FOSL1_HUMAN
ID FOSL1_HUMAN Reviewed; 271 AA.
AC P15407; B4DR11; Q6FG51;
DT 01-APR-1990, integrated into UniProtKB/Swiss-Prot.
DT 01-APR-1990, sequence version 1.
DT 03-AUG-2022, entry version 193.
DE RecName: Full=Fos-related antigen 1;
DE Short=FRA-1;
GN Name=FOSL1; Synonyms=FRA1;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
RC TISSUE=Endothelial cell;
RX PubMed=2107490;
RA Matsui M., Tokuhara M., Konuma Y., Nomura N., Ishizaki R.;
RT "Isolation of human fos-related genes and their expression during monocyte-
RT macrophage differentiation.";
RL Oncogene 5:249-255(1990).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC TISSUE=Blood;
RA Albagha O.M.E., Ralston S.H.;
RT "Intron/exon structure of the human fos related antigen, identification of
RT a novel pseudogene.";
RL Submitted (JUL-2000) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RX PubMed=14702039; DOI=10.1038/ng1285;
RA Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
RA Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
RA Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
RA Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
RA Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H.,
RA Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M.,
RA Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K.,
RA Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T.,
RA Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M.,
RA Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S.,
RA Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H.,
RA Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K.,
RA Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N.,
RA Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
RA Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
RA Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
RA Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
RA Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y.,
RA Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K.,
RA Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T.,
RA Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T.,
RA Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y.,
RA Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H.,
RA Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y.,
RA Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H.,
RA Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O.,
RA Isogai T., Sugano S.;
RT "Complete sequencing and characterization of 21,243 full-length human
RT cDNAs.";
RL Nat. Genet. 36:40-45(2004).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RA Ebert L., Schick M., Neubert P., Schatten R., Henze S., Korn B.;
RT "Cloning of human full open reading frames in Gateway(TM) system entry
RT vector (pDONR201).";
RL Submitted (JUN-2004) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=16554811; DOI=10.1038/nature04632;
RA Taylor T.D., Noguchi H., Totoki Y., Toyoda A., Kuroki Y., Dewar K.,
RA Lloyd C., Itoh T., Takeda T., Kim D.-W., She X., Barlow K.F., Bloom T.,
RA Bruford E., Chang J.L., Cuomo C.A., Eichler E., FitzGerald M.G.,
RA Jaffe D.B., LaButti K., Nicol R., Park H.-S., Seaman C., Sougnez C.,
RA Yang X., Zimmer A.R., Zody M.C., Birren B.W., Nusbaum C., Fujiyama A.,
RA Hattori M., Rogers J., Lander E.S., Sakaki Y.;
RT "Human chromosome 11 DNA sequence and analysis including novel gene
RT identification.";
RL Nature 440:497-500(2006).
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M.,
RA Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J.,
RA Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S.,
RA Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H.,
RA Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K.,
RA Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D.,
RA Hunkapiller M.W., Myers E.W., Venter J.C.;
RL Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN [7]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=Skin;
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 [8]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-5.
RX PubMed=8230424; DOI=10.1128/jvi.67.12.7001-7007.1993;
RA Tsuchiya H., Fujii M., Niki T., Tokuhara M., Matsui M., Seiki M.;
RT "Human T-cell leukemia virus type 1 Tax activates transcription of the
RT human fra-1 gene through multiple cis elements responsive to transmembrane
RT signals.";
RL J. Virol. 67:7001-7007(1993).
RN [9]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-265, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=20068231; DOI=10.1126/scisignal.2000475;
RA Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L.,
RA Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S., Mann M.;
RT "Quantitative phosphoproteomics reveals widespread full phosphorylation
RT site occupancy during mitosis.";
RL Sci. Signal. 3:RA3-RA3(2010).
CC -!- SUBUNIT: Heterodimer (By similarity). Interacts with the BAF
CC multiprotein chromatin-remodeling complex subunits SMARCB1 and SMARCD1
CC (By similarity). Interacts with ARID1A and JUN (By similarity).
CC {ECO:0000250|UniProtKB:P47930, ECO:0000250|UniProtKB:P48755}.
