FOSL2_HUMAN
ID FOSL2_HUMAN Reviewed; 326 AA.
AC P15408; B2RD58; B3KP27; B4DYV4; Q6FG46;
DT 01-APR-1990, integrated into UniProtKB/Swiss-Prot.
DT 01-APR-1990, sequence version 1.
DT 03-AUG-2022, entry version 191.
DE RecName: Full=Fos-related antigen 2;
DE Short=FRA-2;
GN Name=FOSL2; Synonyms=FRA2;
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 2).
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 [LARGE SCALE MRNA] (ISOFORMS 1 AND 3).
RC TISSUE=Lung, and Tongue;
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 [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=Retina;
RX PubMed=17974005; DOI=10.1186/1471-2164-8-399;
RA Bechtel S., Rosenfelder H., Duda A., Schmidt C.P., Ernst U.,
RA Wellenreuther R., Mehrle A., Schuster C., Bahr A., Bloecker H., Heubner D.,
RA Hoerlein A., Michel G., Wedler H., Koehrer K., Ottenwaelder B., Poustka A.,
RA Wiemann S., Schupp I.;
RT "The full-ORF clone resource of the German cDNA consortium.";
RL BMC Genomics 8:399-399(2007).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RA Halleck A., Ebert L., Mkoundinya M., Schick M., Eisenstein S., Neubert P.,
RA Kstrang K., Schatten R., Shen B., Henze S., Mar W., Korn B., Zuo D., Hu Y.,
RA LaBaer J.;
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=15815621; DOI=10.1038/nature03466;
RA Hillier L.W., Graves T.A., Fulton R.S., Fulton L.A., Pepin K.H., Minx P.,
RA Wagner-McPherson C., Layman D., Wylie K., Sekhon M., Becker M.C.,
RA Fewell G.A., Delehaunty K.D., Miner T.L., Nash W.E., Kremitzki C., Oddy L.,
RA Du H., Sun H., Bradshaw-Cordum H., Ali J., Carter J., Cordes M., Harris A.,
RA Isak A., van Brunt A., Nguyen C., Du F., Courtney L., Kalicki J.,
RA Ozersky P., Abbott S., Armstrong J., Belter E.A., Caruso L., Cedroni M.,
RA Cotton M., Davidson T., Desai A., Elliott G., Erb T., Fronick C., Gaige T.,
RA Haakenson W., Haglund K., Holmes A., Harkins R., Kim K., Kruchowski S.S.,
RA Strong C.M., Grewal N., Goyea E., Hou S., Levy A., Martinka S., Mead K.,
RA McLellan M.D., Meyer R., Randall-Maher J., Tomlinson C.,
RA Dauphin-Kohlberg S., Kozlowicz-Reilly A., Shah N., Swearengen-Shahid S.,
RA Snider J., Strong J.T., Thompson J., Yoakum M., Leonard S., Pearman C.,
RA Trani L., Radionenko M., Waligorski J.E., Wang C., Rock S.M.,
RA Tin-Wollam A.-M., Maupin R., Latreille P., Wendl M.C., Yang S.-P., Pohl C.,
RA Wallis J.W., Spieth J., Bieri T.A., Berkowicz N., Nelson J.O., Osborne J.,
RA Ding L., Meyer R., Sabo A., Shotland Y., Sinha P., Wohldmann P.E.,
RA Cook L.L., Hickenbotham M.T., Eldred J., Williams D., Jones T.A., She X.,
RA Ciccarelli F.D., Izaurralde E., Taylor J., Schmutz J., Myers R.M.,
RA Cox D.R., Huang X., McPherson J.D., Mardis E.R., Clifton S.W., Warren W.C.,
RA Chinwalla A.T., Eddy S.R., Marra M.A., Ovcharenko I., Furey T.S.,
RA Miller W., Eichler E.E., Bork P., Suyama M., Torrents D., Waterston R.H.,
RA Wilson R.K.;
RT "Generation and annotation of the DNA sequences of human chromosomes 2 and
RT 4.";
RL Nature 434:724-731(2005).
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 (SEP-2005) to the EMBL/GenBank/DDBJ databases.
RN [7]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=Lung;
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 PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-200, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=17081983; DOI=10.1016/j.cell.2006.09.026;
RA Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P., Mann M.;
RT "Global, in vivo, and site-specific phosphorylation dynamics in signaling
RT networks.";
RL Cell 127:635-648(2006).
