Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Basket 0
(max 400 entries)x

Your basket is currently empty.

Select item(s) and click on "Add to basket" to create your own collection here
(400 entries max)

P78545

- ELF3_HUMAN

UniProt

P78545 - ELF3_HUMAN

Protein

ETS-related transcription factor Elf-3

Gene

ELF3

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
    • BLAST
    • Align
    • Format
    • Add to basket
    • History
      Entry version 137 (01 Oct 2014)
      Sequence version 1 (01 May 1997)
      Previous versions | rss
    • Help video
    • Feedback
    • Comment

    Functioni

    Transcriptional activator that binds and transactivates ETS sequences containing the consensus nucleotide core sequence GGA[AT]. Acts synergistically with POU2F3 to transactivate the SPRR2A promoter and with RUNX1 to transactivate the ANGPT1 promoter. Also transactivates collagenase, CCL20, CLND7, FLG, KRT8, NOS2, PTGS2, SPRR2B, TGFBR2 and TGM3 promoters. Represses KRT4 promoter activity. Involved in mediating vascular inflammation. May play an important role in epithelial cell differentiation and tumorigenesis. May be a critical downstream effector of the ERBB2 signaling pathway. May be associated with mammary gland development and involution. Plays an important role in the regulation of transcription with TATA-less promoters in preimplantation embryos, which is essential in preimplantation development By similarity.By similarity

    Regions

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    DNA bindingi273 – 35583ETSPROSITE-ProRule annotationAdd
    BLAST

    GO - Molecular functioni

    1. protein binding Source: UniProtKB
    2. sequence-specific DNA binding Source: InterPro
    3. sequence-specific DNA binding RNA polymerase II transcription factor activity Source: RefGenome
    4. sequence-specific DNA binding transcription factor activity Source: UniProtKB
    5. transcription coactivator activity Source: UniProtKB

    GO - Biological processi

    1. blastocyst development Source: Ensembl
    2. epidermis development Source: UniProtKB
    3. epithelial cell differentiation Source: UniProtKB
    4. extracellular matrix organization Source: Ensembl
    5. inflammatory response Source: UniProtKB
    6. mammary gland involution Source: UniProtKB
    7. multicellular organismal development Source: ProtInc
    8. negative regulation of transcription, DNA-templated Source: UniProtKB
    9. positive regulation of transcription, DNA-templated Source: UniProtKB
    10. positive regulation of transcription from RNA polymerase II promoter Source: Ensembl
    11. regulation of transcription from RNA polymerase II promoter Source: RefGenome
    12. transcription from RNA polymerase II promoter Source: ProtInc

    Keywords - Molecular functioni

    Activator, Developmental protein, Repressor

    Keywords - Biological processi

    Differentiation, Inflammatory response, Transcription, Transcription regulation

    Keywords - Ligandi

    DNA-binding

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    ETS-related transcription factor Elf-3
    Alternative name(s):
    E74-like factor 3
    Epithelial-restricted with serine box
    Epithelium-restricted Ets protein ESX
    Epithelium-specific Ets transcription factor 1
    Short name:
    ESE-1
    Gene namesi
    Name:ELF3Imported
    Synonyms:ERTImported, ESXImported, JEN
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 1

    Organism-specific databases

    HGNCiHGNC:3318. ELF3.

    Subcellular locationi

    Cytoplasm 3 Publications. Nucleus 3 PublicationsPROSITE-ProRule annotation
    Note: Localizes to the cytoplasm where it has been shown to transform MCF-12A mammary epithelial cells via a novel cytoplasmic mechanism. Also transiently expressed and localized to the nucleus where it induces apoptosis in non-transformed breast epithelial cells MCF-10A and MCF-12A via a transcription-dependent mechanism.3 Publications

