Skip Header

You are using a version of Internet Explorer that may not display all features of this website. Please upgrade to a modern browser.
Contribute Send feedback
Read comments (?) or add your own

P27577 (ETS1_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 148. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Interactions·Alt products·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Protein C-ets-1
Alternative name(s):
p54
Gene names
Name:Ets1
Synonyms:Ets-1
OrganismMus musculus (Mouse) [Reference proteome]
Taxonomic identifier10090 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus

Protein attributes

Sequence length440 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Transcription factor. Directly controls the expression of cytokine and chemokine genes in a wide variety of different cellular contexts. May control the differentiation, survival and proliferation of lymphoid cells. May also regulate angiogenesis through regulation of expression of genes controlling endothelial cell migration and invasion By similarity.

Subunit structure

Binds DNA as a homodimer; homodimerization is required for transcription activation. Interacts with DAXX By similarity. Interacts with UBE2I By similarity. Interacts with SP100; the interaction is direct and modulates ETS1 transcriptional activity By similarity. Interacts with MAF and MAFB. Interacts with PAX5; the interaction alters DNA-binding properties. Ref.5 Ref.6

Subcellular location

Nucleus.

Post-translational modification

Sumoylated on Lys-15 and Lys-227, preferentially with SUMO2; which inhibits transcriptional activity. Ref.7

Ubiquitinated; which induces proteasomal degradation. Ref.7

Sequence similarities

Belongs to the ETS family.

Contains 1 ETS DNA-binding domain.

Contains 1 PNT (pointed) domain.

Ontologies

Keywords
   Biological processImmunity
Transcription
Transcription regulation
   Cellular componentNucleus
   Coding sequence diversityAlternative splicing
   DiseaseProto-oncogene
   LigandDNA-binding
   PTMAcetylation
Isopeptide bond
Phosphoprotein
Ubl conjugation
   Technical term3D-structure
Complete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processPML body organization

Inferred from electronic annotation. Source: Ensembl

angiogenesis involved in wound healing

Inferred from electronic annotation. Source: Ensembl

apoptotic nuclear changes

Inferred from electronic annotation. Source: Ensembl

cell differentiation

Inferred from Biological aspect of Ancestor. Source: RefGenome

cell motility

Inferred from electronic annotation. Source: Ensembl

cellular response to hydrogen peroxide

Inferred from electronic annotation. Source: Ensembl

estrous cycle phase

Inferred from electronic annotation. Source: Ensembl

female pregnancy

Inferred from electronic annotation. Source: Ensembl

hypothalamus development

Inferred from electronic annotation. Source: Ensembl

immune system process

Inferred from electronic annotation. Source: UniProtKB-KW

negative regulation of cell cycle

Inferred from electronic annotation. Source: Ensembl

pituitary gland development

Inferred from electronic annotation. Source: Ensembl

positive regulation of angiogenesis

Inferred from electronic annotation. Source: Ensembl

positive regulation of cell proliferation

Inferred from electronic annotation. Source: Ensembl

positive regulation of endothelial cell migration

Inferred from sequence or structural similarity. Source: UniProtKB

positive regulation of erythrocyte differentiation

Inferred from sequence or structural similarity. Source: UniProtKB

positive regulation of transcription from RNA polymerase II promoter

Inferred from direct assay PubMed 12464608. Source: MGI

positive regulation of transcription, DNA-templated

Inferred from sequence or structural similarity. Source: UniProtKB

regulation of angiogenesis

Inferred from sequence or structural similarity. Source: UniProtKB

regulation of extracellular matrix disassembly

Inferred from electronic annotation. Source: Ensembl

regulation of transcription from RNA polymerase II promoter

Inferred from direct assay PubMed 15541767. Source: MGI

response to antibiotic

Inferred from electronic annotation. Source: Ensembl

response to estradiol

Inferred from electronic annotation. Source: Ensembl

response to hypoxia

Inferred from electronic annotation. Source: Ensembl

response to interleukin-1

Inferred from electronic annotation. Source: Ensembl

response to laminar fluid shear stress

Inferred from electronic annotation. Source: Ensembl

response to mechanical stimulus

Inferred from electronic annotation. Source: Ensembl

   Cellular_componentnucleus

Inferred from sequence or structural similarity. Source: UniProtKB

transcription factor complex

Inferred from direct assay PubMed 12464608. Source: MGI

   Molecular_functionDNA binding

Inferred from direct assay PubMed 7774816. Source: UniProtKB

protein binding

Inferred from physical interaction PubMed 7774816PubMed 9199349. Source: UniProtKB

sequence-specific DNA binding

Inferred from direct assay PubMed 1409581. Source: MGI

sequence-specific DNA binding RNA polymerase II transcription factor activity

Inferred from Biological aspect of Ancestor. Source: RefGenome

sequence-specific DNA binding transcription factor activity

Inferred from sequence or structural similarity. Source: UniProtKB

Complete GO annotation...

Binary interactions

With

Entry

#Exp.

IntAct

Notes

TLX1P313142EBI-4289053,EBI-2820655From a different organism.
TLX3O437112EBI-4289053,EBI-3939165From a different organism.

