P27577 (ETS1_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Protein C-ets-1

Alternative name(s):
p54

Gene names

Name:	Ets1
Synonyms:	Ets-1

Organism

Mus musculus (Mouse) [Reference proteome]

Taxonomic identifier

10090 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Opisthokonta › Metazoa › Eumetazoa › Bilateria › Deuterostomia › Chordata › Craniata › Vertebrata › Gnathostomata › Teleostomi › Euteleostomi › Sarcopterygii › Tetrapoda › Amniota › Mammalia › Theria › Eutheria › Euarchontoglires › Glires › Rodentia › Sciurognathi › Muroidea › Muridae › Murinae › Mus › Mus

Protein attributes

Sequence length	440 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 By similarity.
Subunit structure	Binds DNA as a homodimer. Binds to DAXX. Interacts with UBE2I By similarity. Interacts with MAF and MAFB. Interacts with PAX5, the interaction alters DNA-binding properties. Ref.5 Ref.6
Subcellular location	Nucleus.
Post-translational modification	Sumoylated on Lys-15 and Lys-227, preferentially with SUMO2; which inhibits transcriptional activity. Ref.7 Ubiquitinated; which induces proteasomal degradation. Ref.7
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	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 electronic annotation. Source: Compara angiogenesis involved in wound healing Inferred from electronic annotation. Source: Compara cell motility Inferred from electronic annotation. Source: Compara 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 induction of apoptosis Inferred from electronic annotation. Source: Compara negative regulation of cell cycle Inferred from electronic annotation. Source: Compara 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 erythrocyte differentiation Inferred from sequence or structural similarity. Source: UniProtKB positive regulation of transcription from RNA polymerase II promoter Inferred from direct assay PubMed 12464608. Source: MGI regulation of extracellular matrix disassembly Inferred from electronic annotation. Source: Compara response to antibiotic Inferred from electronic annotation. Source: Compara 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 electronic annotation. Source: Compara
Cellular_component	transcription factor complex Inferred from direct assay PubMed 12464608. Source: MGI
Molecular_function	sequence-specific DNA binding Inferred from direct assay PubMed 1409581. Source: MGI sequence-specific DNA binding transcription factor activity Inferred from sequence or structural similarity. Source: UniProtKB
Complete GO annotation...

Binary interactions

With	Entry	#Exp.	IntAct	Notes
TLX1	P31314	2	EBI-4289053,EBI-2820655	From a different organism.
TLX3	O43711	2	EBI-4289053,EBI-3939165	From a different organism.

Alternative products

This entry describes 1 isoform produced by alternative splicing. [Select]

Note: At least 2 isoforms are produced.

Isoform 1 (identifier: P27577-1)

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.

