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P14921

- ETS1_HUMAN

UniProt

P14921 - ETS1_HUMAN

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Protein

Protein C-ets-1

Gene

ETS1

Organism
Homo sapiens (Human)
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.4 Publications

Regions

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

GO - Molecular functioni

  1. DNA binding Source: UniProtKB
  2. sequence-specific DNA binding Source: Ensembl
  3. sequence-specific DNA binding RNA polymerase II transcription factor activity Source: RefGenome
  4. sequence-specific DNA binding transcription factor activity Source: BHF-UCL
  5. 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
Complete GO annotation...

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
Complete GO annotation...

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

BgeeiP14921.
CleanExiHS_ETS1.
ExpressionAtlasiP14921. baseline and differential.
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
RFWD2Q8NHY23EBI-913224,EBI-1176214
SP100P234974EBI-913209,EBI-751145
SRCP129312EBI-913224,EBI-621482
SRSF11Q055192EBI-913209,EBI-1051785
TAL1P175422EBI-913209,EBI-1753878

Protein-protein interaction databases

BioGridi108414. 40 interactions.
IntActiP14921. 67 interactions.
MINTiMINT-122911.
STRINGi9606.ENSP00000376436.

Structurei

Secondary structure

1
441
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi304 – 31310Combined sources
Helixi323 – 3308Combined sources
Beta strandi331 – 3344Combined sources
Helixi337 – 3459Combined sources
Helixi348 – 3503Combined sources
Turni351 – 3533Combined sources
Beta strandi354 – 3563Combined sources
Beta strandi358 – 3614Combined 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
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[»]
3WTSX-ray2.35C/H276-441[»]
3WTTX-ray2.35C/H276-441[»]
3WTUX-ray2.70C/H276-441[»]
3WTVX-ray2.70C/H276-441[»]
3WTWX-ray2.90C/H276-441[»]
3WTXX-ray2.80C/H276-441[»]
3WTYX-ray2.70C/H276-441[»]
3WTZX-ray2.61A/B276-441[»]
3WU0X-ray2.60A/B276-441[»]
3WU1X-ray2.40B333-441[»]
4L0YX-ray2.50B296-441[»]
4L0ZX-ray2.70B296-441[»]
4L18X-ray2.30B/F296-441[»]
4LG0X-ray2.19B331-440[»]
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.
GeneTreeiENSGT00760000118907.
HOGENOMiHOG000285953.
HOVERGENiHBG003088.
InParanoidiP14921.
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

        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
NGAALCALGK DCFLELAPDF VGDILWEHLE ILQKEDVKPY QVNGVNPAYP
160 170 180 190 200
ESRYTSDYFI SYGIEHAQCV PPSEFSEPSF ITESYQTLHP ISSEELLSLK
210 220 230 240 250
YENDYPSVIL RDPLQTDTLQ NDYFAIKQEV VTPDNMCMGR TSRGKLGGQD
260 270 280 290 300
SFESIESYDS CDRLTQSWSS QSSFNSLQRV PSYDSFDSED 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 E
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:
EMBLi
GenBanki
DDBJi
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:
EMBLi
GenBanki
DDBJi
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:
PDBei
RCSB PDBi
PDBji
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 [» ]
3WTS X-ray 2.35 C/H 276-441 [» ]
3WTT X-ray 2.35 C/H 276-441 [» ]
3WTU X-ray 2.70 C/H 276-441 [» ]
3WTV X-ray 2.70 C/H 276-441 [» ]
3WTW X-ray 2.90 C/H 276-441 [» ]
3WTX X-ray 2.80 C/H 276-441 [» ]
3WTY X-ray 2.70 C/H 276-441 [» ]
3WTZ X-ray 2.61 A/B 276-441 [» ]
3WU0 X-ray 2.60 A/B 276-441 [» ]
3WU1 X-ray 2.40 B 333-441 [» ]
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 [» ]
4LG0 X-ray 2.19 B 331-440 [» ]
ProteinModelPortali P14921.
SMRi P14921. Positions 29-138, 297-441.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 108414. 40 interactions.
IntActi P14921. 67 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.
GeneTreei ENSGT00760000118907.
HOGENOMi HOG000285953.
HOVERGENi HBG003088.
InParanoidi P14921.
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 13644631.
PROi P14921.
SOURCEi Search...

Gene expression databases

Bgeei P14921.
CleanExi HS_ETS1.
ExpressionAtlasi P14921. baseline and differential.
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

« Hide 'large scale' publications
  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: November 26, 2014
This is version 168 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