ID ETS1_MOUSE STANDARD; PRT; 440 AA. AC P27577; Q61403; DT 01-AUG-1992, integrated into UniProtKB/Swiss-Prot. DT 01-FEB-1995, sequence version 2. DT 16-MAY-2006, entry version 63. DE C-ets-1 protein (p54). GN Name=Ets1; Synonyms=Ets-1; OS Mus musculus (Mouse). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi; OC Muroidea; Muridae; Murinae; Mus. OX NCBI_TaxID=10090; RN [1] RP NUCLEOTIDE SEQUENCE [MRNA]. RC STRAIN=BALB/c; TISSUE=Fibroblast; RA Watson D.K., Seth A., Smyth F.E., Schweinfest C.W., Papas T.S.; RT "The chicken, mouse and human ETS-1 proteins all have predicted masses RT of 50 kDa, but have different electrophoretic mobilities."; RL (In) Papas T.S. (eds.); RL Oncogenesis, pp.221-232, Gulf Publishing Company, Houston (1990). RN [2] RP NUCLEOTIDE SEQUENCE [MRNA]. RC STRAIN=BALB/c; TISSUE=Thymus; RX MEDLINE=90299137; PubMed=2163347; RA Gunther C.V., Nye J.A., Bryner R.S., Graves B.J.; RT "Sequence-specific DNA binding of the proto-oncoprotein ets-1 defines RT a transcriptional activator sequence within the long terminal repeat RT of the Moloney murine sarcoma virus."; RL Genes Dev. 4:667-679(1990). RN [3] RP NUCLEOTIDE SEQUENCE [MRNA]. RC STRAIN=BALB/c; TISSUE=Thymus; RX MEDLINE=90370376; PubMed=2204020; RA Chen J.H.; RT "Cloning, sequencing, and expression of mouse c-ets-1 cDNA in RT baculovirus expression system."; RL Oncogene Res. 5:277-285(1990). RN [4] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. RC STRAIN=Czech II; TISSUE=Mammary gland; RX MEDLINE=22388257; PubMed=12477932; DOI=10.1073/pnas.242603899; RA Strausberg R.L., Feingold E.A., Grouse L.H., Derge J.G., RA Klausner R.D., Collins F.S., Wagner L., Shenmen C.M., Schuler G.D., RA Altschul S.F., Zeeberg B., Buetow K.H., Schaefer C.F., Bhat N.K., RA Hopkins R.F., Jordan H., Moore T., Max S.I., Wang J., Hsieh F., RA Diatchenko L., Marusina K., Farmer A.A., Rubin G.M., Hong L., RA Stapleton M., Soares M.B., Bonaldo M.F., Casavant T.L., Scheetz T.E., RA Brownstein M.J., Usdin T.B., Toshiyuki S., Carninci P., Prange C., RA Raha S.S., Loquellano N.A., Peters G.J., Abramson R.D., Mullahy S.J., RA Bosak S.A., McEwan P.J., McKernan K.J., Malek J.A., Gunaratne P.H., RA Richards S., Worley K.C., Hale S., Garcia A.M., Gay L.J., Hulyk S.W., RA Villalon D.K., Muzny D.M., Sodergren E.J., Lu X., Gibbs R.A., RA Fahey J., Helton E., Ketteman M., Madan A., Rodrigues S., Sanchez A., RA Whiting M., Madan A., Young A.C., Shevchenko Y., Bouffard G.G., RA Blakesley R.W., Touchman J.W., Green E.D., Dickson M.C., RA Rodriguez A.C., Grimwood J., Schmutz J., Myers R.M., RA Butterfield Y.S.N., Krzywinski