HHEX_HUMAN
ID HHEX_HUMAN Reviewed; 270 AA.
AC Q03014; B1AQ17; Q96CE9;
DT 01-JUN-1994, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-1994, sequence version 1.
DT 03-AUG-2022, entry version 204.
DE RecName: Full=Hematopoietically-expressed homeobox protein HHEX;
DE Short=Homeobox protein HEX;
DE AltName: Full=Homeobox protein PRH;
GN Name=HHEX; Synonyms=HEX, PRH, PRHX;
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], AND TISSUE SPECIFICITY.
RX PubMed=1360645; DOI=10.1093/nar/20.21.5661;
RA Crompton M.R., Bartlett T.J., Macgregor A.D., Manfioletti G., Buratti E.,
RA Giancotti V., Goodwin G.H.;
RT "Identification of a novel vertebrate homeobox gene expressed in
RT haematopoietic cells.";
RL Nucleic Acids Res. 20:5661-5667(1992).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA], AND TISSUE SPECIFICITY.
RC TISSUE=Myeloid leukemia cell;
RX PubMed=8103988; DOI=10.1006/bbrc.1993.2140;
RA Hromas R.A., Collins S.J., Radich J.;
RT "PCR cloning of an orphan homeobox gene (PRH) preferentially expressed in
RT myeloid and liver cells.";
RL Biochem. Biophys. Res. Commun. 195:976-983(1993).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Mammary gland;
RX PubMed=14702039; DOI=10.1038/ng1285;
RA Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
RA Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
RA Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
RA Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
RA Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H.,
RA Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M.,
RA Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K.,
RA Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T.,
RA Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M.,
RA Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S.,
RA Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H.,
RA Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K.,
RA Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N.,
RA Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
RA Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
RA Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
RA Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
RA Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y.,
RA Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K.,
RA Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T.,
RA Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T.,
RA Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y.,
RA Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H.,
RA Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y.,
RA Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H.,
RA Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O.,
RA Isogai T., Sugano S.;
RT "Complete sequencing and characterization of 21,243 full-length human
RT cDNAs.";
RL Nat. Genet. 36:40-45(2004).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=15164054; DOI=10.1038/nature02462;
RA Deloukas P., Earthrowl M.E., Grafham D.V., Rubenfield M., French L.,
RA Steward C.A., Sims S.K., Jones M.C., Searle S., Scott C., Howe K.,
RA Hunt S.E., Andrews T.D., Gilbert J.G.R., Swarbreck D., Ashurst J.L.,
RA Taylor A., Battles J., Bird C.P., Ainscough R., Almeida J.P.,
RA Ashwell R.I.S., Ambrose K.D., Babbage A.K., Bagguley C.L., Bailey J.,
RA Banerjee R., Bates K., Beasley H., Bray-Allen S., Brown A.J., Brown J.Y.,
RA Burford D.C., Burrill W., Burton J., Cahill P., Camire D., Carter N.P.,
RA Chapman J.C., Clark S.Y., Clarke G., Clee C.M., Clegg S., Corby N.,
RA Coulson A., Dhami P., Dutta I., Dunn M., Faulkner L., Frankish A.,
RA Frankland J.A., Garner P., Garnett J., Gribble S., Griffiths C.,
RA Grocock R., Gustafson E., Hammond S., Harley J.L., Hart E., Heath P.D.,
RA Ho T.P., Hopkins B., Horne J., Howden P.J., Huckle E., Hynds C.,
RA Johnson C., Johnson D., Kana A., Kay M., Kimberley A.M., Kershaw J.K.,
RA Kokkinaki M., Laird G.K., Lawlor S., Lee H.M., Leongamornlert D.A.,
RA Laird G., Lloyd C., Lloyd D.M., Loveland J., Lovell J., McLaren S.,
RA McLay K.E., McMurray A., Mashreghi-Mohammadi M., Matthews L., Milne S.,
RA Nickerson T., Nguyen M., Overton-Larty E., Palmer S.A., Pearce A.V.,
RA Peck A.I., Pelan S., Phillimore B., Porter K., Rice C.M., Rogosin A.,
RA Ross M.T., Sarafidou T., Sehra H.K., Shownkeen R., Skuce C.D., Smith M.,
RA Standring L., Sycamore N., Tester J., Thorpe A., Torcasso W., Tracey A.,
RA Tromans A., Tsolas J., Wall M., Walsh J., Wang H., Weinstock K., West A.P.,
RA Willey D.L., Whitehead S.L., Wilming L., Wray P.W., Young L., Chen Y.,
RA Lovering R.C., Moschonas N.K., Siebert R., Fechtel K., Bentley D.,
RA Durbin R.M., Hubbard T., Doucette-Stamm L., Beck S., Smith D.R., Rogers J.;
RT "The DNA sequence and comparative analysis of human chromosome 10.";
RL Nature 429:375-381(2004).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Istrail S., Sutton 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 [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Bone marrow, and Uterus;
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 [7]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 122-270, FUNCTION, AND TISSUE SPECIFICITY.
