ELK1_HUMAN
ID ELK1_HUMAN Reviewed; 428 AA.
AC P19419; B2R7H4; O75606; O95058; Q969X8; Q9UJM4;
DT 01-NOV-1990, integrated into UniProtKB/Swiss-Prot.
DT 24-JAN-2001, sequence version 2.
DT 03-AUG-2022, entry version 227.
DE RecName: Full=ETS domain-containing protein Elk-1;
GN Name=ELK1;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), AND VARIANT ASN-183.
RX PubMed=2539641; DOI=10.1126/science.2539641;
RA Rao V.N., Huebner K., Isobe M., Ar-Rushdi A., Croce C.M., Reddy E.S.P.;
RT "elk, tissue-specific ets-related genes on chromosomes X and 14 near
RT translocation breakpoints.";
RL Science 244:66-70(1989).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] (ISOFORM 1).
RX PubMed=9795224; DOI=10.1016/s0378-1119(98)00448-x;
RA Harindranath N., Mills F.C., Mitchell M.P., Meindl A., Max E.E.;
RT "The human elk-1 gene family: the functional gene and two processed
RT pseudogenes embedded in the IgH locus.";
RL Gene 221:215-224(1998).
RN [3]
RP NUCLEOTIDE SEQUENCE (ISOFORM 2).
RA Aryee D.N.T., Kovar H.;
RT "Novel family members HuER71, ELFR, and ELKv among ETS-related genes
RT coexpressed with EWS-FLI1 in Ewing tumor cell lines.";
RL Submitted (APR-1997) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA] (ISOFORM 1).
RC TISSUE=Hippocampus;
RX PubMed=10231026; DOI=10.1093/dnares/6.1.21;
RA Yamauchi T., Toko M., Suga M., Hatakeyama T., Isobe M.;
RT "Structural organization of the human ELK1 gene and its processed
RT pseudogene ELK2 genes.";
RL DNA Res. 6:21-27(1999).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=Urinary bladder;
RX PubMed=14702039; DOI=10.1038/ng1285;
RA Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
RA Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
RA Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
RA Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
RA Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H.,
RA Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M.,
RA Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K.,
RA Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T.,
RA Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M.,
RA Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S.,
RA Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H.,
RA Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K.,
RA Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N.,
RA Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
RA Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
RA Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
RA Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
RA Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y.,
RA Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K.,
RA Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T.,
RA Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T.,
RA Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y.,
RA Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H.,
RA Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y.,
RA Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H.,
RA Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O.,
RA Isogai T., Sugano S.;
RT "Complete sequencing and characterization of 21,243 full-length human
RT cDNAs.";
RL Nat. Genet. 36:40-45(2004).
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=15772651; DOI=10.1038/nature03440;
RA Ross M.T., Grafham D.V., Coffey A.J., Scherer S., McLay K., Muzny D.,
RA Platzer M., Howell G.R., Burrows C., Bird C.P., Frankish A., Lovell F.L.,
