P14921 (ETS1_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Protein C-ets-1

Alternative name(s):
p54

Gene names

Name:	ETS1
Synonyms:	EWSR2

Organism

Homo sapiens (Human) [Reference proteome]

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Opisthokonta › Metazoa › Eumetazoa › Bilateria › Deuterostomia › Chordata › Craniata › Vertebrata › Gnathostomata › Teleostomi › Euteleostomi › Sarcopterygii › Tetrapoda › Amniota › Mammalia › Theria › Eutheria › Euarchontoglires › Primates › Haplorrhini › Simiiformes › Catarrhini › Hominoidea › Hominidae › Homininae › Homo

Protein attributes

Sequence length	441 AA.
Sequence status	Complete.
Protein existence	Evidence 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. Ref.11
Subunit structure	Binds DNA as a homodimer, homodimerization is required for transactivation of the stromelysin-1 promoter. Interacts with MAF and MAFB. Interacts with PAX5, the interaction alters DNA-binding properties By similarity. Binds to DAXX. Interacts with UBE2I. Ref.10 Ref.17
Subcellular location	Cytoplasm. Nucleus. Note: Delocalizes from nucleus to cytoplasm when coexpressed with isoform Ets-1 p27. Ref.3
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.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 process	Immunity Transcription Transcription regulation
Cellular component	Cytoplasm Nucleus
Coding sequence diversity	Alternative splicing
Disease	Proto-oncogene
Ligand	DNA-binding
PTM	Acetylation Isopeptide bond Phosphoprotein Ubl conjugation
Technical term	3D-structure Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	PML body organization Inferred from direct assay PubMed 11909962PubMed 15247905. Source: BHF-UCL angiogenesis involved in wound healing Inferred from electronic annotation. Source: Compara cell motility Inferred from mutant phenotype PubMed 15247905. Source: BHF-UCL cellular response to hydrogen peroxide Inferred from electronic annotation. Source: Compara estrous cycle phase Inferred from electronic annotation. Source: Compara female pregnancy Inferred from electronic annotation. Source: Compara hypothalamus development Inferred from electronic annotation. Source: Compara immune response Traceable author statement PubMed 2187191. Source: ProtInc induction of apoptosis Inferred from direct assay PubMed 9266972. Source: UniProtKB 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: Compara positive regulation of angiogenesis Inferred from electronic annotation. Source: Compara positive regulation of cell migration Inferred from electronic annotation. Source: Compara positive regulation of cell proliferation Inferred from electronic annotation. Source: Compara positive regulation of cellular component movement Inferred from mutant phenotype PubMed 15247905. Source: BHF-UCL 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 PubMed 15247905. Source: BHF-UCL positive regulation of transcription, DNA-dependent Inferred from direct assay Ref.11. Source: UniProtKB regulation of extracellular matrix disassembly Inferred from electronic annotation. Source: Compara response to antibiotic Inferred from direct assay PubMed 9266972. Source: UniProtKB response to estradiol stimulus Inferred from electronic annotation. Source: Compara response to hypoxia Inferred from electronic annotation. Source: Compara response to interleukin-1 Inferred from electronic annotation. Source: Compara response to laminar fluid shear stress Inferred from electronic annotation. Source: Compara response to mechanical stimulus Inferred from electronic annotation. Source: Compara transcription from RNA polymerase II promoter Inferred from direct assay PubMed 7753825. Source: UniProtKB transcription, DNA-dependent Inferred from electronic annotation. Source: UniProtKB-KW
Cellular_component	cytoplasm Inferred from electronic annotation. Source: UniProtKB-SubCell nucleus Inferred from direct assay PubMed 11909962PubMed 15247905. Source: BHF-UCL transcription factor complex Inferred from electronic annotation. Source: Compara
Molecular_function	DNA binding Inferred from sequence or structural similarity. Source: UniProtKB sequence-specific DNA binding Inferred from electronic annotation. Source: Compara sequence-specific DNA binding transcription factor activity Inferred from direct assay PubMed 11909962PubMed 15247905. Source: BHF-UCL transcription factor binding Non-traceable author statement Ref.11. Source: UniProtKB
Complete GO annotation...