    GO - Cellular componenti

    1. cytoplasm Source: UniProtKB-SubCell
    2. nucleus Source: UniProtKB

    Keywords - Cellular componenti

    Cytoplasm, Nucleus

    Pathology & Biotechi

    Mutagenesis

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Mutagenesisi247 – 2504RGRP → AAAA: No effect on transcriptional repression on KRT4 promoter. 1 Publication
    Mutagenesisi315 – 3151W → A: Partially abrogates repressive effect on the KRT4 promoter; when associated with A-319. 1 Publication
    Mutagenesisi319 – 3191K → A: Partially abrogates repressive effect on the KRT4 promoter; when associated with A-315. 1 Publication
    Mutagenesisi334 – 3374RYYY → AAAA: Partially abrogates repressive effect on the KRT4 promoter. 1 Publication

    Organism-specific databases

    PharmGKBiPA27746.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 371371ETS-related transcription factor Elf-3PRO_0000287681Add
    BLAST

    Proteomic databases

    MaxQBiP78545.
    PaxDbiP78545.
    PRIDEiP78545.

    PTM databases

    PhosphoSiteiP78545.

    Expressioni

    Tissue specificityi

    Expressed exclusively in tissues containing a high content of terminally differentiated epithelial cells including mammary gland, colon, trachea, kidney, prostate, uterus, stomach and skin.4 Publications

    Inductioni

    Transcriptionally regulated by ERBB2 receptor signaling in breast cancer epithelial cells. Up-regulated by phorbol 12-myristate 13-acetate (PMA) in bronchial epithelial cells. By retinoic acid in MCF-7 mammary epithelial cells (at protein level).3 Publications

    Gene expression databases

    ArrayExpressiP78545.
    BgeeiP78545.
    CleanExiHS_ELF3.
    GenevestigatoriP78545.

    Organism-specific databases

    HPAiHPA003316.
    HPA003479.

    Interactioni

    Subunit structurei

    Interacts with TBP. Interacts with CREBBP and EP300; these act as transcriptional coactivators of ELF3 and positively modulate its function. Interacts with XRCC5/KU86 and XRCC6/KU70; these inhibit the ability of ELF3 to bind DNA and negatively modulate its transcriptional activity. Associated with CLND7 and POU2F3.4 Publications

    Protein-protein interaction databases

    BioGridi108314. 24 interactions.
    IntActiP78545. 2 interactions.
    STRINGi9606.ENSP00000352673.

    Structurei

    Secondary structure

    1
    371
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Beta strandi60 – 623
    Helixi64 – 663
    Helixi69 – 8214
    Turni92 – 943
    Helixi100 – 1045
    Helixi107 – 1137
    Helixi115 – 1173
    Helixi118 – 13013

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    2E8PNMR-A48-132[»]
    ProteinModelPortaliP78545.
    SMRiP78545. Positions 48-132, 272-366.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiP78545.

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini46 – 13287PNTPROSITE-ProRule annotationAdd
    BLAST

    Motif

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Motifi137 – 14599aaTAD

    Domaini

    the 9aaTAD motif is a transactivation domain present in a large number of yeast and animal transcription factors.1 Publication

    Sequence similaritiesi

    Belongs to the ETS family.Sequence Analysis
    Contains 1 ETS DNA-binding domain.PROSITE-ProRule annotation
    Contains 1 PNT (pointed) domain.PROSITE-ProRule annotation

    Phylogenomic databases

    eggNOGiNOG299956.
    HOVERGENiHBG074143.
    InParanoidiP78545.
    KOiK09429.
    OMAiQLWSKAQ.
    OrthoDBiEOG7M0NRR.
    PhylomeDBiP78545.
    TreeFamiTF318679.

