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Protein

Fos-related antigen 2

Gene

FOSL2

Organism
Homo sapiens (Human)
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

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:FRA2
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640 Componenti: Chromosome 2

Organism-specific databases

HGNCiHGNC:3798. FOSL2.

Subcellular locationi

GO - Cellular componenti

  • nucleoplasm Source: HPA
  • nucleus Source: ProtInc
Complete GO annotation...

Keywords - Cellular componenti

Nucleus

Pathology & Biotechi

Organism-specific databases

PharmGKBiPA28215.

Polymorphism and mutation databases

BioMutaiFOSL2.
DMDMi120487.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 326326Fos-related antigen 2PRO_0000076483Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei1 – 11N-acetylmethionine1 Publication
Modified residuei104 – 1041N6-acetyllysineBy similarity
Modified residuei120 – 1201Phosphoserine1 Publication
Modified residuei200 – 2001Phosphoserine3 Publications
Modified residuei211 – 2111Phosphoserine2 Publications
Modified residuei230 – 2301Phosphoserine2 Publications
Modified residuei320 – 3201Phosphoserine1 Publication

Keywords - PTMi

Acetylation, Phosphoprotein

Proteomic databases

MaxQBiP15408.
PaxDbiP15408.
PRIDEiP15408.

PTM databases

PhosphoSiteiP15408.

Expressioni

Gene expression databases

BgeeiP15408.
CleanExiHS_FOSL2.
ExpressionAtlasiP15408. baseline and differential.
GenevisibleiP15408. HS.

Organism-specific databases

HPAiCAB013460.
HPA004817.
HPA061417.

Interactioni

Subunit structurei

Heterodimer.By similarity

Binary interactionsi

WithEntry#Exp.IntActNotes
CREB5Q02930-35EBI-3893419,EBI-10192698
DDIT3P35638-23EBI-3893419,EBI-10173632
DNAJA3Q96EY1-23EBI-3893419,EBI-3952284
FHL3Q136433EBI-3893419,EBI-741101
FLJ13057Q53SE73EBI-3893419,EBI-10172181
GOPCQ9HD263EBI-3893419,EBI-349832
LUZP4Q9P1273EBI-3893419,EBI-10198848
TRAF1Q130773EBI-3893419,EBI-359224

Protein-protein interaction databases

BioGridi108638. 43 interactions.
DIPiDIP-48788N.
IntActiP15408. 9 interactions.
STRINGi9606.ENSP00000264716.

Structurei

3D structure databases

ProteinModelPortaliP15408.
SMRiP15408. 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.
InParanoidiP15408.
KOiK09030.
OMAiLVFTYPN.
OrthoDBiEOG761BVN.
PhylomeDBiP15408.
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 (3)i

Sequence statusi: Complete.

This entry describes 3 isoformsi produced by alternative splicing. AlignAdd to basket

Isoform 1 (identifier: P15408-1) [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
PPAPGLQPMR SGGGSVGAVV VKQEPLEEDS PSSSSAGLDK AQRSVIKPIS
260 270 280 290 300
IAGGFYGEEP LHTPIVVTST PAVTPGTSNL VFTYPSVLEQ ESPASPSESC
310 320
SKAHRRSSSS GDQSSDSLNS PTLLAL
Length:326
Mass (Da):35,193
Last modified:April 1, 1990 - v1
Checksum:iF61738BE23C5026F
GO
Isoform 2 (identifier: P15408-2) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     1-25: Missing.
     26-34: YSSGGGGQQ → MVQGWRIKS
     154-154: A → AIGPWQVAVPHIPLFPWQ

Note: No experimental confirmation available.
Show »
Length:318
Mass (Da):34,795
Checksum:iC17D7E59D9DABCB4
GO
Isoform 3 (identifier: P15408-3) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     1-39: Missing.

