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   24-JAN-2024, entry version 196.
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}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
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   GlyCosmos; P41970; 6 sites, 2 glycans.
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; 9606-ENSP00000228741; -.
DR   PeptideAtlas; P41970; -.
DR   ProteomicsDB; 55479; -.
DR   Antibodypedia; 898; 450 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   AGR; HGNC:3325; -.
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; DSDCKMA; -.
DR   OrthoDB; 4237692at2759; -.
DR   PhylomeDB; P41970; -.
DR   TreeFam; TF317732; -.
DR   PathwayCommons; P41970; -.
DR   SignaLink; P41970; -.
DR   SIGNOR; P41970; -.
DR   BioGRID-ORCS; 2004; 12 hits in 1180 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 203 other cell types or tissues.
DR   ExpressionAtlas; P41970; baseline and differential.
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:0045892; P:negative regulation of DNA-templated transcription; 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; Winged helix-like DNA-binding domain superfamily/Winged helix DNA-binding domain; 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; ETS; 1.
DR   PANTHER; PTHR11849:SF172; ETS DOMAIN-CONTAINING PROTEIN ELK-3; 1.
DR   Pfam; PF00178; Ets; 1.
DR   PRINTS; PR00454; ETSDOMAIN.
DR   SMART; SM00413; ETS; 1.
DR   SUPFAM; SSF46785; Winged helix' DNA-binding domain; 1.
DR   PROSITE; PS00345; ETS_DOMAIN_1; 1.
DR   PROSITE; PS00346; ETS_DOMAIN_2; 1.
DR   PROSITE; PS50061; ETS_DOMAIN_3; 1.
DR   Genevisible; P41970; HS.
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
//