RC TISSUE=Leukemia, and Peripheral blood monocyte;
RX PubMed=8096636; DOI=10.1093/nar/21.5.1245;
RA Bedford F.K., Ashworth A., Enver T., Wiedemann L.M.;
RT "HEX: a novel homeobox gene expressed during haematopoiesis and conserved
RT between mouse and human.";
RL Nucleic Acids Res. 21:1245-1249(1993).
RN [8]
RP FUNCTION, AND INTERACTION WITH SOX13.
RX PubMed=20028982; DOI=10.1074/jbc.m109.046649;
RA Marfil V., Moya M., Pierreux C.E., Castell J.V., Lemaigre F.P., Real F.X.,
RA Bort R.;
RT "Interaction between Hhex and SOX13 modulates Wnt/TCF activity.";
RL J. Biol. Chem. 285:5726-5737(2010).
RN [9]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-53, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=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 [10]
RP 3D-STRUCTURE MODELING OF 136-196.
RX PubMed=7911091; DOI=10.1016/0014-5793(94)00446-3;
RA Neidle S., Goodwin G.H.;
RT "A homology-based molecular model of the proline-rich homeodomain protein
RT Prh, from haematopoietic cells.";
RL FEBS Lett. 345:93-98(1994).
RN [11]
RP STRUCTURE BY NMR OF 138-194.
RG RIKEN structural genomics initiative (RSGI);
RT "Solution structure of RSGI RUH-028, a homeobox domain from human.";
RL Submitted (NOV-2006) to the PDB data bank.
CC -!- FUNCTION: Recognizes the DNA sequence 5'-ATTAA-3' (By similarity).
CC Transcriptional repressor (By similarity). Activator of WNT-mediated
CC transcription in conjunction with CTNNB1 (PubMed:20028982). Establishes
CC anterior identity at two levels; acts early to enhance canonical WNT-
CC signaling by repressing expression of TLE4, and acts later to inhibit
CC NODAL-signaling by directly targeting NODAL (By similarity). May play a
CC role in hematopoietic differentiation (PubMed:8096636).
CC {ECO:0000250|UniProtKB:P43120, ECO:0000269|PubMed:20028982,
CC ECO:0000269|PubMed:8096636}.
CC -!- SUBUNIT: Interacts with CD81; the interaction prevents nuclear
CC translocation of HHEX (By similarity). Interacts (via N-terminus) with
CC SOX13; abolishes the SOX13-mediated inhibition of WNT-mediated
CC transcriptional activity via competitive inhibition of the SOX13-TCF7
CC complex (PubMed:20028982). {ECO:0000250|UniProtKB:P43120,
CC ECO:0000269|PubMed:20028982}.
