ID FOXJ3_HUMAN Reviewed; 622 AA. AC Q9UPW0; A7MBL7; A7MD18; D3DPW2; Q9NSS7; DT 30-MAY-2000, integrated into UniProtKB/Swiss-Prot. DT 18-MAY-2010, sequence version 2. DT 24-JAN-2024, entry version 185. DE RecName: Full=Forkhead box protein J3; GN Name=FOXJ3; Synonyms=KIAA1041; 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 [LARGE SCALE MRNA] (ISOFORM 1), AND VARIANTS ALA-162 RP AND PRO-377. RC TISSUE=Brain; RX PubMed=10470851; DOI=10.1093/dnares/6.3.197; RA Kikuno R., Nagase T., Ishikawa K., Hirosawa M., Miyajima N., Tanaka A., RA Kotani H., Nomura N., Ohara O.; RT "Prediction of the coding sequences of unidentified human genes. XIV. The RT complete sequences of 100 new cDNA clones from brain which code for large RT proteins in vitro."; RL DNA Res. 6:197-205(1999). RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RX PubMed=16710414; DOI=10.1038/nature04727; RA Gregory S.G., Barlow K.F., McLay K.E., Kaul R., Swarbreck D., Dunham A., RA Scott C.E., Howe K.L., Woodfine K., Spencer C.C.A., Jones M.C., Gillson C., RA Searle S., Zhou Y., Kokocinski F., McDonald L., Evans R., Phillips K., RA Atkinson A., Cooper R., Jones C., Hall R.E., Andrews T.D., Lloyd C., RA Ainscough R., Almeida J.P., Ambrose K.D., Anderson F., Andrew R.W., RA Ashwell R.I.S., Aubin K., Babbage A.K., Bagguley C.L., Bailey J., RA Beasley H., Bethel G., Bird C.P., Bray-Allen S., Brown J.Y., Brown A.J., RA Buckley D., Burton J., Bye J., Carder C., Chapman J.C., Clark S.Y., RA Clarke G., Clee C., Cobley V., Collier R.E., Corby N., Coville G.J., RA Davies J., Deadman R., Dunn M., Earthrowl M., Ellington A.G., Errington H., RA Frankish A., Frankland J., French L., Garner P., Garnett J., Gay L., RA Ghori M.R.J., Gibson R., Gilby L.M., Gillett W., Glithero R.J., RA Grafham D.V., Griffiths C., Griffiths-Jones S., Grocock R., Hammond S., RA Harrison E.S.I., Hart E., Haugen E., Heath P.D., Holmes S., Holt K., RA Howden P.J., Hunt A.R., Hunt S.E., Hunter G., Isherwood J., James R., RA Johnson C., Johnson D., Joy A., Kay M., Kershaw J.K., Kibukawa M., RA Kimberley A.M., King A., Knights A.J., Lad H., Laird G., Lawlor S., RA Leongamornlert D.A., Lloyd D.M., Loveland J., Lovell J., Lush M.J., RA Lyne R., Martin S., Mashreghi-Mohammadi M., Matthews L., Matthews N.S.W., RA McLaren S., Milne S., Mistry S., Moore M.J.F., Nickerson T., O'Dell C.N., RA Oliver K., Palmeiri A., Palmer S.A., Parker A., Patel D., Pearce A.V., RA Peck A.I., Pelan S., Phelps K., Phillimore B.J., Plumb R., Rajan J., RA Raymond C., Rouse G., Saenphimmachak C., Sehra H.K., Sheridan E., RA Shownkeen R., Sims S., Skuce C.D., Smith M., Steward C., Subramanian S., RA Sycamore N., Tracey A., Tromans A., Van Helmond Z., Wall M., Wallis J.M., RA White S., Whitehead S.L., Wilkinson J.E., Willey D.L., Williams H., RA Wilming L., Wray P.W., Wu Z., Coulson A., Vaudin M., Sulston J.E., RA Durbin R.M., Hubbard T., Wooster R., Dunham I., Carter N.P., McVean G., RA Ross M.T., Harrow J., Olson M.V., Beck S., Rogers J., Bentley D.R.; RT "The DNA sequence and biological annotation of human chromosome 1."; RL Nature 441:315-321(2006). RN [3] 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 [4] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1), NUCLEOTIDE SEQUENCE RP [LARGE SCALE MRNA] OF 1-416 (ISOFORM 2), AND VARIANTS ALA-162 AND PRO-377. 