclic compound Source: RGD
  • response to peptide hormone Source: RGD
  • response to progesterone Source: RGD
  • response to toxic substance Source: RGD
  • sleep Source: RGD
  • transcription from RNA polymerase II promoter Source: RGD
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
OrganismiRattus norvegicus (Rat)
Taxonomic identifieri10116 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeRattus
Proteomesi
  • UP000002494 Componenti: Unplaced

Organism-specific databases

RGDi2628. Fosl2.

Subcellular locationi

  • Nucleus PROSITE-ProRule annotation1 Publication

GO - Cellular componenti

  • nucleus Source: RGD
Complete GO annotation...

Keywords - Cellular componenti

Nucleus

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 326326Fos-related antigen 2PRO_0000076485Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei1 – 11N-acetylmethionineBy similarity
Modified residuei104 – 1041N6-acetyllysineBy similarity
Modified residuei120 – 1201PhosphoserineBy similarity
Modified residuei200 – 2001PhosphoserineBy similarity
Cross-linki222 – 222Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)By similarity
Modified residuei230 – 2301PhosphoserineBy similarity
Modified residuei320 – 3201PhosphoserineBy similarity

Keywords - PTMi

Acetylation, Isopeptide bond, Phosphoprotein, Ubl conjugation

Proteomic databases

PaxDbiP51145.

PTM databases

iPTMnetiP51145.

Expressioni

Tissue specificityi

Expressed in the brain cortex. Expressed at night in pineal gland (at protein level). Also expressed in osteoblasts (at protein level).3 Publications

Inductioni

In the pineal gland, exhibits night/day variations with a 4-fold increased expression at night (at protein level). Up-regulation is due to a large degree to the release of norepinephrine from nerve terminals in the pineal gland and cAMP signaling pathway. Nocturnally elevated expression is also observed in the brain cortex. In osteoblasts, up-regulated by PGE2 (at protein level).3 Publications

Interactioni

Subunit structurei

Heterodimer.By similarity

Protein-protein interaction databases

STRINGi10116.ENSRNOP00000064213.

Structurei

3D structure databases

ProteinModelPortaliP51145.
SMRiP51145. Positions 126-184.
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

eggNOGiKOG1414. Eukaryota.
ENOG4111CH5. LUCA.
HOVERGENiHBG005743.
InParanoidiP51145.
KOiK09030.

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]

Sequencei

Sequence statusi: Complete.

P51145-1 [UniParc]FASTAAdd to basket

« 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 VFTYPSVLEQ ESPASPSESC
310 320
SKAHRRSSSS GDQSSDSLNS PTLLAL
Length:326
Mass (Da):35,255
Last modified:December 14, 2011 - v2
Checksum:i07DD44D47D0B790A
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti56 – 561T → TT in AAC52310 (PubMed:7592994).Curated
Sequence conflicti89 – 891A → R in AAC52310 (PubMed:7592994).Curated
Sequence conflicti154 – 1541A → T in AAC52310 (PubMed:7592994).Curated
Sequence conflicti201 – 2011P → S in AAC52310 (PubMed:7592994).Curated
Sequence conflicti206 – 2061L → V in AAC52310 (PubMed:7592994).Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U18913 mRNA. Translation: AAC52310.1.
AY622611 mRNA. Translation: AAT52165.1.
PIRiI55459.
RefSeqiNP_037086.1. NM_012954.1.
UniGeneiRn.10962.

Genome annotation databases

GeneIDi25446.
KEGGirno:25446.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U18913 mRNA. Translation: AAC52310.1.
AY622611 mRNA. Translation: AAT52165.1.
PIRiI55459.
RefSeqiNP_037086.1. NM_012954.1.
UniGeneiRn.10962.

3D structure databases

ProteinModelPortaliP51145.
SMRiP51145. Positions 126-184.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi10116.ENSRNOP00000064213.

PTM databases

iPTMnetiP51145.

Proteomic databases

PaxDbiP51145.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

GeneIDi25446.
KEGGirno:25446.

Organism-specific databases

CTDi2355.
RGDi2628. Fosl2.

Phylogenomic databases

eggNOGiKOG1414. Eukaryota.
ENOG4111CH5. LUCA.
HOVERGENiHBG005743.
InParanoidiP51145.
KOiK09030.

Miscellaneous databases

NextBioi606679.
PROiP51145.

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

  1. "Circadian expression of transcription factor Fra-2 in the rat pineal gland."
    Baler R.D., Klein D.C.
    J. Biol. Chem. 270:27319-27325(1995) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA], TISSUE SPECIFICITY, INDUCTION.
    Strain: Sprague-Dawley.
    Tissue: Pineal gland.
  2. "Fos-related antigen 2 controls protein kinase A-induced CCAAT/enhancer-binding protein beta expression in osteoblasts."
    Chang W., Rewari A., Centrella M., McCarthy T.L.
    J. Biol. Chem. 279:42438-42444(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, SUBCELLULAR LOCATION, TISSUE SPECIFICITY, INDUCTION.
    Strain: Sprague-Dawley.
    Tissue: Osteoblast.
  3. Cited for: TISSUE SPECIFICITY, INDUCTION.

Entry informationi

Entry nameiFOSL2_RAT
AccessioniPrimary (citable) accession number: P51145
Secondary accession number(s): Q6GXE4
Entry historyi
Integrated into UniProtKB/Swiss-Prot: October 1, 1996
Last sequence update: December 14, 2011
Last modified: May 11, 2016
This is version 105 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. SIMILARITY comments
    Index of protein domains and families

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 one 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.