ID FOXJ2_HUMAN Reviewed; 574 AA. AC Q9P0K8; A0AVK4; B2RMP3; Q96PS9; Q9NSN5; DT 27-APR-2001, integrated into UniProtKB/Swiss-Prot. DT 01-OCT-2000, sequence version 1. DT 27-MAR-2024, entry version 197. DE RecName: Full=Forkhead box protein J2; DE AltName: Full=Fork head homologous X; GN Name=FOXJ2; Synonyms=FHX; 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 FOXJ2.L), AND FUNCTION (ISOFORM RP FOXJ2.L). RX PubMed=10777590; DOI=10.1074/jbc.275.17.12909; RA Perez-Sanchez C., Gomez-Ferreria M.A., de la Fuente C.A., Granadino B., RA Velasco G., Esteban A., Rey-Campos J.; RT "FHX, a novel fork head factor with a dual DNA binding specificity."; RL J. Biol. Chem. 275:12909-12916(2000). RN [2] RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM FOXJ2.S), AND FUNCTION (ISOFORMS RP FOXJ2.L AND FOXJ2.S). RX PubMed=10966786; DOI=10.1006/jmbi.2000.3999; RA Perez-Sanchez C., de la Fuente C.A., Gomez-Ferreria M.A., Granadino B., RA Rey-Campos J.; RT "FHX.L and FHX.S, two isoforms of the human fork-head factor FHX (FOXJ2) RT with differential activity."; RL J. Mol. Biol. 301:795-806(2000). RN [3] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM FOXJ2.L). 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 [4] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 458-574 (ISOFORM FOXJ2.L). RC TISSUE=Melanoma; 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 [5] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-161, AND IDENTIFICATION BY RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Embryonic kidney; RX PubMed=17525332; DOI=10.1126/science.1140321; RA Matsuoka S., Ballif B.A., Smogorzewska A., McDonald E.R. III, Hurov K.E., RA Luo J., Bakalarski C.E., Zhao Z., Solimini N., Lerenthal Y., Shiloh Y., RA Gygi S.P., Elledge S.J.; RT "ATM and ATR substrate analysis reveals extensive protein networks RT responsive to DNA damage."; RL Science 316:1160-1166(2007). RN [6] 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 [7] RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RX PubMed=19413330; DOI=10.1021/ac9004309; RA Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J., Mohammed S.; RT "Lys-N and trypsin cover complementary parts of the phosphoproteome in a RT refined SCX-based approach."; RL Anal. Chem. 81:4493-4501(2009). RN [8] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-172, AND IDENTIFICATION BY RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Leukemic T-cell; RX PubMed=19690332; DOI=10.1126/scisignal.2000007; RA Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K., RA Rodionov V., Han D.K.; RT "Quantitative phosphoproteomic analysis of T cell receptor signaling RT reveals system-wide modulation of protein-protein interactions."; RL Sci. Signal. 2:RA46-RA46(2009). RN [9] RP ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, PHOSPHORYLATION [LARGE SCALE RP ANALYSIS] AT SER-3, CLEAVAGE OF INITIATOR METHIONINE [LARGE SCALE RP ANALYSIS], AND IDENTIFICATION BY 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). RN [10] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-46 AND SER-172, AND RP 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 [11] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-46 AND SER-164, AND RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Liver; RX PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014; RA Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., Wang L., RA Ye M., Zou H.; RT "An enzyme assisted RP-RPLC approach for in-depth analysis of human liver RT phosphoproteome."; RL J. Proteomics 96:253-262(2014). CC -!- FUNCTION: [Isoform FOXJ2.L]: Transcriptional activator. Able to bind to CC two different type of DNA binding sites. More effective than isoform CC FOXJ2.S in transcriptional activation (PubMed:10777590, CC PubMed:10966786). Plays an important role in spermatogenesis, CC especially in spermatocyte meiosis (By similarity). CC {ECO:0000250|UniProtKB:Q9ES18, ECO:0000269|PubMed:10777590, CC ECO:0000269|PubMed:10966786}. CC -!