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 [5] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 451-622. RC TISSUE=Amygdala; 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 [6] RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Cervix carcinoma; RX PubMed=18691976; DOI=10.1016/j.molcel.2008.07.007; RA Daub H., Olsen J.V., Bairlein M., Gnad F., Oppermann F.S., Korner R., RA Greff Z., Keri G., Stemmann O., Mann M.; RT "Kinase-selective enrichment enables quantitative phosphoproteomics of the RT kinome across the cell cycle."; RL Mol. Cell 31:438-448(2008). RN [7] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-223, AND IDENTIFICATION BY RP 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 [8] 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 [9] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-223; SER-295 AND SER-489, AND RP IDENTIFICATION BY 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 [10] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-223 AND SER-606, AND RP 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 [11] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-223, 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 PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-223, AND IDENTIFICATION BY RP 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 [13] 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: Transcriptional activator of MEF2C involved in the regulation CC of adult muscle fiber type identity and skeletal muscle regeneration CC (By similarity). Plays an important role in spermatogenesis (By CC similarity). Required for the survival of spermatogonia and CC participates in spermatocyte meiosis (By similarity). CC {ECO:0000250|UniProtKB:Q8BUR3}. CC -!- INTERACTION: CC Q9UPW0; Q9HC98-4: NEK6; NbExp=3; IntAct=EBI-523002, EBI-11750983; CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000255|PROSITE-ProRule:PRU00089}. CC -!- ALTERNATIVE PRODUCTS: CC Event=Alternative splicing; Named isoforms=2; CC Name=1; CC IsoId=Q9UPW0-1; Sequence=Displayed; CC Name=2; CC IsoId=Q9UPW0-2; Sequence=VSP_010367; CC -!- SEQUENCE CAUTION: CC Sequence=BAA82993.2; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305}; 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; AB028964; BAA82993.2; ALT_INIT; mRNA. DR EMBL; AC096540; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; AC114492; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; CH471059; EAX07162.1; -; Genomic_DNA. DR EMBL; CH471059; EAX07163.1; -; Genomic_DNA. DR EMBL; CH471059; EAX07164.1; -; Genomic_DNA. DR EMBL; CH471059; EAX07165.1; -; Genomic_DNA. DR EMBL; BC014182; AAH14182.1; -; mRNA. DR EMBL; BC151828; AAI51829.1; -; mRNA. DR EMBL; BC152441; AAI52442.1; -; mRNA. DR EMBL; AL157422; CAB75651.2; -; mRNA. DR CCDS; CCDS30689.1; -. [Q9UPW0-1] DR CCDS; CCDS55594.1; -. [Q9UPW0-2] DR