Alternative products

This entry describes 1 isoform produced by alternative splicing. [Select]

Note: At least 2 isoforms are produced.
Isoform 1 (identifier: P27577-1)

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.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 440440Protein C-ets-1
PRO_0000204070

Regions

Domain51 – 13686PNT
DNA binding335 – 41581ETS
Region130 – 243114Activation domain; required for transcription activation By similarity

Amino acid modifications

Modified residue81N6-acetyllysine By similarity
Modified residue151N6-acetyllysine; alternate By similarity
Modified residue381Phosphothreonine; by MAPK Ref.8
Modified residue2231Phosphotyrosine By similarity
Modified residue2701Phosphoserine By similarity
Modified residue2851Phosphoserine By similarity
Modified residue3051N6-acetyllysine By similarity
Cross-link15Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO); alternate Ref.7
Cross-link227Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO) Ref.7

Experimental info

Sequence conflict281D → E in AAA63299. Ref.1
Sequence conflict281D → E in CAA39310. Ref.3
Sequence conflict371L → S in CAA39310. Ref.3
Sequence conflict51 – 522AT → SY in CAA39310. Ref.3
Sequence conflict551G → P in AAA63299. Ref.1
Sequence conflict631L → R in CAA39310. Ref.3
Sequence conflict741E → D in CAA39310. Ref.3
Sequence conflict961Q → H in CAA39310. Ref.3
Sequence conflict1051L → V in CAA39310. Ref.3
Sequence conflict1571D → V in CAA39310. Ref.3
Sequence conflict2111Q → R in CAA39310. Ref.3
Sequence conflict2171D → E in CAA39310. Ref.3
Sequence conflict2251A → R in CAA39310. Ref.3
Sequence conflict2341D → N in CAA39310. Ref.3
Sequence conflict3601G → C in CAA39310. Ref.3
Sequence conflict3831K → S in CAA39310. Ref.3
Sequence conflict3921G → A in CAA39310. Ref.3
Sequence conflict408 – 4092KR → NA in CAA39310. Ref.3
Sequence conflict4131R → A in CAA39310. Ref.3

Secondary structure

............................................. 440
Helix Strand Turn

Details...

Sequences

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

Last modified February 1, 1995. Version 2.
Checksum: 151164D83C41B143

FASTA44050,202
        10         20         30         40         50         60 
MKAAVDLKPT LTIIKTEKVD LELFPSPDME CADVPLLTPS SKEMMSQALK ATFSGFTKEQ 

        70         80         90        100        110        120 
QRLGIPKDPR QWTETHVRDW VMWAVNEFSL KGVDFQKFCM SGAALCALGK ECFLELAPDF 

       130        140        150        160        170        180 
VGDILWEHLE ILQKEDVKPY QVNGANPTYP ESCYTSDYFI SYGIEHAQCV PPSEFSEPSF 

       190        200        210        220        230        240 
ITESYQTLHP ISSEELLSLK YENDYPSVIL QDPLQTDTLQ TDYFAIKQEV LTPDNMCLGR 

       250        260        270        280        290        300 
ASRGKLGGQD SFESVESYDS CDRLTQSWSS QSSFNSLQRV PSYDSFDYED YPAALPNHKP 

       310        320        330        340        350        360 
KGTFKDYVRD RADLNKDKPV IPAAALAGYT GSGPIQLWQF LLELLTDKSC QSFISWTGDG 

       370        380        390        400        410        420 
WEFKLSDPDE VARRWGKRKN KPKMNYEKLS RGLRYYYDKN IIHKTAGKRY VYRFVCDLQS 

