FOXD2_HUMAN
ID FOXD2_HUMAN Reviewed; 495 AA.
AC O60548; Q5SVZ3;
DT 30-MAY-2000, integrated into UniProtKB/Swiss-Prot.
DT 26-FEB-2008, sequence version 2.
DT 03-AUG-2022, entry version 169.
DE RecName: Full=Forkhead box protein D2;
DE AltName: Full=Forkhead-related protein FKHL17;
DE AltName: Full=Forkhead-related transcription factor 9;
DE Short=FREAC-9;
GN Name=FOXD2; Synonyms=FKHL17, FREAC9;
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], TISSUE SPECIFICITY, AND VARIANT PRO-368.
RX PubMed=9403061; DOI=10.1006/geno.1997.4986;
RA Ernstsson S., Betz R., Lagercrantz S., Larsson C., Ericksson S.,
RA Cederberg A., Carlsson P., Enerbaeck S.;
RT "Cloning and characterization of freac-9 (FKHL17), a novel kidney-expressed
RT human forkhead gene that maps to chromosome 1p32-p34.";
RL Genomics 46:78-85(1997).
RN [2]
RP SEQUENCE REVISION.
RA Enerbaeck S.;
RL Submitted (APR-1998) to the EMBL/GenBank/DDBJ databases.
RN [3]
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 [4]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-96, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
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).
CC -!- FUNCTION: Probable transcription factor involved in embryogenesis and
CC somatogenesis. {ECO:0000250}.
CC -!- INTERACTION:
CC O60548; Q03989: ARID5A; NbExp=3; IntAct=EBI-17282008, EBI-948603;
CC O60548; A2RRN7: CADPS; NbExp=3; IntAct=EBI-17282008, EBI-10179719;
CC O60548; A8MQ03: CYSRT1; NbExp=3; IntAct=EBI-17282008, EBI-3867333;
CC O60548; O75593: FOXH1; NbExp=3; IntAct=EBI-17282008, EBI-1759806;
CC O60548; Q3LI76: KRTAP15-1; NbExp=3; IntAct=EBI-17282008, EBI-11992140;
CC O60548; Q3LHN2: KRTAP19-2; NbExp=3; IntAct=EBI-17282008, EBI-12196745;
CC O60548; Q3SYF9: KRTAP19-7; NbExp=3; IntAct=EBI-17282008, EBI-10241353;
CC O60548; Q3LI59: KRTAP21-2; NbExp=3; IntAct=EBI-17282008, EBI-18395721;
CC O60548; Q9BYR7: KRTAP3-2; NbExp=3; IntAct=EBI-17282008, EBI-751260;
CC O60548; Q3LI66: KRTAP6-2; NbExp=3; IntAct=EBI-17282008, EBI-11962084;
CC O60548; Q8IUC2: KRTAP8-1; NbExp=3; IntAct=EBI-17282008, EBI-10261141;
CC O60548; Q9Y5V3: MAGED1; NbExp=3; IntAct=EBI-17282008, EBI-716006;
CC O60548; A8MTQ0: NOTO; NbExp=3; IntAct=EBI-17282008, EBI-17490746;
CC O60548; Q16633: POU2AF1; NbExp=3; IntAct=EBI-17282008, EBI-943588;
CC O60548; Q96LM6: TEX37; NbExp=3; IntAct=EBI-17282008, EBI-743976;
CC O60548; Q08117-2: TLE5; NbExp=3; IntAct=EBI-17282008, EBI-11741437;
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000255|PROSITE-ProRule:PRU00089}.
CC -!- TISSUE SPECIFICITY: Kidney specific. {ECO:0000269|PubMed:9403061}.
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DR EMBL; AF042832; AAC15421.1; -; mRNA.
DR EMBL; AL607122; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR CCDS; CCDS30708.1; -.
DR RefSeq; NP_004465.3; NM_004474.3.
DR AlphaFoldDB; O60548; -.
DR SMR; O60548; -.
DR BioGRID; 108595; 25.
DR IntAct; O60548; 19.
DR STRING; 9606.ENSP00000335493; -.
DR iPTMnet; O60548; -.
DR PhosphoSitePlus; O60548; -.
DR BioMuta; FOXD2; -.
DR jPOST; O60548; -.
DR MassIVE; O60548; -.
DR PaxDb; O60548; -.
DR PeptideAtlas; O60548; -.
DR PRIDE; O60548; -.