PIR; T46900; T46900. DR RefSeq; NP_001185779.1; NM_001198850.1. [Q9UPW0-1] DR RefSeq; NP_001185780.1; NM_001198851.1. [Q9UPW0-1] DR RefSeq; NP_001185781.1; NM_001198852.1. [Q9UPW0-2] DR RefSeq; NP_055762.3; NM_014947.4. [Q9UPW0-1] DR RefSeq; XP_011539328.1; XM_011541026.2. DR AlphaFoldDB; Q9UPW0; -. DR SMR; Q9UPW0; -. DR BioGRID; 116553; 33. DR IntAct; Q9UPW0; 18. DR MINT; Q9UPW0; -. DR STRING; 9606.ENSP00000361653; -. DR GlyGen; Q9UPW0; 1 site, 1 O-linked glycan (1 site). DR iPTMnet; Q9UPW0; -. DR PhosphoSitePlus; Q9UPW0; -. DR BioMuta; FOXJ3; -. DR DMDM; 296434510; -. DR EPD; Q9UPW0; -. DR jPOST; Q9UPW0; -. DR MassIVE; Q9UPW0; -. DR MaxQB; Q9UPW0; -. DR PaxDb; 9606-ENSP00000361653; -. DR PeptideAtlas; Q9UPW0; -. DR ProteomicsDB; 85458; -. [Q9UPW0-1] DR ProteomicsDB; 85459; -. [Q9UPW0-2] DR Pumba; Q9UPW0; -. DR Antibodypedia; 32193; 225 antibodies from 27 providers. DR DNASU; 22887; -. DR Ensembl; ENST00000361346.6; ENSP00000354620.1; ENSG00000198815.9. [Q9UPW0-1] DR Ensembl; ENST00000361776.5; ENSP00000354449.1; ENSG00000198815.9. [Q9UPW0-2] DR Ensembl; ENST00000372572.5; ENSP00000361653.1; ENSG00000198815.9. [Q9UPW0-1] DR Ensembl; ENST00000372573.5; ENSP00000361654.1; ENSG00000198815.9. [Q9UPW0-1] DR Ensembl; ENST00000545068.5; ENSP00000439044.1; ENSG00000198815.9. [Q9UPW0-1] DR GeneID; 22887; -. DR KEGG; hsa:22887; -. DR MANE-Select; ENST00000361346.6; ENSP00000354620.1; NM_014947.5; NP_055762.3. DR UCSC; uc001che.3; human. [Q9UPW0-1] DR AGR; HGNC:29178; -. DR CTD; 22887; -. DR DisGeNET; 22887; -. DR GeneCards; FOXJ3; -. DR HGNC; HGNC:29178; FOXJ3. DR HPA; ENSG00000198815; Low tissue specificity. DR MIM; 616035; gene. DR neXtProt; NX_Q9UPW0; -. DR OpenTargets; ENSG00000198815; -. DR PharmGKB; PA134945417; -. DR VEuPathDB; HostDB:ENSG00000198815; -. DR eggNOG; KOG2294; Eukaryota. DR GeneTree; ENSGT00940000160362; -. DR HOGENOM; CLU_030503_0_0_1; -. DR InParanoid; Q9UPW0; -. DR OMA; HMACNIG; -. DR OrthoDB; 5385885at2759; -. DR PhylomeDB; Q9UPW0; -. DR TreeFam; TF333250; -. DR PathwayCommons; Q9UPW0; -. DR SignaLink; Q9UPW0; -. DR SIGNOR; Q9UPW0; -. DR BioGRID-ORCS; 22887; 15 hits in 1181 CRISPR screens. DR ChiTaRS; FOXJ3; human. DR GenomeRNAi; 22887; -. DR Pharos; Q9UPW0; Tbio. DR PRO; PR:Q9UPW0; -. DR Proteomes; UP000005640; Chromosome 1. DR RNAct; Q9UPW0; Protein. DR Bgee; ENSG00000198815; Expressed in middle temporal gyrus and 214 other cell types or tissues. DR ExpressionAtlas; Q9UPW0; baseline and differential. DR GO; GO:0000785; C:chromatin; ISA:NTNU_SB. DR GO; GO:0005634; C:nucleus; IBA:GO_Central. 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:0000978; F:RNA polymerase II cis-regulatory region sequence-specific DNA binding; IBA:GO_Central. DR GO; GO:0043565; F:sequence-specific DNA binding; IDA:NTNU_SB. 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: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 GO; GO:0007283; P:spermatogenesis; ISS:UniProtKB. DR CDD; cd20052; FH_FOXJ3; 1. DR Gene3D; 1.10.10.10; Winged helix-like DNA-binding domain superfamily/Winged helix DNA-binding domain; 1. DR InterPro; IPR001766; Fork_head_dom. DR InterPro; IPR045912; FOXJ2/3-like. DR InterPro; IPR018122; TF_fork_head_CS_1. 