ID ELF5_HUMAN Reviewed; 265 AA. AC Q9UKW6; A6XAE6; A8K452; O95175; Q8N2K9; Q96QY3; Q9UKW5; DT 05-JUL-2005, integrated into UniProtKB/Swiss-Prot. DT 05-JUL-2005, sequence version 2. DT 24-JAN-2024, entry version 174. DE RecName: Full=ETS-related transcription factor Elf-5; DE AltName: Full=E74-like factor 5; DE AltName: Full=Epithelium-restricted ESE-1-related Ets factor; DE AltName: Full=Epithelium-specific Ets transcription factor 2; DE Short=ESE-2; GN Name=ELF5; Synonyms=ESE2; 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] (ISOFORMS 2 AND 4), AND TISSUE SPECIFICITY. RC TISSUE=Lung; RX PubMed=9840936; DOI=10.1038/sj.onc.1202198; RA Zhou J., Ng A.Y., Tymms M.J., Jermiin L.S., Seth A.K., Thomas R.S., RA Kola I.; RT "A novel transcription factor, ELF5, belongs to the ELF subfamily of ETS RT genes and maps to human chromosome 11p13-15, a region subject to LOH and RT rearrangement in human carcinoma cell lines."; RL Oncogene 17:2719-2732(1998). RN [2] RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1 AND 2), FUNCTION, TISSUE RP SPECIFICITY, AND ALTERNATIVE SPLICING. RX PubMed=10506207; DOI=10.1074/jbc.274.41.29439; RA Oettgen P., Kas K., Dube A., Gu X., Grall F., Thamrongsak U., Akbarali Y., RA Finger E., Boltax J., Endress G., Munger K., Kunsch C., Libermann T.A.; RT "Characterization of ESE-2, a novel ESE-1-related Ets transcription factor RT that is restricted to glandular epithelium and differentiated RT keratinocytes."; RL J. Biol. Chem. 274:29439-29452(1999). RN [3] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 3). RC TISSUE=Kidney; 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=16554811; DOI=10.1038/nature04632; RA Taylor T.D., Noguchi H., Totoki Y., Toyoda A., Kuroki Y., Dewar K., RA Lloyd C., Itoh T., Takeda T., Kim D.-W., She X., Barlow K.F., Bloom T., RA Bruford E., Chang J.L., Cuomo C.A., Eichler E., FitzGerald M.G., RA Jaffe D.B., LaButti K., Nicol R., Park H.-S., Seaman C., Sougnez C., RA Yang X., Zimmer A.R., Zody M.C., Birren B.W., Nusbaum C., Fujiyama A., RA Hattori M., Rogers J., Lander E.S., Sakaki Y.; RT "Human chromosome 11 DNA sequence and analysis including novel gene RT identification."; RL Nature 440:497-500(2006). RN [5] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RA Mural R.J., Istrail S., Sutton G.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] (ISOFORM 2). RC TISSUE=Urinary bladder; 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). CC -!- FUNCTION: Transcriptionally activator that may play a role in CC regulating the later stages of keratinocytes terminal differentiation. CC {ECO:0000269|PubMed:10506207}. CC -!- FUNCTION: Isoform 2 binds to DNA sequences containing the consensus CC nucleotide core sequence GGA[AT]. Transcriptionally activates SPRR2A CC and the parotid gland-specific PSP promoters. CC {ECO:0000269|PubMed:10506207}. CC -!- INTERACTION: CC Q9UKW6; Q9NS18: GLRX2; NbExp=3; IntAct=EBI-747605, EBI-12102178; CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000255|PROSITE-ProRule:PRU00237}. CC -!- ALTERNATIVE PRODUCTS: CC Event=Alternative splicing; Named isoforms=4; CC Name=1; Synonyms=ESE-2a; CC IsoId=Q9UKW6-1; Sequence=Displayed; CC Name=2; Synonyms=ESE-2b; CC IsoId=Q9UKW6-2; Sequence=VSP_014510; CC Name=3; CC IsoId=Q9UKW6-3; Sequence=VSP_014510, VSP_014511, VSP_014512; CC Name=4; CC IsoId=Q9UKW6-4; Sequence=VSP_014510, VSP_054662; CC -!