ELK1_RAT
ID ELK1_RAT Reviewed; 427 AA.
AC A4GTP4;
DT 14-OCT-2015, integrated into UniProtKB/Swiss-Prot.
DT 17-APR-2007, sequence version 1.
DT 03-AUG-2022, entry version 120.
DE RecName: Full=ETS domain-containing protein Elk-1 {ECO:0000305};
GN Name=Elk1 {ECO:0000312|RGD:1598663};
OS Rattus norvegicus (Rat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Rattus.
OX NCBI_TaxID=10116;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC STRAIN=Sprague-Dawley {ECO:0000312|EMBL:ABO27185.1};
RC TISSUE=Hippocampus {ECO:0000312|EMBL:ABO27185.1};
RA Tyan S.-W., Tsai M.-C., Lin C.-L., Ma Y.-L., Lee E.H.Y.;
RT "Serum- and glucocorticoid-inducible kinase 1 regulates zif268 expression
RT through the mediation of SRF and CREB1.";
RL Submitted (FEB-2007) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Brown Norway;
RX PubMed=15057822; DOI=10.1038/nature02426;
RA Gibbs R.A., Weinstock G.M., Metzker M.L., Muzny D.M., Sodergren E.J.,
RA Scherer S., Scott G., Steffen D., Worley K.C., Burch P.E., Okwuonu G.,
RA Hines S., Lewis L., Deramo C., Delgado O., Dugan-Rocha S., Miner G.,
RA Morgan M., Hawes A., Gill R., Holt R.A., Adams M.D., Amanatides P.G.,
RA Baden-Tillson H., Barnstead M., Chin S., Evans C.A., Ferriera S.,
RA Fosler C., Glodek A., Gu Z., Jennings D., Kraft C.L., Nguyen T.,
RA Pfannkoch C.M., Sitter C., Sutton G.G., Venter J.C., Woodage T., Smith D.,
RA Lee H.-M., Gustafson E., Cahill P., Kana A., Doucette-Stamm L.,
RA Weinstock K., Fechtel K., Weiss R.B., Dunn D.M., Green E.D.,
RA Blakesley R.W., Bouffard G.G., De Jong P.J., Osoegawa K., Zhu B., Marra M.,
RA Schein J., Bosdet I., Fjell C., Jones S., Krzywinski M., Mathewson C.,
RA Siddiqui A., Wye N., McPherson J., Zhao S., Fraser C.M., Shetty J.,
RA Shatsman S., Geer K., Chen Y., Abramzon S., Nierman W.C., Havlak P.H.,
RA Chen R., Durbin K.J., Egan A., Ren Y., Song X.-Z., Li B., Liu Y., Qin X.,
RA Cawley S., Cooney A.J., D'Souza L.M., Martin K., Wu J.Q.,
RA Gonzalez-Garay M.L., Jackson A.R., Kalafus K.J., McLeod M.P.,
RA Milosavljevic A., Virk D., Volkov A., Wheeler D.A., Zhang Z., Bailey J.A.,
RA Eichler E.E., Tuzun E., Birney E., Mongin E., Ureta-Vidal A., Woodwark C.,
RA Zdobnov E., Bork P., Suyama M., Torrents D., Alexandersson M., Trask B.J.,
RA Young J.M., Huang H., Wang H., Xing H., Daniels S., Gietzen D., Schmidt J.,
RA Stevens K., Vitt U., Wingrove J., Camara F., Mar Alba M., Abril J.F.,
RA Guigo R., Smit A., Dubchak I., Rubin E.M., Couronne O., Poliakov A.,
RA Huebner N., Ganten D., Goesele C., Hummel O., Kreitler T., Lee Y.-A.,
RA Monti J., Schulz H., Zimdahl H., Himmelbauer H., Lehrach H., Jacob H.J.,
RA Bromberg S., Gullings-Handley J., Jensen-Seaman M.I., Kwitek A.E.,
RA Lazar J., Pasko D., Tonellato P.J., Twigger S., Ponting C.P., Duarte J.M.,
RA Rice S., Goodstadt L., Beatson S.A., Emes R.D., Winter E.E., Webber C.,
RA Brandt P., Nyakatura G., Adetobi M., Chiaromonte F., Elnitski L.,