    Family and domain databases

    Gene3Di1.10.10.10. 1 hit.
    1.10.150.50. 1 hit.
    InterProiIPR017956. AT_hook_DNA-bd_motif.
    IPR000418. Ets_dom.
    IPR003118. Pointed_dom.
    IPR013761. SAM/pointed.
    IPR011991. WHTH_DNA-bd_dom.
    [Graphical view]
    PfamiPF00178. Ets. 1 hit.
    PF02198. SAM_PNT. 1 hit.
    [Graphical view]
    PRINTSiPR00454. ETSDOMAIN.
    SMARTiSM00384. AT_hook. 1 hit.
    SM00413. ETS. 1 hit.
    SM00251. SAM_PNT. 1 hit.
    [Graphical view]
    SUPFAMiSSF47769. SSF47769. 1 hit.
    PROSITEiPS50061. ETS_DOMAIN_3. 1 hit.
    PS51433. PNT. 1 hit.
    [Graphical view]

    Sequences (2)i

    Sequence statusi: Complete.

    This entry describes 2 isoformsi produced by alternative splicing. Align

    Note: Additional isoforms may exist.1 Publication

    Isoform 11 Publication (identifier: P78545-1) [UniParc]FASTAAdd to Basket

    Also known as: ESE-1b1 Publication

    This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

    « Hide

    MAATCEISNI FSNYFSAMYS SEDSTLASVP PAATFGADDL VLTLSNPQMS    50
    LEGTEKASWL GEQPQFWSKT QVLDWISYQV EKNKYDASAI DFSRCDMDGA 100
    TLCNCALEEL RLVFGPLGDQ LHAQLRDLTS SSSDELSWII ELLEKDGMAF 150
    QEALDPGPFD QGSPFAQELL DDGQQASPYH PGSCGAGAPS PGSSDVSTAG 200
    TGASRSSHSS DSGGSDVDLD PTDGKLFPSD GFRDCKKGDP KHGKRKRGRP 250
    RKLSKEYWDC LEGKKSKHAP RGTHLWEFIR DILIHPELNE GLMKWENRHE 300
    GVFKFLRSEA VAQLWGQKKK NSNMTYEKLS RAMRYYYKRE ILERVDGRRL 350
    VYKFGKNSSG WKEEEVLQSR N 371
    Length:371
    Mass (Da):41,454
    Last modified:May 1, 1997 - v1
    Checksum:i81A23A7DECBE2EF9
    GO
    Isoform 21 Publication (identifier: P78545-2) [UniParc]FASTAAdd to Basket

    Also known as: ESE-1a1 Publication

    The sequence of this isoform differs from the canonical sequence as follows:
         173-195: Missing.

    Show »
    Length:348
    Mass (Da):39,357
    Checksum:iAE2A6D3633CA305E
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti3 – 31A → T in AAM70481. (PubMed:14997048)Curated
    Sequence conflicti55 – 562EK → GE in CAD29859. (PubMed:12119107)Curated
    Sequence conflicti68 – 681S → L in AAM70481. (PubMed:14997048)Curated
    Sequence conflicti129 – 1302TS → SA in CAD29859. (PubMed:12119107)Curated
    Sequence conflicti134 – 1341D → Y in AAM70481. (PubMed:14997048)Curated
    Sequence conflicti160 – 1612DQ → GE in CAD29859. (PubMed:12119107)Curated
    Sequence conflicti201 – 2011T → A in CAD29859. (PubMed:12119107)Curated
    Sequence conflicti242 – 2421H → L in CAG33387. 1 PublicationCurated
    Sequence conflicti244 – 2441K → E in CAD97611. (PubMed:17974005)Curated
    Sequence conflicti257 – 2571Y → C in AAM70481. (PubMed:14997048)Curated
    Sequence conflicti269 – 2691A → G in CAD29859. (PubMed:12119107)Curated

    Natural variant

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti317 – 3171Q → K.
    Corresponds to variant rs1135542 [ dbSNP | Ensembl ].
    VAR_048945

    Alternative sequence

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Alternative sequencei173 – 19523Missing in isoform 2. 1 PublicationVSP_052433Add
    BLAST

