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Database: UniProt
Entry: Q9UKW6
LinkDB: Q9UKW6
Original site: Q9UKW6 
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   07-OCT-2020, entry version 158.
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}.
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   SMR; Q9UKW6; -.
DR   BioGRID; 108316; 9.
DR   IntAct; Q9UKW6; 7.
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; 1759; -.
DR   ProteomicsDB; 84900; -. [Q9UKW6-1]
DR   ProteomicsDB; 84901; -. [Q9UKW6-2]
DR   ProteomicsDB; 84902; -. [Q9UKW6-3]
DR   Antibodypedia; 25870; 248 antibodies.
DR   DNASU; 2001; -.
DR   Ensembl; ENST00000257832; ENSP00000257832; ENSG00000135374. [Q9UKW6-2]
DR   Ensembl; ENST00000312319; ENSP00000311010; ENSG00000135374. [Q9UKW6-1]
DR   Ensembl; ENST00000429939; ENSP00000407589; ENSG00000135374. [Q9UKW6-4]
DR   Ensembl; ENST00000532417; ENSP00000436386; ENSG00000135374. [Q9UKW6-3]
DR   GeneID; 2001; -.
DR   KEGG; hsa:2001; -.
DR   UCSC; uc001mvo.2; human. [Q9UKW6-1]
DR   CTD; 2001; -.
DR   DisGeNET; 2001; -.
DR   EuPathDB; HostDB:ENSG00000135374.9; -.
DR   GeneCards; ELF5; -.
DR   HGNC; HGNC:3320; ELF5.
DR   HPA; ENSG00000135374; Group enriched (breast, ductus deferens, salivary gland, seminal vesicle).
DR   MIM; 605169; gene.
DR   neXtProt; NX_Q9UKW6; -.
DR   OpenTargets; ENSG00000135374; -.
DR   PharmGKB; PA27748; -.
DR   eggNOG; KOG3804; Eukaryota.
DR   GeneTree; ENSGT00940000160980; -.
DR   HOGENOM; CLU_048172_1_0_1; -.
DR   InParanoid; Q9UKW6; -.
DR   KO; K17101; -.
DR   OMA; NCLKASG; -.
DR   PhylomeDB; Q9UKW6; -.
DR   TreeFam; TF318679; -.
DR   PathwayCommons; Q9UKW6; -.
DR   BioGRID-ORCS; 2001; 4 hits in 894 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 thoracic mammary gland and 107 other tissues.
DR   ExpressionAtlas; Q9UKW6; baseline and differential.
DR   Genevisible; Q9UKW6; HS.
DR   GO; GO:0005737; C:cytoplasm; IEA:Ensembl.
DR   GO; GO:0042025; C:host cell nucleus; IEA:InterPro.
DR   GO; GO:0000790; C:nuclear chromatin; ISA:NTNU_SB.
DR   GO; GO:0005634; C:nucleus; IBA:GO_Central.
DR   GO; GO:0001228; F:DNA-binding transcription activator activity, RNA polymerase II-specific; IEA:Ensembl.
DR   GO; GO:0000981; F:DNA-binding transcription factor activity, RNA polymerase II-specific; ISA:NTNU_SB.
DR   GO; GO:0000977; F:RNA polymerase II transcription regulatory region sequence-specific DNA binding; IEA:Ensembl.
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:0001712; P:ectodermal cell fate commitment; IEA:Ensembl.
DR   GO; GO:0060644; P:mammary gland epithelial cell differentiation; IEA:Ensembl.
DR   GO; GO:0045596; P:negative regulation of cell differentiation; IEA:Ensembl.
DR   GO; GO:0006357; P:regulation of transcription by RNA polymerase II; IBA:GO_Central.
DR   GO; GO:0035019; P:somatic stem cell population maintenance; IEA:Ensembl.
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; 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: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:0000244|PDB:1WWX"
FT   TURN            186..188
FT                   /evidence="ECO:0000244|PDB:1WWX"
FT   STRAND          194..197
FT                   /evidence="ECO:0000244|PDB:1WWX"
FT   TURN            198..201
FT                   /evidence="ECO:0000244|PDB:1WWX"
FT   STRAND          202..204
FT                   /evidence="ECO:0000244|PDB:1WWX"
FT   HELIX           208..218
FT                   /evidence="ECO:0000244|PDB:1WWX"
FT   HELIX           226..239
FT                   /evidence="ECO:0000244|PDB:1WWX"
FT   STRAND          240..243
FT                   /evidence="ECO:0000244|PDB:1WWX"
FT   STRAND          246..253
FT                   /evidence="ECO:0000244|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
//
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