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ETS domain-containing protein Elk-1

 ELK1_RAT                Reviewed;         427 AA.
A4GTP4;
14-OCT-2015, integrated into UniProtKB/Swiss-Prot.
17-APR-2007, sequence version 1.
10-OCT-2018, entry version 105.
RecName: Full=ETS domain-containing protein Elk-1 {ECO:0000305};
Name=Elk1 {ECO:0000312|RGD:1598663};
Rattus norvegicus (Rat).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
Muroidea; Muridae; Murinae; Rattus.
NCBI_TaxID=10116;
[1]
NUCLEOTIDE SEQUENCE [MRNA].
STRAIN=Sprague-Dawley {ECO:0000312|EMBL:ABO27185.1};
TISSUE=Hippocampus {ECO:0000312|EMBL:ABO27185.1};
Tyan S.-W., Tsai M.-C., Lin C.-L., Ma Y.-L., Lee E.H.Y.;
"Serum- and glucocorticoid-inducible kinase 1 regulates zif268
expression through the mediation of SRF and CREB1.";
Submitted (FEB-2007) to the EMBL/GenBank/DDBJ databases.
[2]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=Brown Norway;
PubMed=15057822; DOI=10.1038/nature02426;
Gibbs R.A., Weinstock G.M., Metzker M.L., Muzny D.M., Sodergren E.J.,
Scherer S., Scott G., Steffen D., Worley K.C., Burch P.E., Okwuonu G.,
Hines S., Lewis L., Deramo C., Delgado O., Dugan-Rocha S., Miner G.,
Morgan M., Hawes A., Gill R., Holt R.A., Adams M.D., Amanatides P.G.,
Baden-Tillson H., Barnstead M., Chin S., Evans C.A., Ferriera S.,
Fosler C., Glodek A., Gu Z., Jennings D., Kraft C.L., Nguyen T.,
Pfannkoch C.M., Sitter C., Sutton G.G., Venter J.C., Woodage T.,
Smith D., Lee H.-M., Gustafson E., Cahill P., Kana A.,
Doucette-Stamm L., Weinstock K., Fechtel K., Weiss R.B., Dunn D.M.,
Green E.D., Blakesley R.W., Bouffard G.G., De Jong P.J., Osoegawa K.,
Zhu B., Marra M., Schein J., Bosdet I., Fjell C., Jones S.,
Krzywinski M., Mathewson C., Siddiqui A., Wye N., McPherson J.,
Zhao S., Fraser C.M., Shetty J., Shatsman S., Geer K., Chen Y.,
Abramzon S., Nierman W.C., Havlak P.H., Chen R., Durbin K.J., Egan A.,
Ren Y., Song X.-Z., Li B., Liu Y., Qin X., Cawley S., Cooney A.J.,
D'Souza L.M., Martin K., Wu J.Q., Gonzalez-Garay M.L., Jackson A.R.,
Kalafus K.J., McLeod M.P., Milosavljevic A., Virk D., Volkov A.,
Wheeler D.A., Zhang Z., Bailey J.A., Eichler E.E., Tuzun E.,
Birney E., Mongin E., Ureta-Vidal A., Woodwark C., Zdobnov E.,
Bork P., Suyama M., Torrents D., Alexandersson M., Trask B.J.,
Young J.M., Huang H., Wang H., Xing H., Daniels S., Gietzen D.,
Schmidt J., Stevens K., Vitt U., Wingrove J., Camara F., Mar Alba M.,
Abril J.F., Guigo R., Smit A., Dubchak I., Rubin E.M., Couronne O.,
Poliakov A., Huebner N., Ganten D., Goesele C., Hummel O.,
Kreitler T., Lee Y.-A., Monti J., Schulz H., Zimdahl H.,
Himmelbauer H., Lehrach H., Jacob H.J., Bromberg S.,
Gullings-Handley J., Jensen-Seaman M.I., Kwitek A.E., Lazar J.,
Pasko D., Tonellato P.J., Twigger S., Ponting C.P., Duarte J.M.,
Rice S., Goodstadt L., Beatson S.A., Emes R.D., Winter E.E.,
Webber C., Brandt P., Nyakatura G., Adetobi M., Chiaromonte F.,
Elnitski L., Eswara P., Hardison R.C., Hou M., Kolbe D., Makova K.,
Miller W., Nekrutenko A., Riemer C., Schwartz S., Taylor J., Yang S.,
Zhang Y., Lindpaintner K., Andrews T.D., Caccamo M., Clamp M.,
Clarke L., Curwen V., Durbin R.M., Eyras E., Searle S.M., Cooper G.M.,
Batzoglou S., Brudno M., Sidow A., Stone E.A., Payseur B.A.,
Bourque G., Lopez-Otin C., Puente X.S., Chakrabarti K., Chatterji S.,
Dewey C., Pachter L., Bray N., Yap V.B., Caspi A., Tesler G.,
Pevzner P.A., Haussler D., Roskin K.M., Baertsch R., Clawson H.,
Furey T.S., Hinrichs A.S., Karolchik D., Kent W.J., Rosenbloom K.R.,
Trumbower H., Weirauch M., Cooper D.N., Stenson P.D., Ma B., Brent M.,
Arumugam M., Shteynberg D., Copley R.R., Taylor M.S., Riethman H.,
Mudunuri U., Peterson J., Guyer M., Felsenfeld A., Old S., Mockrin S.,
Collins F.S.;
"Genome sequence of the Brown Norway rat yields insights into
mammalian evolution.";
Nature 428:493-521(2004).