CC -!- INTERACTION:
CC P15407; P18848: ATF4; NbExp=2; IntAct=EBI-744510, EBI-492498;
CC P15407; Q9NR55: BATF3; NbExp=3; IntAct=EBI-744510, EBI-10312707;
CC P15407; Q96HB5: CCDC120; NbExp=3; IntAct=EBI-744510, EBI-744556;
CC P15407; P28329-3: CHAT; NbExp=3; IntAct=EBI-744510, EBI-25837549;
CC P15407; Q02930-3: CREB5; NbExp=6; IntAct=EBI-744510, EBI-10192698;
CC P15407; P22607: FGFR3; NbExp=3; IntAct=EBI-744510, EBI-348399;
CC P15407; Q0VDC6: FKBP1A; NbExp=3; IntAct=EBI-744510, EBI-10226858;
CC P15407; Q96CN9: GCC1; NbExp=3; IntAct=EBI-744510, EBI-746252;
CC P15407; Q14957: GRIN2C; NbExp=3; IntAct=EBI-744510, EBI-8285963;
CC P15407; P06396: GSN; NbExp=3; IntAct=EBI-744510, EBI-351506;
CC P15407; P01112: HRAS; NbExp=3; IntAct=EBI-744510, EBI-350145;
CC P15407; P54652: HSPA2; NbExp=3; IntAct=EBI-744510, EBI-356991;
CC P15407; P05412: JUN; NbExp=10; IntAct=EBI-744510, EBI-852823;
CC P15407; P17275: JUNB; NbExp=9; IntAct=EBI-744510, EBI-748062;
CC P15407; O60333-2: KIF1B; NbExp=3; IntAct=EBI-744510, EBI-10975473;
CC P15407; Q9BVG8-5: KIFC3; NbExp=3; IntAct=EBI-744510, EBI-14069005;
CC P15407; O95751: LDOC1; NbExp=3; IntAct=EBI-744510, EBI-740738;
CC P15407; Q9Y5B8: NME7; NbExp=9; IntAct=EBI-744510, EBI-744782;
CC P15407; Q13526: PIN1; NbExp=3; IntAct=EBI-744510, EBI-714158;
CC P15407; Q9Y3C5: RNF11; NbExp=3; IntAct=EBI-744510, EBI-396669;
CC P15407; Q9NYJ8: TAB2; NbExp=4; IntAct=EBI-744510, EBI-358708;
CC P15407; P22415: USF1; NbExp=6; IntAct=EBI-744510, EBI-1054489;
CC P15407; O76024: WFS1; NbExp=3; IntAct=EBI-744510, EBI-720609;
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:P51145}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=P15407-1; Sequence=Displayed;
CC Name=2;
CC IsoId=P15407-2; Sequence=VSP_055566;
CC -!- SIMILARITY: Belongs to the bZIP family. Fos subfamily. {ECO:0000305}.
CC -!- WEB RESOURCE: Name=Atlas of Genetics and Cytogenetics in Oncology and
CC Haematology;
CC URL="http://atlasgeneticsoncology.org/Genes/FOSL1ID40622ch11q13.html";
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DR EMBL; X16707; CAA34679.1; -; mRNA.
DR EMBL; AJ297411; CAC50237.1; -; Genomic_DNA.
DR EMBL; AJ297412; CAC50237.1; JOINED; Genomic_DNA.
DR EMBL; AJ297413; CAC50237.1; JOINED; Genomic_DNA.
DR EMBL; AK299050; BAG61123.1; -; mRNA.
DR EMBL; CR542257; CAG47053.1; -; mRNA.
DR EMBL; CR542278; CAG47074.1; -; mRNA.
DR EMBL; AP006287; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH471076; EAW74469.1; -; Genomic_DNA.
DR EMBL; BC016648; AAH16648.1; -; mRNA.
DR CCDS; CCDS76436.1; -. [P15407-2]
DR CCDS; CCDS8121.1; -. [P15407-1]
DR PIR; S15750; S15750.
DR RefSeq; NP_001287773.1; NM_001300844.1.
DR RefSeq; NP_001287784.1; NM_001300855.1.
DR RefSeq; NP_001287785.1; NM_001300856.1.
DR RefSeq; NP_001287786.1; NM_001300857.1. [P15407-2]
DR RefSeq; NP_005429.1; NM_005438.4. [P15407-1]
DR AlphaFoldDB; P15407; -.
DR SMR; P15407; -.
DR BioGRID; 113742; 68.