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 440

440

Protein C-ets-1

PRO_0000204070

Regions

Domain

51 – 136

86

PNT

DNA binding

335 – 415

81

ETS

Amino acid modifications

Modified residue

8

1

N6-acetyllysine By similarity

Modified residue

15

1

N6-acetyllysine By similarity

Modified residue

38

1

Phosphothreonine; by MAPK Ref.8

Modified residue

223

1

Phosphotyrosine By similarity

Modified residue

270

1

Phosphoserine By similarity

Modified residue

285

1

Phosphoserine By similarity

Modified residue

305

1

N6-acetyllysine By similarity

Cross-link

15

Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO) Ref.7

Cross-link

227

Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO) Ref.7

Experimental info

Sequence conflict

28

1

D → E in AAA63299. Ref.1

Sequence conflict

28

1

D → E in CAA39310. Ref.3

Sequence conflict

37

1

L → S in CAA39310. Ref.3

Sequence conflict

51 – 52

2

AT → SY in CAA39310. Ref.3

Sequence conflict

55

1

G → P in AAA63299. Ref.1

Sequence conflict

63

1

L → R in CAA39310. Ref.3

Sequence conflict

74

1

E → D in CAA39310. Ref.3

Sequence conflict

96

1

Q → H in CAA39310. Ref.3

Sequence conflict

105

1

L → V in CAA39310. Ref.3

Sequence conflict

157

1

D → V in CAA39310. Ref.3

Sequence conflict

211

1

Q → R in CAA39310. Ref.3

Sequence conflict

217

1

D → E in CAA39310. Ref.3

Sequence conflict

225

1

A → R in CAA39310. Ref.3

Sequence conflict

234

1

D → N in CAA39310. Ref.3

Sequence conflict

360

1

G → C in CAA39310. Ref.3

Sequence conflict

383

1

K → S in CAA39310. Ref.3

Sequence conflict

392

1

G → A in CAA39310. Ref.3

Sequence conflict

408 – 409

2

KR → NA in CAA39310. Ref.3

Sequence conflict

413

1

R → A in CAA39310. Ref.3

Secondary structure

1

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440

Helix Strand Turn

Details...

Turn

39 – 42

4

Helix

43 – 52

10

Helix

54 – 62

9

Beta strand

67 – 69

3

Helix

74 – 88

15

Turn

95 – 98

4

Helix

102 – 107

6

Helix

109 – 116

8

Helix

119 – 134

16

Helix

304 – 312

9

Turn

313 – 315

3

Beta strand

318 – 321

4

Helix

323 – 330

8

Helix

337 – 345

9

Helix

348 – 350

3

Turn

351 – 353

3

Beta strand

354 – 356

3

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 1 [UniParc]. Last modified February 1, 1995. Version 2. Checksum: 151164D83C41B143	FASTA	440	50,202
	10 20 30 40 50 60 MKAAVDLKPT LTIIKTEKVD LELFPSPDME CADVPLLTPS SKEMMSQALK ATFSGFTKEQ 70 80 90 100 110 120 QRLGIPKDPR QWTETHVRDW VMWAVNEFSL KGVDFQKFCM SGAALCALGK ECFLELAPDF 130 140 150 160 170 180 VGDILWEHLE ILQKEDVKPY QVNGANPTYP ESCYTSDYFI SYGIEHAQCV PPSEFSEPSF 190 200 210 220 230 240 ITESYQTLHP ISSEELLSLK YENDYPSVIL QDPLQTDTLQ TDYFAIKQEV LTPDNMCLGR 250 260 270 280 290 300 ASRGKLGGQD SFESVESYDS CDRLTQSWSS QSSFNSLQRV PSYDSFDYED 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

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"The chicken, mouse and human ETS-1 proteins all have predicted masses of 50 kDa, but have different electrophoretic mobilities." Watson D.K., Seth A., Smyth F.E., Schweinfest C.W., Papas T.S. (In) Papas T.S. (eds.); Oncogenesis, pp.221-232, Gulf Publishing Company, Houston (1990) Cited for: NUCLEOTIDE SEQUENCE [MRNA]. Strain: BALB/c. Tissue: Fibroblast.
[2]	"Sequence-specific DNA binding of the proto-oncoprotein ets-1 defines a transcriptional activator sequence within the long terminal repeat of the Moloney murine sarcoma virus." Gunther C.V., Nye J.A., Bryner R.S., Graves B.J. Genes Dev. 4:667-679(1990) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA]. Strain: BALB/c. Tissue: Thymus.
[3]	"Cloning, sequencing, and expression of mouse c-ets-1 cDNA in baculovirus expression system." Chen J.H. Oncogene Res. 5:277-285(1990) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA]. Strain: BALB/c. Tissue: Thymus.
[4]	"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]. Strain: Czech II. Tissue: Mammary gland.
[5]	"c-Maf interacts with c-Myb to regulate transcription of an early myeloid gene during differentiation." Hedge S.P., Kumar A., Kurschner C., Shapiro L.H. Mol. Cell. Biol. 18:2729-2737(1998) [PubMed] [Europe PMC] [Abstract] Cited for: INTERACTION WITH MAF.
[6]	"MafB is an inducer of monocytic differentiation." Kelly L.M., Englmeier U., Lafon I., Sieweke M.H., Graf T. EMBO J. 19:1987-1997(2000) [PubMed] [Europe PMC] [Abstract] Cited for: INTERACTION WITH MAFB.
[7]	"Regulation of the Ets-1 transcription factor by sumoylation and ubiquitinylation." Ji Z., Degerny C., Vintonenko N., Deheuninck J., Foveau B., Leroy C., Coll J., Tulasne D., Baert J.-L., Fafeur V. Oncogene 26:395-406(2007) [PubMed] [Europe PMC] [Abstract] Cited for: SUMOYLATION AT LYS-15 AND LYS-227, UBIQUITINATION.
[8]	"Structure of the ets-1 pointed domain and mitogen-activated protein kinase phosphorylation site." Slupsky C.M., Gentile L.N., Donaldson L.W., Mackereth C.D., Seidel J.J., Graves B.J., McIntosh L.P. Proc. Natl. Acad. Sci. U.S.A. 95:12129-12134(1998) [PubMed] [Europe PMC] [Abstract] Cited for: STRUCTURE BY NMR OF 29-138, PHOSPHORYLATION AT THR-38.
[9]	"Solution structure of the ETS domain from murine Ets-1: a winged helix-turn-helix DNA binding motif." Donaldson L.W., Petersen J.M., Graves B.J., McIntosh L.P. EMBO J. 15:125-134(1996) [PubMed] [Europe PMC] [Abstract] Cited for: STRUCTURE BY NMR OF 332-415.
[10]	"Structural studies of Ets-1/Pax5 complex formation on DNA." Garvie C.W., Hagman J., Wolberger C. Mol. Cell 8:1267-1276(2001) [PubMed] [Europe PMC] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (2.25 ANGSTROMS) OF 331-440 IN COMPLEX WITH HUMAN PAX5 AND DNA.
+	Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ