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    U73843 mRNA. Translation: AAB65823.1.
    U73844 mRNA. Translation: AAB65824.1.
    U97156 mRNA. Translation: AAC51884.1.
    U66894 mRNA. Translation: AAB58075.1.
    AF016295 mRNA. Translation: AAB96586.1.
    AF017307 mRNA. Translation: AAB67238.1.
    AF110184 Genomic DNA. Translation: AAD45237.1.
    BN000001 Genomic DNA. Translation: CAD29859.1.
    AF517841 mRNA. Translation: AAM70481.1.
    CR457106 mRNA. Translation: CAG33387.1.
    AK312273 mRNA. Translation: BAG35203.1.
    BX537368 mRNA. Translation: CAD97611.1.
    AL691482 Genomic DNA. Translation: CAI14961.1.
    CH471067 Genomic DNA. Translation: EAW91389.1.
    BC003569 mRNA. Translation: AAH03569.1.
    CCDSiCCDS1419.1. [P78545-1]
    RefSeqiNP_001107781.1. NM_001114309.1. [P78545-1]
    NP_004424.3. NM_004433.4. [P78545-1]
    UniGeneiHs.603657.

    Genome annotation databases

    EnsembliENST00000359651; ENSP00000352673; ENSG00000163435. [P78545-1]
    ENST00000367283; ENSP00000356252; ENSG00000163435. [P78545-1]
    ENST00000367284; ENSP00000356253; ENSG00000163435. [P78545-1]
    GeneIDi1999.
    KEGGihsa:1999.
    UCSCiuc001gxg.4. human. [P78545-1]

    Polymorphism databases

    DMDMi74739735.

    Keywords - Coding sequence diversityi

    Alternative splicing, Polymorphism

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    U73843 mRNA. Translation: AAB65823.1 .
    U73844 mRNA. Translation: AAB65824.1 .
    U97156 mRNA. Translation: AAC51884.1 .
    U66894 mRNA. Translation: AAB58075.1 .
    AF016295 mRNA. Translation: AAB96586.1 .
    AF017307 mRNA. Translation: AAB67238.1 .
    AF110184 Genomic DNA. Translation: AAD45237.1 .
    BN000001 Genomic DNA. Translation: CAD29859.1 .
    AF517841 mRNA. Translation: AAM70481.1 .
    CR457106 mRNA. Translation: CAG33387.1 .
    AK312273 mRNA. Translation: BAG35203.1 .
    BX537368 mRNA. Translation: CAD97611.1 .
    AL691482 Genomic DNA. Translation: CAI14961.1 .
    CH471067 Genomic DNA. Translation: EAW91389.1 .
    BC003569 mRNA. Translation: AAH03569.1 .
    CCDSi CCDS1419.1. [P78545-1 ]
    RefSeqi NP_001107781.1. NM_001114309.1. [P78545-1 ]
    NP_004424.3. NM_004433.4. [P78545-1 ]
    UniGenei Hs.603657.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    2E8P NMR - A 48-132 [» ]
    ProteinModelPortali P78545.
    SMRi P78545. Positions 48-132, 272-366.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 108314. 24 interactions.
    IntActi P78545. 2 interactions.
    STRINGi 9606.ENSP00000352673.

    Chemistry

    BindingDBi P78545.
    ChEMBLi CHEMBL2111426.

    PTM databases

    PhosphoSitei P78545.

    Polymorphism databases

    DMDMi 74739735.

    Proteomic databases

    MaxQBi P78545.
    PaxDbi P78545.
    PRIDEi P78545.

    Protocols and materials databases

    DNASUi 1999.
    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000359651 ; ENSP00000352673 ; ENSG00000163435 . [P78545-1 ]
    ENST00000367283 ; ENSP00000356252 ; ENSG00000163435 . [P78545-1 ]
    ENST00000367284 ; ENSP00000356253 ; ENSG00000163435 . [P78545-1 ]
    GeneIDi 1999.
    KEGGi hsa:1999.
    UCSCi uc001gxg.4. human. [P78545-1 ]

    Organism-specific databases

    CTDi 1999.
    GeneCardsi GC01P201977.
    HGNCi HGNC:3318. ELF3.
    HPAi HPA003316.
    HPA003479.
    MIMi 602191. gene.
    neXtProti NX_P78545.
    PharmGKBi PA27746.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi NOG299956.
    HOVERGENi HBG074143.
    InParanoidi P78545.
    KOi K09429.
    OMAi QLWSKAQ.
    OrthoDBi EOG7M0NRR.
    PhylomeDBi P78545.
    TreeFami TF318679.