DR ProteomicsDB; 49466; -.
DR Antibodypedia; 32890; 116 antibodies from 21 providers.
DR DNASU; 2306; -.
DR Ensembl; ENST00000334793.6; ENSP00000335493.6; ENSG00000186564.6.
DR GeneID; 2306; -.
DR KEGG; hsa:2306; -.
DR MANE-Select; ENST00000334793.6; ENSP00000335493.6; NM_004474.4; NP_004465.3.
DR UCSC; uc001crm.3; human.
DR CTD; 2306; -.
DR DisGeNET; 2306; -.
DR GeneCards; FOXD2; -.
DR HGNC; HGNC:3803; FOXD2.
DR HPA; ENSG00000186564; Tissue enhanced (intestine).
DR MIM; 602211; gene.
DR neXtProt; NX_O60548; -.
DR OpenTargets; ENSG00000186564; -.
DR PharmGKB; PA28220; -.
DR VEuPathDB; HostDB:ENSG00000186564; -.
DR eggNOG; KOG2294; Eukaryota.
DR GeneTree; ENSGT00940000157140; -.
DR HOGENOM; CLU_040357_5_0_1; -.
DR InParanoid; O60548; -.
DR OMA; GCCCEIM; -.
DR OrthoDB; 1270467at2759; -.
DR PhylomeDB; O60548; -.
DR TreeFam; TF316127; -.
DR PathwayCommons; O60548; -.
DR SignaLink; O60548; -.
DR SIGNOR; O60548; -.
DR BioGRID-ORCS; 2306; 13 hits in 1102 CRISPR screens.
DR ChiTaRS; FOXD2; human.
DR GenomeRNAi; 2306; -.
DR Pharos; O60548; Tbio.
DR PRO; PR:O60548; -.
DR Proteomes; UP000005640; Chromosome 1.
DR RNAct; O60548; protein.
DR Bgee; ENSG00000186564; Expressed in mucosa of transverse colon and 88 other tissues.
DR Genevisible; O60548; HS.
DR GO; GO:0000785; C:chromatin; ISA:NTNU_SB.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR GO; GO:0001228; F:DNA-binding transcription activator activity, RNA polymerase II-specific; IDA:NTNU_SB.
DR GO; GO:0003700; F:DNA-binding transcription factor activity; TAS:ProtInc.
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:0009653; P:anatomical structure morphogenesis; IBA:GO_Central.
DR GO; GO:0030154; P:cell differentiation; IBA:GO_Central.
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 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 DNA-binding; Nucleus; Phosphoprotein; Reference proteome; Transcription;
KW Transcription regulation.
FT CHAIN 1..495
FT /note="Forkhead box protein D2"
FT /id="PRO_0000091815"
FT DNA_BIND 126..217
FT /note="Fork-head"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00089"
FT REGION 14..122
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 312..347
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 397..444
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 96
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT VARIANT 368
FT /note="A -> P (in dbSNP:rs2405913)"
FT /evidence="ECO:0000269|PubMed:9403061"
FT /id="VAR_061185"
FT CONFLICT 293
FT /note="H -> HPH (in Ref. 1; AAC15421)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 495 AA; 48748 MW; E905950E1FA94565 CRC64;
MTLGSCCCEI MSSESSPAAL SEADADIDVV GGGSGGGELP ARSGPRAPRD VLPHGHEPPA
EEAEADLAED EEESGGCSDG EPRALASRGA AAAAGSPGPG AAAARGAAGP GPGPPSGGAA
TRSPLVKPPY SYIALITMAI LQSPKKRLTL SEICEFISGR FPYYREKFPA WQNSIRHNLS
LNDCFVKIPR EPGNPGKGNY WTLDPESADM FDNGSFLRRR KRFKRQPLPP PHPHPHPHPE
LLLRGGAAAA GDPGAFLPGF AAYGAYGYGY GLALPAYGAP PPGPAPHPHP HPHAFAFAAA
AAAAPCQLSV PPGRAAAPPP GPPTASVFAG AGSAPAPAPA SGSGPGPGPA GLPAFLGAEL
GCAKAFYAAS LSPPAAGTAA GLPTALLRQG LKTDAGGGAG GGGAGAGQRP SFSIDHIMGH
GGGGAAPPGA GEGSPGPPFA AAAGPGGQAQ VLAMLTAPAL APVAGHIRLS HPGDALLSSG
SRFASKVAGL SGCHF