RA Eswara P., Hardison R.C., Hou M., Kolbe D., Makova K., Miller W.,
RA Nekrutenko A., Riemer C., Schwartz S., Taylor J., Yang S., Zhang Y.,
RA Lindpaintner K., Andrews T.D., Caccamo M., Clamp M., Clarke L., Curwen V.,
RA Durbin R.M., Eyras E., Searle S.M., Cooper G.M., Batzoglou S., Brudno M.,
RA Sidow A., Stone E.A., Payseur B.A., Bourque G., Lopez-Otin C., Puente X.S.,
RA Chakrabarti K., Chatterji S., Dewey C., Pachter L., Bray N., Yap V.B.,
RA Caspi A., Tesler G., Pevzner P.A., Haussler D., Roskin K.M., Baertsch R.,
RA Clawson H., Furey T.S., Hinrichs A.S., Karolchik D., Kent W.J.,
RA Rosenbloom K.R., Trumbower H., Weirauch M., Cooper D.N., Stenson P.D.,
RA Ma B., Brent M., Arumugam M., Shteynberg D., Copley R.R., Taylor M.S.,
RA Riethman H., Mudunuri U., Peterson J., Guyer M., Felsenfeld A., Old S.,
RA Mockrin S., Collins F.S.;
RT "Genome sequence of the Brown Norway rat yields insights into mammalian
RT evolution.";
RL Nature 428:493-521(2004).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Adams M.D., Myers E.W., Smith H.O., Venter J.C.;
RL Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP FUNCTION, AND PHOSPHORYLATION.
RX PubMed=17156131; DOI=10.1111/j.1471-4159.2006.04263.x;
RA Park J.B., Kim E.J., Yang E.J., Seo S.R., Chung K.C.;
RT "JNK- and Rac1-dependent induction of immediate early gene pip92 suppresses
RT neuronal differentiation.";
RL J. Neurochem. 100:555-566(2007).
CC -!- FUNCTION: Transcription factor that binds to purine-rich DNA sequences.
CC Forms a ternary complex with SRF and the ETS and SRF motifs of the
CC serum response element (SRE) on the promoter region of immediate early
CC genes such as FOS and IER2 (By similarity) (PubMed:17156131). Induces
CC target gene transcription upon JNK-signaling pathway stimulation
CC (PubMed:17156131). {ECO:0000250|UniProtKB:P19419,
CC ECO:0000269|PubMed:17156131}.
CC -!- SUBUNIT: Interacts in its sumoylated form with PIAS2/PIASX which
CC enhances its transcriptional activator activity. Interacts with MAD2L2;
CC the interaction is direct and promotes phosphorylation by the kinases
CC MAPK8 and/or MAPK9. Interacts with POU1F1.
CC {ECO:0000250|UniProtKB:P19419}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:P19419}.
CC -!- PTM: Sumoylation represses transcriptional activator activity as it
CC results in recruitment of HDAC2 to target gene promoters which leads to
CC decreased histone acetylation and reduced transactivator activity. It
CC also regulates nuclear retention. {ECO:0000250|UniProtKB:P19419}.
CC -!- PTM: On mitogenic stimulation, phosphorylated on C-terminal serine and
CC threonine residues by MAPK1. Ser-382 and Ser-388 are the preferred
CC sites for MAPK1. In vitro, phosphorylation by MAPK1 potentiates ternary
CC complex formation with the serum responses factors, SRE and SRF. Also
CC phosphorylated on Ser-382 by MAPK8 and/or MAKP9. Phosphorylation leads
CC to loss of sumoylation and restores transcriptional activator activity.