    Miscellaneous databases

    ChiTaRSi ELF3. human.
    EvolutionaryTracei P78545.
    GenomeRNAii 1999.
    NextBioi 8087.
    PROi P78545.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi P78545.
    Bgeei P78545.
    CleanExi HS_ELF3.
    Genevestigatori P78545.

    Family and domain databases

    Gene3Di 1.10.10.10. 1 hit.
    1.10.150.50. 1 hit.
    InterProi IPR017956. AT_hook_DNA-bd_motif.
    IPR000418. Ets_dom.
    IPR003118. Pointed_dom.
    IPR013761. SAM/pointed.
    IPR011991. WHTH_DNA-bd_dom.
    [Graphical view ]
    Pfami PF00178. Ets. 1 hit.
    PF02198. SAM_PNT. 1 hit.
    [Graphical view ]
    PRINTSi PR00454. ETSDOMAIN.
    SMARTi SM00384. AT_hook. 1 hit.
    SM00413. ETS. 1 hit.
    SM00251. SAM_PNT. 1 hit.
    [Graphical view ]
    SUPFAMi SSF47769. SSF47769. 1 hit.
    PROSITEi PS50061. ETS_DOMAIN_3. 1 hit.
    PS51433. PNT. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "Isolation and characterization of a novel epithelium-specific transcription factor, ESE-1, a member of the ets family."
      Oettgen P., Alani R.M., Barcinski M.A., Brown L., Akbarali Y., Boltax J., Kunsch C., Munger K., Libermann T.A.
      Mol. Cell. Biol. 17:4419-4433(1997) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1 AND 2), FUNCTION, ALTERNATIVE SPLICING, TISSUE SPECIFICITY.
    2. "The expression of a novel, epithelium-specific ets transcription factor is restricted to the most differentiated layers in the epidermis."
      Andreoli J.M., Jang S.-I., Chung E., Coticchia C.M., Steinert P.M., Markova N.G.
      Nucleic Acids Res. 25:4287-4295(1997) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), FUNCTION, TISSUE SPECIFICITY.
    3. "ESX: a structurally unique Ets overexpressed early during human breast tumorigenesis."
      Chang C.-H., Scott G.K., Kuo W.-L., Xiong X., Suzdaltseva Y., Park J.W., Sayre P., Erny K., Collins C., Gray J.W., Benz C.C.
      Oncogene 14:1617-1622(1997) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), FUNCTION, TISSUE SPECIFICITY.
      Tissue: PlacentaImported.
    4. "A novel epithelial-expressed ETS gene, ELF3: human and murine cDNA sequences, murine genomic organization, human mapping to 1q32.2 and expression in tissues and cancer."
      Tymms M.J., Ng A.Y.N., Thomas R.S., Schutte B.C., Zhou J., Eyre H.J., Sutherland G.R., Seth A., Rosenberg M., Papas T., Debouck C., Kola I.
      Oncogene 15:2449-2462(1997) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), FUNCTION, TISSUE SPECIFICITY.
      Tissue: Fetal lungImported.
    5. "A novel ets-related transcription factor, ERT/ESX/ESE-1, regulates expression of the transforming growth factor-beta type II receptor."
      Choi S.-G., Yi Y., Kim Y.-S., Kato M., Chang J., Chung H.-W., Hahm K.-B., Yang H.-K., Rhee H.H., Bang Y.-J., Kim S.-J.
      J. Biol. Chem. 273:110-117(1998) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), FUNCTION.
      Tissue: PlacentaImported.
    6. "Exon 4-encoded acidic domain in the epithelium-restricted Ets factor, ESX, confers potent transactivating capacity and binds to TATA-binding protein (TBP)."
      Chang C.-H., Scott G.K., Baldwin M.A., Benz C.C.
      Oncogene 18:3682-3695(1999) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] (ISOFORM 1), FUNCTION, INTERACTION WITH TBP, SUBCELLULAR LOCATION.
    7. "Human aminopeptidase B (rnpep) on chromosome 1q32.2: complementary DNA, genomic structure and expression."
      Piesse C., Tymms M., Garrafa E., Gouzy C., Lacasa M., Cadel S., Cohen P., Foulon T.