RA Howe K.L., Ashurst J.L., Fulton R.S., Sudbrak R., Wen G., Jones M.C.,
RA Hurles M.E., Andrews T.D., Scott C.E., Searle S., Ramser J., Whittaker A.,
RA Deadman R., Carter N.P., Hunt S.E., Chen R., Cree A., Gunaratne P.,
RA Havlak P., Hodgson A., Metzker M.L., Richards S., Scott G., Steffen D.,
RA Sodergren E., Wheeler D.A., Worley K.C., Ainscough R., Ambrose K.D.,
RA Ansari-Lari M.A., Aradhya S., Ashwell R.I., Babbage A.K., Bagguley C.L.,
RA Ballabio A., Banerjee R., Barker G.E., Barlow K.F., Barrett I.P.,
RA Bates K.N., Beare D.M., Beasley H., Beasley O., Beck A., Bethel G.,
RA Blechschmidt K., Brady N., Bray-Allen S., Bridgeman A.M., Brown A.J.,
RA Brown M.J., Bonnin D., Bruford E.A., Buhay C., Burch P., Burford D.,
RA Burgess J., Burrill W., Burton J., Bye J.M., Carder C., Carrel L.,
RA Chako J., Chapman J.C., Chavez D., Chen E., Chen G., Chen Y., Chen Z.,
RA Chinault C., Ciccodicola A., Clark S.Y., Clarke G., Clee C.M., Clegg S.,
RA Clerc-Blankenburg K., Clifford K., Cobley V., Cole C.G., Conquer J.S.,
RA Corby N., Connor R.E., David R., Davies J., Davis C., Davis J., Delgado O.,
RA Deshazo D., Dhami P., Ding Y., Dinh H., Dodsworth S., Draper H.,
RA Dugan-Rocha S., Dunham A., Dunn M., Durbin K.J., Dutta I., Eades T.,
RA Ellwood M., Emery-Cohen A., Errington H., Evans K.L., Faulkner L.,
RA Francis F., Frankland J., Fraser A.E., Galgoczy P., Gilbert J., Gill R.,
RA Gloeckner G., Gregory S.G., Gribble S., Griffiths C., Grocock R., Gu Y.,
RA Gwilliam R., Hamilton C., Hart E.A., Hawes A., Heath P.D., Heitmann K.,
RA Hennig S., Hernandez J., Hinzmann B., Ho S., Hoffs M., Howden P.J.,
RA Huckle E.J., Hume J., Hunt P.J., Hunt A.R., Isherwood J., Jacob L.,
RA Johnson D., Jones S., de Jong P.J., Joseph S.S., Keenan S., Kelly S.,
RA Kershaw J.K., Khan Z., Kioschis P., Klages S., Knights A.J., Kosiura A.,
RA Kovar-Smith C., Laird G.K., Langford C., Lawlor S., Leversha M., Lewis L.,
RA Liu W., Lloyd C., Lloyd D.M., Loulseged H., Loveland J.E., Lovell J.D.,
RA Lozado R., Lu J., Lyne R., Ma J., Maheshwari M., Matthews L.H.,
RA McDowall J., McLaren S., McMurray A., Meidl P., Meitinger T., Milne S.,
RA Miner G., Mistry S.L., Morgan M., Morris S., Mueller I., Mullikin J.C.,
RA Nguyen N., Nordsiek G., Nyakatura G., O'dell C.N., Okwuonu G., Palmer S.,
RA Pandian R., Parker D., Parrish J., Pasternak S., Patel D., Pearce A.V.,
RA Pearson D.M., Pelan S.E., Perez L., Porter K.M., Ramsey Y., Reichwald K.,
RA Rhodes S., Ridler K.A., Schlessinger D., Schueler M.G., Sehra H.K.,
RA Shaw-Smith C., Shen H., Sheridan E.M., Shownkeen R., Skuce C.D.,
RA Smith M.L., Sotheran E.C., Steingruber H.E., Steward C.A., Storey R.,
RA Swann R.M., Swarbreck D., Tabor P.E., Taudien S., Taylor T., Teague B.,
RA Thomas K., Thorpe A., Timms K., Tracey A., Trevanion S., Tromans A.C.,
RA d'Urso M., Verduzco D., Villasana D., Waldron L., Wall M., Wang Q.,
RA Warren J., Warry G.L., Wei X., West A., Whitehead S.L., Whiteley M.N.,
RA Wilkinson J.E., Willey D.L., Williams G., Williams L., Williamson A.,
RA Williamson H., Wilming L., Woodmansey R.L., Wray P.W., Yen J., Zhang J.,
RA Zhou J., Zoghbi H., Zorilla S., Buck D., Reinhardt R., Poustka A.,
RA Rosenthal A., Lehrach H., Meindl A., Minx P.J., Hillier L.W., Willard H.F.,
RA Wilson R.K., Waterston R.H., Rice C.M., Vaudin M., Coulson A., Nelson D.L.,
RA Weinstock G., Sulston J.E., Durbin R.M., Hubbard T., Gibbs R.A., Beck S.,
RA Rogers J., Bentley D.R.;
RT "The DNA sequence of the human X chromosome.";
RL Nature 434:325-337(2005).