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Mural R.J., Adams M.D., Myers E.W., Smith H.O., Venter J.C.;
Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
[4]
FUNCTION, AND PHOSPHORYLATION.
PubMed=17156131; DOI=10.1111/j.1471-4159.2006.04263.x;
Park J.B., Kim E.J., Yang E.J., Seo S.R., Chung K.C.;
"JNK- and Rac1-dependent induction of immediate early gene pip92
suppresses neuronal differentiation.";
J. Neurochem. 100:555-566(2007).
-!- FUNCTION: Transcription factor that binds to purine-rich DNA
sequences. Forms a ternary complex with SRF and the ETS and SRF
motifs of the serum response element (SRE) on the promoter region
of immediate early genes such as FOS and IER2 (By similarity)
(PubMed:17156131). Induces target gene transcription upon JNK-
signaling pathway stimulation (PubMed:17156131).
{ECO:0000250|UniProtKB:P19419, ECO:0000269|PubMed:17156131}.
-!- SUBUNIT: Interacts in its sumoylated form with PIAS2/PIASX which
enhances its transcriptional activator activity. Interacts with
MAD2L2; the interaction is direct and promotes phosphorylation by
the kinases MAPK8 and/or MAPK9. Interacts with POU1F1.
{ECO:0000250|UniProtKB:P19419}.
-!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:P19419}.
-!- PTM: Sumoylation represses transcriptional activator activity as
it results in recruitment of HDAC2 to target gene promoters which
leads to decreased histone acetylation and reduced transactivator
activity. It also regulates nuclear retention.
{ECO:0000250|UniProtKB:P19419}.
-!- PTM: On mitogenic stimulation, phosphorylated on C-terminal serine
and threonine residues by MAPK1. Ser-382 and Ser-388 are the
preferred sites for MAPK1. In vitro, phosphorylation by MAPK1
potentiates ternary complex formation with the serum responses
factors, SRE and SRF. Also phosphorylated on Ser-382 by MAPK8
and/or MAKP9. Phosphorylation leads to loss of sumoylation and
restores transcriptional activator activity. Phosphorylated and
activated by CAMK4, MAPK11, MAPK12 and MAPK14 (By similarity).
Upon bFGF stimulus, phosphorylated by PAK1 (PubMed:17156131).
{ECO:0000250|UniProtKB:P19419, ECO:0000269|PubMed:17156131}.
-!- SIMILARITY: Belongs to the ETS family.
{ECO:0000255|RuleBase:RU004019}.
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EMBL; EF429098; ABO27185.1; -; mRNA.
EMBL; AABR07036739; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; CH474009; EDL97728.1; -; Genomic_DNA.
RefSeq; NP_001101529.1; NM_001108059.3.
RefSeq; XP_006256676.1; XM_006256614.2.
UniGene; Rn.203416; -.
ProteinModelPortal; A4GTP4; -.
SMR; A4GTP4; -.
CORUM; A4GTP4; -.
STRING; 10116.ENSRNOP00000013522; -.
iPTMnet; A4GTP4; -.
PhosphoSitePlus; A4GTP4; -.
PaxDb; A4GTP4; -.
Ensembl; ENSRNOT00000013522; ENSRNOP00000013522; ENSRNOG00000010171.
GeneID; 314436; -.
KEGG; rno:314436; -.
UCSC; RGD:1598663; rat.
CTD; 2002; -.
RGD; 1598663; Elk1.
eggNOG; KOG3806; Eukaryota.
eggNOG; ENOG410Z0ZF; LUCA.
GeneTree; ENSGT00760000118907; -.
HOGENOM; HOG000237332; -.
HOVERGEN; HBG004344; -.
InParanoid; A4GTP4; -.
KO; K04375; -.
OMA; RRATHRF; -.
OrthoDB; EOG091G0CL4; -.
PhylomeDB; A4GTP4; -.
TreeFam; TF317732; -.
PRO; PR:A4GTP4; -.
Proteomes; UP000002494; Chromosome X.
Bgee; ENSRNOG00000010171; Expressed in 10 organ(s), highest expression level in skeletal muscle tissue.
Genevisible; A4GTP4; RN.
GO; GO:0043679; C:axon terminus; IDA:RGD.
GO; GO:0005737; C:cytoplasm; IDA:RGD.
GO; GO:0030425; C:dendrite; IDA:RGD.
GO; GO:0005739; C:mitochondrion; IDA:RGD.
GO; GO:0043025; C:neuronal cell body; IDA:RGD.
GO; GO:0005654; C:nucleoplasm; IEA:Ensembl.
GO; GO:0005634; C:nucleus; IDA:RGD.