      Gene 292:129-140(2002) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] (ISOFORM 1).
    8. "Partially unspliced and fully spliced ELF3 mRNA, including a new Alu element in human breast cancer."
      Kaplan M.H., Wang X.P., Xu H.P., Dosik M.H.
      Breast Cancer Res. Treat. 83:171-187(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), ALTERNATIVE SPLICING.
      Tissue: Mammary cancer1 Publication.
    9. "Cloning of human full open reading frames in Gateway(TM) system entry vector (pDONR201)."
      Ebert L., Schick M., Neubert P., Schatten R., Henze S., Korn B.
      Submitted (JUN-2004) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
    10. "Complete sequencing and characterization of 21,243 full-length human cDNAs."
      Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.
      , Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.
      Nat. Genet. 36:40-45(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
      Tissue: Urinary bladder.
    11. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
      Tissue: Retina.
    12. "The DNA sequence and biological annotation of human chromosome 1."
      Gregory S.G., Barlow K.F., McLay K.E., Kaul R., Swarbreck D., Dunham A., Scott C.E., Howe K.L., Woodfine K., Spencer C.C.A., Jones M.C., Gillson C., Searle S., Zhou Y., Kokocinski F., McDonald L., Evans R., Phillips K.
      , Atkinson A., Cooper R., Jones C., Hall R.E., Andrews T.D., Lloyd C., Ainscough R., Almeida J.P., Ambrose K.D., Anderson F., Andrew R.W., Ashwell R.I.S., Aubin K., Babbage A.K., Bagguley C.L., Bailey J., Beasley H., Bethel G., Bird C.P., Bray-Allen S., Brown J.Y., Brown A.J., Buckley D., Burton J., Bye J., Carder C., Chapman J.C., Clark S.Y., Clarke G., Clee C., Cobley V., Collier R.E., Corby N., Coville G.J., Davies J., Deadman R., Dunn M., Earthrowl M., Ellington A.G., Errington H., Frankish A., Frankland J., French L., Garner P., Garnett J., Gay L., Ghori M.R.J., Gibson R., Gilby L.M., Gillett W., Glithero R.J., Grafham D.V., Griffiths C., Griffiths-Jones S., Grocock R., Hammond S., Harrison E.S.I., Hart E., Haugen E., Heath P.D., Holmes S., Holt K., Howden P.J., Hunt A.R., Hunt S.E., Hunter G., Isherwood J., James R., Johnson C., Johnson D., Joy A., Kay M., Kershaw J.K., Kibukawa M., Kimberley A.M., King A., Knights A.J., Lad H., Laird G., Lawlor S., Leongamornlert D.A., Lloyd D.M., Loveland J., Lovell J., Lush M.J., Lyne R., Martin S., Mashreghi-Mohammadi M., Matthews L., Matthews N.S.W., McLaren S., Milne S., Mistry S., Moore M.J.F., Nickerson T., O'Dell C.N., Oliver K., Palmeiri A., Palmer S.A., Parker A., Patel D., Pearce A.V., Peck A.I., Pelan S., Phelps K., Phillimore B.J., Plumb R., Rajan J., Raymond C., Rouse G., Saenphimmachak C., Sehra H.K., Sheridan E., Shownkeen R., Sims S., Skuce C.D., Smith M., Steward C., Subramanian S., Sycamore N., Tracey A., Tromans A., Van Helmond Z., Wall M., Wallis J.M., White S., Whitehead S.L., Wilkinson J.E., Willey D.L., Williams H., Wilming L., Wray P.W., Wu Z., Coulson A., Vaudin M., Sulston J.E., Durbin R.M., Hubbard T., Wooster R., Dunham I., Carter N.P., McVean G., Ross M.T., Harrow J., Olson M.V., Beck S., Rogers J., Bentley D.R.
      Nature 441:315-321(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    13. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    14. "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
      The MGC Project Team
      Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
      Tissue: LungImported.
