FOXJ3_HUMAN
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 03-AUG-2022, entry version 177.
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};
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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. [Q9UPW0-1]
DR AlphaFoldDB; Q9UPW0; -.
DR SMR; Q9UPW0; -.
DR BioGRID; 116553; 28.
DR IntAct; Q9UPW0; 18.
DR MINT; Q9UPW0; -.
DR STRING; 9606.ENSP00000361653; -.
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; Q9UPW0; -.
DR PeptideAtlas; Q9UPW0; -.
DR PRIDE; Q9UPW0; -.
DR ProteomicsDB; 85458; -. [Q9UPW0-1]
DR ProteomicsDB; 85459; -. [Q9UPW0-2]
DR Antibodypedia; 32193; 197 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 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; QSLSQQX; -.
DR OrthoDB; 1270467at2759; -.
DR PhylomeDB; Q9UPW0; -.
DR TreeFam; TF333250; -.
DR PathwayCommons; Q9UPW0; -.
DR SignaLink; Q9UPW0; -.
DR SIGNOR; Q9UPW0; -.
DR BioGRID-ORCS; 22887; 15 hits in 1103 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 212 other tissues.
DR ExpressionAtlas; Q9UPW0; baseline and differential.
DR Genevisible; Q9UPW0; HS.
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; cd00059; FH; 1.
DR Gene3D; 1.10.10.10; -; 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; PTHR46078; 1.
DR Pfam; PF00250; Forkhead; 1.
DR PRINTS; PR00053; FORKHEAD.
DR SMART; SM00339; FH; 1.
DR SUPFAM; SSF46785; SSF46785; 1.
DR PROSITE; PS00657; FORK_HEAD_1; 1.
DR PROSITE; PS00658; FORK_HEAD_2; 1.
DR PROSITE; PS50039; FORK_HEAD_3; 1.
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
