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P43268 (ETV4_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 123. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (6) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Alt products·Sequence annotation·Sequences·References·Web links·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
ETS translocation variant 4
Alternative name(s):
Adenovirus E1A enhancer-binding protein
E1A-F
Polyomavirus enhancer activator 3 homolog
Short name=Protein PEA3
Gene names
Name:ETV4
Synonyms:E1AF, PEA3
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length484 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Transcriptional activator that binds to the enhancer of the adenovirus E1A gene; the core-binding sequence is 5'[AC]GGA[AT]GT-3'. Ref.8

Subcellular location

Nucleus.

Post-translational modification

Sumoylated; enhanced upon ERK/MAP kinase pathway activation, it positively regulates the transcriptional activator capacity. Sumoylation at Lys-96 probably requires phosphorylation at Ser-101. Transiently polysumoylated and desumoylated by SENP1. Sumoylation is a prerequisite to polyubiquitination which in turn increases proteasomal-mediated degradation. Probably polyubiquitinated by RNF4 and deubiquitinated by USP2. Ref.8

Sequence similarities

Belongs to the ETS family.

Contains 1 ETS DNA-binding domain.

Sequence caution

The sequence AAA95991.1 differs from that shown. Reason: Erroneous initiation.

Ontologies

Keywords
   Biological processTranscription
Transcription regulation
   Cellular componentNucleus
   Coding sequence diversityAlternative splicing
Polymorphism
   LigandDNA-binding
   Molecular functionActivator
   PTMIsopeptide bond
Phosphoprotein
Ubl conjugation
   Technical term3D-structure
Complete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processbranching involved in mammary gland duct morphogenesis

Inferred from electronic annotation. Source: Ensembl

cell differentiation

Inferred from Biological aspect of Ancestor. Source: RefGenome

motor neuron axon guidance

Inferred from electronic annotation. Source: Ensembl

negative regulation of mammary gland epithelial cell proliferation

Inferred from electronic annotation. Source: Ensembl

positive regulation of transcription, DNA-templated

Inferred from electronic annotation. Source: Ensembl

regulation of branching involved in mammary gland duct morphogenesis

Inferred from electronic annotation. Source: Ensembl

regulation of transcription from RNA polymerase II promoter

Inferred from Biological aspect of Ancestor. Source: RefGenome

stem cell differentiation

Inferred from electronic annotation. Source: Ensembl

transcription from RNA polymerase II promoter

Inferred from Biological aspect of Ancestor. Source: GOC

   Cellular_componentnucleolus

Inferred from direct assay. Source: HPA

   Molecular_functionsequence-specific DNA binding

Inferred from electronic annotation. Source: InterPro

sequence-specific DNA binding RNA polymerase II transcription factor activity

Inferred from Biological aspect of Ancestor. Source: RefGenome

Complete GO annotation...

Alternative products

This entry describes 3 isoforms produced by alternative splicing. [Align] [Select]
Isoform 1 (identifier: P43268-1)

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.
Isoform 2 (identifier: P43268-2)

The sequence of this isoform differs from the canonical sequence as follows:
     1-39: Missing.
Note: No experimental confirmation available.
Isoform 3 (identifier: P43268-3)

The sequence of this isoform differs from the canonical sequence as follows:
     1-277: Missing.
Note: No experimental confirmation available.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 484484ETS translocation variant 4
PRO_0000204116

Regions

DNA binding341 – 42181ETS
Compositional bias49 – 7527Asp/Glu-rich (acidic)
Compositional bias148 – 24497Gln-rich

Amino acid modifications

Modified residue1011Phosphoserine Ref.8
Cross-link96Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO) Ref.8
Cross-link226Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO) Ref.8
Cross-link260Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO) Ref.8

Natural variations

Alternative sequence1 – 277277Missing in isoform 3.
VSP_055314
Alternative sequence1 – 3939Missing in isoform 2.
VSP_046036
Natural variant1951F → I. Ref.3
Corresponds to variant rs150119757 [ dbSNP | Ensembl ].
VAR_069110
Natural variant4371R → C.
Corresponds to variant rs34260468 [ dbSNP | Ensembl ].
VAR_048950

