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Protein

ETS-related transcription factor Elf-3

Gene

ELF3

Organism
Homo sapiens (Human)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

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

GO - Biological processi

  • blastocyst development Source: Ensembl
  • epidermis development Source: UniProtKB
  • epithelial cell differentiation Source: UniProtKB
  • extracellular matrix organization Source: Ensembl
  • inflammatory response Source: UniProtKB
  • mammary gland involution Source: UniProtKB
  • multicellular organismal development Source: ProtInc
  • negative regulation of transcription, DNA-templated Source: UniProtKB
  • positive regulation of transcription, DNA-templated Source: UniProtKB
  • regulation of transcription from RNA polymerase II promoter Source: GO_Central
  • transcription from RNA polymerase II promoter Source: ProtInc
Complete GO annotation...

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 Componenti: Chromosome 1

Organism-specific databases

HGNCiHGNC:3318. ELF3.

Subcellular locationi

GO - Cellular componenti

  • cytoplasm Source: UniProtKB-SubCell
  • nucleus Source: UniProtKB
Complete GO annotation...

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.

Polymorphism and mutation databases

BioMutaiELF3.
DMDMi74739735.

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

BgeeiP78545.
CleanExiHS_ELF3.
ExpressionAtlasiP78545. baseline and differential.
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. 29 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 – 623Combined sources
Helixi64 – 663Combined sources
Helixi69 – 8214Combined sources
Turni92 – 943Combined sources
Helixi100 – 1045Combined sources
Helixi107 – 1137Combined sources
Helixi115 – 1173Combined sources
Helixi118 – 13013Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
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.
GeneTreeiENSGT00760000118996.
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. AlignAdd to basket

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

        10         20         30         40         50
MAATCEISNI FSNYFSAMYS SEDSTLASVP PAATFGADDL VLTLSNPQMS
60 70 80 90 100
LEGTEKASWL GEQPQFWSKT QVLDWISYQV EKNKYDASAI DFSRCDMDGA
110 120 130 140 150
TLCNCALEEL RLVFGPLGDQ LHAQLRDLTS SSSDELSWII ELLEKDGMAF
160 170 180 190 200
QEALDPGPFD QGSPFAQELL DDGQQASPYH PGSCGAGAPS PGSSDVSTAG
210 220 230 240 250
TGASRSSHSS DSGGSDVDLD PTDGKLFPSD GFRDCKKGDP KHGKRKRGRP
260 270 280 290 300
RKLSKEYWDC LEGKKSKHAP RGTHLWEFIR DILIHPELNE GLMKWENRHE
310 320 330 340 350
GVFKFLRSEA VAQLWGQKKK NSNMTYEKLS RAMRYYYKRE ILERVDGRRL
360 370
VYKFGKNSSG WKEEEVLQSR N
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 (Ref. 9) Curated
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:
EMBLi
GenBanki
DDBJi
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]

Keywords - Coding sequence diversityi

Alternative splicing, Polymorphism

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
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.

3D structure databases

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

Protein-protein interaction databases

BioGridi108314. 29 interactions.
IntActiP78545. 2 interactions.
STRINGi9606.ENSP00000352673.

Chemistry

ChEMBLiCHEMBL2111426.

PTM databases

PhosphoSiteiP78545.

Polymorphism and mutation databases

BioMutaiELF3.
DMDMi74739735.

Proteomic databases

MaxQBiP78545.
PaxDbiP78545.
PRIDEiP78545.

Protocols and materials databases

DNASUi1999.
Structural Biology KnowledgebaseSearch...

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]

Organism-specific databases

CTDi1999.
GeneCardsiGC01P201977.
HGNCiHGNC:3318. ELF3.
HPAiHPA003316.
HPA003479.
MIMi602191. gene.
neXtProtiNX_P78545.
PharmGKBiPA27746.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiNOG299956.
GeneTreeiENSGT00760000118996.
HOVERGENiHBG074143.
InParanoidiP78545.
KOiK09429.
OMAiQLWSKAQ.
OrthoDBiEOG7M0NRR.
PhylomeDBiP78545.
TreeFamiTF318679.

Miscellaneous databases

ChiTaRSiELF3. human.
EvolutionaryTraceiP78545.
GenomeRNAii1999.
NextBioi8087.
PROiP78545.
SOURCEiSearch...

Gene expression databases

BgeeiP78545.
CleanExiHS_ELF3.
ExpressionAtlasiP78545. baseline and differential.
GenevestigatoriP78545.

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]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  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: April 29, 2015
This is version 142 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

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into Uniref entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.