RN [7]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M.,
RA Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J.,
RA Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S.,
RA Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H.,
RA Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K.,
RA Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D.,
RA Hunkapiller M.W., Myers E.W., Venter J.C.;
RL Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN [8]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=Uterus;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [9]
RP PROTEIN SEQUENCE OF 318-331; 336-364 AND 380-408, FUNCTION, PHOSPHORYLATION
RP AT SER-324; THR-336; SER-383; SER-389 AND SER-422, AND MUTAGENESIS OF
RP SER-324; THR-336; THR-353; THR-363; THR-368; SER-383; SER-389; THR-417 AND
RP SER-422.
RX PubMed=7889942; DOI=10.1002/j.1460-2075.1995.tb07076.x;
RA Gille H., Kortenjann M., Thomae O., Moomaw C., Slaughter C., Cobb M.H.,
RA Shaw P.E.;
RT "ERK phosphorylation potentiates Elk-1-mediated ternary complex formation
RT and transactivation.";
RL EMBO J. 14:951-962(1995).
RN [10]
RP DOMAINS, AND FUNCTION.
RX PubMed=1630903; DOI=10.1093/nar/20.13.3317;
RA Janknecht R., Nordheim A.;
RT "Elk-1 protein domains required for direct and SRF-assisted DNA-binding.";
RL Nucleic Acids Res. 20:3317-3324(1992).
RN [11]
RP PHOSPHORYLATION BY CAMK4.
RX PubMed=8855261; DOI=10.1073/pnas.93.20.10803;
RA Enslen H., Tokumitsu H., Stork P.J., Davis R.J., Soderling T.R.;
RT "Regulation of mitogen-activated protein kinases by a calcium/calmodulin-
RT dependent protein kinase cascade.";
RL Proc. Natl. Acad. Sci. U.S.A. 93:10803-10808(1996).
RN [12]
RP PHOSPHORYLATION BY MAPK11; MAPK12 AND MAPK14.
RX PubMed=9430721; DOI=10.1074/jbc.273.3.1741;
RA Enslen H., Raingeaud J., Davis R.J.;
RT "Selective activation of p38 mitogen-activated protein (MAP) kinase
RT isoforms by the MAP kinase kinases MKK3 and MKK6.";
RL J. Biol. Chem. 273:1741-1748(1998).
RN [13]
RP PHOSPHORYLATION AT THR-353; THR-363; THR-368; SER-383; SER-389 AND THR-417.
RX PubMed=10637505; DOI=10.1038/sj.onc.1203362;
RA Cruzalegui F.H., Cano E., Treisman R.;
RT "ERK activation induces phosphorylation of Elk-1 at multiple S/T-P motifs
RT to high stoichiometry.";
RL Oncogene 18:7948-7957(1999).
RN [14]
RP SUMOYLATION AT LYS-249, AND MUTAGENESIS OF LYS-230 AND LYS-249.
RX PubMed=12887893; DOI=10.1016/s1097-2765(03)00265-x;
RA Yang S.-H., Jaffray E., Hay R.T., Sharrocks A.D.;
RT "Dynamic interplay of the SUMO and ERK pathways in regulating Elk-1
RT transcriptional activity.";
RL Mol. Cell 12:63-74(2003).
RN [15]
RP SUMOYLATION AT LYS-230; LYS-249 AND LYS-254, AND MUTAGENESIS OF LYS-230;
RP LYS-249 AND LYS-254.
RX PubMed=15210726; DOI=10.1083/jcb.200310136;
RA Salinas S., Briancon-Marjollet A., Bossis G., Lopez M.-A., Piechaczyk M.,
RA Jariel-Encontre I., Debant A., Hipskind R.A.;
RT "SUMOylation regulates nucleo-cytoplasmic shuttling of Elk-1.";
RL J. Cell Biol. 165:767-773(2004).
RN [16]
RP SUMOYLATION.
RX PubMed=14992729; DOI=10.1016/s1097-2765(04)00060-7;
RA Yang S.-H., Sharrocks A.D.;
RT "SUMO promotes HDAC-mediated transcriptional repression.";
RL Mol. Cell 13:611-617(2004).
RN [17]
RP INTERACTION WITH PIAS2.
RX PubMed=15920481; DOI=10.1038/sj.emboj.7600690;
RA Yang S.-H., Sharrocks A.D.;
RT "PIASx acts as an Elk-1 coactivator by facilitating derepression.";
RL EMBO J. 24:2161-2171(2005).