Experimental info

Mutagenesis961K → R: Altered sumoylation pattern. Loss of sumoylation, ubiquitination and transcriptional activator function; when associated with R-226 and R-260. Ref.8
Mutagenesis981E → A: Loss of polysumoylation and ubiquitination; when associated with A-228; A-262; A-324 and A-443. Ref.8
Mutagenesis1011S → A: Loss of sumoylation at K-96. Ref.8
Mutagenesis1011S → E: Normal sumoylation at K-96. Ref.8
Mutagenesis1021P → A: Loss of sumoylation at K-96. Ref.8
Mutagenesis2261K → R: Altered sumoylation pattern. Loss of sumoylation, ubiquitination and transcriptional activator function; when associated with R-96 and R-260. Ref.8
Mutagenesis2281E → A: Loss of polysumoylation and ubiquitination; when associated with A-98; A-262; A-324 and A-443. Ref.8
Mutagenesis2601K → R: Altered sumoylation pattern. Loss of sumoylation, ubiquitination and transcriptional activator function; when associated with R-96 and R-226. Ref.8
Mutagenesis2621E → A: Loss of polysumoylation and ubiquitination; when associated with A-98; A-228; A-324 and A-443. Ref.8
Mutagenesis3241E → A: Loss of polysumoylation and ubiquitination; when associated with A-98; A-228; A-262 and A-443. Ref.8
Mutagenesis4431E → A: Loss of polysumoylation and ubiquitination; when associated with A-98; A-228; A-262 and A-324. Ref.8
Sequence conflict24 – 274GNGS → EMSD in BAA02234. Ref.6

Secondary structure

.................. 484
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
Isoform 1 [UniParc].

Last modified April 12, 2005. Version 3.
Checksum: BA9864F3C690A8C1

FASTA48453,938
        10         20         30         40         50         60 
MERRMKAGYL DQQVPYTFSS KSPGNGSLRE ALIGPLGKLM DPGSLPPLDS EDLFQDLSHF 

        70         80         90        100        110        120 
QETWLAEAQV PDSDEQFVPD FHSENLAFHS PTTRIKKEPQ SPRTDPALSC SRKPPLPYHH 

       130        140        150        160        170        180 
GEQCLYSSAY DPPRQIAIKS PAPGALGQSP LQPFPRAEQR NFLRSSGTSQ PHPGHGYLGE 

       190        200        210        220        230        240 
HSSVFQQPLD ICHSFTSQGG GREPLPAPYQ HQLSEPCPPY PQQSFKQEYH DPLYEQAGQP 

       250        260        270        280        290        300 
AVDQGGVNGH RYPGAGVVIK QEQTDFAYDS DVTGCASMYL HTEGFSGPSP GDGAMGYGYE 

       310        320        330        340        350        360 
KPLRPFPDDV CVVPEKFEGD IKQEGVGAFR EGPPYQRRGA LQLWQFLVAL LDDPTNAHFI 

       370        380        390        400        410        420 
AWTGRGMEFK LIEPEEVARL WGIQKNRPAM NYDKLSRSLR YYYEKGIMQK VAGERYVYKF 

       430        440        450        460        470        480 
VCEPEALFSL AFPDNQRPAL KAEFDRPVSE EDTVPLSHLD ESPAYLPELA GPAQPFGPKG 


GYSY 

« Hide

Isoform 2 [UniParc].

Checksum: 391745C2ADC1C064
Show »

FASTA44549,659
Isoform 3 [UniParc].