Note: No experimental confirmation available.
Show »
Length:287
Mass (Da):31,095
Checksum:iF198987B0A81B778
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti89 – 891A → V in BX647822 (PubMed:17974005).Curated
Sequence conflicti111 – 1111G → D in BAG51539 (PubMed:14702039).Curated
Sequence conflicti298 – 2981E → G in BAG37805 (PubMed:14702039).Curated

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei1 – 3939Missing in isoform 3. 1 PublicationVSP_042083Add
BLAST
Alternative sequencei1 – 2525Missing in isoform 2. 1 PublicationVSP_039127Add
BLAST
Alternative sequencei26 – 349YSSGGGGQQ → MVQGWRIKS in isoform 2. 1 PublicationVSP_039128
Alternative sequencei154 – 1541A → AIGPWQVAVPHIPLFPWQ in isoform 2. 1 PublicationVSP_039129

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X16706 mRNA. Translation: CAA34678.1.
AK055579 mRNA. Translation: BAG51539.1.
AK302622 mRNA. Translation: BAG63866.1.
AK315415 mRNA. Translation: BAG37805.1.
BX647822 mRNA. No translation available.
CR542262 mRNA. Translation: CAG47058.1.
AC104695 Genomic DNA. Translation: AAY14908.1.
CH471053 Genomic DNA. Translation: EAX00538.1.
CH471053 Genomic DNA. Translation: EAX00539.1.
BC022791 mRNA. Translation: AAH22791.1.
CCDSiCCDS1766.1. [P15408-1]
PIRiS15749.
RefSeqiNP_005244.1. NM_005253.3. [P15408-1]
UniGeneiHs.220971.
Hs.596972.

Genome annotation databases

EnsembliENST00000264716; ENSP00000264716; ENSG00000075426.
ENST00000379619; ENSP00000368939; ENSG00000075426. [P15408-2]
GeneIDi2355.
KEGGihsa:2355.
UCSCiuc002rma.3. human. [P15408-1]
uc021vfg.1. human. [P15408-2]

Keywords - Coding sequence diversityi

Alternative splicing

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X16706 mRNA. Translation: CAA34678.1.
AK055579 mRNA. Translation: BAG51539.1.
AK302622 mRNA. Translation: BAG63866.1.
AK315415 mRNA. Translation: BAG37805.1.
BX647822 mRNA. No translation available.
CR542262 mRNA. Translation: CAG47058.1.
AC104695 Genomic DNA. Translation: AAY14908.1.
CH471053 Genomic DNA. Translation: EAX00538.1.
CH471053 Genomic DNA. Translation: EAX00539.1.
BC022791 mRNA. Translation: AAH22791.1.
CCDSiCCDS1766.1. [P15408-1]
PIRiS15749.
RefSeqiNP_005244.1. NM_005253.3. [P15408-1]
UniGeneiHs.220971.
Hs.596972.

3D structure databases

ProteinModelPortaliP15408.
SMRiP15408. Positions 125-187.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi108638. 43 interactions.
DIPiDIP-48788N.
IntActiP15408. 9 interactions.
STRINGi9606.ENSP00000264716.

PTM databases

PhosphoSiteiP15408.

Polymorphism and mutation databases

BioMutaiFOSL2.
DMDMi120487.

Proteomic databases

MaxQBiP15408.
PaxDbiP15408.
PRIDEiP15408.

Protocols and materials databases

DNASUi2355.
Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000264716; ENSP00000264716; ENSG00000075426.
ENST00000379619; ENSP00000368939; ENSG00000075426. [P15408-2]
GeneIDi2355.
KEGGihsa:2355.
UCSCiuc002rma.3. human. [P15408-1]
uc021vfg.1. human. [P15408-2]

Organism-specific databases

CTDi2355.
GeneCardsiGC02P028615.
HGNCiHGNC:3798. FOSL2.
HPAiCAB013460.
HPA004817.
HPA061417.
MIMi601575. gene.
neXtProtiNX_P15408.
PharmGKBiPA28215.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiNOG301361.
GeneTreeiENSGT00730000110541.
HOGENOMiHOG000234334.
HOVERGENiHBG005743.
InParanoidiP15408.
KOiK09030.
OMAiLVFTYPN.
OrthoDBiEOG761BVN.
PhylomeDBiP15408.
TreeFamiTF326301.

Miscellaneous databases

ChiTaRSiFOSL2. human.
GeneWikiiFOSL2.
GenomeRNAii2355.
NextBioi9551.
PROiP15408.
SOURCEiSearch...

Gene expression databases

BgeeiP15408.
CleanExiHS_FOSL2.
ExpressionAtlasiP15408. baseline and differential.
GenevisibleiP15408. HS.