RN [18]
RP INTERACTION WITH MAD2L2, PHOSPHORYLATION AT SER-383, AND MUTAGENESIS OF
RP SER-383.
RX PubMed=17296730; DOI=10.1128/mcb.02276-06;
RA Zhang L., Yang S.H., Sharrocks A.D.;
RT "Rev7/MAD2B links c-Jun N-terminal protein kinase pathway signaling to
RT activation of the transcription factor Elk-1.";
RL Mol. Cell. Biol. 27:2861-2869(2007).
RN [19]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=18669648; DOI=10.1073/pnas.0805139105;
RA Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,
RA Elledge S.J., Gygi S.P.;
RT "A quantitative atlas of mitotic phosphorylation.";
RL Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008).
RN [20]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-324 AND SER-422, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Leukemic T-cell;
RX PubMed=19690332; DOI=10.1126/scisignal.2000007;
RA Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K.,
RA Rodionov V., Han D.K.;
RT "Quantitative phosphoproteomic analysis of T cell receptor signaling
RT reveals system-wide modulation of protein-protein interactions.";
RL Sci. Signal. 2:RA46-RA46(2009).
RN [21]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-324, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma, and Erythroleukemia;
RX PubMed=23186163; DOI=10.1021/pr300630k;
RA Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J.,
RA Mohammed S.;
RT "Toward a comprehensive characterization of a human cancer cell
RT phosphoproteome.";
RL J. Proteome Res. 12:260-271(2013).
RN [22]
RP INTERACTION WITH POU1F1.
RX PubMed=26612202; DOI=10.1093/hmg/ddv486;
RA Sobrier M.L., Tsai Y.C., Perez C., Leheup B., Bouceba T., Duquesnoy P.,
RA Copin B., Sizova D., Penzo A., Stanger B.Z., Cooke N.E., Liebhaber S.A.,
RA Amselem S.;
RT "Functional characterization of a human POU1F1 mutation associated with
RT isolated growth hormone deficiency: a novel etiology for IGHD.";
RL Hum. Mol. Genet. 25:472-483(2016).
RN [23]
RP X-RAY CRYSTALLOGRAPHY (2.1 ANGSTROMS) OF 1-94.
RX PubMed=10742173; DOI=10.1038/74055;
RA Mo Y., Vaessen B., Johnston K., Marmorstein R.;
RT "Structure of the elk-1-DNA complex reveals how DNA-distal residues affect
RT ETS domain recognition of DNA.";
RL Nat. Struct. Biol. 7:292-297(2000).
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. Induces target gene transcription upon JNK-
CC signaling pathway stimulation (By similarity).
CC {ECO:0000250|UniProtKB:A4GTP4, ECO:0000269|PubMed:1630903,
CC ECO:0000269|PubMed:7889942}.
CC -!- SUBUNIT: Interacts in its sumoylated form with PIAS2/PIASX which
CC enhances its transcriptional activator activity (PubMed:15920481).
CC Interacts with MAD2L2; the interaction is direct and promotes
CC phosphorylation by the kinases MAPK8 and/or MAPK9 (PubMed:17296730).
CC Interacts with POU1F1 (PubMed:26612202). {ECO:0000269|PubMed:15920481,
CC ECO:0000269|PubMed:17296730, ECO:0000269|PubMed:26612202}.
CC -!- INTERACTION:
CC P19419; P05067: APP; NbExp=3; IntAct=EBI-726632, EBI-77613;
CC P19419; Q06787-7: FMR1; NbExp=3; IntAct=EBI-726632, EBI-25856644;
CC P19419; O00358: FOXE1; NbExp=8; IntAct=EBI-726632, EBI-11317834;
CC P19419; P27361: MAPK3; NbExp=2; IntAct=EBI-726632, EBI-73995;
CC P19419; Q16236: NFE2L2; NbExp=5; IntAct=EBI-726632, EBI-2007911;
CC P19419; P63165: SUMO1; NbExp=5; IntAct=EBI-726632, EBI-80140;
CC P19419; P63279: UBE2I; NbExp=7; IntAct=EBI-726632, EBI-80168;
CC P19419-1; P63165: SUMO1; NbExp=2; IntAct=EBI-15799641, EBI-80140;
CC -!- SUBCELLULAR LOCATION: Nucleus.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=P19419-1; Sequence=Displayed;
CC Name=2; Synonyms=ELKV;
CC IsoId=P19419-2; Sequence=VSP_001466, VSP_001467;
CC -!- TISSUE SPECIFICITY: Lung and testis.
