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Protein

Protein C-ets-1

Gene

Ets1

Organism
Mus musculus (Mouse)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

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).By similarity

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
DNA bindingi335 – 41581ETSPROSITE-ProRule annotationAdd
BLAST

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Biological processi

Immunity, Transcription, Transcription regulation

Keywords - Ligandi

DNA-binding

Enzyme and pathway databases

ReactomeiREACT_339940. Oncogene Induced Senescence.

Names & Taxonomyi

Protein namesi
Recommended name:
Protein C-ets-1
Alternative name(s):
p54
Gene namesi
Name:Ets1
Synonyms:Ets-1
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
ProteomesiUP000000589 Componenti: Chromosome 9

Organism-specific databases

MGIiMGI:95455. Ets1.

Subcellular locationi

GO - Cellular componenti

  • cytoplasm Source: MGI
  • intercellular bridge Source: MGI
  • nucleoplasm Source: MGI
  • nucleus Source: UniProtKB
  • transcription factor complex Source: MGI
Complete GO annotation...

Keywords - Cellular componenti

Nucleus

Pathology & Biotechi

Keywords - Diseasei

Proto-oncogene

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 440440Protein C-ets-1PRO_0000204070Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei8 – 81N6-acetyllysineBy similarity
Modified residuei15 – 151N6-acetyllysine; alternateBy similarity
Cross-linki15 – 15Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO); alternate
Modified residuei38 – 381Phosphothreonine; by MAPK1 Publication
Modified residuei223 – 2231PhosphotyrosineBy similarity
Cross-linki227 – 227Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO)
Modified residuei270 – 2701PhosphoserineBy similarity
Modified residuei285 – 2851PhosphoserineBy similarity
Modified residuei305 – 3051N6-acetyllysineBy similarity

Post-translational modificationi

Sumoylated on Lys-15 and Lys-227, preferentially with SUMO2; which inhibits transcriptional activity.1 Publication
Ubiquitinated; which induces proteasomal degradation.1 Publication

Keywords - PTMi

Acetylation, Isopeptide bond, Phosphoprotein, Ubl conjugation

Proteomic databases

MaxQBiP27577.
PRIDEiP27577.

PTM databases

PhosphoSiteiP27577.

Expressioni

Gene expression databases

BgeeiP27577.
CleanExiMM_ETS1.
ExpressionAtlasiP27577. baseline and differential.
GenevisibleiP27577. MM.

Interactioni

Subunit structurei

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.By similarity3 Publications

Binary interactionsi

WithEntry#Exp.IntActNotes
TLX1P313142EBI-4289053,EBI-2820655From a different organism.
TLX3O437112EBI-4289053,EBI-3939165From a different organism.

Protein-protein interaction databases

BioGridi204765. 4 interactions.
DIPiDIP-41848N.
IntActiP27577. 3 interactions.
MINTiMINT-194860.
STRINGi10090.ENSMUSP00000034534.

Structurei

Secondary structure

1
440
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Turni39 – 424Combined sources
Helixi43 – 5210Combined sources
Helixi54 – 629Combined sources
Beta strandi67 – 693Combined sources
Helixi74 – 8815Combined sources
Turni95 – 984Combined sources
Helixi102 – 1076Combined sources
Helixi109 – 1168Combined sources
Helixi119 – 13416Combined sources
Helixi304 – 3129Combined sources
Turni313 – 3153Combined sources
Beta strandi318 – 3214Combined sources
Helixi323 – 3308Combined sources
Helixi337 – 3459Combined sources
Helixi348 – 3503Combined sources
Turni351 – 3533Combined sources
Beta strandi354 – 3563Combined sources
Beta strandi362 – 3643Combined sources
Helixi368 – 37912Combined sources
Helixi386 – 39510Combined sources
Turni396 – 4005Combined sources
Beta strandi401 – 4044Combined sources
Beta strandi408 – 4147Combined sources
Helixi418 – 4225Combined sources
Helixi426 – 4327Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
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[»]
DisProtiDP00111.
ProteinModelPortaliP27577.
SMRiP27577. Positions 29-138, 297-440.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP27577.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini51 – 13686PNTPROSITE-ProRule annotationAdd
BLAST

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni130 – 243114Activation domain; required for transcription activationBy similarityAdd
BLAST

Sequence similaritiesi

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

Phylogenomic databases

eggNOGiNOG305402.
GeneTreeiENSGT00760000118907.
HOGENOMiHOG000285953.
HOVERGENiHBG003088.
InParanoidiP27577.
OMAiDEMATQE.
OrthoDBiEOG77127T.
PhylomeDBiP27577.
TreeFamiTF316214.

