Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Basket 0
(max 400 entries)x

Your basket is currently empty.

Select item(s) and click on "Add to basket" to create your own collection here
(400 entries max)

P14921

- ETS1_HUMAN

UniProt

P14921 - ETS1_HUMAN

Protein

Protein C-ets-1

Gene

ETS1

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
    • BLAST
    • Align
    • Format
    • Add to basket
    • History
      Entry version 166 (01 Oct 2014)
      Sequence version 1 (01 Apr 1990)
      Previous versions | rss
    • Help video
    • Feedback
    • Comment

    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.4 Publications

    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: Ensembl
    4. sequence-specific DNA binding RNA polymerase II transcription factor activity Source: RefGenome
    5. sequence-specific DNA binding transcription factor activity Source: BHF-UCL
    6. transcription factor binding Source: UniProtKB

    GO - Biological processi

    1. angiogenesis involved in wound healing Source: Ensembl
    2. cell motility Source: BHF-UCL
    3. cellular response to hydrogen peroxide Source: Ensembl
    4. estrous cycle phase Source: Ensembl
    5. female pregnancy Source: Ensembl
    6. hypothalamus development Source: Ensembl
    7. immune response Source: ProtInc
    8. negative regulation of cell cycle Source: UniProtKB
    9. negative regulation of cell proliferation Source: ProtInc
    10. pituitary gland development Source: Ensembl
    11. PML body organization Source: BHF-UCL
    12. positive regulation of angiogenesis Source: Ensembl
    13. positive regulation of cell proliferation Source: Ensembl
    14. positive regulation of cellular component movement Source: BHF-UCL
    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: BHF-UCL
    18. positive regulation of transcription from RNA polymerase II promoter Source: BHF-UCL
    19. regulation of angiogenesis Source: UniProtKB
    20. regulation of apoptotic process Source: UniProt
    21. regulation of extracellular matrix disassembly Source: Ensembl
    22. response to antibiotic Source: UniProtKB
    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
    28. transcription from RNA polymerase II promoter Source: GOC

    Keywords - Biological processi

    Immunity, Transcription, Transcription regulation

    Keywords - Ligandi

    DNA-binding

    Enzyme and pathway databases

    ReactomeiREACT_169325. Oncogene Induced Senescence.
    SignaLinkiP14921.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Protein C-ets-1
    Alternative name(s):
    p54
    Gene namesi
    Name:ETS1
    Synonyms:EWSR2
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 11

    Organism-specific databases

    HGNCiHGNC:3488. ETS1.

    Subcellular locationi

    Cytoplasm. Nucleus
    Note: Delocalizes from nucleus to cytoplasm when coexpressed with isoform Ets-1 p27.

    GO - Cellular componenti

    1. cytoplasm Source: HPA
    2. intercellular bridge Source: HPA
    3. nucleoplasm Source: Reactome
    4. nucleus Source: BHF-UCL
    5. transcription factor complex Source: Ensembl

    Keywords - Cellular componenti

    Cytoplasm, Nucleus

    Pathology & Biotechi

    Keywords - Diseasei

    Proto-oncogene

    Organism-specific databases

    Orphaneti536. Systemic lupus erythematosus.
    PharmGKBiPA27902.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 441441Protein C-ets-1PRO_0000204069Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei8 – 81N6-acetyllysine1 Publication
    Modified residuei15 – 151N6-acetyllysine; alternate1 Publication
    Cross-linki15 – 15Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO); alternateBy similarity
    Modified residuei38 – 381Phosphothreonine; by MAPKBy similarity
    Modified residuei223 – 2231Phosphotyrosine1 Publication
    Cross-linki227 – 227Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO)By similarity
    Modified residuei270 – 2701Phosphoserine1 Publication
    Modified residuei285 – 2851Phosphoserine1 Publication
    Modified residuei305 – 3051N6-acetyllysine1 Publication

    Post-translational modificationi

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

    Keywords - PTMi

    Acetylation, Isopeptide bond, Phosphoprotein, Ubl conjugation

    Proteomic databases

    MaxQBiP14921.
    PaxDbiP14921.
    PRIDEiP14921.