Binary interactions

With	Entry	#Exp.	IntAct	Notes
APLP2	Q06481	2	EBI-913209,EBI-79306
ARID4B	Q4LE39	2	EBI-913209,EBI-2680990
C17orf62	Q9BQA9	3	EBI-913209,EBI-2680384
DAXX	Q9UER7-1	3	EBI-913224,EBI-287635
EIF5B	O60841	2	EBI-913209,EBI-928530
Gfi1	P70338	2	EBI-913209,EBI-3954754	From a different organism.
JUN	P05412	3	EBI-913209,EBI-852823
MEIS1	O00470	2	EBI-913209,EBI-1210694
PRKDC	P78527	2	EBI-913209,EBI-352053
SRSF11	Q05519	2	EBI-913209,EBI-1051785

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 key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 441

441

Protein C-ets-1

PRO_0000204069

Regions

Domain

51 – 136

86

PNT

DNA binding

335 – 415

81

ETS

Amino acid modifications

Modified residue

8

1

N6-acetyllysine Ref.14

Modified residue

15

1

N6-acetyllysine; alternate Ref.14

Modified residue

38

1

Phosphothreonine; by MAPK By similarity

Modified residue

223

1

Phosphotyrosine Ref.12

Modified residue

270

1

Phosphoserine Ref.13

Modified residue

285

1

Phosphoserine Ref.13

Modified residue

305

1

N6-acetyllysine Ref.14

Cross-link

15

Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO); alternate By similarity

Cross-link

227

Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO) By similarity

Natural variations

Alternative sequence

1 – 27

27

MKAAV…LFPSP → MSYFVDSAGSSPVPYSAPRP AVVRQGPSNTYEDPRMNCGF QSNYHQQRPCYPFWDEMATQ EVPTGLEHCVS in isoform 3.

VSP_043152

Alternative sequence

28 – 243

216

Missing in isoform Ets-1 p27.

VSP_046056

Alternative sequence

244 – 330

87

Missing in isoform c-ETS-1B.

VSP_001464

Experimental info

Sequence conflict

162

1

Y → C in AAB28747. Ref.8

Sequence conflict

236 – 243

8

MCMGRTSR → FLPPPLPP in AAA52409. Ref.9

Sequence conflict

255

1

I → V in AAY19514. Ref.3

Sequence conflict

332 – 337

6

SGPIQL → RRPPAA in AAA52409. Ref.9

Secondary structure

1

.

.

.

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.

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441

Helix Strand Turn

Details...

Helix

304 – 313

10

Helix

323 – 330

8

Beta strand

331 – 333

3

Helix

337 – 345

9

Helix

348 – 350

3

Turn

351 – 353

3

Beta strand

354 – 356

3

Beta strand

358 – 361

4

Beta strand

362 – 364

3

Helix

368 – 379

12

Helix

386 – 395

10

Turn

396 – 400

5

Beta strand

401 – 404

4

Beta strand

408 – 414

7

Helix

418 – 422

5

Helix

426 – 432

7

Sequences

	Sequence		Length	Mass (Da)
	Isoform c-ETS-1A (Ets-1 p51) [UniParc]. Last modified April 1, 1990. Version 1. Checksum: 3B66BCC464B393FB	FASTA	441	50,408
	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
	Isoform c-ETS-1B (Ets-1 p42) [UniParc]. Checksum: 6C3313F2DBE3CF88	FASTA	354	40,786
	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 TSRGSGPIQL WQFLLELLTD KSCQSFISWT GDGWEFKLSD PDEVARRWGK RKNKPKMNYE 310 320 330 340 350 KLSRGLRYYY DKNIIHKTAG KRYVYRFVCD LQSLLGYTPE ELHAMLDVKP DADE
	Isoform 3 [UniParc]. Checksum: 8A6B816BAEB91149	FASTA	485	55,412
	10 20 30 40 50 60 MSYFVDSAGS SPVPYSAPRP AVVRQGPSNT YEDPRMNCGF QSNYHQQRPC YPFWDEMATQ 70 80 90 100 110 120 EVPTGLEHCV SDMECADVPL LTPSSKEMMS QALKATFSGF TKEQQRLGIP KDPRQWTETH 130 140 150 160 170 180 VRDWVMWAVN EFSLKGVDFQ KFCMNGAALC ALGKDCFLEL APDFVGDILW EHLEILQKED 190 200 210 220 230 240 VKPYQVNGVN PAYPESRYTS DYFISYGIEH AQCVPPSEFS EPSFITESYQ TLHPISSEEL 250 260 270 280 290 300 LSLKYENDYP SVILRDPLQT DTLQNDYFAI KQEVVTPDNM CMGRTSRGKL GGQDSFESIE 310 320 330 340 350 360 SYDSCDRLTQ SWSSQSSFNS LQRVPSYDSF DSEDYPAALP NHKPKGTFKD YVRDRADLNK 370 380 390 400 410 420 DKPVIPAAAL AGYTGSGPIQ LWQFLLELLT DKSCQSFISW TGDGWEFKLS DPDEVARRWG 430 440 450 460 470 480 KRKNKPKMNY EKLSRGLRYY YDKNIIHKTA GKRYVYRFVC DLQSLLGYTP EELHAMLDVK PDADE
	Isoform Ets-1 p27 (Ets-1Delta(III-VI)) [UniParc]. Checksum: 5A01096FCEDE9FEA	FASTA	225	25,697
	10 20 30 40 50 60 MKAAVDLKPT LTIIKTEKVD LELFPSPGKL GGQDSFESIE SYDSCDRLTQ SWSSQSSFNS 70 80 90 100 110 120 LQRVPSYDSF DSEDYPAALP NHKPKGTFKD YVRDRADLNK DKPVIPAAAL AGYTGSGPIQ 130 140 150 160 170 180 LWQFLLELLT DKSCQSFISW TGDGWEFKLS DPDEVARRWG KRKNKPKMNY EKLSRGLRYY 190 200 210 220 YDKNIIHKTA GKRYVYRFVC DLQSLLGYTP EELHAMLDVK PDADE

