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UniProtKB/Swiss-Prot entry P14921


[Entry info] [Name and origin] [References] [Comments] [Cross-references] [Keywords] [Features] [Sequence] [Tools]

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Entry information
Entry name ETS1_HUMAN
Primary accession number P14921
Secondary accession numbers Q14278 Q16080
Integrated into Swiss-Prot on April 1, 1990
Sequence was last modified on April 1, 1990 (Sequence version 1)
Annotations were last modified on    June 16, 2009 (Entry version 108)
Name and origin of the protein
Protein name Protein C-ets-1
Synonym p54
Gene name
Name: ETS1
Synonyms: EWSR2
From
Homo sapiens (Human) [TaxID: 9606] 
Taxonomy Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae; Homo.
Protein existence 1: Evidence at protein level;
References
[1]
NUCLEOTIDE SEQUENCE [MRNA].
PubMed=3060801 [NCBI, ExPASy, EBI, Israel, Japan]
Reddy E.S.P., Rao V.N.;
"Structure, expression and alternative splicing of the human c-ets-1 proto-oncogene.";
Oncogene Res. 3:239-246(1988).
[2]
NUCLEOTIDE SEQUENCE [MRNA].
DOI=10.1073/pnas.85.21.7862; PubMed=2847145 [NCBI, ExPASy, EBI, Israel, Japan]
Watson D.K., McWilliams M.J., Lapis P., Lautenberger J.A., Schweinfest C.W., Papas T.S.;
"Mammalian ets-1 and ets-2 genes encode highly conserved proteins.";
Proc. Natl. Acad. Sci. U.S.A. 85:7862-7866(1988).
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM C-ETS-1A).
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.;
"Cloning of human full-length CDSs in BD Creator(TM) system donor vector.";
Submitted (MAY-2003) to the EMBL/GenBank/DDBJ databases.
[4]
NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-27.
DOI=10.1093/nar/20.11.2699; PubMed=1614856 [NCBI, ExPASy, EBI, Israel, Japan]
Majerus M.-A., Bibollet-Ruche F., Telliez J.-B., Wasylyk B., Bailleul B.;
"Serum, AP-1 and Ets-1 stimulate the human ets-1 promoter.";
Nucleic Acids Res. 20:2699-2703(1992).
[5]
NUCLEOTIDE SEQUENCE [MRNA] OF 146-174.
PubMed=8231246 [NCBI, ExPASy, EBI, Israel, Japan]
Collyn d'Hooghe M., Galiegue-Zouitina S., Szymiczek D., Lantoine D., Quief S., Loucheux-Lefebvre M.H., Kerckaert J.P.;
"Quantitative and qualitative variation of ETS-1 transcripts in hematologic malignancies.";
Leukemia 7:1777-1785(1993).
[6]
NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 236-337.
DOI=10.1073/pnas.82.21.7294; PubMed=2997781 [NCBI, ExPASy, EBI, Israel, Japan]
Watson D.K., McWilliams-Smith M.J., Nunn M.F., Duesberg P.H., O'Brien S.J., Papas T.S.;
"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.";
Proc. Natl. Acad. Sci. U.S.A. 82:7294-7298(1985).
[7]
INTERACTION WITH UBE2I.
DOI=10.1038/sj.onc.1201301; PubMed=9333025 [NCBI, ExPASy, EBI, Israel, Japan]
Hahn S.L., Criqui-Filipe P., Wasylyk B.;
"Modulation of ETS-1 transcriptional activity by huUBC9, a ubiquitin-conjugating enzyme.";
Oncogene 15:1489-1495(1997).
[8]
FUNCTION.
DOI=10.1038/sj.onc.1203385; PubMed=10698492 [NCBI, ExPASy, EBI, Israel, Japan]
Li R., Pei H., Watson D.K., Papas T.S.;
"EAP1/Daxx interacts with ETS1 and represses transcriptional activation of ETS1 target genes.";
Oncogene 19:745-753(2000).
[9]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-205 AND TYR-223, AND MASS SPECTROMETRY.
DOI=10.1038/nbt1046; PubMed=15592455 [NCBI, ExPASy, EBI, Israel, Japan]
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.;
"Immunoaffinity profiling of tyrosine phosphorylation in cancer cells.";
Nat. Biotechnol. 23:94-101(2005).
[10]
STRUCTURE BY NMR OF 320-415.
DOI=10.1016/0092-8674(95)90189-2; PubMed=8521493 [NCBI, ExPASy, EBI, Israel, Japan]
Werner M.H., Clore G.M., Fisher C.L., Fisher R.J., Trinh L., Shiloach J., Gronenborn A.M.;
"The solution structure of the human ETS1-DNA complex reveals a novel mode of binding and true side chain intercalation.";
Cell 83:761-771(1995).
Comments
Copyright
Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms. Distributed under the Creative Commons Attribution-NoDerivs License.
Cross-references
Sequence databases
EMBL
X14798; CAA32904.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
X14798; CAA32903.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
J04101; AAA52410.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
X65469; -; NOT_ANNOTATED_CDS; Genomic_DNA.[EMBL / GenBank / DDBJ]
S67063; AAB28747.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
BT019452; AAV38259.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
M11921; AAA52409.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
IPI IPI00028127; -.
IPI00218351; -.
PIR A32066; TVHUET.
RefSeq NP_005229.1; -.
UniGene Hs.369438
3D structure databases
PDB
1GVJ; X-ray; 1.53 A; A/B=297-441.[ExPASy / RCSB / EBI]
2NNY; X-ray; 2.58 A; A/B=280-441.[ExPASy / RCSB / EBI]
2STT; NMR; -; A=320-415.[ExPASy / RCSB / EBI]
2STW; NMR; -; A=320-415.[ExPASy / RCSB / EBI]
Detailed list of linked structures.