RN [9]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-211 AND SER-230, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=18669648; DOI=10.1073/pnas.0805139105;
RA Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,
RA Elledge S.J., Gygi S.P.;
RT "A quantitative atlas of mitotic phosphorylation.";
RL Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008).
RN [10]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-120; SER-200; SER-211;
RP SER-230 AND SER-320, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE
RP 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).
RN [11]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-200, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=21406692; DOI=10.1126/scisignal.2001570;
RA Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J., Johansen P.T.,
RA Kratchmarova I., Kassem M., Mann M., Olsen J.V., Blagoev B.;
RT "System-wide temporal characterization of the proteome and phosphoproteome
RT of human embryonic stem cell differentiation.";
RL Sci. Signal. 4:RS3-RS3(2011).
RN [12]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT MET-1, AND IDENTIFICATION BY MASS
RP SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=22814378; DOI=10.1073/pnas.1210303109;
RA Van Damme P., Lasa M., Polevoda B., Gazquez C., Elosegui-Artola A.,
RA Kim D.S., De Juan-Pardo E., Demeyer K., Hole K., Larrea E., Timmerman E.,
RA Prieto J., Arnesen T., Sherman F., Gevaert K., Aldabe R.;
RT "N-terminal acetylome analyses and functional insights of the N-terminal
RT acetyltransferase NatB.";
RL Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012).
RN [13]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-120; SER-200; SER-230 AND
RP SER-308, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma, and Erythroleukemia;
RX PubMed=23186163; DOI=10.1021/pr300630k;
RA Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J.,
RA Mohammed S.;
RT "Toward a comprehensive characterization of a human cancer cell
RT phosphoproteome.";
RL J. Proteome Res. 12:260-271(2013).
RN [14]
RP SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-222, AND IDENTIFICATION BY MASS
RP SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=25218447; DOI=10.1038/nsmb.2890;
RA Hendriks I.A., D'Souza R.C., Yang B., Verlaan-de Vries M., Mann M.,
RA Vertegaal A.C.;
RT "Uncovering global SUMOylation signaling networks in a site-specific
RT manner.";
RL Nat. Struct. Mol. Biol. 21:927-936(2014).
RN [15]
RP SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-222, AND IDENTIFICATION BY MASS
RP SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=25114211; DOI=10.1073/pnas.1413825111;
RA Impens F., Radoshevich L., Cossart P., Ribet D.;
RT "Mapping of SUMO sites and analysis of SUMOylation changes induced by
RT external stimuli.";
RL Proc. Natl. Acad. Sci. U.S.A. 111:12432-12437(2014).
RN [16]
RP SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-222, AND IDENTIFICATION BY MASS
RP SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=25772364; DOI=10.1016/j.celrep.2015.02.033;
RA Hendriks I.A., Treffers L.W., Verlaan-de Vries M., Olsen J.V.,
RA Vertegaal A.C.;
RT "SUMO-2 orchestrates chromatin modifiers in response to DNA damage.";
RL Cell Rep. 10:1778-1791(2015).
RN [17]
RP SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-222, AND IDENTIFICATION BY MASS
RP SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=25755297; DOI=10.1074/mcp.o114.044792;
RA Xiao Z., Chang J.G., Hendriks I.A., Sigurdsson J.O., Olsen J.V.,
RA Vertegaal A.C.;
RT "System-wide analysis of SUMOylation dynamics in response to replication
RT stress reveals novel small ubiquitin-like modified target proteins and
RT acceptor lysines relevant for genome stability.";
RL Mol. Cell. Proteomics 14:1419-1434(2015).
RN [18]
RP SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-35; LYS-104; LYS-222 AND LYS-240,
RP AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=28112733; DOI=10.1038/nsmb.3366;
RA Hendriks I.A., Lyon D., Young C., Jensen L.J., Vertegaal A.C.,
RA Nielsen M.L.;
RT "Site-specific mapping of the human SUMO proteome reveals co-modification
RT with phosphorylation.";
RL Nat. Struct. Mol. Biol. 24:325-336(2017).
CC -!- FUNCTION: Controls osteoclast survival and size (By similarity). As a
CC dimer with JUN, activates LIF transcription (By similarity). Activates
CC CEBPB transcription in PGE2-activated osteoblasts (By similarity).
CC {ECO:0000250|UniProtKB:P47930, ECO:0000250|UniProtKB:P51145}.