    15. "Over-expression of ERT(ESX/ESE-1/ELF3), an ets-related transcription factor, induces endogenous TGF-beta type II receptor expression and restores the TGF-beta signaling pathway in Hs578t human breast cancer cells."
      Chang J., Lee C., Hahm K.-B., Yi Y., Choi S.-G., Kim S.-J.
      Oncogene 19:151-154(2000) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION.
    16. "Dual function of the epithelial specific ets transcription factor, ELF3, in modulating differentiation."
      Brembeck F.H., Opitz O.G., Libermann T.A., Rustgi A.K.
      Oncogene 19:1941-1949(2000) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, MUTAGENESIS OF 247-ARG--PRO-250; TRP-315; LYS-319 AND 334-ARG--TYR-337.
    17. "ESE-1 is a novel transcriptional mediator of inflammation that interacts with NF-kappa B to regulate the inducible nitric-oxide synthase gene."
      Rudders S., Gaspar J., Madore R., Voland C., Grall F., Patel A., Pellacani A., Perrella M.A., Libermann T.A., Oettgen P.
      J. Biol. Chem. 276:3302-3309(2001) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION.
    18. "Sequence-specific enhancer binding protein is responsible for the differential expression of ERT/ESX/ELF-3/ESE-1/jen gene in human gastric cancer cell lines: implication for the loss of TGF-beta type II receptor expression."
      Park S.H., Kim Y.S., Park B.-K., Hougaard S., Kim S.-J.
      Oncogene 20:1235-1245(2001) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION.
    19. Cited for: INDUCTION.
    20. "The epithelial-specific ETS transcription factor ESX/ESE-1/Elf-3 modulates breast cancer-associated gene expression."
      Eckel K.L., Tentler J.J., Cappetta G.J., Diamond S.E., Gutierrez-Hartmann A.
      DNA Cell Biol. 22:79-94(2003) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION.
    21. "ESE-1, an enterocyte-specific Ets transcription factor, regulates MIP-3alpha gene expression in Caco-2 human colonic epithelial cells."
      Kwon J.H., Keates S., Simeonidis S., Grall F., Libermann T.A., Keates A.C.
      J. Biol. Chem. 278:875-884(2003) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION.
    22. "Distinct functional interactions of human Skn-1 isoforms with Ese-1 during keratinocyte terminal differentiation."
      Cabral A., Fischer D.F., Vermeij W.P., Backendorf C.
      J. Biol. Chem. 278:17792-17799(2003) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, SUBUNIT.
    23. "Interplay between proximal and distal promoter elements is required for squamous differentiation marker induction in the bronchial epithelium: role for ESE-1, Sp1, and AP-1 proteins."
      Reddy S.P.M., Vuong H., Adiseshaiah P.
      J. Biol. Chem. 278:21378-21387(2003) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, INDUCTION.
    24. "ESE-1 is a novel transcriptional mediator of angiopoietin-1 expression in the setting of inflammation."
      Brown C., Gaspar J., Pettit A., Lee R., Gu X., Wang H., Manning C., Voland C., Goldring S.R., Goldring M.B., Libermann T.A., Gravallese E.M., Oettgen P.
      J. Biol. Chem. 279:12794-12803(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION.
    25. "Positive and negative modulation of the transcriptional activity of the ETS factor ESE-1 through interaction with p300, CREB-binding protein, and Ku 70/86."
      Wang H., Fang R., Cho J.-Y., Libermann T.A., Oettgen P.
      J. Biol. Chem. 279:25241-25250(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, INTERACTION WITH CREBBP; EP300; XRCC5 AND XRCC6.