GO; GO:0003682; F:chromatin binding; IDA:RGD.
GO; GO:0003690; F:double-stranded DNA binding; IDA:RGD.
GO; GO:0000978; F:RNA polymerase II proximal promoter sequence-specific DNA binding; IDA:RGD.
GO; GO:0000981; F:RNA polymerase II transcription factor activity, sequence-specific DNA binding; IBA:GO_Central.
GO; GO:0001085; F:RNA polymerase II transcription factor binding; IEA:Ensembl.
GO; GO:0001077; F:transcriptional activator activity, RNA polymerase II proximal promoter sequence-specific DNA binding; IEA:Ensembl.
GO; GO:0030154; P:cell differentiation; IBA:GO_Central.
GO; GO:0071480; P:cellular response to gamma radiation; IDA:RGD.
GO; GO:0071396; P:cellular response to lipid; IDA:RGD.
GO; GO:0071394; P:cellular response to testosterone stimulus; IEP:RGD.
GO; GO:1901216; P:positive regulation of neuron death; IMP:RGD.
GO; GO:0045944; P:positive regulation of transcription by RNA polymerase II; IDA:MGI.
GO; GO:0071774; P:response to fibroblast growth factor; IDA:UniProtKB.
GO; GO:0009416; P:response to light stimulus; IDA:RGD.
Gene3D; 1.10.10.10; -; 1.
InterPro; IPR000418; Ets_dom.
InterPro; IPR036388; WH-like_DNA-bd_sf.
InterPro; IPR036390; WH_DNA-bd_sf.
Pfam; PF00178; Ets; 1.
PRINTS; PR00454; ETSDOMAIN.
SMART; SM00413; ETS; 1.
SUPFAM; SSF46785; SSF46785; 1.
PROSITE; PS00345; ETS_DOMAIN_1; 1.
PROSITE; PS00346; ETS_DOMAIN_2; 1.
PROSITE; PS50061; ETS_DOMAIN_3; 1.
1: Evidence at protein level;
Complete proteome; DNA-binding; Isopeptide bond; Nucleus;
Phosphoprotein; Reference proteome; Transcription;
Transcription regulation; Ubl conjugation.
CHAIN 1 427 ETS domain-containing protein Elk-1.
/FTId=PRO_0000433929.
DNA_BIND 5 86 ETS. {ECO:0000255|PROSITE-
ProRule:PRU00237}.
REGION 348 398 Sufficient for interaction with MAD2L2.
{ECO:0000250|UniProtKB:P19419}.
MOD_RES 323 323 Phosphoserine; by MAPK1.
{ECO:0000250|UniProtKB:P19419}.
MOD_RES 335 335 Phosphothreonine; by MAPK1.
{ECO:0000250|UniProtKB:P19419}.
MOD_RES 352 352 Phosphothreonine; by MAPK1.
{ECO:0000250|UniProtKB:P19419}.
MOD_RES 362 362 Phosphothreonine; by MAPK1.
{ECO:0000250|UniProtKB:P19419}.
MOD_RES 367 367 Phosphothreonine; by MAPK1.
{ECO:0000250|UniProtKB:P19419}.
MOD_RES 382 382 Phosphoserine; by MAPK1 and MAPK8.
{ECO:0000250|UniProtKB:P19419}.
MOD_RES 388 388 Phosphoserine; by MAPK1.
{ECO:0000250|UniProtKB:P19419}.
MOD_RES 416 416 Phosphothreonine; by MAPK1.
{ECO:0000250|UniProtKB:P19419}.
MOD_RES 421 421 Phosphoserine; by MAPK1.
{ECO:0000250|UniProtKB:P19419}.
CROSSLNK 229 229 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in SUMO).
{ECO:0000250|UniProtKB:P19419}.
CROSSLNK 248 248 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in SUMO).
{ECO:0000250|UniProtKB:P19419}.
CROSSLNK 253 253 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in SUMO).
{ECO:0000250|UniProtKB:P19419}.
SEQUENCE 427 AA; 45272 MW; C318C5A55E4785E7 CRC64;
MDPSVTLWQF LLQLLREQGN GHIISWTSRD GGEFKLVDAE EVARLWGLRK NKTNMNYDKL
SRALRYYYDK NIIRKVSGQK FVYKFVSYPE VAGCSTEDCP PQPEVSVTSA VAMAPATVHS
GPGDNATGKP GTPKGAGMTG QGGLARSSRN EYMRSGLYST FTIQSLQPQP PLHPRPASVL
PNTTPAGVPA PPSGSRSTSP NPLEACLEAE EAGLPLQVIL TPPEAPNQKS EELSLNPGFG
RPQPPEVKVE GPKEELEVTE VGGFSPEAVK AEQEVSPSEG LLARLPAILT ENTAQVCGLS
TSTTEITQPQ KGRKPRDLEL PLSPSLLGGQ GPERTPGSGT SSGLQAQGPA LTPSLLPTHT
LTPVLLTPSS LPPSIHFWST LSPIAPRSPA KLSFQFPSSG SAQVHIPSIS VDGLSTPVVL
SPGPQKP


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