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P14921 (ETS1_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 161. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (4) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Interactions·Alt products·Sequence annotation·Sequences·References·Web links·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Protein C-ets-1
Alternative name(s):
p54
Gene names
Name:ETS1
Synonyms:EWSR2
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length441 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

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. Ref.11 Ref.12 Ref.13 Ref.15

Subunit structure

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. Ref.10 Ref.12 Ref.13 Ref.20

Subcellular location

Cytoplasm. Nucleus. Note: Delocalizes from nucleus to cytoplasm when coexpressed with isoform Ets-1p27. Ref.3 Ref.12

Tissue specificity

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. Ref.3 Ref.18

Induction

Up-regulated by retinoic acid, VEGF, TNF-alpha/TNFA, lipopolysaccharide and in response to hypoxia (at protein level). Ref.15

Post-translational modification

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

Ubiquitinated; which induces proteasomal degradation By similarity.

Sequence similarities

Belongs to the ETS family.

Contains 1 ETS DNA-binding domain.

Contains 1 PNT (pointed) domain.

Ontologies

Keywords
   Biological processImmunity
Transcription
Transcription regulation
   Cellular componentCytoplasm
Nucleus
   Coding sequence diversityAlternative splicing
   DiseaseProto-oncogene
   LigandDNA-binding
   PTMAcetylation
Isopeptide bond
Phosphoprotein
Ubl conjugation
   Technical term3D-structure
Complete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processPML body organization

Inferred from direct assay Ref.12Ref.13. Source: BHF-UCL

angiogenesis involved in wound healing

Inferred from electronic annotation. Source: Ensembl

apoptotic nuclear changes

Inferred from direct assay PubMed 9266972. Source: UniProtKB

cell motility

Inferred from mutant phenotype Ref.13. Source: BHF-UCL

cellular response to hydrogen peroxide

Inferred from electronic annotation. Source: Ensembl

estrous cycle phase

Inferred from electronic annotation. Source: Ensembl

execution phase of apoptosis

Inferred from direct assay PubMed 9266972. Source: UniProtKB

female pregnancy

Inferred from electronic annotation. Source: Ensembl

hypothalamus development

Inferred from electronic annotation. Source: Ensembl

immune response

Traceable author statement PubMed 2187191. Source: ProtInc

negative regulation of cell cycle

Inferred from direct assay PubMed 9266972. Source: UniProtKB

negative regulation of cell proliferation

Traceable author statement PubMed 2187191. Source: ProtInc

pituitary gland development

Inferred from electronic annotation. Source: Ensembl

positive regulation of angiogenesis

Inferred from electronic annotation. Source: Ensembl

positive regulation of cell proliferation

Inferred from electronic annotation. Source: Ensembl

positive regulation of cellular component movement

Inferred from mutant phenotype Ref.13. Source: BHF-UCL

positive regulation of endothelial cell migration

Inferred from mutant phenotype Ref.15. Source: UniProtKB

positive regulation of erythrocyte differentiation

Inferred from direct assay PubMed 8620536. Source: UniProtKB

positive regulation of transcription from RNA polymerase II promoter

Inferred from direct assay Ref.13. Source: BHF-UCL

positive regulation of transcription, DNA-templated

Inferred from direct assay Ref.12. Source: BHF-UCL

regulation of angiogenesis

Inferred from mutant phenotype Ref.15. Source: UniProtKB

regulation of extracellular matrix disassembly

Inferred from electronic annotation. Source: Ensembl

response to antibiotic

Inferred from direct assay PubMed 9266972. Source: UniProtKB

response to estradiol

Inferred from electronic annotation. Source: Ensembl

response to hypoxia

Inferred from electronic annotation. Source: Ensembl

response to interleukin-1

Inferred from electronic annotation. Source: Ensembl

response to laminar fluid shear stress

Inferred from electronic annotation. Source: Ensembl

response to mechanical stimulus

Inferred from electronic annotation. Source: Ensembl

transcription from RNA polymerase II promoter

Inferred from direct assay PubMed 7753825. Source: UniProtKB

transcription, DNA-templated

Inferred from electronic annotation. Source: UniProtKB-KW

   Cellular_componentcytoplasm

Inferred from direct assay. Source: HPA

intercellular bridge

Inferred from direct assay. Source: HPA

nucleoplasm

Traceable author statement. Source: Reactome

nucleus

Inferred from direct assay Ref.12Ref.13. Source: BHF-UCL

transcription factor complex

Inferred from electronic annotation. Source: Ensembl

   Molecular_functionDNA binding

Inferred from sequence or structural similarity. Source: UniProtKB

sequence-specific DNA binding

Inferred from electronic annotation. Source: Ensembl

sequence-specific DNA binding transcription factor activity

Inferred from direct assay Ref.12Ref.13. Source: BHF-UCL

transcription factor binding

Non-traceable author statement Ref.11. Source: UniProtKB

Complete GO annotation...

