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P27577

- ETS1_MOUSE

UniProt

P27577 - ETS1_MOUSE

Protein

Protein C-ets-1

Gene

Ets1

Organism
Mus musculus (Mouse)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
    • BLAST
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    • History
      Entry version 150 (01 Oct 2014)
      Sequence version 2 (01 Feb 1995)
      Previous versions | rss
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    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

    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. angiogenesis involved in wound healing Source: Ensembl
    2. apoptotic nuclear changes Source: Ensembl
    3. cell differentiation Source: RefGenome
    4. cell motility Source: Ensembl
    5. cellular response to hydrogen peroxide Source: Ensembl
    6. estrous cycle phase Source: Ensembl
    7. female pregnancy Source: Ensembl
    8. hypothalamus development Source: Ensembl
    9. immune system process Source: UniProtKB-KW
    10. negative regulation of cell cycle Source: Ensembl
    11. pituitary gland development Source: Ensembl
    12. PML body organization 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, DNA-templated Source: UniProtKB
    18. positive regulation of transcription from RNA polymerase II promoter Source: MGI
    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

    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

    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

    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.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. 3 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 – 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.
    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.
    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

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti28 – 281D → E in AAA63299. 1 PublicationCurated
    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. 1 PublicationCurated
    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:
    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

    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: October 1, 2014
    This is version 150 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