Checksum: F06C459C28B09DF5
Show »

FASTA20723,422

References

« Hide 'large scale' references
[1]"22 genes from chromosome 17q21: cloning, sequencing, and characterization of mutations in breast cancer families and tumors."
Friedman L.S., Ostermeyer E.A., Lynch E.D., Szabo C.I., Meza J.E., Anderson L.A., Dowd P., Lee M.K., Rowell S.E., Ellison J., Boyd J., King M.-C.
Genomics 25:256-263(1995) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
[2]"Genomic organization of the human e1af gene, a member of Ets transcription factors."
Coutte L., Monte D., Baert J.-L., de Launoit Y.
Gene 240:201-207(1999) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[3]"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. expand/collapse author list , 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] (ISOFORMS 1 AND 2), VARIANT ILE-195.
Tissue: Amygdala.
[4]"DNA sequence of human chromosome 17 and analysis of rearrangement in the human lineage."
Zody M.C., Garber M., Adams D.J., Sharpe T., Harrow J., Lupski J.R., Nicholson C., Searle S.M., Wilming L., Young S.K., Abouelleil A., Allen N.R., Bi W., Bloom T., Borowsky M.L., Bugalter B.E., Butler J., Chang J.L. expand/collapse author list , Chen C.-K., Cook A., Corum B., Cuomo C.A., de Jong P.J., DeCaprio D., Dewar K., FitzGerald M., Gilbert J., Gibson R., Gnerre S., Goldstein S., Grafham D.V., Grocock R., Hafez N., Hagopian D.S., Hart E., Norman C.H., Humphray S., Jaffe D.B., Jones M., Kamal M., Khodiyar V.K., LaButti K., Laird G., Lehoczky J., Liu X., Lokyitsang T., Loveland J., Lui A., Macdonald P., Major J.E., Matthews L., Mauceli E., McCarroll S.A., Mihalev A.H., Mudge J., Nguyen C., Nicol R., O'Leary S.B., Osoegawa K., Schwartz D.C., Shaw-Smith C., Stankiewicz P., Steward C., Swarbreck D., Venkataraman V., Whittaker C.A., Yang X., Zimmer A.R., Bradley A., Hubbard T., Birren B.W., Rogers J., Lander E.S., Nusbaum C.
Nature 440:1045-1049(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[5]"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] (ISOFORMS 1 AND 3).
Tissue: Colon.
[6]"Isolation of a cDNA encoding the adenovirus E1A enhancer binding protein: a new human member of the ets oncogene family."
Higashino F., Yoshida K., Fujinaga K., Kamio K., Fujinaga K.
Nucleic Acids Res. 21:547-553(1993) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 23-484 (ISOFORM 1).
[7]"A quantitative atlas of mitotic phosphorylation."
Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E., Elledge S.J., Gygi S.P.
Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Cervix carcinoma.
[8]"Extracellular signal-regulated kinase mitogen-activated protein kinase signaling initiates a dynamic interplay between sumoylation and ubiquitination to regulate the activity of the transcriptional activator PEA3."
Guo B., Sharrocks A.D.
Mol. Cell. Biol. 29:3204-3218(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, SUMOYLATION AT LYS-96; LYS-226 AND LYS-260, DESUMOYLATION BY SENP1, PHOSPHORYLATION AT SER-101, UBIQUITINATION BY RNF4, DEUBIQUITINATION BY UPS2, MUTAGENESIS OF LYS-96; GLU-98; SER-101; PRO-102; LYS-226; GLU-228; LYS-260; GLU-262; GLU-324 AND GLU-443.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
U18018 mRNA. Translation: AAA95991.1. Different initiation.
AF095890 expand/collapse EMBL AC list , AF095887, AF095888, AF095889 Genomic DNA. Translation: AAD09186.1.
AK290429 mRNA. Translation: BAF83118.1.
AK299019 mRNA. Translation: BAH12929.1.
AK315961 mRNA. Translation: BAH14332.1.
AC068675 Genomic DNA. No translation available.
BC007242 mRNA. No translation available.
BC016623 mRNA. Translation: AAH16623.1.
D12765 mRNA. Translation: BAA02234.1.
CCDSCCDS11465.1. [P43268-1]
CCDS58553.1. [P43268-2]
PIRS35534.
RefSeqNP_001073143.1. NM_001079675.2. [P43268-1]
NP_001248366.1. NM_001261437.1. [P43268-2]
NP_001248367.1. NM_001261438.1. [P43268-2]
NP_001977.1. NM_001986.2. [P43268-1]
UniGeneHs.434059.