DR ComplexPortal; CPX-6417; bZIP transcription factor complex, ATF2-FOSL1.
DR ComplexPortal; CPX-6478; bZIP transcription factor complex, ATF3-FOSL1.
DR ComplexPortal; CPX-6565; bZIP transcription factor complex, ATF4-FOSL1.
DR DIP; DIP-660N; -.
DR IntAct; P15407; 39.
DR MINT; P15407; -.
DR STRING; 9606.ENSP00000310170; -.
DR iPTMnet; P15407; -.
DR PhosphoSitePlus; P15407; -.
DR BioMuta; FOSL1; -.
DR EPD; P15407; -.
DR jPOST; P15407; -.
DR MassIVE; P15407; -.
DR MaxQB; P15407; -.
DR PaxDb; P15407; -.
DR PeptideAtlas; P15407; -.
DR PRIDE; P15407; -.
DR ProteomicsDB; 4915; -.
DR ProteomicsDB; 53136; -. [P15407-1]
DR Antibodypedia; 3828; 419 antibodies from 40 providers.
DR DNASU; 8061; -.
DR Ensembl; ENST00000312562.7; ENSP00000310170.2; ENSG00000175592.9. [P15407-1]
DR Ensembl; ENST00000448083.6; ENSP00000393302.2; ENSG00000175592.9. [P15407-2]
DR GeneID; 8061; -.
DR KEGG; hsa:8061; -.
DR MANE-Select; ENST00000312562.7; ENSP00000310170.2; NM_005438.5; NP_005429.1.
DR UCSC; uc001ogg.2; human. [P15407-1]
DR CTD; 8061; -.
DR DisGeNET; 8061; -.
DR GeneCards; FOSL1; -.
DR HGNC; HGNC:13718; FOSL1.
DR HPA; ENSG00000175592; Tissue enhanced (esophagus, urinary bladder).
DR MIM; 136515; gene.
DR neXtProt; NX_P15407; -.
DR OpenTargets; ENSG00000175592; -.
DR PharmGKB; PA28214; -.
DR VEuPathDB; HostDB:ENSG00000175592; -.
DR eggNOG; KOG1414; Eukaryota.
DR GeneTree; ENSGT00940000160034; -.
DR HOGENOM; CLU_131869_0_0_1; -.
DR InParanoid; P15407; -.
DR OMA; LEPADSC; -.
DR PhylomeDB; P15407; -.
DR TreeFam; TF326301; -.
DR PathwayCommons; P15407; -.
DR Reactome; R-HSA-9031628; NGF-stimulated transcription.
DR SignaLink; P15407; -.
DR SIGNOR; P15407; -.
DR BioGRID-ORCS; 8061; 178 hits in 1120 CRISPR screens.
DR ChiTaRS; FOSL1; human.
DR GeneWiki; FOSL1; -.
DR GenomeRNAi; 8061; -.
DR Pharos; P15407; Tbio.
DR PRO; PR:P15407; -.
DR Proteomes; UP000005640; Chromosome 11.
DR RNAct; P15407; protein.
DR Bgee; ENSG00000175592; Expressed in cartilage tissue and 122 other tissues.
DR ExpressionAtlas; P15407; baseline and differential.
DR Genevisible; P15407; HS.
DR GO; GO:0000785; C:chromatin; ISA:NTNU_SB.
DR GO; GO:0005829; C:cytosol; IEA:Ensembl.
DR GO; GO:0043005; C:neuron projection; IEA:Ensembl.
DR GO; GO:0005654; C:nucleoplasm; IDA:HPA.
DR GO; GO:0005634; C:nucleus; IBA:GO_Central.
DR GO; GO:0042734; C:presynaptic membrane; IEA:Ensembl.
DR GO; GO:0090575; C:RNA polymerase II transcription regulator complex; IPI:ComplexPortal.
DR GO; GO:0001228; F:DNA-binding transcription activator activity, RNA polymerase II-specific; IEA:Ensembl.
DR GO; GO:0003700; F:DNA-binding transcription factor activity; TAS:ProtInc.
DR GO; GO:0000981; F:DNA-binding transcription factor activity, RNA polymerase II-specific; ISA:NTNU_SB.