PDBsum 1GVJ; -.
2NNY; -.
2STT; -.
2STW; -.
SMR P14921; 29-138.
ModBase P14921.
Protein-protein interaction databases
IntAct P14921; 3.
PTM databases
PhosphoSite P14921; -.
Enzyme and pathway databases
Pathway_Interaction_DB angiopoietinreceptor_pathway; Angiopoietin receptor Tie2-mediated signaling.
bcr_5pathway; BCR signaling pathway.
hif1_tfpathway; HIF-1-alpha transcription factor network.
il4_2pathway; IL4-mediated signaling events.
Organism-specific databases
GeneCards GC11M127833; -.
H-InvDB HIX0010260; -.
HGNC HGNC:3488; ETS1.
GenAtlas ETS1.
HPA CAB002575; -.
MIM 164720; gene. [NCBI / EBI]
PharmGKB PA27902; -.
Gene expression databases
ArrayExpress P14921; -.
Bgee P14921; -.
CleanEx HS_ETS1; -.
GermOnline ENSG00000134954; Homo sapiens.
Ontologies
GO
GO:0005634; Cellular component: nucleus (inferred from direct assay from UniProtKB).
GO:0043565; Molecular function: sequence-specific DNA binding (inferred from electronic annotation from InterPro).
GO:0003700; Molecular function: transcription factor activity (inferred from direct assay from UniProtKB).
GO:0008134; Molecular function: transcription factor binding (non-traceable author statement from UniProtKB).
GO:0048870; Biological process: cell motility (inferred from mutant phenotype from UniProtKB).
GO:0006955; Biological process: immune response (traceable author statement from ProtInc).
GO:0008285; Biological process: negative regulation of cell proliferation (traceable author statement from ProtInc).
GO:0030578; Biological process: PML body organization (inferred from direct assay from UniProtKB).
GO:0051272; Biological process: positive regulation of cell motion (inferred from mutant phenotype from UniProtKB).
GO:0045648; Biological process: positive regulation of erythrocyte differentiation (inferred from direct assay from UniProtKB).
GO:0010552; Biological process: positive regulation of specific transcription from RNA polymerase II promoter (inferred from direct assay from UniProtKB).
GO:0006350; Biological process: transcription (inferred from electronic annotation from UniProtKB-KW).
QuickGo view.
Family and domain databases
InterPro IPR000418; Ets.
IPR003118; SAM_PNT.
IPR013761; SAM_type.
IPR016311; Transforming_factor_C-ets.
IPR011991; Wing_hlx_DNA_bd.
Graphical view of domain structure.
Gene3D G3DSA:1.10.150.50; SAM_type; 1.
G3DSA:1.10.10.10; Wing_hlx_DNA_bd; 1.
Pfam PF00178; Ets; 1.
PF02198; SAM_PNT; 1.
Pfam graphical view of domain structure.
PIRSF PIRSF001698; Transforming_factor_C-ets; 1.
PRINTS PR00454; ETSDOMAIN.
SMART SM00413; ETS; 1.
SM00251; SAM_PNT; 1.
SMART graphical view of domain structure.
PROSITE PS00345; ETS_DOMAIN_1; 1.
PS00346; ETS_DOMAIN_2; 1.
PS50061; ETS_DOMAIN_3; 1.
PS51433; PNT; 1.
PROSITE graphical view of domain structure (profiles).
Proteomic databases
PRIDE P14921; -.
Genome annotation databases
Ensembl ENSG00000134954; Homo sapiens. [Contig view]
GeneID 2113; -.
KEGG hsa:2113; -.
Phylogenomic databases
HOVERGEN P14921; -.
Other
NextBio 8539; -.
SOURCE ETS1; Homo sapiens.
ProtoNet P14921.
UniRef View cluster of proteins with at least 50% / 90% / 100% identity.
Keywords
3D-structure; Alternative splicing; DNA-binding; Isopeptide bond; Nucleus; Phosphoprotein; Proto-oncogene; Transcription; Transcription regulation; Ubl conjugation.
Features
SEVIEWER logo Feature table viewer FT aligner logo Feature aligner
KeyFrom   To Length Description FTId
CHAIN   1   441  441     Protein C-ets-1. PRO_0000204069
DOMAIN   51   136  86     PNT. 
DNA_BIND   335   415  81     ETS. 
MOD_RES   38    38        Phosphothreonine; by MAPK (By similarity). 
MOD_RES   205   205        Phosphotyrosine. 
MOD_RES   223   223        Phosphotyrosine. 
CROSSLNK   15    15        Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO) (By similarity). 
CROSSLNK   227   227        Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO) (By similarity). 
VAR_SEQ   244   330        Missing (in isoform c-ETS-1B). VSP_001464
CONFLICT   162   162        Y -> C (in Ref. 5; AAB28747). 
CONFLICT   236   243        MCMGRTSR -> FLPPPLPP (in Ref. 6). 
CONFLICT   332   337        SGPIQL -> RRPPAA (in Ref. 6). 
HELIX   304   313  10      
HELIX   323   330  8      
HELIX   337   345  9      
HELIX   348   350  3      
TURN   351   353  3      
STRAND   354   356  3      
STRAND   362   364  3      
HELIX   368   379  12      
HELIX   386   395  10      
TURN   396   400  5      
STRAND   401   404  4      
STRAND   408   414  7      
HELIX   418   422  5      
HELIX   426   432  7      
Sequence information
Length: 441 AA [This is the length of the unprocessed precursor] Molecular weight: 50408 Da [This is the MW of the unprocessed precursor] CRC64: 3B66BCC464B393FB [This is a checksum on the sequence]
        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 

P14921 in FASTA format

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