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; FORKHEAD BOX PROTEIN J2 FAMILY MEMBER; 1. DR PANTHER; PTHR46078:SF3; FORKHEAD BOX PROTEIN J3; 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; PS00657; FORK_HEAD_1; 1. DR PROSITE; PS00658; FORK_HEAD_2; 1. DR PROSITE; PS50039; FORK_HEAD_3; 1. DR Genevisible; Q9UPW0; HS. PE 1: Evidence at protein level; KW Alternative splicing; Differentiation; DNA-binding; Meiosis; Nucleus; KW Phosphoprotein; Reference proteome; Spermatogenesis; Transcription; KW Transcription regulation. FT CHAIN 1..622 FT /note="Forkhead box protein J3" FT /id="PRO_0000091855" FT DNA_BIND 77..168 FT /note="Fork-head" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00089" FT REGION 145..178 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 249..274 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 316..450 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 161..175 FT /note="Basic and acidic residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 316..376 FT /note="Polar residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 377..401 FT /note="Pro residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 402..419 FT /note="Polar residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 431..450 FT /note="Polar residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT MOD_RES 223 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:18669648, FT ECO:0007744|PubMed:19690332, ECO:0007744|PubMed:20068231, FT ECO:0007744|PubMed:21406692, ECO:0007744|PubMed:23186163" FT MOD_RES 295 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:19690332" FT MOD_RES 489 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:19690332" FT MOD_RES 606 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:20068231" FT VAR_SEQ 177..210 FT /note="Missing (in isoform 2)" FT /evidence="ECO:0000303|PubMed:15489334" FT /id="VSP_010367" FT VARIANT 162 FT /note="V -> A (in dbSNP:rs343376)" FT /evidence="ECO:0000269|PubMed:10470851, FT ECO:0000269|PubMed:15489334" FT /id="VAR_039104" FT VARIANT 377 FT /note="T -> P (in dbSNP:rs1139978)" FT /evidence="ECO:0000269|PubMed:10470851, FT ECO:0000269|PubMed:15489334" FT /id="VAR_039105" FT CONFLICT 485 FT /note="G -> GG (in Ref. 5; CAB75651)" FT /evidence="ECO:0000305" SQ SEQUENCE 622 AA; 68960 MW; 2C53E63C76AF057B CRC64; MGLYGQACPS VTSLRMTSEL ESSLTSMDWL PQLTMRAAIQ KSDATQNAHG TGISKKNALL DPNTTLDQEE VQQHKDGKPP YSYASLITFA INSSPKKKMT LSEIYQWICD NFPYYREAGS GWKNSIRHNL SLNKCFLKVP RSKDDPGKGS YWAIDTNPKE DVLPTRPKKR ARSVERASTP YSIDSDSLGM ECIISGSASP TLAINTVTNK VTLYNTDQDG SDSPRSSLNN SLSDQSLASV NLNSVGSVHS YTPVTSHPES VSQSLTPQQQ PQYNLPERDK QLLFSEYNFE DLSASFRSLY KSVFEQSLSQ QGLMNIPSES SQQSHTSCTY QHSPSSTVST HPHSNQSSLS NSHGSGLNTT GSNSVAQVSL SHPQMHTQPS PHPPHRPHGL PQHPQRSPHP APHPQQHSQL QSPHPQHPSP HQHIQHHPNH QHQTLTHQAP PPPQQVSCNS GVSNDWYATL DMLKESCRIA SSVNWSDVDL SQFQGLMESM RQADLKNWSL DQVQFADLCS SLNQFFTQTG LIHSQSNVQQ NVCHGAMHPT KPSQHIGTGN LYIDSRQNLP PSVMPPPGYP HIPQALSTPG TTMAGHHRAM NQQHMMPSQA FQMRRSLPPD DIQDDFDWDS IV //