FOXN3_HUMAN
ID FOXN3_HUMAN Reviewed; 490 AA.
AC O00409; Q96II7; Q9UIE7;
DT 30-MAY-2000, integrated into UniProtKB/Swiss-Prot.
DT 01-JUL-1997, sequence version 1.
DT 03-AUG-2022, entry version 203.
DE RecName: Full=Forkhead box protein N3;
DE AltName: Full=Checkpoint suppressor 1;
GN Name=FOXN3; Synonyms=C14orf116, CHES1;
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 1).
RX PubMed=9154802; DOI=10.1128/mcb.17.6.3037;
RA Pati D., Keller C., Groudine M., Plon S.E.;
RT "Reconstitution of a MEC1-independent checkpoint in yeast by expression of
RT a novel human fork head cDNA.";
RL Mol. Cell. Biol. 17:3037-3046(1997).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=12508121; DOI=10.1038/nature01348;
RA Heilig R., Eckenberg R., Petit J.-L., Fonknechten N., Da Silva C.,
RA Cattolico L., Levy M., Barbe V., De Berardinis V., Ureta-Vidal A.,
RA Pelletier E., Vico V., Anthouard V., Rowen L., Madan A., Qin S., Sun H.,
RA Du H., Pepin K., Artiguenave F., Robert C., Cruaud C., Bruels T.,
RA Jaillon O., Friedlander L., Samson G., Brottier P., Cure S., Segurens B.,
RA Aniere F., Samain S., Crespeau H., Abbasi N., Aiach N., Boscus D.,
RA Dickhoff R., Dors M., Dubois I., Friedman C., Gouyvenoux M., James R.,
RA Madan A., Mairey-Estrada B., Mangenot S., Martins N., Menard M., Oztas S.,
RA Ratcliffe A., Shaffer T., Trask B., Vacherie B., Bellemere C., Belser C.,
RA Besnard-Gonnet M., Bartol-Mavel D., Boutard M., Briez-Silla S.,
RA Combette S., Dufosse-Laurent V., Ferron C., Lechaplais C., Louesse C.,
RA Muselet D., Magdelenat G., Pateau E., Petit E., Sirvain-Trukniewicz P.,
RA Trybou A., Vega-Czarny N., Bataille E., Bluet E., Bordelais I., Dubois M.,
RA Dumont C., Guerin T., Haffray S., Hammadi R., Muanga J., Pellouin V.,
RA Robert D., Wunderle E., Gauguet G., Roy A., Sainte-Marthe L., Verdier J.,
RA Verdier-Discala C., Hillier L.W., Fulton L., McPherson J., Matsuda F.,
RA Wilson R., Scarpelli C., Gyapay G., Wincker P., Saurin W., Quetier F.,
RA Waterston R., Hood L., Weissenbach J.;
RT "The DNA sequence and analysis of human chromosome 14.";
RL Nature 421:601-607(2003).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RC TISSUE=Muscle;
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 FUNCTION, AND INTERACTION WITH SNW1.
RX PubMed=16102918; DOI=10.1016/j.gene.2005.06.014;
RA Scott K.L., Plon S.E.;
RT "CHES1/FOXN3 interacts with Ski-interacting protein and acts as a
RT transcriptional repressor.";
RL Gene 359:119-126(2005).
RN [5]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-85, 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 [6]
RP IDENTIFICATION BY 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).
CC -!- FUNCTION: Acts as a transcriptional repressor. May be involved in DNA
CC damage-inducible cell cycle arrests (checkpoints).
CC {ECO:0000269|PubMed:16102918}.
CC -!- SUBUNIT: Interacts through its C-terminus with the C-terminus of
CC SNW1/SKIP. {ECO:0000269|PubMed:16102918}.
CC -!- INTERACTION:
CC O00409; Q13573: SNW1; NbExp=3; IntAct=EBI-372721, EBI-632715;
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000305}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=O00409-1; Sequence=Displayed;
CC Name=2;
CC IsoId=O00409-2; Sequence=VSP_001551;
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DR EMBL; U68723; AAB58252.1; -; mRNA.
DR EMBL; AC007263; AAF18259.1; -; Genomic_DNA.