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.
CC -!- PTM: On mitogenic stimulation, phosphorylated on C-terminal serine and
CC threonine residues by MAPK1. Ser-383 and Ser-389 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-383 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. Upon
CC bFGF stimulus, phosphorylated by PAK1 (By similarity).
CC {ECO:0000250|UniProtKB:A4GTP4, ECO:0000269|PubMed:10637505,
CC ECO:0000269|PubMed:17296730, ECO:0000269|PubMed:7889942,
CC ECO:0000269|PubMed:8855261, ECO:0000269|PubMed:9430721}.
CC -!- SIMILARITY: Belongs to the ETS family. {ECO:0000305}.
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DR EMBL; M25269; AAA52384.1; -; mRNA.
DR EMBL; AF080616; AAC82466.1; -; Genomic_DNA.
DR EMBL; AF000672; AAD00862.1; -; mRNA.
DR EMBL; AB016193; BAA36616.1; -; mRNA.
DR EMBL; AB016194; BAA36617.1; -; Genomic_DNA.
DR EMBL; AK312984; BAG35821.1; -; mRNA.
DR EMBL; AL009172; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH471164; EAW59321.1; -; Genomic_DNA.
DR EMBL; BC056150; AAH56150.1; -; mRNA.
DR CCDS; CCDS14283.1; -. [P19419-1]
DR CCDS; CCDS59165.1; -. [P19419-2]
DR PIR; A41354; TVHUEK.
DR RefSeq; NP_001107595.1; NM_001114123.2. [P19419-1]
DR RefSeq; NP_001244097.1; NM_001257168.1. [P19419-2]
DR RefSeq; NP_005220.2; NM_005229.4. [P19419-1]
DR RefSeq; XP_016884828.1; XM_017029339.1.
DR PDB; 1DUX; X-ray; 2.10 A; C/F=1-94.
DR PDB; 5VVT; X-ray; 2.80 A; B/D=378-385.
DR PDBsum; 1DUX; -.
DR PDBsum; 5VVT; -.
DR AlphaFoldDB; P19419; -.
DR SMR; P19419; -.
DR BioGRID; 108317; 107.
DR CORUM; P19419; -.
DR DIP; DIP-36057N; -.
DR ELM; P19419; -.
DR IntAct; P19419; 87.
DR MINT; P19419; -.
DR STRING; 9606.ENSP00000483056; -.
DR BindingDB; P19419; -.
DR ChEMBL; CHEMBL4453; -.
DR GlyGen; P19419; 1 site, 1 O-linked glycan (1 site).
DR iPTMnet; P19419; -.
DR PhosphoSitePlus; P19419; -.
DR BioMuta; ELK1; -.
DR DMDM; 12643407; -.
DR EPD; P19419; -.
DR jPOST; P19419; -.
DR MassIVE; P19419; -.
DR MaxQB; P19419; -.
DR PaxDb; P19419; -.
DR PeptideAtlas; P19419; -.
DR PRIDE; P19419; -.
DR ProteomicsDB; 53656; -. [P19419-1]
DR ProteomicsDB; 53657; -. [P19419-2]
DR Antibodypedia; 3538; 1311 antibodies from 49 providers.
DR DNASU; 2002; -.
DR Ensembl; ENST00000247161.7; ENSP00000247161.3; ENSG00000126767.18. [P19419-1]
DR Ensembl; ENST00000343894.8; ENSP00000345585.4; ENSG00000126767.18. [P19419-2]
DR Ensembl; ENST00000376983.8; ENSP00000366182.3; ENSG00000126767.18. [P19419-1]
DR GeneID; 2002; -.
DR KEGG; hsa:2002; -.