    PTM databases

    PhosphoSiteiP14921.

    Expressioni

    Tissue specificityi

    Highly expressed within lymphoid cells. Isoforms c-ETS-1A and Ets-1 p27 are both detected in all fetal tissues tested, but vary with tissue type in adult tissues. None is detected in brain or kidney.2 Publications

    Inductioni

    Up-regulated by retinoic acid, VEGF, TNF-alpha/TNFA, lipopolysaccharide and in response to hypoxia (at protein level).1 Publication

    Gene expression databases

    ArrayExpressiP14921.
    BgeeiP14921.
    CleanExiHS_ETS1.
    GenevestigatoriP14921.

    Organism-specific databases

    HPAiCAB002575.
    HPA042870.

    Interactioni

    Subunit structurei

    Binds DNA as a homodimer; homodimerization is required for transcription activation. Interacts with MAF and MAFB. Interacts with PAX5; the interaction alters DNA-binding properties By similarity. Interacts with DAXX. Interacts with UBE2I. Interacts with SP100; the interaction is direct and modulates ETS1 transcriptional activity.By similarity4 Publications

    Binary interactionsi

    WithEntry#Exp.IntActNotes
    APLP2Q064812EBI-913209,EBI-79306
    ARID4BQ4LE392EBI-913209,EBI-2680990
    C17orf62Q9BQA93EBI-913209,EBI-2680384
    DAXXQ9UER7-13EBI-913224,EBI-287635
    EIF5BO608412EBI-913209,EBI-928530
    Gfi1P703382EBI-913209,EBI-3954754From a different organism.
    JUNP054123EBI-913209,EBI-852823
    MAPK1P284823EBI-913209,EBI-959949
    MEIS1O004702EBI-913209,EBI-1210694
    PRKDCP785272EBI-913209,EBI-352053
    SP100P234974EBI-913209,EBI-751145
    SRSF11Q055192EBI-913209,EBI-1051785
    TAL1P175422EBI-913209,EBI-1753878

    Protein-protein interaction databases

    BioGridi108414. 39 interactions.
    IntActiP14921. 65 interactions.
    MINTiMINT-122911.
    STRINGi9606.ENSP00000376436.

    Structurei

    Secondary structure

    1
    441
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Helixi304 – 31310
    Helixi323 – 3308
    Beta strandi331 – 3333
    Helixi337 – 3459
    Helixi348 – 3503
    Turni351 – 3533
    Beta strandi354 – 3563
    Beta strandi358 – 3614
    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
    1GVJX-ray1.53A/B297-441[»]
    2NNYX-ray2.58A/B280-441[»]
    2STTNMR-A320-415[»]
    2STWNMR-A320-415[»]
    3MFKX-ray3.00A/B280-441[»]
    3RI4X-ray3.00A/D280-441[»]
    4L0YX-ray2.50B296-441[»]
    4L0ZX-ray2.70B296-441[»]
    4L18X-ray2.30B/F296-441[»]
    ProteinModelPortaliP14921.
    SMRiP14921. Positions 29-138, 297-441.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiP14921.

    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 activationAdd
    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.
    KOiK02678.
    OMAiDEMATQE.
    OrthoDBiEOG77127T.
    PhylomeDBiP14921.
    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]

    Sequences (5)i

    Sequence statusi: Complete.