References

	« Hide 'large scale' referencesShow '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. , 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]	"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, MASS SPECTROMETRY.
[13]	"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, MASS SPECTROMETRY. Tissue: Leukemic T-cell.
[14]	"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, MASS SPECTROMETRY.
[15]	"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.
[16]	"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.
[17]	"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.

IPI

IPI00028127.
IPI00218351.
IPI00742887.
IPI00884353.

PIR

TVHUET. A32066.

RefSeq

NP_001137292.1. NM_001143820.1.
NP_001155894.1. NM_001162422.1.
NP_005229.1. NM_005238.3.

UniGene

Hs.369438.

3D structure databases

PDBe
RCSB PDB
PDBj

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	[»]

ProteinModelPortal

P14921.

ModBase

Search...

Protein-protein interaction databases

IntAct

P14921. 57 interactions.

MINT

MINT-122911.

STRING

9606.ENSP00000376436.

PTM databases

PhosphoSite

P14921.

Polymorphism databases

DMDM

119641.

Proteomic databases

PaxDb

P14921.

PRIDE

P14921.

Protocols and materials databases

DNASU

2113.

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

Ensembl

ENST00000319397; ENSP00000324578; ENSG00000134954.
ENST00000345075; ENSP00000340485; ENSG00000134954.
ENST00000392668; ENSP00000376436; ENSG00000134954.
ENST00000526145; ENSP00000433500; ENSG00000134954.
ENST00000535549; ENSP00000441430; ENSG00000134954.

GeneID

2113.

KEGG

hsa:2113.

UCSC

uc010sbs.1. human.

Organism-specific databases

CTD

2113.

GeneCards

GC11M128328.

HGNC

HGNC:3488. ETS1.

HPA

CAB002575.

MIM

164720. gene.

neXtProt

NX_P14921.

PharmGKB

PA27902.

GenAtlas

Search...

Phylogenomic databases

eggNOG

NOG305402.

HOGENOM

HOG000285953.

HOVERGEN

HBG003088.

KO

K02678.

OMA

FWDEMAT.

PhylomeDB

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.

Gene expression databases

ArrayExpress

P14921.

Bgee

P14921.

CleanEx

HS_ETS1.

Genevestigator

P14921.

GermOnline

ENSG00000134954. Homo sapiens.

Family and domain databases

Gene3D

1.10.10.10. 1 hit.
1.10.150.50. 1 hit.

InterPro

IPR000418. Ets_dom.
IPR003118. Pointed_dom.
IPR013761. SAM/pointed.
IPR016311. Transform_prot_C-ets.
IPR011991. WHTH_DNA-bd_dom.
[Graphical view]

Pfam

PF00178. Ets. 1 hit.
PF02198. SAM_PNT. 1 hit.
[Graphical view]

PIRSF

PIRSF001698. Transforming_factor_C-ets. 1 hit.

PRINTS

PR00454. ETSDOMAIN.

SMART

SM00413. ETS. 1 hit.
SM00251. SAM_PNT. 1 hit.
[Graphical view]

SUPFAM

SSF47769. SAM_homology. 1 hit.

PROSITE

PS00345. ETS_DOMAIN_1. 1 hit.
PS00346. ETS_DOMAIN_2. 1 hit.
PS50061. ETS_DOMAIN_3. 1 hit.
PS51433. PNT. 1 hit.
[Graphical view]

ProtoNet

Search...

Other

ChiTaRS

ETS1. human.

EvolutionaryTrace

P14921.

GenomeRNAi

2113.

NextBio

35465342.

SOURCE

Search...

Entry information

Entry name

ETS1_HUMAN

Accession

Primary (citable) accession number: P14921
Secondary accession number(s): A9UL17 , F5GYX9, Q14278, Q16080, Q6N087

Entry history

Integrated into UniProtKB/Swiss-Prot:	April 1, 1990
Last sequence update:	April 1, 1990
Last modified:	May 1, 2013
This is version 151 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program

Disclaimer

Any 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.