- TISSUE SPECIFICITY: Expressed exclusively in tissues with a high CC content of epithelial cells. Highly expressed in salivary gland, CC mammary gland, kidney and prostate. Weakly expressed in placenta and CC lung. Isoform 1 and isoform 2 are differentially expressed in different CC tissues. In the kidney, only isoform 1 was expressed, while prostate CC expressed both isoforms, with levels of isoform 2 being higher. CC Expression is up-regulated during keratinocyte differentiation. Several CC epithelial carcinoma cell lines showed lack of expression. CC {ECO:0000269|PubMed:10506207, ECO:0000269|PubMed:9840936}. CC -!- DOMAIN: The PNT domain acts as a transcriptional activator. CC {ECO:0000250}. CC -!- SIMILARITY: Belongs to the ETS family. {ECO:0000305}. 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; AF049703; AAC79755.1; -; mRNA. DR EMBL; DQ123839; AAZ98848.1; -; mRNA. DR EMBL; AF115402; AAD22960.1; -; mRNA. DR EMBL; AF115403; AAD22961.1; -; mRNA. DR EMBL; AK074633; BAC11101.1; -; mRNA. DR EMBL; AK290817; BAF83506.1; -; mRNA. DR EMBL; AL137224; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; CH471064; EAW68169.1; -; Genomic_DNA. DR EMBL; BC029743; AAH29743.1; -; mRNA. DR CCDS; CCDS58129.1; -. [Q9UKW6-4] DR CCDS; CCDS7892.1; -. [Q9UKW6-1] DR CCDS; CCDS7893.1; -. [Q9UKW6-2] DR RefSeq; NP_001230009.1; NM_001243080.1. [Q9UKW6-4] DR RefSeq; NP_001230010.1; NM_001243081.1. DR RefSeq; NP_001413.1; NM_001422.3. [Q9UKW6-2] DR RefSeq; NP_938195.1; NM_198381.1. [Q9UKW6-1] DR PDB; 1WWX; NMR; -; A=172-265. DR PDBsum; 1WWX; -. DR AlphaFoldDB; Q9UKW6; -. DR SMR; Q9UKW6; -. DR BioGRID; 108316; 47. DR IntAct; Q9UKW6; 44. DR MINT; Q9UKW6; -. DR STRING; 9606.ENSP00000311010; -. DR PhosphoSitePlus; Q9UKW6; -. DR BioMuta; ELF5; -. DR DMDM; 68565549; -. DR MassIVE; Q9UKW6; -. DR PaxDb; 9606-ENSP00000311010; -. DR PeptideAtlas; Q9UKW6; -. DR ProteomicsDB; 84900; -. [Q9UKW6-1] DR Antibodypedia; 25870; 294 antibodies from 29 providers. DR DNASU; 2001; -. DR Ensembl; ENST00000257832.7; ENSP00000257832.3; ENSG00000135374.11. [Q9UKW6-2] DR Ensembl; ENST00000312319.6; ENSP00000311010.2; ENSG00000135374.11. [Q9UKW6-1] DR Ensembl; ENST00000429939.6; ENSP00000407589.2; ENSG00000135374.11. [Q9UKW6-4] DR Ensembl; ENST00000532417.1; ENSP00000436386.1; ENSG00000135374.11. [Q9UKW6-3] DR GeneID; 2001; -. DR KEGG; hsa:2001; -. DR MANE-Select; ENST00000257832.7; ENSP00000257832.3; NM_001422.4; NP_001413.1. [Q9UKW6-2] DR UCSC; uc001mvo.2; human. [Q9UKW6-1] DR AGR; HGNC:3320; -. DR CTD; 2001; -. DR DisGeNET; 2001; -. DR GeneCards; ELF5; -. DR HGNC; HGNC:3320; ELF5. DR HPA; ENSG00000135374; Group enriched (breast, salivary gland). DR MIM; 605169; gene. DR neXtProt; NX_Q9UKW6; -. DR OpenTargets; ENSG00000135374; -. DR PharmGKB; PA27748; -. DR VEuPathDB; HostDB:ENSG00000135374; -. DR eggNOG; KOG3804; Eukaryota. DR GeneTree; ENSGT00940000160980; -. DR HOGENOM; CLU_048172_1_0_1; -. DR InParanoid; Q9UKW6; -. DR OrthoDB; 3686750at2759; -. DR PhylomeDB; Q9UKW6; -. DR TreeFam; TF318679; -. DR PathwayCommons; Q9UKW6; -. DR SignaLink; Q9UKW6; -. DR BioGRID-ORCS; 2001; 9 hits in 1170 CRISPR screens. DR ChiTaRS; ELF5; human. DR EvolutionaryTrace; Q9UKW6; -. DR GeneWiki; ELF5; -. DR GenomeRNAi; 2001; -. DR Pharos; Q9UKW6; Tbio. DR PRO; PR:Q9UKW6; -. DR Proteomes; UP000005640; Chromosome 11. DR RNAct; Q9UKW6; Protein. DR Bgee; ENSG00000135374; Expressed in parotid gland and 101 other cell types or tissues. DR