    This entry describes 5 isoformsi produced by alternative splicing. Align

    Isoform c-ETS-1A (identifier: P14921-1) [UniParc]FASTAAdd to Basket

    Also known as: Ets-1 p51

    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
    NGAALCALGK DCFLELAPDF VGDILWEHLE ILQKEDVKPY QVNGVNPAYP 150
    ESRYTSDYFI SYGIEHAQCV PPSEFSEPSF ITESYQTLHP ISSEELLSLK 200
    YENDYPSVIL RDPLQTDTLQ NDYFAIKQEV VTPDNMCMGR TSRGKLGGQD 250
    SFESIESYDS CDRLTQSWSS QSSFNSLQRV PSYDSFDSED YPAALPNHKP 300
    KGTFKDYVRD RADLNKDKPV IPAAALAGYT GSGPIQLWQF LLELLTDKSC 350
    QSFISWTGDG WEFKLSDPDE VARRWGKRKN KPKMNYEKLS RGLRYYYDKN 400
    IIHKTAGKRY VYRFVCDLQS LLGYTPEELH AMLDVKPDAD E 441
    Length:441
    Mass (Da):50,408
    Last modified:April 1, 1990 - v1
    Checksum:i3B66BCC464B393FB
    GO
    Isoform c-ETS-1B (identifier: P14921-2) [UniParc]FASTAAdd to Basket

    Also known as: Ets-1 p42

    The sequence of this isoform differs from the canonical sequence as follows:
         244-330: Missing.

    Show »
    Length:354
    Mass (Da):40,786
    Checksum:i6C3313F2DBE3CF88
    GO
    Isoform 3 (identifier: P14921-3) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         1-27: MKAAVDLKPTLTIIKTEKVDLELFPSP → MSYFVDSAGS...VPTGLEHCVS

    Note: No experimental confirmation available.

    Show »
    Length:485
    Mass (Da):55,412
    Checksum:i8A6B816BAEB91149
    GO
    Isoform Ets-1 p27 (identifier: P14921-4) [UniParc]FASTAAdd to Basket

    Also known as: Ets-1Delta(III-VI)

    The sequence of this isoform differs from the canonical sequence as follows:
         28-243: Missing.

    Note: Acts as a dominant-negative for isoform c-ETS-1A.

    Show »
    Length:225
    Mass (Da):25,697
    Checksum:i5A01096FCEDE9FEA
    GO
    Isoform 5 (identifier: P14921-5) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         262-272: DRLTQSWSSQS → GQEMGKEEKQT
         273-441: Missing.

    Note: No experimental confirmation available.

    Show »
    Length:272
    Mass (Da):30,860
    Checksum:i20D7FF9557D80D46
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti162 – 1621Y → C in AAB28747. (PubMed:8231246)Curated
    Sequence conflicti236 – 2438MCMGRTSR → FLPPPLPP in AAA52409. (PubMed:2997781)Curated
    Sequence conflicti255 – 2551I → V in AAY19514. (PubMed:19377509)Curated
    Sequence conflicti332 – 3376SGPIQL → RRPPAA in AAA52409. (PubMed:2997781)Curated

    Alternative sequence

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Alternative sequencei1 – 2727MKAAV…LFPSP → MSYFVDSAGSSPVPYSAPRP AVVRQGPSNTYEDPRMNCGF QSNYHQQRPCYPFWDEMATQ EVPTGLEHCVS in isoform 3. 1 PublicationVSP_043152Add
    BLAST
    Alternative sequencei28 – 243216Missing in isoform Ets-1 p27. 1 PublicationVSP_046056Add
    BLAST
    Alternative sequencei244 – 33087Missing in isoform c-ETS-1B. CuratedVSP_001464Add
    BLAST
    Alternative sequencei262 – 27211DRLTQSWSSQS → GQEMGKEEKQT in isoform 5. 1 PublicationVSP_055485Add
    BLAST
    Alternative sequencei273 – 441169Missing in isoform 5. 1 PublicationVSP_055486Add
    BLAST