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}.
CC -!- INTERACTION:
CC P15408; P15336: ATF2; NbExp=6; IntAct=EBI-3893419, EBI-1170906;
CC P15408; P17544: ATF7; NbExp=2; IntAct=EBI-3893419, EBI-765623;
CC P15408; Q9BYV9: BACH2; NbExp=4; IntAct=EBI-3893419, EBI-1642333;
CC P15408; Q02930-3: CREB5; NbExp=13; IntAct=EBI-3893419, EBI-10192698;
CC P15408; Q15438: CYTH1; NbExp=3; IntAct=EBI-3893419, EBI-997830;
CC P15408; P35638: DDIT3; NbExp=6; IntAct=EBI-3893419, EBI-742651;
CC P15408; P35638-2: DDIT3; NbExp=3; IntAct=EBI-3893419, EBI-10173632;
CC P15408; Q96EY1-2: DNAJA3; NbExp=3; IntAct=EBI-3893419, EBI-3952284;
CC P15408; P22607: FGFR3; NbExp=3; IntAct=EBI-3893419, EBI-348399;
CC P15408; Q13643: FHL3; NbExp=4; IntAct=EBI-3893419, EBI-741101;
CC P15408; Q53SE7: FLJ13057; NbExp=3; IntAct=EBI-3893419, EBI-10172181;
CC P15408; Q9HD26: GOPC; NbExp=4; IntAct=EBI-3893419, EBI-349832;
CC P15408; P06396: GSN; NbExp=3; IntAct=EBI-3893419, EBI-351506;
CC P15408; P01112: HRAS; NbExp=3; IntAct=EBI-3893419, EBI-350145;
CC P15408; P05412: JUN; NbExp=11; IntAct=EBI-3893419, EBI-852823;
CC P15408; P17275: JUNB; NbExp=8; IntAct=EBI-3893419, EBI-748062;
CC P15408; P17535: JUND; NbExp=4; IntAct=EBI-3893419, EBI-2682803;
CC P15408; Q68G74: LHX8; NbExp=3; IntAct=EBI-3893419, EBI-8474075;
CC P15408; Q5T3J3: LRIF1; NbExp=3; IntAct=EBI-3893419, EBI-473196;
CC P15408; Q9P127: LUZP4; NbExp=3; IntAct=EBI-3893419, EBI-10198848;
CC P15408; Q6FHY5: MEOX2; NbExp=3; IntAct=EBI-3893419, EBI-16439278;
CC P15408; Q16236: NFE2L2; NbExp=6; IntAct=EBI-3893419, EBI-2007911;
CC P15408; Q9Y5B8: NME7; NbExp=3; IntAct=EBI-3893419, EBI-744782;
CC P15408; P62487: POLR2G; NbExp=3; IntAct=EBI-3893419, EBI-347928;
CC P15408; Q13077: TRAF1; NbExp=5; IntAct=EBI-3893419, EBI-359224;
CC P15408; Q9UMX0: UBQLN1; NbExp=3; IntAct=EBI-3893419, EBI-741480;
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:P51145}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=3;
CC Name=1;
CC IsoId=P15408-1; Sequence=Displayed;
CC Name=2;
CC IsoId=P15408-2; Sequence=VSP_039127, VSP_039128, VSP_039129;
CC Name=3;
CC IsoId=P15408-3; Sequence=VSP_042083;
CC -!- SIMILARITY: Belongs to the bZIP family. Fos subfamily. {ECO:0000305}.
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DR EMBL; X16706; CAA34678.1; -; mRNA.
DR EMBL; AK055579; BAG51539.1; -; mRNA.
DR EMBL; AK302622; BAG63866.1; -; mRNA.
DR EMBL; AK315415; BAG37805.1; -; mRNA.
DR EMBL; BX647822; -; NOT_ANNOTATED_CDS; mRNA.
DR EMBL; CR542262; CAG47058.1; -; mRNA.
DR EMBL; AC104695; AAY14908.1; -; Genomic_DNA.
DR EMBL; CH471053; EAX00538.1; -; Genomic_DNA.
DR EMBL; CH471053; EAX00539.1; -; Genomic_DNA.
DR EMBL; BC022791; AAH22791.1; -; mRNA.
DR CCDS; CCDS1766.1; -. [P15408-1]
DR PIR; S15749; S15749.