CC Phosphorylated and activated by CAMK4, MAPK11, MAPK12 and MAPK14 (By
CC similarity). Upon bFGF stimulus, phosphorylated by PAK1
CC (PubMed:17156131). {ECO:0000250|UniProtKB:P19419,
CC ECO:0000269|PubMed:17156131}.
CC -!- SIMILARITY: Belongs to the ETS family. {ECO:0000255|RuleBase:RU004019}.
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DR EMBL; EF429098; ABO27185.1; -; mRNA.
DR EMBL; AABR07036739; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH474009; EDL97728.1; -; Genomic_DNA.
DR RefSeq; NP_001101529.1; NM_001108059.3.
DR RefSeq; XP_006256676.1; XM_006256614.2.
DR AlphaFoldDB; A4GTP4; -.
DR SMR; A4GTP4; -.
DR CORUM; A4GTP4; -.
DR STRING; 10116.ENSRNOP00000013522; -.
DR iPTMnet; A4GTP4; -.
DR PhosphoSitePlus; A4GTP4; -.
DR PaxDb; A4GTP4; -.
DR Ensembl; ENSRNOT00000013522; ENSRNOP00000013522; ENSRNOG00000010171.
DR GeneID; 314436; -.
DR KEGG; rno:314436; -.
DR UCSC; RGD:1598663; rat.
DR CTD; 2002; -.
DR RGD; 1598663; Elk1.
DR eggNOG; KOG3806; Eukaryota.
DR GeneTree; ENSGT00940000157571; -.
DR HOGENOM; CLU_036905_0_0_1; -.
DR InParanoid; A4GTP4; -.
DR OMA; NTAQVCG; -.
DR OrthoDB; 981551at2759; -.
DR PhylomeDB; A4GTP4; -.
DR TreeFam; TF317732; -.
DR PRO; PR:A4GTP4; -.
DR Proteomes; UP000002494; Chromosome X.
DR Proteomes; UP000234681; Chromosome x.
DR Bgee; ENSRNOG00000010171; Expressed in skeletal muscle tissue and 19 other tissues.
DR Genevisible; A4GTP4; RN.
DR GO; GO:0043679; C:axon terminus; IDA:RGD.
DR GO; GO:0005737; C:cytoplasm; IDA:RGD.
DR GO; GO:0030425; C:dendrite; IDA:RGD.
DR GO; GO:0005739; C:mitochondrion; IDA:RGD.
DR GO; GO:0043025; C:neuronal cell body; IDA:RGD.
DR GO; GO:0005654; C:nucleoplasm; IEA:Ensembl.
DR GO; GO:0005634; C:nucleus; IDA:RGD.
DR GO; GO:0003682; F:chromatin binding; IDA:RGD.
DR GO; GO:0001228; F:DNA-binding transcription activator activity, RNA polymerase II-specific; ISO:RGD.
DR GO; GO:0003700; F:DNA-binding transcription factor activity; ISO:RGD.
DR GO; GO:0000981; F:DNA-binding transcription factor activity, RNA polymerase II-specific; IBA:GO_Central.
DR GO; GO:0003690; F:double-stranded DNA binding; IDA:RGD.
DR GO; GO:0030374; F:nuclear receptor coactivator activity; ISO:RGD.
DR GO; GO:0000978; F:RNA polymerase II cis-regulatory region sequence-specific DNA binding; IDA:RGD.
DR GO; GO:0061629; F:RNA polymerase II-specific DNA-binding transcription factor binding; ISO:RGD.
DR GO; GO:1990837; F:sequence-specific double-stranded DNA binding; ISO:RGD.
DR GO; GO:0000976; F:transcription cis-regulatory region binding; ISO:RGD.
DR GO; GO:0030154; P:cell differentiation; IBA:GO_Central.
DR GO; GO:0071480; P:cellular response to gamma radiation; IDA:RGD.
DR GO; GO:0071396; P:cellular response to lipid; IDA:RGD.
DR GO; GO:0071394; P:cellular response to testosterone stimulus; IEP:RGD.
DR GO; GO:0010467; P:gene expression; ISO:RGD.