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    X14798 mRNA. Translation: CAA32904.1.
    X14798 mRNA. Translation: CAA32903.1.
    J04101 mRNA. Translation: AAA52410.1.
    X65469 Genomic DNA. No translation available.
    S67063 mRNA. Translation: AAB28747.1.
    AY943926 mRNA. Translation: AAY19514.1.
    BT019452 mRNA. Translation: AAV38259.1.
    BX640634 mRNA. Translation: CAE45783.1.
    AP001995 Genomic DNA. No translation available.
    AP003397 Genomic DNA. No translation available.
    CH471065 Genomic DNA. Translation: EAW67709.1.
    BC017314 mRNA. Translation: AAH17314.1.
    M11921 Genomic DNA. Translation: AAA52409.1.
    CCDSiCCDS44767.1. [P14921-3]
    CCDS53724.1. [P14921-4]
    CCDS8475.1. [P14921-1]
    PIRiA32066. TVHUET.
    RefSeqiNP_001137292.1. NM_001143820.1. [P14921-3]
    NP_001155894.1. NM_001162422.1. [P14921-4]
    NP_005229.1. NM_005238.3. [P14921-1]
    UniGeneiHs.369438.

    Genome annotation databases

    EnsembliENST00000319397; ENSP00000324578; ENSG00000134954. [P14921-1]
    ENST00000392668; ENSP00000376436; ENSG00000134954. [P14921-3]
    ENST00000526145; ENSP00000433500; ENSG00000134954. [P14921-2]
    ENST00000531611; ENSP00000435666; ENSG00000134954. [P14921-5]
    ENST00000535549; ENSP00000441430; ENSG00000134954. [P14921-4]
    GeneIDi2113.
    KEGGihsa:2113.
    UCSCiuc001qej.2. human. [P14921-3]
    uc010sbs.1. human. [P14921-1]

    Polymorphism databases

    DMDMi119641.

    Keywords - Coding sequence diversityi

    Alternative splicing

    Cross-referencesi

    Web resourcesi

    Atlas of Genetics and Cytogenetics in Oncology and Haematology

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    X14798 mRNA. Translation: CAA32904.1 .
    X14798 mRNA. Translation: CAA32903.1 .
    J04101 mRNA. Translation: AAA52410.1 .
    X65469 Genomic DNA. No translation available.
    S67063 mRNA. Translation: AAB28747.1 .
    AY943926 mRNA. Translation: AAY19514.1 .
    BT019452 mRNA. Translation: AAV38259.1 .
    BX640634 mRNA. Translation: CAE45783.1 .
    AP001995 Genomic DNA. No translation available.
    AP003397 Genomic DNA. No translation available.
    CH471065 Genomic DNA. Translation: EAW67709.1 .
    BC017314 mRNA. Translation: AAH17314.1 .
    M11921 Genomic DNA. Translation: AAA52409.1 .
    CCDSi CCDS44767.1. [P14921-3 ]
    CCDS53724.1. [P14921-4 ]
    CCDS8475.1. [P14921-1 ]
    PIRi A32066. TVHUET.
    RefSeqi NP_001137292.1. NM_001143820.1. [P14921-3 ]
    NP_001155894.1. NM_001162422.1. [P14921-4 ]
    NP_005229.1. NM_005238.3. [P14921-1 ]
    UniGenei Hs.369438.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    1GVJ X-ray 1.53 A/B 297-441 [» ]
    2NNY X-ray 2.58 A/B 280-441 [» ]
    2STT NMR - A 320-415 [» ]
    2STW NMR - A 320-415 [» ]
    3MFK X-ray 3.00 A/B 280-441 [» ]
    3RI4 X-ray 3.00 A/D 280-441 [» ]
    4L0Y X-ray 2.50 B 296-441 [» ]
    4L0Z X-ray 2.70 B 296-441 [» ]
    4L18 X-ray 2.30 B/F 296-441 [» ]
    ProteinModelPortali P14921.
    SMRi P14921. Positions 29-138, 297-441.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 108414. 39 interactions.
    IntActi P14921. 65 interactions.
    MINTi MINT-122911.
    STRINGi 9606.ENSP00000376436.

    PTM databases

    PhosphoSitei P14921.

    Polymorphism databases

    DMDMi 119641.

    Proteomic databases

    MaxQBi P14921.
    PaxDbi P14921.
    PRIDEi P14921.