       430        440 
LLGYTPEELH AMLDVKPDAD 

« Hide

References

« Hide 'large scale' references
[1]"The chicken, mouse and human ETS-1 proteins all have predicted masses of 50 kDa, but have different electrophoretic mobilities."
Watson D.K., Seth A., Smyth F.E., Schweinfest C.W., Papas T.S.
(In) Papas T.S. (eds.); Oncogenesis, pp.221-232, Gulf Publishing Company, Houston (1990)
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
Strain: BALB/c.
Tissue: Fibroblast.
[2]"Sequence-specific DNA binding of the proto-oncoprotein ets-1 defines a transcriptional activator sequence within the long terminal repeat of the Moloney murine sarcoma virus."
Gunther C.V., Nye J.A., Bryner R.S., Graves B.J.
Genes Dev. 4:667-679(1990) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
Strain: BALB/c.
Tissue: Thymus.
[3]"Cloning, sequencing, and expression of mouse c-ets-1 cDNA in baculovirus expression system."
Chen J.H.
Oncogene Res. 5:277-285(1990) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
Strain: BALB/c.
Tissue: Thymus.
[4]"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].
Strain: Czech II.
Tissue: Mammary gland.
[5]"c-Maf interacts with c-Myb to regulate transcription of an early myeloid gene during differentiation."
Hedge S.P., Kumar A., Kurschner C., Shapiro L.H.
Mol. Cell. Biol. 18:2729-2737(1998) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH MAF.
[6]"MafB is an inducer of monocytic differentiation."
Kelly L.M., Englmeier U., Lafon I., Sieweke M.H., Graf T.
EMBO J. 19:1987-1997(2000) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH MAFB.
[7]"Regulation of the Ets-1 transcription factor by sumoylation and ubiquitinylation."
Ji Z., Degerny C., Vintonenko N., Deheuninck J., Foveau B., Leroy C., Coll J., Tulasne D., Baert J.-L., Fafeur V.
Oncogene 26:395-406(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: SUMOYLATION AT LYS-15 AND LYS-227, UBIQUITINATION.
[8]"Structure of the ets-1 pointed domain and mitogen-activated protein kinase phosphorylation site."
Slupsky C.M., Gentile L.N., Donaldson L.W., Mackereth C.D., Seidel J.J., Graves B.J., McIntosh L.P.
Proc. Natl. Acad. Sci. U.S.A. 95:12129-12134(1998) [PubMed] [Europe PMC] [Abstract]
Cited for: STRUCTURE BY NMR OF 29-138, PHOSPHORYLATION AT THR-38.
[9]"Solution structure of the ETS domain from murine Ets-1: a winged helix-turn-helix DNA binding motif."
Donaldson L.W., Petersen J.M., Graves B.J., McIntosh L.P.
EMBO J. 15:125-134(1996) [PubMed] [Europe PMC] [Abstract]
Cited for: STRUCTURE BY NMR OF 332-415.
[10]"Structural studies of Ets-1/Pax5 complex formation on DNA."
Garvie C.W., Hagman J., Wolberger C.
Mol. Cell 8:1267-1276(2001) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.25 ANGSTROMS) OF 331-440 IN COMPLEX WITH HUMAN PAX5 AND DNA.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
M58482 mRNA. Translation: AAA63299.1.
X53953 mRNA. Translation: CAA37904.1.
X55787 mRNA. Translation: CAA39310.1.
BC010588 mRNA. Translation: AAH10588.1.
CCDSCCDS22954.1. [P27577-1]
PIRA35875. A30487.
I48291.
RefSeqNP_035938.2. NM_011808.2. [P27577-1]
UniGeneMm.292415.

3D structure databases

PDBe
RCSB-PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
1K78X-ray2.25B/F331-440[»]
1K79X-ray2.40A/D331-440[»]
1K7AX-ray2.80A/D331-440[»]
1MD0X-ray2.00A/B300-440[»]
1MDMX-ray2.80B280-440[»]
1R36NMR-A301-440[»]
2JV3NMR-A29-138[»]
2KMDNMR-A29-138[»]
DisProtDP00111.
ProteinModelPortalP27577.
SMRP27577. Positions 29-138, 297-440.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid204765. 3 interactions.
DIPDIP-41848N.
IntActP27577. 3 interactions.
MINTMINT-194860.
STRING10090.ENSMUSP00000034534.

PTM databases

PhosphoSiteP27577.

Proteomic databases

MaxQBP27577.
PRIDEP27577.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENSMUST00000034534; ENSMUSP00000034534; ENSMUSG00000032035. [P27577-1]
GeneID23871.
KEGGmmu:23871.
UCSCuc009osb.1. mouse. [P27577-1]

Organism-specific databases

CTD2113.
MGIMGI:95455. Ets1.

Phylogenomic databases

eggNOGNOG305402.
HOGENOMHOG000285953.
HOVERGENHBG003088.
InParanoidP27577.
KOK02678.
OMADEMATQE.
OrthoDBEOG77127T.
PhylomeDBP27577.
TreeFamTF316214.

Gene expression databases

ArrayExpressP27577.
BgeeP27577.
CleanExMM_ETS1.
GenevestigatorP27577.

Family and domain databases

Gene3D1.10.10.10. 1 hit.
1.10.150.50. 1 hit.
InterProIPR000418. Ets_dom.
IPR003118. Pointed_dom.
IPR013761. SAM/pointed.
IPR016311. Transform_prot_C-ets.
IPR011991. WHTH_DNA-bd_dom.
[Graphical view]
PfamPF00178. Ets. 1 hit.
PF02198. SAM_PNT. 1 hit.
[Graphical view]
PIRSFPIRSF001698. Transforming_factor_C-ets. 1 hit.
PRINTSPR00454. ETSDOMAIN.
SMARTSM00413. ETS. 1 hit.
SM00251. SAM_PNT. 1 hit.
[Graphical view]
SUPFAMSSF47769. SSF47769. 1 hit.
PROSITEPS00345. ETS_DOMAIN_1. 1 hit.
PS00346. ETS_DOMAIN_2. 1 hit.
PS50061. ETS_DOMAIN_3. 1 hit.
PS51433. PNT. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

ChiTaRSETS1. mouse.
EvolutionaryTraceP27577.
NextBio303577.
PROP27577.
SOURCESearch...

Entry information

Entry nameETS1_MOUSE
AccessionPrimary (citable) accession number: P27577
Secondary accession number(s): Q61403
Entry history
Integrated into UniProtKB/Swiss-Prot: August 1, 1992
Last sequence update: February 1, 1995
Last modified: July 9, 2014
This is version 148 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

MGD cross-references

Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot