ELK3_HUMAN
ID ELK3_HUMAN Reviewed; 407 AA.
AC P41970; B2R6S6; Q6FG57; Q6GU29; Q9UD17;
DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot.
DT 17-OCT-2006, sequence version 2.
DT 03-AUG-2022, entry version 188.
DE RecName: Full=ETS domain-containing protein Elk-3;
DE AltName: Full=ETS-related protein ERP;
DE AltName: Full=ETS-related protein NET;
DE AltName: Full=Serum response factor accessory protein 2;
DE Short=SAP-2;
DE Short=SRF accessory protein 2;
GN Name=ELK3; Synonyms=NET, SAP2;
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].
RX PubMed=7958835; DOI=10.1101/gad.8.13.1502;
RA Giovane A., Pintzas A., Maira S.-M., Sobieszczuk P., Wasylyk B.;
RT "Net, a new ets transcription factor that is activated by Ras.";
RL Genes Dev. 8:1502-1513(1994).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC TISSUE=Placenta;
RX PubMed=7540136; DOI=10.1002/j.1460-2075.1995.tb07257.x;
RA Price M.A., Rogers A.E., Treisman R.;
RT "Comparative analysis of the ternary complex factors Elk-1, SAP-1a and SAP-
RT 2 (ERP/NET).";
RL EMBO J. 14:2589-2601(1995).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RA Ebert L., Schick M., Neubert P., Schatten R., Henze S., Korn B.;
RT "Cloning of human full open reading frames in Gateway(TM) system entry
RT vector (pDONR201).";
RL Submitted (JUN-2004) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
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 [5]
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 [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Brain;
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 [7]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-115, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=18691976; DOI=10.1016/j.molcel.2008.07.007;
RA Daub H., Olsen J.V., Bairlein M., Gnad F., Oppermann F.S., Korner R.,
RA Greff Z., Keri G., Stemmann O., Mann M.;
RT "Kinase-selective enrichment enables quantitative phosphoproteomics of the
RT kinome across the cell cycle.";
RL Mol. Cell 31:438-448(2008).
RN [8]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-396, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
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 [9]
RP SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-92 AND LYS-165, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=28112733; DOI=10.1038/nsmb.3366;
RA Hendriks I.A., Lyon D., Young C., Jensen L.J., Vertegaal A.C.,
RA Nielsen M.L.;
RT "Site-specific mapping of the human SUMO proteome reveals co-modification
RT with phosphorylation.";
RL Nat. Struct. Mol. Biol. 24:325-336(2017).
CC -!- FUNCTION: May be a negative regulator of transcription, but can
CC activate transcription when coexpressed with Ras, Src or Mos. Forms a
CC ternary complex with the serum response factor and the ETS and SRF
CC motifs of the Fos serum response element.
CC -!- SUBUNIT: Interacts with CTBP1.
CC -!- INTERACTION:
CC P41970; Q9NP55: BPIFA1; NbExp=3; IntAct=EBI-1758534, EBI-953896;
CC P41970; P46108: CRK; NbExp=4; IntAct=EBI-1758534, EBI-886;
CC P41970; Q13449: LSAMP; NbExp=3; IntAct=EBI-1758534, EBI-4314821;
CC P41970; P16333: NCK1; NbExp=3; IntAct=EBI-1758534, EBI-389883;
CC P41970; Q9BVL2: NUP58; NbExp=3; IntAct=EBI-1758534, EBI-2811583;
CC P41970; Q99471: PFDN5; NbExp=3; IntAct=EBI-1758534, EBI-357275;
CC P41970; P27986: PIK3R1; NbExp=2; IntAct=EBI-1758534, EBI-79464;
CC P41970; Q02446: SP4; NbExp=3; IntAct=EBI-1758534, EBI-10198587;
CC -!- SUBCELLULAR LOCATION: Nucleus.
