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P27577

- ETS1_MOUSE

UniProt

P27577 - ETS1_MOUSE

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Protein
Protein C-ets-1
Gene
Ets1, Ets-1
Organism
Mus musculus (Mouse)
Status
Reviewed - 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.

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
DNA bindingi335 – 41581ETS
Add
BLAST

GO - Molecular functioni

  1. DNA binding Source: UniProtKB
  2. protein binding Source: UniProtKB
  3. sequence-specific DNA binding Source: MGI
  4. sequence-specific DNA binding RNA polymerase II transcription factor activity Source: RefGenome
  5. sequence-specific DNA binding transcription factor activity Source: UniProtKB

GO - Biological processi

  1. PML body organization Source: Ensembl
  2. angiogenesis involved in wound healing Source: Ensembl
  3. apoptotic nuclear changes Source: Ensembl
  4. cell differentiation Source: RefGenome
  5. cell motility Source: Ensembl
  6. cellular response to hydrogen peroxide Source: Ensembl
  7. estrous cycle phase Source: Ensembl
  8. female pregnancy Source: Ensembl
  9. hypothalamus development Source: Ensembl
  10. immune system process Source: UniProtKB-KW
  11. negative regulation of cell cycle Source: Ensembl
  12. pituitary gland development Source: Ensembl
  13. positive regulation of angiogenesis Source: Ensembl
  14. positive regulation of cell proliferation Source: Ensembl
  15. positive regulation of endothelial cell migration Source: UniProtKB
  16. positive regulation of erythrocyte differentiation Source: UniProtKB
  17. positive regulation of transcription from RNA polymerase II promoter Source: MGI
  18. positive regulation of transcription, DNA-templated Source: UniProtKB
  19. regulation of angiogenesis Source: UniProtKB
  20. regulation of extracellular matrix disassembly Source: Ensembl
  21. regulation of transcription from RNA polymerase II promoter Source: MGI
  22. response to antibiotic Source: Ensembl
  23. response to estradiol Source: Ensembl
  24. response to hypoxia Source: Ensembl
  25. response to interleukin-1 Source: Ensembl
  26. response to laminar fluid shear stress Source: Ensembl
  27. response to mechanical stimulus Source: Ensembl
Complete GO annotation...

Keywords - Biological processi

Immunity, Transcription, Transcription regulation

Keywords - Ligandi

DNA-binding

Enzyme and pathway databases

ReactomeiREACT_188971. 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: Chromosome 9

Organism-specific databases

MGIiMGI:95455. Ets1.

Subcellular locationi

GO - Cellular componenti

  1. nucleus Source: UniProtKB
  2. 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-1
PRO_0000204070Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei8 – 81N6-acetyllysine By similarity
Modified residuei15 – 151N6-acetyllysine; alternate By similarity
Cross-linki15 – 15Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO); alternate1 Publication
Modified residuei38 – 381Phosphothreonine; by MAPK1 Publication
Modified residuei223 – 2231Phosphotyrosine By similarity
Cross-linki227 – 227Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO)1 Publication
Modified residuei270 – 2701Phosphoserine By similarity
Modified residuei285 – 2851Phosphoserine By similarity
Modified residuei305 – 3051N6-acetyllysine By 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

ArrayExpressiP27577.
BgeeiP27577.
CleanExiMM_ETS1.
GenevestigatoriP27577.

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.2 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. 3 interactions.
DIPiDIP-41848N.
IntActiP27577. 3 interactions.
MINTiMINT-194860.
STRINGi10090.ENSMUSP00000034534.

Structurei

Secondary structure

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

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
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.

Miscellaneous databases

EvolutionaryTraceiP27577.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini51 – 13686PNT
Add
BLAST

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni130 – 243114Activation domain; required for transcription activation By similarity
Add
BLAST

Sequence similaritiesi

Belongs to the ETS family.

Phylogenomic databases

eggNOGiNOG305402.
HOGENOMiHOG000285953.
HOVERGENiHBG003088.
InParanoidiP27577.
KOiK02678.
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. Align