DR GO; GO:0000978; F:RNA polymerase II cis-regulatory region sequence-specific DNA binding; IDA:BHF-UCL.
DR GO; GO:1990837; F:sequence-specific double-stranded DNA binding; IDA:ARUK-UCL.
DR GO; GO:0006968; P:cellular defense response; TAS:ProtInc.
DR GO; GO:0031668; P:cellular response to extracellular stimulus; IEA:Ensembl.
DR GO; GO:0006935; P:chemotaxis; TAS:ProtInc.
DR GO; GO:0007565; P:female pregnancy; IEA:Ensembl.
DR GO; GO:0001701; P:in utero embryonic development; IEA:Ensembl.
DR GO; GO:0140467; P:integrated stress response signaling; IC:ComplexPortal.
DR GO; GO:0007612; P:learning; IEA:Ensembl.
DR GO; GO:0008285; P:negative regulation of cell population proliferation; IEA:Ensembl.
DR GO; GO:0060674; P:placenta blood vessel development; IEA:Ensembl.
DR GO; GO:0043065; P:positive regulation of apoptotic process; IEA:Ensembl.
DR GO; GO:0045787; P:positive regulation of cell cycle; IEA:Ensembl.
DR GO; GO:0008284; P:positive regulation of cell population proliferation; TAS:ProtInc.
DR GO; GO:0051091; P:positive regulation of DNA-binding transcription factor activity; IEA:Ensembl.
DR GO; GO:2000144; P:positive regulation of DNA-templated transcription, initiation; IDA:CACAO.
DR GO; GO:1902895; P:positive regulation of miRNA transcription; IDA:BHF-UCL.
DR GO; GO:0006357; P:regulation of transcription by RNA polymerase II; IBA:GO_Central.
DR GO; GO:0051591; P:response to cAMP; IEA:Ensembl.
DR GO; GO:0051412; P:response to corticosterone; IEA:Ensembl.
DR GO; GO:0034097; P:response to cytokine; IEA:Ensembl.
DR GO; GO:0009629; P:response to gravity; IEA:Ensembl.
DR GO; GO:0042542; P:response to hydrogen peroxide; IEA:Ensembl.
DR GO; GO:0009612; P:response to mechanical stimulus; IEA:Ensembl.
DR GO; GO:0032570; P:response to progesterone; IEA:Ensembl.
DR GO; GO:0009615; P:response to virus; TAS:ProtInc.
DR GO; GO:0009410; P:response to xenobiotic stimulus; IEA:Ensembl.
DR GO; GO:0007296; P:vitellogenesis; IEA:Ensembl.
DR InterPro; IPR000837; AP-1.
DR InterPro; IPR004827; bZIP.
DR InterPro; IPR046347; bZIP_sf.
DR InterPro; IPR029815; Fra1.
DR PANTHER; PTHR23351; PTHR23351; 1.
DR PANTHER; PTHR23351:SF6; PTHR23351:SF6; 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 Alternative splicing; DNA-binding; Nucleus; Phosphoprotein;
KW Reference proteome.
FT CHAIN 1..271
FT /note="Fos-related antigen 1"
FT /id="PRO_0000076479"
FT DOMAIN 105..168
FT /note="bZIP"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00978"
FT REGION 1..34
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 68..112
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 107..127
FT /note="Basic motif"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00978"
FT REGION 133..161
FT /note="Leucine-zipper"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00978"
FT REGION 173..202
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 237..271
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 68..85
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 97..112
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 237..262
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 265
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:20068231"
FT VAR_SEQ 34..135
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_055566"
SQ SEQUENCE 271 AA; 29413 MW; 1B6492D709E66570 CRC64;
MFRDFGEPGP SSGNGGGYGG PAQPPAAAQA AQQKFHLVPS INTMSGSQEL QWMVQPHFLG
PSSYPRPLTY PQYSPPQPRP GVIRALGPPP GVRRRPCEQI SPEEEERRRV RRERNKLAAA
KCRNRRKELT DFLQAETDKL EDEKSGLQRE IEELQKQKER LELVLEAHRP ICKIPEGAKE
GDTGSTSGTS SPPAPCRPVP CISLSPGPVL EPEALHTPTL MTTPSLTPFT PSLVFTYPST
PEPCASAHRK SSSSSGDPSS DPLGSPTLLA L