    26. "The ETS transcription factor ESE-1 transforms MCF-12A human mammary epithelial cells via a novel cytoplasmic mechanism."
      Prescott J.D., Koto K.S.N., Singh M., Gutierrez-Hartmann A.
      Mol. Cell. Biol. 24:5548-5564(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, SUBCELLULAR LOCATION.
    27. "ESX induces transformation and functional epithelial to mesenchymal transition in MCF-12A mammary epithelial cells."
      Schedin P.J., Eckel-Mahan K.L., McDaniel S.M., Prescott J.D., Brodsky K.S., Tentler J.J., Gutierrez-Hartmann A.
      Oncogene 23:1766-1779(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION.
    28. "The Ets transcription factor ESE-1 mediates induction of the COX-2 gene by LPS in monocytes."
      Grall F.T., Prall W.C., Wei W., Gu X., Cho J.-Y., Choy B.K., Zerbini L.F., Inan M.S., Goldring S.R., Gravallese E.M., Goldring M.B., Oettgen P., Libermann T.A.
      FEBS J. 272:1676-1687(2005) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION.
    29. "Identification of an epithelial-specific enhancer regulating ESX expression."
      Neve R.M., Parmar H., Amend C., Chen C., Rizzino A., Benz C.C.
      Gene 367:118-125(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, INDUCTION.
    30. "Expression of claudin7 is tightly associated with epithelial structures in synovial sarcomas and regulated by an Ets family transcription factor, ELF3."
      Kohno Y., Okamoto T., Ishibe T., Nagayama S., Shima Y., Nishijo K., Shibata K.R., Fukiage K., Otsuka S., Uejima D., Araki N., Naka N., Nakashima Y., Aoyama T., Nakayama T., Nakamura T., Toguchida J.
      J. Biol. Chem. 281:38941-38950(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, SUBUNIT, SUBCELLULAR LOCATION.
    31. "Nine-amino-acid transactivation domain: establishment and prediction utilities."
      Piskacek S., Gregor M., Nemethova M., Grabner M., Kovarik P., Piskacek M.
      Genomics 89:756-768(2007) [PubMed] [Europe PMC] [Abstract]
      Cited for: DOMAIN.
    32. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    33. "Solution structure of the N-terminal SAM-domain of E74-like factor 3."
      RIKEN structural genomics initiative (RSGI)
      Submitted (JUL-2007) to the PDB data bank
      Cited for: STRUCTURE BY NMR OF 45-132.

    Entry informationi

    Entry nameiELF3_HUMAN
    AccessioniPrimary (citable) accession number: P78545
    Secondary accession number(s): B2R5Q6
    , Q6IAP8, Q7RU03, Q7Z3X2, Q8NFG2, Q99718
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: May 15, 2007
    Last sequence update: May 1, 1997
    Last modified: October 1, 2014
    This is version 137 of the entry and version 1 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programChordata Protein Annotation Program
    DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

    Miscellaneousi

    Keywords - Technical termi

    3D-structure, Complete proteome, Reference proteome

    Documents

    1. Human chromosome 1
      Human chromosome 1: entries, gene names and cross-references to MIM
    2. Human entries with polymorphisms or disease mutations
      List of human entries with polymorphisms or disease mutations
    3. Human polymorphisms and disease mutations
      Index of human polymorphisms and disease mutations
    4. MIM cross-references
      Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
    5. PDB cross-references
      Index of Protein Data Bank (PDB) cross-references
    6. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3