DR MANE-Select; ENST00000376983.8; ENSP00000366182.3; NM_001114123.3; NP_001107595.1.
DR UCSC; uc004dik.6; human. [P19419-1]
DR CTD; 2002; -.
DR DisGeNET; 2002; -.
DR GeneCards; ELK1; -.
DR HGNC; HGNC:3321; ELK1.
DR HPA; ENSG00000126767; Low tissue specificity.
DR MIM; 311040; gene.
DR neXtProt; NX_P19419; -.
DR OpenTargets; ENSG00000126767; -.
DR PharmGKB; PA27749; -.
DR VEuPathDB; HostDB:ENSG00000126767; -.
DR eggNOG; KOG3806; Eukaryota.
DR GeneTree; ENSGT00940000157571; -.
DR HOGENOM; CLU_036905_0_0_1; -.
DR InParanoid; P19419; -.
DR OMA; NTAQVCG; -.
DR PhylomeDB; P19419; -.
DR TreeFam; TF317732; -.
DR PathwayCommons; P19419; -.
DR Reactome; R-HSA-198753; ERK/MAPK targets.
DR Reactome; R-HSA-9031628; NGF-stimulated transcription.
DR Reactome; R-HSA-9609690; HCMV Early Events.
DR Reactome; R-HSA-9634638; Estrogen-dependent nuclear events downstream of ESR-membrane signaling.
DR SignaLink; P19419; -.
DR SIGNOR; P19419; -.
DR BioGRID-ORCS; 2002; 35 hits in 730 CRISPR screens.
DR ChiTaRS; ELK1; human.
DR EvolutionaryTrace; P19419; -.
DR GeneWiki; ELK1; -.
DR GenomeRNAi; 2002; -.
DR Pharos; P19419; Tbio.
DR PRO; PR:P19419; -.
DR Proteomes; UP000005640; Chromosome X.
DR RNAct; P19419; protein.
DR Bgee; ENSG00000126767; Expressed in olfactory bulb and 204 other tissues.
DR ExpressionAtlas; P19419; baseline and differential.
DR Genevisible; P19419; HS.
DR GO; GO:0043679; C:axon terminus; IEA:Ensembl.
DR GO; GO:0000785; C:chromatin; ISA:NTNU_SB.
DR GO; GO:0030425; C:dendrite; IEA:Ensembl.
DR GO; GO:0005739; C:mitochondrion; IEA:Ensembl.
DR GO; GO:0043025; C:neuronal cell body; IEA:Ensembl.
DR GO; GO:0005654; C:nucleoplasm; IDA:HPA.
DR GO; GO:0005634; C:nucleus; IDA:BHF-UCL.
DR GO; GO:0003682; F:chromatin binding; IEA:Ensembl.
DR GO; GO:0001228; F:DNA-binding transcription activator activity, RNA polymerase II-specific; IDA:NTNU_SB.
DR GO; GO:0003700; F:DNA-binding transcription factor activity; IDA:UniProtKB.
DR GO; GO:0000981; F:DNA-binding transcription factor activity, RNA polymerase II-specific; ISA:NTNU_SB.
DR GO; GO:0030374; F:nuclear receptor coactivator activity; IMP:ARUK-UCL.
DR GO; GO:0000978; F:RNA polymerase II cis-regulatory region sequence-specific DNA binding; IDA:NTNU_SB.
DR GO; GO:0061629; F:RNA polymerase II-specific DNA-binding transcription factor binding; IPI:UniProtKB.
DR GO; GO:1990837; F:sequence-specific double-stranded DNA binding; IDA:ARUK-UCL.
DR GO; GO:0000976; F:transcription cis-regulatory region binding; IDA:ARUK-UCL.
DR GO; GO:0030154; P:cell differentiation; IBA:GO_Central.
DR GO; GO:0071480; P:cellular response to gamma radiation; IEA:Ensembl.
DR GO; GO:0071394; P:cellular response to testosterone stimulus; IEA:Ensembl.
DR GO; GO:0010467; P:gene expression; IEA:Ensembl.
DR GO; GO:0001889; P:liver development; IEA:Ensembl.
