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P78545

- ELF3_HUMAN

UniProt

P78545 - ELF3_HUMAN

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Protein
ETS-related transcription factor Elf-3
Gene
ELF3, ERT, ESX, JEN
Organism
Homo sapiens (Human)
Status
Reviewed - 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.21 Publications

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
DNA bindingi273 – 35583ETS
Add
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 from RNA polymerase II promoter Source: Ensembl
  10. positive regulation of transcription, DNA-templated Source: UniProtKB
  11. regulation of transcription from RNA polymerase II promoter Source: RefGenome
  12. 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:ELF3
Synonyms:ERT, ESX, JEN
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640: Chromosome 1

Organism-specific databases

HGNCiHGNC:3318. ELF3.

Subcellular locationi

Cytoplasm. Nucleus
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
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.

PTM / Processingi

Molecule processing

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

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.

Miscellaneous databases

EvolutionaryTraceiP78545.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini46 – 13287PNT
Add
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.

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.

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

Also known as: ESE-1b

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-1a

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

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 Publication
VSP_052433Add
BLAST

Sequence conflict

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

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

« 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: Placenta.
  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 lung.
  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: Placenta.
  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 cancer.
  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: Lung.
  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: July 9, 2014
This is version 136 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

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