- FUNCTION: [Isoform FOXJ2.S]: Transcriptional activator. CC {ECO:0000269|PubMed:10966786}. CC -!- INTERACTION: CC Q9P0K8; Q9H0L4: CSTF2T; NbExp=3; IntAct=EBI-2869608, EBI-747012; CC Q9P0K8; Q9H6Z9: EGLN3; NbExp=6; IntAct=EBI-2869608, EBI-1175354; CC Q9P0K8; Q9P0K8: FOXJ2; NbExp=2; IntAct=EBI-2869608, EBI-2869608; CC -!- SUBCELLULAR LOCATION: Nucleus. CC -!- ALTERNATIVE PRODUCTS: CC Event=Alternative splicing; Named isoforms=2; CC Name=FOXJ2.L; Synonyms=FHX.L; CC IsoId=Q9P0K8-1; Sequence=Displayed; CC Name=FOXJ2.S; Synonyms=FHX.S; CC IsoId=Q9P0K8-2; Sequence=VSP_001544; CC -!- TISSUE SPECIFICITY: Widely expressed. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; AF155132; AAF65927.1; -; mRNA. DR EMBL; AF155133; AAK49016.1; -; mRNA. DR EMBL; BC126396; AAI26397.1; -; mRNA. DR EMBL; BC136305; AAI36306.1; -; mRNA. DR EMBL; AL161978; CAB82315.1; -; mRNA. DR CCDS; CCDS8587.1; -. [Q9P0K8-1] DR PIR; T47161; T47161. DR RefSeq; NP_060886.1; NM_018416.2. [Q9P0K8-1] DR AlphaFoldDB; Q9P0K8; -. DR SMR; Q9P0K8; -. DR BioGRID; 120920; 81. DR IntAct; Q9P0K8; 74. DR MINT; Q9P0K8; -. DR STRING; 9606.ENSP00000162391; -. DR iPTMnet; Q9P0K8; -. DR PhosphoSitePlus; Q9P0K8; -. DR BioMuta; FOXJ2; -. DR DMDM; 13626933; -. DR EPD; Q9P0K8; -. DR jPOST; Q9P0K8; -. DR MassIVE; Q9P0K8; -. DR MaxQB; Q9P0K8; -. DR PaxDb; 9606-ENSP00000162391; -. DR PeptideAtlas; Q9P0K8; -. DR ProteomicsDB; 83564; -. [Q9P0K8-1] DR ProteomicsDB; 83565; -. [Q9P0K8-2] DR Pumba; Q9P0K8; -. DR Antibodypedia; 1748; 186 antibodies from 20 providers. DR DNASU; 55810; -. DR Ensembl; ENST00000162391.8; ENSP00000162391.3; ENSG00000065970.9. [Q9P0K8-1] DR Ensembl; ENST00000428177.2; ENSP00000403411.2; ENSG00000065970.9. [Q9P0K8-2] DR GeneID; 55810; -. DR KEGG; hsa:55810; -. DR MANE-Select; ENST00000162391.8; ENSP00000162391.3; NM_018416.3; NP_060886.1. DR UCSC; uc001qtt.2; human. [Q9P0K8-1] DR AGR; HGNC:24818; -. DR CTD; 55810; -. DR DisGeNET; 55810; -. DR GeneCards; FOXJ2; -. DR HGNC; HGNC:24818; FOXJ2. DR HPA; ENSG00000065970; Low tissue specificity. DR MIM; 619162; gene. DR neXtProt; NX_Q9P0K8; -. DR OpenTargets; ENSG00000065970; -. DR PharmGKB; PA134982817; -. DR VEuPathDB; HostDB:ENSG00000065970; -. DR eggNOG; KOG2294; Eukaryota. DR GeneTree; ENSGT00940000161053; -. DR HOGENOM; CLU_034661_0_0_1; -. DR InParanoid; Q9P0K8; -. DR OMA; SHFSELM; -. DR OrthoDB; 5385885at2759; -. DR PhylomeDB; Q9P0K8; -. DR TreeFam; TF333250; -. DR PathwayCommons; Q9P0K8; -. DR SignaLink; Q9P0K8; -. DR BioGRID-ORCS; 55810; 13 hits in 1176 CRISPR screens. DR ChiTaRS; FOXJ2; human. DR GeneWiki; FOXJ2; -. DR GenomeRNAi; 55810; -. DR Pharos; Q9P0K8; Tbio. DR PRO; PR:Q9P0K8; -. DR Proteomes; UP000005640; Chromosome 12. DR RNAct; Q9P0K8; Protein. DR Bgee; ENSG00000065970; Expressed in nipple and 210 other cell types or tissues. DR GO; GO:0000785; C:chromatin; ISA:NTNU_SB. DR GO; GO:0001650; C:fibrillar center; IDA:HPA. DR GO; GO:0005654; C:nucleoplasm; IDA:HPA. DR GO; GO:0005634; C:nucleus; IDA:BHF-UCL. DR GO; GO:0001228; F:DNA-binding transcription activator activity, RNA polymerase II-specific; IDA:NTNU_SB. DR GO; GO:0000981; F:DNA-binding transcription factor activity, RNA polymerase II-specific; ISA:NTNU_SB. DR GO; GO:0042802; F:identical protein binding; IPI:IntAct. DR GO; GO:0000978; F:RNA polymerase II cis-regulatory region sequence-specific DNA binding; IDA:NTNU_SB. DR GO; GO:0043565; F:sequence-specific DNA binding; IDA:UniProtKB. DR GO; GO:1990837; F:sequence-specific double-stranded DNA binding; IDA:ARUK-UCL. DR GO; GO:0030154; P:cell differentiation; IEA:UniProtKB-KW. DR GO; GO:0007141; P:male meiosis I; ISS:UniProtKB. DR GO; GO:0016525; P:negative regulation of angiogenesis; IMP:BHF-UCL. DR GO; GO:0110059; P:negative regulation of blood vessel endothelial cell differentiation; IDA:BHF-UCL. DR GO; GO:0045893; P:positive regulation of DNA-templated