CC -!- INTERACTION:
CC Q03014; Q8IZP0-5: ABI1; NbExp=3; IntAct=EBI-747421, EBI-11743294;
CC Q03014; Q9NYB9-2: ABI2; NbExp=3; IntAct=EBI-747421, EBI-11096309;
CC Q03014; Q9NRW3: APOBEC3C; NbExp=3; IntAct=EBI-747421, EBI-1044593;
CC Q03014; A8MQ03: CYSRT1; NbExp=3; IntAct=EBI-747421, EBI-3867333;
CC Q03014; P28799: GRN; NbExp=3; IntAct=EBI-747421, EBI-747754;
CC Q03014; Q5VWX1: KHDRBS2; NbExp=3; IntAct=EBI-747421, EBI-742808;
CC Q03014; Q8IUG1: KRTAP1-3; NbExp=3; IntAct=EBI-747421, EBI-11749135;
CC Q03014; P60370: KRTAP10-5; NbExp=3; IntAct=EBI-747421, EBI-10172150;
CC Q03014; P60371: KRTAP10-6; NbExp=3; IntAct=EBI-747421, EBI-12012928;
CC Q03014; P60409: KRTAP10-7; NbExp=3; IntAct=EBI-747421, EBI-10172290;
CC Q03014; P60410: KRTAP10-8; NbExp=6; IntAct=EBI-747421, EBI-10171774;
CC Q03014; Q8IUB9: KRTAP19-1; NbExp=3; IntAct=EBI-747421, EBI-12811111;
CC Q03014; Q9BYR9: KRTAP2-4; NbExp=3; IntAct=EBI-747421, EBI-14065470;
CC Q03014; Q6L8G8: KRTAP5-7; NbExp=3; IntAct=EBI-747421, EBI-11987425;
CC Q03014; O75690: KRTAP5-8; NbExp=3; IntAct=EBI-747421, EBI-12134621;
CC Q03014; P26371: KRTAP5-9; NbExp=3; IntAct=EBI-747421, EBI-3958099;
CC Q03014; Q3LI64: KRTAP6-1; NbExp=3; IntAct=EBI-747421, EBI-12111050;
CC Q03014; Q3LI66: KRTAP6-2; NbExp=3; IntAct=EBI-747421, EBI-11962084;
CC Q03014; Q99750: MDFI; NbExp=3; IntAct=EBI-747421, EBI-724076;
CC Q03014; P0DPK4: NOTCH2NLC; NbExp=3; IntAct=EBI-747421, EBI-22310682;
CC Q03014; Q99471: PFDN5; NbExp=3; IntAct=EBI-747421, EBI-357275;
CC Q03014; O43586: PSTPIP1; NbExp=3; IntAct=EBI-747421, EBI-1050964;
CC Q03014; Q15415: RBMY1J; NbExp=3; IntAct=EBI-747421, EBI-8642021;
CC Q03014; Q08117-2: TLE5; NbExp=3; IntAct=EBI-747421, EBI-11741437;
CC Q03014; Q05BL1: TP53BP2; NbExp=3; IntAct=EBI-747421, EBI-11952721;
CC Q03014; O76024: WFS1; NbExp=3; IntAct=EBI-747421, EBI-720609;
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:P43120}.
CC -!- TISSUE SPECIFICITY: Liver and promyelocytic leukemia cell line HL-60.
CC {ECO:0000269|PubMed:1360645, ECO:0000269|PubMed:8096636,
CC ECO:0000269|PubMed:8103988}.
CC -!- DEVELOPMENTAL STAGE: Expressed during hematopoiesis.
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DR EMBL; X67235; CAA47661.1; -; mRNA.
DR EMBL; L16499; AAA02988.1; -; mRNA.
DR EMBL; AK314891; BAG37405.1; -; mRNA.
DR EMBL; AL590080; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH471066; EAW50087.1; -; Genomic_DNA.
DR EMBL; CH471066; EAW50088.1; -; Genomic_DNA.
DR EMBL; BC014336; AAH14336.1; -; mRNA.
DR EMBL; BC015110; AAH15110.1; -; mRNA.
DR EMBL; BC050638; AAH50638.1; -; mRNA.
DR EMBL; Z21533; CAA79730.1; -; mRNA.
DR CCDS; CCDS7423.1; -.
DR PIR; JN0767; JN0767.
DR RefSeq; NP_002720.1; NM_002729.4.
DR PDB; 2E1O; NMR; -; A=138-194.
DR PDBsum; 2E1O; -.
DR AlphaFoldDB; Q03014; -.
DR SMR; Q03014; -.
DR BioGRID; 109335; 41.
DR IntAct; Q03014; 31.
DR MINT; Q03014; -.
DR STRING; 9606.ENSP00000282728; -.
DR iPTMnet; Q03014; -.
DR PhosphoSitePlus; Q03014; -.
DR BioMuta; HHEX; -.
DR DMDM; 547658; -.
DR EPD; Q03014; -.
DR jPOST; Q03014; -.
DR MassIVE; Q03014; -.
DR MaxQB; Q03014; -.
DR PaxDb; Q03014; -.
DR PeptideAtlas; Q03014; -.