Alternative products

This entry describes 4 isoforms produced by alternative splicing. [Align] [Select]
Isoform c-ETS-1A (identifier: P14921-1)

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.
Isoform c-ETS-1B (identifier: P14921-2)

Also known as: Ets-1 p42;

The sequence of this isoform differs from the canonical sequence as follows:
     244-330: Missing.
Isoform 3 (identifier: P14921-3)

The sequence of this isoform differs from the canonical sequence as follows:
     1-27: MKAAVDLKPTLTIIKTEKVDLELFPSP → MSYFVDSAGS...VPTGLEHCVS
Note: No experimental confirmation available.
Isoform Ets-1 p27 (identifier: P14921-4)

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.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 441441Protein C-ets-1
PRO_0000204069

Regions

Domain51 – 13686PNT
DNA binding335 – 41581ETS
Region130 – 243114Activation domain; required for transcription activation

Amino acid modifications

Modified residue81N6-acetyllysine Ref.17
Modified residue151N6-acetyllysine; alternate Ref.17
Modified residue381Phosphothreonine; by MAPK By similarity
Modified residue2231Phosphotyrosine Ref.14
Modified residue2701Phosphoserine Ref.16
Modified residue2851Phosphoserine Ref.16
Modified residue3051N6-acetyllysine Ref.17
Cross-link15Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO); alternate By similarity
Cross-link227Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO) By similarity

Natural variations

Alternative sequence1 – 2727MKAAV…LFPSP → MSYFVDSAGSSPVPYSAPRP AVVRQGPSNTYEDPRMNCGF QSNYHQQRPCYPFWDEMATQ EVPTGLEHCVS in isoform 3.
VSP_043152
Alternative sequence28 – 243216Missing in isoform Ets-1 p27.
VSP_046056
Alternative sequence244 – 33087Missing in isoform c-ETS-1B.
VSP_001464

Experimental info

Sequence conflict1621Y → C in AAB28747. Ref.8
Sequence conflict236 – 2438MCMGRTSR → FLPPPLPP in AAA52409. Ref.9
Sequence conflict2551I → V in AAY19514. Ref.3
Sequence conflict332 – 3376SGPIQL → RRPPAA in AAA52409. Ref.9

Secondary structure

........................... 441
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
Isoform c-ETS-1A (Ets-1 p51) [UniParc].

Last modified April 1, 1990. Version 1.
Checksum: 3B66BCC464B393FB

FASTA44150,408
        10         20         30         40         50         60 
MKAAVDLKPT LTIIKTEKVD LELFPSPDME CADVPLLTPS SKEMMSQALK ATFSGFTKEQ 

        70         80         90        100        110        120 
QRLGIPKDPR QWTETHVRDW VMWAVNEFSL KGVDFQKFCM NGAALCALGK DCFLELAPDF 

       130        140        150        160        170        180 
VGDILWEHLE ILQKEDVKPY QVNGVNPAYP ESRYTSDYFI SYGIEHAQCV PPSEFSEPSF 

       190        200        210        220        230        240 
ITESYQTLHP ISSEELLSLK YENDYPSVIL RDPLQTDTLQ NDYFAIKQEV VTPDNMCMGR 

       250        260        270        280        290        300 
TSRGKLGGQD SFESIESYDS CDRLTQSWSS QSSFNSLQRV PSYDSFDSED YPAALPNHKP 

       310        320        330        340        350        360 
KGTFKDYVRD RADLNKDKPV IPAAALAGYT GSGPIQLWQF LLELLTDKSC QSFISWTGDG 

       370        380        390        400        410        420 
WEFKLSDPDE VARRWGKRKN KPKMNYEKLS RGLRYYYDKN IIHKTAGKRY VYRFVCDLQS 

       430        440 
LLGYTPEELH AMLDVKPDAD E 

« Hide

Isoform c-ETS-1B (Ets-1 p42) [UniParc].

Checksum: 6C3313F2DBE3CF88
Show »

FASTA35440,786
Isoform 3 [UniParc].

Checksum: 8A6B816BAEB91149
Show »

FASTA48555,412
Isoform Ets-1 p27 (Ets-1Delta(III-VI)) [UniParc].

Checksum: 5A01096FCEDE9FEA
Show »