Family and domain databases

Gene3Di1.10.10.10. 1 hit.
1.10.150.50. 1 hit.
InterProiIPR000418. Ets_dom.
IPR003118. Pointed_dom.
IPR013761. SAM/pointed.
IPR016311. Transform_prot_C-ets.
IPR011991. WHTH_DNA-bd_dom.
[Graphical view]
PfamiPF00178. Ets. 1 hit.
PF02198. SAM_PNT. 1 hit.
[Graphical view]
PIRSFiPIRSF001698. Transforming_factor_C-ets. 1 hit.
PRINTSiPR00454. ETSDOMAIN.
SMARTiSM00413. ETS. 1 hit.
SM00251. SAM_PNT. 1 hit.
[Graphical view]
SUPFAMiSSF47769. SSF47769. 1 hit.
PROSITEiPS00345. ETS_DOMAIN_1. 1 hit.
PS00346. ETS_DOMAIN_2. 1 hit.
PS50061. ETS_DOMAIN_3. 1 hit.
PS51433. PNT. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

This entry describes 1 isoform i produced by alternative splicing. AlignAdd to basket

Note: At least 2 isoforms are produced.

Isoform 1 (identifier: P27577-1) [UniParc]FASTAAdd to basket

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
MKAAVDLKPT LTIIKTEKVD LELFPSPDME CADVPLLTPS SKEMMSQALK
60 70 80 90 100
ATFSGFTKEQ QRLGIPKDPR QWTETHVRDW VMWAVNEFSL KGVDFQKFCM
110 120 130 140 150
SGAALCALGK ECFLELAPDF VGDILWEHLE ILQKEDVKPY QVNGANPTYP
160 170 180 190 200
ESCYTSDYFI SYGIEHAQCV PPSEFSEPSF ITESYQTLHP ISSEELLSLK
210 220 230 240 250
YENDYPSVIL QDPLQTDTLQ TDYFAIKQEV LTPDNMCLGR ASRGKLGGQD
260 270 280 290 300
SFESVESYDS CDRLTQSWSS QSSFNSLQRV PSYDSFDYED YPAALPNHKP
310 320 330 340 350
KGTFKDYVRD RADLNKDKPV IPAAALAGYT GSGPIQLWQF LLELLTDKSC
360 370 380 390 400
QSFISWTGDG WEFKLSDPDE VARRWGKRKN KPKMNYEKLS RGLRYYYDKN
410 420 430 440
IIHKTAGKRY VYRFVCDLQS LLGYTPEELH AMLDVKPDAD
Length:440
Mass (Da):50,202
Last modified:February 1, 1995 - v2
Checksum:i151164D83C41B143
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti28 – 281D → E in AAA63299 (Ref. 1) Curated
Sequence conflicti28 – 281D → E in CAA39310 (PubMed:2204020).Curated
Sequence conflicti37 – 371L → S in CAA39310 (PubMed:2204020).Curated
Sequence conflicti51 – 522AT → SY in CAA39310 (PubMed:2204020).Curated
Sequence conflicti55 – 551G → P in AAA63299 (Ref. 1) Curated
Sequence conflicti63 – 631L → R in CAA39310 (PubMed:2204020).Curated
Sequence conflicti74 – 741E → D in CAA39310 (PubMed:2204020).Curated
Sequence conflicti96 – 961Q → H in CAA39310 (PubMed:2204020).Curated
Sequence conflicti105 – 1051L → V in CAA39310 (PubMed:2204020).Curated
Sequence conflicti157 – 1571D → V in CAA39310 (PubMed:2204020).Curated
Sequence conflicti211 – 2111Q → R in CAA39310 (PubMed:2204020).Curated
Sequence conflicti217 – 2171D → E in CAA39310 (PubMed:2204020).Curated
Sequence conflicti225 – 2251A → R in CAA39310 (PubMed:2204020).Curated
Sequence conflicti234 – 2341D → N in CAA39310 (PubMed:2204020).Curated
Sequence conflicti360 – 3601G → C in CAA39310 (PubMed:2204020).Curated
Sequence conflicti383 – 3831K → S in CAA39310 (PubMed:2204020).Curated
Sequence conflicti392 – 3921G → A in CAA39310 (PubMed:2204020).Curated
Sequence conflicti408 – 4092KR → NA in CAA39310 (PubMed:2204020).Curated
Sequence conflicti413 – 4131R → A in CAA39310 (PubMed:2204020).Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M58482 mRNA. Translation: AAA63299.1.
X53953 mRNA. Translation: CAA37904.1.
X55787 mRNA. Translation: CAA39310.1.
BC010588 mRNA. Translation: AAH10588.1.
CCDSiCCDS22954.1. [P27577-1]
PIRiA30487. A35875.
I48291.
RefSeqiNP_035938.2. NM_011808.2. [P27577-1]
UniGeneiMm.292415.