DR GO; GO:0001889; P:liver development; ISO:RGD.
DR GO; GO:0030324; P:lung development; ISO:RGD.
DR GO; GO:1901216; P:positive regulation of neuron death; IMP:RGD.
DR GO; GO:0045944; P:positive regulation of transcription by RNA polymerase II; IDA:MGI.
DR GO; GO:0045893; P:positive regulation of transcription, DNA-templated; ISO:RGD.
DR GO; GO:0006357; P:regulation of transcription by RNA polymerase II; IBA:GO_Central.
DR GO; GO:0006355; P:regulation of transcription, DNA-templated; ISO:RGD.
DR GO; GO:0071774; P:response to fibroblast growth factor; IDA:UniProtKB.
DR GO; GO:0009416; P:response to light stimulus; IDA:RGD.
DR Gene3D; 1.10.10.10; -; 1.
DR InterPro; IPR000418; Ets_dom.
DR InterPro; IPR046328; ETS_fam.
DR InterPro; IPR036388; WH-like_DNA-bd_sf.
DR InterPro; IPR036390; WH_DNA-bd_sf.
DR PANTHER; PTHR11849; PTHR11849; 1.
DR Pfam; PF00178; Ets; 1.
DR PRINTS; PR00454; ETSDOMAIN.
DR SMART; SM00413; ETS; 1.
DR SUPFAM; SSF46785; SSF46785; 1.
DR PROSITE; PS00345; ETS_DOMAIN_1; 1.
DR PROSITE; PS00346; ETS_DOMAIN_2; 1.
DR PROSITE; PS50061; ETS_DOMAIN_3; 1.
PE 1: Evidence at protein level;
KW DNA-binding; Isopeptide bond; Nucleus; Phosphoprotein; Reference proteome;
KW Transcription; Transcription regulation; Ubl conjugation.
FT CHAIN 1..427
FT /note="ETS domain-containing protein Elk-1"
FT /id="PRO_0000433929"
FT DNA_BIND 5..86
FT /note="ETS"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00237"
FT REGION 116..146
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 166..202
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 226..252
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 300..350
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 348..398
FT /note="Sufficient for interaction with MAD2L2"
FT /evidence="ECO:0000250|UniProtKB:P19419"
FT COMPBIAS 334..350
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 323
FT /note="Phosphoserine; by MAPK1"
FT /evidence="ECO:0000250|UniProtKB:P19419"
FT MOD_RES 335
FT /note="Phosphothreonine; by MAPK1"
FT /evidence="ECO:0000250|UniProtKB:P19419"
FT MOD_RES 352
FT /note="Phosphothreonine; by MAPK1"
FT /evidence="ECO:0000250|UniProtKB:P19419"
FT MOD_RES 362
FT /note="Phosphothreonine; by MAPK1"
FT /evidence="ECO:0000250|UniProtKB:P19419"
FT MOD_RES 367
FT /note="Phosphothreonine; by MAPK1"
FT /evidence="ECO:0000250|UniProtKB:P19419"
FT MOD_RES 382
FT /note="Phosphoserine; by MAPK1 and MAPK8"
FT /evidence="ECO:0000250|UniProtKB:P19419"
FT MOD_RES 388
FT /note="Phosphoserine; by MAPK1"
FT /evidence="ECO:0000250|UniProtKB:P19419"
FT MOD_RES 416
FT /note="Phosphothreonine; by MAPK1"
FT /evidence="ECO:0000250|UniProtKB:P19419"
FT MOD_RES 421
FT /note="Phosphoserine; by MAPK1"
FT /evidence="ECO:0000250|UniProtKB:P19419"
FT CROSSLNK 229
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO)"
FT /evidence="ECO:0000250|UniProtKB:P19419"
FT CROSSLNK 248
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO)"
FT /evidence="ECO:0000250|UniProtKB:P19419"
FT CROSSLNK 253
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO)"
FT /evidence="ECO:0000250|UniProtKB:P19419"
SQ 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