DR RefSeq; NP_005244.1; NM_005253.3. [P15408-1]
DR RefSeq; XP_016859226.1; XM_017003737.1.
DR AlphaFoldDB; P15408; -.
DR SMR; P15408; -.
DR BioGRID; 108638; 78.
DR ComplexPortal; CPX-6418; bZIP transcription factor complex, ATF2-FOSL2.
DR ComplexPortal; CPX-6479; bZIP transcription factor complex, ATF3-FOSL2.
DR ComplexPortal; CPX-6785; bZIP transcription factor complex, ATF7-FOSL2.
DR DIP; DIP-48788N; -.
DR IntAct; P15408; 72.
DR MINT; P15408; -.
DR STRING; 9606.ENSP00000264716; -.
DR GlyGen; P15408; 7 sites, 2 O-linked glycans (7 sites).
DR iPTMnet; P15408; -.
DR PhosphoSitePlus; P15408; -.
DR BioMuta; FOSL2; -.
DR DMDM; 120487; -.
DR EPD; P15408; -.
DR jPOST; P15408; -.
DR MassIVE; P15408; -.
DR MaxQB; P15408; -.
DR PaxDb; P15408; -.
DR PeptideAtlas; P15408; -.
DR PRIDE; P15408; -.
DR ProteomicsDB; 53137; -. [P15408-1]
DR ProteomicsDB; 53138; -. [P15408-2]
DR ProteomicsDB; 53139; -. [P15408-3]
DR Antibodypedia; 1415; 592 antibodies from 36 providers.
DR DNASU; 2355; -.
DR Ensembl; ENST00000264716.9; ENSP00000264716.4; ENSG00000075426.12. [P15408-1]
DR Ensembl; ENST00000379619.5; ENSP00000368939.1; ENSG00000075426.12. [P15408-2]
DR GeneID; 2355; -.
DR KEGG; hsa:2355; -.
DR MANE-Select; ENST00000264716.9; ENSP00000264716.4; NM_005253.4; NP_005244.1.
DR UCSC; uc002rma.4; human. [P15408-1]
DR CTD; 2355; -.
DR DisGeNET; 2355; -.
DR GeneCards; FOSL2; -.
DR HGNC; HGNC:3798; FOSL2.
DR HPA; ENSG00000075426; Low tissue specificity.
DR MIM; 601575; gene.
DR neXtProt; NX_P15408; -.
DR OpenTargets; ENSG00000075426; -.
DR PharmGKB; PA28215; -.
DR VEuPathDB; HostDB:ENSG00000075426; -.
DR eggNOG; KOG1414; Eukaryota.
DR GeneTree; ENSGT00940000158876; -.
DR HOGENOM; CLU_049742_2_1_1; -.
DR InParanoid; P15408; -.
DR OMA; PNMLEPE; -.
DR OrthoDB; 1221590at2759; -.
DR PhylomeDB; P15408; -.
DR TreeFam; TF326301; -.
DR PathwayCommons; P15408; -.
DR SignaLink; P15408; -.
DR SIGNOR; P15408; -.
DR BioGRID-ORCS; 2355; 40 hits in 1098 CRISPR screens.
DR ChiTaRS; FOSL2; human.
DR GeneWiki; FOSL2; -.
DR GenomeRNAi; 2355; -.
DR Pharos; P15408; Tbio.
DR PRO; PR:P15408; -.
DR Proteomes; UP000005640; Chromosome 2.
DR RNAct; P15408; protein.
DR Bgee; ENSG00000075426; Expressed in left adrenal gland cortex and 187 other tissues.
DR ExpressionAtlas; P15408; baseline and differential.
DR Genevisible; P15408; HS.
DR GO; GO:0000785; C:chromatin; ISA:NTNU_SB.
DR GO; GO:0005654; C:nucleoplasm; IDA:HPA.
DR GO; GO:0005634; C:nucleus; IBA:GO_Central.
DR GO; GO:0090575; C:RNA polymerase II transcription regulator complex; IPI:ComplexPortal.
DR GO; GO:0003682; F:chromatin binding; IEA:Ensembl.
DR GO; GO:0001228; F:DNA-binding transcription activator activity, RNA polymerase II-specific; IDA:NTNU_SB.
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; IBA:GO_Central.
DR GO; GO:0000977; F:RNA polymerase II transcription regulatory region sequence-specific DNA binding; IDA:NTNU_SB.