    Protocols and materials databases

    DNASUi 2113.
    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000319397 ; ENSP00000324578 ; ENSG00000134954 . [P14921-1 ]
    ENST00000392668 ; ENSP00000376436 ; ENSG00000134954 . [P14921-3 ]
    ENST00000526145 ; ENSP00000433500 ; ENSG00000134954 . [P14921-2 ]
    ENST00000531611 ; ENSP00000435666 ; ENSG00000134954 . [P14921-5 ]
    ENST00000535549 ; ENSP00000441430 ; ENSG00000134954 . [P14921-4 ]
    GeneIDi 2113.
    KEGGi hsa:2113.
    UCSCi uc001qej.2. human. [P14921-3 ]
    uc010sbs.1. human. [P14921-1 ]

    Organism-specific databases

    CTDi 2113.
    GeneCardsi GC11M128328.
    HGNCi HGNC:3488. ETS1.
    HPAi CAB002575.
    HPA042870.
    MIMi 164720. gene.
    neXtProti NX_P14921.
    Orphaneti 536. Systemic lupus erythematosus.
    PharmGKBi PA27902.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi NOG305402.
    HOGENOMi HOG000285953.
    HOVERGENi HBG003088.
    KOi K02678.
    OMAi DEMATQE.
    OrthoDBi EOG77127T.
    PhylomeDBi P14921.
    TreeFami TF316214.

    Enzyme and pathway databases

    Reactomei REACT_169325. Oncogene Induced Senescence.
    SignaLinki P14921.

    Miscellaneous databases

    ChiTaRSi ETS1. human.
    EvolutionaryTracei P14921.
    GeneWikii ETS1.
    GenomeRNAii 2113.
    NextBioi 35465342.
    PROi P14921.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi P14921.
    Bgeei P14921.
    CleanExi HS_ETS1.
    Genevestigatori P14921.