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

MKAAVDLKPT LTIIKTEKVD LELFPSPDME CADVPLLTPS SKEMMSQALK    50
ATFSGFTKEQ QRLGIPKDPR QWTETHVRDW VMWAVNEFSL KGVDFQKFCM 100
SGAALCALGK ECFLELAPDF VGDILWEHLE ILQKEDVKPY QVNGANPTYP 150
ESCYTSDYFI SYGIEHAQCV PPSEFSEPSF ITESYQTLHP ISSEELLSLK 200
YENDYPSVIL QDPLQTDTLQ TDYFAIKQEV LTPDNMCLGR ASRGKLGGQD 250
SFESVESYDS CDRLTQSWSS QSSFNSLQRV PSYDSFDYED YPAALPNHKP 300
KGTFKDYVRD RADLNKDKPV IPAAALAGYT GSGPIQLWQF LLELLTDKSC 350
QSFISWTGDG WEFKLSDPDE VARRWGKRKN KPKMNYEKLS RGLRYYYDKN 400
IIHKTAGKRY VYRFVCDLQS LLGYTPEELH AMLDVKPDAD 440
Length:440
Mass (Da):50,202
Last modified:February 1, 1995 - v2
Checksum:i151164D83C41B143
GO

Sequence conflict

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

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
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.
KEGGimmu:23871.
UCSCiuc009osb.1. mouse. [P27577-1]

Keywords - Coding sequence diversityi

Alternative splicing

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
M58482 mRNA. Translation: AAA63299.1 .
X53953 mRNA. Translation: CAA37904.1 .
X55787 mRNA. Translation: CAA39310.1 .
BC010588 mRNA. Translation: AAH10588.1 .
CCDSi CCDS22954.1. [P27577-1 ]
PIRi A30487. A35875.
I48291.
RefSeqi NP_035938.2. NM_011808.2. [P27577-1 ]
UniGenei Mm.292415.

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
1K78 X-ray 2.25 B/F 331-440 [» ]
1K79 X-ray 2.40 A/D 331-440 [» ]
1K7A X-ray 2.80 A/D 331-440 [» ]
1MD0 X-ray 2.00 A/B 300-440 [» ]
1MDM X-ray 2.80 B 280-440 [» ]
1R36 NMR - A 301-440 [» ]
2JV3 NMR - A 29-138 [» ]
2KMD NMR - A 29-138 [» ]
DisProti DP00111.
ProteinModelPortali P27577.
SMRi P27577. Positions 29-138, 297-440.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 204765. 3 interactions.
DIPi DIP-41848N.
IntActi P27577. 3 interactions.
MINTi MINT-194860.
STRINGi 10090.ENSMUSP00000034534.

PTM databases

PhosphoSitei P27577.

Proteomic databases

MaxQBi P27577.
PRIDEi P27577.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENSMUST00000034534 ; ENSMUSP00000034534 ; ENSMUSG00000032035 . [P27577-1 ]
GeneIDi 23871.
KEGGi mmu:23871.
UCSCi uc009osb.1. mouse. [P27577-1 ]

Organism-specific databases

CTDi 2113.
MGIi MGI:95455. Ets1.

Phylogenomic databases

eggNOGi NOG305402.
HOGENOMi HOG000285953.
HOVERGENi HBG003088.
InParanoidi P27577.
KOi K02678.
OMAi DEMATQE.
OrthoDBi EOG77127T.
PhylomeDBi P27577.
TreeFami TF316214.

Enzyme and pathway databases

Reactomei REACT_188971. Oncogene Induced Senescence.

Miscellaneous databases

ChiTaRSi ETS1. mouse.
EvolutionaryTracei P27577.
NextBioi 303577.
PROi P27577.
SOURCEi Search...

Gene expression databases

ArrayExpressi P27577.
Bgeei P27577.
CleanExi MM_ETS1.
Genevestigatori P27577.

Family and domain databases

Gene3Di 1.10.10.10. 1 hit.
1.10.150.50. 1 hit.
InterProi IPR000418. Ets_dom.
IPR003118. Pointed_dom.
IPR013761. SAM/pointed.
IPR016311. Transform_prot_C-ets.
IPR011991. WHTH_DNA-bd_dom.
[Graphical view ]
Pfami PF00178. Ets. 1 hit.
PF02198. SAM_PNT. 1 hit.
[Graphical view ]
PIRSFi PIRSF001698. Transforming_factor_C-ets. 1 hit.
PRINTSi PR00454. ETSDOMAIN.
SMARTi SM00413. ETS. 1 hit.
SM00251. SAM_PNT. 1 hit.
[Graphical view ]
SUPFAMi SSF47769. SSF47769. 1 hit.
PROSITEi PS00345. ETS_DOMAIN_1. 1 hit.
PS00346. ETS_DOMAIN_2. 1 hit.
PS50061. ETS_DOMAIN_3. 1 hit.
PS51433. PNT. 1 hit.
[Graphical view ]
ProtoNeti Search...

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: September 3, 2014
This is version 149 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

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