M58482 mRNA. Translation: AAA63299.1.
X53953 mRNA. Translation: CAA37904.1.
X55787 mRNA. Translation: CAA39310.1.
BC010588 mRNA. Translation: AAH10588.1.

IPI

IPI00117744.

PIR

A35875. A30487.
I48291.

RefSeq

NP_035938.2. NM_011808.2.

UniGene

Mm.292415.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
1K78	X-ray	2.25	B/F	331-440	[»]
1K79	X-ray	2.40	A/D	331-440	[»]
1K7A	X-ray	2.80	A/D	331-440	[»]
1MD0	X-ray	2.00	A/B	300-440	[»]
1MDM	X-ray	2.80	B	280-440	[»]
1R36	NMR	-	A	301-440	[»]
2JV3	NMR	-	A	29-138	[»]
2KMD	NMR	-	A	29-138	[»]

ProteinModelPortal

P27577.

SMR

P27577. Positions 29-138, 297-440.

ModBase

Search...

Protein-protein interaction databases

DIP

DIP-41848N.

IntAct

P27577. 3 interactions.

STRING

10090.ENSMUSP00000034534.

PTM databases

PhosphoSite

P27577.

Proteomic databases

PRIDE

P27577.

Protocols and materials databases

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

Ensembl

ENSMUST00000034534; ENSMUSP00000034534; ENSMUSG00000032035.

GeneID

23871.

KEGG

mmu:23871.

Organism-specific databases

CTD

2113.

MGI

MGI:95455. Ets1.

Phylogenomic databases

eggNOG

NOG305402.

HOGENOM

HOG000285953.

HOVERGEN

HBG003088.

InParanoid

P27577.

KO

K02678.

OMA

FWDEMAT.

Gene expression databases

ArrayExpress

P27577.

Bgee

P27577.

CleanEx

MM_ETS1.

Genevestigator

P27577.

GermOnline

ENSMUSG00000032035. Mus musculus.

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. mouse.

EvolutionaryTrace

P27577.

NextBio

303577.

SOURCE

Search...

Entry information

Entry name

ETS1_MOUSE

Accession

Primary (citable) accession number: P27577
Secondary accession number(s): Q61403

Entry history

Integrated into UniProtKB/Swiss-Prot:	August 1, 1992
Last sequence update:	February 1, 1995
Last modified:	May 1, 2013
This is version 136 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program