DR PRIDE; Q03014; -.
DR ProteomicsDB; 58161; -.
DR Antibodypedia; 16484; 516 antibodies from 35 providers.
DR DNASU; 3087; -.
DR Ensembl; ENST00000282728.10; ENSP00000282728.5; ENSG00000152804.11.
DR GeneID; 3087; -.
DR KEGG; hsa:3087; -.
DR MANE-Select; ENST00000282728.10; ENSP00000282728.5; NM_002729.5; NP_002720.1.
DR UCSC; uc001kid.4; human.
DR CTD; 3087; -.
DR DisGeNET; 3087; -.
DR GeneCards; HHEX; -.
DR HGNC; HGNC:4901; HHEX.
DR HPA; ENSG00000152804; Tissue enhanced (bone marrow, liver, thyroid gland).
DR MIM; 604420; gene.
DR neXtProt; NX_Q03014; -.
DR OpenTargets; ENSG00000152804; -.
DR PharmGKB; PA29274; -.
DR VEuPathDB; HostDB:ENSG00000152804; -.
DR eggNOG; KOG0483; Eukaryota.
DR GeneTree; ENSGT00940000161748; -.
DR HOGENOM; CLU_081944_0_0_1; -.
DR InParanoid; Q03014; -.
DR OMA; AGPLYPF; -.
DR OrthoDB; 1596695at2759; -.
DR PhylomeDB; Q03014; -.
DR TreeFam; TF325047; -.
DR PathwayCommons; Q03014; -.
DR SignaLink; Q03014; -.
DR SIGNOR; Q03014; -.
DR BioGRID-ORCS; 3087; 28 hits in 1113 CRISPR screens.
DR EvolutionaryTrace; Q03014; -.
DR GeneWiki; HHEX; -.
DR GenomeRNAi; 3087; -.
DR Pharos; Q03014; Tbio.
DR PRO; PR:Q03014; -.
DR Proteomes; UP000005640; Chromosome 10.
DR RNAct; Q03014; protein.
DR Bgee; ENSG00000152804; Expressed in secondary oocyte and 145 other tissues.
DR ExpressionAtlas; Q03014; baseline and differential.
DR Genevisible; Q03014; HS.
DR GO; GO:0000785; C:chromatin; ISA:NTNU_SB.
DR GO; GO:0005737; C:cytoplasm; IDA:BHF-UCL.
DR GO; GO:0005634; C:nucleus; IDA:BHF-UCL.
DR GO; GO:0032993; C:protein-DNA complex; IDA:BHF-UCL.
DR GO; GO:0008301; F:DNA binding, bending; IDA:BHF-UCL.
DR GO; GO:0001228; F:DNA-binding transcription activator activity, RNA polymerase II-specific; IMP:GO_Central.
DR GO; GO:0000981; F:DNA-binding transcription factor activity, RNA polymerase II-specific; ISA:NTNU_SB.
DR GO; GO:0140297; F:DNA-binding transcription factor binding; IDA:BHF-UCL.
DR GO; GO:0001227; F:DNA-binding transcription repressor activity, RNA polymerase II-specific; IDA:NTNU_SB.
DR GO; GO:0008190; F:eukaryotic initiation factor 4E binding; IDA:BHF-UCL.
DR GO; GO:0042803; F:protein homodimerization activity; IPI:BHF-UCL.
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:BHF-UCL.
DR GO; GO:0017025; F:TBP-class protein binding; TAS:BHF-UCL.
DR GO; GO:0000976; F:transcription cis-regulatory region binding; IDA:BHF-UCL.
DR GO; GO:0009952; P:anterior/posterior pattern specification; ISS:UniProtKB.
DR GO; GO:0030183; P:B cell differentiation; ISS:BHF-UCL.
DR GO; GO:0030154; P:cell differentiation; IBA:GO_Central.
DR GO; GO:0071103; P:DNA conformation change; IDA:BHF-UCL.
DR GO; GO:0006406; P:mRNA export from nucleus; IDA:BHF-UCL.
DR GO; GO:0016525; P:negative regulation of angiogenesis; ISS:BHF-UCL.
DR GO; GO:0045736; P:negative regulation of cyclin-dependent protein serine/threonine kinase activity; IDA:BHF-UCL.