transcription; IDA:UniProtKB. DR GO; GO:0045944; P:positive regulation of transcription by RNA polymerase II; IDA:NTNU_SB. DR GO; GO:1904707; P:positive regulation of vascular associated smooth muscle cell proliferation; IDA:BHF-UCL. DR GO; GO:0006357; P:regulation of transcription by RNA polymerase II; IBA:GO_Central. DR GO; GO:0007283; P:spermatogenesis; ISS:UniProtKB. DR CDD; cd20051; FH_FOXJ2; 1. DR Gene3D; 1.10.10.10; Winged helix-like DNA-binding domain superfamily/Winged helix DNA-binding domain; 1. DR InterPro; IPR047393; FH_FOXJ2. DR InterPro; IPR001766; Fork_head_dom. DR InterPro; IPR045912; FOXJ2/3-like. DR InterPro; IPR030456; TF_fork_head_CS_2. DR InterPro; IPR036388; WH-like_DNA-bd_sf. DR InterPro; IPR036390; WH_DNA-bd_sf. DR PANTHER; PTHR46078:SF1; FORKHEAD BOX PROTEIN J2; 1. DR PANTHER; PTHR46078; FORKHEAD BOX PROTEIN J2 FAMILY MEMBER; 1. DR Pfam; PF00250; Forkhead; 1. DR PRINTS; PR00053; FORKHEAD. DR SMART; SM00339; FH; 1. DR SUPFAM; SSF46785; Winged helix' DNA-binding domain; 1. DR PROSITE; PS00658; FORK_HEAD_2; 1. DR PROSITE; PS50039; FORK_HEAD_3; 1. DR Genevisible; Q9P0K8; HS. PE 1: Evidence at protein level; KW Acetylation; Activator; Alternative splicing; Differentiation; DNA-binding; KW Meiosis; Nucleus; Phosphoprotein; Reference proteome; Spermatogenesis; KW Transcription; Transcription regulation. FT INIT_MET 1 FT /note="Removed" FT /evidence="ECO:0007744|PubMed:20068231" FT CHAIN 2..574 FT /note="Forkhead box protein J2" FT /id="PRO_0000091853" FT DNA_BIND 66..143 FT /note="Fork-head" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00089" FT REGION 26..61 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 125..233 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 267..408 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 537..574 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 32..53 FT /note="Polar residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 146..165 FT /note="Basic and acidic residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 187..210 FT /note="Polar residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 267..299 FT /note="Polar residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 300..317 FT /note="Pro residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 384..398 FT /note="Pro residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT MOD_RES 2 FT /note="N-acetylalanine" FT /evidence="ECO:0007744|PubMed:20068231" FT MOD_RES 3 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:20068231" FT MOD_RES 46 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:23186163, FT ECO:0007744|PubMed:24275569" FT MOD_RES 161 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:17525332" FT MOD_RES 164 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:24275569" FT MOD_RES 172 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:19690332, FT ECO:0007744|PubMed:23186163" FT VAR_SEQ 513..574 FT /note="VNSYGHPQAPHLYPGPSPMYPIPTQDSAGYNRPAHHMVPRPSVPPPGANEEI FT PDDFDWDLIT -> GTAPSQLPWRWRLC (in isoform FOXJ2.S)" FT /evidence="ECO:0000303|PubMed:10966786" FT /id="VSP_001544" FT VARIANT 229 FT /note="P -> R (in dbSNP:rs879211194)" FT /id="VAR_049162" FT VARIANT 310 FT /note="P -> S (in dbSNP:rs2277415)" FT /id="VAR_021842" SQ SEQUENCE 574 AA; 62395 MW; 258120EDAE4B11EB CRC64; MASDLESSLT SIDWLPQLTL RATIEKLGSA SQAGPPGSSR KCSPGSPTDP NATLSKDEAA VHQDGKPRYS YATLITYAIN SSPAKKMTLS EIYRWICDNF PYYKNAGIGW KNSIRHNLSL NKCFRKVPRP RDDPGKGSYW TIDTCPDISR KRRHPPDDDL SQDSPEQEAS KSPRGGVAGS GEASLPPEGN PQMSLQSPTS IASYSQGTGS VDGGAVAAGA SGRESAEGPP PLYNTNHDFK FSYSEINFQD LSWSFRNLYK SMLEKSSSSS QHGFSSLLGD IPPSNNYYMY QQQQPPPPQQ QQQQQQPPQP PPQQSQPQQQ QAPAQGPSAV GGAPPLHTPS TDGCTPPGGK QAGAEGYGPP PVMAMHPPPL QHGGYHPHQH HPHSHPAQQP PPPQPQAQGQ APINNTGFAF PSDWCSNIDS LKESFKMVNR LNWSSIEQSQ FSELMESLRQ AEQKNWTLDQ HHIANLCDSL NHFLTQTGHV PPQGGTHRPP APARIADSCA LTSGKQESAM SQVNSYGHPQ APHLYPGPSP MYPIPTQDSA GYNRPAHHMV PRPSVPPPGA NEEIPDDFDW DLIT //