FASTA22525,697

References

« Hide 'large scale' references
[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]"Mammalian ets-1 and ets-2 genes encode highly conserved proteins."
Watson D.K., McWilliams M.J., Lapis P., Lautenberger J.A., Schweinfest C.W., Papas T.S.
Proc. Natl. Acad. Sci. U.S.A. 85:7862-7866(1988) [PubMed] [Europe PMC] [Abstract]
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]"The full-ORF clone resource of the German cDNA consortium."
Bechtel S., Rosenfelder H., Duda A., Schmidt C.P., Ernst U., Wellenreuther R., Mehrle A., Schuster C., Bahr A., Bloecker H., Heubner D., Hoerlein A., Michel G., Wedler H., Koehrer K., Ottenwaelder B., Poustka A., Wiemann S., Schupp I.
BMC Genomics 8:399-399(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 3).
Tissue: Endometrium.
[6]"Human chromosome 11 DNA sequence and analysis including novel gene identification."
Taylor T.D., Noguchi H., Totoki Y., Toyoda A., Kuroki Y., Dewar K., Lloyd C., Itoh T., Takeda T., Kim D.-W., She X., Barlow K.F., Bloom T., Bruford E., Chang J.L., Cuomo C.A., Eichler E., FitzGerald M.G. expand/collapse author list , Jaffe D.B., LaButti K., Nicol R., Park H.-S., Seaman C., Sougnez C., Yang X., Zimmer A.R., Zody M.C., Birren B.W., Nusbaum C., Fujiyama A., Hattori M., Rogers J., Lander E.S., Sakaki Y.
Nature 440:497-500(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[7]"Serum, AP-1 and Ets-1 stimulate the human ets-1 promoter."
Majerus M.-A., Bibollet-Ruche F., Telliez J.-B., Wasylyk B., Bailleul B.
Nucleic Acids Res. 20:2699-2703(1992) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-27.
[8]"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.
[9]"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.
[10]"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.
[11]"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.
[12]"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.
[13]"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.
[14]"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].
[15]"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.
[16]"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.
[17]"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].
[18]"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.
[19]"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.
[20]"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.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
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.
M11921 Genomic DNA. Translation: AAA52409.1.
PIRTVHUET. A32066.
RefSeqNP_001137292.1. NM_001143820.1.
NP_001155894.1. NM_001162422.1.
NP_005229.1. NM_005238.3.
UniGeneHs.369438.

3D structure databases

PDBe
RCSB PDB
PDBj
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[»]
ProteinModelPortalP14921.
SMRP14921. Positions 29-138, 297-441.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid108414. 39 interactions.
IntActP14921. 63 interactions.
MINTMINT-122911.
STRING9606.ENSP00000376436.

PTM databases

PhosphoSiteP14921.

Polymorphism databases

DMDM119641.

Proteomic databases

PaxDbP14921.
PRIDEP14921.

Protocols and materials databases

DNASU2113.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000319397; ENSP00000324578; ENSG00000134954. [P14921-1]
ENST00000345075; ENSP00000340485; ENSG00000134954. [P14921-2]
ENST00000392668; ENSP00000376436; ENSG00000134954. [P14921-3]
ENST00000526145; ENSP00000433500; ENSG00000134954. [P14921-2]
ENST00000535549; ENSP00000441430; ENSG00000134954. [P14921-4]
GeneID2113.
KEGGhsa:2113.
UCSCuc001qej.2. human. [P14921-3]
uc010sbs.1. human. [P14921-1]

Organism-specific databases

CTD2113.
GeneCardsGC11M128328.
HGNCHGNC:3488. ETS1.
HPACAB002575.
HPA042870.
MIM164720. gene.
neXtProtNX_P14921.
Orphanet536. Systemic lupus erythematosus.
PharmGKBPA27902.
GenAtlasSearch...

Phylogenomic databases

eggNOGNOG305402.
HOGENOMHOG000285953.
HOVERGENHBG003088.
KOK02678.
OMADEMATQE.
OrthoDBEOG77127T.
PhylomeDBP14921.
TreeFamTF316214.

Enzyme and pathway databases

ReactomeREACT_120956. Cellular responses to stress.
SignaLinkP14921.

Gene expression databases

ArrayExpressP14921.
BgeeP14921.
CleanExHS_ETS1.
GenevestigatorP14921.

Family and domain databases

Gene3D1.10.10.10. 1 hit.
1.10.150.50. 1 hit.
InterProIPR000418. Ets_dom.
IPR003118. Pointed_dom.
IPR013761. SAM/pointed.
IPR016311. Transform_prot_C-ets.
IPR011991. WHTH_DNA-bd_dom.
[Graphical view]
PfamPF00178. Ets. 1 hit.
PF02198. SAM_PNT. 1 hit.
[Graphical view]
PIRSFPIRSF001698. Transforming_factor_C-ets. 1 hit.
PRINTSPR00454. ETSDOMAIN.
SMARTSM00413. ETS. 1 hit.
SM00251. SAM_PNT. 1 hit.
[Graphical view]
SUPFAMSSF47769. SSF47769. 1 hit.
PROSITEPS00345. ETS_DOMAIN_1. 1 hit.
PS00346. ETS_DOMAIN_2. 1 hit.
PS50061. ETS_DOMAIN_3. 1 hit.
PS51433. PNT. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

ChiTaRSETS1. human.
EvolutionaryTraceP14921.
GeneWikiETS1.
GenomeRNAi2113.
NextBio35465342.
PROP14921.
SOURCESearch...

Entry information

Entry nameETS1_HUMAN
AccessionPrimary (citable) accession number: P14921
Secondary accession number(s): A9UL17 expand/collapse secondary AC list , F5GYX9, Q14278, Q16080, Q6N087
Entry history
Integrated into UniProtKB/Swiss-Prot: April 1, 1990
Last sequence update: April 1, 1990
Last modified: April 16, 2014
This is version 161 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (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.

Relevant documents

SIMILARITY comments

Index of protein domains and families

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

MIM cross-references

Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot

Human chromosome 11

Human chromosome 11: entries, gene names and cross-references to MIM