3D structure databases

PDBe
RCSB-PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
4CO8X-ray1.05A338-470[»]
ProteinModelPortalP43268.
SMRP43268. Positions 338-434.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid108419. 13 interactions.
DIPDIP-748N.
IntActP43268. 2 interactions.
STRING9606.ENSP00000321835.

PTM databases

PhosphoSiteP43268.

Polymorphism databases

DMDM62512145.

Proteomic databases

MaxQBP43268.
PaxDbP43268.
PRIDEP43268.

Protocols and materials databases

DNASU2118.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000319349; ENSP00000321835; ENSG00000175832. [P43268-1]
ENST00000393664; ENSP00000377273; ENSG00000175832. [P43268-1]
ENST00000538265; ENSP00000443846; ENSG00000175832. [P43268-2]
ENST00000545954; ENSP00000440023; ENSG00000175832. [P43268-2]
ENST00000591713; ENSP00000465718; ENSG00000175832. [P43268-1]
GeneID2118.
KEGGhsa:2118.
UCSCuc002idw.3. human. [P43268-1]

Organism-specific databases

CTD2118.
GeneCardsGC17M041605.
HGNCHGNC:3493. ETV4.
HPAHPA005768.
MIM600711. gene.
neXtProtNX_P43268.
Orphanet319. Ewing sarcoma.
PharmGKBPA27907.
GenAtlasSearch...

Phylogenomic databases

eggNOGNOG258471.
HOGENOMHOG000230986.
HOVERGENHBG000231.
InParanoidP43268.
KOK15592.
OMAHEVGIAS.
OrthoDBEOG7K9K2M.
PhylomeDBP43268.
TreeFamTF316214.

Enzyme and pathway databases

SignaLinkP43268.

Gene expression databases

ArrayExpressP43268.
BgeeP43268.
CleanExHS_ETV4.
GenevestigatorP43268.

Family and domain databases

Gene3D1.10.10.10. 1 hit.
InterProIPR000418. Ets_dom.
IPR006715. ETS_PEA3_N.
IPR011991. WHTH_DNA-bd_dom.
[Graphical view]
PfamPF00178. Ets. 1 hit.
PF04621. ETS_PEA3_N. 1 hit.
[Graphical view]
PRINTSPR00454. ETSDOMAIN.
SMARTSM00413. ETS. 1 hit.
[Graphical view]
PROSITEPS00345. ETS_DOMAIN_1. 1 hit.
PS00346. ETS_DOMAIN_2. 1 hit.
PS50061. ETS_DOMAIN_3. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

ChiTaRSETV4. human.
GeneWikiETV4.
GenomeRNAi2118.
NextBio8559.
PROP43268.
SOURCESearch...

Entry information

Entry nameETV4_HUMAN
AccessionPrimary (citable) accession number: P43268
Secondary accession number(s): A8K314 expand/collapse secondary AC list , B7Z5J3, B7Z9J6, Q96AW9
Entry history
Integrated into UniProtKB/Swiss-Prot: November 1, 1995
Last sequence update: April 12, 2005
Last modified: July 9, 2014
This is version 123 of the entry and version 3 of the sequence. [Complete history]
Entry statusReviewed (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.

Relevant documents

SIMILARITY comments

Index of protein domains and families

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

MIM cross-references

Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot

Human polymorphisms and disease mutations

Index of human polymorphisms and disease mutations

Human entries with polymorphisms or disease mutations

List of human entries with polymorphisms or disease mutations

Human chromosome 17

Human chromosome 17: entries, gene names and cross-references to MIM