DR GO; GO:0030324; P:lung development; IEA:Ensembl.
DR GO; GO:1901216; P:positive regulation of neuron death; IEA:Ensembl.
DR GO; GO:0045944; P:positive regulation of transcription by RNA polymerase II; IDA:UniProtKB.
DR GO; GO:0045893; P:positive regulation of transcription, DNA-templated; IDA:UniProtKB.
DR GO; GO:0006357; P:regulation of transcription by RNA polymerase II; IBA:GO_Central.
DR GO; GO:0071774; P:response to fibroblast growth factor; ISS:UniProtKB.
DR GO; GO:0009416; P:response to light stimulus; IEA:Ensembl.
DR Gene3D; 1.10.10.10; -; 1.
DR IDEAL; IID00146; -.
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 3D-structure; Activator; Alternative splicing; Direct protein sequencing;
KW DNA-binding; Isopeptide bond; Nucleus; Phosphoprotein; Reference proteome;
KW Transcription; Transcription regulation; Ubl conjugation.
FT CHAIN 1..428
FT /note="ETS domain-containing protein Elk-1"
FT /id="PRO_0000204095"
FT DNA_BIND 5..86
FT /note="ETS"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00237"
FT REGION 121..149
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 165..205
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 228..358
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 349..399
FT /note="Sufficient for interaction with MAD2L2"
FT /evidence="ECO:0000269|PubMed:17296730"
FT COMPBIAS 248..262
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 324
FT /note="Phosphoserine; by MAPK1"
FT /evidence="ECO:0000269|PubMed:7889942,
FT ECO:0007744|PubMed:19690332, ECO:0007744|PubMed:23186163"
FT MOD_RES 336
FT /note="Phosphothreonine; by MAPK1"
FT /evidence="ECO:0000269|PubMed:7889942"
FT MOD_RES 353
FT /note="Phosphothreonine; by MAPK1"
FT /evidence="ECO:0000269|PubMed:10637505"
FT MOD_RES 363
FT /note="Phosphothreonine; by MAPK1"
FT /evidence="ECO:0000269|PubMed:10637505"
FT MOD_RES 368
FT /note="Phosphothreonine; by MAPK1"
FT /evidence="ECO:0000269|PubMed:10637505"
FT MOD_RES 383
FT /note="Phosphoserine; by MAPK1 and MAPK8"
FT /evidence="ECO:0000269|PubMed:10637505,
FT ECO:0000269|PubMed:17296730, ECO:0000269|PubMed:7889942"
FT MOD_RES 389
FT /note="Phosphoserine; by MAPK1"
FT /evidence="ECO:0000269|PubMed:10637505,
FT ECO:0000269|PubMed:7889942"
FT MOD_RES 417
FT /note="Phosphothreonine; by MAPK1"
FT /evidence="ECO:0000269|PubMed:10637505"
FT MOD_RES 422
FT /note="Phosphoserine; by MAPK1"
FT /evidence="ECO:0000269|PubMed:7889942,
FT ECO:0007744|PubMed:19690332"
FT CROSSLNK 230
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO)"
FT /evidence="ECO:0000269|PubMed:15210726"
FT CROSSLNK 249
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO)"
FT /evidence="ECO:0000269|PubMed:12887893,
FT ECO:0000269|PubMed:15210726"
FT CROSSLNK 254
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO)"
FT /evidence="ECO:0000269|PubMed:15210726"
FT VAR_SEQ 91..95
FT /note="VAGCS -> SHCAP (in isoform 2)"
FT /evidence="ECO:0000305"
FT /id="VSP_001466"
FT VAR_SEQ 96..428
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000305"
FT /id="VSP_001467"
FT VARIANT 144
FT /note="G -> S (in dbSNP:rs1997639)"
FT /id="VAR_017108"
FT VARIANT 183
FT /note="S -> N (in dbSNP:rs1059579)"
FT /evidence="ECO:0000269|PubMed:2539641"
FT /id="VAR_017109"
FT MUTAGEN 230
FT /note="K->R: 9-fold increase in transcriptional activator
FT activity; when associated with R-249. Reduction in
FT sumoylation."