ExpressionAtlas; Q9UKW6; baseline and differential. DR GO; GO:0000785; C:chromatin; ISA:NTNU_SB. DR GO; GO:0005634; C:nucleus; IBA:GO_Central. DR GO; GO:0000981; F:DNA-binding transcription factor activity, RNA polymerase II-specific; ISA:NTNU_SB. DR GO; GO:1990837; F:sequence-specific double-stranded DNA binding; IDA:ARUK-UCL. DR GO; GO:0006357; P:regulation of transcription by RNA polymerase II; IBA:GO_Central. DR CDD; cd08538; SAM_PNT-ESE-2-like; 1. DR Gene3D; 1.10.150.50; Transcription Factor, Ets-1; 1. DR Gene3D; 1.10.10.10; Winged helix-like DNA-binding domain superfamily/Winged helix DNA-binding domain; 1. DR InterPro; IPR000418; Ets_dom. DR InterPro; IPR046328; ETS_fam. DR InterPro; IPR003118; Pointed_dom. DR InterPro; IPR013761; SAM/pointed_sf. DR InterPro; IPR036388; WH-like_DNA-bd_sf. DR InterPro; IPR036390; WH_DNA-bd_sf. DR PANTHER; PTHR11849; ETS; 1. DR PANTHER; PTHR11849:SF15; ETS-RELATED TRANSCRIPTION FACTOR ELF-5; 1. DR Pfam; PF00178; Ets; 1. DR Pfam; PF02198; SAM_PNT; 1. DR PRINTS; PR00454; ETSDOMAIN. DR SMART; SM00413; ETS; 1. DR SMART; SM00251; SAM_PNT; 1. DR SUPFAM; SSF47769; SAM/Pointed domain; 1. DR SUPFAM; SSF46785; Winged helix' DNA-binding domain; 1. DR PROSITE; PS00346; ETS_DOMAIN_2; 1. DR PROSITE; PS50061; ETS_DOMAIN_3; 1. DR PROSITE; PS51433; PNT; 1. DR Genevisible; Q9UKW6; HS. PE 1: Evidence at protein level; KW 3D-structure; Activator; Alternative splicing; DNA-binding; Nucleus; KW Reference proteome; Transcription; Transcription regulation. FT CHAIN 1..265 FT /note="ETS-related transcription factor Elf-5" FT /id="PRO_0000204092" FT DOMAIN 43..129 FT /note="PNT" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00762" FT DNA_BIND 173..254 FT /note="ETS" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00237" FT VAR_SEQ 1..10 FT /note="Missing (in isoform 2, isoform 3 and isoform 4)" FT /evidence="ECO:0000303|PubMed:10506207, FT ECO:0000303|PubMed:14702039, ECO:0000303|PubMed:15489334, FT ECO:0000303|PubMed:9840936" FT /id="VSP_014510" FT VAR_SEQ 51..146 FT /note="ACDSYWTSVHPEYWTKRHVWEWLQFCCDQYKLDTNCISFCNFNISGLQLCSM FT TQEEFVEAAGLCGEYLYFILQNIRTQGYSFFNDAEESKATIKDY -> D (in FT isoform 4)" FT /evidence="ECO:0000303|PubMed:9840936" FT /id="VSP_054662" FT VAR_SEQ 130..148 FT /note="YSFFNDAEESKATIKDYAD -> QCSEGQTSRGGTRIRTKQL (in FT isoform 3)" FT /evidence="ECO:0000303|PubMed:14702039" FT /id="VSP_014511" FT VAR_SEQ 149..265 FT /note="Missing (in isoform 3)" FT /evidence="ECO:0000303|PubMed:14702039" FT /id="VSP_014512" FT CONFLICT 250 FT /note="V -> M (in Ref. 2; AAD22960/AAD22961)" FT /evidence="ECO:0000305" FT HELIX 175..184 FT /evidence="ECO:0007829|PDB:1WWX" FT TURN 186..188 FT /evidence="ECO:0007829|PDB:1WWX" FT STRAND 194..197 FT /evidence="ECO:0007829|PDB:1WWX" FT TURN 198..201 FT /evidence="ECO:0007829|PDB:1WWX" FT STRAND 202..204 FT /evidence="ECO:0007829|PDB:1WWX" FT HELIX 208..218 FT /evidence="ECO:0007829|PDB:1WWX" FT HELIX 226..239 FT /evidence="ECO:0007829|PDB:1WWX" FT STRAND 240..243 FT /evidence="ECO:0007829|PDB:1WWX" FT STRAND 246..253 FT /evidence="ECO:0007829|PDB:1WWX" SQ SEQUENCE 265 AA; 31263 MW; 43821A79A45768FE CRC64; MPSLPHSHRV MLDSVTHSTF LPNASFCDPL MSWTDLFSNE EYYPAFEHQT ACDSYWTSVH PEYWTKRHVW EWLQFCCDQY KLDTNCISFC NFNISGLQLC SMTQEEFVEA AGLCGEYLYF ILQNIRTQGY SFFNDAEESK ATIKDYADSN CLKTSGIKSQ DCHSHSRTSL QSSHLWEFVR DLLLSPEENC GILEWEDREQ GIFRVVKSEA LAKMWGQRKK NDRMTYEKLS RALRYYYKTG ILERVDRRLV YKFGKNAHGW QEDKL //