ELF5_HUMAN
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 03-AUG-2022, entry version 166.
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}.
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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; Q9UKW6; -.
DR PeptideAtlas; Q9UKW6; -.
DR PRIDE; Q9UKW6; -.
DR ProteomicsDB; 84900; -. [Q9UKW6-1]
DR Antibodypedia; 25870; 268 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 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 PhylomeDB; Q9UKW6; -.
DR TreeFam; TF318679; -.
DR PathwayCommons; Q9UKW6; -.
DR SignaLink; Q9UKW6; -.
DR BioGRID-ORCS; 2001; 9 hits in 1092 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 tissues.
DR ExpressionAtlas; Q9UKW6; baseline and differential.
DR Genevisible; Q9UKW6; HS.
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:0030154; P:cell differentiation; IBA:GO_Central.
DR GO; GO:0006357; P:regulation of transcription by RNA polymerase II; IBA:GO_Central.
DR Gene3D; 1.10.10.10; -; 1.
DR Gene3D; 1.10.150.50; -; 1.
DR InterPro; IPR033069; Elf5.
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; PTHR11849; 1.
DR PANTHER; PTHR11849:SF15; PTHR11849:SF15; 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; SSF46785; SSF46785; 1.
DR SUPFAM; SSF47769; SSF47769; 1.
DR PROSITE; PS00346; ETS_DOMAIN_2; 1.
DR PROSITE; PS50061; ETS_DOMAIN_3; 1.
DR PROSITE; PS51433; PNT; 1.
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