DR GO; GO:0008219; P:cell death; TAS:ProtInc.
DR GO; GO:0003334; P:keratinocyte development; IEA:Ensembl.
DR GO; GO:0048146; P:positive regulation of fibroblast proliferation; IEA:Ensembl.
DR GO; GO:0045944; P:positive regulation of transcription by RNA polymerase II; IDA:NTNU_SB.
DR GO; GO:0006357; P:regulation of transcription by RNA polymerase II; IBA:GO_Central.
DR InterPro; IPR000837; AP-1.
DR InterPro; IPR004827; bZIP.
DR InterPro; IPR046347; bZIP_sf.
DR InterPro; IPR029814; Fra2.
DR PANTHER; PTHR23351; PTHR23351; 1.
DR PANTHER; PTHR23351:SF25; PTHR23351:SF25; 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 Acetylation; Alternative splicing; DNA-binding; Isopeptide bond; Nucleus;
KW Phosphoprotein; Reference proteome; Transcription;
KW Transcription regulation; Ubl conjugation.
FT CHAIN 1..326
FT /note="Fos-related antigen 2"
FT /id="PRO_0000076483"
FT DOMAIN 124..187
FT /note="bZIP"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00978"
FT REGION 1..39
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 110..131
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 126..128
FT /note="Basic motif"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00978"
FT REGION 129..136
FT /note="Leucine-zipper"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00978"
FT REGION 193..242
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 289..326
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..32
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 1
FT /note="N-acetylmethionine"
FT /evidence="ECO:0007744|PubMed:22814378"
FT MOD_RES 104
FT /note="N6-acetyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:P47930"
FT MOD_RES 120
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:20068231,
FT ECO:0007744|PubMed:23186163"
FT MOD_RES 200
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17081983,
FT ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:21406692,
FT ECO:0007744|PubMed:23186163"
FT MOD_RES 211
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648,
FT ECO:0007744|PubMed:20068231"
FT MOD_RES 230
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648,
FT ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:23186163"
FT MOD_RES 308
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 320
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:20068231"
FT CROSSLNK 35
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:28112733"
FT CROSSLNK 104
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2); alternate"
FT /evidence="ECO:0007744|PubMed:28112733"
FT CROSSLNK 222
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO1); alternate"
FT /evidence="ECO:0007744|PubMed:25114211"
FT CROSSLNK 222
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2); alternate"
FT /evidence="ECO:0007744|PubMed:25114211,
FT ECO:0007744|PubMed:25218447, ECO:0007744|PubMed:25755297,
FT ECO:0007744|PubMed:25772364, ECO:0007744|PubMed:28112733"
FT CROSSLNK 240
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:28112733"
FT VAR_SEQ 1..39
FT /note="Missing (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_042083"
FT VAR_SEQ 1..25
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:2107490"
FT /id="VSP_039127"
FT VAR_SEQ 26..34
FT /note="YSSGGGGQQ -> MVQGWRIKS (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:2107490"
FT /id="VSP_039128"
FT VAR_SEQ 154
FT /note="A -> AIGPWQVAVPHIPLFPWQ (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:2107490"
FT /id="VSP_039129"
FT CONFLICT 89
FT /note="A -> V (in Ref. 3; BX647822)"
FT /evidence="ECO:0000305"
FT CONFLICT 111
FT /note="G -> D (in Ref. 2; BAG51539)"
FT /evidence="ECO:0000305"
FT CONFLICT 298
FT /note="E -> G (in Ref. 2; BAG37805)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 326 AA; 35193 MW; F61738BE23C5026F CRC64;
MYQDYPGNFD TSSRGSSGSP AHAESYSSGG GGQQKFRVDM PGSGSAFIPT INAITTSQDL
QWMVQPTVIT SMSNPYPRSH PYSPLPGLAS VPGHMALPRP GVIKTIGTTV GRRRRDEQLS
PEEEEKRRIR RERNKLAAAK CRNRRRELTE KLQAETEELE EEKSGLQKEI AELQKEKEKL
EFMLVAHGPV CKISPEERRS PPAPGLQPMR SGGGSVGAVV VKQEPLEEDS PSSSSAGLDK
AQRSVIKPIS IAGGFYGEEP LHTPIVVTST PAVTPGTSNL VFTYPSVLEQ ESPASPSESC
SKAHRRSSSS GDQSSDSLNS PTLLAL