M.I., Skalska U., Smailus D.E., RA Schnerch A., Schein J.E., Jones S.J.M., Marra M.A.; RT "Generation and initial analysis of more than 15,000 full-length human RT and mouse cDNA sequences."; RL Proc. Natl. Acad. Sci. U.S.A. 99:16899-16903(2002). RN [5] RP STRUCTURE BY NMR OF 29-138. RX MEDLINE=98445336; PubMed=9770451; DOI=10.1073/pnas.95.21.12129; RA Slupsky C.M., Gentile L.N., Donaldson L.W., Mackereth C.D., RA Seidel J.J., Graves B.J., McIntosh L.P.; RT "Structure of the ets-1 pointed domain and mitogen-activated protein RT kinase phosphorylation site."; RL Proc. Natl. Acad. Sci. U.S.A. 95:12129-12134(1998). RN [6] RP STRUCTURE BY NMR OF 332-415. RX MEDLINE=96176767; PubMed=8598195; RA Donaldson L.W., Petersen J.M., Graves B.J., McIntosh L.P.; RT "Solution structure of the ETS domain from murine Ets-1: a winged RT helix-turn-helix DNA binding motif."; RL EMBO J. 15:125-134(1996). CC -!- FUNCTION: Transcription factor. CC -!- SUBUNIT: Binds to DAXX. CC -!- SUBCELLULAR LOCATION: Nucleus. CC -!- ALTERNATIVE PRODUCTS: CC Event=Alternative splicing; Named isoforms=1; CC Comment=At least 2 isoforms are produced; CC Name=1; CC IsoId=P27577-1; Sequence=Displayed; CC -!- SIMILARITY: Belongs to the ETS family. CC -!- SIMILARITY: Contains 1 ETS DNA-binding domain. CC -!- SIMILARITY: Contains 1 PNT (pointed) domain. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; M58482; AAA63299.1; -; mRNA. DR EMBL; X53953; CAA37904.1; -; mRNA. DR EMBL; X55787; CAA39310.1; -; mRNA. DR EMBL; BC010588; AAH10588.1; -; mRNA. DR PIR; A30487; A35875. DR PIR; I48291; I48291. DR UniGene; Mm.292415; -. DR PDB; 1BQV; NMR; @=29-138. DR PDB; 1K78; X-ray; B/F=331-440. DR PDB; 1K79; X-ray; A/D=331-440. DR PDB; 1K7A; X-ray; A/D=331-440. DR PDB; 1MD0; X-ray; A/B=300-440. DR PDB; 1MDM; X-ray; B=280-440. DR PDB; 1R36; NMR; A=301-440. DR TRANSFAC; T00111; -. DR Ensembl; ENSMUSG00000032035; Mus musculus. DR MGI; MGI:95455; Ets1. DR LinkHub; P27577; -. DR GO; GO:0005634; C:nucleus; ISS. DR GO; GO:0003700; F:transcription factor activity; ISS. DR GO; GO:0008134; F:transcription factor binding; ISS. DR GO; GO:0045648; P:positive regulation of erythrocyte differen...; ISS. DR GO; GO:0045941; P:positive regulation of transcription; ISS. DR InterPro; IPR000418; Ets. DR InterPro; IPR002341; HSF_ETS_DNA_bd. DR InterPro; IPR010993; SAM_homology. DR InterPro; IPR003118; SAM_PNT. DR InterPro; IPR011991; Wing_hlx_DNA_bd. DR Pfam; PF00178; Ets; 1. DR Pfam; PF02198; SAM_PNT; 1. DR PRINTS; PR00454; ETSDOMAIN. DR SMART; SM00413; ETS; 1. DR SMART; SM00251; SAM_PNT; 1. DR PROSITE; PS00345; ETS_DOMAIN_1; 