    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. "Structure, expression and alternative splicing of the human c-ets-1 proto-oncogene."
      Reddy E.S.P., Rao V.N.
      Oncogene Res. 3:239-246(1988) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA].
    2. Cited for: NUCLEOTIDE SEQUENCE [MRNA].
    3. "Ets-1 p27: a novel Ets-1 isoform with dominant-negative effects on the transcriptional properties and the subcellular localization of Ets-1 p51."
      Laitem C., Leprivier G., Choul-Li S., Begue A., Monte D., Larsimont D., Dumont P., Duterque-Coquillaud M., Aumercier M.
      Oncogene 28:2087-2099(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM ETS-1 P27), ALTERNATIVE SPLICING, SUBCELLULAR LOCATION, TISSUE SPECIFICITY.
    4. "Cloning of human full-length CDSs in BD Creator(TM) system donor vector."
      Kalnine N., Chen X., Rolfs A., Halleck A., Hines L., Eisenstein S., Koundinya M., Raphael J., Moreira D., Kelley T., LaBaer J., Lin Y., Phelan M., Farmer A.
      Submitted (MAY-2003) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM C-ETS-1A).
    5. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 3).
      Tissue: Endometrium.
    6. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    7. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    8. "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] (ISOFORM 5).
      Tissue: Lung.
    9. Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-27.
    10. "Quantitative and qualitative variation of ETS-1 transcripts in hematologic malignancies."
      Collyn d'Hooghe M., Galiegue-Zouitina S., Szymiczek D., Lantoine D., Quief S., Loucheux-Lefebvre M.H., Kerckaert J.P.
      Leukemia 7:1777-1785(1993) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 146-174.
    11. "The ets sequence from the transforming gene of avian erythroblastosis virus, E26, has unique domains on human chromosomes 11 and 21: both loci are transcriptionally active."
      Watson D.K., McWilliams-Smith M.J., Nunn M.F., Duesberg P.H., O'Brien S.J., Papas T.S.
      Proc. Natl. Acad. Sci. U.S.A. 82:7294-7298(1985) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 236-337.
    12. "Modulation of ETS-1 transcriptional activity by huUBC9, a ubiquitin-conjugating enzyme."
      Hahn S.L., Criqui-Filipe P., Wasylyk B.
      Oncogene 15:1489-1495(1997) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH UBE2I.
    13. "EAP1/Daxx interacts with ETS1 and represses transcriptional activation of ETS1 target genes."
      Li R., Pei H., Watson D.K., Papas T.S.
      Oncogene 19:745-753(2000) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION.
    14. "Sp100 interacts with ETS-1 and stimulates its transcriptional activity."
      Wasylyk C., Schlumberger S.E., Criqui-Filipe P., Wasylyk B.
      Mol. Cell. Biol. 22:2687-2702(2002) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION AS A TRANSCRIPTIONAL ACTIVATOR, INTERACTION WITH SP100, SUBCELLULAR LOCATION, ACTIVATION DOMAIN.
    15. "SP100 expression modulates ETS1 transcriptional activity and inhibits cell invasion."
      Yordy J.S., Li R., Sementchenko V.I., Pei H., Muise-Helmericks R.C., Watson D.K.
      Oncogene 23:6654-6665(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION AS A TRANSCRIPTIONAL ACTIVATOR, INTERACTION WITH SP100.
    16. "Immunoaffinity profiling of tyrosine phosphorylation in cancer cells."
      Rush J., Moritz A., Lee K.A., Guo A., Goss V.L., Spek E.J., Zhang H., Zha X.-M., Polakiewicz R.D., Comb M.J.
      Nat. Biotechnol. 23:94-101(2005) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-223, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    17. "SP100 inhibits ETS1 activity in primary endothelial cells."
      Yordy J.S., Moussa O., Pei H., Chaussabel D., Li R., Watson D.K.
      Oncogene 24:916-931(2005) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION IN ENDOTHELIAL CELL MIGRATION, INDUCTION.
    18. "Quantitative phosphoproteomic analysis of T cell receptor signaling reveals system-wide modulation of protein-protein interactions."
      Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K., Rodionov V., Han D.K.
      Sci. Signal. 2:RA46-RA46(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-270 AND SER-285, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Leukemic T-cell.
    19. "Lysine acetylation targets protein complexes and co-regulates major cellular functions."
      Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T.C., Olsen J.V., Mann M.
      Science 325:834-840(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-8; LYS-15 AND LYS-305, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    20. "Transcription factor Ets-1 in cytokine and chemokine gene regulation."
      Russell L., Garrett-Sinha L.A.
      Cytokine 51:217-226(2010) [PubMed] [Europe PMC] [Abstract]
      Cited for: REVIEW ON FUNCTION, TISSUE SPECIFICITY.
    21. "The solution structure of the human ETS1-DNA complex reveals a novel mode of binding and true side chain intercalation."
      Werner M.H., Clore G.M., Fisher C.L., Fisher R.J., Trinh L., Shiloach J., Gronenborn A.M.
      Cell 83:761-771(1995) [PubMed] [Europe PMC] [Abstract]
      Cited for: STRUCTURE BY NMR OF 320-415.
    22. "Regulation of the transcription factor Ets-1 by DNA-mediated homo-dimerization."
      Lamber E.P., Vanhille L., Textor L.C., Kachalova G.S., Sieweke M.H., Wilmanns M.
      EMBO J. 27:2006-2017(2008) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (2.58 ANGSTROMS) OF 280-441 IN COMPLEX WITH DNA, SUBUNIT.

    Entry informationi

    Entry nameiETS1_HUMAN
    AccessioniPrimary (citable) accession number: P14921
    Secondary accession number(s): A9UL17
    , F5GYX9, Q14278, Q16080, Q6N087, Q96AC5
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: April 1, 1990
    Last sequence update: April 1, 1990
    Last modified: October 1, 2014
    This is version 166 of the entry and version 1 of the sequence. [Complete history]
    Entry statusiReviewed (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.

    Miscellaneousi

    Keywords - Technical termi

    3D-structure, Complete proteome, Reference proteome

    Documents

    1. Human chromosome 11
      Human chromosome 11: entries, gene names and cross-references to MIM
    2. MIM cross-references
      Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
    3. PDB cross-references
      Index of Protein Data Bank (PDB) cross-references
    4. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3