FOXJ2_HUMAN
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 03-AUG-2022, entry version 188.
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.
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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; 80.
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; Q9P0K8; -.
DR PeptideAtlas; Q9P0K8; -.
DR PRIDE; Q9P0K8; -.
DR ProteomicsDB; 83564; -. [Q9P0K8-1]
DR ProteomicsDB; 83565; -. [Q9P0K8-2]
DR Antibodypedia; 1748; 169 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 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; 1270467at2759; -.
DR PhylomeDB; Q9P0K8; -.
DR TreeFam; TF333250; -.
DR PathwayCommons; Q9P0K8; -.
DR SignaLink; Q9P0K8; -.
DR BioGRID-ORCS; 55810; 13 hits in 1100 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 208 other tissues.
DR Genevisible; Q9P0K8; HS.
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:0045944; P:positive regulation of transcription by RNA polymerase II; IDA:NTNU_SB.
DR GO; GO:0045893; P:positive regulation of transcription, DNA-templated; IDA:UniProtKB.
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; cd00059; FH; 1.
DR Gene3D; 1.10.10.10; -; 1.
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; PTHR46078; 1.
DR Pfam; PF00250; Forkhead; 1.
DR PRINTS; PR00053; FORKHEAD.
DR SMART; SM00339; FH; 1.
DR SUPFAM; SSF46785; SSF46785; 1.
DR PROSITE; PS00658; FORK_HEAD_2; 1.
DR PROSITE; PS50039; FORK_HEAD_3; 1.
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:rs35642012)"
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