CC -!- SIMILARITY: Belongs to the ETS family. {ECO:0000305}.
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DR EMBL; Z36715; CAA85309.1; -; mRNA.
DR EMBL; CR542251; CAG47047.1; -; mRNA.
DR EMBL; AK312694; BAG35573.1; -; mRNA.
DR EMBL; CH471054; EAW97561.1; -; Genomic_DNA.
DR EMBL; BC017371; AAH17371.1; -; mRNA.
DR CCDS; CCDS9060.1; -.
DR PIR; I38062; I38062.
DR RefSeq; NP_005221.2; NM_005230.3.
DR RefSeq; XP_006719338.1; XM_006719275.3.
DR AlphaFoldDB; P41970; -.
DR SMR; P41970; -.
DR BioGRID; 108319; 113.
DR CORUM; P41970; -.
DR ELM; P41970; -.
DR IntAct; P41970; 113.
DR STRING; 9606.ENSP00000228741; -.
DR GlyGen; P41970; 6 sites, 2 O-linked glycans (6 sites).
DR iPTMnet; P41970; -.
DR PhosphoSitePlus; P41970; -.
DR BioMuta; ELK3; -.
DR DMDM; 116241349; -.
DR EPD; P41970; -.
DR jPOST; P41970; -.
DR MassIVE; P41970; -.
DR MaxQB; P41970; -.
DR PaxDb; P41970; -.
DR PeptideAtlas; P41970; -.
DR PRIDE; P41970; -.
DR ProteomicsDB; 55479; -.
DR Antibodypedia; 898; 394 antibodies from 27 providers.
DR DNASU; 2004; -.
DR Ensembl; ENST00000228741.8; ENSP00000228741.3; ENSG00000111145.8.
DR GeneID; 2004; -.
DR KEGG; hsa:2004; -.
DR MANE-Select; ENST00000228741.8; ENSP00000228741.3; NM_005230.4; NP_005221.2.
DR UCSC; uc001teo.2; human.
DR CTD; 2004; -.
DR DisGeNET; 2004; -.
DR GeneCards; ELK3; -.
DR HGNC; HGNC:3325; ELK3.
DR HPA; ENSG00000111145; Low tissue specificity.
DR MIM; 600247; gene.
DR neXtProt; NX_P41970; -.
DR OpenTargets; ENSG00000111145; -.
DR PharmGKB; PA27752; -.
DR VEuPathDB; HostDB:ENSG00000111145; -.
DR eggNOG; KOG3806; Eukaryota.
DR GeneTree; ENSGT00940000157129; -.
DR HOGENOM; CLU_036905_1_0_1; -.
DR InParanoid; P41970; -.
DR OMA; DKHITRP; -.
DR OrthoDB; 981551at2759; -.
DR PhylomeDB; P41970; -.
DR TreeFam; TF317732; -.
DR PathwayCommons; P41970; -.
DR SignaLink; P41970; -.
DR SIGNOR; P41970; -.
DR BioGRID-ORCS; 2004; 10 hits in 1102 CRISPR screens.
DR ChiTaRS; ELK3; human.
DR GeneWiki; ELK3; -.
DR GenomeRNAi; 2004; -.
DR Pharos; P41970; Tbio.
DR PRO; PR:P41970; -.
DR Proteomes; UP000005640; Chromosome 12.
DR RNAct; P41970; protein.
DR Bgee; ENSG00000111145; Expressed in bronchial epithelial cell and 201 other tissues.
DR ExpressionAtlas; P41970; baseline and differential.
DR Genevisible; P41970; HS.
DR GO; GO:0000785; C:chromatin; ISA:NTNU_SB.
DR GO; GO:0005739; C:mitochondrion; IDA:HPA.
DR GO; GO:0005654; C:nucleoplasm; IDA:HPA.
DR GO; GO:0005634; C:nucleus; IBA:GO_Central.
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; NAS:ProtInc.