FT /evidence="ECO:0000269|PubMed:12887893,
FT ECO:0000269|PubMed:15210726"
FT MUTAGEN 249
FT /note="K->R: 9-fold increase in transcriptional activator
FT activity; when associated with R-230. Reduction in
FT sumoylation."
FT /evidence="ECO:0000269|PubMed:12887893,
FT ECO:0000269|PubMed:15210726"
FT MUTAGEN 254
FT /note="K->R: Reduction in sumoylation."
FT /evidence="ECO:0000269|PubMed:15210726"
FT MUTAGEN 324
FT /note="S->A: No effect on ternary complex formation but
FT loss of transcriptional activity positive regulation by
FT MAD2L2."
FT /evidence="ECO:0000269|PubMed:7889942"
FT MUTAGEN 336
FT /note="T->A: No effect on ternary complex formation."
FT /evidence="ECO:0000269|PubMed:7889942"
FT MUTAGEN 353
FT /note="T->A: No effect on ternary complex formation."
FT /evidence="ECO:0000269|PubMed:7889942"
FT MUTAGEN 363
FT /note="T->A: No effect on ternary complex formation."
FT /evidence="ECO:0000269|PubMed:7889942"
FT MUTAGEN 368
FT /note="T->A: No effect on ternary complex formation."
FT /evidence="ECO:0000269|PubMed:7889942"
FT MUTAGEN 383
FT /note="S->A: 17% reduction in ternary complex formation."
FT /evidence="ECO:0000269|PubMed:17296730,
FT ECO:0000269|PubMed:7889942"
FT MUTAGEN 389
FT /note="S->A: 34% reduction in ternary complex formation."
FT /evidence="ECO:0000269|PubMed:7889942"
FT MUTAGEN 417
FT /note="T->A: No effect on ternary complex formation."
FT /evidence="ECO:0000269|PubMed:7889942"
FT MUTAGEN 422
FT /note="S->A: Slight reduction in ternary complex
FT formation."
FT /evidence="ECO:0000269|PubMed:7889942"
FT HELIX 7..17
FT /evidence="ECO:0007829|PDB:1DUX"
FT STRAND 19..23
FT /evidence="ECO:0007829|PDB:1DUX"
FT STRAND 25..28
FT /evidence="ECO:0007829|PDB:1DUX"
FT TURN 29..32
FT /evidence="ECO:0007829|PDB:1DUX"
FT STRAND 33..35
FT /evidence="ECO:0007829|PDB:1DUX"
FT HELIX 39..48
FT /evidence="ECO:0007829|PDB:1DUX"
FT TURN 49..51
FT /evidence="ECO:0007829|PDB:1DUX"
FT HELIX 57..67
FT /evidence="ECO:0007829|PDB:1DUX"
FT TURN 68..71
FT /evidence="ECO:0007829|PDB:1DUX"
FT STRAND 72..75
FT /evidence="ECO:0007829|PDB:1DUX"
FT STRAND 82..87
FT /evidence="ECO:0007829|PDB:1DUX"
SQ SEQUENCE 428 AA; 44888 MW; 68F71F8ADB9D38CA CRC64;
MDPSVTLWQF LLQLLREQGN GHIISWTSRD GGEFKLVDAE EVARLWGLRK NKTNMNYDKL
SRALRYYYDK NIIRKVSGQK FVYKFVSYPE VAGCSTEDCP PQPEVSVTST MPNVAPAAIH
AAPGDTVSGK PGTPKGAGMA GPGGLARSSR NEYMRSGLYS TFTIQSLQPQ PPPHPRPAVV
LPSAAPAGAA APPSGSRSTS PSPLEACLEA EEAGLPLQVI LTPPEAPNLK SEELNVEPGL
GRALPPEVKV EGPKEELEVA GERGFVPETT KAEPEVPPQE GVPARLPAVV MDTAGQAGGH
AASSPEISQP QKGRKPRDLE LPLSPSLLGG PGPERTPGSG SGSGLQAPGP ALTPSLLPTH
TLTPVLLTPS SLPPSIHFWS TLSPIAPRSP AKLSFQFPSS GSAQVHIPSI SVDGLSTPVV
LSPGPQKP