Genome annotation databases

EnsembliENSMUST00000034534; ENSMUSP00000034534; ENSMUSG00000032035. [P27577-1]
GeneIDi23871.
UCSCiuc009osb.1. mouse. [P27577-1]

Keywords - Coding sequence diversityi

Alternative splicing

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M58482 mRNA. Translation: AAA63299.1.
X53953 mRNA. Translation: CAA37904.1.
X55787 mRNA. Translation: CAA39310.1.
BC010588 mRNA. Translation: AAH10588.1.
CCDSiCCDS22954.1. [P27577-1]
PIRiA30487. A35875.
I48291.
RefSeqiNP_035938.2. NM_011808.2. [P27577-1]
UniGeneiMm.292415.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
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[»]
DisProtiDP00111.
ProteinModelPortaliP27577.
SMRiP27577. Positions 29-138, 297-440.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi204765. 4 interactions.
DIPiDIP-41848N.
IntActiP27577. 3 interactions.
MINTiMINT-194860.
STRINGi10090.ENSMUSP00000034534.

PTM databases

PhosphoSiteiP27577.

Proteomic databases

MaxQBiP27577.
PRIDEiP27577.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSMUST00000034534; ENSMUSP00000034534; ENSMUSG00000032035. [P27577-1]
GeneIDi23871.
UCSCiuc009osb.1. mouse. [P27577-1]

Organism-specific databases

CTDi2113.
MGIiMGI:95455. Ets1.

Phylogenomic databases

eggNOGiNOG305402.
GeneTreeiENSGT00760000118907.
HOGENOMiHOG000285953.
HOVERGENiHBG003088.
InParanoidiP27577.
OMAiDEMATQE.
OrthoDBiEOG77127T.
PhylomeDBiP27577.
TreeFamiTF316214.

Enzyme and pathway databases

ReactomeiREACT_339940. Oncogene Induced Senescence.

Miscellaneous databases

ChiTaRSiEts1. mouse.
EvolutionaryTraceiP27577.
NextBioi303577.
PROiP27577.
SOURCEiSearch...

Gene expression databases

BgeeiP27577.
CleanExiMM_ETS1.
ExpressionAtlasiP27577. baseline and differential.
GenevisibleiP27577. MM.

Family and domain databases

Gene3Di1.10.10.10. 1 hit.
1.10.150.50. 1 hit.
InterProiIPR000418. Ets_dom.
IPR003118. Pointed_dom.
IPR013761. SAM/pointed.
IPR016311. Transform_prot_C-ets.
IPR011991. WHTH_DNA-bd_dom.
[Graphical view]
PfamiPF00178. Ets. 1 hit.
PF02198. SAM_PNT. 1 hit.
[Graphical view]
PIRSFiPIRSF001698. Transforming_factor_C-ets. 1 hit.
PRINTSiPR00454. ETSDOMAIN.
SMARTiSM00413. ETS. 1 hit.
SM00251. SAM_PNT. 1 hit.
[Graphical view]
SUPFAMiSSF47769. SSF47769. 1 hit.
PROSITEiPS00345. ETS_DOMAIN_1. 1 hit.
PS00346. ETS_DOMAIN_2. 1 hit.
PS50061. ETS_DOMAIN_3. 1 hit.
PS51433. PNT. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  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.

Entry informationi

Entry nameiETS1_MOUSE
AccessioniPrimary (citable) accession number: P27577
Secondary accession number(s): Q61403
Entry historyi
Integrated into UniProtKB/Swiss-Prot: August 1, 1992
Last sequence update: February 1, 1995
Last modified: July 22, 2015
This is version 159 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

Documents

  1. MGD cross-references
    Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
  2. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  3. 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.