DR GO; GO:0000981; F:DNA-binding transcription factor activity, RNA polymerase II-specific; ISA:NTNU_SB.
DR GO; GO:0001227; F:DNA-binding transcription repressor activity, RNA polymerase II-specific; IDA:BHF-UCL.
DR GO; GO:0032422; F:purine-rich negative regulatory element binding; IDA:HGNC-UCL.
DR GO; GO:0000978; F:RNA polymerase II cis-regulatory region sequence-specific DNA binding; IDA:NTNU_SB.
DR GO; GO:1990837; F:sequence-specific double-stranded DNA binding; IDA:ARUK-UCL.
DR GO; GO:0001525; P:angiogenesis; IEA:Ensembl.
DR GO; GO:0030154; P:cell differentiation; IBA:GO_Central.
DR GO; GO:0045892; P:negative regulation of transcription, DNA-templated; IDA:HGNC-UCL.
DR GO; GO:0045944; P:positive regulation of transcription by RNA polymerase II; IDA:NTNU_SB.
DR GO; GO:0006357; P:regulation of transcription by RNA polymerase II; IBA:GO_Central.
DR GO; GO:0007165; P:signal transduction; TAS:ProtInc.
DR GO; GO:0042060; P:wound healing; IEA:Ensembl.
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 Activator; DNA-binding; Isopeptide bond; Nucleus; Phosphoprotein;
KW Reference proteome; Repressor; Transcription; Transcription regulation;
KW Ubl conjugation.
FT CHAIN 1..407
FT /note="ETS domain-containing protein Elk-3"
FT /id="PRO_0000204097"
FT DNA_BIND 5..85
FT /note="ETS"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00237"
FT REGION 234..253
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 271..298
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 273..277
FT /note="CTBP-binding motif"
FT COMPBIAS 271..285
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 115
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18691976"
FT MOD_RES 396
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT CROSSLNK 92
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:28112733"
FT CROSSLNK 165
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:28112733"
FT VARIANT 169
FT /note="P -> L (in dbSNP:rs35332676)"
FT /id="VAR_048946"
FT CONFLICT 114
FT /note="A -> V (in Ref. 1; CAA85309)"
FT /evidence="ECO:0000305"
FT CONFLICT 117
FT /note="E -> G (in Ref. 3; CAG47047)"
FT /evidence="ECO:0000305"
FT CONFLICT 128
FT /note="A -> V (in Ref. 1; CAA85309)"
FT /evidence="ECO:0000305"
FT CONFLICT 152
FT /note="Q -> E (in Ref. 1; CAA85309)"
FT /evidence="ECO:0000305"
FT CONFLICT 163
FT /note="T -> R (in Ref. 1; CAA85309)"
FT /evidence="ECO:0000305"
FT CONFLICT 249
FT /note="N -> K (in Ref. 1; CAA85309)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 407 AA; 44240 MW; DD4515270ECED1E3 CRC64;
MESAITLWQF LLQLLLDQKH EHLICWTSND GEFKLLKAEE VAKLWGLRKN KTNMNYDKLS
RALRYYYDKN IIKKVIGQKF VYKFVSFPEI LKMDPHAVEI SRESLLLQDS DCKASPEGRE
AHKHGLAALR STSRNEYIHS GLYSSFTINS LQNPPDAFKA IKTEKLEEPP EDSPPVEEVR
TVIRFVTNKT DKHVTRPVVS LPSTSEAAAA SAFLASSVSA KISSLMLPNA ASISSASPFS
SRSPSLSPNS PLPSEHRSLF LEAACHDSDS LEPLNLSSGS KTKSPSLPPK AKKPKGLEIS
APPLVLSGTD IGSIALNSPA LPSGSLTPAF FTAQTPNGLL LTPSPLLSSI HFWSSLSPVA
PLSPARLQGP STLFQFPTLL NGHMPVPIPS LDRAASPVLL SSNSQKS