DR EMBL; AL138478; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AL356805; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AL357093; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC007506; AAH07506.1; -; mRNA.
DR CCDS; CCDS32138.1; -. [O00409-2]
DR CCDS; CCDS41977.1; -. [O00409-1]
DR RefSeq; NP_001078940.1; NM_001085471.1. [O00409-1]
DR RefSeq; NP_005188.2; NM_005197.3. [O00409-2]
DR PDB; 6NCE; X-ray; 2.60 A; A=112-210.
DR PDB; 6NCM; X-ray; 2.70 A; A/B=112-210.
DR PDBsum; 6NCE; -.
DR PDBsum; 6NCM; -.
DR AlphaFoldDB; O00409; -.
DR SMR; O00409; -.
DR BioGRID; 107537; 55.
DR IntAct; O00409; 17.
DR MINT; O00409; -.
DR STRING; 9606.ENSP00000343288; -.
DR GlyGen; O00409; 1 site, 1 O-linked glycan (1 site).
DR iPTMnet; O00409; -.
DR PhosphoSitePlus; O00409; -.
DR BioMuta; FOXN3; -.
DR EPD; O00409; -.
DR jPOST; O00409; -.
DR MassIVE; O00409; -.
DR MaxQB; O00409; -.
DR PaxDb; O00409; -.
DR PeptideAtlas; O00409; -.
DR PRIDE; O00409; -.
DR ProteomicsDB; 47870; -. [O00409-1]
DR ProteomicsDB; 47871; -. [O00409-2]
DR Antibodypedia; 13438; 146 antibodies from 24 providers.
DR DNASU; 1112; -.
DR Ensembl; ENST00000261302.9; ENSP00000261302.5; ENSG00000053254.16. [O00409-1]
DR Ensembl; ENST00000345097.8; ENSP00000343288.4; ENSG00000053254.16. [O00409-1]
DR Ensembl; ENST00000555353.5; ENSP00000452227.1; ENSG00000053254.16. [O00409-2]
DR Ensembl; ENST00000557258.6; ENSP00000452005.1; ENSG00000053254.16. [O00409-2]
DR Ensembl; ENST00000615335.4; ENSP00000479114.1; ENSG00000053254.16. [O00409-2]
DR GeneID; 1112; -.
DR KEGG; hsa:1112; -.
DR MANE-Select; ENST00000557258.6; ENSP00000452005.1; NM_005197.4; NP_005188.2. [O00409-2]
DR UCSC; uc001xxn.5; human. [O00409-1]
DR CTD; 1112; -.
DR DisGeNET; 1112; -.
DR GeneCards; FOXN3; -.
DR HGNC; HGNC:1928; FOXN3.
DR HPA; ENSG00000053254; Low tissue specificity.
DR MIM; 602628; gene.
DR neXtProt; NX_O00409; -.
DR OpenTargets; ENSG00000053254; -.
DR PharmGKB; PA26460; -.
DR VEuPathDB; HostDB:ENSG00000053254; -.
DR eggNOG; KOG2294; Eukaryota.
DR GeneTree; ENSGT00940000155937; -.
DR HOGENOM; CLU_032050_0_0_1; -.
DR InParanoid; O00409; -.
DR OMA; XSIGKGS; -.
DR PhylomeDB; O00409; -.
DR TreeFam; TF105083; -.
DR PathwayCommons; O00409; -.
DR SignaLink; O00409; -.
DR SIGNOR; O00409; -.
DR BioGRID-ORCS; 1112; 14 hits in 1095 CRISPR screens.
DR ChiTaRS; FOXN3; human.
DR GeneWiki; FOXN3; -.
DR GenomeRNAi; 1112; -.
DR Pharos; O00409; Tbio.
DR PRO; PR:O00409; -.
DR Proteomes; UP000005640; Chromosome 14.
DR RNAct; O00409; protein.
DR Bgee; ENSG00000053254; Expressed in paraflocculus and 208 other tissues.
DR ExpressionAtlas; O00409; baseline and differential.
DR Genevisible; O00409; HS.
DR GO; GO:0000785; C:chromatin; ISA:NTNU_SB.