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. "Isolation of human fos-related genes and their expression during monocyte-macrophage differentiation."
    Matsui M., Tokuhara M., Konuma Y., Nomura N., Ishizaki R.
    Oncogene 5:249-255(1990) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2).
    Tissue: Endothelial cell.
  2. "Complete sequencing and characterization of 21,243 full-length human cDNAs."
    Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.
    , Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.
    Nat. Genet. 36:40-45(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 3).
    Tissue: Lung and Tongue.
  3. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
    Tissue: Retina.
  4. "Cloning of human full open reading frames in Gateway(TM) system entry vector (pDONR201)."
    Halleck A., Ebert L., Mkoundinya M., Schick M., Eisenstein S., Neubert P., Kstrang K., Schatten R., Shen B., Henze S., Mar W., Korn B., Zuo D., Hu Y., LaBaer J.
    Submitted (JUN-2004) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
  5. "Generation and annotation of the DNA sequences of human chromosomes 2 and 4."
    Hillier L.W., Graves T.A., Fulton R.S., Fulton L.A., Pepin K.H., Minx P., Wagner-McPherson C., Layman D., Wylie K., Sekhon M., Becker M.C., Fewell G.A., Delehaunty K.D., Miner T.L., Nash W.E., Kremitzki C., Oddy L., Du H.
    , Sun H., Bradshaw-Cordum H., Ali J., Carter J., Cordes M., Harris A., Isak A., van Brunt A., Nguyen C., Du F., Courtney L., Kalicki J., Ozersky P., Abbott S., Armstrong J., Belter E.A., Caruso L., Cedroni M., Cotton M., Davidson T., Desai A., Elliott G., Erb T., Fronick C., Gaige T., Haakenson W., Haglund K., Holmes A., Harkins R., Kim K., Kruchowski S.S., Strong C.M., Grewal N., Goyea E., Hou S., Levy A., Martinka S., Mead K., McLellan M.D., Meyer R., Randall-Maher J., Tomlinson C., Dauphin-Kohlberg S., Kozlowicz-Reilly A., Shah N., Swearengen-Shahid S., Snider J., Strong J.T., Thompson J., Yoakum M., Leonard S., Pearman C., Trani L., Radionenko M., Waligorski J.E., Wang C., Rock S.M., Tin-Wollam A.-M., Maupin R., Latreille P., Wendl M.C., Yang S.-P., Pohl C., Wallis J.W., Spieth J., Bieri T.A., Berkowicz N., Nelson J.O., Osborne J., Ding L., Meyer R., Sabo A., Shotland Y., Sinha P., Wohldmann P.E., Cook L.L., Hickenbotham M.T., Eldred J., Williams D., Jones T.A., She X., Ciccarelli F.D., Izaurralde E., Taylor J., Schmutz J., Myers R.M., Cox D.R., Huang X., McPherson J.D., Mardis E.R., Clifton S.W., Warren W.C., Chinwalla A.T., Eddy S.R., Marra M.A., Ovcharenko I., Furey T.S., Miller W., Eichler E.E., Bork P., Suyama M., Torrents D., Waterston R.H., Wilson R.K.
    Nature 434:724-731(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  6. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  7. "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).
    Tissue: Lung.
  8. "Global, in vivo, and site-specific phosphorylation dynamics in signaling networks."
    Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P., Mann M.
    Cell 127:635-648(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-200, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  9. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-211 AND SER-230, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  10. "Quantitative phosphoproteomics reveals widespread full phosphorylation site occupancy during mitosis."
    Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L., Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S., Mann M.
    Sci. Signal. 3:RA3-RA3(2010) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-120; SER-200; SER-211; SER-230 AND SER-320, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  11. "System-wide temporal characterization of the proteome and phosphoproteome of human embryonic stem cell differentiation."
    Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J., Johansen P.T., Kratchmarova I., Kassem M., Mann M., Olsen J.V., Blagoev B.
    Sci. Signal. 4:RS3-RS3(2011) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-200, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  12. Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT MET-1, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].

Entry informationi

Entry nameiFOSL2_HUMAN
AccessioniPrimary (citable) accession number: P15408
Secondary accession number(s): B2RD58
, B3KP27, B4DYV4, Q6FG46
Entry historyi
Integrated into UniProtKB/Swiss-Prot: April 1, 1990
Last sequence update: April 1, 1990
Last modified: July 22, 2015
This is version 141 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. Human chromosome 2
    Human chromosome 2: entries, gene names and cross-references to MIM
  2. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  3. 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.