DR GO; GO:0010944; P:negative regulation of transcription by competitive promoter binding; TAS:BHF-UCL.
DR GO; GO:0000122; P:negative regulation of transcription by RNA polymerase II; IDA:BHF-UCL.
DR GO; GO:0010621; P:negative regulation of transcription by transcription factor localization; IC:BHF-UCL.
DR GO; GO:0045892; P:negative regulation of transcription, DNA-templated; IDA:BHF-UCL.
DR GO; GO:0030948; P:negative regulation of vascular endothelial growth factor receptor signaling pathway; ISS:BHF-UCL.
DR GO; GO:0016973; P:poly(A)+ mRNA export from nucleus; IMP:BHF-UCL.
DR GO; GO:0090263; P:positive regulation of canonical Wnt signaling pathway; IMP:UniProtKB.
DR GO; GO:0045944; P:positive regulation of transcription by RNA polymerase II; IDA:BHF-UCL.
DR GO; GO:0045893; P:positive regulation of transcription, DNA-templated; IMP:UniProtKB.
DR GO; GO:0030177; P:positive regulation of Wnt signaling pathway; ISS:UniProtKB.
DR GO; GO:0034504; P:protein localization to nucleus; IDA:BHF-UCL.
DR GO; GO:0070663; P:regulation of leukocyte proliferation; IDA:BHF-UCL.
DR GO; GO:0006357; P:regulation of transcription by RNA polymerase II; IBA:GO_Central.
DR GO; GO:0016055; P:Wnt signaling pathway; IEA:UniProtKB-KW.
DR CDD; cd00086; homeodomain; 1.
DR InterPro; IPR009057; Homeobox-like_sf.
DR InterPro; IPR017970; Homeobox_CS.
DR InterPro; IPR001356; Homeobox_dom.
DR InterPro; IPR020479; Homeobox_metazoa.
DR Pfam; PF00046; Homeodomain; 1.
DR PRINTS; PR00024; HOMEOBOX.
DR SMART; SM00389; HOX; 1.
DR SUPFAM; SSF46689; SSF46689; 1.
DR PROSITE; PS00027; HOMEOBOX_1; 1.
DR PROSITE; PS50071; HOMEOBOX_2; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Developmental protein; Differentiation; DNA-binding;
KW Homeobox; Nucleus; Phosphoprotein; Reference proteome; Repressor;
KW Transcription; Transcription regulation; Wnt signaling pathway.
FT CHAIN 1..270
FT /note="Hematopoietically-expressed homeobox protein HHEX"
FT /id="PRO_0000049074"
FT DNA_BIND 137..196
FT /note="Homeobox"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00108"
FT REGION 1..137
FT /note="Interaction with SOX13"
FT /evidence="ECO:0000269|PubMed:20028982"
FT REGION 137..270
FT /note="Required for WNT signaling induction"
FT /evidence="ECO:0000269|PubMed:20028982"
FT REGION 194..270
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 194..214
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 215..245
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 53
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT CONFLICT 115
FT /note="L -> V (in Ref. 2; AAA02988)"
FT /evidence="ECO:0000305"
FT CONFLICT 171
FT /note="A -> T (in Ref. 6; AAH14336)"
FT /evidence="ECO:0000305"
FT HELIX 146..158
FT /evidence="ECO:0007829|PDB:2E1O"
FT HELIX 164..173
FT /evidence="ECO:0007829|PDB:2E1O"
FT HELIX 178..194
FT /evidence="ECO:0007829|PDB:2E1O"
SQ SEQUENCE 270 AA; 30022 MW; 9C16BB6D494475FC CRC64;
MQYPHPGPAA GAVGVPLYAP TPLLQPAHPT PFYIEDILGR GPAAPTPAPT LPSPNSSFTS
LVSPYRTPVY EPTPIHPAFS HHSAAALAAA YGPGGFGGPL YPFPRTVNDY THALLRHDPL
GKPLLWSPFL QRPLHKRKGG QVRFSNDQTI ELEKKFETQK YLSPPERKRL AKMLQLSERQ
VKTWFQNRRA KWRRLKQENP QSNKKEELES LDSSCDQRQD LPSEQNKGAS LDSSQCSPSP
ASQEDLESEI SEDSDQEVDI EGDKSYFNAG