DR GO; GO:0005634; C:nucleus; IBA:GO_Central.
DR GO; GO:0000987; F:cis-regulatory region sequence-specific DNA binding; IBA:GO_Central.
DR GO; GO:0003700; F:DNA-binding transcription factor activity; IBA:GO_Central.
DR GO; GO:0000981; F:DNA-binding transcription factor activity, RNA polymerase II-specific; ISA:NTNU_SB.
DR GO; GO:0008022; F:protein C-terminus binding; IPI:UniProtKB.
DR GO; GO:0097094; P:craniofacial suture morphogenesis; IEA:Ensembl.
DR GO; GO:0007095; P:mitotic G2 DNA damage checkpoint signaling; IGI:UniProtKB.
DR GO; GO:0045892; P:negative regulation of transcription, DNA-templated; IDA:UniProtKB.
DR GO; GO:0006355; P:regulation of transcription, DNA-templated; IBA:GO_Central.
DR CDD; cd00059; FH; 1.
DR Gene3D; 1.10.10.10; -; 1.
DR InterPro; IPR001766; Fork_head_dom.
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 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 3D-structure; Alternative splicing; Cell cycle; DNA-binding; Nucleus;
KW Phosphoprotein; Reference proteome; Repressor; Transcription;
KW Transcription regulation.
FT CHAIN 1..490
FT /note="Forkhead box protein N3"
FT /id="PRO_0000091869"
FT DNA_BIND 113..204
FT /note="Fork-head"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00089"
FT REGION 1..21
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 86..108
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 315..458
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 340..380
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 381..418
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 432..457
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 83
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q499D0"
FT MOD_RES 85
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19690332"
FT MOD_RES 97
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q499D0"
FT MOD_RES 448
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q499D0"
FT VAR_SEQ 249..271
FT /note="DPDIDAASAMMLLNTPPEIQAGF -> V (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_001551"
FT VARIANT 337
FT /note="Y -> H (in dbSNP:rs1804717)"
FT /id="VAR_049163"
FT HELIX 119..129
FT /evidence="ECO:0007829|PDB:6NCE"
FT STRAND 133..135
FT /evidence="ECO:0007829|PDB:6NCE"
FT HELIX 137..147
FT /evidence="ECO:0007829|PDB:6NCE"
FT HELIX 149..152
FT /evidence="ECO:0007829|PDB:6NCE"
FT HELIX 158..168
FT /evidence="ECO:0007829|PDB:6NCE"
FT STRAND 172..175
FT /evidence="ECO:0007829|PDB:6NCE"
FT STRAND 188..191
FT /evidence="ECO:0007829|PDB:6NCE"
FT TURN 193..195
FT /evidence="ECO:0007829|PDB:6NCE"
FT HELIX 196..205
FT /evidence="ECO:0007829|PDB:6NCE"
SQ SEQUENCE 490 AA; 53835 MW; EE07975A592C8C01 CRC64;
MGPVMPPSKK PESSGISVSS GLSQCYGGSG FSKALQEDDD LDFSLPDIRL EEGAMEDEEL
TNLNWLHESK NLLKSFGESV LRSVSPVQDL DDDTPPSPAH SDMPYDARQN PNCKPPYSFS
CLIFMAIEDS PTKRLPVKDI YNWILEHFPY FANAPTGWKN SVRHNLSLNK CFKKVDKERS
QSIGKGSLWC IDPEYRQNLI QALKKTPYHP HPHVFNTPPT CPQAYQSTSG PPIWPGSTFF
KRNGALLQDP DIDAASAMML LNTPPEIQAG FPPGVIQNGA RVLSRGLFPG VRPLPITPIG
VTAAMRNGIT SCRMRTESEP SCGSPVVSGD PKEDHNYSSA KSSNARSTSP TSDSISSSSS
SADDHYEFAT KGSQEGSEGS EGSFRSHESP SDTEEDDRKH SQKEPKDSLG DSGYASQHKK
RQHFAKARKV PSDTLPLKKR RTEKPPESDD EEMKEAAGSL LHLAGIRSCL NNITNRTAKG
QKEQKETTKN