1. DR PROSITE; PS00346; ETS_DOMAIN_2; 1. DR PROSITE; PS50061; ETS_DOMAIN_3; 1. KW 3D-structure; Alternative splicing; DNA-binding; Nuclear protein; KW Phosphorylation; Proto-oncogene; Transcription; KW Transcription regulation. FT CHAIN 1 440 C-ets-1 protein. FT /FTId=PRO_0000204070. FT DOMAIN 53 136 PNT. FT DNA_BIND 335 415 ETS. FT MOD_RES 38 38 Phosphothreonine (by MAPK). FT MOD_RES 205 205 Phosphotyrosine (By similarity). FT MOD_RES 223 223 Phosphotyrosine (By similarity). FT CONFLICT 28 28 D -> E (in Ref. 1 and 3). FT CONFLICT 37 37 L -> S (in Ref. 3). FT CONFLICT 51 52 AT -> SY (in Ref. 3). FT CONFLICT 55 55 G -> P (in Ref. 1). FT CONFLICT 63 63 L -> R (in Ref. 3). FT CONFLICT 74 74 E -> D (in Ref. 3). FT CONFLICT 96 96 Q -> H (in Ref. 3). FT CONFLICT 105 105 L -> V (in Ref. 3). FT CONFLICT 157 157 D -> V (in Ref. 3). FT CONFLICT 211 211 Q -> R (in Ref. 3). FT CONFLICT 217 217 D -> E (in Ref. 3). FT CONFLICT 225 225 A -> R (in Ref. 3). FT CONFLICT 234 234 D -> N (in Ref. 3). FT CONFLICT 360 360 G -> C (in Ref. 3). FT CONFLICT 383 383 K -> S (in Ref. 3). FT CONFLICT 392 392 G -> A (in Ref. 3). FT CONFLICT 408 409 KR -> NA (in Ref. 3). FT CONFLICT 413 413 R -> A (in Ref. 3). FT STRAND 33 34 FT STRAND 36 37 FT STRAND 40 41 FT STRAND 47 48 FT TURN 53 54 FT HELIX 55 61 FT TURN 62 63 FT STRAND 67 67 FT TURN 69 70 FT STRAND 71 71 FT HELIX 74 87 FT TURN 88 89 FT STRAND 92 92 FT HELIX 95 98 FT STRAND 100 101 FT HELIX 102 111 FT TURN 112 112 FT HELIX 113 116 FT STRAND 117 117 FT TURN 119 120 FT HELIX 121 132 FT STRAND 302 302 FT HELIX 304 312 FT TURN 313 315 FT STRAND 317 317 FT STRAND 320 321 FT HELIX 323 330 FT TURN 331 331 FT STRAND 333 334 FT HELIX 337 345 FT TURN 346 346 FT HELIX 348 350 FT TURN 351 353 FT STRAND 355 356 FT STRAND 358 359 FT TURN 360 361 FT STRAND 362 364 FT STRAND 366 367 FT HELIX 368 379 FT TURN 380 380 FT TURN 382 383 FT HELIX 386 395 FT TURN 396 400 FT STRAND 401 404 FT TURN 406 407 FT STRAND 408 414 FT STRAND 416 416 FT HELIX 418 422 FT STRAND 423 423 FT HELIX 426 432 FT TURN 433 434 SQ SEQUENCE 440 AA; 50202 MW; 151164D83C41B143 CRC64; MKAAVDLKPT LTIIKTEKVD LELFPSPDME CADVPLLTPS SKEMMSQALK ATFSGFTKEQ QRLGIPKDPR QWTETHVRDW VMWAVNEFSL KGVDFQKFCM SGAALCALGK ECFLELAPDF VGDILWEHLE ILQKEDVKPY QVNGANPTYP ESCYTSDYFI SYGIEHAQCV PPSEFSEPSF ITESYQTLHP ISSEELLSLK YENDYPSVIL QDPLQTDTLQ TDYFAIKQEV LTPDNMCLGR ASRGKLGGQD SFESVESYDS CDRLTQSWSS QSSFNSLQRV PSYDSFDYED YPAALPNHKP KGTFKDYVRD RADLNKDKPV IPAAALAGYT GSGPIQLWQF LLELLTDKSC QSFISWTGDG WEFKLSDPDE VARRWGKRKN KPKMNYEKLS RGLRYYYDKN IIHKTAGKRY VYRFVCDLQS LLGYTPEELH AMLDVKPDAD //