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 27-MAR-2024, entry version 213. DE RecName: Full=Hematopoietically-expressed homeobox protein HHEX; DE Short=Homeobox protein HEX; DE AltName: Full=Homeobox protein PRH; DE AltName: Full=Proline-rich homeodomain protein {ECO:0000303|PubMed:7911091}; 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, INTERACTION WITH EIF4E, SUBCELLULAR LOCATION, AND MUTAGENESIS OF RP 23-LEU-LEU-24; ARG-188 AND ARG-189. RX PubMed=12554669; DOI=10.1093/emboj/cdg069; RA Topisirovic I., Culjkovic B., Cohen N., Perez J.M., Skrabanek L., RA Borden K.L.; RT "The proline-rich homeodomain protein, PRH, is a tissue-specific inhibitor RT of eIF4E-dependent cyclin D1 mRNA transport and growth."; RL EMBO J. 22:689-703(2003). RN [9] 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 [10] 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 [11] 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 [12] 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). Inhibits CC EIF4E-mediated mRNA nuclear export (PubMed:12554669). May play a role CC in hematopoietic differentiation (PubMed:8096636). CC {ECO:0000250|UniProtKB:P43120, ECO:0000269|PubMed:12554669, CC ECO:0000269|PubMed:20028982, 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). Interacts with EIF4E; the interaction CC inhibits EIF4E-mediated mRNA nuclear export (PubMed:12554669). CC {ECO:0000250|UniProtKB:P43120, ECO:0000269|PubMed:12554669, 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}. Nucleus, CC nuclear body {ECO:0000269|PubMed:12554669}. Cytoplasm CC {ECO:0000269|PubMed:12554669}. 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. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- 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; 9606-ENSP00000282728; -. DR PeptideAtlas; Q03014; -. DR ProteomicsDB; 58161; -. DR Pumba; Q03014; -. DR Antibodypedia; 16484; 566 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 AGR; HGNC:4901; -. 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; AGIQNQE; -. DR OrthoDB; 5362922at2759; -. DR PhylomeDB; Q03014; -. DR TreeFam; TF325047; -. DR PathwayCommons; Q03014; -. DR SignaLink; Q03014; -. DR SIGNOR; Q03014; -. DR BioGRID-ORCS; 3087; 34 hits in 1199 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 147 other cell types or tissues. DR ExpressionAtlas; Q03014; baseline and differential. DR GO; GO:0000785; C:chromatin; ISA:NTNU_SB. DR GO; GO:0005737; C:cytoplasm; IDA:BHF-UCL. DR GO; GO:0016604; C:nuclear body; IEA:UniProtKB-SubCell. 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:0045892; P:negative regulation of DNA-templated transcription; 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: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:0045893; P:positive regulation of DNA-templated transcription; IMP:UniProtKB. DR GO; GO:0045944; P:positive regulation of transcription by RNA polymerase II; IDA:BHF-UCL. 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 Gene3D; 1.10.10.60; Homeodomain-like; 1. DR InterPro; IPR009057; Homeobox-like_sf. DR InterPro; IPR017970; Homeobox_CS. DR InterPro; IPR001356; Homeobox_dom. DR InterPro; IPR020479; Homeobox_metazoa. DR PANTHER; PTHR24324:SF5; HEMATOPOIETICALLY-EXPRESSED HOMEOBOX PROTEIN HHEX; 1. DR PANTHER; PTHR24324; HOMEOBOX PROTEIN HHEX; 1. DR Pfam; PF00046; Homeodomain; 1. DR PRINTS; PR00024; HOMEOBOX. DR SMART; SM00389; HOX; 1. DR SUPFAM; SSF46689; Homeodomain-like; 1. DR PROSITE; PS00027; HOMEOBOX_1; 1. DR PROSITE; PS50071; HOMEOBOX_2; 1. DR Genevisible; Q03014; HS. PE 1: Evidence at protein level; KW 3D-structure; Cytoplasm; Developmental protein; Differentiation; KW DNA-binding; Homeobox; Nucleus; Phosphoprotein; Reference proteome; KW Repressor; 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 MUTAGEN 23..24 FT /note="LL->AA: Abolishes interaction with EIF4E and FT inhibitory effect on EIF4E-mediated mRNA nuclear export." FT /evidence="ECO:0000269|PubMed:12554669" FT MUTAGEN 188 FT /note="R->A: Loss of nuclear localization; when associated FT with A-189." FT /evidence="ECO:0000269|PubMed:12554669" FT MUTAGEN 189 FT /note="R->A: Loss of nuclear localization; when associated FT with A-188." FT /evidence="ECO:0000269|PubMed:12554669" 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 //